|
Name |
Accession |
Description |
Interval |
E-value |
| PRK08315 |
PRK08315 |
AMP-binding domain protein; Validated |
53-606 |
0e+00 |
|
AMP-binding domain protein; Validated
Pssm-ID: 236236 [Multi-domain] Cd Length: 559 Bit Score: 800.95 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218563680 53 SYVHGLSSHPLQSSTVDQCLQATVERYPDREAMVFVQDGIRKTFAEFYQDVEKAAAGLLAAGLKRGDRLGMWGPNIYEWV 132
Cdd:PRK08315 3 SYVRGPTDVPLLEQTIGQLLDRTAARYPDREALVYRDQGLRWTYREFNEEVDALAKGLLALGIEKGDRVGIWAPNVPEWV 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218563680 133 LMQFATAKAGIILVAVNPAYQLQEVEFALRKVQCNAVVCPTKFKSQHYCDMLKQLCPEMETASPGGIKSSRLPDLHTVIV 212
Cdd:PRK08315 83 LTQFATAKIGAILVTINPAYRLSELEYALNQSGCKALIAADGFKDSDYVAMLYELAPELATCEPGQLQSARLPELRRVIF 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218563680 213 TDSQ-QPGSFLLKDLMQAGSSQHYQQLQDLQKKLVCDDPINIQFTSGTTGKPKGATLSHHNIVNNAYFTGMRIGYNwrKN 291
Cdd:PRK08315 163 LGDEkHPGMLNFDELLALGRAVDDAELAARQATLDPDDPINIQYTSGTTGFPKGATLTHRNILNNGYFIGEAMKLT--EE 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218563680 292 VRICLPVPLYHCFGSVGGGVIMALYGTTVIFPSTGYDGRANLRAIEKEKCTFVYGTPTMYIDMLGQPDLAKFDLSSVRGG 371
Cdd:PRK08315 241 DRLCIPVPLYHCFGMVLGNLACVTHGATMVYPGEGFDPLATLAAVEEERCTALYGVPTMFIAELDHPDFARFDLSSLRTG 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218563680 372 IAAGSPCPPEVMRKILNVMGIKEMVIGYGTTENSPVTFCGFPVDSAERKIETVGCISPHTEAKVVDPTTGEIVPLGAQGE 451
Cdd:PRK08315 321 IMAGSPCPIEVMKRVIDKMHMSEVTIAYGMTETSPVSTQTRTDDPLEKRVTTVGRALPHLEVKIVDPETGETVPRGEQGE 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218563680 452 LMIRGYCVMLEYWQDEEKTRECITKDRWYKTGDIASLDQFAYCKIEGRIKDLIIRGGENIYPAEIEQFLHTHPKILEAQV 531
Cdd:PRK08315 401 LCTRGYSVMKGYWNDPEKTAEAIDADGWMHTGDLAVMDEEGYVNIVGRIKDMIIRGGENIYPREIEEFLYTHPKIQDVQV 480
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 218563680 532 VGVKDERMGEEVCACIRLKEGQECTVEEIKAYCKGKIAHYKVPRYILFVQDYPLTITGKIQKHKLRERTEKQLGL 606
Cdd:PRK08315 481 VGVPDEKYGEEVCAWIILRPGATLTEEDVRDFCRGKIAHYKIPRYIRFVDEFPMTVTGKIQKFKMREMMIEELGL 555
|
|
| FACL_like_2 |
cd05917 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
247-597 |
0e+00 |
|
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ATP-dependent activation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions.
Pssm-ID: 341241 [Multi-domain] Cd Length: 349 Bit Score: 656.66 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218563680 247 CDDPINIQFTSGTTGKPKGATLSHHNIVNNAYFTGMRIGynWRKNVRICLPVPLYHCFGSVGGGVIMALYGTTVIFPSTG 326
Cdd:cd05917 1 PDDVINIQFTSGTTGSPKGATLTHHNIVNNGYFIGERLG--LTEQDRLCIPVPLFHCFGSVLGVLACLTHGATMVFPSPS 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218563680 327 YDGRANLRAIEKEKCTFVYGTPTMYIDMLGQPDLAKFDLSSVRGGIAAGSPCPPEVMRKILNVMGIKEMVIGYGTTENSP 406
Cdd:cd05917 79 FDPLAVLEAIEKEKCTALHGVPTMFIAELEHPDFDKFDLSSLRTGIMAGAPCPPELMKRVIEVMNMKDVTIAYGMTETSP 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218563680 407 VTFCGFPVDSAERKIETVGCISPHTEAKVVDPTTGEIVPLGAQGELMIRGYCVMLEYWQDEEKTRECITKDRWYKTGDIA 486
Cdd:cd05917 159 VSTQTRTDDSIEKRVNTVGRIMPHTEAKIVDPEGGIVPPVGVPGELCIRGYSVMKGYWNDPEKTAEAIDGDGWLHTGDLA 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218563680 487 SLDQFAYCKIEGRIKDLIIRGGENIYPAEIEQFLHTHPKILEAQVVGVKDERMGEEVCACIRLKEGQECTVEEIKAYCKG 566
Cdd:cd05917 239 VMDEDGYCRIVGRIKDMIIRGGENIYPREIEEFLHTHPKVSDVQVVGVPDERYGEEVCAWIRLKEGAELTEEDIKAYCKG 318
|
330 340 350
....*....|....*....|....*....|.
gi 218563680 567 KIAHYKVPRYILFVQDYPLTITGKIQKHKLR 597
Cdd:cd05917 319 KIAHYKVPRYVFFVDEFPLTVSGKIQKFKLR 349
|
|
| PRK12583 |
PRK12583 |
acyl-CoA synthetase; Provisional |
53-606 |
0e+00 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 237145 [Multi-domain] Cd Length: 558 Bit Score: 643.75 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218563680 53 SYVHGLSSHPLQSSTVDQCLQATVERYPDREAMVFVQDGIRKTFAEFYQDVEKAAAGLLAAGLKRGDRLGMWGPNIYEWV 132
Cdd:PRK12583 5 SYYQGGGDKPLLTQTIGDAFDATVARFPDREALVVRHQALRYTWRQLADAVDRLARGLLALGVQPGDRVGIWAPNCAEWL 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218563680 133 LMQFATAKAGIILVAVNPAYQLQEVEFALRKVQCNAVVCPTKFKSQHYCDMLKQLCPEMETASPGGIKSSRLPDLHTVIV 212
Cdd:PRK12583 85 LTQFATARIGAILVNINPAYRASELEYALGQSGVRWVICADAFKTSDYHAMLQELLPGLAEGQPGALACERLPELRGVVS 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218563680 213 TDSQQPGSFL-LKDLMQAGSSQHYQQLQDLQKKLVCDDPINIQFTSGTTGKPKGATLSHHNIVNNAYFTGMRIGYNwrKN 291
Cdd:PRK12583 165 LAPAPPPGFLaWHELQARGETVSREALAERQASLDRDDPINIQYTSGTTGFPKGATLSHHNILNNGYFVAESLGLT--EH 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218563680 292 VRICLPVPLYHCFGSVGGGVIMALYGTTVIFPSTGYDGRANLRAIEKEKCTFVYGTPTMYIDMLGQPDLAKFDLSSVRGG 371
Cdd:PRK12583 243 DRLCVPVPLYHCFGMVLANLGCMTVGACLVYPNEAFDPLATLQAVEEERCTALYGVPTMFIAELDHPQRGNFDLSSLRTG 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218563680 372 IAAGSPCPPEVMRKILNVMGIKEMVIGYGTTENSPVTFCGFPVDSAERKIETVGCISPHTEAKVVDPTtGEIVPLGAQGE 451
Cdd:PRK12583 323 IMAGAPCPIEVMRRVMDEMHMAEVQIAYGMTETSPVSLQTTAADDLERRVETVGRTQPHLEVKVVDPD-GATVPRGEIGE 401
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218563680 452 LMIRGYCVMLEYWQDEEKTRECITKDRWYKTGDIASLDQFAYCKIEGRIKDLIIRGGENIYPAEIEQFLHTHPKILEAQV 531
Cdd:PRK12583 402 LCTRGYSVMKGYWNNPEATAESIDEDGWMHTGDLATMDEQGYVRIVGRSKDMIIRGGENIYPREIEEFLFTHPAVADVQV 481
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 218563680 532 VGVKDERMGEEVCACIRLKEGQECTVEEIKAYCKGKIAHYKVPRYILFVQDYPLTITGKIQKHKLRERTEKQLGL 606
Cdd:PRK12583 482 FGVPDEKYGEEIVAWVRLHPGHAASEEELREFCKARIAHFKVPRYFRFVDEFPMTVTGKVQKFRMREISIEELAL 556
|
|
| MenE/FadK |
COG0318 |
O-succinylbenzoic acid-CoA ligase MenE or related acyl-CoA synthetase (AMP-forming) [Lipid ... |
68-599 |
2.03e-164 |
|
O-succinylbenzoic acid-CoA ligase MenE or related acyl-CoA synthetase (AMP-forming) [Lipid transport and metabolism]; O-succinylbenzoic acid-CoA ligase MenE or related acyl-CoA synthetase (AMP-forming) is part of the Pathway/BioSystem: Menaquinone biosynthesis
Pssm-ID: 440087 [Multi-domain] Cd Length: 452 Bit Score: 477.00 E-value: 2.03e-164
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218563680 68 VDQCLQATVERYPDREAMVFvqDGIRKTFAEFYQDVEKAAAGLLAAGLKRGDRLGMWGPNIYEWVLMQFATAKAGIILVA 147
Cdd:COG0318 1 LADLLRRAAARHPDRPALVF--GGRRLTYAELDARARRLAAALRALGVGPGDRVALLLPNSPEFVVAFLAALRAGAVVVP 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218563680 148 VNPAYQLQEVEFALRKVQCNAVVCptkfksqhycdmlkqlcpemetaspggikssrlpdlhtvivtdsqqpgsfllkdlm 227
Cdd:COG0318 79 LNPRLTAEELAYILEDSGARALVT-------------------------------------------------------- 102
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218563680 228 qagssqhyqqlqdlqkklvcddpINIQFTSGTTGKPKGATLSHHNIVNNAYftGMRIGYNWRKNVRICLPVPLYHCFGSV 307
Cdd:COG0318 103 -----------------------ALILYTSGTTGRPKGVMLTHRNLLANAA--AIAAALGLTPGDVVLVALPLFHVFGLT 157
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218563680 308 GGGVIMALYGTTVIFPsTGYDGRANLRAIEKEKCTFVYGTPTMYIDMLGQPDLAKFDLSSVRGGIAAGSPCPPEVMRKIL 387
Cdd:COG0318 158 VGLLAPLLAGATLVLL-PRFDPERVLELIERERVTVLFGVPTMLARLLRHPEFARYDLSSLRLVVSGGAPLPPELLERFE 236
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218563680 388 NVMGIkEMVIGYGTTENSPVTFCGfPVDSAERKIETVGCISPHTEAKVVDPTtGEIVPLGAQGELMIRGYCVMLEYWQDE 467
Cdd:COG0318 237 ERFGV-RIVEGYGLTETSPVVTVN-PEDPGERRPGSVGRPLPGVEVRIVDED-GRELPPGEVGEIVVRGPNVMKGYWNDP 313
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218563680 468 EKTRECItKDRWYKTGDIASLDQFAYCKIEGRIKDLIIRGGENIYPAEIEQFLHTHPKILEAQVVGVKDERMGEEVCACI 547
Cdd:COG0318 314 EATAEAF-RDGWLRTGDLGRLDEDGYLYIVGRKKDMIISGGENVYPAEVEEVLAAHPGVAEAAVVGVPDEKWGERVVAFV 392
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|..
gi 218563680 548 RLKEGQECTVEEIKAYCKGKIAHYKVPRYILFVQDYPLTITGKIQKHKLRER 599
Cdd:COG0318 393 VLRPGAELDAEELRAFLRERLARYKVPRRVEFVDELPRTASGKIDRRALRER 444
|
|
| FC-FACS_FadD_like |
cd05936 |
Prokaryotic long-chain fatty acid CoA synthetases similar to Escherichia coli FadD; This ... |
72-597 |
2.00e-127 |
|
Prokaryotic long-chain fatty acid CoA synthetases similar to Escherichia coli FadD; This subfamily of the AMP-forming adenylation family contains Escherichia coli FadD and similar prokaryotic fatty acid CoA synthetases. FadD was characterized as a long-chain fatty acid CoA synthetase. The gene fadD is regulated by the fatty acid regulatory protein FadR. Fatty acid CoA synthetase catalyzes the formation of fatty acyl-CoA in a two-step reaction: the formation of a fatty acyl-AMP molecule as an intermediate, followed by the formation of a fatty acyl-CoA. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions.
Pssm-ID: 341259 [Multi-domain] Cd Length: 468 Bit Score: 382.68 E-value: 2.00e-127
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218563680 72 LQATVERYPDREAMVFvqDGIRKTFAEFYQDVEKAAAGLLAAGLKRGDRLGMWGPNIYEWVLMQFATAKAGIILVAVNPA 151
Cdd:cd05936 5 LEEAARRFPDKTALIF--MGRKLTYRELDALAEAFAAGLQNLGVQPGDRVALMLPNCPQFPIAYFGALKAGAVVVPLNPL 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218563680 152 YQLQEVEFALRKVQCNAVVCPTKFKSqhycdmlkqlcpemetaspgGIKSSRLPDLhTVIVTDsqqpgsfllkdlmqags 231
Cdd:cd05936 83 YTPRELEHILNDSGAKALIVAVSFTD--------------------LLAAGAPLGE-RVALTP----------------- 124
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218563680 232 sqhyqqlqdlqkklvcDDPINIQFTSGTTGKPKGATLSHHNIVNNAYFTGMRIGYNWRKNVRICLPVPLYHCFG-SVGGG 310
Cdd:cd05936 125 ----------------EDVAVLQYTSGTTGVPKGAMLTHRNLVANALQIKAWLEDLLEGDDVVLAALPLFHVFGlTVALL 188
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218563680 311 VIMALYGTTVIFPStgYDGRANLRAIEKEKCTFVYGTPTMYIDMLGQPDLAKFDLSSVRGGIAAGSPCPPEVMRKILNVM 390
Cdd:cd05936 189 LPLALGATIVLIPR--FRPIGVLKEIRKHRVTIFPGVPTMYIALLNAPEFKKRDFSSLRLCISGGAPLPVEVAERFEELT 266
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218563680 391 G--IKEmviGYGTTENSPVTfCGFPVDsAERKIETVGCISPHTEAKVVDPTtGEIVPLGAQGELMIRGYCVMLEYWQDEE 468
Cdd:cd05936 267 GvpIVE---GYGLTETSPVV-AVNPLD-GPRKPGSIGIPLPGTEVKIVDDD-GEELPPGEVGELWVRGPQVMKGYWNRPE 340
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218563680 469 KTRECITkDRWYKTGDIASLDQFAYCKIEGRIKDLIIRGGENIYPAEIEQFLHTHPKILEAQVVGVKDERMGEEVCACIR 548
Cdd:cd05936 341 ETAEAFV-DGWLRTGDIGYMDEDGYFFIVDRKKDMIIVGGFNVYPREVEEVLYEHPAVAEAAVVGVPDPYSGEAVKAFVV 419
|
490 500 510 520
....*....|....*....|....*....|....*....|....*....
gi 218563680 549 LKEGQECTVEEIKAYCKGKIAHYKVPRYILFVQDYPLTITGKIQKHKLR 597
Cdd:cd05936 420 LKEGASLTEEEIIAFCREQLAGYKVPRQVEFRDELPKSAVGKILRRELR 468
|
|
| PRK07656 |
PRK07656 |
long-chain-fatty-acid--CoA ligase; Validated |
67-599 |
5.18e-124 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236072 [Multi-domain] Cd Length: 513 Bit Score: 375.78 E-value: 5.18e-124
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218563680 67 TVDQCLQATVERYPDREAMVFvqDGIRKTFAEFYQDVEKAAAGLLAAGLKRGDRLGMWGPNIYEWVLMQFATAKAGIILV 146
Cdd:PRK07656 6 TLPELLARAARRFGDKEAYVF--GDQRLTYAELNARVRRAAAALAALGIGKGDRVAIWAPNSPHWVIAALGALKAGAVVV 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218563680 147 AVNPAYQLQEVEFALRKVQCNAVVCptkfksqhycdmLKQLCPEMETASPggikssRLPDLHTVIV----TDSQQPGSFL 222
Cdd:PRK07656 84 PLNTRYTADEAAYILARGDAKALFV------------LGLFLGVDYSATT------RLPALEHVVIceteEDDPHTEKMK 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218563680 223 LKDLMQAGSSQHYQQLqdlqkKLVCDDPINIQFTSGTTGKPKGATLSHHNIVNNAYFTGMRIGYnwRKNVRICLPVPLYH 302
Cdd:PRK07656 146 TFTDFLAAGDPAERAP-----EVDPDDVADILFTSGTTGRPKGAMLTHRQLLSNAADWAEYLGL--TEGDRYLAANPFFH 218
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218563680 303 CFGsVGGGVIMALY-GTTVIfPSTGYDGRANLRAIEKEKCTFVYGTPTMYIDMLGQPDLAKFDLSSVRGGIAAGSPCPPE 381
Cdd:PRK07656 219 VFG-YKAGVNAPLMrGATIL-PLPVFDPDEVFRLIETERITVLPGPPTMYNSLLQHPDRSAEDLSSLRLAVTGAASMPVA 296
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218563680 382 V---MRKILNVMGIKEmviGYGTTENSPV-TFCGfPVDSAERKIETVGCISPHTEAKVVDPTtGEIVPLGAQGELMIRGY 457
Cdd:PRK07656 297 LlerFESELGVDIVLT---GYGLSEASGVtTFNR-LDDDRKTVAGTIGTAIAGVENKIVNEL-GEEVPVGEVGELLVRGP 371
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218563680 458 CVMLEYWQDEEKTRECITKDRWYKTGDIASLDQFAYCKIEGRIKDLIIRGGENIYPAEIEQFLHTHPKILEAQVVGVKDE 537
Cdd:PRK07656 372 NVMKGYYDDPEATAAAIDADGWLHTGDLGRLDEEGYLYIVDRKKDMFIVGGFNVYPAEVEEVLYEHPAVAEAAVIGVPDE 451
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 218563680 538 RMGEEVCACIRLKEGQECTVEEIKAYCKGKIAHYKVPRYILFVQDYPLTITGKIQKHKLRER 599
Cdd:PRK07656 452 RLGEVGKAYVVLKPGAELTEEELIAYCREHLAKYKVPRSIEFLDELPKNATGKVLKRALREK 513
|
|
| AFD_class_I |
cd04433 |
Adenylate forming domain, Class I, also known as the ANL superfamily; This family is known as ... |
249-592 |
2.15e-119 |
|
Adenylate forming domain, Class I, also known as the ANL superfamily; This family is known as the ANL (acyl-CoA synthetases, the NRPS adenylation domains, and the Luciferase enzymes) superfamily. It includes acyl- and aryl-CoA ligases, as well as the adenylation domain of nonribosomal peptide synthetases and firefly luciferases.The adenylate-forming enzymes catalyze an ATP-dependent two-step reaction to first activate a carboxylate substrate as an adenylate and then transfer the carboxylate to the pantetheine group of either coenzyme A or an acyl-carrier protein. The active site of the domain is located at the interface of a large N-terminal subdomain and a smaller C-terminal subdomain.
Pssm-ID: 341228 [Multi-domain] Cd Length: 336 Bit Score: 357.37 E-value: 2.15e-119
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218563680 249 DPINIQFTSGTTGKPKGATLSHHNIVNNAYFTGMRIGYnwRKNVRICLPVPLYHCFGsvGGGVIMALY--GTTVIFPstG 326
Cdd:cd04433 1 DPALILYTSGTTGKPKGVVLSHRNLLAAAAALAASGGL--TEGDVFLSTLPLFHIGG--LFGLLGALLagGTVVLLP--K 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218563680 327 YDGRANLRAIEKEKCTFVYGTPTMYIDMLGQPDLAKFDLSSVRGGIAAGSPCPPEVMRKILNVMGIKeMVIGYGTTENSP 406
Cdd:cd04433 75 FDPEAALELIEREKVTILLGVPTLLARLLKAPESAGYDLSSLRALVSGGAPLPPELLERFEEAPGIK-LVNGYGLTETGG 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218563680 407 VTFCGFPvDSAERKIETVGCISPHTEAKVVDPTTGEiVPLGAQGELMIRGYCVMLEYWQDEEKTREcITKDRWYKTGDIA 486
Cdd:cd04433 154 TVATGPP-DDDARKPGSVGRPVPGVEVRIVDPDGGE-LPPGEIGELVVRGPSVMKGYWNNPEATAA-VDEDGWYRTGDLG 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218563680 487 SLDQFAYCKIEGRIKDLIIRGGENIYPAEIEQFLHTHPKILEAQVVGVKDERMGEEVCACIRLKEGQECTVEEIKAYCKG 566
Cdd:cd04433 231 RLDEDGYLYIVGRLKDMIKSGGENVYPAEVEAVLLGHPGVAEAAVVGVPDPEWGERVVAVVVLRPGADLDAEELRAHVRE 310
|
330 340
....*....|....*....|....*.
gi 218563680 567 KIAHYKVPRYILFVQDYPLTITGKIQ 592
Cdd:cd04433 311 RLAPYKVPRRVVFVDALPRTASGKID 336
|
|
| AMP-binding |
pfam00501 |
AMP-binding enzyme; |
72-507 |
4.63e-118 |
|
AMP-binding enzyme;
Pssm-ID: 459834 [Multi-domain] Cd Length: 417 Bit Score: 357.01 E-value: 4.63e-118
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218563680 72 LQATVERYPDREAMVfVQDGIRKTFAEFYQDVEKAAAGLLAAGLKRGDRLGMWGPNIYEWVLMQFATAKAGIILVAVNPA 151
Cdd:pfam00501 1 LERQAARTPDKTALE-VGEGRRLTYRELDERANRLAAGLRALGVGKGDRVAILLPNSPEWVVAFLACLKAGAVYVPLNPR 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218563680 152 YQLQEVEFALRKVQCNAVVCPTKFKsqhycdmLKQLCPEMEtaspggikssRLPDLHTVIVTDSQQPGSFLLKDLMQAGS 231
Cdd:pfam00501 80 LPAEELAYILEDSGAKVLITDDALK-------LEELLEALG----------KLEVVKLVLVLDRDPVLKEEPLPEEAKPA 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218563680 232 SQHYQQLQDLQKklvcDDPINIQFTSGTTGKPKGATLSHHNIVNNAYFTGMRIGYNWR--KNVRICLPVPLYHCFGsVGG 309
Cdd:pfam00501 143 DVPPPPPPPPDP----DDLAYIIYTSGTTGKPKGVMLTHRNLVANVLSIKRVRPRGFGlgPDDRVLSTLPLFHDFG-LSL 217
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218563680 310 GVIMALY--GTTVIFPSTG-YDGRANLRAIEKEKCTFVYGTPTMYIDMLGQPDLAKFDLSSVRGGIAAGSPCPPEVMRKI 386
Cdd:pfam00501 218 GLLGPLLagATVVLPPGFPaLDPAALLELIERYKVTVLYGVPTLLNMLLEAGAPKRALLSSLRLVLSGGAPLPPELARRF 297
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218563680 387 LNVMGIkEMVIGYGTTENSPVTFCGFPVDSAERKIETVGCISPHTEAKVVDPTTGEIVPLGAQGELMIRGYCVMLEYWQD 466
Cdd:pfam00501 298 RELFGG-ALVNGYGLTETTGVVTTPLPLDEDLRSLGSVGRPLPGTEVKIVDDETGEPVPPGEPGELCVRGPGVMKGYLND 376
|
410 420 430 440
....*....|....*....|....*....|....*....|.
gi 218563680 467 EEKTRECITKDRWYKTGDIASLDQFAYCKIEGRIKDLIIRG 507
Cdd:pfam00501 377 PELTAEAFDEDGWYRTGDLGRRDEDGYLEIVGRKKDQIKLG 417
|
|
| PRK06187 |
PRK06187 |
long-chain-fatty-acid--CoA ligase; Validated |
67-599 |
8.83e-115 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 235730 [Multi-domain] Cd Length: 521 Bit Score: 352.18 E-value: 8.83e-115
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218563680 67 TVDQCLQATVERYPDREAMVFvqDGIRKTFAEFYQDVEKAAAGLLAAGLKRGDRLGMWGPNIYEWVLMQFATAKAGIILV 146
Cdd:PRK06187 7 TIGRILRHGARKHPDKEAVYF--DGRRTTYAELDERVNRLANALRALGVKKGDRVAVFDWNSHEYLEAYFAVPKIGAVLH 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218563680 147 AVNPAYQLQEVEFALRkvQCNAVVCptkFKSQHYCDMLKQLCPEMETASpggikssrlpdlHTVIVTDSQQPGSFLLK-- 224
Cdd:PRK06187 85 PINIRLKPEEIAYILN--DAEDRVV---LVDSEFVPLLAAILPQLPTVR------------TVIVEGDGPAAPLAPEVge 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218563680 225 --DLMQAGSSQHYQQLQDLqkklvcDDPINIQFTSGTTGKPKGATLSHHNIVNNAYFTGMRIGynWRKNVRICLPVPLYH 302
Cdd:PRK06187 148 yeELLAAASDTFDFPDIDE------NDAAAMLYTSGTTGHPKGVVLSHRNLFLHSLAVCAWLK--LSRDDVYLVIVPMFH 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218563680 303 CFGSvggGV-IMALY-GTTVIFPSTgYDGRANLRAIEKEKCTFVYGTPTMYIDMLGQPDLAKFDLSSVRGGIAAGSPCPP 380
Cdd:PRK06187 220 VHAW---GLpYLALMaGAKQVIPRR-FDPENLLDLIETERVTFFFAVPTIWQMLLKAPRAYFVDFSSLRLVIYGGAALPP 295
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218563680 381 EVMRKILNVMGIKeMVIGYGTTENSPVTFCGFP---VDSAERKIETVGCISPHTEAKVVDPTtGEIVP--LGAQGELMIR 455
Cdd:PRK06187 296 ALLREFKEKFGID-LVQGYGMTETSPVVSVLPPedqLPGQWTKRRSAGRPLPGVEARIVDDD-GDELPpdGGEVGEIIVR 373
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218563680 456 GYCVMLEYWQDEEKTRECITKDrWYKTGDIASLDQFAYCKIEGRIKDLIIRGGENIYPAEIEQFLHTHPKILEAQVVGVK 535
Cdd:PRK06187 374 GPWLMQGYWNRPEATAETIDGG-WLHTGDVGYIDEDGYLYITDRIKDVIISGGENIYPRELEDALYGHPAVAEVAVIGVP 452
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 218563680 536 DERMGEEVCACIRLKEGQECTVEEIKAYCKGKIAHYKVPRYILFVQDYPLTITGKIQKHKLRER 599
Cdd:PRK06187 453 DEKWGERPVAVVVLKPGATLDAKELRAFLRGRLAKFKLPKRIAFVDELPRTSVGKILKRVLREQ 516
|
|
| FACL_FadD13-like |
cd17631 |
fatty acyl-CoA synthetase, including FadD13; This family contains fatty acyl-CoA synthetases, ... |
75-593 |
5.12e-114 |
|
fatty acyl-CoA synthetase, including FadD13; This family contains fatty acyl-CoA synthetases, including Mycobacterium tuberculosis acid-induced operon MymA encoding the fatty acyl-CoA synthetase FadD13 which is essential for virulence and intracellular growth of the pathogen. The fatty acyl-CoA synthetase activates lipids before entering into the metabolic pathways and is also involved in transmembrane lipid transport. However, unlike soluble fatty acyl-CoA synthetases, but like the mammalian integral-membrane very-long-chain acyl-CoA synthetases, FadD13 accepts lipid substrates up to the maximum length of C26, and this is facilitated by an extensive hydrophobic tunnel from the active site to a positively charged patch. Also included is feruloyl-CoA synthetase (Fcs) in Rhodococcus strains where it is involved in biotechnological vanillin production from eugenol and ferulic acid via a non-beta-oxidative pathway.
Pssm-ID: 341286 [Multi-domain] Cd Length: 435 Bit Score: 347.29 E-value: 5.12e-114
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218563680 75 TVERYPDREAMVFvqDGIRKTFAEFYQDVEKAAAGLLAAGLKRGDRLGMWGPNIYEWVLMQFATAKAGIILVAVNpaYQL 154
Cdd:cd17631 4 RARRHPDRTALVF--GGRSLTYAELDERVNRLAHALRALGVAKGDRVAVLSKNSPEFLELLFAAARLGAVFVPLN--FRL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218563680 155 QEVEFAlrkvqcnavvcptkfksqhycdmlkqlcpemetaspggikssrlpdlhtvivtdsqqpgsFLLKDlmqAGSsqh 234
Cdd:cd17631 80 TPPEVA------------------------------------------------------------YILAD---SGA--- 93
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218563680 235 yqqlqdlqkKLVCDDPINIQFTSGTTGKPKGATLSHHNIVNNAYFTGMRIGYNwRKNVRIClPVPLYHCFGS-VGGGVIM 313
Cdd:cd17631 94 ---------KVLFDDLALLMYTSGTTGRPKGAMLTHRNLLWNAVNALAALDLG-PDDVLLV-VAPLFHIGGLgVFTLPTL 162
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218563680 314 ALYGTTVIFPstGYDGRANLRAIEKEKCTFVYGTPTMYIDMLGQPDLAKFDLSSVRGGIAAGSPCPPEVMRkILNVMGIK 393
Cdd:cd17631 163 LRGGTVVILR--KFDPETVLDLIERHRVTSFFLVPTMIQALLQHPRFATTDLSSLRAVIYGGAPMPERLLR-ALQARGVK 239
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218563680 394 eMVIGYGTTENSPVTfCGFPVDSAERKIETVGCISPHTEAKVVDPTtGEIVPLGAQGELMIRGYCVMLEYWQDEEKTREC 473
Cdd:cd17631 240 -FVQGYGMTETSPGV-TFLSPEDHRRKLGSAGRPVFFVEVRIVDPD-GREVPPGEVGEIVVRGPHVMAGYWNRPEATAAA 316
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218563680 474 ItKDRWYKTGDIASLDQFAYCKIEGRIKDLIIRGGENIYPAEIEQFLHTHPKILEAQVVGVKDERMGEEVCACIRLKEGQ 553
Cdd:cd17631 317 F-RDGWFHTGDLGRLDEDGYLYIVDRKKDMIISGGENVYPAEVEDVLYEHPAVAEVAVIGVPDEKWGEAVVAVVVPRPGA 395
|
490 500 510 520
....*....|....*....|....*....|....*....|
gi 218563680 554 ECTVEEIKAYCKGKIAHYKVPRYILFVQDYPLTITGKIQK 593
Cdd:cd17631 396 ELDEDELIAHCRERLARYKIPKSVEFVDALPRNATGKILK 435
|
|
| Firefly_Luc_like |
cd05911 |
Firefly luciferase of light emitting insects and 4-Coumarate-CoA Ligase (4CL); This family ... |
95-592 |
1.95e-93 |
|
Firefly luciferase of light emitting insects and 4-Coumarate-CoA Ligase (4CL); This family contains insect firefly luciferases that share significant sequence similarity to plant 4-coumarate:coenzyme A ligases, despite their functional diversity. Luciferase catalyzes the production of light in the presence of MgATP, molecular oxygen, and luciferin. In the first step, luciferin is activated by acylation of its carboxylate group with ATP, resulting in an enzyme-bound luciferyl adenylate. In the second step, luciferyl adenylate reacts with molecular oxygen, producing an enzyme-bound excited state product (Luc=O*) and releasing AMP. This excited-state product then decays to the ground state (Luc=O), emitting a quantum of visible light.
Pssm-ID: 341237 [Multi-domain] Cd Length: 486 Bit Score: 295.66 E-value: 1.95e-93
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218563680 95 TFAEFYQDVEKAAAGLLAAGLKRGDRLGMWGPNIYEWVLMQFATAKAGIILVAVNPAYQLQEVEFALRKVQCNAVVCPTK 174
Cdd:cd05911 12 TYAQLRTLSRRLAAGLRKLGLKKGDVVGIISPNSTYYPPVFLGCLFAGGIFSAANPIYTADELAHQLKISKPKVIFTDPD 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218563680 175 FKsqhycdmlkqlcPEMETASPGGIKSSRlpdlhtVIVTDSQQPGSFLLKDLMQAGSSQHYQqLQDLQKKLVCDDPINIQ 254
Cdd:cd05911 92 GL------------EKVKEAAKELGPKDK------IIVLDDKPDGVLSIEDLLSPTLGEEDE-DLPPPLKDGKDDTAAIL 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218563680 255 FTSGTTGKPKGATLSHHNIVNNAYFTGMRIGYNWRKNVRICLPVPLYHCFGsVGGGVIMALYGTTVIFpSTGYDGRANLR 334
Cdd:cd05911 153 YSSGTTGLPKGVCLSHRNLIANLSQVQTFLYGNDGSNDVILGFLPLYHIYG-LFTTLASLLNGATVII-MPKFDSELFLD 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218563680 335 AIEKEKCTFVYGTPTMYIDMLGQPDLAKFDLSSVRGGIAAGSPCPPEVMRKILNVMGIKEMVIGYGTTENSPVTFCGFPV 414
Cdd:cd05911 231 LIEKYKITFLYLVPPIAAALAKSPLLDKYDLSSLRVILSGGAPLSKELQELLAKRFPNATIKQGYGMTETGGILTVNPDG 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218563680 415 DSaerKIETVGCISPHTEAKVVDPTTGEIVPLGAQGELMIRGYCVMLEYWQDEEKTRECITKDRWYKTGDIASLDQFAYC 494
Cdd:cd05911 311 DD---KPGSVGRLLPNVEAKIVDDDGKDSLGPNEPGEICVRGPQVMKGYYNNPEATKETFDEDGWLHTGDIGYFDEDGYL 387
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218563680 495 KIEGRIKDLIIRGGENIYPAEIEQFLHTHPKILEAQVVGVKDERMGEEVCACIRLKEGQECTVEEIKAYCKGKIAHYKVP 574
Cdd:cd05911 388 YIVDRKKELIKYKGFQVAPAELEAVLLEHPGVADAAVIGIPDEVSGELPRAYVVRKPGEKLTEKEVKDYVAKKVASYKQL 467
|
490
....*....|....*....
gi 218563680 575 RY-ILFVQDYPLTITGKIQ 592
Cdd:cd05911 468 RGgVVFVDEIPKSASGKIL 486
|
|
| Acs |
COG0365 |
Acyl-coenzyme A synthetase/AMP-(fatty) acid ligase [Lipid transport and metabolism]; |
71-603 |
3.54e-92 |
|
Acyl-coenzyme A synthetase/AMP-(fatty) acid ligase [Lipid transport and metabolism];
Pssm-ID: 440134 [Multi-domain] Cd Length: 565 Bit Score: 294.71 E-value: 3.54e-92
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218563680 71 CLQATVERYPDREAMVFV-QDGIRK--TFAEFYQDVEKAAAGLLAAGLKRGDRLGMWGPNIYEWVLMQFATAKAGIILVA 147
Cdd:COG0365 14 CLDRHAEGRGDKVALIWEgEDGEERtlTYAELRREVNRFANALRALGVKKGDRVAIYLPNIPEAVIAMLACARIGAVHSP 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218563680 148 VNPAYQLQEVEFALRKVQCNAVVCPTkfkSQHYCDMLKQLCPEMETAspggikSSRLPDLHTVIV-----TDSQQPGSFL 222
Cdd:COG0365 94 VFPGFGAEALADRIEDAEAKVLITAD---GGLRGGKVIDLKEKVDEA------LEELPSLEHVIVvgrtgADVPMEGDLD 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218563680 223 LKDLMQAGSSQHyqqlqdlqkklVC-----DDPINIQFTSGTTGKPKGATLSHHNIVNNAYFTgMRIGYNWRKNVRiclp 297
Cdd:COG0365 165 WDELLAAASAEF-----------EPeptdaDDPLFILYTSGTTGKPKGVVHTHGGYLVHAATT-AKYVLDLKPGDV---- 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218563680 298 vplYHCFGSVG------GGVIMALY-GTTVIFpstgYDGRAN-------LRAIEKEKCTFVYGTPTmYIDML---GQPDL 360
Cdd:COG0365 229 ---FWCTADIGwatghsYIVYGPLLnGATVVL----YEGRPDfpdpgrlWELIEKYGVTVFFTAPT-AIRALmkaGDEPL 300
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218563680 361 AKFDLSSVRGGIAAGSPCPPEVMRKILNVMGIkEMVIGYGTTE-NSPV--TFCGFPVdsaerKIETVGCISPHTEAKVVD 437
Cdd:COG0365 301 KKYDLSSLRLLGSAGEPLNPEVWEWWYEAVGV-PIVDGWGQTEtGGIFisNLPGLPV-----KPGSMGKPVPGYDVAVVD 374
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218563680 438 PtTGEIVPLGAQGELMIRGYC--VMLEYWQDEEKTRECI--TKDRWYKTGDIASLDQFAYCKIEGRIKDLIIRGGENIYP 513
Cdd:COG0365 375 E-DGNPVPPGEEGELVIKGPWpgMFRGYWNDPERYRETYfgRFPGWYRTGDGARRDEDGYFWILGRSDDVINVSGHRIGT 453
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218563680 514 AEIEQFLHTHPKILEAQVVGVKDERMGEEVCACIRLKEGQECT---VEEIKAYCKGKIAHYKVPRYILFVQDYPLTITGK 590
Cdd:COG0365 454 AEIESALVSHPAVAEAAVVGVPDEIRGQVVKAFVVLKPGVEPSdelAKELQAHVREELGPYAYPREIEFVDELPKTRSGK 533
|
570
....*....|...
gi 218563680 591 IQKHKLRERTEKQ 603
Cdd:COG0365 534 IMRRLLRKIAEGR 546
|
|
| PRK08316 |
PRK08316 |
acyl-CoA synthetase; Validated |
64-599 |
2.28e-90 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 181381 [Multi-domain] Cd Length: 523 Bit Score: 288.75 E-value: 2.28e-90
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218563680 64 QSSTVDQCLQATVERYPDREAMVFvqDGIRKTFAEFYQDVEKAAAGLLAAGLKRGDRLGMWGPNIYEWVLMQFATAKAGI 143
Cdd:PRK08316 9 RRQTIGDILRRSARRYPDKTALVF--GDRSWTYAELDAAVNRVAAALLDLGLKKGDRVAALGHNSDAYALLWLACARAGA 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218563680 144 ILVAVNPAYQLQEVEFALRKVQCNAVVCPTkfksqhycDMLKQLCPEMETASPGGIKSSRLPDLhtvivtdSQQPGSFL- 222
Cdd:PRK08316 87 VHVPVNFMLTGEELAYILDHSGARAFLVDP--------ALAPTAEAALALLPVDTLILSLVLGG-------REAPGGWLd 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218563680 223 LKDLMQAGSSQhyqqlqDLQKKLVCDDPINIQFTSGTTGKPKGATLSHHNIVnnAYFTGMRIGYNWRKNVRICLPVPLYH 302
Cdd:PRK08316 152 FADWAEAGSVA------EPDVELADDDLAQILYTSGTESLPKGAMLTHRALI--AEYVSCIVAGDMSADDIPLHALPLYH 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218563680 303 CFG-SVGGGVIMALYGTTVIFPSTgyDGRANLRAIEKEKCTFVYGTPTMYIDMLGQPDLAKFDLSSVRGGIAAGSPCPPE 381
Cdd:PRK08316 224 CAQlDVFLGPYLYVGATNVILDAP--DPELILRTIEAERITSFFAPPTVWISLLRHPDFDTRDLSSLRKGYYGASIMPVE 301
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218563680 382 V---MRKILNVMGIKEMvigYGTTENSPV-TFCGfPvDSAERKIETVGCISPHTEAKVVDPTtGEIVPLGAQGELMIRGY 457
Cdd:PRK08316 302 VlkeLRERLPGLRFYNC---YGQTEIAPLaTVLG-P-EEHLRRPGSAGRPVLNVETRVVDDD-GNDVAPGEVGEIVHRSP 375
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218563680 458 CVMLEYWQDEEKTRECItKDRWYKTGDIASLDQFAYCKIEGRIKDLIIRGGENIYPAEIEQFLHTHPKILEAQVVGVKDE 537
Cdd:PRK08316 376 QLMLGYWDDPEKTAEAF-RGGWFHSGDLGVMDEEGYITVVDRKKDMIKTGGENVASREVEEALYTHPAVAEVAVIGLPDP 454
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 218563680 538 RMGEEVCACIRLKEGQECTVEEIKAYCKGKIAHYKVPRYILFVQDYPLTITGKIQKHKLRER 599
Cdd:PRK08316 455 KWIEAVTAVVVPKAGATVTEDELIAHCRARLAGFKVPKRVIFVDELPRNPSGKILKRELRER 516
|
|
| FadD3 |
cd17638 |
acyl-CoA synthetase FadD3 and similar proteins; This family contains long chain fatty acid CoA ... |
249-593 |
1.39e-88 |
|
acyl-CoA synthetase FadD3 and similar proteins; This family contains long chain fatty acid CoA ligases, including FadD3 which is an acyl-CoA synthetase that initiates catabolism of cholesterol rings C and D in actinobacteria. The cholesterol catabolic pathway occurs in most mycolic acid-containing actinobacteria, such as Rhodococcus jostii RHA1, and is critical for Mycobacterium tuberculosis (Mtb) during infection. FadD3 catalyzes the ATP-dependent CoA thioesterification of 3a-alpha-H-4alpha(3'-propanoate)-7a-beta-methylhexahydro-1,5-indanedione (HIP) to yield HIP-CoA. Hydroxylated analogs of HIP, 5alpha-OH HIP and 1beta-OH HIP, can also be used.
Pssm-ID: 341293 [Multi-domain] Cd Length: 330 Bit Score: 277.85 E-value: 1.39e-88
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218563680 249 DPINIQFTSGTTGKPKGATLSHHNIVnnayftgmRIGYNWRKNV------RICLPVPLYHCFGSVGGGVIMALYGTTVIf 322
Cdd:cd17638 1 DVSDIMFTSGTTGRSKGVMCAHRQTL--------RAAAAWADCAdlteddRYLIINPFFHTFGYKAGIVACLLTGATVV- 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218563680 323 PSTGYDGRANLRAIEKEKCTFVYGTPTMYIDMLGQPDLAKFDLSSVRGGIAAGSPCPPEVMRKILNVMGIKEMVIGYGTT 402
Cdd:cd17638 72 PVAVFDVDAILEAIERERITVLPGPPTLFQSLLDHPGRKKFDLSSLRAAVTGAATVPVELVRRMRSELGFETVLTAYGLT 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218563680 403 ENSPVTFCGfPVDSAERKIETVGCISPHTEAKVVDPttgeivplgaqGELMIRGYCVMLEYWQDEEKTRECITKDRWYKT 482
Cdd:cd17638 152 EAGVATMCR-PGDDAETVATTCGRACPGFEVRIADD-----------GEVLVRGYNVMQGYLDDPEATAEAIDADGWLHT 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218563680 483 GDIASLDQFAYCKIEGRIKDLIIRGGENIYPAEIEQFLHTHPKILEAQVVGVKDERMGEEVCACIRLKEGQECTVEEIKA 562
Cdd:cd17638 220 GDVGELDERGYLRITDRLKDMYIVGGFNVYPAEVEGALAEHPGVAQVAVIGVPDERMGEVGKAFVVARPGVTLTEEDVIA 299
|
330 340 350
....*....|....*....|....*....|.
gi 218563680 563 YCKGKIAHYKVPRYILFVQDYPLTITGKIQK 593
Cdd:cd17638 300 WCRERLANYKVPRFVRFLDELPRNASGKVMK 330
|
|
| CHC_CoA_lg |
cd05903 |
Cyclohexanecarboxylate-CoA ligase (also called cyclohex-1-ene-1-carboxylate:CoA ligase); ... |
93-598 |
6.44e-88 |
|
Cyclohexanecarboxylate-CoA ligase (also called cyclohex-1-ene-1-carboxylate:CoA ligase); Cyclohexanecarboxylate-CoA ligase activates the aliphatic ring compound, cyclohexanecarboxylate, for degradation. It catalyzes the synthesis of cyclohexanecarboxylate-CoA thioesters in a two-step reaction involving the formation of cyclohexanecarboxylate-AMP anhydride, followed by the nucleophilic substitution of AMP by CoA.
Pssm-ID: 341229 [Multi-domain] Cd Length: 437 Bit Score: 279.65 E-value: 6.44e-88
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218563680 93 RKTFAEFYQDVEKAAAGLLAAGLKRGDRLGMWGPNIYEWVLMQFATAKAGIILVAVNPAYQLQEVEFALRKVQCNAVVCP 172
Cdd:cd05903 1 RLTYSELDTRADRLAAGLAALGVGPGDVVAFQLPNWWEFAVLYLACLRIGAVTNPILPFFREHELAFILRRAKAKVFVVP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218563680 173 TKFKSQHYCDMlkqlcpemetaspggikssrlpdlhtvivtdsqqPgsfllkdlmqagssqhyqqlqdlqkklvcDDPIN 252
Cdd:cd05903 81 ERFRQFDPAAM----------------------------------P-----------------------------DAVAL 97
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218563680 253 IQFTSGTTGKPKGATLSHHNIVNNAYFTGMRIGYNWRknVRICLPVPLYHCFGSVGGGVIMALYGTTVIFPSTgYDGRAN 332
Cdd:cd05903 98 LLFTSGTTGEPKGVMHSHNTLSASIRQYAERLGLGPG--DVFLVASPMAHQTGFVYGFTLPLLLGAPVVLQDI-WDPDKA 174
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218563680 333 LRAIEKEKCTFVYGTPTMYIDMLGQPDLAKFDLSSVRGGIAAGSPCPPEVMRKILNVMGIKeMVIGYGTTEN-SPVTFCg 411
Cdd:cd05903 175 LALMREHGVTFMMGATPFLTDLLNAVEEAGEPLSRLRTFVCGGATVPRSLARRAAELLGAK-VCSAYGSTECpGAVTSI- 252
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218563680 412 fPVDSAERKIETVGCISPHTEAKVVDpTTGEIVPLGAQGELMIRGYCVMLEYWQDEEKTRECItKDRWYKTGDIASLDQF 491
Cdd:cd05903 253 -TPAPEDRRLYTDGRPLPGVEIKVVD-DTGATLAPGVEGELLSRGPSVFLGYLDRPDLTADAA-PEGWFRTGDLARLDED 329
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218563680 492 AYCKIEGRIKDLIIRGGENIYPAEIEQFLHTHPKILEAQVVGVKDERMGEEVCACIRLKEGQECTVEEIKAYCKGK-IAH 570
Cdd:cd05903 330 GYLRITGRSKDIIIRGGENIPVLEVEDLLLGHPGVIEAAVVALPDERLGERACAVVVTKSGALLTFDELVAYLDRQgVAK 409
|
490 500
....*....|....*....|....*...
gi 218563680 571 YKVPRYILFVQDYPLTITGKIQKHKLRE 598
Cdd:cd05903 410 QYWPERLVHVDDLPRTPSGKVQKFRLRE 437
|
|
| 4CL |
cd05904 |
4-Coumarate-CoA Ligase (4CL); 4-Coumarate:coenzyme A ligase is a key enzyme in the ... |
76-604 |
1.76e-87 |
|
4-Coumarate-CoA Ligase (4CL); 4-Coumarate:coenzyme A ligase is a key enzyme in the phenylpropanoid metabolic pathway for monolignol and flavonoid biosynthesis. It catalyzes the synthesis of hydroxycinnamate-CoA thioesters in a two-step reaction, involving the formation of hydroxycinnamate-AMP anhydride and the nucleophilic substitution of AMP by CoA. The phenylpropanoid pathway is one of the most important secondary metabolism pathways in plants and hydroxycinnamate-CoA thioesters are the precursors of lignin and other important phenylpropanoids.
Pssm-ID: 341230 [Multi-domain] Cd Length: 505 Bit Score: 280.66 E-value: 1.76e-87
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218563680 76 VERYPDREAMVFVQDGIRKTFAEFYQDVEKAAAGLLAAGLKRGDRLGMWGPNIYEWVLMQFATAKAGIILVAVNPAYQLQ 155
Cdd:cd05904 15 ASAHPSRPALIDAATGRALTYAELERRVRRLAAGLAKRGGRKGDVVLLLSPNSIEFPVAFLAVLSLGAVVTTANPLSTPA 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218563680 156 EVEfalrkvqcnavvcptkfksqhycdmlKQlcpeMETASPGGIKSS-----RLPDLH-TVIVTDSQQPGSFLLKDLMQA 229
Cdd:cd05904 95 EIA--------------------------KQ----VKDSGAKLAFTTaelaeKLASLAlPVVLLDSAEFDSLSFSDLLFE 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218563680 230 GSSQHYQQLQDLQkklvcDDPINIQFTSGTTGKPKGATLSHHNIVNNAYFTGMRIGYNWRKNVRICLPVPLYHCFGSVGG 309
Cdd:cd05904 145 ADEAEPPVVVIKQ-----DDVAALLYSSGTTGRSKGVMLTHRNLIAMVAQFVAGEGSNSDSEDVFLCVLPMFHIYGLSSF 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218563680 310 GV-IMALYGTTVIFPStgYDGRANLRAIEKEKCTFVYGTPTMYIDMLGQPDLAKFDLSSVRGGIAAGSPCPPEVM----R 384
Cdd:cd05904 220 ALgLLRLGATVVVMPR--FDLEELLAAIERYKVTHLPVVPPIVLALVKSPIVDKYDLSSLRQIMSGAAPLGKELIeafrA 297
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218563680 385 KILNVmgikEMVIGYGTTENSPVTFCGFPVDSAERKIETVGCISPHTEAKVVDPTTGEIVPLGAQGELMIRGYCVMLEYW 464
Cdd:cd05904 298 KFPNV----DLGQGYGMTESTGVVAMCFAPEKDRAKYGSVGRLVPNVEAKIVDPETGESLPPNQTGELWIRGPSIMKGYL 373
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218563680 465 QDEEKTRECITKDRWYKTGDIASLDQFAYCKIEGRIKDLIIRGGENIYPAEIEQFLHTHPKILEAQVVGVKDERMGEEVC 544
Cdd:cd05904 374 NNPEATAATIDKEGWLHTGDLCYIDEDGYLFIVDRLKELIKYKGFQVAPAELEALLLSHPEILDAAVIPYPDEEAGEVPM 453
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|
gi 218563680 545 ACIRLKEGQECTVEEIKAYCKGKIAHYKVPRYILFVQDYPLTITGKIqkhkLRerteKQL 604
Cdd:cd05904 454 AFVVRKPGSSLTEDEIMDFVAKQVAPYKKVRKVAFVDAIPKSPSGKI----LR----KEL 505
|
|
| FACL_fum10p_like |
cd05926 |
Subfamily of fatty acid CoA ligase (FACL) similar to Fum10p of Gibberella moniliformis; FACL ... |
80-598 |
4.83e-87 |
|
Subfamily of fatty acid CoA ligase (FACL) similar to Fum10p of Gibberella moniliformis; FACL catalyzes the formation of fatty acyl-CoA in a two-step reaction: the formation of a fatty acyl-AMP molecule as an intermediate, followed by the formation of a fatty acyl-CoA. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions. Fum10p is a fatty acid CoA ligase involved in the synthesis of fumonisin, a polyketide mycotoxin, in Gibberella moniliformis.
Pssm-ID: 341249 [Multi-domain] Cd Length: 493 Bit Score: 279.20 E-value: 4.83e-87
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218563680 80 PDREAMVFVQDGIRKTFAEFYQDVEKAAAGLLAAGLKRGDRLGMWGPNIYEWVLMQFATAKAGIILVAVNPAYQLQEVEF 159
Cdd:cd05926 1 PDAPALVVPGSTPALTYADLAELVDDLARQLAALGIKKGDRVAIALPNGLEFVVAFLAAARAGAVVAPLNPAYKKAEFEF 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218563680 160 ALRKVQCNAVVCPTKFKSqhycdmlkqlcPEMETASPGGIKSSRLP-DLHTVIVTDSQQPGSFLLKDLMQAGSSQHYQQl 238
Cdd:cd05926 81 YLADLGSKLVLTPKGELG-----------PASRAASKLGLAILELAlDVGVLIRAPSAESLSNLLADKKNAKSEGVPLP- 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218563680 239 qdlqkklvcDDPINIQFTSGTTGKPKGATLSHHNIVNNAyfTGMRIGYNWRKNVRICLPVPLYHCFGSVGGgVIMALY-G 317
Cdd:cd05926 149 ---------DDLALILHTSGTTGRPKGVPLTHRNLAASA--TNITNTYKLTPDDRTLVVMPLFHVHGLVAS-LLSTLAaG 216
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218563680 318 TTVIFPStGYDGRANLRAIEKEKCTFVYGTPTMYIDMLGQPDLAKFD-LSSVRGGIAAGSPCPPEVMRKILNVMGIKemV 396
Cdd:cd05926 217 GSVVLPP-RFSASTFWPDVRDYNATWYTAVPTIHQILLNRPEPNPESpPPKLRFIRSCSASLPPAVLEALEATFGAP--V 293
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218563680 397 I-GYGTTENSPVTFCGfPVDSAERKIETVGcISPHTEAKVVDPTtGEIVPLGAQGELMIRGYCVMLEYWQDEEKTRECIT 475
Cdd:cd05926 294 LeAYGMTEAAHQMTSN-PLPPGPRKPGSVG-KPVGVEVRILDED-GEILPPGVVGEICLRGPNVTRGYLNNPEANAEAAF 370
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218563680 476 KDRWYKTGDIASLDQFAYCKIEGRIKDLIIRGGENIYPAEIEQFLHTHPKILEAQVVGVKDERMGEEVCACIRLKEGQEC 555
Cdd:cd05926 371 KDGWFRTGDLGYLDADGYLFLTGRIKELINRGGEKISPLEVDGVLLSHPAVLEAVAFGVPDEKYGEEVAAAVVLREGASV 450
|
490 500 510 520
....*....|....*....|....*....|....*....|...
gi 218563680 556 TVEEIKAYCKGKIAHYKVPRYILFVQDYPLTITGKIQKHKLRE 598
Cdd:cd05926 451 TEEELRAFCRKHLAAFKVPKKVYFVDELPKTATGKIQRRKVAE 493
|
|
| ttLC_FACS_AEE21_like |
cd12118 |
Fatty acyl-CoA synthetases similar to LC-FACS from Thermus thermophiles and Arabidopsis; This ... |
72-598 |
1.59e-85 |
|
Fatty acyl-CoA synthetases similar to LC-FACS from Thermus thermophiles and Arabidopsis; This family includes fatty acyl-CoA synthetases that can activate medium to long-chain fatty acids. These enzymes catalyze the ATP-dependent acylation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. Fatty acyl-CoA synthetases are responsible for fatty acid degradation as well as physiological regulation of cellular functions via the production of fatty acyl-CoA esters. The fatty acyl-CoA synthetase from Thermus thermophiles in this family has been shown to catalyze the long-chain fatty acid, myristoyl acid. Also included in this family are acyl activating enzymes from Arabidopsis, which contains a large number of proteins from this family with up to 63 different genes, many of which are uncharacterized.
Pssm-ID: 341283 [Multi-domain] Cd Length: 486 Bit Score: 274.95 E-value: 1.59e-85
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218563680 72 LQATVERYPDREAMVFVqdGIRKTFAEFYQDVEKAAAGLLAAGLKRGDRLGMWGPNIYEWVLMQFATAKAGIILVAVNPA 151
Cdd:cd12118 10 LERAAAVYPDRTSIVYG--DRRYTWRQTYDRCRRLASALAALGISRGDTVAVLAPNTPAMYELHFGVPMAGAVLNALNTR 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218563680 152 YQLQEVEFALRKVQCNavvcptkfksqhycdmlkqlcpemetaspggikssrlpdlhtVIVTDSQqpgsFLLKDLMQAGS 231
Cdd:cd12118 88 LDAEEIAFILRHSEAK------------------------------------------VLFVDRE----FEYEDLLAEGD 121
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218563680 232 SQHyqqlqDLQKKLVCDDPINIQFTSGTTGKPKGATLSHH----NIVNNAYFTGM--RIGYNWrknvriclPVPLYHCFG 305
Cdd:cd12118 122 PDF-----EWIPPADEWDPIALNYTSGTTGRPKGVVYHHRgaylNALANILEWEMkqHPVYLW--------TLPMFHCNG 188
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218563680 306 SVGGGVIMALYGTTVIFPSTgyDGRANLRAIEKEKCTFVYGTPTMYIDMLGQPDLAKFDLSSVRGGIAAGSPcPPEVMRK 385
Cdd:cd12118 189 WCFPWTVAAVGGTNVCLRKV--DAKAIYDLIEKHKVTHFCGAPTVLNMLANAPPSDARPLPHRVHVMTAGAP-PPAAVLA 265
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218563680 386 ILNVMGIKeMVIGYGTTENS-PVTFC-------GFPVDSAERKI--ETVGCISpHTEAKVVDPTTGEIVPLGAQ--GELM 453
Cdd:cd12118 266 KMEELGFD-VTHVYGLTETYgPATVCawkpewdELPTEERARLKarQGVRYVG-LEEVDVLDPETMKPVPRDGKtiGEIV 343
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218563680 454 IRGYCVMLEYWQDEEKTRECiTKDRWYKTGDIASLDQFAYCKIEGRIKDLIIRGGENIYPAEIEQFLHTHPKILEAQVVG 533
Cdd:cd12118 344 FRGNIVMKGYLKNPEATAEA-FRGGWFHSGDLAVIHPDGYIEIKDRSKDIIISGGENISSVEVEGVLYKHPAVLEAAVVA 422
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 218563680 534 VKDERMGEEVCACIRLKEGQECTVEEIKAYCKGKIAHYKVPRYILFVqDYPLTITGKIQKHKLRE 598
Cdd:cd12118 423 RPDEKWGEVPCAFVELKEGAKVTEEEIIAFCREHLAGFMVPKTVVFG-ELPKTSTGKIQKFVLRD 486
|
|
| EntE |
COG1021 |
EntE, 2,3-dihydroxybenzoate-AMP synthase component of non-ribosomal peptide synthetase ... |
67-599 |
4.01e-85 |
|
EntE, 2,3-dihydroxybenzoate-AMP synthase component of non-ribosomal peptide synthetase [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 440644 [Multi-domain] Cd Length: 533 Bit Score: 275.49 E-value: 4.01e-85
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218563680 67 TVDQCLQATVERYPDREAMVfvqDGIRK-TFAEFYQDVEKAAAGLLAAGLKRGDR----LgmwgPNIYEWVLMQFATAKA 141
Cdd:COG1021 26 TLGDLLRRRAERHPDRIAVV---DGERRlSYAELDRRADRLAAGLLALGLRPGDRvvvqL----PNVAEFVIVFFALFRA 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218563680 142 GIILVAVNPAYQLQEVEFALRKVQCNAVVCPTKFKSQHYCDMLKQLCpemetaspggiksSRLPDLHTVIVTDsqQPGSF 221
Cdd:COG1021 99 GAIPVFALPAHRRAEISHFAEQSEAVAYIIPDRHRGFDYRALARELQ-------------AEVPSLRHVLVVG--DAGEF 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218563680 222 L-LKDLMQAGSSQHYQQLQDlqkklvcDDPINIQFTSGTTGKPKGATLSHhnivnNAYFtgmrigYNWRKNVRIC----- 295
Cdd:COG1021 164 TsLDALLAAPADLSEPRPDP-------DDVAFFQLSGGTTGLPKLIPRTH-----DDYL------YSVRASAEICgldad 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218563680 296 ------LPVPlyHCFGSVGGGVIMALY--GTTVIFPSTGYDgrANLRAIEKEKCTFVYGTPTMYIDMLGQPDLAKFDLSS 367
Cdd:COG1021 226 tvylaaLPAA--HNFPLSSPGVLGVLYagGTVVLAPDPSPD--TAFPLIERERVTVTALVPPLALLWLDAAERSRYDLSS 301
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218563680 368 VRGGIAAGSPCPPEVMRKILNVMGIKEMVIgYGTTEnSPVTFCGfPVDSAERKIETVGC-ISPHTEAKVVDPTtGEIVPL 446
Cdd:COG1021 302 LRVLQVGGAKLSPELARRVRPALGCTLQQV-FGMAE-GLVNYTR-LDDPEEVILTTQGRpISPDDEVRIVDED-GNPVPP 377
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218563680 447 GAQGELMIRGYCVMLEYWQDEEKTRECITKDRWYKTGDIASLDQFAYCKIEGRIKDLIIRGGENIYPAEIEQFLHTHPKI 526
Cdd:COG1021 378 GEVGELLTRGPYTIRGYYRAPEHNARAFTPDGFYRTGDLVRRTPDGYLVVEGRAKDQINRGGEKIAAEEVENLLLAHPAV 457
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 218563680 527 LEAQVVGVKDERMGEEVCACIRLKeGQECTVEEIKAYCKGK-IAHYKVPRYILFVQDYPLTITGKIQKHKLRER 599
Cdd:COG1021 458 HDAAVVAMPDEYLGERSCAFVVPR-GEPLTLAELRRFLRERgLAAFKLPDRLEFVDALPLTAVGKIDKKALRAA 530
|
|
| PRK13295 |
PRK13295 |
cyclohexanecarboxylate-CoA ligase; Reviewed |
67-598 |
5.81e-85 |
|
cyclohexanecarboxylate-CoA ligase; Reviewed
Pssm-ID: 171961 [Multi-domain] Cd Length: 547 Bit Score: 275.39 E-value: 5.81e-85
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218563680 67 TVDQCLQATVERYPDREAMVFVQDGI----RKTFAEFYQDVEKAAAGLLAAGLKRGDRLGMWGPNIYEWVLMQFATAKAG 142
Cdd:PRK13295 25 TINDDLDACVASCPDKTAVTAVRLGTgaprRFTYRELAALVDRVAVGLARLGVGRGDVVSCQLPNWWEFTVLYLACSRIG 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218563680 143 IILVAVNPAYQLQEVEFALRKVQCNAVVCPTKFKSQHYCDMLKQLCPEmetaspggikssrLPDLHTVIVTDSQQPGSF- 221
Cdd:PRK13295 105 AVLNPLMPIFRERELSFMLKHAESKVLVVPKTFRGFDHAAMARRLRPE-------------LPALRHVVVVGGDGADSFe 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218563680 222 -LLkdlmqagSSQHYQQLQDLQKKLVC-----DDPINIQFTSGTTGKPKGATLSHHNIVNN--AYFTGMRIGYNwrkNVr 293
Cdd:PRK13295 172 aLL-------ITPAWEQEPDAPAILARlrpgpDDVTQLIYTSGTTGEPKGVMHTANTLMANivPYAERLGLGAD---DV- 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218563680 294 ICLPVPLYHCFGSVGGGVIMALYGTTVIFPSTgYDGRANLRAIEKEKCTFVYGTPTMYIDMLGQPDLAKFDLSSVRGGIA 373
Cdd:PRK13295 241 ILMASPMAHQTGFMYGLMMPVMLGATAVLQDI-WDPARAAELIRTEGVTFTMASTPFLTDLTRAVKESGRPVSSLRTFLC 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218563680 374 AGSPCPPEVMRKILNVMGIKeMVIGYGTTENSPVTFcGFPVDSAERKIETVGCISPHTEAKVVDPTtGEIVPLGAQGELM 453
Cdd:PRK13295 320 AGAPIPGALVERARAALGAK-IVSAWGMTENGAVTL-TKLDDPDERASTTDGCPLPGVEVRVVDAD-GAPLPAGQIGRLQ 396
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218563680 454 IRGYCVMLEYWQDEEKTREciTKDRWYKTGDIASLDQFAYCKIEGRIKDLIIRGGENIYPAEIEQFLHTHPKILEAQVVG 533
Cdd:PRK13295 397 VRGCSNFGGYLKRPQLNGT--DADGWFDTGDLARIDADGYIRISGRSKDVIIRGGENIPVVEIEALLYRHPAIAQVAIVA 474
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 218563680 534 VKDERMGEEVCACIRLKEGQECTVEEIKAYCKG-KIAHYKVPRYILFVQDYPLTITGKIQKHKLRE 598
Cdd:PRK13295 475 YPDERLGERACAFVVPRPGQSLDFEEMVEFLKAqKVAKQYIPERLVVRDALPRTPSGKIQKFRLRE 540
|
|
| PRK06839 |
PRK06839 |
o-succinylbenzoate--CoA ligase; |
116-600 |
2.18e-84 |
|
o-succinylbenzoate--CoA ligase;
Pssm-ID: 168698 [Multi-domain] Cd Length: 496 Bit Score: 272.50 E-value: 2.18e-84
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218563680 116 KRGDRLGMWGPNIYEWVLMQFATAKAGIILVAVNPAYQLQEVEFALRKvqcnavvcptkfksqhycDMLKQLCPEMETAS 195
Cdd:PRK06839 51 KKGERIAILSQNSLEYIVLLFAIAKVECIAVPLNIRLTENELIFQLKD------------------SGTTVLFVEKTFQN 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218563680 196 PGGIKSSRLPDLHTVIVTDSqqpgsfllkdlmqAGSSQHyqQLQDLQKKlVCDDPINIQFTSGTTGKPKGATLSHHNI-- 273
Cdd:PRK06839 113 MALSMQKVSYVQRVISITSL-------------KEIEDR--KIDNFVEK-NESASFIICYTSGTTGKPKGAVLTQENMfw 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218563680 274 --VNNAYFTGMRIgynwrKNVRICLpVPLYHcFGSVGGGVIMALYGTTVIFPSTGYDGRANLRAIEKEKCTFVYGTPTMY 351
Cdd:PRK06839 177 naLNNTFAIDLTM-----HDRSIVL-LPLFH-IGGIGLFAFPTLFAGGVIIVPRKFEPTKALSMIEKHKVTVVMGVPTIH 249
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218563680 352 IDMLGQPDLAKFDLSSVRGGIAAGSPCPPEVMRKILNvMGIKeMVIGYGTTENSPVTFCgFPVDSAERKIETVGCISPHT 431
Cdd:PRK06839 250 QALINCSKFETTNLQSVRWFYNGGAPCPEELMREFID-RGFL-FGQGFGMTETSPTVFM-LSEEDARRKVGSIGKPVLFC 326
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218563680 432 EAKVVDPTTGEiVPLGAQGELMIRGYCVMLEYWQDEEKTRECItKDRWYKTGDIASLDQFAYCKIEGRIKDLIIRGGENI 511
Cdd:PRK06839 327 DYELIDENKNK-VEVGEVGELLIRGPNVMKEYWNRPDATEETI-QDGWLCTGDLARVDEDGFVYIVGRKKEMIISGGENI 404
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218563680 512 YPAEIEQFLHTHPKILEAQVVGVKDERMGEEVCACIRLKEGQECTVEEIKAYCKGKIAHYKVPRYILFVQDYPLTITGKI 591
Cdd:PRK06839 405 YPLEVEQVINKLSDVYEVAVVGRQHVKWGEIPIAFIVKKSSSVLIEKDVIEHCRLFLAKYKIPKEIVFLKELPKNATGKI 484
|
....*....
gi 218563680 592 QKHKLRERT 600
Cdd:PRK06839 485 QKAQLVNQL 493
|
|
| PRK06710 |
PRK06710 |
long-chain-fatty-acid--CoA ligase; Validated |
44-603 |
1.05e-83 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 180666 [Multi-domain] Cd Length: 563 Bit Score: 272.68 E-value: 1.05e-83
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218563680 44 PPSIPTlTTSYvhglSSHPLQsstvdQCLQATVERYPDREAMVFVQDGIrkTFAEFYQDVEKAAAGLLAAGLKRGDRLGM 123
Cdd:PRK06710 12 PEEIPS-TISY----DIQPLH-----KYVEQMASRYPEKKALHFLGKDI--TFSVFHDKVKRFANYLQKLGVEKGDRVAI 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218563680 124 WGPNIYEWVLMQFATAKAGIILVAVNPAYQLQEVEFALRKVQCNAVVCptkfksqhyCDMLKQLCPEMETASP-GGIKSS 202
Cdd:PRK06710 80 MLPNCPQAVIGYYGTLLAGGIVVQTNPLYTERELEYQLHDSGAKVILC---------LDLVFPRVTNVQSATKiEHVIVT 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218563680 203 RLPDL----HTVIVTDSQQPGSFLLKDLMQAGSSQHYQQLQ---DLQKKLVCD---DPINIQFTSGTTGKPKGATLSHHN 272
Cdd:PRK06710 151 RIADFlpfpKNLLYPFVQKKQSNLVVKVSESETIHLWNSVEkevNTGVEVPCDpenDLALLQYTGGTTGFPKGVMLTHKN 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218563680 273 IVNNAyFTGMRIGYNWRKNVRICLPV-PLYHCFG--SVGGGVIMALYgTTVIFPStgYDGRANLRAIEKEKCTFVYGTPT 349
Cdd:PRK06710 231 LVSNT-LMGVQWLYNCKEGEEVVLGVlPFFHVYGmtAVMNLSIMQGY-KMVLIPK--FDMKMVFEAIKKHKVTLFPGAPT 306
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218563680 350 MYIDMLGQPDLAKFDLSSVRGGIAAGSPCPPEVMRKILNVMGIKeMVIGYGTTENSPVTFCGFPVDsaERKIETVGCISP 429
Cdd:PRK06710 307 IYIALLNSPLLKEYDISSIRACISGSAPLPVEVQEKFETVTGGK-LVEGYGLTESSPVTHSNFLWE--KRVPGSIGVPWP 383
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218563680 430 HTEAKVVDPTTGEIVPLGAQGELMIRGYCVMLEYWQDEEKTrECITKDRWYKTGDIASLDQFAYCKIEGRIKDLIIRGGE 509
Cdd:PRK06710 384 DTEAMIMSLETGEALPPGEIGEIVVKGPQIMKGYWNKPEET-AAVLQDGWLHTGDVGYMDEDGFFYVKDRKKDMIVASGF 462
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218563680 510 NIYPAEIEQFLHTHPKILEAQVVGVKDERMGEEVCACIRLKEGQECTVEEIKAYCKGKIAHYKVPRYILFVQDYPLTITG 589
Cdd:PRK06710 463 NVYPREVEEVLYEHEKVQEVVTIGVPDPYRGETVKAFVVLKEGTECSEEELNQFARKYLAAYKVPKVYEFRDELPKTTVG 542
|
570
....*....|....
gi 218563680 590 KIQKHKLRERTEKQ 603
Cdd:PRK06710 543 KILRRVLIEEEKRK 556
|
|
| PRK08314 |
PRK08314 |
long-chain-fatty-acid--CoA ligase; Validated |
72-606 |
8.38e-82 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236235 [Multi-domain] Cd Length: 546 Bit Score: 267.21 E-value: 8.38e-82
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218563680 72 LQATVERYPDREAMVFVqdGIRKTFAEFYQDVEKAAAG-LLAAGLKRGDRLGMWGPNIYEWVLMQFATAKAGIILVAVNP 150
Cdd:PRK08314 16 LEVSARRYPDKTAIVFY--GRAISYRELLEEAERLAGYlQQECGVRKGDRVLLYMQNSPQFVIAYYAILRANAVVVPVNP 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218563680 151 AYQLQEVEFALRKVQCNAVVCptkfksqhycdmLKQLCPEMETASpggiksSRLPdLHTVIVTD-----SQQPG----SF 221
Cdd:PRK08314 94 MNREEELAHYVTDSGARVAIV------------GSELAPKVAPAV------GNLR-LRHVIVAQysdylPAEPEiavpAW 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218563680 222 LLKDL-MQAGSSQHYQQLQD-LQKKLV-------CDDPINIQFTSGTTGKPKGATLSH----HNIVNnayftgmriGYNW 288
Cdd:PRK08314 155 LRAEPpLQALAPGGVVAWKEaLAAGLAppphtagPDDLAVLPYTSGTTGVPKGCMHTHrtvmANAVG---------SVLW 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218563680 289 RKNV--RICLPV-PLYHCFGSVGGgVIMALY--GTTVIFPStgYDGRANLRAIEKEKCTFVYGTPTMYIDMLGQPDLAKF 363
Cdd:PRK08314 226 SNSTpeSVVLAVlPLFHVTGMVHS-MNAPIYagATVVLMPR--WDREAAARLIERYRVTHWTNIPTMVVDFLASPGLAER 302
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218563680 364 DLSSVR---GGiaaGSPCPPEVMRKILNVMGIKeMVIGYGTTENSPVTFCGfPVDSAerKIETVGCISPHTEAKVVDPTT 440
Cdd:PRK08314 303 DLSSLRyigGG---GAAMPEAVAERLKELTGLD-YVEGYGLTETMAQTHSN-PPDRP--KLQCLGIPTFGVDARVIDPET 375
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218563680 441 GEIVPLGAQGELMIRGYCVMLEYWQDEEKTREC-ITKD--RWYKTGDIASLDQFAYCKIEGRIKDLIIRGGENIYPAEIE 517
Cdd:PRK08314 376 LEELPPGEVGEIVVHGPQVFKGYWNRPEATAEAfIEIDgkRFFRTGDLGRMDEEGYFFITDRLKRMINASGFKVWPAEVE 455
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218563680 518 QFLHTHPKILEAQVVGVKDERMGEEVCACIRLKEGQECTV--EEIKAYCKGKIAHYKVPRYILFVQDYPLTITGKIQKHK 595
Cdd:PRK08314 456 NLLYKHPAIQEACVIATPDPRRGETVKAVVVLRPEARGKTteEEIIAWAREHMAAYKYPRIVEFVDSLPKSGSGKILWRQ 535
|
570
....*....|.
gi 218563680 596 LRERTEKQLGL 606
Cdd:PRK08314 536 LQEQEKARAAK 546
|
|
| PRK05605 |
PRK05605 |
long-chain-fatty-acid--CoA ligase; Validated |
22-605 |
1.33e-81 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 235531 [Multi-domain] Cd Length: 573 Bit Score: 267.25 E-value: 1.33e-81
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218563680 22 FPQRPWTPFIASqqscaihvDNPPSIPTLTTSYVHglsshplqsstvdqCLQATVERYPDREAMVFVqdGIRKTFAEFYQ 101
Cdd:PRK05605 10 FADKPWLQSYAP--------WTPHDLDYGDTTLVD--------------LYDNAVARFGDRPALDFF--GATTTYAELGK 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218563680 102 DVEKAAAGLLAAGLKRGDRLGMWGPNIYEWVLMQFATAKAGIILVAVNPAYQLQEVEFALR----KVqcnAVVC------ 171
Cdd:PRK05605 66 QVRRAAAGLRALGVRPGDRVAIVLPNCPQHIVAFYAVLRLGAVVVEHNPLYTAHELEHPFEdhgaRV---AIVWdkvapt 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218563680 172 ------PTKFKSQHYCDM------LKQLC---P---------EMETASPGGIKSSRLpdlhtvivTDSQQPGsfllkdlm 227
Cdd:PRK05605 143 verlrrTTPLETIVSVNMiaamplLQRLAlrlPipalrkaraALTGPAPGTVPWETL--------VDAAIGG-------- 206
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218563680 228 QAGSSQHYqqlqdlqkKLVCDDPINIQFTSGTTGKPKGATLSHHNIVNNAyftgmRIGYNW-----RKNVRICLPVPLYH 302
Cdd:PRK05605 207 DGSDVSHP--------RPTPDDVALILYTSGTTGKPKGAQLTHRNLFANA-----AQGKAWvpglgDGPERVLAALPMFH 273
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218563680 303 CFG-SVGGGVIMALYGTTVIFPStgYDGRANLRAIEKEKCTFVYGTPTMYIDMLGQPDLAKFDLSSVRGGIAAGSPCPPE 381
Cdd:PRK05605 274 AYGlTLCLTLAVSIGGELVLLPA--PDIDLILDAMKKHPPTWLPGVPPLYEKIAEAAEERGVDLSGVRNAFSGAMALPVS 351
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218563680 382 VMRKILNVMGIKeMVIGYGTTENSPVTfCGFPVdSAERKIETVGCISPHTEAKVVDP-TTGEIVPLGAQGELMIRGYCVM 460
Cdd:PRK05605 352 TVELWEKLTGGL-LVEGYGLTETSPII-VGNPM-SDDRRPGYVGVPFPDTEVRIVDPeDPDETMPDGEEGELLVRGPQVF 428
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218563680 461 LEYWQDEEKTRECITkDRWYKTGDIASLDQFAYCKIEGRIKDLIIRGGENIYPAEIEQFLHTHPKILEAQVVGVKDERMG 540
Cdd:PRK05605 429 KGYWNRPEETAKSFL-DGWFRTGDVVVMEEDGFIRIVDRIKELIITGGFNVYPAEVEEVLREHPGVEDAAVVGLPREDGS 507
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 218563680 541 EEVCACIRLKEGQECTVEEIKAYCKGKIAHYKVPRYILFVQDYPLTITGKIQKHKLRERTEKQLG 605
Cdd:PRK05605 508 EEVVAAVVLEPGAALDPEGLRAYCREHLTRYKVPRRFYHVDELPRDQLGKVRRREVREELLEKLG 572
|
|
| PRK06087 |
PRK06087 |
medium-chain fatty-acid--CoA ligase; |
73-605 |
1.51e-81 |
|
medium-chain fatty-acid--CoA ligase;
Pssm-ID: 180393 [Multi-domain] Cd Length: 547 Bit Score: 266.61 E-value: 1.51e-81
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218563680 73 QATVERYPDREAMVFVQdGIRKTFAEFYQDVEKAAAGLLAAGLKRGDRLGMWGPNIYEWVLMQFATAKAGIILVAVNPAY 152
Cdd:PRK06087 30 QQTARAMPDKIAVVDNH-GASYTYSALDHAASRLANWLLAKGIEPGDRVAFQLPGWCEFTIIYLACLKVGAVSVPLLPSW 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218563680 153 QLQEVEFALRKVQCNAVVCPTKFKSQHYCDMLKQLcpemetaspggikSSRLPDLHTVIVTDSQQPGSfllKDLMQAGSS 232
Cdd:PRK06087 109 REAELVWVLNKCQAKMFFAPTLFKQTRPVDLILPL-------------QNQLPQLQQIVGVDKLAPAT---SSLSLSQII 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218563680 233 QHYQQLQDlQKKLVCDDPINIQFTSGTTGKPKGATLSHHNIV-NNAYFTGmRIGYNWrkNVRICLPVPLYHCFGSVGGgV 311
Cdd:PRK06087 173 ADYEPLTT-AITTHGDELAAVLFTSGTEGLPKGVMLTHNNILaSERAYCA-RLNLTW--QDVFMMPAPLGHATGFLHG-V 247
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218563680 312 I--MALYGTTV---IFPSTgydgrANLRAIEKEKCTFVYG-TPTMYiDMLGQPDLAKFDLSSVRGGIAAGSPCPPEVMRK 385
Cdd:PRK06087 248 TapFLIGARSVlldIFTPD-----ACLALLEQQRCTCMLGaTPFIY-DLLNLLEKQPADLSALRFFLCGGTTIPKKVARE 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218563680 386 ILNvMGIKEMVIgYGTTENSPVTFCGfPVDSAERKIETVGCISPHTEAKVVDPTTGEiVPLGAQGELMIRGYCVMLEYWQ 465
Cdd:PRK06087 322 CQQ-RGIKLLSV-YGSTESSPHAVVN-LDDPLSRFMHTDGYAAAGVEIKVVDEARKT-LPPGCEGEEASRGPNVFMGYLD 397
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218563680 466 DEEKTRECITKDRWYKTGDIASLDQFAYCKIEGRIKDLIIRGGENIYPAEIEQFLHTHPKILEAQVVGVKDERMGEEVCA 545
Cdd:PRK06087 398 EPELTARALDEEGWYYSGDLCRMDEAGYIKITGRKKDIIVRGGENISSREVEDILLQHPKIHDACVVAMPDERLGERSCA 477
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 218563680 546 CIRLKEG-QECTVEEIKAY-CKGKIAHYKVPRYILFVQDYPLTITGKIQKHKLRERTEKQLG 605
Cdd:PRK06087 478 YVVLKAPhHSLTLEEVVAFfSRKRVAKYKYPEHIVVIDKLPRTASGKIQKFLLRKDIMRRLT 539
|
|
| LC_FACS_like |
cd05935 |
Putative long-chain fatty acid CoA ligase; The members of this family are putative long-chain ... |
95-591 |
2.86e-75 |
|
Putative long-chain fatty acid CoA ligase; The members of this family are putative long-chain fatty acyl-CoA synthetases, which catalyze the ATP-dependent activation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. Fatty acyl-CoA synthetases are responsible for fatty acid degradation as well as physiological regulation of cellular functions via the production of fatty acyl-CoA esters.
Pssm-ID: 341258 [Multi-domain] Cd Length: 430 Bit Score: 246.62 E-value: 2.86e-75
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218563680 95 TFAEFYQDVEKAAAGLLAAGLKRGDRLGMWGPNIYEWVLMQFATAKAGIILVAVNPAYQLQEVEFALrkvqcnavvcptk 174
Cdd:cd05935 3 TYLELLEVVKKLASFLSNKGVRKGDRVGICLQNSPQYVIAYFAIWRANAVVVPINPMLKERELEYIL------------- 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218563680 175 fksqhycdmlkqlcpemetaSPGGIKssrlpdlhTVIVTDSQqpgsfllkdlmqagssqhyqqlqdlqkklvcDDPINIQ 254
Cdd:cd05935 70 --------------------NDSGAK--------VAVVGSEL-------------------------------DDLALIP 90
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218563680 255 FTSGTTGKPKGATLSHHNIVNNAyfTGMRIGYNWRKNVRICLPVPLYHCFGSVGGgVIMALYGTTVIFPSTGYDGRANLR 334
Cdd:cd05935 91 YTSGTTGLPKGCMHTHFSAAANA--LQSAVWTGLTPSDVILACLPLFHVTGFVGS-LNTAVYVGGTYVLMARWDRETALE 167
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218563680 335 AIEKEKCTFVYGTPTMYIDMLGQPDLAKFDLSSVRGGIAAGSPCPPEVMRKILNVMGIKEMViGYGTTENSPVTFCGFPv 414
Cdd:cd05935 168 LIEKYKVTFWTNIPTMLVDLLATPEFKTRDLSSLKVLTGGGAPMPPAVAEKLLKLTGLRFVE-GYGLTETMSQTHTNPP- 245
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218563680 415 dsAERKIETVGCISPHTEAKVVDPTTGEIVPLGAQGELMIRGYCVMLEYWQDEEKTRECITKD---RWYKTGDIASLDQF 491
Cdd:cd05935 246 --LRPKLQCLGIP*FGVDARVIDIETGRELPPNEVGEIVVRGPQIFKGYWNRPEETEESFIEIkgrRFFRTGDLGYMDEE 323
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218563680 492 AYCKIEGRIKDLIIRGGENIYPAEIEQFLHTHPKILEAQVVGVKDERMGEEVCACIRLKEGQ--ECTVEEIKAYCKGKIA 569
Cdd:cd05935 324 GYFFFVDRVKRMINVSGFKVWPAEVEAKLYKHPAI*EVCVISVPDERVGEEVKAFIVLRPEYrgKVTEEDIIEWAREQMA 403
|
490 500
....*....|....*....|..
gi 218563680 570 HYKVPRYILFVQDYPLTITGKI 591
Cdd:cd05935 404 AYKYPREVEFVDELPRSASGKI 425
|
|
| MCS |
cd05941 |
Malonyl-CoA synthetase (MCS); MCS catalyzes the formation of malonyl-CoA in a two-step ... |
81-598 |
1.34e-74 |
|
Malonyl-CoA synthetase (MCS); MCS catalyzes the formation of malonyl-CoA in a two-step reaction consisting of the adenylation of malonate with ATP, followed by malonyl transfer from malonyl-AMP to CoA. Malonic acid and its derivatives are the building blocks of polyketides and malonyl-CoA serves as the substrate of polyketide synthases. Malonyl-CoA synthetase has broad substrate tolerance and can activate a variety of malonyl acid derivatives. MCS may play an important role in biosynthesis of polyketides, the important secondary metabolites with therapeutic and agrochemical utility.
Pssm-ID: 341264 [Multi-domain] Cd Length: 442 Bit Score: 244.89 E-value: 1.34e-74
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218563680 81 DREAMVFvqDGIRKTFAEFYQDVEKAAAG-LLAAGLKRGDRLGMWGPNIYEWVLMQFATAKAGIILVAVNPAYQLQEVEF 159
Cdd:cd05941 1 DRIAIVD--DGDSITYADLVARAARLANRlLALGKDLRGDRVAFLAPPSAEYVVAQLAIWRAGGVAVPLNPSYPLAELEY 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218563680 160 alrkvqcnavvcptkfksqhycdmlkqlcpemetaspggikssrlpdlhtvIVTDSQQpgSFLLKDLMqagssqhyqqlq 239
Cdd:cd05941 79 ---------------------------------------------------VITDSEP--SLVLDPAL------------ 93
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218563680 240 dlqkklvcddpinIQFTSGTTGKPKGATLSHHNIVNNAyfTGMRIGYNWRKNVRICLPVPLYHCFGsVGGGVIMALY-GT 318
Cdd:cd05941 94 -------------ILYTSGTTGRPKGVVLTHANLAANV--RALVDAWRWTEDDVLLHVLPLHHVHG-LVNALLCPLFaGA 157
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218563680 319 TVIFpSTGYDGRANLRAIEKEKCTFVYGTPTMYIDMLGQPDLAKFDLSSVRGGIAAG--------SPCPPEVMRKILNVM 390
Cdd:cd05941 158 SVEF-LPKFDPKEVAISRLMPSITVFMGVPTIYTRLLQYYEAHFTDPQFARAAAAERlrlmvsgsAALPVPTLEEWEAIT 236
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218563680 391 G--IKEMvigYGTTENSPVTFCGFpvdSAERKIETVGCISPHTEAKVVDPTTGEIVPLGAQGELMIRGYCVMLEYWQDEE 468
Cdd:cd05941 237 GhtLLER---YGMTEIGMALSNPL---DGERRPGTVGMPLPGVQARIVDEETGEPLPRGEVGEIQVRGPSVFKEYWNKPE 310
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218563680 469 KTRECITKDRWYKTGDIASLDQFAYCKIEGRIKDLII-RGGENIYPAEIEQFLHTHPKILEAQVVGVKDERMGEEVCACI 547
Cdd:cd05941 311 ATKEEFTDDGWFKTGDLGVVDEDGYYWILGRSSVDIIkSGGYKVSALEIERVLLAHPGVSECAVIGVPDPDWGERVVAVV 390
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|..
gi 218563680 548 RLKEGQEC-TVEEIKAYCKGKIAHYKVPRYILFVQDYPLTITGKIQKHKLRE 598
Cdd:cd05941 391 VLRAGAAAlSLEELKEWAKQRLAPYKRPRRLILVDELPRNAMGKVNKKELRK 442
|
|
| FACL_DitJ_like |
cd05934 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
95-597 |
8.46e-74 |
|
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ATP-dependent activation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions. Members of this family include DitJ from Pseudomonas and similar proteins.
Pssm-ID: 341257 [Multi-domain] Cd Length: 422 Bit Score: 242.20 E-value: 8.46e-74
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218563680 95 TFAEFYQDVEKAAAGLLAAGLKRGDRLGMWGPNIYEWVLMQFATAKAGIILVAVNPAYQLQEVEFALRKVQCNAVVCptk 174
Cdd:cd05934 5 TYAELLRESARIAAALAALGIRPGDRVALMLDNCPEFLFAWFALAKLGAVLVPINTALRGDELAYIIDHSGAQLVVV--- 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218563680 175 fksqhycdmlkqlcpemetaspggikssrlpdlhtvivtdsqqpgsfllkdlmqagssqhyqqlqdlqkklvcdDPINIQ 254
Cdd:cd05934 82 --------------------------------------------------------------------------DPASIL 87
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218563680 255 FTSGTTGKPKGATLSHHNIVNNAYFTGMRIGYnwRKNVRICLPVPLYHcFGSVGGGVIMALY--GTTVIFPStgYDGRAN 332
Cdd:cd05934 88 YTSGTTGPPKGVVITHANLTFAGYYSARRFGL--GEDDVYLTVLPLFH-INAQAVSVLAALSvgATLVLLPR--FSASRF 162
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218563680 333 LRAIEKEKCTFVYGTPTMYIDMLGQPDLAKFDLSSVRggIAAGSPCPPEVMRKILNVMGIKeMVIGYGTTENSpVTFCGf 412
Cdd:cd05934 163 WSDVRRYGATVTNYLGAMLSYLLAQPPSPDDRAHRLR--AAYGAPNPPELHEEFEERFGVR-LLEGYGMTETI-VGVIG- 237
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218563680 413 PVDSAERkietVGCI---SPHTEAKVVDPTTGEiVPLGAQGELMIR---GYCVMLEYWQDEEKTRECItKDRWYKTGDIA 486
Cdd:cd05934 238 PRDEPRR----PGSIgrpAPGYEVRIVDDDGQE-LPAGEPGELVIRglrGWGFFKGYYNMPEATAEAM-RNGWFHTGDLG 311
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218563680 487 SLDQFAYCKIEGRIKDLIIRGGENIYPAEIEQFLHTHPKILEAQVVGVKDERMGEEVCACIRLKEGQECTVEEIKAYCKG 566
Cdd:cd05934 312 YRDADGFFYFVDRKKDMIRRRGENISSAEVERAILRHPAVREAAVVAVPDEVGEDEVKAVVVLRPGETLDPEELFAFCEG 391
|
490 500 510
....*....|....*....|....*....|.
gi 218563680 567 KIAHYKVPRYILFVQDYPLTITGKIQKHKLR 597
Cdd:cd05934 392 QLAYFKVPRYIRFVDDLPKTPTEKVAKAQLR 422
|
|
| PRK07059 |
PRK07059 |
Long-chain-fatty-acid--CoA ligase; Validated |
62-597 |
9.34e-73 |
|
Long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 235923 [Multi-domain] Cd Length: 557 Bit Score: 243.39 E-value: 9.34e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218563680 62 PLQSSTVDQCLQATVERYPDREAmvFVQDGIRKTFAEFYQDVEKAAAGLLAAGLKRGDRLGMWGPNIYEWVLMQFATAKA 141
Cdd:PRK07059 19 ASQYPSLADLLEESFRQYADRPA--FICMGKAITYGELDELSRALAAWLQSRGLAKGARVAIMMPNVLQYPVAIAAVLRA 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218563680 142 GIILVAVNPAYQLQEVEFALRKVQCNAVVCPTKFKSQHYCDMLKQLCPEMETASPG---GIKSsrlpdlHTV-------- 210
Cdd:PRK07059 97 GYVVVNVNPLYTPRELEHQLKDSGAEAIVVLENFATTVQQVLAKTAVKHVVVASMGdllGFKG------HIVnfvvrrvk 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218563680 211 -IVTDSQQPGSFLLKDLMQAGSSQHYQQLqdlqkKLVCDDPINIQFTSGTTGKPKGATLSHHNIVNNAYFTG--MRIGYN 287
Cdd:PRK07059 171 kMVPAWSLPGHVRFNDALAEGARQTFKPV-----KLGPDDVAFLQYTGGTTGVSKGATLLHRNIVANVLQMEawLQPAFE 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218563680 288 WRKNVR----IClPVPLYHCFG-SVGGGVIMALYGTTVIFPSTgYDGRANLRAIEKEKCTFVYGTPTMYIDMLGQPDLAK 362
Cdd:PRK07059 246 KKPRPDqlnfVC-ALPLYHIFAlTVCGLLGMRTGGRNILIPNP-RDIPGFIKELKKYQVHIFPAVNTLYNALLNNPDFDK 323
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218563680 363 FDLSSVR----GGIAAGSPcppeVMRKILNVMG--IKEmviGYGTTENSPVTFCGfPVDSAERKiETVGCISPHTEAKVV 436
Cdd:PRK07059 324 LDFSKLIvangGGMAVQRP----VAERWLEMTGcpITE---GYGLSETSPVATCN-PVDATEFS-GTIGLPLPSTEVSIR 394
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218563680 437 DpTTGEIVPLGAQGELMIRGYCVMLEYWQDEEKTRECITKDRWYKTGDIASLDQFAYCKIEGRIKDLIIRGGENIYPAEI 516
Cdd:PRK07059 395 D-DDGNDLPLGEPGEICIRGPQVMAGYWNRPDETAKVMTADGFFRTGDVGVMDERGYTKIVDRKKDMILVSGFNVYPNEI 473
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218563680 517 EQFLHTHPKILEAQVVGVKDERMGEEVCACIrLKEGQECTVEEIKAYCKGKIAHYKVPRYILFVQDYPLTITGKIQKHKL 596
Cdd:PRK07059 474 EEVVASHPGVLEVAAVGVPDEHSGEAVKLFV-VKKDPALTEEDVKAFCKERLTNYKRPKFVEFRTELPKTNVGKILRREL 552
|
.
gi 218563680 597 R 597
Cdd:PRK07059 553 R 553
|
|
| PRK08276 |
PRK08276 |
long-chain-fatty-acid--CoA ligase; Validated |
254-599 |
1.03e-69 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236215 [Multi-domain] Cd Length: 502 Bit Score: 234.03 E-value: 1.03e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218563680 254 QFTSGTTGKPKG--ATLSHHNI---VNNAYFTGMRIGYNWRKNVRIClPVPLYHCFGSVGGGVIMALYGTTVIFPstGYD 328
Cdd:PRK08276 146 LYSSGTTGRPKGikRPLPGLDPdeaPGMMLALLGFGMYGGPDSVYLS-PAPLYHTAPLRFGMSALALGGTVVVME--KFD 222
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218563680 329 GRANLRAIEKEKCTFVYGTPTMYIDMLGQPD--LAKFDLSSVRGGIAAGSPCPPEVMRKILNVMG--IKEMvigYGTTEN 404
Cdd:PRK08276 223 AEEALALIERYRVTHSQLVPTMFVRMLKLPEevRARYDVSSLRVAIHAAAPCPVEVKRAMIDWWGpiIHEY---YASSEG 299
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218563680 405 SPVTFCGfPVDSAERKiETVGciSP-HTEAKVVDPTtGEIVPLGAQGELMIRGYCVMLEYWQDEEKTRECITKDRWYKTG 483
Cdd:PRK08276 300 GGVTVIT-SEDWLAHP-GSVG--KAvLGEVRILDED-GNELPPGEIGTVYFEMDGYPFEYHNDPEKTAAARNPHGWVTVG 374
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218563680 484 DIASLDQFAYCKIEGRIKDLIIRGGENIYPAEIEQFLHTHPKILEAQVVGVKDERMGEEVCACIRLKEGQECTVE---EI 560
Cdd:PRK08276 375 DVGYLDEDGYLYLTDRKSDMIISGGVNIYPQEIENLLVTHPKVADVAVFGVPDEEMGERVKAVVQPADGADAGDAlaaEL 454
|
330 340 350
....*....|....*....|....*....|....*....
gi 218563680 561 KAYCKGKIAHYKVPRYILFVQDYPLTITGKIQKHKLRER 599
Cdd:PRK08276 455 IAWLRGRLAHYKCPRSIDFEDELPRTPTGKLYKRRLRDR 493
|
|
| ttLC_FACS_AlkK_like |
cd12119 |
Fatty acyl-CoA synthetases similar to LC-FACS from Thermus thermophiles; This family includes ... |
93-598 |
2.42e-69 |
|
Fatty acyl-CoA synthetases similar to LC-FACS from Thermus thermophiles; This family includes fatty acyl-CoA synthetases that can activate medium-chain to long-chain fatty acids. They catalyze the ATP-dependent acylation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. The fatty acyl-CoA synthetases are responsible for fatty acid degradation as well as physiological regulation of cellular functions via the production of fatty acyl-CoA esters. The fatty acyl-CoA synthetase from Thermus thermophiles in this family catalyzes the long-chain fatty acid, myristoyl acid, while another member in this family, the AlkK protein identified from Pseudomonas oleovorans, targets medium chain fatty acids. This family also includes uncharacterized FACS proteins.
Pssm-ID: 341284 [Multi-domain] Cd Length: 518 Bit Score: 233.29 E-value: 2.42e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218563680 93 RKTFAEFYQDVEKAAAGLLAAGLKRGDRLG--MWgpNIYEWVLMQFATAKAGIILVAVNPAYQLQEVEFALRKVQCNAVv 170
Cdd:cd12119 25 RYTYAEVAERARRLANALRRLGVKPGDRVAtlAW--NTHRHLELYYAVPGMGAVLHTINPRLFPEQIAYIINHAEDRVV- 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218563680 171 cptkFKSQHYCDMLKQLCPemetaspggikssRLPDLHTVIVTDSQQPGsfLLKDLMQAGssqHYQQLQDlQKKLVCD-- 248
Cdd:cd12119 102 ----FVDRDFLPLLEAIAP-------------RLPTVEHVVVMTDDAAM--PEPAGVGVL---AYEELLA-AESPEYDwp 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218563680 249 -----DPINIQFTSGTTGKPKGATLSHHNIVNNAYFTGMRIGYNWRKNvRICLP-VPLYHcfgsVGG-GV--IMALYGTT 319
Cdd:cd12119 159 dfdenTAAAICYTSGTTGNPKGVVYSHRSLVLHAMAALLTDGLGLSES-DVVLPvVPMFH----VNAwGLpyAAAMVGAK 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218563680 320 VIFPSTGYDGRANLRAIEKEKCTFVYGTPTMYIDMLGQPDLAKFDLSSVRGGIAAGSPCPPEVMRKILNvMGIkEMVIGY 399
Cdd:cd12119 234 LVLPGPYLDPASLAELIEREGVTFAAGVPTVWQGLLDHLEANGRDLSSLRRVVIGGSAVPRSLIEAFEE-RGV-RVIHAW 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218563680 400 GTTENSPVTFCGFP--------VDSAERKIETVGCISPHTEAKVVDPTTGEIVPLG-AQGELMIRGYCVMLEYWQDEEKT 470
Cdd:cd12119 312 GMTETSPLGTVARPpsehsnlsEDEQLALRAKQGRPVPGVELRIVDDDGRELPWDGkAVGELQVRGPWVTKSYYKNDEES 391
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218563680 471 REcITKDRWYKTGDIASLDQFAYCKIEGRIKDLIIRGGENIYPAEIEQFLHTHPKILEAQVVGVKDERMGEEVCACIRLK 550
Cdd:cd12119 392 EA-LTEDGWLRTGDVATIDEDGYLTITDRSKDVIKSGGEWISSVELENAIMAHPAVAEAAVIGVPHPKWGERPLAVVVLK 470
|
490 500 510 520
....*....|....*....|....*....|....*....|....*...
gi 218563680 551 EGQECTVEEIKAYCKGKIAHYKVPRYILFVQDYPLTITGKIQKHKLRE 598
Cdd:cd12119 471 EGATVTAEELLEFLADKVAKWWLPDDVVFVDEIPKTSTGKIDKKALRE 518
|
|
| PRK12492 |
PRK12492 |
long-chain-fatty-acid--CoA ligase; Provisional |
67-598 |
2.42e-69 |
|
long-chain-fatty-acid--CoA ligase; Provisional
Pssm-ID: 171539 [Multi-domain] Cd Length: 562 Bit Score: 234.72 E-value: 2.42e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218563680 67 TVDQCLQATVERYPDREAmvFVQDGIRKTFAEF-YQDVEKAAAGLLAAGLKRGDRLGMWGPNIYEWVLMQFATAKAGIIL 145
Cdd:PRK12492 25 SVVEVFERSCKKFADRPA--FSNLGVTLSYAELeRHSAAFAAYLQQHTDLVPGDRIAVQMPNVLQYPIAVFGALRAGLIV 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218563680 146 VAVNPAYQLQEVEFALRKVQCNAVVcptkfksqhYCDMLKQLCPEM--ETASPGGIKSsRLPDL---------HTVI--- 211
Cdd:PRK12492 103 VNTNPLYTAREMRHQFKDSGARALV---------YLNMFGKLVQEVlpDTGIEYLIEA-KMGDLlpaakgwlvNTVVdkv 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218563680 212 ---VTDSQQPGSFLLKDLMQAGSSQHYQQLqdlqkKLVCDDPINIQFTSGTTGKPKGATLSHHNIVNN-----AYF--TG 281
Cdd:PRK12492 173 kkmVPAYHLPQAVPFKQALRQGRGLSLKPV-----PVGLDDIAVLQYTGGTTGLAKGAMLTHGNLVANmlqvrACLsqLG 247
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218563680 282 MRIGYNWRKNVRICL-PVPLYHCFGSVGGGVIMALYGTTVIFPSTGYDGRANLRAIEKEKCTFVYGTPTMYIDMLGQPDL 360
Cdd:PRK12492 248 PDGQPLMKEGQEVMIaPLPLYHIYAFTANCMCMMVSGNHNVLITNPRDIPGFIKELGKWRFSALLGLNTLFVALMDHPGF 327
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218563680 361 AKFDLSSVRGGIAAGSPCPPEVMRKILNVMGIKeMVIGYGTTENSPVTfCGFPVDSAERkIETVGCISPHTEAKVVDPTT 440
Cdd:PRK12492 328 KDLDFSALKLTNSGGTALVKATAERWEQLTGCT-IVEGYGLTETSPVA-STNPYGELAR-LGTVGIPVPGTALKVIDDDG 404
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218563680 441 GEIvPLGAQGELMIRGYCVMLEYWQDEEKTRECITKDRWYKTGDIASLDQFAYCKIEGRIKDLIIRGGENIYPAEIEQFL 520
Cdd:PRK12492 405 NEL-PLGERGELCIKGPQVMKGYWQQPEATAEALDAEGWFKTGDIAVIDPDGFVRIVDRKKDLIIVSGFNVYPNEIEDVV 483
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 218563680 521 HTHPKILEAQVVGVKDERMGEEVCACIRLKEGQeCTVEEIKAYCKGKIAHYKVPRYILFVQDYPLTITGKIQKHKLRE 598
Cdd:PRK12492 484 MAHPKVANCAAIGVPDERSGEAVKLFVVARDPG-LSVEELKAYCKENFTGYKVPKHIVLRDSLPMTPVGKILRRELRD 560
|
|
| PRK05677 |
PRK05677 |
long-chain-fatty-acid--CoA ligase; Validated |
54-606 |
3.66e-69 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 168170 [Multi-domain] Cd Length: 562 Bit Score: 234.27 E-value: 3.66e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218563680 54 YVHGLSS--HPLQSSTVDQCLQATVERYPDREAmvFVQDGIRKTFAEFY-QDVEKAAAGLLAAGLKRGDRLGMWGPNIYE 130
Cdd:PRK05677 10 YPAGIAAeiNPDEYPNIQAVLKQSCQRFADKPA--FSNLGKTLTYGELYkLSGAFAAWLQQHTDLKPGDRIAVQLPNVLQ 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218563680 131 WVLMQFATAKAGIILVAVNPAYQLQEVEFALRKVQCNAVVCptkfksqhycdmLKQLCPEMETASP-GGIKS---SRLPD 206
Cdd:PRK05677 88 YPVAVFGAMRAGLIVVNTNPLYTAREMEHQFNDSGAKALVC------------LANMAHLAEKVLPkTGVKHvivTEVAD 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218563680 207 LHTVI---------------VTDSQQPGSFLLKDLMQAGssqHYQQLQDLQKKLvcDDPINIQFTSGTTGKPKGATLSHH 271
Cdd:PRK05677 156 MLPPLkrllinavvkhvkkmVPAYHLPQAVKFNDALAKG---AGQPVTEANPQA--DDVAVLQYTGGTTGVAKGAMLTHR 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218563680 272 NIVNNAYFTGMRIGYNWRKNVRICL-PVPLYHCFGSVGGGVIMALYGTTVIFPSTGYDGRANLRAIEKEKCTFVYGTPTM 350
Cdd:PRK05677 231 NLVANMLQCRALMGSNLNEGCEILIaPLPLYHIYAFTFHCMAMMLIGNHNILISNPRDLPAMVKELGKWKFSGFVGLNTL 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218563680 351 YIDMLGQPDLAKFDLSSVRGGIAAGSPCPPEVMRKILNVMGIkEMVIGYGTTENSPVTfCGFPVDSAErkIETVGCISPH 430
Cdd:PRK05677 311 FVALCNNEAFRKLDFSALKLTLSGGMALQLATAERWKEVTGC-AICEGYGMTETSPVV-SVNPSQAIQ--VGTIGIPVPS 386
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218563680 431 TEAKVVDPTtGEIVPLGAQGELMIRGYCVMLEYWQDEEKTRECITKDRWYKTGDIASLDQFAYCKIEGRIKDLIIRGGEN 510
Cdd:PRK05677 387 TLCKVIDDD-GNELPLGEVGELCVKGPQVMKGYWQRPEATDEILDSDGWLKTGDIALIQEDGYMRIVDRKKDMILVSGFN 465
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218563680 511 IYPAEIEQFLHTHPKILEAQVVGVKDERMGEEVCACIRLKEGQECTVEEIKAYCKGKIAHYKVPRYILFVQDYPLTITGK 590
Cdd:PRK05677 466 VYPNELEDVLAALPGVLQCAAIGVPDEKSGEAIKVFVVVKPGETLTKEQVMEHMRANLTGYKVPKAVEFRDELPTTNVGK 545
|
570
....*....|....*.
gi 218563680 591 IQKHKLRERTEKQLGL 606
Cdd:PRK05677 546 ILRRELRDEELKKAGL 561
|
|
| PRK08162 |
PRK08162 |
acyl-CoA synthetase; Validated |
72-599 |
2.27e-67 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236169 [Multi-domain] Cd Length: 545 Bit Score: 228.68 E-value: 2.27e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218563680 72 LQATVERYPDREAMVfvQDGIRKTFAEFYQDVEKAAAGLLAAGLKRGDRLGMWGPNIYEWVLMQFATAKAGIILVAVNPA 151
Cdd:PRK08162 24 LERAAEVYPDRPAVI--HGDRRRTWAETYARCRRLASALARRGIGRGDTVAVLLPNIPAMVEAHFGVPMAGAVLNTLNTR 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218563680 152 YQLQEVEFALRKVQCNAVVCPTKFksqhycdmlkqlcpeMETASPGgikSSRLPDLHTVIV-------TDSQQPGSFLLK 224
Cdd:PRK08162 102 LDAASIAFMLRHGEAKVLIVDTEF---------------AEVAREA---LALLPGPKPLVIdvddpeyPGGRFIGALDYE 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218563680 225 DLMQAGSSQHYQQLQDlqkklvcD--DPINIQFTSGTTGKPKGaTLSHH-----NIVNNAYFTGM--RIGYNWrknvric 295
Cdd:PRK08162 164 AFLASGDPDFAWTLPA-------DewDAIALNYTSGTTGNPKG-VVYHHrgaylNALSNILAWGMpkHPVYLW------- 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218563680 296 lPVPLYHCFGSVGGGVIMALYGTTVIFPStgYDGRANLRAIEKEKCTFVYGTPTMYIDMLGQPDLAKFDLSSVRGGIAAG 375
Cdd:PRK08162 229 -TLPMFHCNGWCFPWTVAARAGTNVCLRK--VDPKLIFDLIREHGVTHYCGAPIVLSALINAPAEWRAGIDHPVHAMVAG 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218563680 376 SPCPPEVMRKILNvMGIKEMVIgYGTTEN-SPVTFC-------GFPVDSAERKIETVGCISPHTEA-KVVDPTTGEIVPL 446
Cdd:PRK08162 306 AAPPAAVIAKMEE-IGFDLTHV-YGLTETyGPATVCawqpewdALPLDERAQLKARQGVRYPLQEGvTVLDPDTMQPVPA 383
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218563680 447 GAQ--GELMIRGYCVMLEYWQDEEKTRECItKDRWYKTGDIASLDQFAYCKIEGRIKDLIIRGGENIYPAEIEQFLHTHP 524
Cdd:PRK08162 384 DGEtiGEIMFRGNIVMKGYLKNPKATEEAF-AGGWFHTGDLAVLHPDGYIKIKDRSKDIIISGGENISSIEVEDVLYRHP 462
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 218563680 525 KILEAQVVGVKDERMGEEVCACIRLKEGQECTVEEIKAYCKGKIAHYKVPRYILFVQdYPLTITGKIQKHKLRER 599
Cdd:PRK08162 463 AVLVAAVVAKPDPKWGEVPCAFVELKDGASATEEEIIAHCREHLAGFKVPKAVVFGE-LPKTSTGKIQKFVLREQ 536
|
|
| PRK12406 |
PRK12406 |
long-chain-fatty-acid--CoA ligase; Provisional |
93-605 |
1.79e-66 |
|
long-chain-fatty-acid--CoA ligase; Provisional
Pssm-ID: 183506 [Multi-domain] Cd Length: 509 Bit Score: 225.35 E-value: 1.79e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218563680 93 RKTFAEFYQDVEKAAAGLLAAGLKRGDRLGMWGPNIYEWVLMQFATAKAGIILVAVNPAYQLQEVEFALRKvqcnavvCP 172
Cdd:PRK12406 11 RRSFDELAQRAARAAGGLAALGVRPGDCVALLMRNDFAFFEAAYAAMRLGAYAVPVNWHFKPEEIAYILED-------SG 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218563680 173 TKFKSQHyCDMLKQL-------CPEMETASPGGIKSS-RLPDLHTvivtdSQQPGSFLLKDLMQAGSSqhYQQLQDLQkk 244
Cdd:PRK12406 84 ARVLIAH-ADLLHGLasalpagVTVLSVPTPPEIAAAyRISPALL-----TPPAGAIDWEGWLAQQEP--YDGPPVPQ-- 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218563680 245 lvcddPINIQFTSGTTGKPKGATLSHHNIVNNAYFTGMRI-GYNWRKNVRICLPVPLYHCFGSVGGGVIMALYGTTVIFP 323
Cdd:PRK12406 154 -----PQSMIYTSGTTGHPKGVRRAAPTPEQAAAAEQMRAlIYGLKPGIRALLTGPLYHSAPNAYGLRAGRLGGVLVLQP 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218563680 324 StgYDGRANLRAIEKEKCTFVYGTPTMYIDMLGQPD--LAKFDLSSVRGGIAAGSPCPPEVMRKILNVMG--IKEMvigY 399
Cdd:PRK12406 229 R--FDPEELLQLIERHRITHMHMVPTMFIRLLKLPEevRAKYDVSSLRHVIHAAAPCPADVKRAMIEWWGpvIYEY---Y 303
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218563680 400 GTTENSPVTFCGfpVDSAERKIETVGCISPHTEAKVVDpTTGEIVPLGAQGELMIR--GYcVMLEYWQDEEKTREcITKD 477
Cdd:PRK12406 304 GSTESGAVTFAT--SEDALSHPGTVGKAAPGAELRFVD-EDGRPLPQGEIGEIYSRiaGN-PDFTYHNKPEKRAE-IDRG 378
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218563680 478 RWYKTGDIASLDQFAYCKIEGRIKDLIIRGGENIYPAEIEQFLHTHPKILEAQVVGVKDERMGEEVCACIRLKEGQECTV 557
Cdd:PRK12406 379 GFITSGDVGYLDADGYLFLCDRKRDMVISGGVNIYPAEIEAVLHAVPGVHDCAVFGIPDAEFGEALMAVVEPQPGATLDE 458
|
490 500 510 520
....*....|....*....|....*....|....*....|....*...
gi 218563680 558 EEIKAYCKGKIAHYKVPRYILFVQDYPLTITGKIQKHKLRERTEKQLG 605
Cdd:PRK12406 459 ADIRAQLKARLAGYKVPKHIEIMAELPREDSGKIFKRRLRDPYWANAG 506
|
|
| PRK07786 |
PRK07786 |
long-chain-fatty-acid--CoA ligase; Validated |
80-599 |
2.88e-66 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 169098 [Multi-domain] Cd Length: 542 Bit Score: 225.81 E-value: 2.88e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218563680 80 PDREAMVFVqdGIRKTFAEFYQDVEKAAAGLLAAGLKRGDRLGMWGPNIYEWVLMQFATAKAGIILVAVNPAYQLQEVEF 159
Cdd:PRK07786 31 PDAPALRFL--GNTTTWRELDDRVAALAGALSRRGVGFGDRVLILMLNRTEFVESVLAANMLGAIAVPVNFRLTPPEIAF 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218563680 160 ALRKVQCNAVVCPtkfksqhycDMLKQLCPEMETASPGgikssrlpdLHTVIVT-DSQQPGSFLLKDLMQAGSSQHyqQL 238
Cdd:PRK07786 109 LVSDCGAHVVVTE---------AALAPVATAVRDIVPL---------LSTVVVAgGSSDDSVLGYEDLLAEAGPAH--AP 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218563680 239 QDLQKklvcDDPINIQFTSGTTGKPKGATLSHHNIVNNAyFTGMR-IGYNWRKNVRIClPVPLYHC--FGSVGGGVImaL 315
Cdd:PRK07786 169 VDIPN----DSPALIMYTSGTTGRPKGAVLTHANLTGQA-MTCLRtNGADINSDVGFV-GVPLFHIagIGSMLPGLL--L 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218563680 316 YGTTVIFPSTGYDGRANLRAIEKEKCTFVYGTPTMYIDMLGQPDLAKFDLS-SVRGGIAAgsPCPPEVMRKILNVMGIKE 394
Cdd:PRK07786 241 GAPTVIYPLGAFDPGQLLDVLEAEKVTGIFLVPAQWQAVCAEQQARPRDLAlRVLSWGAA--PASDTLLRQMAATFPEAQ 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218563680 395 MVIGYGTTENSPVTfCGFPVDSAERKIETVGCISPHTEAKVVDPTTGEiVPLGAQGELMIRGYCVMLEYWQDEEKTRECI 474
Cdd:PRK07786 319 ILAAFGQTEMSPVT-CMLLGEDAIRKLGSVGKVIPTVAARVVDENMND-VPVGEVGEIVYRAPTLMSGYWNNPEATAEAF 396
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218563680 475 TKDrWYKTGDIASLDQFAYCKIEGRIKDLIIRGGENIYPAEIEQFLHTHPKILEAQVVGVKDERMGEEVCACIRLK-EGQ 553
Cdd:PRK07786 397 AGG-WFHSGDLVRQDEEGYVWVVDRKKDMIISGGENIYCAEVENVLASHPDIVEVAVIGRADEKWGEVPVAVAAVRnDDA 475
|
490 500 510 520
....*....|....*....|....*....|....*....|....*.
gi 218563680 554 ECTVEEIKAYCKGKIAHYKVPRYILFVQDYPLTITGKIQKHKLRER 599
Cdd:PRK07786 476 ALTLEDLAEFLTDRLARYKHPKALEIVDALPRNPAGKVLKTELRER 521
|
|
| BCL_4HBCL |
cd05959 |
Benzoate CoA ligase (BCL) and 4-Hydroxybenzoate-Coenzyme A Ligase (4-HBA-CoA ligase); Benzoate ... |
86-597 |
2.40e-65 |
|
Benzoate CoA ligase (BCL) and 4-Hydroxybenzoate-Coenzyme A Ligase (4-HBA-CoA ligase); Benzoate CoA ligase and 4-hydroxybenzoate-coenzyme A ligase catalyze the first activating step for benzoate and 4-hydroxybenzoate catabolic pathways, respectively. Although these two enzymes share very high sequence homology, they have their own substrate preference. The reaction proceeds via a two-step process; the first ATP-dependent step forms the substrate-AMP intermediate, while the second step forms the acyl-CoA ester, releasing the AMP. Aromatic compounds represent the second most abundant class of organic carbon compounds after carbohydrates. Some bacteria can use benzoic acid or benzenoid compounds as the sole source of carbon and energy through degradation. Benzoate CoA ligase and 4-hydroxybenzoate-Coenzyme A ligase are key enzymes of this process.
Pssm-ID: 341269 [Multi-domain] Cd Length: 508 Bit Score: 222.63 E-value: 2.40e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218563680 86 VFVQDGIRKTFAEFYQDVEKAAAGLLAAGLKRGDRLGMWGPNIYEWVLMQFATAKAGIILVAVNPAYQLQEVEFALRKVQ 165
Cdd:cd05959 22 AFIDDAGSLTYAELEAEARRVAGALRALGVKREERVLLIMLDTVDFPTAFLGAIRAGIVPVPVNTLLTPDDYAYYLEDSR 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218563680 166 CNAVVCptkfkSQHYCDMLKQLCPEMEtaspggikssrlPDLHTVIVTDSQQPgsfllkdlmQAGSSQHYQQLQDLQKKL 245
Cdd:cd05959 102 ARVVVV-----SGELAPVLAAALTKSE------------HTLVVLIVSGGAGP---------EAGALLLAELVAAEAEQL 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218563680 246 V-----CDDPINIQFTSGTTGKPKGATLSHHNIVNNAYFTGMRIGYNWRKNVriCLPVP-LYHCFGsVGGGVI--MALYG 317
Cdd:cd05959 156 KpaathADDPAFWLYSSGSTGRPKGVVHLHADIYWTAELYARNVLGIREDDV--CFSAAkLFFAYG-LGNSLTfpLSVGA 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218563680 318 TTVIFPstgydGR----ANLRAIEKEKCTFVYGTPTMYIDMLGQPDLAKFDLSSVRGGIAAGSPCPPEVMRKILNVMGIk 393
Cdd:cd05959 233 TTVLMP-----ERptpaAVFKRIRRYRPTVFFGVPTLYAAMLAAPNLPSRDLSSLRLCVSAGEALPAEVGERWKARFGL- 306
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218563680 394 EMVIGYGTTENSPVTFCGFPVDSaerKIETVGCISPHTEAKVVDPTtGEIVPLGAQGELMIRGYCVMLEYWQDEEKTREC 473
Cdd:cd05959 307 DILDGIGSTEMLHIFLSNRPGRV---RYGTTGKPVPGYEVELRDED-GGDVADGEPGELYVRGPSSATMYWNNRDKTRDT 382
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218563680 474 ItKDRWYKTGDIASLDQFAYCKIEGRIKDLIIRGGENIYPAEIEQFLHTHPKILEAQVVGVKDERMGEEVCACIRLKEGQ 553
Cdd:cd05959 383 F-QGEWTRTGDKYVRDDDGFYTYAGRADDMLKVSGIWVSPFEVESALVQHPAVLEAAVVGVEDEDGLTKPKAFVVLRPGY 461
|
490 500 510 520
....*....|....*....|....*....|....*....|....*..
gi 218563680 554 ECT---VEEIKAYCKGKIAHYKVPRYILFVQDYPLTITGKIQKHKLR 597
Cdd:cd05959 462 EDSealEEELKEFVKDRLAPYKYPRWIVFVDELPKTATGKIQRFKLR 508
|
|
| PRK08751 |
PRK08751 |
long-chain fatty acid--CoA ligase; |
64-598 |
3.11e-65 |
|
long-chain fatty acid--CoA ligase;
Pssm-ID: 181546 [Multi-domain] Cd Length: 560 Bit Score: 223.60 E-value: 3.11e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218563680 64 QSSTVDQCLQATVERYPDREAmvFVQDGIRKTFAEFYQDVEK-AAAGLLAAGLKRGDRLGMWGPNIYEWVLMQFATAKAG 142
Cdd:PRK08751 23 QFRTVAEVFATSVAKFADRPA--YHSFGKTITYREADQLVEQfAAYLLGELQLKKGDRVALMMPNCLQYPIATFGVLRAG 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218563680 143 IILVAVNPAYQLQEVEFALRKVQCNAVVCPTKFksqhyCDMLKQLCPEMETASpggIKSSRLPDLHTV------------ 210
Cdd:PRK08751 101 LTVVNVNPLYTPRELKHQLIDSGASVLVVIDNF-----GTTVQQVIADTPVKQ---VITTGLGDMLGFpkaalvnfvvky 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218563680 211 ---IVTDSQQPGSFLLKDLMQAGSSQHYQQLQdlqkkLVCDDPINIQFTSGTTGKPKGATLSHHNIVNNayftgMRIGYN 287
Cdd:PRK08751 173 vkkLVPEYRINGAIRFREALALGRKHSMPTLQ-----IEPDDIAFLQYTGGTTGVAKGAMLTHRNLVAN-----MQQAHQ 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218563680 288 W--------RKNVRICLPVPLYHCFGSVGGGVIMALYGTTVIFPSTGYDGRANLRAIEKEKCTFVYGTPTMYIDMLGQPD 359
Cdd:PRK08751 243 WlagtgkleEGCEVVITALPLYHIFALTANGLVFMKIGGCNHLISNPRDMPGFVKELKKTRFTAFTGVNTLFNGLLNTPG 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218563680 360 LAKFDLSSVRGGIAAGSPCPPEVMRKILNVMGIKeMVIGYGTTENSPVTfCGFPVDSAERKiETVGCISPHTEAKVVDpT 439
Cdd:PRK08751 323 FDQIDFSSLKMTLGGGMAVQRSVAERWKQVTGLT-LVEAYGLTETSPAA-CINPLTLKEYN-GSIGLPIPSTDACIKD-D 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218563680 440 TGEIVPLGAQGELMIRGYCVMLEYWQDEEKTRECITKDRWYKTGDIASLDQFAYCKIEGRIKDLIIRGGENIYPAEIEQF 519
Cdd:PRK08751 399 AGTVLAIGEIGELCIKGPQVMKGYWKRPEETAKVMDADGWLHTGDIARMDEQGFVYIVDRKKDMILVSGFNVYPNEIEDV 478
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 218563680 520 LHTHPKILEAQVVGVKDERMGEEVCACIrLKEGQECTVEEIKAYCKGKIAHYKVPRYILFVQDYPLTITGKIQKHKLRE 598
Cdd:PRK08751 479 IAMMPGVLEVAAVGVPDEKSGEIVKVVI-VKKDPALTAEDVKAHARANLTGYKQPRIIEFRKELPKTNVGKILRRELRD 556
|
|
| PRK07529 |
PRK07529 |
AMP-binding domain protein; Validated |
72-599 |
3.28e-65 |
|
AMP-binding domain protein; Validated
Pssm-ID: 236043 [Multi-domain] Cd Length: 632 Bit Score: 225.22 E-value: 3.28e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218563680 72 LQATVERYPDREAMVFVQDGIRK------TFAEFYQDVEKAAAGLLAAGLKRGDRLGMWGPNIYEWVLMQFATAKAGIIl 145
Cdd:PRK07529 31 LSRAAARHPDAPALSFLLDADPLdrpetwTYAELLADVTRTANLLHSLGVGPGDVVAFLLPNLPETHFALWGGEAAGIA- 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218563680 146 VAVNP---AYQLQEVefaLRKVQCNAVVCPTKFKSQhycDMLKQLCPEMEtaspggikssRLPDLHTVIVTDSQQ--PGS 220
Cdd:PRK07529 110 NPINPllePEQIAEL---LRAAGAKVLVTLGPFPGT---DIWQKVAEVLA----------ALPELRTVVEVDLARylPGP 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218563680 221 FLLKDLMQAGSSQH----YQQLQDLQK--KLVCDDPINIQ-----F-TSGTTGKPKGATLSHHNIVNNAYFTGMRIGYNw 288
Cdd:PRK07529 174 KRLAVPLIRRKAHArildFDAELARQPgdRLFSGRPIGPDdvaayFhTGGTTGMPKLAQHTHGNEVANAWLGALLLGLG- 252
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218563680 289 RKNVRIClPVPLYHCFGSVGGGVIMALYGTTVIFPS-TGYDGR---ANL-RAIEKEKCTFVYGTPTMYIDMLGQPdLAKF 363
Cdd:PRK07529 253 PGDTVFC-GLPLFHVNALLVTGLAPLARGAHVVLATpQGYRGPgviANFwKIVERYRINFLSGVPTVYAALLQVP-VDGH 330
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218563680 364 DLSSVRGGIAAGSPCPPEVMRKILNVMGIKeMVIGYGTTENSPVTFCGFPvdSAERKIETVGCISPHTEAKVV--DPTTG 441
Cdd:PRK07529 331 DISSLRYALCGAAPLPVEVFRRFEAATGVR-IVEGYGLTEATCVSSVNPP--DGERRIGSVGLRLPYQRVRVVilDDAGR 407
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218563680 442 EIVPLGAQ--GELMIRGYCVMLEYwQDEEKTRECITKDRWYKTGDIASLDQFAYCKIEGRIKDLIIRGGENIYPAEIEQF 519
Cdd:PRK07529 408 YLRDCAVDevGVLCIAGPNVFSGY-LEAAHNKGLWLEDGWLNTGDLGRIDADGYFWLTGRAKDLIIRGGHNIDPAAIEEA 486
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218563680 520 LHTHPKILEAQVVGVKDERMGEEVCACIRLKEGQECTVEEIKAYCKGKIAH-YKVPRYILFVQDYPLTITGKIQKHKLRE 598
Cdd:PRK07529 487 LLRHPAVALAAAVGRPDAHAGELPVAYVQLKPGASATEAELLAFARDHIAErAAVPKHVRILDALPKTAVGKIFKPALRR 566
|
.
gi 218563680 599 R 599
Cdd:PRK07529 567 D 567
|
|
| PRK06164 |
PRK06164 |
acyl-CoA synthetase; Validated |
72-604 |
1.30e-64 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 235722 [Multi-domain] Cd Length: 540 Bit Score: 221.54 E-value: 1.30e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218563680 72 LQATVERYPDreAMVFVQDGIRKTFAEFYQDVEKAAAGLLAAGLKRGDRLGMWGPNIYEWVLMQFATAKAGIILVAVNPA 151
Cdd:PRK06164 16 LDAHARARPD--AVALIDEDRPLSRAELRALVDRLAAWLAAQGVRRGDRVAVWLPNCIEWVVLFLACARLGATVIAVNTR 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218563680 152 YQLQEVEFALRKVQCNAVVCPTKFKSQHYCDMLkqlcpemetaspGGIKSSRLPDLHTVIVTD---SQQPGSFLLKDLMQ 228
Cdd:PRK06164 94 YRSHEVAHILGRGRARWLVVWPGFKGIDFAAIL------------AAVPPDALPPLRAIAVVDdaaDATPAPAPGARVQL 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218563680 229 AGssQHYQQ-LQDLQKKLVCDDPINIQF-TSGTTGKPK-----GATLSHHN-IVNNAYftgmriGYNwrKNVRICLPVPL 300
Cdd:PRK06164 162 FA--LPDPApPAAAGERAADPDAGALLFtTSGTTSGPKlvlhrQATLLRHArAIARAY------GYD--PGAVLLAALPF 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218563680 301 YHCFGSVGGGVIMALYGTTVIFPStgYDGRANLRAIEKEKCTFVYGTPTMYIDMLGQPDLAKfDLSSVRG-GIAAGSPCP 379
Cdd:PRK06164 232 CGVFGFSTLLGALAGGAPLVCEPV--FDAARTARALRRHRVTHTFGNDEMLRRILDTAGERA-DFPSARLfGFASFAPAL 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218563680 380 PEVMRKILNvmgiKEMVIG--YGTTENSPVtFCGFPVDSAER-KIETVGC-ISPHTEAKVVDPTTGEIVPLGAQGELMIR 455
Cdd:PRK06164 309 GELAALARA----RGVPLTglYGSSEVQAL-VALQPATDPVSvRIEGGGRpASPEARVRARDPQDGALLPDGESGEIEIR 383
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218563680 456 GYCVMLEYWQDEEKTRECITKDRWYKTGDIASL---DQFAYckiEGRIKDLIIRGGENIYPAEIEQFLHTHPKILEAQVV 532
Cdd:PRK06164 384 APSLMRGYLDNPDATARALTDDGYFRTGDLGYTrgdGQFVY---QTRMGDSLRLGGFLVNPAEIEHALEALPGVAAAQVV 460
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 218563680 533 GVkdERMGEEVC-ACIRLKEGQECTVEEIKAYCKGKIAHYKVPRYILFVQDYPLTITG---KIQKHKLRERTEKQL 604
Cdd:PRK06164 461 GA--TRDGKTVPvAFVIPTDGASPDEAGLMAACREALAGFKVPARVQVVEAFPVTESAngaKIQKHRLREMAQARL 534
|
|
| FAA1 |
COG1022 |
Long-chain acyl-CoA synthetase (AMP-forming) [Lipid transport and metabolism]; |
67-538 |
1.35e-64 |
|
Long-chain acyl-CoA synthetase (AMP-forming) [Lipid transport and metabolism];
Pssm-ID: 440645 [Multi-domain] Cd Length: 603 Bit Score: 222.67 E-value: 1.35e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218563680 67 TVDQCLQATVERYPDREAMVFVQDGIRK--TFAEFYQDVEKAAAGLLAAGLKRGDRLGMWGPNIYEWVLMQFATAKAGII 144
Cdd:COG1022 12 TLPDLLRRRAARFPDRVALREKEDGIWQslTWAEFAERVRALAAGLLALGVKPGDRVAILSDNRPEWVIADLAILAAGAV 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218563680 145 LVAVNPAYQLQEVEFALRKVQCNAVVCPTKfksqhycDMLKQLCPEMEtaspggikssRLPDLHTVIVTD----SQQPGS 220
Cdd:COG1022 92 TVPIYPTSSAEEVAYILNDSGAKVLFVEDQ-------EQLDKLLEVRD----------ELPSLRHIVVLDprglRDDPRL 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218563680 221 FLLKDLMQAGSS-QHYQQLQDLQKKLVCDDPINIQFTSGTTGKPKGATLSHHNIVNNAyftgmrigynwrKNVRICLPV- 298
Cdd:COG1022 155 LSLDELLALGREvADPAELEARRAAVKPDDLATIIYTSGTTGRPKGVMLTHRNLLSNA------------RALLERLPLg 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218563680 299 ---------PLYHCFGSVGGGVIMAlYGTTVIFPStgyDGR---ANLRAIekeKCTFVYGTP--------TMYIDMLGQP 358
Cdd:COG1022 223 pgdrtlsflPLAHVFERTVSYYALA-AGATVAFAE---SPDtlaEDLREV---KPTFMLAVPrvwekvyaGIQAKAEEAG 295
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218563680 359 DLAK--FD----------------------------------LSSVR---GG-----IAAGSPCPPEVMRkILNVMGIKe 394
Cdd:COG1022 296 GLKRklFRwalavgrryararlagkspslllrlkhaladklvFSKLRealGGrlrfaVSGGAALGPELAR-FFRALGIP- 373
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218563680 395 MVIGYGTTENSPVTFCGFPvdsAERKIETVGCISPHTEAKvvdpttgeivpLGAQGELMIRGYCVMLEYWQDEEKTRECI 474
Cdd:COG1022 374 VLEGYGLTETSPVITVNRP---GDNRIGTVGPPLPGVEVK-----------IAEDGEILVRGPNVMKGYYKNPEATAEAF 439
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 218563680 475 TKDRWYKTGDIASLDQFAYCKIEGRIKDLII-RGGENIYPAEIEQFLHTHPKILEAQVVGvkDER 538
Cdd:COG1022 440 DADGWLHTGDIGELDEDGFLRITGRKKDLIVtSGGKNVAPQPIENALKASPLIEQAVVVG--DGR 502
|
|
| PRK08974 |
PRK08974 |
long-chain-fatty-acid--CoA ligase FadD; |
65-604 |
1.93e-64 |
|
long-chain-fatty-acid--CoA ligase FadD;
Pssm-ID: 236359 [Multi-domain] Cd Length: 560 Bit Score: 221.47 E-value: 1.93e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218563680 65 SSTVDQCLQAtVERYPDREAmvFVQDG----IRK------TFAEFYQDVEKAaagllaaglKRGDRLGMWGPNIYEWVLM 134
Cdd:PRK08974 23 QSLVDMFEQA-VARYADQPA--FINMGevmtFRKleersrAFAAYLQNGLGL---------KKGDRVALMMPNLLQYPIA 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218563680 135 QFATAKAGIILVAVNPAYQLQEVEFALRKVQCNAVVCPTKFKSQhycdmLKQLCPEMEtaspggIKS---SRLPDL---- 207
Cdd:PRK08974 91 LFGILRAGMIVVNVNPLYTPRELEHQLNDSGAKAIVIVSNFAHT-----LEKVVFKTP------VKHvilTRMGDQlsta 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218563680 208 -HTVI----------VTDSQQPGSFLLKDLMQAGssqhyQQLQDLQKKLVCDDPINIQFTSGTTGKPKGATLSHHNIVNN 276
Cdd:PRK08974 160 kGTLVnfvvkyikrlVPKYHLPDAISFRSALHKG-----RRMQYVKPELVPEDLAFLQYTGGTTGVAKGAMLTHRNMLAN 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218563680 277 ------AYFTGMRIGYNWrknvrICLPVPLYHCFG-SVGGGVIMALYGTTVIFpSTGYDGRANLRAIEKEKCTFVYGTPT 349
Cdd:PRK08974 235 leqakaAYGPLLHPGKEL-----VVTALPLYHIFAlTVNCLLFIELGGQNLLI-TNPRDIPGFVKELKKYPFTAITGVNT 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218563680 350 MYIDMLGQPDLAKFDLSSVRGGIAAGSPCPPEVMRKILNVMGiKEMVIGYGTTENSP-VTFCgfPVDSAERKiETVGCIS 428
Cdd:PRK08974 309 LFNALLNNEEFQELDFSSLKLSVGGGMAVQQAVAERWVKLTG-QYLLEGYGLTECSPlVSVN--PYDLDYYS-GSIGLPV 384
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218563680 429 PHTEAKVVDpTTGEIVPLGAQGELMIRGYCVMLEYWQDEEKTRECItKDRWYKTGDIASLDQFAYCKIEGRIKDLIIRGG 508
Cdd:PRK08974 385 PSTEIKLVD-DDGNEVPPGEPGELWVKGPQVMLGYWQRPEATDEVI-KDGWLATGDIAVMDEEGFLRIVDRKKDMILVSG 462
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218563680 509 ENIYPAEIEQFLHTHPKILEAQVVGVKDERMGEEVCACIrLKEGQECTVEEIKAYCKGKIAHYKVPRYILFVQDYPLTIT 588
Cdd:PRK08974 463 FNVYPNEIEDVVMLHPKVLEVAAVGVPSEVSGEAVKIFV-VKKDPSLTEEELITHCRRHLTGYKVPKLVEFRDELPKSNV 541
|
570
....*....|....*.
gi 218563680 589 GKIQKHKLRERTEKQL 604
Cdd:PRK08974 542 GKILRRELRDEARAKV 557
|
|
| PRK09088 |
PRK09088 |
acyl-CoA synthetase; Validated |
80-600 |
2.78e-64 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 181644 [Multi-domain] Cd Length: 488 Bit Score: 219.29 E-value: 2.78e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218563680 80 PDREAMVFVQDGIRKTFAEFYQDVEKAAAGLLAAGLKRGDRLGMWGPNIYEWVLMQFATAKAGIILVAVNpaYQLQEVEF 159
Cdd:PRK09088 9 PQRLAAVDLALGRRWTYAELDALVGRLAAVLRRRGCVDGERLAVLARNSVWLVALHFACARVGAIYVPLN--WRLSASEL 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218563680 160 -ALrkvqcnavvcptkfksqhycdmlkqlcpeMETASPggikssrlpdlhTVIVTDSQ-QPGSFLLKDLmqAGSSQHYQQ 237
Cdd:PRK09088 87 dAL-----------------------------LQDAEP------------RLLLGDDAvAAGRTDVEDL--AAFIASADA 123
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218563680 238 LQ-DLQKKLVCDDPINIQFTSGTTGKPKGATLSHHNIVNNAYFTGmRIGYNWRKNVRIClPVPLYHCFGSVGGGVIMALY 316
Cdd:PRK09088 124 LEpADTPSIPPERVSLILFTSGTSGQPKGVMLSERNLQQTAHNFG-VLGRVDAHSSFLC-DAPMFHIIGLITSVRPVLAV 201
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218563680 317 GTTVIFpSTGYDGRANLRAIEKEK--CTFVYGTPTMYIDMLGQPDLAKFDLSSVRGGIAAGSPCPPEVMRKILNvMGIKe 394
Cdd:PRK09088 202 GGSILV-SNGFEPKRTLGRLGDPAlgITHYFCVPQMAQAFRAQPGFDAAALRHLTALFTGGAPHAAEDILGWLD-DGIP- 278
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218563680 395 MVIGYGTTENSpvTFCGFPVDSA--ERKIETVGCISPHTEAKVVDpTTGEIVPLGAQGELMIRGYCVMLEYWQDEEKTRE 472
Cdd:PRK09088 279 MVDGFGMSEAG--TVFGMSVDCDviRAKAGAAGIPTPTVQTRVVD-DQGNDCPAGVPGELLLRGPNLSPGYWRRPQATAR 355
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218563680 473 CITKDRWYKTGDIASLDQFAYCKIEGRIKDLIIRGGENIYPAEIEQFLHTHPKILEAQVVGVKDERMGEEVCACIRLKEG 552
Cdd:PRK09088 356 AFTGDGWFRTGDIARRDADGFFWVVDRKKDMFISGGENVYPAEIEAVLADHPGIRECAVVGMADAQWGEVGYLAIVPADG 435
|
490 500 510 520
....*....|....*....|....*....|....*....|....*...
gi 218563680 553 QECTVEEIKAYCKGKIAHYKVPRYILFVQDYPLTITGKIQKHKLRERT 600
Cdd:PRK09088 436 APLDLERIRSHLSTRLAKYKVPKHLRLVDALPRTASGKLQKARLRDAL 483
|
|
| CBAL |
cd05923 |
4-Chlorobenzoate-CoA ligase (CBAL); CBAL catalyzes the conversion of 4-chlorobenzoate (4-CB) ... |
67-596 |
2.11e-63 |
|
4-Chlorobenzoate-CoA ligase (CBAL); CBAL catalyzes the conversion of 4-chlorobenzoate (4-CB) to 4-chlorobenzoyl-coenzyme A (4-CB-CoA) by the two-step adenylation and thioester-forming reactions. 4-Chlorobenzoate (4-CBA) is an environmental pollutant derived from microbial breakdown of aromatic pollutants, such as polychlorinated biphenyls (PCBs), DDT, and certain herbicides. The 4-CBA degrading pathway converts 4-CBA to the metabolite 4-hydroxybezoate (4-HBA), allowing some soil-dwelling microbes to utilize 4-CBA as an alternate carbon source. This pathway consists of three chemical steps catalyzed by 4-CBA-CoA ligase, 4-CBA-CoA dehalogenase, and 4HBA-CoA thioesterase in sequential reactions.
Pssm-ID: 341247 [Multi-domain] Cd Length: 493 Bit Score: 216.99 E-value: 2.11e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218563680 67 TVDQCLQATVERYPDREAMVFVQDGIRKTFAEFYQDVEKAAAGLLAAGLKRGDRLGMWGPNIYEWVLMQFATAKAGIILV 146
Cdd:cd05923 2 TVFEMLRRAASRAPDACAIADPARGLRLTYSELRARIEAVAARLHARGLRPGQRVAVVLPNSVEAVIALLALHRLGAVPA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218563680 147 AVNPAYQLQEVEFALRKVQ-CNAVVCPTKFKSQhyCDMLKQLCPEMETASPGgiksSRLPDLHTVIVTDSQ-QPGsfllk 224
Cdd:cd05923 82 LINPRLKAAELAELIERGEmTAAVIAVDAQVMD--AIFQSGVRVLALSDLVG----LGEPESAGPLIEDPPrEPE----- 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218563680 225 dlmqagssqhyqqlqdlqkklvcdDPINIQFTSGTTGKPKGATLSHHNIVNNAYFTGMRIGYNW-RKNVRICLpVPLYHC 303
Cdd:cd05923 151 ------------------------QPAFVFYTSGTTGLPKGAVIPQRAAESRVLFMSTQAGLRHgRHNVVLGL-MPLYHV 205
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218563680 304 FGsVGGGVIMALYGTTVIFPSTGYDGRANLRAIEKEKCTFVYGTPTMYIDMLGQPDLAKFDLSSVRGGIAAGSPCPPEVM 383
Cdd:cd05923 206 IG-FFAVLVAALALDGTYVVVEEFDPADALKLIEQERVTSLFATPTHLDALAAAAEFAGLKLSSLRHVTFAGATMPDAVL 284
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218563680 384 RKILNVMGIKEMVIgYGTTENSPVTFCGFPvdsaerKIETVGCISPHTEAKVVD--PTTGEIVPLGAQGELMIR--GYCV 459
Cdd:cd05923 285 ERVNQHLPGEKVNI-YGTTEAMNSLYMRDA------RTGTEMRPGFFSEVRIVRigGSPDEALANGEEGELIVAaaADAA 357
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218563680 460 MLEYWQDEEKTRECItKDRWYKTGDIASLDQFAYCKIEGRIKDLIIRGGENIYPAEIEQFLHTHPKILEAQVVGVKDERM 539
Cdd:cd05923 358 FTGYLNQPEATAKKL-QDGWYRTGDVGYVDPSGDVRILGRVDDMIISGGENIHPSEIERVLSRHPGVTEVVVIGVADERW 436
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*...
gi 218563680 540 GEEVCACIRLKEGQeCTVEEIKAYCK-GKIAHYKVPRYILFVQDYPLTITGKIQKHKL 596
Cdd:cd05923 437 GQSVTACVVPREGT-LSADELDQFCRaSELADFKRPRRYFFLDELPKNAMNKVLRRQL 493
|
|
| OSB_CoA_lg |
cd05912 |
O-succinylbenzoate-CoA ligase (also known as O-succinylbenzoate-CoA synthase, OSB-CoA ... |
236-598 |
5.33e-63 |
|
O-succinylbenzoate-CoA ligase (also known as O-succinylbenzoate-CoA synthase, OSB-CoA synthetase, or MenE); O-succinylbenzoic acid-CoA synthase catalyzes the coenzyme A (CoA)- and ATP-dependent conversion of o-succinylbenzoic acid to o-succinylbenzoyl-CoA. The reaction is the fourth step of the biosynthesis pathway of menaquinone (vitamin K2). In certain bacteria, menaquinone is used during fumarate reduction in anaerobic respiration. In cyanobacteria, the product of the menaquinone pathway is phylloquinone (2-methyl-3-phytyl-1,4-naphthoquinone), a molecule used exclusively as an electron transfer cofactor in Photosystem 1. In green sulfur bacteria and heliobacteria, menaquinones are used as loosely bound secondary electron acceptors in the photosynthetic reaction center.
Pssm-ID: 341238 [Multi-domain] Cd Length: 411 Bit Score: 213.36 E-value: 5.33e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218563680 236 QQLQDLQKKlvCDDPINIQFTSGTTGKPKGATLSHHNIVNNAYFTGMRIGYNwrKNVRICLPVPLYHcfgsVGGGVIM-- 313
Cdd:cd05912 67 FQLKDSDVK--LDDIATIMYTSGTTGKPKGVQQTFGNHWWSAIGSALNLGLT--EDDNWLCALPLFH----ISGLSILmr 138
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218563680 314 -ALYGTTVIFPSTgYDGRANLRAIEKEKCTFVYGTPTMYIDMLGQpdLAKFDLSSVRGGIAAGSPCPPEVMRKILNvMGI 392
Cdd:cd05912 139 sVIYGMTVYLVDK-FDAEQVLHLINSGKVTIISVVPTMLQRLLEI--LGEGYPNNLRCILLGGGPAPKPLLEQCKE-KGI 214
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218563680 393 KeMVIGYGTTENSPvTFCGFPVDSAERKIETVGCISPHTEAKVVDPTtgeiVPLGAQGELMIRGYCVMLEYWQDEEKTRE 472
Cdd:cd05912 215 P-VYQSYGMTETCS-QIVTLSPEDALNKIGSAGKPLFPVELKIEDDG----QPPYEVGEILLKGPNVTKGYLNRPDATEE 288
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218563680 473 CItKDRWYKTGDIASLDQFAYCKIEGRIKDLIIRGGENIYPAEIEQFLHTHPKILEAQVVGVKDERMGEEVCACIRLKeg 552
Cdd:cd05912 289 SF-ENGWFKTGDIGYLDEEGFLYVLDRRSDLIISGGENIYPAEIEEVLLSHPAIKEAGVVGIPDDKWGQVPVAFVVSE-- 365
|
330 340 350 360
....*....|....*....|....*....|....*....|....*.
gi 218563680 553 QECTVEEIKAYCKGKIAHYKVPRYILFVQDYPLTITGKIQKHKLRE 598
Cdd:cd05912 366 RPISEEELIAYCSEKLAKYKVPKKIYFVDELPRTASGKLLRHELKQ 411
|
|
| PRK13391 |
PRK13391 |
acyl-CoA synthetase; Provisional |
76-599 |
1.45e-62 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 184022 [Multi-domain] Cd Length: 511 Bit Score: 214.94 E-value: 1.45e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218563680 76 VERYPDREAMVFVQDGIRKTFAEFYQDVEKAAAGLLAAGLKRGDRLGMWGPNIYEWVLMQFATAKAGIILVAVNPAYQLQ 155
Cdd:PRK13391 7 AQTTPDKPAVIMASTGEVVTYRELDERSNRLAHLFRSLGLKRGDHVAIFMENNLRYLEVCWAAERSGLYYTCVNSHLTPA 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218563680 156 EVEFALRKVQCNAVVCptkfKSQHYcdmlkQLCPEMETASPGGikssrLPDLhtVIVTDSQQPGsfllkdlmqagssqhY 235
Cdd:PRK13391 87 EAAYIVDDSGARALIT----SAAKL-----DVARALLKQCPGV-----RHRL--VLDGDGELEG---------------F 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218563680 236 QQLQDLQKKLVcDDPI-------NIQFTSGTTGKPKG--ATLSHHNIVNNAYFTGM-RIGYNWRKNVRICLPVPLYHCFG 305
Cdd:PRK13391 136 VGYAEAVAGLP-ATPIadeslgtDMLYSSGTTGRPKGikRPLPEQPPDTPLPLTAFlQRLWGFRSDMVYLSPAPLYHSAP 214
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218563680 306 SVGGGVIMALYGTTVIFPStgYDGRANLRAIEKEKCTFVYGTPTMYIDMLGQPDLA--KFDLSSVRGGIAAGSPCPPEVM 383
Cdd:PRK13391 215 QRAVMLVIRLGGTVIVMEH--FDAEQYLALIEEYGVTHTQLVPTMFSRMLKLPEEVrdKYDLSSLEVAIHAAAPCPPQVK 292
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218563680 384 RKILNVMG--IKEMvigYGTTENSPVTFCgfpvDSAERKIE--TVGCI---SPHteakVVDPTtGEIVPLGAQGELMIRG 456
Cdd:PRK13391 293 EQMIDWWGpiIHEY---YAATEGLGFTAC----DSEEWLAHpgTVGRAmfgDLH----ILDDD-GAELPPGEPGTIWFEG 360
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218563680 457 yCVMLEYWQDEEKTRECITKDR-WYKTGDIASLDQFAYCKIEGRIKDLIIRGGENIYPAEIEQFLHTHPKILEAQVVGVK 535
Cdd:PRK13391 361 -GRPFEYLNDPAKTAEARHPDGtWSTVGDIGYVDEDGYLYLTDRAAFMIISGGVNIYPQEAENLLITHPKVADAAVFGVP 439
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 218563680 536 DERMGEEVCACIRLKEGQECTV---EEIKAYCKGKIAHYKVPRYILFVQDYPLTITGKIQKHKLRER 599
Cdd:PRK13391 440 NEDLGEEVKAVVQPVDGVDPGPalaAELIAFCRQRLSRQKCPRSIDFEDELPRLPTGKLYKRLLRDR 506
|
|
| FACL_like_4 |
cd05944 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
256-597 |
3.21e-61 |
|
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ATP-dependent activation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions.
Pssm-ID: 341266 [Multi-domain] Cd Length: 359 Bit Score: 207.33 E-value: 3.21e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218563680 256 TSGTTGKPKGATLSHHNIVNNAYFTGMRIGYNWRKNVrIClPVPLYHCFGSVGGGVIMALYGTTVIFPS-TGYDGRA--- 331
Cdd:cd05944 10 TGGTTGTPKLAQHTHSNEVYNAWMLALNSLFDPDDVL-LC-GLPLFHVNGSVVTLLTPLASGAHVVLAGpAGYRNPGlfd 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218563680 332 NL-RAIEKEKCTFVYGTPTMYIDMLGQPDLAkfDLSSVRGGIAAGSPCPPEVMRKILNVMGIKeMVIGYGTTENSPVTFC 410
Cdd:cd05944 88 NFwKLVERYRITSLSTVPTVYAALLQVPVNA--DISSLRFAMSGAAPLPVELRARFEDATGLP-VVEGYGLTEATCLVAV 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218563680 411 GFPvdSAERKIETVGCISPHTEAKVV--DPTTGEIVPLGAQ--GELMIRGYCVMLEYWQDEEKtRECITKDRWYKTGDIA 486
Cdd:cd05944 165 NPP--DGPKRPGSVGLRLPYARVRIKvlDGVGRLLRDCAPDevGEICVAGPGVFGGYLYTEGN-KNAFVADGWLNTGDLG 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218563680 487 SLDQFAYCKIEGRIKDLIIRGGENIYPAEIEQFLHTHPKILEAQVVGVKDERMGEEVCACIRLKEGQECTVEEIKAYCKG 566
Cdd:cd05944 242 RLDADGYLFITGRAKDLIIRGGHNIDPALIEEALLRHPAVAFAGAVGQPDAHAGELPVAYVQLKPGAVVEEEELLAWARD 321
|
330 340 350
....*....|....*....|....*....|..
gi 218563680 567 KIAHY-KVPRYILFVQDYPLTITGKIQKHKLR 597
Cdd:cd05944 322 HVPERaAVPKHIEVLEELPVTAVGKVFKPALR 353
|
|
| PRK06145 |
PRK06145 |
acyl-CoA synthetase; Validated |
78-601 |
8.75e-61 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 102207 [Multi-domain] Cd Length: 497 Bit Score: 210.13 E-value: 8.75e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218563680 78 RYPDREAMVFVQDGIrkTFAEFYQDVEKAAAGLLAAGLKRGDRLGMWGPNIYEWVLMQFATAKAGIILVAVNpaYQLQEV 157
Cdd:PRK06145 14 RTPDRAALVYRDQEI--SYAEFHQRILQAAGMLHARGIGQGDVVALLMKNSAAFLELAFAASYLGAVFLPIN--YRLAAD 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218563680 158 EFALRKVQCNAvvcptkfksqhycdmlKQLCPEMETASPGGIKssrlpdlHTVIVTDSQ-QPGSFLLKDLMQAGSSQHYQ 236
Cdd:PRK06145 90 EVAYILGDAGA----------------KLLLVDEEFDAIVALE-------TPKIVIDAAaQADSRRLAQGGLEIPPQAAV 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218563680 237 QLQDLQKklvcddpinIQFTSGTTGKPKGATLSHHNIVNNAYFTGMRIGYNwrKNVRICLPVPLYHcfgsVG-----GGV 311
Cdd:PRK06145 147 APTDLVR---------LMYTSGTTDRPKGVMHSYGNLHWKSIDHVIALGLT--ASERLLVVGPLYH----VGafdlpGIA 211
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218563680 312 IMALYGTTVIfpSTGYDGRANLRAIEKEKCTFVYGTPTMYIDMLGQPDLAKFDLSSVRGGIAAGSPCPPEVMRKILNVMG 391
Cdd:PRK06145 212 VLWVGGTLRI--HREFDPEAVLAAIERHRLTCAWMAPVMLSRVLTVPDRDRFDLDSLAWCIGGGEKTPESRIRDFTRVFT 289
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218563680 392 IKEMVIGYGTTEnspvTFCGFPVDSAERKIETVGCIS---PHTEAKVVDpTTGEIVPLGAQGELMIRGYCVMLEYWQDEE 468
Cdd:PRK06145 290 RARYIDAYGLTE----TCSGDTLMEAGREIEKIGSTGralAHVEIRIAD-GAGRWLPPNMKGEICMRGPKVTKGYWKDPE 364
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218563680 469 KTRECITKDrWYKTGDIASLDQFAYCKIEGRIKDLIIRGGENIYPAEIEQFLHTHPKILEAQVVGVKDERMGEEVCACIR 548
Cdd:PRK06145 365 KTAEAFYGD-WFRSGDVGYLDEEGFLYLTDRKKDMIISGGENIASSEVERVIYELPEVAEAAVIGVHDDRWGERITAVVV 443
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|...
gi 218563680 549 LKEGQECTVEEIKAYCKGKIAHYKVPRYILFVQDYPLTITGKIQKHKLRERTE 601
Cdd:PRK06145 444 LNPGATLTLEALDRHCRQRLASFKVPRQLKVRDELPRNPSGKVLKRVLRDELN 496
|
|
| PRK07514 |
PRK07514 |
malonyl-CoA synthase; Validated |
137-599 |
9.00e-61 |
|
malonyl-CoA synthase; Validated
Pssm-ID: 181011 [Multi-domain] Cd Length: 504 Bit Score: 210.12 E-value: 9.00e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218563680 137 ATAKAGIILVAVNPAYQLQEVEFALRKVQCNAVVC-PTKFksqhycDMLKQLcpemetASPGGIKssrlpdlhTVIVTDS 215
Cdd:PRK07514 72 ATLRAGAVFLPLNTAYTLAELDYFIGDAEPALVVCdPANF------AWLSKI------AAAAGAP--------HVETLDA 131
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218563680 216 QQPGSFLlkdlmqAGSSQHYQQLQDLQKKLvcDDPINIQFTSGTTGKPKGATLSHHNIVNNAyFTGMRIgynWR---KNV 292
Cdd:PRK07514 132 DGTGSLL------EAAAAAPDDFETVPRGA--DDLAAILYTSGTTGRSKGAMLSHGNLLSNA-LTLVDY---WRftpDDV 199
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218563680 293 RI-CLPVplYHCFG-SVGGGVIMaLYGTTVIFPStGYDGRANLRAIEKekCTFVYGTPTMYIDMLGQPDLAKFDLSSVRG 370
Cdd:PRK07514 200 LIhALPI--FHTHGlFVATNVAL-LAGASMIFLP-KFDPDAVLALMPR--ATVMMGVPTFYTRLLQEPRLTREAAAHMRL 273
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218563680 371 GIAAGSPCPPEVMRKILNVMG--IKEMvigYGTTENSPVTfcGFPVDSaERKIETVGCISPHTEAKVVDPTTGEIVPLGA 448
Cdd:PRK07514 274 FISGSAPLLAETHREFQERTGhaILER---YGMTETNMNT--SNPYDG-ERRAGTVGFPLPGVSLRVTDPETGAELPPGE 347
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218563680 449 QGELMIRGYCVMLEYWQDEEKTRECITKDRWYKTGDIASLDQFAYCKIEGRIKDLIIRGGENIYPAEIEQFLHTHPKILE 528
Cdd:PRK07514 348 IGMIEVKGPNVFKGYWRMPEKTAEEFRADGFFITGDLGKIDERGYVHIVGRGKDLIISGGYNVYPKEVEGEIDELPGVVE 427
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 218563680 529 AQVVGVKDERMGEEVCACIRLKEGQECTVEEIKAYCKGKIAHYKVPRYILFVQDYPLTITGKIQKHKLRER 599
Cdd:PRK07514 428 SAVIGVPHPDFGEGVTAVVVPKPGAALDEAAILAALKGRLARFKQPKRVFFVDELPRNTMGKVQKNLLREQ 498
|
|
| menE |
TIGR01923 |
O-succinylbenzoate-CoA ligase; This model represents an enzyme, O-succinylbenzoate-CoA ligase, ... |
95-596 |
2.35e-60 |
|
O-succinylbenzoate-CoA ligase; This model represents an enzyme, O-succinylbenzoate-CoA ligase, which is involved in the fourth step of the menaquinone biosynthesis pathway. O-succinylbenzoate-CoA ligase, together with menB - naphtoate synthase, take 2-succinylbenzoate and convert it into 1,4-di-hydroxy-2- naphtoate. [Biosynthesis of cofactors, prosthetic groups, and carriers, Menaquinone and ubiquinone]
Pssm-ID: 162605 [Multi-domain] Cd Length: 436 Bit Score: 207.30 E-value: 2.35e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218563680 95 TFAEFYQDVEKAAAGLLAAGLKRGDRLGMWGPNIYEWVLMQFATAKAGIILVAVNPAYQLQEVEFALRKVQCNAVVCPTK 174
Cdd:TIGR01923 1 TWQDLDCEAAHLAKALKAQGIRSGSRVALVGQNSIEMVLLLHACLLLGAEIAMLNTRLTENERTNQLEDLDVQLLLTDSL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218563680 175 FKSQhycdmlkqlcpemetaspggikssrlpdlhtVIVTDSqqpgsflLKDLMQAGSSQhyqqlQDLQKKLVCDDPINIQ 254
Cdd:TIGR01923 81 LEEK-------------------------------DFQADS-------LDRIEAAGRYE-----TSLSASFNMDQIATLM 117
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218563680 255 FTSGTTGKPKGATLSHHNIVNNAYFTGMRIGY----NWrknvriCLPVPLYHcfgsVGG-GVIM--ALYGTTVIFPstgy 327
Cdd:TIGR01923 118 FTSGTTGKPKAVPHTFRNHYASAVGSKENLGFteddNW------LLSLPLYH----ISGlSILFrwLIEGATLRIV---- 183
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218563680 328 DGRANL-RAIEKEKCTFVYGTPTMYIDMLgQPDLAKFDLSSVRGGiaaGSPCPPEVMRKILNvMGIkEMVIGYGTTENSP 406
Cdd:TIGR01923 184 DKFNQLlEMIANERVTHISLVPTQLNRLL-DEGGHNENLRKILLG---GSAIPAPLIEEAQQ-YGL-PIYLSYGMTETCS 257
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218563680 407 vTFCGFPVDSAERKIEtVGCISPHTEAKV-VDPTTGeivplgaQGELMIRGYCVMLEYWQDEEkTRECITKDRWYKTGDI 485
Cdd:TIGR01923 258 -QVTTATPEMLHARPD-VGRPLAGREIKIkVDNKEG-------HGEIMVKGANLMKGYLYQGE-LTPAFEQQGWFNTGDI 327
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218563680 486 ASLDQFAYCKIEGRIKDLIIRGGENIYPAEIEQFLHTHPKILEAQVVGVKDERMGEEVCACIRLkEGQECtVEEIKAYCK 565
Cdd:TIGR01923 328 GELDGEGFLYVLGRRDDLIISGGENIYPEEIETVLYQHPGIQEAVVVPKPDAEWGQVPVAYIVS-ESDIS-QAKLIAYLT 405
|
490 500 510
....*....|....*....|....*....|.
gi 218563680 566 GKIAHYKVPRYILFVQDYPLTITGKIQKHKL 596
Cdd:TIGR01923 406 EKLAKYKVPIAFEKLDELPYNASGKILRNQL 436
|
|
| PRK06178 |
PRK06178 |
acyl-CoA synthetase; Validated |
44-601 |
4.75e-60 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 235724 [Multi-domain] Cd Length: 567 Bit Score: 209.51 E-value: 4.75e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218563680 44 PPSIPTlTTSYVHGlsshplqSSTVDQCLQATVERYPDREAMVFVqdGIRKTFAEFYQDVEKAAAGLLAAGLKRGDRLGM 123
Cdd:PRK06178 19 PAGIPR-EPEYPHG-------ERPLTEYLRAWARERPQRPAIIFY--GHVITYAELDELSDRFAALLRQRGVGAGDRVAV 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218563680 124 WGPNIYEWVLMQFATAKAGIILVAVNPAYQLQEVEFALRKVQCNAVVCPTKFksqhyCDMLKQLCPEmeTASPGGIKSS- 202
Cdd:PRK06178 89 FLPNCPQFHIVFFGILKLGAVHVPVSPLFREHELSYELNDAGAEVLLALDQL-----APVVEQVRAE--TSLRHVIVTSl 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218563680 203 --RLPDLHTVIVTDS------QQPGSFLLKDLMQAGSSQHYQQLQDLqkklvcDDPINIQFTSGTTGKPKGATLSHHNIV 274
Cdd:PRK06178 162 adVLPAEPTLPLPDSlraprlAAAGAIDLLPALRACTAPVPLPPPAL------DALAALNYTGGTTGMPKGCEHTQRDMV 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218563680 275 NNA---YFTGMRIGYNwrknvriclPVPL--YHCFGSVGG--GVIMALY-GTTVIFpSTGYDGRANLRAIEKEKCTFVYG 346
Cdd:PRK06178 236 YTAaaaYAVAVVGGED---------SVFLsfLPEFWIAGEnfGLLFPLFsGATLVL-LARWDAVAFMAAVERYRVTRTVM 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218563680 347 TPTMYIDMLGQPDLAKFDLSSVR--GGIAAGSPCPPEVMRKILNVMGIKEMVIGYGTTE-NSPVTF-CGFPVDSAERKIE 422
Cdd:PRK06178 306 LVDNAVELMDHPRFAEYDLSSLRqvRVVSFVKKLNPDYRQRWRALTGSVLAEAAWGMTEtHTCDTFtAGFQDDDFDLLSQ 385
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218563680 423 T--VGCISPHTEAKVVDPTTGEIVPLGAQGELMIRGYCVMLEYWQDEEKTRECItKDRWYKTGDIASLDQFAYCKIEGRI 500
Cdd:PRK06178 386 PvfVGLPVPGTEFKICDFETGELLPLGAEGEIVVRTPSLLKGYWNKPEATAEAL-RDGWLHTGDIGKIDEQGFLHYLGRR 464
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218563680 501 KDLIIRGGENIYPAEIEQFLHTHPKILEAQVVGVKDERMGEEVCACIRLKEGQECTVEEIKAYCKGKIAHYKVPRyILFV 580
Cdd:PRK06178 465 KEMLKVNGMSVFPSEVEALLGQHPAVLGSAVVGRPDPDKGQVPVAFVQLKPGADLTAAALQAWCRENMAVYKVPE-IRIV 543
|
570 580
....*....|....*....|.
gi 218563680 581 QDYPLTITGKIQKHKLRERTE 601
Cdd:PRK06178 544 DALPMTATGKVRKQDLQALAE 564
|
|
| PRK06188 |
PRK06188 |
acyl-CoA synthetase; Validated |
69-599 |
2.45e-59 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 235731 [Multi-domain] Cd Length: 524 Bit Score: 206.76 E-value: 2.45e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218563680 69 DQCLQAtVERYPDREAMVFvqDGIRKTFAEFYQDVEKAAAGLLAAGLKRGDRLGMWGPNIYEWVLMQFATAKAGIILVAV 148
Cdd:PRK06188 16 HLLVSA-LKRYPDRPALVL--GDTRLTYGQLADRISRYIQAFEALGLGTGDAVALLSLNRPEVLMAIGAAQLAGLRRTAL 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218563680 149 NP-------AYQLQEVEFALrkvqcnAVVCPTKFksqhycdmlkqlcpemetASPGGIKSSRLPDLHTVIVTDSQQPGSf 221
Cdd:PRK06188 93 HPlgslddhAYVLEDAGIST------LIVDPAPF------------------VERALALLARVPSLKHVLTLGPVPDGV- 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218563680 222 llkDLMQAGSSQHYQQLQDLQkklVCDDPINIQFTSGTTGKPKGATLSHHNIVNNAyfTGMRIGYNWRKNVRICLPVPLY 301
Cdd:PRK06188 148 ---DLLAAAAKFGPAPLVAAA---LPPDIAGLAYTGGTTGKPKGVMGTHRSIATMA--QIQLAEWEWPADPRFLMCTPLS 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218563680 302 HcfgsVGGGVIMA--LYGTTVIFpSTGYDGRANLRAIEKEKCTFVYGTPTMYIDMLGQPDLAKFDLSSVRGGIAAGSPCP 379
Cdd:PRK06188 220 H----AGGAFFLPtlLRGGTVIV-LAKFDPAEVLRAIEEQRITATFLVPTMIYALLDHPDLRTRDLSSLETVYYGASPMS 294
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218563680 380 PEVMRKILNVMGikeMVIG--YGTTEnSPVTFCGFP----VDSAERKIETVGCISPHTEAKVVDPTtGEIVPLGAQGELM 453
Cdd:PRK06188 295 PVRLAEAIERFG---PIFAqyYGQTE-APMVITYLRkrdhDPDDPKRLTSCGRPTPGLRVALLDED-GREVAQGEVGEIC 369
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218563680 454 IRGYCVMLEYWQDEEKTRECItKDRWYKTGDIASLDQFAYCKIEGRIKDLIIRGGENIYPAEIEQFLHTHPKILEAQVVG 533
Cdd:PRK06188 370 VRGPLVMDGYWNRPEETAEAF-RDGWLHTGDVAREDEDGFYYIVDRKKDMIVTGGFNVFPREVEDVLAEHPAVAQVAVIG 448
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 218563680 534 VKDERMGEEVCACIRLKEGQECTVEEIKAYCKGKIAHYKVPRYILFVQDYPLTITGKIQKHKLRER 599
Cdd:PRK06188 449 VPDEKWGEAVTAVVVLRPGAAVDAAELQAHVKERKGSVHAPKQVDFVDSLPLTALGKPDKKALRAR 514
|
|
| PRK03640 |
PRK03640 |
o-succinylbenzoate--CoA ligase; |
72-603 |
1.66e-58 |
|
o-succinylbenzoate--CoA ligase;
Pssm-ID: 235146 [Multi-domain] Cd Length: 483 Bit Score: 203.27 E-value: 1.66e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218563680 72 LQATVERYPDREAMVFvqDGIRKTFAEFYQDVEKAAAGLLAAGLKRGDRLGMWGPNIYEWVLMQFATAKAGIILVAVNPA 151
Cdd:PRK03640 8 LKQRAFLTPDRTAIEF--EEKKVTFMELHEAVVSVAGKLAALGVKKGDRVALLMKNGMEMILVIHALQQLGAVAVLLNTR 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218563680 152 YQLQEVEFALRKVQCNAVVCPTKFKSQHYcdmlkqlcpemetaspgGIKSSRLPDLhtvivtdsqqpgsfllkdlmQAGS 231
Cdd:PRK03640 86 LSREELLWQLDDAEVKCLITDDDFEAKLI-----------------PGISVKFAEL--------------------MNGP 128
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218563680 232 SQHyqqlQDLQKKLVCDDPINIQFTSGTTGKPKGATLSHHN----IVNNAYFTGMRIGYNWrknvrIClPVPLYHcfgsV 307
Cdd:PRK03640 129 KEE----AEIQEEFDLDEVATIMYTSGTTGKPKGVIQTYGNhwwsAVGSALNLGLTEDDCW-----LA-AVPIFH----I 194
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218563680 308 GGGVIM---ALYGTTVIFPSTgYDGRANLRAIEKEKCTFVYGTPTMYIDMLGQPDLAKFDlSSVRGGIAAGSPCPPEVM- 383
Cdd:PRK03640 195 SGLSILmrsVIYGMRVVLVEK-FDAEKINKLLQTGGVTIISVVSTMLQRLLERLGEGTYP-SSFRCMLLGGGPAPKPLLe 272
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218563680 384 ---RKILNVmgikemVIGYGTTENSPvTFCGFPVDSAERKIETVGCISPHTEAKVVDptTGEIVPLGAQGELMIRGYCVM 460
Cdd:PRK03640 273 qckEKGIPV------YQSYGMTETAS-QIVTLSPEDALTKLGSAGKPLFPCELKIEK--DGVVVPPFEEGEIVVKGPNVT 343
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218563680 461 LEYWQDEEKTRECItKDRWYKTGDIASLDQFAYCKIEGRIKDLIIRGGENIYPAEIEQFLHTHPKILEAQVVGVKDERMG 540
Cdd:PRK03640 344 KGYLNREDATRETF-QDGWFKTGDIGYLDEEGFLYVLDRRSDLIISGGENIYPAEIEEVLLSHPGVAEAGVVGVPDDKWG 422
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 218563680 541 EEVCACIRLkeGQECTVEEIKAYCKGKIAHYKVPRYILFVQDYPLTITGKIQKHKLRERTEKQ 603
Cdd:PRK03640 423 QVPVAFVVK--SGEVTEEELRHFCEEKLAKYKVPKRFYFVEELPRNASGKLLRHELKQLVEEM 483
|
|
| BACL_like |
cd05929 |
Bacterial Bile acid CoA ligases and similar proteins; Bile acid-Coenzyme A ligase catalyzes ... |
253-598 |
7.00e-58 |
|
Bacterial Bile acid CoA ligases and similar proteins; Bile acid-Coenzyme A ligase catalyzes the formation of bile acid-CoA conjugates in a two-step reaction: the formation of a bile acid-AMP molecule as an intermediate, followed by the formation of a bile acid-CoA. This ligase requires a bile acid with a free carboxyl group, ATP, Mg2+, and CoA for synthesis of the final bile acid-CoA conjugate. The bile acid-CoA ligation is believed to be the initial step in the bile acid 7alpha-dehydroxylation pathway in the intestinal bacterium Eubacterium sp.
Pssm-ID: 341252 [Multi-domain] Cd Length: 473 Bit Score: 201.45 E-value: 7.00e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218563680 253 IQFTSGTTGKPKGATLSH-HNIVNNAYFTGMRIGYNWRKNVRICLPVPLYHCFGSVGGGVIMALYGTTVIFPStgYDGRA 331
Cdd:cd05929 130 MLYSGGTTGRPKGIKRGLpGGPPDNDTLMAAALGFGPGADSVYLSPAPLYHAAPFRWSMTALFMGGTLVLMEK--FDPEE 207
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218563680 332 NLRAIEKEKCTFVYGTPTMYIDMLGQPD--LAKFDLSSVRGGIAAGSPCPPEVMRKILNVMG--IKEMvigYGTTENSPV 407
Cdd:cd05929 208 FLRLIERYRVTFAQFVPTMFVRLLKLPEavRNAYDLSSLKRVIHAAAPCPPWVKEQWIDWGGpiIWEY---YGGTEGQGL 284
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218563680 408 TFCgfpvdSAERKIETVGCISPHTEAKV--VDpTTGEIVPLGAQGELMIR-GYCVmlEYWQDEEKTRECITKDRWYKTGD 484
Cdd:cd05929 285 TII-----NGEEWLTHPGSVGRAVLGKVhiLD-EDGNEVPPGEIGEVYFAnGPGF--EYTNDPEKTAAARNEGGWSTLGD 356
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218563680 485 IASLDQFAYCKIEGRIKDLIIRGGENIYPAEIEQFLHTHPKILEAQVVGVKDERMGEEVCACIR---LKEGQECTVEEIK 561
Cdd:cd05929 357 VGYLDEDGYLYLTDRRSDMIISGGVNIYPQEIENALIAHPKVLDAAVVGVPDEELGQRVHAVVQpapGADAGTALAEELI 436
|
330 340 350
....*....|....*....|....*....|....*..
gi 218563680 562 AYCKGKIAHYKVPRYILFVQDYPLTITGKIQKHKLRE 598
Cdd:cd05929 437 AFLRDRLSRYKCPRSIEFVAELPRDDTGKLYRRLLRD 473
|
|
| ABCL |
cd05958 |
2-aminobenzoate-CoA ligase (ABCL); ABCL catalyzes the initial step in the 2-aminobenzoate ... |
118-597 |
5.78e-57 |
|
2-aminobenzoate-CoA ligase (ABCL); ABCL catalyzes the initial step in the 2-aminobenzoate aerobic degradation pathway by activating 2-aminobenzoate to 2-aminobenzoyl-CoA. The reaction is carried out via a two-step process; the first step is ATP-dependent and forms a 2-aminobenzoyl-AMP intermediate, and the second step forms the 2-aminobenzoyl-CoA ester and releases the AMP. 2-Aminobenzoyl-CoA is further converted to 2-amino-5-oxo-cyclohex-1-ene-1-carbonyl-CoA catalyzed by 2-aminobenzoyl-CoA monooxygenase/reductase. ABCL has been purified from cells aerobically grown with 2-aminobenzoate as sole carbon, energy, and nitrogen source, and has been characterized as a monomer.
Pssm-ID: 341268 [Multi-domain] Cd Length: 439 Bit Score: 198.09 E-value: 5.78e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218563680 118 GDRLGMWGPNIYEWVLMQFATAKAGIILVAVNPAYQLQEVEFALRkvqcnavvcptkfksqhYCDMLKQLCPEMETASpg 197
Cdd:cd05958 36 GNRVLLRGSNSPELVACWFGIQKAGAIAVATMPLLRPKELAYILD-----------------KARITVALCAHALTAS-- 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218563680 198 gikssrlpdlhtvivtdsqqpgsfllkdlmqagssqhyqqlqdlqkklvcDDPINIQFTSGTTGKPKGATLSHHNIVNNA 277
Cdd:cd05958 97 --------------------------------------------------DDICILAFTSGTTGAPKATMHFHRDPLASA 126
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218563680 278 YFTGMRIgYNWRKNVRICLPVPLYHCFGsVGGGVIMALY--GTTVIFPSTGYDGRanLRAIEKEKCTFVYGTPTMYIDML 355
Cdd:cd05958 127 DRYAVNV-LRLREDDRFVGSPPLAFTFG-LGGVLLFPFGvgASGVLLEEATPDLL--LSAIARYKPTVLFTAPTAYRAML 202
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218563680 356 GQPDLAKFDLSSVRGGIAAGSPCPPEVMRKILNVMGIkEMVIGYGTTENSPVTFCGFPVDSaerKIETVGCISPHTEAKV 435
Cdd:cd05958 203 AHPDAAGPDLSSLRKCVSAGEALPAALHRAWKEATGI-PIIDGIGSTEMFHIFISARPGDA---RPGATGKPVPGYEAKV 278
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218563680 436 VDpTTGEIVPLGAQGELMIRGYCVmleYWQDEEKTRECITKDRWYKTGDIASLDQFAYCKIEGRIKDLIIRGGENIYPAE 515
Cdd:cd05958 279 VD-DEGNPVPDGTIGRLAVRGPTG---CRYLADKRQRTYVQGGWNITGDTYSRDPDGYFRHQGRSDDMIVSGGYNIAPPE 354
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218563680 516 IEQFLHTHPKILEAQVVGVKDERMGEEVCACIRLKEGQ---ECTVEEIKAYCKGKIAHYKVPRYILFVQDYPLTITGKIQ 592
Cdd:cd05958 355 VEDVLLQHPAVAECAVVGHPDESRGVVVKAFVVLRPGVipgPVLARELQDHAKAHIAPYKYPRAIEFVTELPRTATGKLQ 434
|
....*
gi 218563680 593 KHKLR 597
Cdd:cd05958 435 RFALR 439
|
|
| ACLS-CaiC |
cd17637 |
acyl-CoA synthetase (AMP-forming)/AMP-acid ligase II; This family contains fatty acid CoA ... |
249-591 |
7.21e-57 |
|
acyl-CoA synthetase (AMP-forming)/AMP-acid ligase II; This family contains fatty acid CoA ligases, including acyl-CoA synthetase (AMP-forming)/AMP-acid ligase II, most of which are yet to be characterized, but may be similar to Carnitine-CoA ligase (CaiC) which catalyzes the transfer of CoA to carnitine. Fatty acyl-CoA ligases catalyze the ATP-dependent activation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions.
Pssm-ID: 341292 [Multi-domain] Cd Length: 333 Bit Score: 194.80 E-value: 7.21e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218563680 249 DPINIQFTSGTTGKPKGATLSHHNIVNNAYFTGMRIGYNWRKnvrICL-PVPLYHCfgsvgGGVIMALY-----GTTVIF 322
Cdd:cd17637 1 DPFVIIHTAAVAGRPRGAVLSHGNLIAANLQLIHAMGLTEAD---VYLnMLPLFHI-----AGLNLALAtfhagGANVVM 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218563680 323 PStgYDGRANLRAIEKEKCTFVYGTPTMYIDMLGQPDLAKFDLSSVR--GGIAAgspcpPEVMRKILNVMGIKeMVIGYG 400
Cdd:cd17637 73 EK--FDPAEALELIEEEKVTLMGSFPPILSNLLDAAEKSGVDLSSLRhvLGLDA-----PETIQRFEETTGAT-FWSLYG 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218563680 401 TTENS-PVTFCgfpvDSAERKiETVGCISPHTEAKVVDPTTGEiVPLGAQGELMIRGYCVMLEYWQDEEKTrECITKDRW 479
Cdd:cd17637 145 QTETSgLVTLS----PYRERP-GSAGRPGPLVRVRIVDDNDRP-VPAGETGEIVVRGPLVFQGYWNLPELT-AYTFRNGW 217
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218563680 480 YKTGDIASLDQFAYCKIEGRI--KDLIIRGGENIYPAEIEQFLHTHPKILEAQVVGVKDERMGEEVCACIRLKEGQECTV 557
Cdd:cd17637 218 HHTGDLGRFDEDGYLWYAGRKpeKELIKPGGENVYPAEVEKVILEHPAIAEVCVIGVPDPKWGEGIKAVCVLKPGATLTA 297
|
330 340 350
....*....|....*....|....*....|....
gi 218563680 558 EEIKAYCKGKIAHYKVPRYILFVQDYPLTITGKI 591
Cdd:cd17637 298 DELIEFVGSRIARYKKPRYVVFVEALPKTADGSI 331
|
|
| PLN02330 |
PLN02330 |
4-coumarate--CoA ligase-like 1 |
76-599 |
1.61e-56 |
|
4-coumarate--CoA ligase-like 1
Pssm-ID: 215189 [Multi-domain] Cd Length: 546 Bit Score: 199.82 E-value: 1.61e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218563680 76 VERYPDREAMVFVQDGIRKTFAEFYQDVEKAAAGLLAAGLKRGDRLGMWGPNIYEWVLMQFATAKAGIILVAVNPAYQLQ 155
Cdd:PLN02330 38 AELYADKVAFVEAVTGKAVTYGEVVRDTRRFAKALRSLGLRKGQVVVVVLPNVAEYGIVALGIMAAGGVFSGANPTALES 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218563680 156 EVEFALRKVQCNAVVCptkfKSQHYcdmlkqlcpemetaspGGIKSSRLPdlhTVIVTDSQQPGSFLLKDLMQA----GS 231
Cdd:PLN02330 118 EIKKQAEAAGAKLIVT----NDTNY----------------GKVKGLGLP---VIVLGEEKIEGAVNWKELLEAadraGD 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218563680 232 SQHYQQLqdLQKKLvCDDPiniqFTSGTTGKPKGATLSHHNIVNNAYFTGMRIGYNWRKNVRICLPVPLYHCFGSVG-GG 310
Cdd:PLN02330 175 TSDNEEI--LQTDL-CALP----FSSGTTGISKGVMLTHRNLVANLCSSLFSVGPEMIGQVVTLGLIPFFHIYGITGiCC 247
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218563680 311 VIMALYGTTVIFpsTGYDGRANLRAIEKEKCTFVYGTPTMYIDMLGQPDLAKFDLSSV--RGGIAAGSPCPPEVMRKILN 388
Cdd:PLN02330 248 ATLRNKGKVVVM--SRFELRTFLNALITQEVSFAPIVPPIILNLVKNPIVEEFDLSKLklQAIMTAAAPLAPELLTAFEA 325
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218563680 389 VMGIKEMVIGYGTTENSPVTFCGFPVDSAE--RKIETVGCISPHTEAKVVDPTTGEIVPLGAQGELMIRGYCVMLEYWQD 466
Cdd:PLN02330 326 KFPGVQVQEAYGLTEHSCITLTHGDPEKGHgiAKKNSVGFILPNLEVKFIDPDTGRSLPKNTPGELCVRSQCVMQGYYNN 405
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218563680 467 EEKTRECITKDRWYKTGDIASLDQFAYCKIEGRIKDLIIRGGENIYPAEIEQFLHTHPKILEAQVVGVKDERMGEEVCAC 546
Cdd:PLN02330 406 KEETDRTIDEDGWLHTGDIGYIDDDGDIFIVDRIKELIKYKGFQVAPAELEAILLTHPSVEDAAVVPLPDEEAGEIPAAC 485
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|...
gi 218563680 547 IRLKEGQECTVEEIKAYCKGKIAHYKVPRYILFVQDYPLTITGKIQKHKLRER 599
Cdd:PLN02330 486 VVINPKAKESEEDILNFVAANVAHYKKVRVVQFVDSIPKSLSGKIMRRLLKEK 538
|
|
| AAS_C |
cd05909 |
C-terminal domain of the acyl-acyl carrier protein synthetase (also called ... |
248-600 |
2.40e-56 |
|
C-terminal domain of the acyl-acyl carrier protein synthetase (also called 2-acylglycerophosphoethanolamine acyltransferase, Aas); Acyl-acyl carrier protein synthase (Aas) is a membrane protein responsible for a minor pathway of incorporating exogenous fatty acids into membrane phospholipids. Its in vitro activity is characterized by the ligation of free fatty acids between 8 and 18 carbons in length to the acyl carrier protein sulfydryl group (ACP-SH) in the presence of ATP and Mg2+. However, its in vivo function is as a 2-acylglycerophosphoethanolamine (2-acyl-GPE) acyltransferase. The reaction occurs in two steps: the acyl chain is first esterified to acyl carrier protein (ACP) via a thioester bond, followed by a second step where the acyl chain is transferred to a 2-acyllysophospholipid, thus completing the transacylation reaction. This model represents the C-terminal domain of the enzyme, which belongs to the class I adenylate-forming enzyme family, including acyl-CoA synthetases.
Pssm-ID: 341235 [Multi-domain] Cd Length: 490 Bit Score: 197.94 E-value: 2.40e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218563680 248 DDPINIQFTSGTTGKPKGATLSHHNIVNNAYFTGMRIGYNwrKNVRICLPVPLYHCFGSVGGGVIMALYGTTVIFPSTGY 327
Cdd:cd05909 147 DDPAVILFTSGSEGLPKGVVLSHKNLLANVEQITAIFDPN--PEDVVFGALPFFHSFGLTGCLWLPLLSGIKVVFHPNPL 224
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218563680 328 DGRANLRAIEKEKCTFVYGTPT--MYIDMLGQPDlakfDLSSVRGGIAAGSPCPPEVMRKILNVMGIKeMVIGYGTTENS 405
Cdd:cd05909 225 DYKKIPELIYDKKATILLGTPTflRGYARAAHPE----DFSSLRLVVAGAEKLKDTLRQEFQEKFGIR-ILEGYGTTECS 299
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218563680 406 PVTFCGFPvdSAERKIETVGCISPHTEAKVVDPTTGEIVPLGAQGELMIRGYCVMLEYWQDEEKTrECITKDRWYKTGDI 485
Cdd:cd05909 300 PVISVNTP--QSPNKEGTVGRPLPGMEVKIVSVETHEEVPIGEGGLLLVRGPNVMLGYLNEPELT-SFAFGDGWYDTGDI 376
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218563680 486 ASLDQFAYCKIEGRIKDLIIRGGENIYPAEIEQFLHTH-PKILEAQVVGVKDERMGEEVCACIRLKEGqecTVEEIKAYC 564
Cdd:cd05909 377 GKIDGEGFLTITGRLSRFAKIAGEMVSLEAIEDILSEIlPEDNEVAVVSVPDGRKGEKIVLLTTTTDT---DPSSLNDIL 453
|
330 340 350
....*....|....*....|....*....|....*..
gi 218563680 565 K-GKIAHYKVPRYILFVQDYPLTITGKIQKHKLRERT 600
Cdd:cd05909 454 KnAGISNLAKPSYIHQVEEIPLLGTGKPDYVTLKALA 490
|
|
| 23DHB-AMP_lg |
cd05920 |
2,3-dihydroxybenzoate-AMP ligase; 2,3-dihydroxybenzoate-AMP ligase activates 2, ... |
64-596 |
4.15e-56 |
|
2,3-dihydroxybenzoate-AMP ligase; 2,3-dihydroxybenzoate-AMP ligase activates 2,3-dihydroxybenzoate (DHB) by ligation of AMP from ATP with the release of pyrophosphate. However, it can also catalyze the ATP-PPi exchange for 2,3-DHB analogs, such as salicyclic acid (o-hydrobenzoate), as well as 2,4-DHB and 2,5-DHB, but with less efficiency. Proteins in this family are the stand-alone adenylation components of non-ribosomal peptide synthases (NRPSs) involved in the biosynthesis of siderophores, which are low molecular weight iron-chelating compounds synthesized by many bacteria to aid in the acquisition of this vital trace elements. In Escherichia coli, the 2,3-dihydroxybenzoate-AMP ligase is called EntE, the adenylation component of the enterobactin NRPS system.
Pssm-ID: 341244 [Multi-domain] Cd Length: 482 Bit Score: 196.78 E-value: 4.15e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218563680 64 QSSTVDQCLQATVERYPDREAMVfvQDGIRKTFAEFYQDVEKAAAGLLAAGLKRGDRLGMWGPNIYEWVLMQFATAKAGI 143
Cdd:cd05920 13 QDEPLGDLLARSAARHPDRIAVV--DGDRRLTYRELDRRADRLAAGLRGLGIRPGDRVVVQLPNVAEFVVLFFALLRLGA 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218563680 144 ILVAVNPAYQLQEVefalrkvqcnavvcptkfksQHYCDmlkqlcpemetaspggikssrlpdlHTvivtdsqQPGSFLL 223
Cdd:cd05920 91 VPVLALPSHRRSEL--------------------SAFCA-------------------------HA-------EAVAYIV 118
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218563680 224 KDlmQAGSSQHYQQLQDLQKKlvCDDPINIQFTSGTTGKPKGATLSHhnivnNAYftgmriGYNWRKNVRIC-------- 295
Cdd:cd05920 119 PD--RHAGFDHRALARELAES--IPEVALFLLSGGTTGTPKLIPRTH-----NDY------AYNVRASAEVCgldqdtvy 183
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218563680 296 LPV-PLYHCFGSVGGGVIMALY-GTTVIFPSTGYDGRAnLRAIEKEKCTFVYGTPTMYIDMLGQPDLAKFDLSSVRGGIA 373
Cdd:cd05920 184 LAVlPAAHNFPLACPGVLGTLLaGGRVVLAPDPSPDAA-FPLIEREGVTVTALVPALVSLWLDAAASRRADLSSLRLLQV 262
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218563680 374 AGSPCPPEVMRKILNVMGIKEMVIgYGTTENSpVTFCGFPvDSAERKIETVG-CISPHTEAKVVDPTtGEIVPLGAQGEL 452
Cdd:cd05920 263 GGARLSPALARRVPPVLGCTLQQV-FGMAEGL-LNYTRLD-DPDEVIIHTQGrPMSPDDEIRVVDEE-GNPVPPGEEGEL 338
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218563680 453 MIRGYCVMLEYWQDEEKTRECITKDRWYKTGDIASLDQFAYCKIEGRIKDLIIRGGENIYPAEIEQFLHTHPKILEAQVV 532
Cdd:cd05920 339 LTRGPYTIRGYYRAPEHNARAFTPDGFYRTGDLVRRTPDGYLVVEGRIKDQINRGGEKIAAEEVENLLLRHPAVHDAAVV 418
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 218563680 533 GVKDERMGEEVCACIRLKeGQECTVEEIKAYCKGK-IAHYKVPRYILFVQDYPLTITGKIQKHKL 596
Cdd:cd05920 419 AMPDELLGERSCAFVVLR-DPPPSAAQLRRFLRERgLAAYKLPDRIEFVDSLPLTAVGKIDKKAL 482
|
|
| caiC |
PRK08008 |
putative crotonobetaine/carnitine-CoA ligase; Validated |
65-597 |
6.29e-56 |
|
putative crotonobetaine/carnitine-CoA ligase; Validated
Pssm-ID: 181195 [Multi-domain] Cd Length: 517 Bit Score: 197.21 E-value: 6.29e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218563680 65 SSTVDQCLQATVERYPDREAMVFVQ---DGIRKTFAEFYQDVEKAAAGLLAAGLKRGDRLGMWGPNIYEWVLMQFATAKA 141
Cdd:PRK08008 6 GQHLRQMWDDLADVYGHKTALIFESsggVVRRYSYLELNEEINRTANLFYSLGIRKGDKVALHLDNCPEFIFCWFGLAKI 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218563680 142 GIILVAVNPAYQLQEVEFALRKVQCNAVVCPTKFKSqhycdMLKQLCPEMETAspggikssrlpdLHTVIVTDSQQPgsf 221
Cdd:PRK08008 86 GAIMVPINARLLREESAWILQNSQASLLVTSAQFYP-----MYRQIQQEDATP------------LRHICLTRVALP--- 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218563680 222 llkdlmQAGSSQHYQQLQDLQKKLVC-------DDPINIQFTSGTTGKPKGATLSHHNIVNNAYFTGMRIgyNWRKNVRI 294
Cdd:PRK08008 146 ------ADDGVSSFTQLKAQQPATLCyapplstDDTAEILFTSGTTSRPKGVVITHYNLRFAGYYSAWQC--ALRDDDVY 217
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218563680 295 CLPVPLYH--CFGSVGGGVIMAlyGTTVIFPSTgYDGRANLRAIEKEKCTFVYGTPTMYIDMLGQPdlakfdlssvrggi 372
Cdd:PRK08008 218 LTVMPAFHidCQCTAAMAAFSA--GATFVLLEK-YSARAFWGQVCKYRATITECIPMMIRTLMVQP-------------- 280
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218563680 373 aagsPCPPE---VMRKILNVMGIKE-------------MVIGYGTTEnspvTFCGFPVDSA--ERKIETVGCISPHTEAK 434
Cdd:PRK08008 281 ----PSANDrqhCLREVMFYLNLSDqekdafeerfgvrLLTSYGMTE----TIVGIIGDRPgdKRRWPSIGRPGFCYEAE 352
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218563680 435 VVDpTTGEIVPLGAQGELMIRGY---CVMLEYWQDEEKTRECITKDRWYKTGDIASLDQFAYCKIEGRIKDLIIRGGENI 511
Cdd:PRK08008 353 IRD-DHNRPLPAGEIGEICIKGVpgkTIFKEYYLDPKATAKVLEADGWLHTGDTGYVDEEGFFYFVDRRCNMIKRGGENV 431
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218563680 512 YPAEIEQFLHTHPKILEAQVVGVKDERMGEEVCACIRLKEGQECTVEEIKAYCKGKIAHYKVPRYILFVQDYPLTITGKI 591
Cdd:PRK08008 432 SCVELENIIATHPKIQDIVVVGIKDSIRDEAIKAFVVLNEGETLSEEEFFAFCEQNMAKFKVPSYLEIRKDLPRNCSGKI 511
|
....*.
gi 218563680 592 QKHKLR 597
Cdd:PRK08008 512 IKKNLK 517
|
|
| Firefly_Luc |
cd17642 |
insect luciferase, similar to plant 4-coumarate: CoA ligases; This family contains insect ... |
61-598 |
7.57e-56 |
|
insect luciferase, similar to plant 4-coumarate: CoA ligases; This family contains insect firefly luciferases that share significant sequence similarity to plant 4-coumarate:coenzyme A ligases, despite their functional diversity. Luciferase catalyzes the production of light in the presence of MgATP, molecular oxygen, and luciferin. In the first step, luciferin is activated by acylation of its carboxylate group with ATP, resulting in an enzyme-bound luciferyl adenylate. In the second step, luciferyl adenylate reacts with molecular oxygen, producing an enzyme-bound excited state product (Luc=O*) and releasing AMP. This excited-state product then decays to the ground state (Luc=O), emitting a quantum of visible light.
Pssm-ID: 341297 [Multi-domain] Cd Length: 532 Bit Score: 197.36 E-value: 7.57e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218563680 61 HPLQSSTVDQCLQATVERY---PDREAMVFVQDGIRKTFAEFYQDVEKAAAGLLAAGLKRGDRLGMWGPNIYEWVLMQFA 137
Cdd:cd17642 9 YPLEDGTAGEQLHKAMKRYasvPGTIAFTDAHTGVNYSYAEYLEMSVRLAEALKKYGLKQNDRIAVCSENSLQFFLPVIA 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218563680 138 TAKAGIILVAVNPAYQLQEVEFALRKVQCNAVVCptkfkSQHYCDMLKQLcpemetaspggikSSRLPDLHTVIVTDSQQ 217
Cdd:cd17642 89 GLFIGVGVAPTNDIYNERELDHSLNISKPTIVFC-----SKKGLQKVLNV-------------QKKLKIIKTIIILDSKE 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218563680 218 pgsfllkdlmqagssqHYQQLQDLQKKLVCDDPIN-------------------IQFTSGTTGKPKGATLSHHNIVnnAY 278
Cdd:cd17642 151 ----------------DYKGYQCLYTFITQNLPPGfneydfkppsfdrdeqvalIMNSSGSTGLPKGVQLTHKNIV--AR 212
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218563680 279 FTGMR---IGYNWRKNVRICLPVPLYHCFG--------SVGGGVIMAlygttvifpsTGYDGRANLRAIEKEKCTFVYGT 347
Cdd:cd17642 213 FSHARdpiFGNQIIPDTAILTVIPFHHGFGmfttlgylICGFRVVLM----------YKFEEELFLRSLQDYKVQSALLV 282
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218563680 348 PTMYIDMLGQPDLAKFDLSSVRGGIAAGSPCPPEV---MRKILNVMGIKEmviGYGTTENS------PVTFCgfpvdsae 418
Cdd:cd17642 283 PTLFAFFAKSTLVDKYDLSNLHEIASGGAPLSKEVgeaVAKRFKLPGIRQ---GYGLTETTsailitPEGDD-------- 351
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218563680 419 rKIETVGCISPHTEAKVVDPTTGEIVPLGAQGELMIRGYCVMLEYWQDEEKTRECITKDRWYKTGDIASLDQFAYCKIEG 498
Cdd:cd17642 352 -KPGAVGKVVPFFYAKVVDLDTGKTLGPNERGELCVKGPMIMKGYVNNPEATKALIDKDGWLHSGDIAYYDEDGHFFIVD 430
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218563680 499 RIKDLIIRGGENIYPAEIEQFLHTHPKILEAQVVGVKDERMGEEVCACIRLKEGQECTVEEIKAYCKGKIAHYKVPR-YI 577
Cdd:cd17642 431 RLKSLIKYKGYQVPPAELESILLQHPKIFDAGVAGIPDEDAGELPAAVVVLEAGKTMTEKEVMDYVASQVSTAKRLRgGV 510
|
570 580
....*....|....*....|.
gi 218563680 578 LFVQDYPLTITGKIQKHKLRE 598
Cdd:cd17642 511 KFVDEVPKGLTGKIDRRKIRE 531
|
|
| VL_LC_FACS_like |
cd05907 |
Long-chain fatty acid CoA synthetases and Bubblegum-like very long-chain fatty acid CoA ... |
95-533 |
1.32e-55 |
|
Long-chain fatty acid CoA synthetases and Bubblegum-like very long-chain fatty acid CoA synthetases; This family includes long-chain fatty acid (C12-C20) CoA synthetases and Bubblegum-like very long-chain (>C20) fatty acid CoA synthetases. FACS catalyzes the formation of fatty acyl-CoA in a two-step reaction: the formation of a fatty acyl-AMP molecule as an intermediate, and the formation of a fatty acyl-CoA. Eukaryotes generally have multiple isoforms of LC-FACS genes with multiple splice variants. For example, nine genes are found in Arabidopsis and six genes are expressed in mammalian cells. Drosophila melanogaster mutant bubblegum (BGM) have elevated levels of very-long-chain fatty acids (VLCFA) caused by a defective gene later named bubblegum. The human homolog (hsBG) of bubblegum has been characterized as a very long chain fatty acid CoA synthetase that functions specifically in the brain; hsBG may play a central role in brain VLCFA metabolism and myelinogenesis. Free fatty acids must be "activated" to their CoA thioesters before participating in most catabolic and anabolic reactions.
Pssm-ID: 341233 [Multi-domain] Cd Length: 452 Bit Score: 194.74 E-value: 1.32e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218563680 95 TFAEFYQDVEKAAAGLLAAGLKRGDRLGMWGPNIYEWVLMQFATAKAGIILVAVNPAYQLQEVEFALRKVQCNAVVCPTK 174
Cdd:cd05907 7 TWAEFAEEVRALAKGLIALGVEPGDRVAILSRNRPEWTIADLAILAIGAVPVPIYPTSSAEQIAYILNDSEAKALFVEDP 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218563680 175 fksqhycdmlkqlcpemetaspggikssrlpdlhtvivtdsqqpgsfllkdlmqagssqhyqqlqdlqkklvcDDPINIQ 254
Cdd:cd05907 87 -------------------------------------------------------------------------DDLATII 93
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218563680 255 FTSGTTGKPKGATLSHHNIVNNAYFTGMRIGYnwRKNVRICLPVPLYHCFGSVGGGVIMALYGTTVIFPSTGYDGRANLR 334
Cdd:cd05907 94 YTSGTTGRPKGVMLSHRNILSNALALAERLPA--TEGDRHLSFLPLAHVFERRAGLYVPLLAGARIYFASSAETLLDDLS 171
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218563680 335 AIekeKCTFVYGTPTMY------IDMLGQPDLAK--FDL---SSVRGGIAAGSPCPPEVMRkILNVMGIkEMVIGYGTTE 403
Cdd:cd05907 172 EV---RPTVFLAVPRVWekvyaaIKVKAVPGLKRklFDLavgGRLRFAASGGAPLPAELLH-FFRALGI-PVYEGYGLTE 246
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218563680 404 NSPVTFCGFPVDsaeRKIETVGcisphteaKVVDPTTgeiVPLGAQGELMIRGYCVMLEYWQDEEKTRECITKDRWYKTG 483
Cdd:cd05907 247 TSAVVTLNPPGD---NRIGTVG--------KPLPGVE---VRIADDGEILVRGPNVMLGYYKNPEATAEALDADGWLHTG 312
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|.
gi 218563680 484 DIASLDQFAYCKIEGRIKDLII-RGGENIYPAEIEQFLHTHPKILEAQVVG 533
Cdd:cd05907 313 DLGEIDEDGFLHITGRKKDLIItSGGKNISPEPIENALKASPLISQAVVIG 363
|
|
| PRK06155 |
PRK06155 |
crotonobetaine/carnitine-CoA ligase; Provisional |
60-599 |
1.24e-54 |
|
crotonobetaine/carnitine-CoA ligase; Provisional
Pssm-ID: 235719 [Multi-domain] Cd Length: 542 Bit Score: 194.59 E-value: 1.24e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218563680 60 SHPLQSSTVDQCLQATVERYPDREAMVFvqDGIRKTFAEFYQDVEKAAAGLLAAGLKRGDRLGMWGPNIYEWVLMQFATA 139
Cdd:PRK06155 15 PLPPSERTLPAMLARQAERYPDRPLLVF--GGTRWTYAEAARAAAAAAHALAAAGVKRGDRVALMCGNRIEFLDVFLGCA 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218563680 140 KAGIILVAVNPAYQLQEVEFALRKVQCNAVVCPTkfksqhycdmlkQLCPEMETASPGgikssRLPDLHTVIV---TDSQ 216
Cdd:PRK06155 93 WLGAIAVPINTALRGPQLEHILRNSGARLLVVEA------------ALLAALEAADPG-----DLPLPAVWLLdapASVS 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218563680 217 QPGSFLLKDLMQAGSSQHYQQLQDlqkklvcDDPINIQFTSGTTGKPKGATLSHHNI----VNNAYFTGMRIGynwrkNV 292
Cdd:PRK06155 156 VPAGWSTAPLPPLDAPAPAAAVQP-------GDTAAILYTSGTTGPSKGVCCPHAQFywwgRNSAEDLEIGAD-----DV 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218563680 293 rICLPVPLYH-----CFGSVgggvimALYGTTVI----FPSTGYdgranLRAIEKEKCTFVYGTPTMYIDMLGQPDLAKF 363
Cdd:PRK06155 224 -LYTTLPLFHtnalnAFFQA------LLAGATYVleprFSASGF-----WPAVRRHGATVTYLLGAMVSILLSQPARESD 291
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218563680 364 DLSSVRGGIAAGSPcpPEVMRKILNVMGIkEMVIGYGTTE-NSPvtfcgFPVDSAERKIETVGCISPHTEAKVVDpTTGE 442
Cdd:PRK06155 292 RAHRVRVALGPGVP--AALHAAFRERFGV-DLLDGYGSTEtNFV-----IAVTHGSQRPGSMGRLAPGFEARVVD-EHDQ 362
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218563680 443 IVPLGAQGELMIRG---YCVMLEYWQDEEKTRECiTKDRWYKTGDIASLDQFAYCKIEGRIKDLIIRGGENIYPAEIEQF 519
Cdd:PRK06155 363 ELPDGEPGELLLRAdepFAFATGYFGMPEKTVEA-WRNLWFHTGDRVVRDADGWFRFVDRIKDAIRRRGENISSFEVEQV 441
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218563680 520 LHTHPKILEAQVVGVKDERMGEEVCACIRLKEGQECTVEEIKAYCKGKIAHYKVPRYILFVQDYPLTITGKIQKHKLRER 599
Cdd:PRK06155 442 LLSHPAVAAAAVFPVPSELGEDEVMAAVVLRDGTALEPVALVRHCEPRLAYFAVPRYVEFVAALPKTENGKVQKFVLREQ 521
|
|
| BCL_like |
cd05919 |
Benzoate CoA ligase (BCL) and similar adenylate forming enzymes; This family contains benzoate ... |
238-597 |
1.85e-53 |
|
Benzoate CoA ligase (BCL) and similar adenylate forming enzymes; This family contains benzoate CoA ligase (BCL) and related ligases that catalyze the acylation of benzoate derivatives, 2-aminobenzoate and 4-hydroxybenzoate. Aromatic compounds represent the second most abundant class of organic carbon compounds after carbohydrates. Xenobiotic aromatic compounds are also a major class of man-made pollutants. Some bacteria use benzoate as the sole source of carbon and energy through benzoate degradation. Benzoate degradation starts with its activation to benzoyl-CoA by benzoate CoA ligase. The reaction catalyzed by benzoate CoA ligase proceeds via a two-step process; the first ATP-dependent step forms an acyl-AMP intermediate, and the second step forms the acyl-CoA ester with release of the AMP.
Pssm-ID: 341243 [Multi-domain] Cd Length: 436 Bit Score: 188.44 E-value: 1.85e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218563680 238 LQDLQKKLVC---DDPINIQFTSGTTGKPKGATLSHHNIVNNAYFTGMRIgYNWRKNVRICLPVPLYHCFGsVGGGVIMA 314
Cdd:cd05919 78 ARDCEARLVVtsaDDIAYLLYSSGTTGPPKGVMHAHRDPLLFADAMAREA-LGLTPGDRVFSSAKMFFGYG-LGNSLWFP 155
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218563680 315 LY-GTTVIFPSTGYDGRANLRAIEKEKCTFVYGTPTMYIDMLGQPDLAKFDLSSVRGGIAAGSPCPPEVMRKILNVMGIk 393
Cdd:cd05919 156 LAvGASAVLNPGWPTAERVLATLARFRPTVLYGVPTFYANLLDSCAGSPDALRSLRLCVSAGEALPRGLGERWMEHFGG- 234
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218563680 394 EMVIGYGTTENSPVTFCGFPvdsAERKIETVGCISPHTEAKVVDPTtGEIVPLGAQGELMIRGYCVMLEYWQDEEKTREC 473
Cdd:cd05919 235 PILDGIGATEVGHIFLSNRP---GAWRLGSTGRPVPGYEIRLVDEE-GHTIPPGEEGDLLVRGPSAAVGYWNNPEKSRAT 310
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218563680 474 ItKDRWYKTGDIASLDQFAYCKIEGRIKDLIIRGGENIYPAEIEQFLHTHPKILEAQVVGVKDERMGEEVCACIRLKEG- 552
Cdd:cd05919 311 F-NGGWYRTGDKFCRDADGWYTHAGRADDMLKVGGQWVSPVEVESLIIQHPAVAEAAVVAVPESTGLSRLTAFVVLKSPa 389
|
330 340 350 360
....*....|....*....|....*....|....*....|....*..
gi 218563680 553 --QECTVEEIKAYCKGKIAHYKVPRYILFVQDYPLTITGKIQKHKLR 597
Cdd:cd05919 390 apQESLARDIHRHLLERLSAHKVPRRIAFVDELPRTATGKLQRFKLR 436
|
|
| A_NRPS |
cd05930 |
The adenylation domain of nonribosomal peptide synthetases (NRPS); The adenylation (A) domain ... |
238-596 |
3.58e-53 |
|
The adenylation domain of nonribosomal peptide synthetases (NRPS); The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester bond to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.
Pssm-ID: 341253 [Multi-domain] Cd Length: 444 Bit Score: 188.12 E-value: 3.58e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218563680 238 LQDLQKKLVCDDPIN---IQFTSGTTGKPKGATLSHHNIVNnaYFTGMRIGYNWRKNVRICLPVPLyhCF-GSVGGGVIM 313
Cdd:cd05930 80 LEDSGAKLVLTDPDDlayVIYTSGSTGKPKGVMVEHRGLVN--LLLWMQEAYPLTPGDRVLQFTSF--SFdVSVWEIFGA 155
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218563680 314 ALYGTTVIF--PSTGYDGRANLRAIEKEKCTFVYGTPTMYIDMLGQPDLAkfDLSSVRGGIAAGSPCPPEVMRKILNVMG 391
Cdd:cd05930 156 LLAGATLVVlpEEVRKDPEALADLLAEEGITVLHLTPSLLRLLLQELELA--ALPSLRLVLVGGEALPPDLVRRWRELLP 233
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218563680 392 IKEMVIGYGTTENS-PVTFCGFPVDSAERKIETVG-CIsPHTEAKVVDPTtGEIVPLGAQGELMIRGYCVMLEYWQDEEK 469
Cdd:cd05930 234 GARLVNLYGPTEATvDATYYRVPPDDEEDGRVPIGrPI-PNTRVYVLDEN-LRPVPPGVPGELYIGGAGLARGYLNRPEL 311
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218563680 470 TRECITKD------RWYKTGDIASLD---QFAYCkieGRIKDLI-IRGgeniY---PAEIEQFLHTHPKILEAQVVGVKD 536
Cdd:cd05930 312 TAERFVPNpfgpgeRMYRTGDLVRWLpdgNLEFL---GRIDDQVkIRG----YrieLGEIEAALLAHPGVREAAVVARED 384
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|
gi 218563680 537 ERMGEEVCACIRLKEGQECTVEEIKAYCKGKIAHYKVPRYILFVQDYPLTITGKIQKHKL 596
Cdd:cd05930 385 GDGEKRLVAYVVPDEGGELDEEELRAHLAERLPDYMVPSAFVVLDALPLTPNGKVDRKAL 444
|
|
| AFD_YhfT-like |
cd17633 |
fatty acid-CoA ligase VraA; This family of acyl-CoA ligases includes Bacillus subtilis YhfT, ... |
249-591 |
1.40e-52 |
|
fatty acid-CoA ligase VraA; This family of acyl-CoA ligases includes Bacillus subtilis YhfT, as well as long-chain fatty acid-CoA ligase VraA, all of which are as yet to be characterized. These proteins belong to the adenylate-forming enzymes which catalyze an ATP-dependent two-step reaction to first activate a carboxylate substrate as an adenylate and then transfer the carboxylate to the pantetheine group of either coenzyme A or an acyl-carrier protein. The active site of the domain is located at the interface of a large N-terminal subdomain and a smaller C-terminal subdomain
Pssm-ID: 341288 [Multi-domain] Cd Length: 320 Bit Score: 182.99 E-value: 1.40e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218563680 249 DPINIQFTSGTTGKPKGATLSHHNIVnnAYFTGMRIGYNWRKNVRICLPVPLYHCFGSVGggVIMALY-GTTVIFpSTGY 327
Cdd:cd17633 1 NPFYIGFTSGTTGLPKAYYRSERSWI--ESFVCNEDLFNISGEDAILAPGPLSHSLFLYG--AISALYlGGTFIG-QRKF 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218563680 328 DGRANLRAIEKEKCTFVYGTPTMyidmLGQPDLAKFDLSSVRGGIAAGSPCPPEVMRKILNVMGIKEMVIGYGTTENSPV 407
Cdd:cd17633 76 NPKSWIRKINQYNATVIYLVPTM----LQALARTLEPESKIKSIFSSGQKLFESTKKKLKNIFPKANLIEFYGTSELSFI 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218563680 408 TFCgfpVDSAERKIETVGCISPHTEAKVVDPTTGEIVPLGAQGELMIRGYCVMleywqdeektrECITKDRWYKTGDIAS 487
Cdd:cd17633 152 TYN---FNQESRPPNSVGRPFPNVEIEIRNADGGEIGKIFVKSEMVFSGYVRG-----------GFSNPDGWMSVGDIGY 217
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218563680 488 LDQFAYCKIEGRIKDLIIRGGENIYPAEIEQFLHTHPKILEAQVVGVKDERMGEEVCACIrlkEGQECTVEEIKAYCKGK 567
Cdd:cd17633 218 VDEEGYLYLVGRESDMIIIGGINIFPTEIESVLKAIPGIEEAIVVGIPDARFGEIAVALY---SGDKLTYKQLKRFLKQK 294
|
330 340
....*....|....*....|....
gi 218563680 568 IAHYKVPRYILFVQDYPLTITGKI 591
Cdd:cd17633 295 LSRYEIPKKIIFVDSLPYTSSGKI 318
|
|
| PRK07788 |
PRK07788 |
acyl-CoA synthetase; Validated |
74-598 |
1.55e-52 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236097 [Multi-domain] Cd Length: 549 Bit Score: 188.60 E-value: 1.55e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218563680 74 ATVERYPDREAmvFVQDGIRKTFAEFYQDVEKAAAGLLAAGLKRGDRLGMWGPNIYEWVLMQFATAKAGIILVAVNPAY- 152
Cdd:PRK07788 57 HAARRAPDRAA--LIDERGTLTYAELDEQSNALARGLLALGVRAGDGVAVLARNHRGFVLALYAAGKVGARIILLNTGFs 134
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218563680 153 --QLQEVefALR-KVqcNAVVcptkfKSQHYCDMLKQLCPEME-------TASPGGIKSSRLPDLHTVIVTDSQ------ 216
Cdd:PRK07788 135 gpQLAEV--AAReGV--KALV-----YDDEFTDLLSALPPDLGrlrawggNPDDDEPSGSTDETLDDLIAGSSTaplpkp 205
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218563680 217 -QPGSFLLkdlmqagssqhyqqlqdlqkklvcddpiniqFTSGTTGKPKGATLSHHNIVnnAYFTGM--RIgyNWRKNVR 293
Cdd:PRK07788 206 pKPGGIVI-------------------------------LTSGTTGTPKGAPRPEPSPL--APLAGLlsRV--PFRAGET 250
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218563680 294 ICLPVPLYHCFGSVGGGVIMALyGTTVIFPSTgYDGRANLRAIEKEKCTFVYGTPTMYIDMLGQPD--LAKFDLSSVRGG 371
Cdd:PRK07788 251 TLLPAPMFHATGWAHLTLAMAL-GSTVVLRRR-FDPEATLEDIAKHKATALVVVPVMLSRILDLGPevLAKYDTSSLKII 328
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218563680 372 IAAGSPCPPEVMRKILNVMG--IKEMvigYGTTENSPVTFCGfPVDSAERKiETVGCISPHTEAKVVDPTtGEIVPLGAQ 449
Cdd:PRK07788 329 FVSGSALSPELATRALEAFGpvLYNL---YGSTEVAFATIAT-PEDLAEAP-GTVGRPPKGVTVKILDEN-GNEVPRGVV 402
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218563680 450 GELMIRGYCVMLEYWQDEEKTRecitKDRWYKTGDIASLDQFAYCKIEGRIKDLIIRGGENIYPAEIEQFLHTHPKILEA 529
Cdd:PRK07788 403 GRIFVGNGFPFEGYTDGRDKQI----IDGLLSSGDVGYFDEDGLLFVDGRDDDMIVSGGENVFPAEVEDLLAGHPDVVEA 478
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 218563680 530 QVVGVKDERMGEEVCACIRLKEGQECTVEEIKAYCKGKIAHYKVPRYILFVQDYPLTITGKIQKHKLRE 598
Cdd:PRK07788 479 AVIGVDDEEFGQRLRAFVVKAPGAALDEDAIKDYVRDNLARYKVPRDVVFLDELPRNPTGKVLKRELRE 547
|
|
| PRK07008 |
PRK07008 |
long-chain-fatty-acid--CoA ligase; Validated |
255-598 |
1.66e-52 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 235908 [Multi-domain] Cd Length: 539 Bit Score: 188.38 E-value: 1.66e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218563680 255 FTSGTTGKPKGATLSHHNIVNNAYFTGM--RIGYNWRKNVricLP-VPLYHCfGSVGGGVIMALYGTTVIFPSTGYDGRA 331
Cdd:PRK07008 183 YTSGTTGNPKGALYSHRSTVLHAYGAALpdAMGLSARDAV---LPvVPMFHV-NAWGLPYSAPLTGAKLVLPGPDLDGKS 258
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218563680 332 NLRAIEKEKCTFVYGTPTMYIDMLGQPDLAKFDLSSVRGGIAAGSPCPPEVMRKILNVMGIkEMVIGYGTTENSPV-TFC 410
Cdd:PRK07008 259 LYELIEAERVTFSAGVPTVWLGLLNHMREAGLRFSTLRRTVIGGSACPPAMIRTFEDEYGV-EVIHAWGMTEMSPLgTLC 337
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218563680 411 -------GFPVDSAERKIETVGCISPHTEAKVVDPTTGEIVPLG-AQGELMIRGYCVMLEYWQDEEKTreciTKDRWYKT 482
Cdd:PRK07008 338 klkwkhsQLPLDEQRKLLEKQGRVIYGVDMKIVGDDGRELPWDGkAFGDLQVRGPWVIDRYFRGDASP----LVDGWFPT 413
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218563680 483 GDIASLDQFAYCKIEGRIKDLIIRGGENIYPAEIEQFLHTHPKILEAQVVGVKDERMGEEVCACIRLKEGQECTVEEIKA 562
Cdd:PRK07008 414 GDVATIDADGFMQITDRSKDVIKSGGEWISSIDIENVAVAHPAVAEAACIACAHPKWDERPLLVVVKRPGAEVTREELLA 493
|
330 340 350
....*....|....*....|....*....|....*.
gi 218563680 563 YCKGKIAHYKVPRYILFVQDYPLTITGKIQKHKLRE 598
Cdd:PRK07008 494 FYEGKVAKWWIPDDVVFVDAIPHTATGKLQKLKLRE 529
|
|
| MACS_like |
cd05972 |
Medium-chain acyl-CoA synthetase (MACS or ACSM); MACS catalyzes the two-step activation of ... |
236-597 |
1.70e-52 |
|
Medium-chain acyl-CoA synthetase (MACS or ACSM); MACS catalyzes the two-step activation of medium chain fatty acids (containing 4-12 carbons). The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. The acyl-CoA is a key intermediate in many important biosynthetic and catabolic processes.
Pssm-ID: 341276 [Multi-domain] Cd Length: 428 Bit Score: 185.62 E-value: 1.70e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218563680 236 QQLQDLQKK-LVCD--DPINIQFTSGTTGKPKGATLSHH----NIVNNAYFTGMR---IGYN-----WRKNVriclpvpL 300
Cdd:cd05972 66 YRLEAAGAKaIVTDaeDPALIYFTSGTTGLPKGVLHTHSyplgHIPTAAYWLGLRpddIHWNiadpgWAKGA-------W 138
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218563680 301 YHCFGSVGGGVimalygTTVIFPSTGYDGRANLRAIEKEKCTFVYGTPTMYiDMLGQPDLAKFDLSSVRGGIAAGSPCPP 380
Cdd:cd05972 139 SSFFGPWLLGA------TVFVYEGPRFDAERILELLERYGVTSFCGPPTAY-RMLIKQDLSSYKFSHLRLVVSAGEPLNP 211
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218563680 381 EVMRKILNVMGIKEMViGYGTTENSPV--TFCGFPVdsaerKIETVGCISPHTEAKVVDpTTGEIVPLGAQGELMIRGYC 458
Cdd:cd05972 212 EVIEWWRAATGLPIRD-GYGQTETGLTvgNFPDMPV-----KPGSMGRPTPGYDVAIID-DDGRELPPGEEGDIAIKLPP 284
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218563680 459 V--MLEYWQDEEKTRECITKDrWYKTGDIASLDQFAYCKIEGRIKDLIIRGGENIYPAEIEQFLHTHPKILEAQVVGVKD 536
Cdd:cd05972 285 PglFLGYVGDPEKTEASIRGD-YYLTGDRAYRDEDGYFWFVGRADDIIKSSGYRIGPFEVESALLEHPAVAEAAVVGSPD 363
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 218563680 537 ERMGEEVCACIRLKEG---QECTVEEIKAYCKGKIAHYKVPRYILFVQDYPLTITGKIQKHKLR 597
Cdd:cd05972 364 PVRGEVVKAFVVLTSGyepSEELAEELQGHVKKVLAPYKYPREIEFVEELPKTISGKIRRVELR 427
|
|
| PLN02860 |
PLN02860 |
o-succinylbenzoate-CoA ligase |
70-597 |
2.78e-52 |
|
o-succinylbenzoate-CoA ligase
Pssm-ID: 215464 [Multi-domain] Cd Length: 563 Bit Score: 188.47 E-value: 2.78e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218563680 70 QCLQATVERYPDreAMVFVQDGIRKTFAEFYQDVEKAAAGLLAAGLKRGDRLGMWGPNIYEWVLMQFATAKAGIILVAVN 149
Cdd:PLN02860 11 QCLTRLATLRGN--AVVTISGNRRRTGHEFVDGVLSLAAGLLRLGLRNGDVVAIAALNSDLYLEWLLAVACAGGIVAPLN 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218563680 150 PAYQLQEVEFALRKVQcnAVVCPTKFKSQHYCDMLKqlcpemetaspggikSSRLPDL--HTVIVTDSQQPGSFLLKDLM 227
Cdd:PLN02860 89 YRWSFEEAKSAMLLVR--PVMLVTDETCSSWYEELQ---------------NDRLPSLmwQVFLESPSSSVFIFLNSFLT 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218563680 228 QAGSSQHYQQLQDLQKKLVCDDPINIQFTSGTTGKPKGATLSHHNIVNNAYFTGMRIGYNwRKNVRICLpVPLYHcFGSV 307
Cdd:PLN02860 152 TEMLKQRALGTTELDYAWAPDDAVLICFTSGTTGRPKGVTISHSALIVQSLAKIAIVGYG-EDDVYLHT-APLCH-IGGL 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218563680 308 GGGVIMALYGTT-VIFPStgYDGRANLRAIEKEKCTFVYGTPTMYIDMLGQPDLAKFDLS--SVRGGIAAGSPCPPEVMR 384
Cdd:PLN02860 229 SSALAMLMVGAChVLLPK--FDAKAALQAIKQHNVTSMITVPAMMADLISLTRKSMTWKVfpSVRKILNGGGSLSSRLLP 306
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218563680 385 KILNVMGIKEMVIGYGTTEN-SPVTF-------CGFPVDSAERKIET------------VGCISPHTEAKVVDPTTGEIv 444
Cdd:PLN02860 307 DAKKLFPNAKLFSAYGMTEAcSSLTFmtlhdptLESPKQTLQTVNQTksssvhqpqgvcVGKPAPHVELKIGLDESSRV- 385
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218563680 445 plgaqGELMIRGYCVMLEYWQDEEKTRECITKDRWYKTGDIASLDQFAYCKIEGRIKDLIIRGGENIYPAEIEQFLHTHP 524
Cdd:PLN02860 386 -----GRILTRGPHVMLGYWGQNSETASVLSNDGWLDTGDIGWIDKAGNLWLIGRSNDRIKTGGENVYPEEVEAVLSQHP 460
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218563680 525 KILEAQVVGVKDERMGEEVCACIRLKEG------------QECTV--EEIKAYCKGK-IAHYKVPR-YILFVQDYPLTIT 588
Cdd:PLN02860 461 GVASVVVVGVPDSRLTEMVVACVRLRDGwiwsdnekenakKNLTLssETLRHHCREKnLSRFKIPKlFVQWRKPFPLTTT 540
|
....*....
gi 218563680 589 GKIQKHKLR 597
Cdd:PLN02860 541 GKIRRDEVR 549
|
|
| benz_CoA_lig |
TIGR02262 |
benzoate-CoA ligase family; Characterized members of this protein family include benzoate-CoA ... |
68-598 |
6.07e-52 |
|
benzoate-CoA ligase family; Characterized members of this protein family include benzoate-CoA ligase, 4-hydroxybenzoate-CoA ligase, 2-aminobenzoate-CoA ligase, etc. Members are related to fatty acid and acetate CoA ligases.
Pssm-ID: 274059 [Multi-domain] Cd Length: 505 Bit Score: 186.20 E-value: 6.07e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218563680 68 VDQCLQATVERyPDREAMVFVQDGIRKTFAEFYQDVEKAAAGLLAAGLKRGDRLGMWGPNIYEWVLMQFATAKAGIILVA 147
Cdd:TIGR02262 6 AEDLLDRNVVE-GRGGKTAFIDDISSLSYGELEAQVRRLAAALRRLGVKREERVLLLMLDGVDFPIAFLGAIRAGIVPVA 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218563680 148 VNPAYQLQEVEFALRKVQCNAVvcptkFKSQhycdmlkQLCPEMETASpggiksSRLPDLHTVIVTDSQQPGSFLLKDLM 227
Cdd:TIGR02262 85 LNTLLTADDYAYMLEDSRARVV-----FVSG-------ALLPVIKAAL------GKSPHLEHRVVVGRPEAGEVQLAELL 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218563680 228 QAGSSQhyqqlqdLQKKLVC-DDPINIQFTSGTTGKPKGATLSHHNIVNNA-YFTGMRIGYnwRKNVRICLPVPLYHCFG 305
Cdd:TIGR02262 147 ATESEQ-------FKPAATQaDDPAFWLYSSGSTGMPKGVVHTHSNPYWTAeLYARNTLGI--REDDVCFSAAKLFFAYG 217
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218563680 306 sVGGGVI--MALYGTTVIFPSTGYDGRAnLRAIEKEKCTFVYGTPTMYIDMLGQPDLAKFDLSSVRGGIAAGSPCPPEVM 383
Cdd:TIGR02262 218 -LGNALTfpMSVGATTVLMGERPTPDAV-FDRLRRHQPTIFYGVPTLYAAMLADPNLPSEDQVRLRLCTSAGEALPAEVG 295
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218563680 384 RKILNVMGIkEMVIGYGTTENSPVTFCGFPVDSaerKIETVGCISPHTEAKVVDpTTGEIVPLGAQGELMIRGYCVMLEY 463
Cdd:TIGR02262 296 QRWQARFGV-DIVDGIGSTEMLHIFLSNLPGDV---RYGTSGKPVPGYRLRLVG-DGGQDVADGEPGELLISGPSSATMY 370
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218563680 464 WQDEEKTRECITKDrWYKTGDIASLDQFAYCKIEGRIKDLIIRGGENIYPAEIEQFLHTHPKILEAQVVGVKDERMGEEV 543
Cdd:TIGR02262 371 WNNRAKSRDTFQGE-WTRSGDKYVRNDDGSYTYAGRTDDMLKVSGIYVSPFEIESALIQHPAVLEAAVVGVADEDGLIKP 449
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*
gi 218563680 544 CACIRLKEGQECTVEEIKAYCKGKIAHYKVPRYILFVQDYPLTITGKIQKHKLRE 598
Cdd:TIGR02262 450 KAFVVLRPGQTALETELKEHVKDRLAPYKYPRWIVFVDDLPKTATGKIQRFKLRE 504
|
|
| PLN02479 |
PLN02479 |
acetate-CoA ligase |
74-605 |
8.54e-52 |
|
acetate-CoA ligase
Pssm-ID: 178097 [Multi-domain] Cd Length: 567 Bit Score: 186.97 E-value: 8.54e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218563680 74 ATVerYPDREAMVfvQDGIRKTFAEFYQDVEKAAAGLLAAGLKRGDRLGMWGPNI---YEwvlMQFATAKAGIILVAVNP 150
Cdd:PLN02479 30 AVV--HPTRKSVV--HGSVRYTWAQTYQRCRRLASALAKRSIGPGSTVAVIAPNIpamYE---AHFGVPMAGAVVNCVNI 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218563680 151 AYQLQEVEFALRKVQCNAVVCPTKFKSqhycdmlkqLCPEMETASPGGIKSSRLPDLHTVIVTDSQQPGSflLKDLMQAG 230
Cdd:PLN02479 103 RLNAPTIAFLLEHSKSEVVMVDQEFFT---------LAEEALKILAEKKKSSFKPPLLIVIGDPTCDPKS--LQYALGKG 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218563680 231 SSQHYQQLQDLQKKLVCDDP------INIQFTSGTTGKPKGATLSHHNI----VNNAYFTGMRIG--YNWrknvriclPV 298
Cdd:PLN02479 172 AIEYEKFLETGDPEFAWKPPadewqsIALGYTSGTTASPKGVVLHHRGAylmaLSNALIWGMNEGavYLW--------TL 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218563680 299 PLYHCFGSVGGGVIMALYGTTVIFPSTgyDGRANLRAIEKEKCTFVYGTPTMYIDMLGQPDLAKF-DLSSVRGGIAAGSP 377
Cdd:PLN02479 244 PMFHCNGWCFTWTLAALCGTNICLRQV--TAKAIYSAIANYGVTHFCAAPVVLNTIVNAPKSETIlPLPRVVHVMTAGAA 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218563680 378 CPPEVMRKiLNVMGIKeMVIGYGTTEN-SPVTFCGF-------PVDSAERKIETVGCISPHTEA-KVVDPTTGEIVPLGA 448
Cdd:PLN02479 322 PPPSVLFA-MSEKGFR-VTHTYGLSETyGPSTVCAWkpewdslPPEEQARLNARQGVRYIGLEGlDVVDTKTMKPVPADG 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218563680 449 Q--GELMIRGYCVMLEYWQDEEKTRECItKDRWYKTGDIASLDQFAYCKIEGRIKDLIIRGGENIYPAEIEQFLHTHPKI 526
Cdd:PLN02479 400 KtmGEIVMRGNMVMKGYLKNPKANEEAF-ANGWFHSGDLGVKHPDGYIEIKDRSKDIIISGGENISSLEVENVVYTHPAV 478
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218563680 527 LEAQVVGVKDERMGEEVCACIRLKEG-----QECTVEEIKAYCKGKIAHYKVPRYILFvQDYPLTITGKIQKHKLRERTe 601
Cdd:PLN02479 479 LEASVVARPDERWGESPCAFVTLKPGvdksdEAALAEDIMKFCRERLPAYWVPKSVVF-GPLPKTATGKIQKHVLRAKA- 556
|
....
gi 218563680 602 KQLG 605
Cdd:PLN02479 557 KEMG 560
|
|
| PRK07798 |
PRK07798 |
acyl-CoA synthetase; Validated |
72-590 |
4.88e-51 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236100 [Multi-domain] Cd Length: 533 Bit Score: 184.32 E-value: 4.88e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218563680 72 LQATVERYPDREAmvFVQDGIRKTFAEFYQDVEKAAAGLLAAGLKRGDRLGMWGPNIYEWVLMQFATAKAGIILVAVNPA 151
Cdd:PRK07798 9 FEAVADAVPDRVA--LVCGDRRLTYAELEERANRLAHYLIAQGLGPGDHVGIYARNRIEYVEAMLGAFKARAVPVNVNYR 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218563680 152 YQLQEVEFALRKVQCNAVVcptkFKSQhYCDMLKQLCPemetaspggikssRLPDLHTVIVTD-----SQQPGSFLLKDL 226
Cdd:PRK07798 87 YVEDELRYLLDDSDAVALV----YERE-FAPRVAEVLP-------------RLPKLRTLVVVEdgsgnDLLPGAVDYEDA 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218563680 227 MQAGSSQhyqqlQDLQKKlvCDDPINIQFTSGTTGKPKGATLSHHNIvnnaYFTGMRiGYNWRKN--------------- 291
Cdd:PRK07798 149 LAAGSPE-----RDFGER--SPDDLYLLYTGGTTGMPKGVMWRQEDI----FRVLLG-GRDFATGepiedeeelakraaa 216
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218563680 292 ----VRICLPvPLYHcfgsvGGG---VIMALY--GTTVIFPSTGYDGRANLRAIEKEKCTFVygtpTMYIDMLGQPDLA- 361
Cdd:PRK07798 217 gpgmRRFPAP-PLMH-----GAGqwaAFAALFsgQTVVLLPDVRFDADEVWRTIEREKVNVI----TIVGDAMARPLLDa 286
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218563680 362 -----KFDLSSVRGGIAAGSPCPPEVMRKILNVMGIKEMVIGYGTTENSpvtFCGFPVdSAERKIETVGC---ISPHTea 433
Cdd:PRK07798 287 leargPYDLSSLFAIASGGALFSPSVKEALLELLPNVVLTDSIGSSETG---FGGSGT-VAKGAVHTGGPrftIGPRT-- 360
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218563680 434 KVVDPTTGEIVP-LGAQGELMIRGYcVMLEYWQDEEKTREC---ITKDRWYKTGDIASLDQfayckiEGRIKDL------ 503
Cdd:PRK07798 361 VVLDEDGNPVEPgSGEIGWIARRGH-IPLGYYKDPEKTAETfptIDGVRYAIPGDRARVEA------DGTITLLgrgsvc 433
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218563680 504 IIRGGENIYPAEIEQFLHTHPKILEAQVVGVKDERMGEEVCACIRLKEGQECTVEEIKAYCKGKIAHYKVPRYILFVQDY 583
Cdd:PRK07798 434 INTGGEKVFPEEVEEALKAHPDVADALVVGVPDERWGQEVVAVVQLREGARPDLAELRAHCRSSLAGYKVPRAIWFVDEV 513
|
....*..
gi 218563680 584 PLTITGK 590
Cdd:PRK07798 514 QRSPAGK 520
|
|
| PRK07470 |
PRK07470 |
acyl-CoA synthetase; Validated |
70-603 |
1.10e-50 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 180988 [Multi-domain] Cd Length: 528 Bit Score: 183.32 E-value: 1.10e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218563680 70 QCLQATVERYPDREAmvFVQDGIRKTFAEFYQDVEKAAAGLLAAGLKRGDRLGMWGPNIYEWVLMQFATAKAGIILVAVN 149
Cdd:PRK07470 11 HFLRQAARRFPDRIA--LVWGDRSWTWREIDARVDALAAALAARGVRKGDRILVHSRNCNQMFESMFAAFRLGAVWVPTN 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218563680 150 PAYQLQEVEFALRKVQCNAVVCPTKFksqhycdmlkqlcPEMETASpggikSSRLPDLHTVIVTDSQqPGSFLLKDLMQA 229
Cdd:PRK07470 89 FRQTPDEVAYLAEASGARAMICHADF-------------PEHAAAV-----RAASPDLTHVVAIGGA-RAGLDYEALVAR 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218563680 230 GSSQHYQQLQDLQkklvcDDPINIQFTSGTTGKPKGATLSHHN---IVNNayftgmrigynwrknvRIC--LP------- 297
Cdd:PRK07470 150 HLGARVANAAVDH-----DDPCWFFFTSGTTGRPKAAVLTHGQmafVITN----------------HLAdlMPgtteqda 208
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218563680 298 ----VPLYHcfgsvGGGV----IMALYGTTVIFPSTGYDGRANLRAIEKEKCTFVYGTPTMYIDMLGQPDLAKFDLSSVR 369
Cdd:PRK07470 209 slvvAPLSH-----GAGIhqlcQVARGAATVLLPSERFDPAEVWALVERHRVTNLFTVPTILKMLVEHPAVDRYDHSSLR 283
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218563680 370 GGIAAGSPCPPEVMRKILNVMGiKEMVIGYGTTEnspVTFC--------GFPVDSAERKIETVGCISPHTEAKVVDpTTG 441
Cdd:PRK07470 284 YVIYAGAPMYRADQKRALAKLG-KVLVQYFGLGE---VTGNitvlppalHDAEDGPDARIGTCGFERTGMEVQIQD-DEG 358
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218563680 442 EIVPLGAQGELMIRGYCVMLEYWQDEEKTRECItKDRWYKTGDIASLDQFAYCKIEGRIKDLIIRGGENIYPAEIEQFLH 521
Cdd:PRK07470 359 RELPPGETGEICVIGPAVFAGYYNNPEANAKAF-RDGWFRTGDLGHLDARGFLYITGRASDMYISGGSNVYPREIEEKLL 437
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218563680 522 THPKILEAQVVGVKDERMGEEVCACIRLKEGQECTVEEIKAYCKGKIAHYKVPRYILFVQDYPLTITGKIQKHKLRERTE 601
Cdd:PRK07470 438 THPAVSEVAVLGVPDPVWGEVGVAVCVARDGAPVDEAELLAWLDGKVARYKLPKRFFFWDALPKSGYGKITKKMVREELE 517
|
..
gi 218563680 602 KQ 603
Cdd:PRK07470 518 ER 519
|
|
| MACS_like_4 |
cd05969 |
Uncharacterized subfamily of Acetyl-CoA synthetase like family (ACS); This family is most ... |
201-599 |
1.13e-50 |
|
Uncharacterized subfamily of Acetyl-CoA synthetase like family (ACS); This family is most similar to acetyl-CoA synthetase. Acetyl-CoA synthetase (ACS) catalyzes the formation of acetyl-CoA from acetate, CoA, and ATP. Synthesis of acetyl-CoA is carried out in a two-step reaction. In the first step, the enzyme catalyzes the synthesis of acetyl-AMP intermediate from acetate and ATP. In the second step, acetyl-AMP reacts with CoA to produce acetyl-CoA. This enzyme is only present in bacteria.
Pssm-ID: 341273 [Multi-domain] Cd Length: 442 Bit Score: 181.16 E-value: 1.13e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218563680 201 SSRLPDLH----------TVIVTDSQQPGSFLLKDLMQAGSSQHYQQLQDLQKKLVCDDPINIQFTSGTTGKPKGATLSH 270
Cdd:cd05969 32 SPRSPELYfsmlgigkigAVICPLFSAFGPEAIRDRLENSEAKVLITTEELYERTDPEDPTLLHYTSGTTGTPKGVLHVH 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218563680 271 hNIVNNAYFTGmrigynwrKNVRICLPVPLYHCFGSVG------GGVIMA-LYGTTVIFPSTGYDGRANLRAIEKEKCTF 343
Cdd:cd05969 112 -DAMIFYYFTG--------KYVLDLHPDDIYWCTADPGwvtgtvYGIWAPwLNGVTNVVYEGRFDAESWYGIIERVKVTV 182
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218563680 344 VYGTPTMyIDML---GQPDLAKFDLSSVRGGIAAGSPCPPEVMRKILNVMGIKeMVIGYGTTENSPVTFCGFPvdSAERK 420
Cdd:cd05969 183 WYTAPTA-IRMLmkeGDELARKYDLSSLRFIHSVGEPLNPEAIRWGMEVFGVP-IHDTWWQTETGSIMIANYP--CMPIK 258
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218563680 421 IETVGCISPHTEAKVVDpTTGEIVPLGAQGELMIR-GYCVMLE-YWQDEEKTRECItKDRWYKTGDIASLDQFAYCKIEG 498
Cdd:cd05969 259 PGSMGKPLPGVKAAVVD-ENGNELPPGTKGILALKpGWPSMFRgIWNDEERYKNSF-IDGWYLTGDLAYRDEDGYFWFVG 336
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218563680 499 RIKDLIIRGGENIYPAEIEQFLHTHPKILEAQVVGVKDERMGEEVCACIRLKEGQECTVE---EIKAYCKGKIAHYKVPR 575
Cdd:cd05969 337 RADDIIKTSGHRVGPFEVESALMEHPAVAEAGVIGKPDPLRGEIIKAFISLKEGFEPSDElkeEIINFVRQKLGAHVAPR 416
|
410 420
....*....|....*....|....
gi 218563680 576 YILFVQDYPLTITGKIQKHKLRER 599
Cdd:cd05969 417 EIEFVDNLPKTRSGKIMRRVLKAK 440
|
|
| PLN02246 |
PLN02246 |
4-coumarate--CoA ligase |
116-599 |
1.15e-50 |
|
4-coumarate--CoA ligase
Pssm-ID: 215137 [Multi-domain] Cd Length: 537 Bit Score: 183.26 E-value: 1.15e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218563680 116 KRGDRLGMWGPNIYEWVLMQFATAKAGIILVAVNPAYQLQEVEFALRKvqCNAVVCPTKfksQHYCDMLKQLcpemetAS 195
Cdd:PLN02246 73 RQGDVVMLLLPNCPEFVLAFLGASRRGAVTTTANPFYTPAEIAKQAKA--SGAKLIITQ---SCYVDKLKGL------AE 141
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218563680 196 PGGIkssrlpdlhTVIVTDSQQPGSFLLKDLMQAGSSQHyqqlqdLQKKLVCDDPINIQFTSGTTGKPKGATLSHHNIVN 275
Cdd:PLN02246 142 DDGV---------TVVTIDDPPEGCLHFSELTQADENEL------PEVEISPDDVVALPYSSGTTGLPKGVMLTHKGLVT 206
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218563680 276 -----------NAYFTGmrigynwrKNVRICLpVPLYH--CFGSVgggVIMALY--GTTVIFPStgYDGRANLRAIEKEK 340
Cdd:PLN02246 207 svaqqvdgenpNLYFHS--------DDVILCV-LPMFHiySLNSV---LLCGLRvgAAILIMPK--FEIGALLELIQRHK 272
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218563680 341 CTFVYGTPTMYIDMLGQPDLAKFDLSSVRGGIAAGSPCPPE----VMRKILN-VMGIkemviGYGTTENSPV-TFC---- 410
Cdd:PLN02246 273 VTIAPFVPPIVLAIAKSPVVEKYDLSSIRMVLSGAAPLGKEledaFRAKLPNaVLGQ-----GYGMTEAGPVlAMClafa 347
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218563680 411 --GFPVDSAerkieTVGCISPHTEAKVVDPTTGEIVPLGAQGELMIRGYCVMLEYWQDEEKTRECITKDRWYKTGDIASL 488
Cdd:PLN02246 348 kePFPVKSG-----SCGTVVRNAELKIVDPETGASLPRNQPGEICIRGPQIMKGYLNDPEATANTIDKDGWLHTGDIGYI 422
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218563680 489 DQFAYCKIEGRIKDLIIRGGENIYPAEIEQFLHTHPKILEAQVVGVKDERMGEEVCACIRLKEGQECTVEEIKAYCKGKI 568
Cdd:PLN02246 423 DDDDELFIVDRLKELIKYKGFQVAPAELEALLISHPSIADAAVVPMKDEVAGEVPVAFVVRSNGSEITEDEIKQFVAKQV 502
|
490 500 510
....*....|....*....|....*....|.
gi 218563680 569 AHYKVPRYILFVQDYPLTITGKIQKHKLRER 599
Cdd:PLN02246 503 VFYKRIHKVFFVDSIPKAPSGKILRKDLRAK 533
|
|
| MACS_AAE_MA_like |
cd05970 |
Medium-chain acyl-CoA synthetase (MACS) of AAE_MA like; MACS catalyzes the two-step activation ... |
72-599 |
3.92e-50 |
|
Medium-chain acyl-CoA synthetase (MACS) of AAE_MA like; MACS catalyzes the two-step activation of medium chain fatty acids (containing 4-12 carbons). The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This family of MACS enzymes is found in archaea and bacteria. It is represented by the acyl-adenylating enzyme from Methanosarcina acetivorans (AAE_MA). AAE_MA is most active with propionate, butyrate, and the branched analogs: 2-methyl-propionate, butyrate, and pentanoate. The specific activity is weaker for smaller or larger acids.
Pssm-ID: 341274 [Multi-domain] Cd Length: 537 Bit Score: 181.92 E-value: 3.92e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218563680 72 LQATVERYPDREAMVFVQD-GIRK--TFAEFYQDVEKAAAGLLAAGLKRGDRLGMWGPNIYE-WVLMqFATAKAGIILVA 147
Cdd:cd05970 23 VDAMAKEYPDKLALVWCDDaGEERifTFAELADYSDKTANFFKAMGIGKGDTVMLTLKRRYEfWYSL-LALHKLGAIAIP 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218563680 148 VNPAYQLQEVEFALRKVQCNAVVCptkfksqhycDMLKQLCPEMETASPGGIKSSRLpdlhtVIVTDSQQPGSFLLKDLM 227
Cdd:cd05970 102 ATHQLTAKDIVYRIESADIKMIVA----------IAEDNIPEEIEKAAPECPSKPKL-----VWVGDPVPEGWIDFRKLI 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218563680 228 qAGSSQHYQQLQDlQKKLVCDDPINIQFTSGTTGKPKgaTLSHhnivNNAYFTGMRIGYNWRKNVRiclPVPLYHCFGSV 307
Cdd:cd05970 167 -KNASPDFERPTA-NSYPCGEDILLVYFSSGTTGMPK--MVEH----DFTYPLGHIVTAKYWQNVR---EGGLHLTVADT 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218563680 308 GGGVIM--ALYG------TTVIFPSTGYDGRANLRAIEKEKCTFVYGTPTMYiDMLGQPDLAKFDLSSVRGGIAAGSPCP 379
Cdd:cd05970 236 GWGKAVwgKIYGqwiagaAVFVYDYDKFDPKALLEKLSKYGVTTFCAPPTIY-RFLIREDLSRYDLSSLRYCTTAGEALN 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218563680 380 PEVMRKILNVMGIKEMViGYGTTENSpVTFCGFPvdSAERKIETVGCISPHTEAKVVDPTtGEIVPLGAQGELMIR---G 456
Cdd:cd05970 315 PEVFNTFKEKTGIKLME-GFGQTETT-LTIATFP--WMEPKPGSMGKPAPGYEIDLIDRE-GRSCEAGEEGEIVIRtskG 389
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218563680 457 YCVML--EYWQDEEKTREcITKDRWYKTGDIASLDQFAYCKIEGRIKDLIIRGGENIYPAEIEQFLHTHPKILEAQVVGV 534
Cdd:cd05970 390 KPVGLfgGYYKDAEKTAE-VWHDGYYHTGDAAWMDEDGYLWFVGRTDDLIKSSGYRIGPFEVESALIQHPAVLECAVTGV 468
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 218563680 535 KDERMGEEVCACIRLKEGQECTVE---EIKAYCKGKIAHYKVPRYILFVQDYPLTITGKIQKHKLRER 599
Cdd:cd05970 469 PDPIRGQVVKATIVLAKGYEPSEElkkELQDHVKKVTAPYKYPRIVEFVDELPKTISGKIRRVEIRER 536
|
|
| MACS_euk |
cd05928 |
Eukaryotic Medium-chain acyl-CoA synthetase (MACS or ACSM); MACS catalyzes the two-step ... |
116-599 |
2.87e-49 |
|
Eukaryotic Medium-chain acyl-CoA synthetase (MACS or ACSM); MACS catalyzes the two-step activation of medium chain fatty acids (containing 4-12 carbons). The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. The acyl-CoA is a key intermediate in many important biosynthetic and catabolic processes. MACS enzymes are localized to mitochondria. Two murine MACS family proteins are found in liver and kidney. In rodents, a MACS member is detected particularly in the olfactory epithelium and is called O-MACS. O-MACS demonstrates substrate preference for the fatty acid lengths of C6-C12.
Pssm-ID: 341251 [Multi-domain] Cd Length: 530 Bit Score: 179.58 E-value: 2.87e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218563680 116 KRGDRLGMWGPNIYEWVLMQFATAKAGIILVAVNPAYQLQEVEFALRKVQCNAVVCPtkfksqhycdmlKQLCPEMETAS 195
Cdd:cd05928 65 QRGDRVAVILPRVPEWWLVNVACIRTGLVFIPGTIQLTAKDILYRLQASKAKCIVTS------------DELAPEVDSVA 132
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218563680 196 pggiksSRLPDLHT-VIVTDSQQPGSFLLKDLMQAGSSQHyqqlqdlqkklVC-----DDPINIQFTSGTTGKPKGATLS 269
Cdd:cd05928 133 ------SECPSLKTkLLVSEKSRDGWLNFKELLNEASTEH-----------HCvetgsQEPMAIYFTSGTTGSPKMAEHS 195
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218563680 270 HHNI-----VNNAYFTGMR---IGYN-----WRKNVRICLPVPLyhcfgsVGGGVI----MALYGTTVIfpstgydgran 332
Cdd:cd05928 196 HSSLglglkVNGRYWLDLTasdIMWNtsdtgWIKSAWSSLFEPW------IQGACVfvhhLPRFDPLVI----------- 258
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218563680 333 LRAIEKEKCTFVYGTPTMYiDMLGQPDLAKFDLSSVRGGIAAGSPCPPEVMRKILNVMGIkEMVIGYGTTENspVTFCGF 412
Cdd:cd05928 259 LKTLSSYPITTFCGAPTVY-RMLVQQDLSSYKFPSLQHCVTGGEPLNPEVLEKWKAQTGL-DIYEGYGQTET--GLICAN 334
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218563680 413 PvDSAERKIETVGCISPHTEAKVVDpTTGEIVPLGAQGELMI-----RGYCVMLEYWQDEEKTRECITKDrWYKTGDIAS 487
Cdd:cd05928 335 F-KGMKIKPGSMGKASPPYDVQIID-DNGNVLPPGTEGDIGIrvkpiRPFGLFSGYVDNPEKTAATIRGD-FYLTGDRGI 411
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218563680 488 LDQFAYCKIEGRIKDLIIRGGENIYPAEIEQFLHTHPKILEAQVVGVKDERMGEEVCACIRL-----KEGQECTVEEIKA 562
Cdd:cd05928 412 MDEDGYFWFMGRADDVINSSGYRIGPFEVESALIEHPAVVESAVVSSPDPIRGEVVKAFVVLapqflSHDPEQLTKELQQ 491
|
490 500 510
....*....|....*....|....*....|....*..
gi 218563680 563 YCKGKIAHYKVPRYILFVQDYPLTITGKIQKHKLRER 599
Cdd:cd05928 492 HVKSVTAPYKYPRKVEFVQELPKTVTGKIQRNELRDK 528
|
|
| OSB_MenE-like |
cd17630 |
O-succinylbenzoic acid-CoA ligase; This family contains O-succinylbenzoyl-CoA (OSB-CoA) ... |
249-599 |
4.13e-49 |
|
O-succinylbenzoic acid-CoA ligase; This family contains O-succinylbenzoyl-CoA (OSB-CoA) synthetase (also known as O-succinylbenzoic acid CoA ligase) that belongs to the ANL superfamily and catalyzes the ligation of CoA to o-succinylbenzoate (OSB). It includes MenE in the bacterial menaquinone biosynthesis pathway which is a promising target for the development of novel antibacterial agents. MenE catalyzes CoA ligation via an acyl-adenylate intermediate; tight-binding inhibitors of MenE based on stable acyl-sulfonyladenosine analogs of this intermediate provide a pathway toward the development of optimized MenE inhibitors.
Pssm-ID: 341285 [Multi-domain] Cd Length: 325 Bit Score: 173.67 E-value: 4.13e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218563680 249 DPINIQFTSGTTGKPKGATLSHHNIVNNAYFTGMRIGYNWRKNVRICLPvpLYHcfgsVGGGVIM---ALYGTTVIFPST 325
Cdd:cd17630 1 RLATVILTSGSTGTPKAVVHTAANLLASAAGLHSRLGFGGGDSWLLSLP--LYH----VGGLAILvrsLLAGAELVLLER 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218563680 326 GydgRANLRAIEKEKCTFVYGTPTMYIDMLgQPDLAKFDLSSVRGGIAAGSPCPPEVMRKILNvMGIkEMVIGYGTTENS 405
Cdd:cd17630 75 N---QALAEDLAPPGVTHVSLVPTQLQRLL-DSGQGPAALKSLRAVLLGGAPIPPELLERAAD-RGI-PLYTTYGMTETA 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218563680 406 PvTFCGFPVDSAERKieTVGCISPHTEAKVVDPttgeivplgaqGELMIRGYCVMLEYWQDEEktRECITKDRWYKTGDI 485
Cdd:cd17630 149 S-QVATKRPDGFGRG--GVGVLLPGRELRIVED-----------GEIWVGGASLAMGYLRGQL--VPEFNEDGWFTTKDL 212
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218563680 486 ASLDQFAYCKIEGRIKDLIIRGGENIYPAEIEQFLHTHPKILEAQVVGVKDERMGEEVCACIRLKEGQecTVEEIKAYCK 565
Cdd:cd17630 213 GELHADGRLTVLGRADNMIISGGENIQPEEIEAALAAHPAVRDAFVVGVPDEELGQRPVAVIVGRGPA--DPAELRAWLK 290
|
330 340 350
....*....|....*....|....*....|....
gi 218563680 566 GKIAHYKVPRYILFVQDYPLTITGKIQKHKLRER 599
Cdd:cd17630 291 DKLARFKLPKRIYPVPELPRTGGGKVDRRALRAW 324
|
|
| PRK08633 |
PRK08633 |
2-acyl-glycerophospho-ethanolamine acyltransferase; Validated |
248-605 |
6.36e-49 |
|
2-acyl-glycerophospho-ethanolamine acyltransferase; Validated
Pssm-ID: 236315 [Multi-domain] Cd Length: 1146 Bit Score: 183.97 E-value: 6.36e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218563680 248 DDPINIQFTSGTTGKPKGATLSHHNIVNNAyfTGMRIGYNWRKNVRICLPVPLYHCFGSVGGGVIMALYGTTVIFPSTGY 327
Cdd:PRK08633 782 DDTATIIFSSGSEGEPKGVMLSHHNILSNI--EQISDVFNLRNDDVILSSLPFFHSFGLTVTLWLPLLEGIKVVYHPDPT 859
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218563680 328 DGRANLRAIEKEKCTFVYGTPTMYIDMLGQPDLAKFDLSSVRGGIAAGSPCPPEVMRKILNVMGIkEMVIGYGTTENSPV 407
Cdd:PRK08633 860 DALGIAKLVAKHRATILLGTPTFLRLYLRNKKLHPLMFASLRLVVAGAEKLKPEVADAFEEKFGI-RILEGYGATETSPV 938
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218563680 408 TFCGFP----VDSAER---KIETVGCISPHTEAKVVDPTTGEIVPLGAQGELMIRGYCVMLEYWQDEEKTRECIT---KD 477
Cdd:PRK08633 939 ASVNLPdvlaADFKRQtgsKEGSVGMPLPGVAVRIVDPETFEELPPGEDGLILIGGPQVMKGYLGDPEKTAEVIKdidGI 1018
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218563680 478 RWYKTGDIASLDQFAYCKIEGRIKDLIIRGGENIYPAEIEQFLHthpKILEAQ-----VVGVKDERMGEEVCACIRLKEG 552
Cdd:PRK08633 1019 GWYVTGDKGHLDEDGFLTITDRYSRFAKIGGEMVPLGAVEEELA---KALGGEevvfaVTAVPDEKKGEKLVVLHTCGAE 1095
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|...
gi 218563680 553 QECTVEEIKAycKGKIAHYKVPRYILFVQDYPLTITGKIQKHKLRERTEKQLG 605
Cdd:PRK08633 1096 DVEELKRAIK--ESGLPNLWKPSRYFKVEALPLLGSGKLDLKGLKELALALLG 1146
|
|
| PRK06018 |
PRK06018 |
putative acyl-CoA synthetase; Provisional |
255-599 |
8.15e-49 |
|
putative acyl-CoA synthetase; Provisional
Pssm-ID: 235673 [Multi-domain] Cd Length: 542 Bit Score: 178.41 E-value: 8.15e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218563680 255 FTSGTTGKPKGATLSHHN------IVNNAYFTGMrigynwrKNVRICLPV-PLYHCfGSVGGGVIMALYGTTVIFPSTGY 327
Cdd:PRK06018 184 YTSGTTGDPKGVLYSHRSnvlhalMANNGDALGT-------SAADTMLPVvPLFHA-NSWGIAFSAPSMGTKLVMPGAKL 255
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218563680 328 DGRANLRAIEKEKCTFVYGTPTMYIDMLGQPDLAKFDLSSVRGGIAAGSPCPPEVMRKILNvMGIkEMVIGYGTTENSPV 407
Cdd:PRK06018 256 DGASVYELLDTEKVTFTAGVPTVWLMLLQYMEKEGLKLPHLKMVVCGGSAMPRSMIKAFED-MGV-EVRHAWGMTEMSPL 333
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218563680 408 --------TFCGFPVDSAERKIETVGCISPHTEAKVVDPTtGEIVPLGAQ--GELMIRGYCVMLEYWQDEEktrECITKD 477
Cdd:PRK06018 334 gtlaalkpPFSKLPGDARLDVLQKQGYPPFGVEMKITDDA-GKELPWDGKtfGRLKVRGPAVAAAYYRVDG---EILDDD 409
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218563680 478 RWYKTGDIASLDQFAYCKIEGRIKDLIIRGGENIYPAEIEQFLHTHPKILEAQVVGVKDERMGEEVCACIRLKEGQECTV 557
Cdd:PRK06018 410 GFFDTGDVATIDAYGYMRITDRSKDVIKSGGEWISSIDLENLAVGHPKVAEAAVIGVYHPKWDERPLLIVQLKPGETATR 489
|
330 340 350 360
....*....|....*....|....*....|....*....|..
gi 218563680 558 EEIKAYCKGKIAHYKVPRYILFVQDYPLTITGKIQKHKLRER 599
Cdd:PRK06018 490 EEILKYMDGKIAKWWMPDDVAFVDAIPHTATGKILKTALREQ 531
|
|
| PLN03102 |
PLN03102 |
acyl-activating enzyme; Provisional |
72-598 |
9.50e-45 |
|
acyl-activating enzyme; Provisional
Pssm-ID: 215576 [Multi-domain] Cd Length: 579 Bit Score: 167.89 E-value: 9.50e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218563680 72 LQATVERYPDREAMVFVQdgIRKTFAEFYQDVEKAAAGLLAAGLKRGDRLGMWGPNIYEWVLMQFATAKAGIILVAVNPA 151
Cdd:PLN03102 20 LKRASECYPNRTSIIYGK--TRFTWPQTYDRCCRLAASLISLNITKNDVVSVLAPNTPAMYEMHFAVPMAGAVLNPINTR 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218563680 152 YQLQEVEFALRKVQCNAVVCPTKFKSqhYCDMLKQLCPEMETAspggikssrlPDLHTVIVTDSQQPGSFLLKDLMQAGS 231
Cdd:PLN03102 98 LDATSIAAILRHAKPKILFVDRSFEP--LAREVLHLLSSEDSN----------LNLPVIFIHEIDFPKRPSSEELDYECL 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218563680 232 SQHYQQLQDLQKKLVC----DDPINIQFTSGTTGKPKGATLSHHNivnnAYFTGMRIGYNWRKNVricLPV-----PLYH 302
Cdd:PLN03102 166 IQRGEPTPSLVARMFRiqdeHDPISLNYTSGTTADPKGVVISHRG----AYLSTLSAIIGWEMGT---CPVylwtlPMFH 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218563680 303 CFGSVGGGVIMALYGTTV-IFPSTGYDGRANlraIEKEKCTFVYGTPTMYIDMLGQPDLAKFDLSSVRGGIAAGSPcPPE 381
Cdd:PLN03102 239 CNGWTFTWGTAARGGTSVcMRHVTAPEIYKN---IEMHNVTHMCCVPTVFNILLKGNSLDLSPRSGPVHVLTGGSP-PPA 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218563680 382 VMRKILNVMGIKEMViGYGTTENS-PVTFCGFPVD------------SAERKIETVGCisphTEAKVVDPTTGEIVPLGA 448
Cdd:PLN03102 315 ALVKKVQRLGFQVMH-AYGLTEATgPVLFCEWQDEwnrlpenqqmelKARQGVSILGL----ADVDVKNKETQESVPRDG 389
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218563680 449 Q--GELMIRGYCVMLEYWQDEEKTRECItKDRWYKTGDIASLDQFAYCKIEGRIKDLIIRGGENIYPAEIEQFLHTHPKI 526
Cdd:PLN03102 390 KtmGEIVIKGSSIMKGYLKNPKATSEAF-KHGWLNTGDVGVIHPDGHVEIKDRSKDIIISGGENISSVEVENVLYKYPKV 468
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218563680 527 LEAQVVGVKDERMGEEVCACIRLKEGQECTVEEIKA----------YCKGKIAHYKVPRYILFVQDYPLTITGKIQKHKL 596
Cdd:PLN03102 469 LETAVVAMPHPTWGETPCAFVVLEKGETTKEDRVDKlvtrerdlieYCRENLPHFMCPRKVVFLQELPKNGNGKILKPKL 548
|
..
gi 218563680 597 RE 598
Cdd:PLN03102 549 RD 550
|
|
| PRK05852 |
PRK05852 |
fatty acid--CoA ligase family protein; |
72-599 |
1.01e-44 |
|
fatty acid--CoA ligase family protein;
Pssm-ID: 235625 [Multi-domain] Cd Length: 534 Bit Score: 166.99 E-value: 1.01e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218563680 72 LQATVERYPDREAMVFVQDGIRKTFAEFYQDVEKAAAGLLAAGLKRGDRLGMWGPNIYEWVLMQFATAKAGIILVAVNPA 151
Cdd:PRK05852 22 VEVAATRLPEAPALVVTADRIAISYRDLARLVDDLAGQLTRSGLLPGDRVALRMGSNAEFVVALLAASRADLVVVPLDPA 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218563680 152 YQLQEVEFALRKVQCNAVVCPTKFKSQHycdmlkqlcpemetASPggikSSRLPDLHTVIVTDSQQPGSFLLKDLMQAGS 231
Cdd:PRK05852 102 LPIAEQRVRSQAAGARVVLIDADGPHDR--------------AEP----TTRWWPLTVNVGGDSGPSGGTLSVHLDAATE 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218563680 232 SQHYQQLQDlqkKLVCDDPInIQFTSGTTGKPKGATLSHHNIVNN--AYFTGMRIGynwRKNVRICLpVPLYHcfgsvGG 309
Cdd:PRK05852 164 PTPATSTPE---GLRPDDAM-IMFTGGTTGLPKMVPWTHANIASSvrAIITGYRLS---PRDATVAV-MPLYH-----GH 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218563680 310 GVIMALYGT-----TVIFPSTG-YDGRANLRAIEKEKCTFVYGTPTMYIDMLGQPDLAKFD-----LSSVRggiAAGSPC 378
Cdd:PRK05852 231 GLIAALLATlasggAVLLPARGrFSAHTFWDDIKAVGATWYTAVPTIHQILLERAATEPSGrkpaaLRFIR---SCSAPL 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218563680 379 PPEVMRKILNVMGiKEMVIGYGTTENS-PVTFCGFP-VDSAERKIETVGCISPHTEA--KVVDPTTGEIVPlGAQGELMI 454
Cdd:PRK05852 308 TAETAQALQTEFA-APVVCAFGMTEAThQVTTTQIEgIGQTENPVVSTGLVGRSTGAqiRIVGSDGLPLPA-GAVGEVWL 385
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218563680 455 RGYCVMLEYWQDEEKTRECITkDRWYKTGDIASLDQFAYCKIEGRIKDLIIRGGENIYPAEIEQFLHTHPKILEAQVVGV 534
Cdd:PRK05852 386 RGTTVVRGYLGDPTITAANFT-DGWLRTGDLGSLSAAGDLSIRGRIKELINRGGEKISPERVEGVLASHPNVMEAAVFGV 464
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 218563680 535 KDERMGEEVCACIRLKEGQECTVEEIKAYCKGKIAHYKVPRYILFVQDYPLTITGKIQKHKLRER 599
Cdd:PRK05852 465 PDQLYGEAVAAVIVPRESAPPTAEELVQFCRERLAAFEIPASFQEASGLPHTAKGSLDRRAVAEQ 529
|
|
| FACL_like_6 |
cd05922 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
248-597 |
1.01e-44 |
|
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ATP-dependent activation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions.
Pssm-ID: 341246 [Multi-domain] Cd Length: 457 Bit Score: 165.31 E-value: 1.01e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218563680 248 DDPINIQFTSGTTGKPKGATLSHHNIVNNAYFTGMRIGYnwRKNVRICLPVPLYHCFG-SVgggVIMALY-GTTVIFPST 325
Cdd:cd05922 117 EDLALLLYTSGSTGSPKLVRLSHQNLLANARSIAEYLGI--TADDRALTVLPLSYDYGlSV---LNTHLLrGATLVLTND 191
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218563680 326 GYDGRANLRAIEKEKCTFVYGTPTMYiDMLGQPDLAKFDLSSVRGGIAAGSPCPPEVMRKILNVMGIKEMVIGYGTTENS 405
Cdd:cd05922 192 GVLDDAFWEDLREHGATGLAGVPSTY-AMLTRLGFDPAKLPSLRYLTQAGGRLPQETIARLRELLPGAQVYVMYGQTEAT 270
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218563680 406 P-VTFcgFPVDSAERKIETVGCISPHTEAKVVDPTtGEIVPLGAQGELMIRGYCVMLEYWQDEEKTRECITKDRWYKTGD 484
Cdd:cd05922 271 RrMTY--LPPERILEKPGSIGLAIPGGEFEILDDD-GTPTPPGEPGEIVHRGPNVMKGYWNDPPYRRKEGRGGGVLHTGD 347
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218563680 485 IASLDQFAYCKIEGRIKDLIIRGGENIYPAEIEQFLHTHPKILEAQVVGVKDErMGEEVCACIRLKEGQECtvEEIKAYC 564
Cdd:cd05922 348 LARRDEDGFLFIVGRRDRMIKLFGNRISPTEIEAAARSIGLIIEAAAVGLPDP-LGEKLALFVTAPDKIDP--KDVLRSL 424
|
330 340 350
....*....|....*....|....*....|...
gi 218563680 565 KGKIAHYKVPRYILFVQDYPLTITGKIQKHKLR 597
Cdd:cd05922 425 AERLPPYKVPATVRVVDELPLTASGKVDYAALR 457
|
|
| FACL_like_5 |
cd05924 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
247-590 |
7.87e-44 |
|
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ATP-dependent activation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions.
Pssm-ID: 341248 [Multi-domain] Cd Length: 364 Bit Score: 160.24 E-value: 7.87e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218563680 247 CDDPINIQFTSGTTGKPKGATLSHHNI----VNNAYF-TGMRIGYNWRKNVR------ICLPV-PLYHCFGSVGGgVIMA 314
Cdd:cd05924 2 SADDLYILYTGGTTGMPKGVMWRQEDIfrmlMGGADFgTGEFTPSEDAHKAAaaaagtVMFPApPLMHGTGSWTA-FGGL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218563680 315 LYGTTVIFPSTGYDGRANLRAIEKEKCTFVygtpTMYIDMLGQP------DLAKFDLSSVRGGIAAGSPCPPEVMRKILN 388
Cdd:cd05924 81 LGGQTVVLPDDRFDPEEVWRTIEKHKVTSM----TIVGDAMARPlidalrDAGPYDLSSLFAISSGGALLSPEVKQGLLE 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218563680 389 VMGIKEMVIGYGTTENSpvtFCGFPVdSAERKIETVGCISPHTEAKVVDPTTGEIVP-LGAQGELMIRGYcVMLEYWQDE 467
Cdd:cd05924 157 LVPNITLVDAFGSSETG---FTGSGH-SAGSGPETGPFTRANPDTVVLDDDGRVVPPgSGGVGWIARRGH-IPLGYYGDE 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218563680 468 EKTRECI-TKD--RWYKTGDIASLDQFAYCKIEGRIKDLIIRGGENIYPAEIEQFLHTHPKILEAQVVGVKDERMGEEVC 544
Cdd:cd05924 232 AKTAETFpEVDgvRYAVPGDRATVEADGTVTLLGRGSVCINTGGEKVFPEEVEEALKSHPAVYDVLVVGRPDERWGQEVV 311
|
330 340 350 360
....*....|....*....|....*....|....*....|....*.
gi 218563680 545 ACIRLKEGQECTVEEIKAYCKGKIAHYKVPRYILFVQDYPLTITGK 590
Cdd:cd05924 312 AVVQLREGAGVDLEELREHCRTRIARYKLPKQVVFVDEIERSPAGK 357
|
|
| ttLC_FACS_like |
cd05915 |
Fatty acyl-CoA synthetases similar to LC-FACS from Thermus thermophiles; This family includes ... |
117-598 |
8.28e-44 |
|
Fatty acyl-CoA synthetases similar to LC-FACS from Thermus thermophiles; This family includes fatty acyl-CoA synthetases that can activate medium-chain to long-chain fatty acids. They catalyze the ATP-dependent acylation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. Fatty acyl-CoA synthetases are responsible for fatty acid degradation as well as physiological regulation of cellular functions via the production of fatty acyl-CoA esters. The fatty acyl-CoA synthetase from Thermus thermophiles in this family has been shown to catalyze the long-chain fatty acid, myristoyl acid, while another member in this family, the AlkK protein identified in Pseudomonas oleovorans, targets medium chain fatty acids. This family also includes an uncharacterized subgroup of FACS.
Pssm-ID: 213283 [Multi-domain] Cd Length: 509 Bit Score: 163.76 E-value: 8.28e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218563680 117 RGDRLGMWGPNIYEWVLMQFATAKAGIILVAVNPAYQLQEVEFALRKVQCNAVVCPTKFKSqhycdmlkqlcpemetasp 196
Cdd:cd05915 48 VGDRVATLGFNHFRHLEAYFAVPGMGAVLHTANPRLSPKEIAYILNHAEDKVLLFDPNLLP------------------- 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218563680 197 ggIKSSRLPDLHTVIVTDSQQPGSFLLKDLMQAGSSqHYQQLQDLQKklvCDdPINIQFTSGTTGKPKGATLSHHNIVNN 276
Cdd:cd05915 109 --LVEAIRGELKTVQHFVVMDEKAPEGYLAYEEALG-EEADPVRVPE---RA-ACGMAYTTGTTGLPKGVVYSHRALVLH 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218563680 277 AYFTGMRIGYNWRKNVRICLPVPLYHCFG-------SVGGGVIMAL---YGTTVIFPStgydgranlraIEKEKCTFVYG 346
Cdd:cd05915 182 SLAASLVDGTALSEKDVVLPVVPMFHVNAwclpyaaTLVGAKQVLPgprLDPASLVEL-----------FDGEGVTFTAG 250
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218563680 347 TPTMYIDMLGQPDLAKFDLSSVRGGIAAGSPcPPEVMRKiLNVMGIKEMVIGYGTTENSPV-TFC-------GFPVDSAE 418
Cdd:cd05915 251 VPTVWLALADYLESTGHRLKTLRRLVVGGSA-APRSLIA-RFERMGVEVRQGYGLTETSPVvVQNfvkshleSLSEEEKL 328
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218563680 419 RKIETVGCISPHTEAKVVDPTTGEIVPLGAQGELM-IRGYCVMLEYWQDEEKTRECITKDRWYKTGDIASLDQFAYCKIE 497
Cdd:cd05915 329 TLKAKTGLPIPLVRLRVADEEGRPVPKDGKALGEVqLKGPWITGGYYGNEEATRSALTPDGFFRTGDIAVWDEEGYVEIK 408
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218563680 498 GRIKDLIIRGGENIYPAEIEQFLHTHPKILEAQVVGVKDERMGEEVCACIRLKEGqECTVEEIKAYCKGKIAHYK-VPRY 576
Cdd:cd05915 409 DRLKDLIKSGGEWISSVDLENALMGHPKVKEAAVVAIPHPKWQERPLAVVVPRGE-KPTPEELNEHLLKAGFAKWqLPDA 487
|
490 500
....*....|....*....|..
gi 218563680 577 ILFVQDYPLTITGKIQKHKLRE 598
Cdd:cd05915 488 YVFAEEIPRTSAGKFLKRALRE 509
|
|
| PLN02574 |
PLN02574 |
4-coumarate--CoA ligase-like |
248-597 |
1.03e-43 |
|
4-coumarate--CoA ligase-like
Pssm-ID: 215312 [Multi-domain] Cd Length: 560 Bit Score: 164.63 E-value: 1.03e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218563680 248 DDPINIQFTSGTTGKPKGATLSHHNIVNN----AYFTGMRIGYNWRKNVRICLpVPLYHCFG----SVGggvIMALYGTT 319
Cdd:PLN02574 198 DDVAAIMYSSGTTGASKGVVLTHRNLIAMvelfVRFEASQYEYPGSDNVYLAA-LPMFHIYGlslfVVG---LLSLGSTI 273
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218563680 320 VIFPStgYDGRANLRAIEKEKCT-FVYGTPTMYIDMLGQPDLAKFDLSSVRGGIAAGSPCPPEVMRKILNVMGIKEMVIG 398
Cdd:PLN02574 274 VVMRR--FDASDMVKVIDRFKVThFPVVPPILMALTKKAKGVCGEVLKSLKQVSCGAAPLSGKFIQDFVQTLPHVDFIQG 351
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218563680 399 YGTTENSPVTFCGFPVDSAeRKIETVGCISPHTEAKVVDPTTGEIVPLGAQGELMIRGYCVMLEYWQDEEKTRECITKDR 478
Cdd:PLN02574 352 YGMTESTAVGTRGFNTEKL-SKYSSVGLLAPNMQAKVVDWSTGCLLPPGNCGELWIQGPGVMKGYLNNPKATQSTIDKDG 430
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218563680 479 WYKTGDIASLDQFAYCKIEGRIKDLIIRGGENIYPAEIEQFLHTHPKILEAQVVGVKDERMGEEVCACIRLKEGQECTVE 558
Cdd:PLN02574 431 WLRTGDIAYFDEDGYLYIVDRLKEIIKYKGFQIAPADLEAVLISHPEIIDAAVTAVPDKECGEIPVAFVVRRQGSTLSQE 510
|
330 340 350
....*....|....*....|....*....|....*....
gi 218563680 559 EIKAYCKGKIAHYKVPRYILFVQDYPLTITGKIQKHKLR 597
Cdd:PLN02574 511 AVINYVAKQVAPYKKVRKVVFVQSIPKSPAGKILRRELK 549
|
|
| PtmA |
cd17636 |
long-chain fatty acid CoA ligase (FadD); This family contains fatty acid CoA ligases, ... |
249-589 |
2.37e-43 |
|
long-chain fatty acid CoA ligase (FadD); This family contains fatty acid CoA ligases, including acyl-CoA synthetase (AMP-forming)/AMP-acid ligase II, most of which are yet to be characterized. Fatty acyl-CoA ligases catalyze the ATP-dependent activation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions.
Pssm-ID: 341291 [Multi-domain] Cd Length: 331 Bit Score: 158.23 E-value: 2.37e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218563680 249 DPINIQFTSGTTGKPKGATLSHHNI----VNNAYFTGMRIGYnwrknvrICLPV-PLYHcFGSVGGGviMALY---GTTV 320
Cdd:cd17636 1 DPVLAIYTAAFSGRPNGALLSHQALlaqaLVLAVLQAIDEGT-------VFLNSgPLFH-IGTLMFT--LATFhagGTNV 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218563680 321 IFPSTgyDGRANLRAIEKEKCTFVYGTPTMYIDMLGQPDLAKFDLSSVRGGIAA------GSPCPPEVMRKilnvMGike 394
Cdd:cd17636 71 FVRRV--DAEEVLELIEAERCTHAFLLPPTIDQIVELNADGLYDLSSLRSSPAApewndmATVDTSPWGRK----PG--- 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218563680 395 mviGYGTTENS-PVTFCGFpvdsAERKIETVGCISPHTEAKVVDPTtGEIVPLGAQGELMIRGYCVMLEYW-QDEEKTRE 472
Cdd:cd17636 142 ---GYGQTEVMgLATFAAL----GGGAIGGAGRPSPLVQVRILDED-GREVPDGEVGEIVARGPTVMAGYWnRPEVNARR 213
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218563680 473 ciTKDRWYKTGDIASLDQFAYCKIEGRIKDLIIRGGENIYPAEIEQFLHTHPKILEAQVVGVKDERMGEEVCACIRLKEG 552
Cdd:cd17636 214 --TRGGWHHTNDLGRREPDGSLSFVGPKTRMIKSGAENIYPAEVERCLRQHPAVADAAVIGVPDPRWAQSVKAIVVLKPG 291
|
330 340 350
....*....|....*....|....*....|....*..
gi 218563680 553 QECTVEEIKAYCKGKIAHYKVPRYILFVQDYPLTITG 589
Cdd:cd17636 292 ASVTEAELIEHCRARIASYKKPKSVEFADALPRTAGG 328
|
|
| PRK13382 |
PRK13382 |
bile acid CoA ligase; |
253-599 |
3.60e-43 |
|
bile acid CoA ligase;
Pssm-ID: 172019 [Multi-domain] Cd Length: 537 Bit Score: 162.62 E-value: 3.60e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218563680 253 IQFTSGTTGKPKGATLSHHNIVNNAYFTGMRIgyNWRKNVRICLPVPLYHCFGSvgGGVIMALYGTTVIFPSTGYDGRAN 332
Cdd:PRK13382 201 ILLTSGTTGTPKGARRSGPGGIGTLKAILDRT--PWRAEEPTVIVAPMFHAWGF--SQLVLAASLACTIVTRRRFDPEAT 276
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218563680 333 LRAIEKEKCTFVYGTPTMYIDMLGQPD--LAKFDLSSVRGGIAAGSPCPPEVMRKILNVMGikeMVI--GYGTTENSPVT 408
Cdd:PRK13382 277 LDLIDRHRATGLAVVPVMFDRIMDLPAevRNRYSGRSLRFAAASGSRMRPDVVIAFMDQFG---DVIynNYNATEAGMIA 353
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218563680 409 fCGFPVDsAERKIETVGCISPHTEAKVVDPTTGEiVPLGAQGELMIRGYCVMLEYWQDEEKTreciTKDRWYKTGDIASL 488
Cdd:PRK13382 354 -TATPAD-LRAAPDTAGRPAEGTEIRILDQDFRE-VPTGEVGTIFVRNDTQFDGYTSGSTKD----FHDGFMASGDVGYL 426
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218563680 489 DQFAYCKIEGRIKDLIIRGGENIYPAEIEQFLHTHPKILEAQVVGVKDERMGEEVCACIRLKEGQECTVEEIKAYCKGKI 568
Cdd:PRK13382 427 DENGRLFVVGRDDEMIVSGGENVYPIEVEKTLATHPDVAEAAVIGVDDEQYGQRLAAFVVLKPGASATPETLKQHVRDNL 506
|
330 340 350
....*....|....*....|....*....|.
gi 218563680 569 AHYKVPRYILFVQDYPLTITGKIQKHKLRER 599
Cdd:PRK13382 507 ANYKVPRDIVVLDELPRGATGKILRRELQAR 537
|
|
| PRK13390 |
PRK13390 |
acyl-CoA synthetase; Provisional |
255-597 |
5.39e-43 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 139538 [Multi-domain] Cd Length: 501 Bit Score: 161.33 E-value: 5.39e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218563680 255 FTSGTTGKPKG--ATLSHHNI---------VNNAYF--TGMRIGYNwrknvriclPVPLYHCFGSVGGGVIMALYGTTVI 321
Cdd:PRK13390 155 YSSGTTGFPKGiqPDLPGRDVdapgdpivaIARAFYdiSESDIYYS---------SAPIYHAAPLRWCSMVHALGGTVVL 225
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218563680 322 fpSTGYDGRANLRAIEKEKCTFVYGTPTMYIDMLGQPD--LAKFDLSSVRGGIAAGSPCPPEVMRKILNVMG--IKEMvi 397
Cdd:PRK13390 226 --AKRFDAQATLGHVERYRITVTQMVPTMFVRLLKLDAdvRTRYDVSSLRAVIHAAAPCPVDVKHAMIDWLGpiVYEY-- 301
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218563680 398 gYGTTENSPVTFcgfpVDSAERkIETVGCI--SPHTEAKVVDpTTGEIVPLGAQGELMIRGYCVMLEYWQDEEKTRECIT 475
Cdd:PRK13390 302 -YSSTEAHGMTF----IDSPDW-LAHPGSVgrSVLGDLHICD-DDGNELPAGRIGTVYFERDRLPFRYLNDPEKTAAAQH 374
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218563680 476 KDR--WYKTGDIASLDQFAYCKIEGRIKDLIIRGGENIYPAEIEQFLHTHPKILEAQVVGVKDERMGEEVCACIRLKEGQ 553
Cdd:PRK13390 375 PAHpfWTTVGDLGSVDEDGYLYLADRKSFMIISGGVNIYPQETENALTMHPAVHDVAVIGVPDPEMGEQVKAVIQLVEGI 454
|
330 340 350 360
....*....|....*....|....*....|....*....|....*..
gi 218563680 554 ECTVE---EIKAYCKGKIAHYKVPRYILFVQDYPLTITGKIQKHKLR 597
Cdd:PRK13390 455 RGSDElarELIDYTRSRIAHYKAPRSVEFVDELPRTPTGKLVKGLLR 501
|
|
| MACS_like_3 |
cd05971 |
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the ... |
248-597 |
1.83e-42 |
|
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the two-step activation of medium chain fatty acids (containing 4-12 carbons). The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. MACS enzymes are localized to mitochondria.
Pssm-ID: 341275 [Multi-domain] Cd Length: 439 Bit Score: 158.36 E-value: 1.83e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218563680 248 DDPINIQFTSGTTGKPKGATLSHHNIVNNAyfTGMRIGYNwrknvriCLPVPLYhCF---------GSVGGGVIMALY-G 317
Cdd:cd05971 88 DDPALIIYTSGTTGPPKGALHAHRVLLGHL--PGVQFPFN-------LFPRDGD-LYwtpadwawiGGLLDVLLPSLYfG 157
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218563680 318 TTVI-FPSTGYDGRANLRAIEKEKCTFVYGTPTMYIDMLGQPDLAKFDLSSVRGGIAAGSPCPPEVM---RKILNVmGIK 393
Cdd:cd05971 158 VPVLaHRMTKFDPKAALDLMSRYGVTTAFLPPTALKMMRQQGEQLKHAQVKLRAIATGGESLGEELLgwaREQFGV-EVN 236
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218563680 394 EMvigYGTTE-NSPVTFCG--FPVDSAerkieTVGCISPHTEAKVVDpTTGEIVPLGAQGELMIRGYC--VMLEYWQDEE 468
Cdd:cd05971 237 EF---YGQTEcNLVIGNCSalFPIKPG-----SMGKPIPGHRVAIVD-DNGTPLPPGEVGEIAVELPDpvAFLGYWNNPS 307
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218563680 469 KTRECITKDrWYKTGDIASLDQFAYCKIEGRIKDLIIRGGENIYPAEIEQFLHTHPKILEAQVVGVKDERMGEEVCACIR 548
Cdd:cd05971 308 ATEKKMAGD-WLLTGDLGRKDSDGYFWYVGRDDDVITSSGYRIGPAEIEECLLKHPAVLMAAVVGIPDPIRGEIVKAFVV 386
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|..
gi 218563680 549 LKEG---QECTVEEIKAYCKGKIAHYKVPRYILFVQDYPLTITGKIQKHKLR 597
Cdd:cd05971 387 LNPGetpSDALAREIQELVKTRLAAHEYPREIEFVNELPRTATGKIRRRELR 438
|
|
| LC_FACL_like |
cd05914 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); The members of this family are ... |
91-593 |
2.59e-41 |
|
Uncharacterized subfamily of fatty acid CoA ligase (FACL); The members of this family are bacterial long-chain fatty acid CoA synthetase, most of which are as yet uncharacterized. LC-FACS catalyzes the formation of fatty acyl-CoA in a two-step reaction: the formation of a fatty acyl-AMP molecule as an intermediate, and the formation of a fatty acyl-CoA. Free fatty acids must be "activated" to their CoA thioesters before participating in most catabolic and anabolic reactions.
Pssm-ID: 341240 [Multi-domain] Cd Length: 463 Bit Score: 155.68 E-value: 2.59e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218563680 91 GIRKTFAEFYQDVEKAAAGLLAAGLKRGDRLGMWGPNIYEWVLMQFATAKAGIILVAVNPAYQLQEVEFALRKVQCNAVV 170
Cdd:cd05914 5 GEPLTYKDLADNIAKFALLLKINGVGTGDRVALMGENRPEWGIAFFAIWTYGAIAVPILAEFTADEVHHILNHSEAKAIF 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218563680 171 CPTKfksqhycdmlkqlcpemetaspggikssrlpdlhtvivtdsqqpgsfllkdlmqagssqhyqqlqdlqkklvcDDP 250
Cdd:cd05914 85 VSDE-------------------------------------------------------------------------DDV 91
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218563680 251 INIQFTSGTTGKPKGATLSHHNIVNNAyfTGMRIGYNWRKNVRICLPVPLYHCFGSVGGGVIMALYGTTVIF----PStg 326
Cdd:cd05914 92 ALINYTSGTTGNSKGVMLTYRNIVSNV--DGVKEVVLLGKGDKILSILPLHHIYPLTFTLLLPLLNGAHVVFldkiPS-- 167
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218563680 327 ydgrANLRAIEKEKCTFVYGTPTMYI-------DMLGQPDLAKF-------------------DLSSVRGG-----IAAG 375
Cdd:cd05914 168 ----AKIIALAFAQVTPTLGVPVPLViekifkmDIIPKLTLKKFkfklakkinnrkirklafkKVHEAFGGnikefVIGG 243
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218563680 376 SPCPPEVMRkILNVMGIKeMVIGYGTTENSPVtFCGFPvdSAERKIETVGCISPHTEAKVVDPTtgeivPLGAQGELMIR 455
Cdd:cd05914 244 AKINPDVEE-FLRTIGFP-YTIGYGMTETAPI-ISYSP--PNRIRLGSAGKVIDGVEVRIDSPD-----PATGEGEIIVR 313
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218563680 456 GYCVMLEYWQDEEKTRECITKDRWYKTGDIASLDQFAYCKIEGRIKDLIIRG-GENIYPAEIEQFLHTHPKILEAQVVgv 534
Cdd:cd05914 314 GPNVMKGYYKNPEATAEAFDKDGWFHTGDLGKIDAEGYLYIRGRKKEMIVLSsGKNIYPEEIEAKINNMPFVLESLVV-- 391
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 218563680 535 kdERMGEEVCACI----RLKEGQECTVEEIKAYCKGKIAHY--KVPRY------ILFVQDYPLTITGKIQK 593
Cdd:cd05914 392 --VQEKKLVALAYidpdFLDVKALKQRNIIDAIKWEVRDKVnqKVPNYkkiskvKIVKEEFEKTPKGKIKR 460
|
|
| PRK04319 |
PRK04319 |
acetyl-CoA synthetase; Provisional |
199-606 |
4.86e-41 |
|
acetyl-CoA synthetase; Provisional
Pssm-ID: 235279 [Multi-domain] Cd Length: 570 Bit Score: 156.98 E-value: 4.86e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218563680 199 IKSSRLPDLHTVIVTD---SQQPGSFLLKDLMQAGSSQHYQQLQDLqkklvcDDPINIQFTSGTTGKPKGAtLSHHNIVN 275
Cdd:PRK04319 159 KPADDLPSLKHVLLVGedvEEGPGTLDFNALMEQASDEFDIEWTDR------EDGAILHYTSGSTGKPKGV-LHVHNAML 231
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218563680 276 NAYFTGmrigyNWRKNVRiclPVPLYHCF---GSVGG---GVIMA-LYGTTVIFPSTGYDGRANLRAIEKEKCTFVYGTP 348
Cdd:PRK04319 232 QHYQTG-----KYVLDLH---EDDVYWCTadpGWVTGtsyGIFAPwLNGATNVIDGGRFSPERWYRILEDYKVTVWYTAP 303
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218563680 349 TMyIDML--GQPDLA-KFDLSSVRGGIAAGSPCPPEVMRKILNVMGikeMVI--GYGTTENSPVTFCGFPvdSAERKIET 423
Cdd:PRK04319 304 TA-IRMLmgAGDDLVkKYDLSSLRHILSVGEPLNPEVVRWGMKVFG---LPIhdNWWMTETGGIMIANYP--AMDIKPGS 377
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218563680 424 VGCISPHTEAKVVDPTTGEIVPlGAQGELMIR-GYCVML-EYWQDEEKTRECITKDrWYKTGDIASLDQFAYCKIEGRIK 501
Cdd:PRK04319 378 MGKPLPGIEAAIVDDQGNELPP-NRMGNLAIKkGWPSMMrGIWNNPEKYESYFAGD-WYVSGDSAYMDEDGYFWFQGRVD 455
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218563680 502 DLIIRGGENIYPAEIEQFLHTHPKILEAQVVGVKDERMGEEVCACIRLKEGQECTVE---EIKAYCKGKIAHYKVPRYIL 578
Cdd:PRK04319 456 DVIKTSGERVGPFEVESKLMEHPAVAEAGVIGKPDPVRGEIIKAFVALRPGYEPSEElkeEIRGFVKKGLGAHAAPREIE 535
|
410 420
....*....|....*....|....*...
gi 218563680 579 FVQDYPLTITGKIQKHKLRERtekQLGL 606
Cdd:PRK04319 536 FKDKLPKTRSGKIMRRVLKAW---ELGL 560
|
|
| PRK07638 |
PRK07638 |
acyl-CoA synthetase; Validated |
241-605 |
7.07e-39 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236071 [Multi-domain] Cd Length: 487 Bit Score: 149.54 E-value: 7.07e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218563680 241 LQKKLVCDDPINIQFTSGTTGKPKGATLSHHNIVNNayFTGMRIGYNWRKNVRICLPVPLYHC---FGSVGggvimALY- 316
Cdd:PRK07638 136 APIENVQNAPFYMGFTSGSTGKPKAFLRAQQSWLHS--FDCNVHDFHMKREDSVLIAGTLVHSlflYGAIS-----TLYv 208
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218563680 317 GTTVIFPSTGYDGRAnLRAIEKEKCTFVYGTPTMyIDMLGQPDlaKFDLSSVRGgIAAGSPCPPEVMRKILNVMGIKEMV 396
Cdd:PRK07638 209 GQTVHLMRKFIPNQV-LDKLETENISVMYTVPTM-LESLYKEN--RVIENKMKI-ISSGAKWEAEAKEKIKNIFPYAKLY 283
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218563680 397 IGYGTTENSPVTFCgFPVDSaERKIETVGciSP-HTEAKVVDPTTGEIVPLGAQGELMIRGYCVMLEYWQDEEKTREcIT 475
Cdd:PRK07638 284 EFYGASELSFVTAL-VDEES-ERRPNSVG--RPfHNVQVRICNEAGEEVQKGEIGTVYVKSPQFFMGYIIGGVLARE-LN 358
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218563680 476 KDRWYKTGDIASLDQFAYCKIEGRIKDLIIRGGENIYPAEIEQFLHTHPKILEAQVVGVKDERMGEEVCACIrlkEGQEc 555
Cdd:PRK07638 359 ADGWMTVRDVGYEDEEGFIYIVGREKNMILFGGINIFPEEIESVLHEHPAVDEIVVIGVPDSYWGEKPVAII---KGSA- 434
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|
gi 218563680 556 TVEEIKAYCKGKIAHYKVPRYILFVQDYPLTITGKIQKHKLRERTEKQLG 605
Cdd:PRK07638 435 TKQQLKSFCLQRLSSFKIPKEWHFVDEIPYTNSGKIARMEAKSWIENQEK 484
|
|
| ACS-like |
cd17634 |
acetate-CoA ligase; This family includes acyl- and aryl-CoA ligases, as well as the ... |
70-591 |
1.72e-37 |
|
acetate-CoA ligase; This family includes acyl- and aryl-CoA ligases, as well as the adenylation domain of nonribosomal peptide synthetases and firefly luciferases. The adenylate-forming enzymes catalyze an ATP-dependent two-step reaction to first activate a carboxylate substrate as an adenylate and then transfer the carboxylate to the pantetheine group of either coenzyme A or an acyl-carrier protein. The active site of the domain is located at the interface of a large N-terminal subdomain and a smaller C-terminal subdomain.
Pssm-ID: 341289 [Multi-domain] Cd Length: 587 Bit Score: 146.95 E-value: 1.72e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218563680 70 QCLQATVERYPDREAMVFVQD---GIRK-TFAEFYQDVEKAAAGLLAAGLKRGDRLGMWGPNIYEWVLMQFATAKAGIIL 145
Cdd:cd17634 57 NALDRHLRENGDRTAIIYEGDdtsQSRTiSYRELHREVCRFAGTLLDLGVKKGDRVAIYMPMIPEAAVAMLACARIGAVH 136
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218563680 146 VAVNPAYQLQEVefALRKVQCNAVVCPTK---FKSQHYCDMLKQLCpemETASPGGikssrlPDLHTVIVTDSQ------ 216
Cdd:cd17634 137 SVIFGGFAPEAV--AGRIIDSSSRLLITAdggVRAGRSVPLKKNVD---DALNPNV------TSVEHVIVLKRTgsdidw 205
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218563680 217 QPGSFL-LKDLMQAGSSQHYQQLQDlqkklvCDDPINIQFTSGTTGKPKGATLSHhnivnnayfTGMRIGYNWR-KNVRI 294
Cdd:cd17634 206 QEGRDLwWRDLIAKASPEHQPEAMN------AEDPLFILYTSGTTGKPKGVLHTT---------GGYLVYAATTmKYVFD 270
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218563680 295 CLPVPLYHCFGSVG----------GGVIMalyGTTVIFpstgYDGRAN-------LRAIEKEKCTFVYGTPTMyIDMLGQ 357
Cdd:cd17634 271 YGPGDIYWCTADVGwvtghsyllyGPLAC---GATTLL----YEGVPNwptparmWQVVDKHGVNILYTAPTA-IRALMA 342
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218563680 358 PD---LAKFDLSSVRGGIAAGSPCPPEVMRKILNVMGIKE--MVIGYGTTENSpvTFCGFPVDSAER-KIETVGCISPHT 431
Cdd:cd17634 343 AGddaIEGTDRSSLRILGSVGEPINPEAYEWYWKKIGKEKcpVVDTWWQTETG--GFMITPLPGAIElKAGSATRPVFGV 420
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218563680 432 EAKVVDpTTGEIVPLGAQGELMIRGYC--VMLEYWQDEEKTRECI--TKDRWYKTGDIASLDQFAYCKIEGRIKDLIIRG 507
Cdd:cd17634 421 QPAVVD-NEGHPQPGGTEGNLVITDPWpgQTRTLFGDHERFEQTYfsTFKGMYFSGDGARRDEDGYYWITGRSDDVINVA 499
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218563680 508 GENIYPAEIEQFLHTHPKILEAQVVGVKDERMGEEVCACIRLKEGQECTVE---EIKAYCKGKIAHYKVPRYILFVQDYP 584
Cdd:cd17634 500 GHRLGTAEIESVLVAHPKVAEAAVVGIPHAIKGQAPYAYVVLNHGVEPSPElyaELRNWVRKEIGPLATPDVVHWVDSLP 579
|
....*..
gi 218563680 585 LTITGKI 591
Cdd:cd17634 580 KTRSGKI 586
|
|
| DltA |
cd05945 |
D-alanine:D-alanyl carrier protein ligase (DltA) and similar proteins; This family includes ... |
248-596 |
1.95e-37 |
|
D-alanine:D-alanyl carrier protein ligase (DltA) and similar proteins; This family includes D-alanyl carrier protein ligase DltA and aliphatic beta-amino acid adenylation enzymes IdnL1 and CmiS6. DltA incorporates D-ala in techoic acids in gram-positive bacteria via a two-step process, starting with adenylation of D-alanine that transfers D-alanine to the D-alanyl carrier protein. IdnL1, a short-chain aliphatic beta-amino acid adenylation enzyme, recognizes 3-aminobutanoic acid, and is involved in the synthesis of the macrolactam antibiotic incednine. CmiS6 is a medium-chain beta-amino acid adenylation enzyme that recognizes 3-aminononanoic acid, and is involved in the synthesis of cremimycin, also a macrolactam antibiotic. The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester bond to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.
Pssm-ID: 341267 [Multi-domain] Cd Length: 449 Bit Score: 144.70 E-value: 1.95e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218563680 248 DDPINIQFTSGTTGKPKGATLSHHNIVnnAYFTGMRIGYNWRKNVRIcLPVPLYH-------CFGSVGGGvimalyGTTV 320
Cdd:cd05945 97 DDNAYIIFTSGSTGRPKGVQISHDNLV--SFTNWMLSDFPLGPGDVF-LNQAPFSfdlsvmdLYPALASG------ATLV 167
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218563680 321 IFPSTGYDGRANL-RAIEKEKCTFVYGTPTmYIDM-LGQPDLAKFDLSSVRGGIAAGSPCPPEVMRK---------ILNv 389
Cdd:cd05945 168 PVPRDATADPKQLfRFLAEHGITVWVSTPS-FAAMcLLSPTFTPESLPSLRHFLFCGEVLPHKTARAlqqrfpdarIYN- 245
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218563680 390 mgikemviGYGTTE-NSPVTFCGFPVDSAER-KIETVGCISPHTEAKVVDpTTGEIVPLGAQGELMIRGYCVMLEYWQDE 467
Cdd:cd05945 246 --------TYGPTEaTVAVTYIEVTPEVLDGyDRLPIGYAKPGAKLVILD-EDGRPVPPGEKGELVISGPSVSKGYLNNP 316
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218563680 468 EKTRECITKD---RWYKTGDIASLD---QFAYCkieGRIKDLIIRGGENIYPAEIEQFLHTHPKILEAQVVGVKDERMGE 541
Cdd:cd05945 317 EKTAAAFFPDegqRAYRTGDLVRLEadgLLFYR---GRLDFQVKLNGYRIELEEIEAALRQVPGVKEAVVVPKYKGEKVT 393
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*..
gi 218563680 542 EVCACIRLKEGQE--CTVeEIKAYCKGKIAHYKVPRYILFVQDYPLTITGKIQKHKL 596
Cdd:cd05945 394 ELIAFVVPKPGAEagLTK-AIKAELAERLPPYMIPRRFVYLDELPLNANGKIDRKAL 449
|
|
| AA-adenyl-dom |
TIGR01733 |
amino acid adenylation domain; This model represents a domain responsible for the specific ... |
116-531 |
3.25e-37 |
|
amino acid adenylation domain; This model represents a domain responsible for the specific recognition of amino acids and activation as adenylyl amino acids. The reaction catalyzed is aa + ATP -> aa-AMP + PPi. These domains are usually found as components of multi-domain non-ribosomal peptide synthetases and are usually called "A-domains" in that context. A-domains are almost invariably followed by "T-domains" (thiolation domains, pfam00550) to which the amino acid adenylate is transferred as a thiol-ester to a bound pantetheine cofactor with the release of AMP (these are also called peptide carrier proteins, or PCPs. When the A-domain does not represent the first module (corresponding to the first amino acid in the product molecule) it is usually preceded by a "C-domain" (condensation domain, pfam00668) which catalyzes the ligation of two amino acid thiol-esters from neighboring modules. This domain is a subset of the AMP-binding domain found in Pfam (pfam00501) which also hits substrate--CoA ligases and luciferases. Sequences scoring in between trusted and noise for this model may be ambiguous as to whether they activate amino acids or other molecules lacking an alpha amino group.
Pssm-ID: 273779 [Multi-domain] Cd Length: 409 Bit Score: 143.17 E-value: 3.25e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218563680 116 KRGDRLGMWGPNIYEWVLMQFATAKAGIILVAVNPAYQLQEVEFALRKVQCNAVVCptkfkSQHYCdmlkqlcpemetas 195
Cdd:TIGR01733 23 GPGDRVAVLLERSAELVVAILAVLKAGAAYVPLDPAYPAERLAFILEDAGARLLLT-----DSALA-------------- 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218563680 196 pggiksSRLPDLHTVIVTDSQQPgsflLKDLMQAGSSQHyqqlqdLQKKLVCDDPINIQFTSGTTGKPKGATLSHHNIVN 275
Cdd:TIGR01733 84 ------SRLAGLVLPVILLDPLE----LAALDDAPAPPP------PDAPSGPDDLAYVIYTSGSTGRPKGVVVTHRSLVN 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218563680 276 naYFTGMRigynWRKNVR---ICLPVPLYHCFGSVGGgVIMALY-GTTVIFPS---TGYDGRANLRAIEKEKCTFVYGTP 348
Cdd:TIGR01733 148 --LLAWLA----RRYGLDpddRVLQFASLSFDASVEE-IFGALLaGATLVVPPedeERDDAALLAALIAEHPVTVLNLTP 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218563680 349 TMYiDMLgqPDLAKFDLSSVRGGIAAGSPCPPEVMRKILNVMGIKEMVIGYGTTENSpVTFCGFPVDSAERKIETVGCIS 428
Cdd:TIGR01733 221 SLL-ALL--AAALPPALASLRLVILGGEALTPALVDRWRARGPGARLINLYGPTETT-VWSTATLVDPDDAPRESPVPIG 296
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218563680 429 ---PHTEAKVVDPTtGEIVPLGAQGELMIRGYCVMLEYWQDEEKTRECITKD--------RWYKTGDIASLD---QFAYC 494
Cdd:TIGR01733 297 rplANTRLYVLDDD-LRPVPVGVVGELYIGGPGVARGYLNRPELTAERFVPDpfaggdgaRLYRTGDLVRYLpdgNLEFL 375
|
410 420 430
....*....|....*....|....*....|....*...
gi 218563680 495 kieGRIKDLI-IRgGENIYPAEIEQFLHTHPKILEAQV 531
Cdd:TIGR01733 376 ---GRIDDQVkIR-GYRIELGEIEAALLRHPGVREAVV 409
|
|
| FAAL |
cd05931 |
Fatty acyl-AMP ligase (FAAL); FAAL belongs to the class I adenylate forming enzyme family and ... |
80-599 |
5.01e-37 |
|
Fatty acyl-AMP ligase (FAAL); FAAL belongs to the class I adenylate forming enzyme family and is homologous to fatty acyl-coenzyme A (CoA) ligases (FACLs). However, FAALs produce only the acyl adenylate and are unable to perform the thioester-forming reaction, while FACLs perform a two-step catalytic reaction; AMP ligation followed by CoA ligation using ATP and CoA as cofactors. FAALs have insertion motifs between the N-terminal and C-terminal subdomains that distinguish them from the FACLs. This insertion motif precludes the binding of CoA, thus preventing CoA ligation. It has been suggested that the acyl adenylates serve as substrates for multifunctional polyketide synthases to permit synthesis of complex lipids such as phthiocerol dimycocerosate, sulfolipids, mycolic acids, and mycobactin.
Pssm-ID: 341254 [Multi-domain] Cd Length: 547 Bit Score: 145.07 E-value: 5.01e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218563680 80 PDREAMVFVQDG----IRKTFAEFYQDVeKAAAGLLAAGLKRGDRLGMWGPNIYEWVLMQFATAKAGIILVAV---NPAY 152
Cdd:cd05931 7 PDRPAYTFLDDEggreETLTYAELDRRA-RAIAARLQAVGKPGDRVLLLAPPGLDFVAAFLGCLYAGAIAVPLpppTPGR 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218563680 153 QLQEVEFALRKVQCNAVVCPTKFksqhycdmlkqlcpemETASPGGIKSSRLPDLHTVIVTDsqqpgsfllkdLMQAGSS 232
Cdd:cd05931 86 HAERLAAILADAGPRVVLTTAAA----------------LAAVRAFAASRPAAGTPRLLVVD-----------LLPDTSA 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218563680 233 QHYQQlqdlqKKLVCDDPINIQFTSGTTGKPKGATLSHHNIVNNayFTGMRIGYNWRKNVRICLPVPLYHCFGSVGGGVI 312
Cdd:cd05931 139 ADWPP-----PSPDPDDIAYLQYTSGSTGTPKGVVVTHRNLLAN--VRQIRRAYGLDPGDVVVSWLPLYHDMGLIGGLLT 211
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218563680 313 MALYGTTVIFPSTG---YDGRANLRAIEKEKCTFVYGtPTMYIDMLGQ----PDLAKFDLSSVRGGIAAGSPCPPEVMRK 385
Cdd:cd05931 212 PLYSGGPSVLMSPAaflRRPLRWLRLISRYRATISAA-PNFAYDLCVRrvrdEDLEGLDLSSWRVALNGAEPVRPATLRR 290
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218563680 386 ILNVM---GIKEMVI--GYGTTENS-PVTFC----GFPVDSAERKI----------------ETVGCISPH--TEAKVVD 437
Cdd:cd05931 291 FAEAFapfGFRPEAFrpSYGLAEATlFVSGGppgtGPVVLRVDRDAlagravavaaddpaarELVSCGRPLpdQEVRIVD 370
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218563680 438 PTTGEIVPLGAQGELMIRGYCVMLEYWQDEEKTREC------ITKDRWYKTGDIASL--DQFaYckIEGRIKDLIIRGGE 509
Cdd:cd05931 371 PETGRELPDGEVGEIWVRGPSVASGYWGRPEATAETfgalaaTDEGGWLRTGDLGFLhdGEL-Y--ITGRLKDLIIVRGR 447
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218563680 510 NIYPAEIEQFL-HTHPKILEAQVV--GVKDERMGEEVCACIRLKEGQECTVEEIKAYCKGKIA--HYKVPRYILFV--QD 582
Cdd:cd05931 448 NHYPQDIEATAeEAHPALRPGCVAafSVPDDGEERLVVVAEVERGADPADLAAIAAAIRAAVAreHGVAPADVVLVrpGS 527
|
570
....*....|....*..
gi 218563680 583 YPLTITGKIQKHKLRER 599
Cdd:cd05931 528 IPRTSSGKIQRRACRAA 544
|
|
| LC_FACS_like |
cd17640 |
Long-chain fatty acid CoA synthetase; This family includes long-chain fatty acid (C12-C20) CoA ... |
248-540 |
1.04e-36 |
|
Long-chain fatty acid CoA synthetase; This family includes long-chain fatty acid (C12-C20) CoA synthetases, including an Arabidopsis gene At4g14070 that plays a role in activation and elongation of exogenous fatty acids. FACS catalyzes the formation of fatty acyl-CoA in a two-step reaction: the formation of a fatty acyl-AMP molecule as an intermediate, and the formation of a fatty acyl-CoA. Eukaryotes generally have multiple isoforms of LC-FACS genes with multiple splice variants. For example, nine genes are found in Arabidopsis and six genes are expressed in mammalian cells. Free fatty acids must be "activated" to their CoA thioesters before participating in most catabolic and anabolic reactions.
Pssm-ID: 341295 [Multi-domain] Cd Length: 468 Bit Score: 142.88 E-value: 1.04e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218563680 248 DDPINIQFTSGTTGKPKGATLSH----HNIVN-NAYFTGmrigynwRKNVRICLPVPLYHCFGSVGGGVIMAlYGTTVIF 322
Cdd:cd17640 88 DDLATIIYTSGTTGNPKGVMLTHanllHQIRSlSDIVPP-------QPGDRFLSILPIWHSYERSAEYFIFA-CGCSQAY 159
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218563680 323 PSTgydgRANLRAIEKEKCTFVYGTPTMYIDM------------LGQPDLAKFDLS--SVRGGIAAGSPCPPEVMRkILN 388
Cdd:cd17640 160 TSI----RTLKDDLKRVKPHYIVSVPRLWESLysgiqkqvskssPIKQFLFLFFLSggIFKFGISGGGALPPHVDT-FFE 234
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218563680 389 VMGIkEMVIGYGTTENSPVTFCGFPvdsAERKIETVGCISPHTEAKVVDPTTGEIVPLGAQGELMIRGYCVMLEYWQDEE 468
Cdd:cd17640 235 AIGI-EVLNGYGLTETSPVVSARRL---KCNVRGSVGRPLPGTEIKIVDPEGNVVLPPGEKGIVWVRGPQVMKGYYKNPE 310
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 218563680 469 KTRECITKDRWYKTGDIASLDQFAYCKIEGRIKDLII-RGGENIYPAEIEQFLHTHPKILEAQVVGVKDERMG 540
Cdd:cd17640 311 ATSKVLDSDGWFNTGDLGWLTCGGELVLTGRAKDTIVlSNGENVEPQPIEEALMRSPFIEQIMVVGQDQKRLG 383
|
|
| AACS_like |
cd05968 |
Uncharacterized acyl-CoA synthetase subfamily similar to Acetoacetyl-CoA synthetase; This ... |
68-597 |
1.37e-36 |
|
Uncharacterized acyl-CoA synthetase subfamily similar to Acetoacetyl-CoA synthetase; This uncharacterized acyl-CoA synthetase family (EC 6.2.1.16, or acetoacetate#CoA ligase or acetoacetate:CoA ligase (AMP-forming)) is highly homologous to acetoacetyl-CoA synthetase. However, the proteins in this family exist in only bacteria and archaea. AACS is a cytosolic ligase that specifically activates acetoacetate to its coenzyme A ester by a two-step reaction. Acetoacetate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This is the first step of the mevalonate pathway of isoprenoid biosynthesis via isopentenyl diphosphate. Isoprenoids are a large class of compounds found in all living organisms.
Pssm-ID: 341272 [Multi-domain] Cd Length: 610 Bit Score: 144.56 E-value: 1.37e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218563680 68 VDQCLQATVERYPDREAMVFV-QDGIRKTFA--EFYQDVEKAAAGLLAAGLKRGDRLGMWGPNIYEWVLMQFATAKAGII 144
Cdd:cd05968 63 VEQLLDKWLADTRTRPALRWEgEDGTSRTLTygELLYEVKRLANGLRALGVGKGDRVGIYLPMIPEIVPAFLAVARIGGI 142
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218563680 145 LVAVNPAYQLQEVEFALRKVQCNAVVCPTKFKSQhycDMLKQLCPEMETASpggiksSRLPDLHTVIV------TDSQQP 218
Cdd:cd05968 143 VVPIFSGFGKEAAATRLQDAEAKALITADGFTRR---GREVNLKEEADKAC------AQCPTVEKVVVvrhlgnDFTPAK 213
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218563680 219 GSFLLKDLMQAGSSQHYQQLQDlqkklvcDDPINIQFTSGTTGKPKGATLSHHNIVNNAYFTgMRIGYNWRKNVRICLPV 298
Cdd:cd05968 214 GRDLSYDEEKETAGDGAERTES-------EDPLMIIYTSGTTGKPKGTVHVHAGFPLKAAQD-MYFQFDLKPGDLLTWFT 285
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218563680 299 PL------YHCFGSVGGGVIMALYGTTVIFPSTGydgraNL-RAIEKEKCTFVYGTPTMYIDMLGQPD--LAKFDLSSVR 369
Cdd:cd05968 286 DLgwmmgpWLIFGGLILGATMVLYDGAPDHPKAD-----RLwRMVEDHEITHLGLSPTLIRALKPRGDapVNAHDLSSLR 360
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218563680 370 GGIAAGSPCPPEVMRKILNVMGIKEM-VIGY-GTTENSPVTFCGFPVdsaeRKIETVG--CISPHTEAKVVD-------P 438
Cdd:cd05968 361 VLGSTGEPWNPEPWNWLFETVGKGRNpIINYsGGTEISGGILGNVLI----KPIKPSSfnGPVPGMKADVLDesgkparP 436
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218563680 439 TTGEIVpLGAQGELMIRGYcvmleyWQDEEKTRECITkDRW---YKTGDIASLDQFAYCKIEGRIKDLIIRGGENIYPAE 515
Cdd:cd05968 437 EVGELV-LLAPWPGMTRGF------WRDEDRYLETYW-SRFdnvWVHGDFAYYDEEGYFYILGRSDDTINVAGKRVGPAE 508
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218563680 516 IEQFLHTHPKILEAQVVGVKDERMGEEVCACIRLKEG---QECTVEEIKAYCKGKIAHYKVPRYILFVQDYPLTITGKIQ 592
Cdd:cd05968 509 IESVLNAHPAVLESAAIGVPHPVKGEAIVCFVVLKPGvtpTEALAEELMERVADELGKPLSPERILFVKDLPKTRNAKVM 588
|
....*
gi 218563680 593 KHKLR 597
Cdd:cd05968 589 RRVIR 593
|
|
| A_NRPS_Bac |
cd17655 |
bacitracin synthetase and related proteins; This family of the adenylation (A) domain of ... |
253-598 |
8.12e-36 |
|
bacitracin synthetase and related proteins; This family of the adenylation (A) domain of nonribosomal peptide synthases (NRPS) includes bacitracin synthetases 1, 2, and 3 (BA1, also known as ATP-dependent cysteine adenylase or cysteine activase, BA2, also known as ATP-dependent lysine adenylase or lysine activase, and BA3, also known as ATP-dependent isoleucine adenylase or isoleucine activase) in Bacilli. Bacitracin is a mixture of related cyclic peptides used as a polypeptide antibiotic. This family also includes gramicidin synthetase 1 involved in synthesis of the cyclic peptide antibiotic gramicidin S via activation of phenylalanine. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.
Pssm-ID: 341310 [Multi-domain] Cd Length: 490 Bit Score: 140.54 E-value: 8.12e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218563680 253 IQFTSGTTGKPKGATLSHHNIVNnaYFTGMRIGYNWRKNVRICLPVPLYhcFGSVGGGVIMALY--GTTVIFP-STGYDG 329
Cdd:cd17655 142 VIYTSGSTGKPKGVMIEHRGVVN--LVEWANKVIYQGEHLRVALFASIS--FDASVTEIFASLLsgNTLYIVRkETVLDG 217
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218563680 330 RANLRAIEKEKCTFVYGTPTmYIDMLGQPDLAKFdlSSVRGGIAAGSPCPPEVMRKILNVMGIKEMVIG-YGTTEnspVT 408
Cdd:cd17655 218 QALTQYIRQNRITIIDLTPA-HLKLLDAADDSEG--LSLKHLIVGGEALSTELAKKIIELFGTNPTITNaYGPTE---TT 291
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218563680 409 FCG--FPVDSAERKIETVGCISP--HTEAKVVDpTTGEIVPLGAQGELMIRGYCVMLEYWQDEEKTRECITKD------R 478
Cdd:cd17655 292 VDAsiYQYEPETDQQVSVPIGKPlgNTRIYILD-QYGRPQPVGVAGELYIGGEGVARGYLNRPELTAEKFVDDpfvpgeR 370
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218563680 479 WYKTGDIASL--DQfaycKIE--GRIKDLI-IRgGENIYPAEIEQFLHTHPKILEAQVVGVKDERMGEEVCACIRLKEgq 553
Cdd:cd17655 371 MYRTGDLARWlpDG----NIEflGRIDHQVkIR-GYRIELGEIEARLLQHPDIKEAVVIARKDEQGQNYLCAYIVSEK-- 443
|
330 340 350 360
....*....|....*....|....*....|....*....|....*
gi 218563680 554 ECTVEEIKAYCKGKIAHYKVPRYILFVQDYPLTITGKIQKHKLRE 598
Cdd:cd17655 444 ELPVAQLREFLARELPDYMIPSYFIKLDEIPLTPNGKVDRKALPE 488
|
|
| PRK07787 |
PRK07787 |
acyl-CoA synthetase; Validated |
248-597 |
2.93e-35 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236096 [Multi-domain] Cd Length: 471 Bit Score: 138.58 E-value: 2.93e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218563680 248 DDPINIQFTSGTTGKPKGATLSHHNIVnnAYFTGMRIGYNWRKNVRICLPVPLYHCFGSVGGgVIMAL-YGTTVI----F 322
Cdd:PRK07787 128 DAPALIVYTSGTTGPPKGVVLSRRAIA--ADLDALAEAWQWTADDVLVHGLPLFHVHGLVLG-VLGPLrIGNRFVhtgrP 204
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218563680 323 PSTGYDGRANLRAiekekcTFVYGTPTMYIDMLGQPDLAKfDLSSVRGGIAAGSPCPPEVMRKILNVMGiKEMVIGYGTT 402
Cdd:PRK07787 205 TPEAYAQALSEGG------TLYFGVPTVWSRIAADPEAAR-ALRGARLLVSGSAALPVPVFDRLAALTG-HRPVERYGMT 276
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218563680 403 EnSPVTfCGFPVDsAERKIETVGCISPHTEAKVVDpTTGEIVPLGAQ--GELMIRGYCVMLEYWQDEEKTRECITKDRWY 480
Cdd:PRK07787 277 E-TLIT-LSTRAD-GERRPGWVGLPLAGVETRLVD-EDGGPVPHDGEtvGELQVRGPTLFDGYLNRPDATAAAFTADGWF 352
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218563680 481 KTGDIASLDQFAYCKIEGRIK-DLIIRGGENIYPAEIEQFLHTHPKILEAQVVGVKDERMGEEVCACIrlKEGQECTVEE 559
Cdd:PRK07787 353 RTGDVAVVDPDGMHRIVGREStDLIKSGGYRIGAGEIETALLGHPGVREAAVVGVPDDDLGQRIVAYV--VGADDVAADE 430
|
330 340 350
....*....|....*....|....*....|....*...
gi 218563680 560 IKAYCKGKIAHYKVPRYILFVQDYPLTITGKIQKHKLR 597
Cdd:PRK07787 431 LIDFVAQQLSVHKRPREVRFVDALPRNAMGKVLKKQLL 468
|
|
| PRK06814 |
PRK06814 |
acyl-[ACP]--phospholipid O-acyltransferase; |
247-591 |
1.23e-34 |
|
acyl-[ACP]--phospholipid O-acyltransferase;
Pssm-ID: 235865 [Multi-domain] Cd Length: 1140 Bit Score: 140.49 E-value: 1.23e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218563680 247 CDDPINIQFTSGTTGKPKGATLSHHNIVNNAYFTGMRIGYNWRKNVRICLPVplYHCFGSVGGGVIMALYGTTV------ 320
Cdd:PRK06814 792 PDDPAVILFTSGSEGTPKGVVLSHRNLLANRAQVAARIDFSPEDKVFNALPV--FHSFGLTGGLVLPLLSGVKVflypsp 869
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218563680 321 ----IFPSTGYDGRAnlraiekekcTFVYGTPTMyidMLGQPDLAK-FDLSSVRGGIAAGSPCPPEVMRKILNVMGIKeM 395
Cdd:PRK06814 870 lhyrIIPELIYDTNA----------TILFGTDTF---LNGYARYAHpYDFRSLRYVFAGAEKVKEETRQTWMEKFGIR-I 935
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218563680 396 VIGYGTTENSPVTFCGFPVDSaerKIETVGCISPHTEAKvVDPTTGeiVPLGaqGELMIRGYCVMLEYWQDEEKTRECIT 475
Cdd:PRK06814 936 LEGYGVTETAPVIALNTPMHN---KAGTVGRLLPGIEYR-LEPVPG--IDEG--GRLFVRGPNVMLGYLRAENPGVLEPP 1007
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218563680 476 KDRWYKTGDIASLDQFAYCKIEGRIKDLIIRGGENIYPAEIEQFLHT-HPKILEAqVVGVKDERMGEEVcacIRLKEGQE 554
Cdd:PRK06814 1008 ADGWYDTGDIVTIDEEGFITIKGRAKRFAKIAGEMISLAAVEELAAElWPDALHA-AVSIPDARKGERI---ILLTTASD 1083
|
330 340 350
....*....|....*....|....*....|....*...
gi 218563680 555 CTVEEIKAYCKGK-IAHYKVPRYILFVQDYPLTITGKI 591
Cdd:PRK06814 1084 ATRAAFLAHAKAAgASELMVPAEIITIDEIPLLGTGKI 1121
|
|
| A_NRPS_TubE_like |
cd05906 |
The adenylation domain (A domain) of a family of nonribosomal peptide synthetases (NRPSs) ... |
72-601 |
1.79e-34 |
|
The adenylation domain (A domain) of a family of nonribosomal peptide synthetases (NRPSs) synthesizing toxins and antitumor agents; The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino)-acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. This family includes NRPSs that synthesize toxins and antitumor agents; for example, TubE for Tubulysine, CrpA for cryptophycin, TdiA for terrequinone A, KtzG for kutzneride, and Vlm1/Vlm2 for Valinomycin. Nonribosomal peptide synthetases are large multifunctional enzymes which synthesize many therapeutically useful peptides. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and, in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.
Pssm-ID: 341232 [Multi-domain] Cd Length: 540 Bit Score: 137.41 E-value: 1.79e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218563680 72 LQATVERYPDReAMVFVQD---GIRKTFAEFYQDVEKAAAGLLAAGLKRGDRLGMWGPNIYEWVLMQFATAKAGIILVAV 148
Cdd:cd05906 16 LLRAAERGPTK-GITYIDAdgsEEFQSYQDLLEDARRLAAGLRQLGLRPGDSVILQFDDNEDFIPAFWACVLAGFVPAPL 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218563680 149 NPAYQLQEVEFALRKVqcnavvcptkfksqhyCDMLKQLcpemetASPGGIKSSRL-PDLHTvIVTDSQQPGSFLL--KD 225
Cdd:cd05906 95 TVPPTYDEPNARLRKL----------------RHIWQLL------GSPVVLTDAELvAEFAG-LETLSGLPGIRVLsiEE 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218563680 226 LMQAGSSQHYQQLQDlqkklvcDDPINIQFTSGTTGKPKGATLSHHNIVN-------NAYFTGMRIGYNWrknvriclpV 298
Cdd:cd05906 152 LLDTAADHDLPQSRP-------DDLALLMLTSGSTGFPKAVPLTHRNILArsagkiqHNGLTPQDVFLNW---------V 215
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218563680 299 PLYHcfgsVGGGV---IMALY-GTTVIFPSTGY---DGRANLRAIEKEKCTFVYGtPTMYIDMLGQ----PDLAKFDLSS 367
Cdd:cd05906 216 PLDH----VGGLVelhLRAVYlGCQQVHVPTEEilaDPLRWLDLIDRYRVTITWA-PNFAFALLNDlleeIEDGTWDLSS 290
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218563680 368 VRGGIAAGSPCPPEVMRKILNVM---GIKEMVI--GYGTTEN-SPVTFC-GFPVDSAERKIETVGCISPH--TEAKVVDP 438
Cdd:cd05906 291 LRYLVNAGEAVVAKTIRRLLRLLepyGLPPDAIrpAFGMTETcSGVIYSrSFPTYDHSQALEFVSLGRPIpgVSMRIVDD 370
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218563680 439 TtGEIVPLGAQGELMIRGYCVMLEYWQDEEKTRECITKDRWYKTGDIASLDQFAYcKIEGRIKDLIIRGGENIYPAEIEQ 518
Cdd:cd05906 371 E-GQLLPEGEVGRLQVRGPVVTKGYYNNPEANAEAFTEDGWFRTGDLGFLDNGNL-TITGRTKDTIIVNGVNYYSHEIEA 448
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218563680 519 FLHTHPkILE---AQVVGVKDERMGEEVCAC-----IRLKEGQECTVEEIKayckgKIAHYKV---PRYILFVQ--DYPL 585
Cdd:cd05906 449 AVEEVP-GVEpsfTAAFAVRDPGAETEELAIffvpeYDLQDALSETLRAIR-----SVVSREVgvsPAYLIPLPkeEIPK 522
|
570
....*....|....*.
gi 218563680 586 TITGKIQKHKLRERTE 601
Cdd:cd05906 523 TSLGKIQRSKLKAAFE 538
|
|
| FADD10 |
cd17635 |
adenylate forming domain, fatty acid CoA ligase (FadD10); This family contains long chain ... |
249-593 |
1.88e-34 |
|
adenylate forming domain, fatty acid CoA ligase (FadD10); This family contains long chain fatty acid CoA ligases, including FadD10 which is involved in the synthesis of a virulence-related lipopeptide. FadD10 is a fatty acyl-AMP ligase (FAAL) that transfers fatty acids to an acyl carrier protein. Structures of FadD10 in apo- and complexed form with dodecanoyl-AMP, show a novel open conformation, facilitated by its unique inter-domain and intermolecular interactions, which is critical for the enzyme to carry out the acyl transfer onto the acyl carrier protein (Rv0100) rather than coenzyme A.
Pssm-ID: 341290 [Multi-domain] Cd Length: 340 Bit Score: 133.54 E-value: 1.88e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218563680 249 DPINIQFTSGTTGKPKGATLSHHNIVNnAYFTGMRIGYNWRKNVRICLPVPLYHCFGSVGGGVIMALYGTTVIFPS-TGY 327
Cdd:cd17635 2 DPLAVIFTSGTTGEPKAVLLANKTFFA-VPDILQKEGLNWVVGDVTYLPLPATHIGGLWWILTCLIHGGLCVTGGEnTTY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218563680 328 dgRANLRAIEKEKCTFVYGTPT-------MYIDMLGQPDLAKFdlssvrggIAAGSPCPPEVMRKILNVMGIKEMVIGYG 400
Cdd:cd17635 81 --KSLFKILTTNAVTTTCLVPTllsklvsELKSANATVPSLRL--------IGYGGSRAIAADVRFIEATGLTNTAQVYG 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218563680 401 TTENSPVTFCGFPVDSAErkIETVGCISPHTEAKVVDpTTGEIVPLGAQGELMIRGYCVMLEYWQDEEKTRECITkDRWY 480
Cdd:cd17635 151 LSETGTALCLPTDDDSIE--INAVGRPYPGVDVYLAA-TDGIAGPSASFGTIWIKSPANMLGYWNNPERTAEVLI-DGWV 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218563680 481 KTGDIASLDQFAYCKIEGRIKDLIIRGGENIYPAEIEQFLHTHPKILEAQVVGVKDERMGEEVCACIrLKEGQEC--TVE 558
Cdd:cd17635 227 NTGDLGERREDGFLFITGRSSESINCGGVKIAPDEVERIAEGVSGVQECACYEISDEEFGELVGLAV-VASAELDenAIR 305
|
330 340 350
....*....|....*....|....*....|....*
gi 218563680 559 EIKAYCKGKIAHYKVPRYILFVQDYPLTITGKIQK 593
Cdd:cd17635 306 ALKHTIRRELEPYARPSTIVIVTDIPRTQSGKVKR 340
|
|
| entE |
PRK10946 |
(2,3-dihydroxybenzoyl)adenylate synthase; |
75-604 |
8.22e-34 |
|
(2,3-dihydroxybenzoyl)adenylate synthase;
Pssm-ID: 236803 [Multi-domain] Cd Length: 536 Bit Score: 135.50 E-value: 8.22e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218563680 75 TVERYPDREAMVfvqDGIRK-TFAEFYQDVEKAAAGLLAAGLKRGDRLGMWGPNIYEWVLMQFATAKAGIilVAVNPAYQ 153
Cdd:PRK10946 32 TRHAASDAIAVI---CGERQfSYRELNQASDNLACSLRRQGIKPGDTALVQLGNVAEFYITFFALLKLGV--APVNALFS 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218563680 154 LQEVE---FAlRKVQCNAVVCPTK---FKSQHYCDMLKQLCPEMEtaspggikssrlpdlhtvIVTDSQQPGSFLLKDLM 227
Cdd:PRK10946 107 HQRSElnaYA-SQIEPALLIADRQhalFSDDDFLNTLVAEHSSLR------------------VVLLLNDDGEHSLDDAI 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218563680 228 QAGSSQHYQQlqdlqkKLVCDDPINIQFTSGTTGKPKGATLSHhnivnNAYFtgmrigYNWRKNVRIC-----------L 296
Cdd:PRK10946 168 NHPAEDFTAT------PSPADEVAFFQLSGGSTGTPKLIPRTH-----NDYY------YSVRRSVEICgftpqtrylcaL 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218563680 297 PVPlyHCF-----GSVG-----GGVIMALY-GTTVIFPstgydgranlrAIEKEKCTFVYGTP---TMYIDMLGQPD--- 359
Cdd:PRK10946 231 PAA--HNYpmsspGALGvflagGTVVLAPDpSATLCFP-----------LIEKHQVNVTALVPpavSLWLQAIAEGGsra 297
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218563680 360 -LAKFDLSSVRG---GIAAGSPCPPEVMRKILNVMGIKEMVIGYGTTEnspvtfcgfpvDSAERKIETVGC-ISPHTEAK 434
Cdd:PRK10946 298 qLASLKLLQVGGarlSETLARRIPAELGCQLQQVFGMAEGLVNYTRLD-----------DSDERIFTTQGRpMSPDDEVW 366
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218563680 435 VVDpTTGEIVPLGAQGELMIRGYCVMLEYWQDEEKTRECITKDRWYKTGDIASLDQFAYCKIEGRIKDLIIRGGENIYPA 514
Cdd:PRK10946 367 VAD-ADGNPLPQGEVGRLMTRGPYTFRGYYKSPQHNASAFDANGFYCSGDLVSIDPDGYITVVGREKDQINRGGEKIAAE 445
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218563680 515 EIEQFLHTHPKILEAQVVGVKDERMGEEVCACIRLKEGQECTVeeIKAYCKGK-IAHYKVPRYILFVQDYPLTITGKIQK 593
Cdd:PRK10946 446 EIENLLLRHPAVIHAALVSMEDELMGEKSCAFLVVKEPLKAVQ--LRRFLREQgIAEFKLPDRVECVDSLPLTAVGKVDK 523
|
570
....*....|.
gi 218563680 594 HKLRERTEKQL 604
Cdd:PRK10946 524 KQLRQWLASRA 534
|
|
| A_NRPS_Srf_like |
cd12117 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including Bacillus subtilis ... |
73-596 |
1.29e-33 |
|
The adenylation domain of nonribosomal peptide synthetases (NRPS), including Bacillus subtilis termination module Surfactin (SrfA-C); The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and, in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions. This family includes the adenylation domain of the Bacillus subtilis termination module (Surfactin domain, SrfA-C) which recognizes a specific amino acid building block, which is then activated and transferred to the terminal thiol of the 4'-phosphopantetheine (Ppan) arm of the downstream peptidyl carrier protein (PCP) domain.
Pssm-ID: 341282 [Multi-domain] Cd Length: 483 Bit Score: 134.25 E-value: 1.29e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218563680 73 QATVERYPDREAmvfVQDGIRK-TFAEFYQDVEKAAAGLLAAGLKRGDRLGMWGPNIYEWVLMQFATAKAGIILVAVNPA 151
Cdd:cd12117 4 EEQAARTPDAVA---VVYGDRSlTYAELNERANRLARRLRAAGVGPGDVVGVLAERSPELVVALLAVLKAGAAYVPLDPE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218563680 152 YQLQEVEFALRKVQCNAVVCPTKFKSQHYCDMLKQLCPEMETASPGGikssrlpDLHTVIvtdsqQPgsfllkdlmqags 231
Cdd:cd12117 81 LPAERLAFMLADAGAKVLLTDRSLAGRAGGLEVAVVIDEALDAGPAG-------NPAVPV-----SP------------- 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218563680 232 sqhyqqlqdlqkklvcDDPINIQFTSGTTGKPKGATLSHHNIVnnayftgmrigynwrknvRICLPvplyHCFGSVGGGV 311
Cdd:cd12117 136 ----------------DDLAYVMYTSGSTGRPKGVAVTHRGVV------------------RLVKN----TNYVTLGPDD 177
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218563680 312 IMALY-------------------GTTVIFP-STGYDGRANLRAIEKEKCTFVYGTPTMYiDMLGQPDLAKFdlSSVRGG 371
Cdd:cd12117 178 RVLQTsplafdastfeiwgallngARLVLAPkGTLLDPDALGALIAEEGVTVLWLTAALF-NQLADEDPECF--AGLREL 254
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218563680 372 IAAGSPCPPEVMRKILNVMGIKEMVIGYGTTENSpvTF-CGFPVDSAERKIETV--GCISPHTEAKVVDPTtGEIVPLGA 448
Cdd:cd12117 255 LTGGEVVSPPHVRRVLAACPGLRLVNGYGPTENT--TFtTSHVVTELDEVAGSIpiGRPIANTRVYVLDED-GRPVPPGV 331
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218563680 449 QGELMIRGYCVMLEYWQDEEKTRECITKD------RWYKTGDIASLDQFAYCKIEGRIKDLI-IRGgENIYPAEIEQFLH 521
Cdd:cd12117 332 PGELYVGGDGLALGYLNRPALTAERFVADpfgpgeRLYRTGDLARWLPDGRLEFLGRIDDQVkIRG-FRIELGEIEAALR 410
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 218563680 522 THPKILEAqVVGVKDERMGE-EVCACIRLKEgqECTVEEIKAYCKGKIAHYKVPRYILFVQDYPLTITGKIQKHKL 596
Cdd:cd12117 411 AHPGVREA-VVVVREDAGGDkRLVAYVVAEG--ALDAAELRAFLRERLPAYMVPAAFVVLDELPLTANGKVDRRAL 483
|
|
| EntF |
COG1020 |
EntF, seryl-AMP synthase component of non-ribosomal peptide synthetase [Secondary metabolites ... |
64-590 |
4.96e-31 |
|
EntF, seryl-AMP synthase component of non-ribosomal peptide synthetase [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 440643 [Multi-domain] Cd Length: 1329 Bit Score: 129.59 E-value: 4.96e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218563680 64 QSSTVDQCLQATVERYPDREAMVFvqDGIRKTFAEFYQdvekaaagllaaglkRGDRLGMW------GPN----IY---- 129
Cdd:COG1020 474 ADATLHELFEAQAARTPDAVAVVF--GDQSLTYAELNA---------------RANRLAHHlralgvGPGdlvgVClers 536
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218563680 130 -EWVLMQFATAKAGIILVAVNPAYQLQEVEFALRKVQCNAVVCPTKFKSqhycdmlkqlcpemetaspggikssRLPDLH 208
Cdd:COG1020 537 lEMVVALLAVLKAGAAYVPLDPAYPAERLAYMLEDAGARLVLTQSALAA-------------------------RLPELG 591
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218563680 209 -TVIVTDSQQPGSFLLKDLMQAGSSQH--YqqlqdlqkklvcddpinIQFTSGTTGKPKGATLSHHNIVNnaYFTGMRIG 285
Cdd:COG1020 592 vPVLALDALALAAEPATNPPVPVTPDDlaY-----------------VIYTSGSTGRPKGVMVEHRALVN--LLAWMQRR 652
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218563680 286 YNWRKNVRICLPVPLyhCF-GSVgGGVIMALY--GTTVIFPSTG-YDGRANLRAIEKEKCTFVYGTPTMYiDMLgqPDLA 361
Cdd:COG1020 653 YGLGPGDRVLQFASL--SFdASV-WEIFGALLsgATLVLAPPEArRDPAALAELLARHRVTVLNLTPSLL-RAL--LDAA 726
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218563680 362 KFDLSSVRGGIAAGSPCPPEVMRKILNVMGIKEMVIGYGTTENSpVTFCGFPVDSAERKIETV--GCISPHTEAKVVDPt 439
Cdd:COG1020 727 PEALPSLRLVLVGGEALPPELVRRWRARLPGARLVNLYGPTETT-VDSTYYEVTPPDADGGSVpiGRPIANTRVYVLDA- 804
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218563680 440 TGEIVPLGAQGELMIRGYCVMLEYWQDEEKTRE-------CITKDRWYKTGDIA------SLDqFAyckieGRIKDLI-I 505
Cdd:COG1020 805 HLQPVPVGVPGELYIGGAGLARGYLNRPELTAErfvadpfGFPGARLYRTGDLArwlpdgNLE-FL-----GRADDQVkI 878
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218563680 506 RGgeniY---PAEIEQFLHTHPKILEAQVVGVKDERMGEEVCACIRLKEGQECTVEEIKAYCKGKIAHYKVPRYILFVQD 582
Cdd:COG1020 879 RG----FrieLGEIEAALLQHPGVREAVVVAREDAPGDKRLVAYVVPEAGAAAAAALLRLALALLLPPYMVPAAVVLLLP 954
|
....*...
gi 218563680 583 YPLTITGK 590
Cdd:COG1020 955 LPLTGNGK 962
|
|
| PRK05620 |
PRK05620 |
long-chain fatty-acid--CoA ligase; |
117-598 |
7.12e-31 |
|
long-chain fatty-acid--CoA ligase;
Pssm-ID: 180167 [Multi-domain] Cd Length: 576 Bit Score: 127.21 E-value: 7.12e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218563680 117 RGDRLGMWGPNIYEWVLMQFATAKAGIILVAVNPAYQLQEVEFALRKVQCNAVVCPTKFKSQhYCDMLKQlCPEMET--- 193
Cdd:PRK05620 63 GDQRVGSMMYNCAEHLEVLFAVACMGAVFNPLNKQLMNDQIVHIINHAEDEVIVADPRLAEQ-LGEILKE-CPCVRAvvf 140
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218563680 194 ASPGGIKSSRLPDLHTVIVTDSQQpgsflLKDlmqaGSSQHYQqLQDLQKklvcDDPINIQFTSGTTGKPKGATLSHHNI 273
Cdd:PRK05620 141 IGPSDADSAAAHMPEGIKVYSYEA-----LLD----GRSTVYD-WPELDE----TTAAAICYSTGTTGAPKGVVYSHRSL 206
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218563680 274 vnnaYFTGMRI----GYNWRKNVRICLPVPLYHCfgsVGGGVIMALY--GTTVIFPSTGYDGRANLRAIEKEKCTFVYGT 347
Cdd:PRK05620 207 ----YLQSLSLrttdSLAVTHGESFLCCVPIYHV---LSWGVPLAAFmsGTPLVFPGPDLSAPTLAKIIATAMPRVAHGV 279
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218563680 348 PTMYIDMLGQPDLAKFDLSSVRGGIAAGSPCPPEVMRKILNVMGIkEMVIGYGTTENSPVTFCGFP---VDSAERKI--E 422
Cdd:PRK05620 280 PTLWIQLMVHYLKNPPERMSLQEIYVGGSAVPPILIKAWEERYGV-DVVHVWGMTETSPVGTVARPpsgVSGEARWAyrV 358
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218563680 423 TVGCISPHTEAKVVDptTGEIVPLG--AQGELMIRGYCVMLEYWQDE----------------EKTRECITKDRWYKTGD 484
Cdd:PRK05620 359 SQGRFPASLEYRIVN--DGQVMESTdrNEGEIQVRGNWVTASYYHSPteegggaastfrgedvEDANDRFTADGWLRTGD 436
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218563680 485 IASLDQFAYCKIEGRIKDLIIRGGENIYPAEIEQFLHTHPKILEAQVVGVKDERMGEEVCACIRLKEGQEC---TVEEIK 561
Cdd:PRK05620 437 VGSVTRDGFLTIHDRARDVIRSGGEWIYSAQLENYIMAAPEVVECAVIGYPDDKWGERPLAVTVLAPGIEPtreTAERLR 516
|
490 500 510
....*....|....*....|....*....|....*..
gi 218563680 562 AYCKGKIAHYKVPRYILFVQDYPLTITGKIQKHKLRE 598
Cdd:PRK05620 517 DQLRDRLPNWMLPEYWTFVDEIDKTSVGKFDKKDLRQ 553
|
|
| MACS_like_2 |
cd05973 |
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the ... |
248-597 |
7.66e-31 |
|
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the two-step activation of medium chain fatty acids (containing 4-12 carbons). The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. MACS enzymes are localized to mitochondria.
Pssm-ID: 341277 [Multi-domain] Cd Length: 437 Bit Score: 125.32 E-value: 7.66e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218563680 248 DDPINIQFTSGTTGKPKGATLSHHNIVnnAYFTGMRIGYNWRKNVRI-CLPVP--LYHCFGSVGGGVIMalyGTTVIFPS 324
Cdd:cd05973 88 SDPFVMMFTSGTTGLPKGVPVPLRALA--AFGAYLRDAVDLRPEDSFwNAADPgwAYGLYYAITGPLAL---GHPTILLE 162
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218563680 325 TGYDGRANLRAIEKEKCTFVYGTPTMYIDMLGQPDLAKFDLS-SVRGGIAAGSPCPPEVMRKILNVMGIKeMVIGYGTTE 403
Cdd:cd05973 163 GGFSVESTWRVIERLGVTNLAGSPTAYRLLMAAGAEVPARPKgRLRRVSSAGEPLTPEVIRWFDAALGVP-IHDHYGQTE 241
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218563680 404 NSPVtFCGFPVDSAERKIETVGCISPHTEAKVVDPTTGEIVPlGAQGELMI----------RGYcvmleyWQDEEKTrec 473
Cdd:cd05973 242 LGMV-LANHHALEHPVHAGSAGRAMPGWRVAVLDDDGDELGP-GEPGRLAIdiansplmwfRGY------QLPDTPA--- 310
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218563680 474 iTKDRWYKTGDIASLD---QFAYCkieGRIKDLIIRGGENIYPAEIEQFLHTHPKILEAQVVGVKDERMGEEVCACIRLK 550
Cdd:cd05973 311 -IDGGYYLTGDTVEFDpdgSFSFI---GRADDVITMSGYRIGPFDVESALIEHPAVAEAAVIGVPDPERTEVVKAFVVLR 386
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|
gi 218563680 551 EGQECTVE---EIKAYCKGKIAHYKVPRYILFVQDYPLTITGKIQKHKLR 597
Cdd:cd05973 387 GGHEGTPAladELQLHVKKRLSAHAYPRTIHFVDELPKTPSGKIQRFLLR 436
|
|
| MACS_like_1 |
cd05974 |
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the ... |
248-600 |
1.27e-30 |
|
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the two-step activation of medium chain fatty acids (containing 4-12 carbons). The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. MACS enzymes are localized to mitochondria.
Pssm-ID: 341278 [Multi-domain] Cd Length: 432 Bit Score: 124.60 E-value: 1.27e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218563680 248 DDPINIQFTSGTTGKPKGATLSHHNI----VNNAYFTGMRIG---YN-----WRKNVRICLPVPLyhcfgSVGGgvimal 315
Cdd:cd05974 85 DDPMLLYFTSGTTSKPKLVEHTHRSYpvghLSTMYWIGLKPGdvhWNisspgWAKHAWSCFFAPW-----NAGA------ 153
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218563680 316 ygTTVIFPSTGYDGRANLRAIEKEKCTFVYGTPTMYiDMLGQPDLAKFDLSsVRGGIAAGSPCPPEVMRKILNVMGIKeM 395
Cdd:cd05974 154 --TVFLFNYARFDAKRVLAALVRYGVTTLCAPPTVW-RMLIQQDLASFDVK-LREVVGAGEPLNPEVIEQVRRAWGLT-I 228
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218563680 396 VIGYGTTE------NSPvtfcGFPVdsaerKIETVGCISPHTEAKVVDPTTGEIvplgAQGELMI-----RGYCVMLEYW 464
Cdd:cd05974 229 RDGYGQTEttalvgNSP----GQPV-----KAGSMGRPLPGYRVALLDPDGAPA----TEGEVALdlgdtRPVGLMKGYA 295
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218563680 465 QDEEKTRECItKDRWYKTGDIASLDQFAYCKIEGRIKDLIIRGGENIYPAEIEQFLHTHPKILEAQVVGVKDERMGEEVC 544
Cdd:cd05974 296 GDPDKTAHAM-RGGYYRTGDIAMRDEDGYLTYVGRADDVFKSSDYRISPFELESVLIEHPAVAEAAVVPSPDPVRLSVPK 374
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*....
gi 218563680 545 ACIRLKEGQECTVE---EIKAYCKGKIAHYKVPRYILFVQdYPLTITGKIQKHKLRERT 600
Cdd:cd05974 375 AFIVLRAGYEPSPEtalEIFRFSRERLAPYKRIRRLEFAE-LPKTISGKIRRVELRRRE 432
|
|
| ACS |
cd05966 |
Acetyl-CoA synthetase (also known as acetate-CoA ligase and acetyl-activating enzyme); ... |
71-605 |
9.29e-30 |
|
Acetyl-CoA synthetase (also known as acetate-CoA ligase and acetyl-activating enzyme); Acetyl-CoA synthetase (ACS, EC 6.2.1.1, acetate#CoA ligase or acetate:CoA ligase (AMP-forming)) catalyzes the formation of acetyl-CoA from acetate, CoA, and ATP. Synthesis of acetyl-CoA is carried out in a two-step reaction. In the first step, the enzyme catalyzes the synthesis of acetyl-AMP intermediate from acetate and ATP. In the second step, acetyl-AMP reacts with CoA to produce acetyl-CoA. This enzyme is widely present in all living organisms. The activity of this enzyme is crucial for maintaining the required levels of acetyl-CoA, a key intermediate in many important biosynthetic and catabolic processes. Acetyl-CoA is used in the biosynthesis of glucose, fatty acids, and cholesterol. It can also be used in the production of energy in the citric acid cycle. Eukaryotes typically have two isoforms of acetyl-CoA synthetase, a cytosolic form involved in biosynthetic processes and a mitochondrial form primarily involved in energy generation.
Pssm-ID: 341270 [Multi-domain] Cd Length: 608 Bit Score: 124.21 E-value: 9.29e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218563680 71 CLQATVERYPDREAMVF----VQDGIRKTFAEFYQDVEKAAAGLLAAGLKRGDRLGMWGPNIYEWVLMQFATAKAGIILV 146
Cdd:cd05966 58 CLDRHLKERGDKVAIIWegdePDQSRTITYRELLREVCRFANVLKSLGVKKGDRVAIYMPMIPELVIAMLACARIGAVHS 137
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218563680 147 AVNPAYQLQEVefALRKVQCNAVVCPTkfksqhyCD---------MLKQLCPE-METAspggikssrlPDLHTVIV---- 212
Cdd:cd05966 138 VVFAGFSAESL--ADRINDAQCKLVIT-------ADggyrggkviPLKEIVDEaLEKC----------PSVEKVLVvkrt 198
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218563680 213 ---TDSQQPGSFLLKDLMQAGSSQHYQQLQDlqkklvCDDPINIQFTSGTTGKPKGATLSHHNIVNNAYFTgMRIGYNWR 289
Cdd:cd05966 199 ggeVPMTEGRDLWWHDLMAKQSPECEPEWMD------SEDPLFILYTSGSTGKPKGVVHTTGGYLLYAATT-FKYVFDYH 271
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218563680 290 knvriclPVPLYHCFGSVG--GGVIMALYG------TTVIF---PSTGYDGRAnLRAIEKEKCTFVYGTPTMyIDML--- 355
Cdd:cd05966 272 -------PDDIYWCTADIGwiTGHSYIVYGplangaTTVMFegtPTYPDPGRY-WDIVEKHKVTIFYTAPTA-IRALmkf 342
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218563680 356 GQPDLAKFDLSSVR--GGIaaGSPCPPEVMRKILNVMGIKEMVIG--YGTTE-----NSPVTF--------CGFPVdsae 418
Cdd:cd05966 343 GDEWVKKHDLSSLRvlGSV--GEPINPEAWMWYYEVIGKERCPIVdtWWQTEtggimITPLPGatplkpgsATRPF---- 416
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218563680 419 rkietvgcisPHTEAKVVDPTTGEIvPLGAQGEL--------MIRGYcvmleyWQDEEKTRECITKD--RWYKTGDIASL 488
Cdd:cd05966 417 ----------FGIEPAILDEEGNEV-EGEVEGYLvikrpwpgMARTI------YGDHERYEDTYFSKfpGYYFTGDGARR 479
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218563680 489 DQFAYCKIEGRIKDLIIRGGENIYPAEIEQFLHTHPKILEAQVVGVKDERMGEEVCACIRLKEGQECTVE---EIKAYCK 565
Cdd:cd05966 480 DEDGYYWITGRVDDVINVSGHRLGTAEVESALVAHPAVAEAAVVGRPHDIKGEAIYAFVTLKDGEEPSDElrkELRKHVR 559
|
570 580 590 600
....*....|....*....|....*....|....*....|..
gi 218563680 566 GKIAHYKVPRYILFVQDYPLTITGKIQKHKLRERT--EKQLG 605
Cdd:cd05966 560 KEIGPIATPDKIQFVPGLPKTRSGKIMRRILRKIAagEEELG 601
|
|
| PRK13383 |
PRK13383 |
acyl-CoA synthetase; Provisional |
72-596 |
5.95e-29 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 139531 [Multi-domain] Cd Length: 516 Bit Score: 120.87 E-value: 5.95e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218563680 72 LQATVERYPDREAMVfvQDGIRKTFAEFYQDVEKAAAGLLAAGLKRGDRLGMWGPNIYEWVLMQFATAKAGIILVAVNPA 151
Cdd:PRK13383 41 LAVTAARWPGRTAII--DDDGALSYRELQRATESLARRLTRDGVAPGRAVGVMCRNGRGFVTAVFAVGLLGADVVPISTE 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218563680 152 YQLQEVEFALRKVQCNAVVCPTKFKSQHYC--DMLKQLCPEMETASPGGIKSSRLPdlhtvivtdsqqPGSFLLkdlmqa 229
Cdd:PRK13383 119 FRSDALAAALRAHHISTVVADNEFAERIAGadDAVAVIDPATAGAEESGGRPAVAA------------PGRIVL------ 180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218563680 230 gssqhyqqlqdlqkklvcddpiniqFTSGTTGKPKGA----TLSHHNIVNNAYFTGMRIgynwRKNVRICLPVPLYHcfg 305
Cdd:PRK13383 181 -------------------------LTSGTTGKPKGVprapQLRSAVGVWVTILDRTRL----RTGSRISVAMPMFH--- 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218563680 306 SVGGGVIM---ALYGTtvIFPSTGYDGRANLRAIEKEKCTFVYGTPTMYIDMLGQPDL--AKFDLSSVRGGIAAGSPCPP 380
Cdd:PRK13383 229 GLGLGMLMltiALGGT--VLTHRHFDAEAALAQASLHRADAFTAVPVVLARILELPPRvrARNPLPQLRVVMSSGDRLDP 306
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218563680 381 EVMRKILNVMGiKEMVIGYGTTE------NSPVTFCGFPvdsaerkiETVGCISPHTEAKVVDPTTGEIVPLgAQGELMI 454
Cdd:PRK13383 307 TLGQRFMDTYG-DILYNGYGSTEvgigalATPADLRDAP--------ETVGKPVAGCPVRILDRNNRPVGPR-VTGRIFV 376
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218563680 455 RGYCVMLEYWQDEEKTreciTKDRWYKTGDIASLDQFAYCKIEGRIKDLIIRGGENIYPAEIEQFLHTHPKILEAQVVGV 534
Cdd:PRK13383 377 GGELAGTRYTDGGGKA----VVDGMTSTGDMGYLDNAGRLFIVGREDDMIISGGENVYPRAVENALAAHPAVADNAVIGV 452
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 218563680 535 KDERMGEEVCACIRLKEGQECTVEEIKAYCKGKIAHYKVPRYILFVQDYPLTITGKIQKHKL 596
Cdd:PRK13383 453 PDERFGHRLAAFVVLHPGSGVDAAQLRDYLKDRVSRFEQPRDINIVSSIPRNPTGKVLRKEL 514
|
|
| A_NRPS_Sfm_like |
cd12115 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including Saframycin A gene ... |
238-596 |
1.77e-27 |
|
The adenylation domain of nonribosomal peptide synthetases (NRPS), including Saframycin A gene cluster from Streptomyces lavendulae; The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions. This family includes the saframycin A gene cluster from Streptomyces lavendulae which implicates the NRPS system for assembling the unusual tetrapeptidyl skeleton in an iterative manner. It also includes saframycin Mx1 produced by Myxococcus xanthus NRPS.
Pssm-ID: 341280 [Multi-domain] Cd Length: 447 Bit Score: 115.49 E-value: 1.77e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218563680 238 LQDLQKKLVCDDPIN---IQFTSGTTGKPKGATLSHHNIVNNAYFTGMRIGYNWRKNV----RICLPVPLYHCFG--SVG 308
Cdd:cd12115 92 LEDAQARLVLTDPDDlayVIYTSGSTGRPKGVAIEHRNAAAFLQWAAAAFSAEELAGVlastSICFDLSVFELFGplATG 171
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218563680 309 GGVIMAlygttvifpstgyDGRANLRAIEKEK-CTFVYGTPTMYIDMLGQPDLAKfdlsSVRGGIAAGSPCPPEVMRKIL 387
Cdd:cd12115 172 GKVVLA-------------DNVLALPDLPAAAeVTLINTVPSAAAELLRHDALPA----SVRVVNLAGEPLPRDLVQRLY 234
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218563680 388 NVMGIKEMVIGYGTTENSPV-TFCgfPVDSAERKIETVGCISPHTEAKVVDpTTGEIVPLGAQGELMIRGYCVMLEYWQD 466
Cdd:cd12115 235 ARLQVERVVNLYGPSEDTTYsTVA--PVPPGASGEVSIGRPLANTQAYVLD-RALQPVPLGVPGELYIGGAGVARGYLGR 311
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218563680 467 EEKTRECITKD------RWYKTGDIASLDQFAYCKIEGRIKDLIIRGGENIYPAEIEQFLHTHPKILEAQVVGVKDERMG 540
Cdd:cd12115 312 PGLTAERFLPDpfgpgaRLYRTGDLVRWRPDGLLEFLGRADNQVKVRGFRIELGEIEAALRSIPGVREAVVVAIGDAAGE 391
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*.
gi 218563680 541 EEVCACIRLKEGQECTVEEIKAYCKGKIAHYKVPRYILFVQDYPLTITGKIQKHKL 596
Cdd:cd12115 392 RRLVAYIVAEPGAAGLVEDLRRHLGTRLPAYMVPSRFVRLDALPLTPNGKIDRSAL 447
|
|
| A_NRPS_AB3403-like |
cd17646 |
Peptide Synthetase; The adenylation (A) domain of NRPS recognizes a specific amino acid or ... |
74-591 |
5.58e-27 |
|
Peptide Synthetase; The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester bond to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.
Pssm-ID: 341301 [Multi-domain] Cd Length: 488 Bit Score: 114.68 E-value: 5.58e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218563680 74 ATVERYPDREAMVFvqDGIRKTFAEFYQDVEKAAAGLLAAGLKRGDRLGMWGPNIYEWVLMQFATAKAGIILVAVNPAYQ 153
Cdd:cd17646 6 EQAARTPDAPAVVD--EGRTLTYRELDERANRLAHLLRARGVGPEDRVAVLLPRSADLVVALLAVLKAGAAYLPLDPGYP 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218563680 154 LQEVEFALRkvQCNAVVCPTkfksqhycdmlkqlcpemETASPGgikssRLPDLHTVIVTDSQQPGSFllkdlmqagssq 233
Cdd:cd17646 84 ADRLAYMLA--DAGPAVVLT------------------TADLAA-----RLPAGGDVALLGDEALAAP------------ 126
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218563680 234 hyqQLQDLQKKLVCDDPINIQFTSGTTGKPKGATLSHHNIVNnaYFTGMRIGYNWRKNVRICLPVPL------YHCFG-- 305
Cdd:cd17646 127 ---PATPPLVPPRPDNLAYVIYTSGSTGRPKGVMVTHAGIVN--RLLWMQDEYPLGPGDRVLQKTPLsfdvsvWELFWpl 201
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218563680 306 SVGGGVIMALygttvifPSTGYDGRANLRAIEKEKCTFVYGTPTMYIDMLGQPDLAkfDLSSVRGGIAAGSPCPPEVMRK 385
Cdd:cd17646 202 VAGARLVVAR-------PGGHRDPAYLAALIREHGVTTCHFVPSMLRVFLAEPAAG--SCASLRRVFCSGEALPPELAAR 272
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218563680 386 ILNVMGIkEMVIGYGTTENSpVTFCGFPVDSAERKIET-VGCISPHTEAKVVDPTtGEIVPLGAQGELMIRGYCVMLEYW 464
Cdd:cd17646 273 FLALPGA-ELHNLYGPTEAA-IDVTHWPVRGPAETPSVpIGRPVPNTRLYVLDDA-LRPVPVGVPGELYLGGVQLARGYL 349
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218563680 465 QDEEKTRECITKD------RWYKTGDIA------SLDqfaYCkieGRIKDLI-IRGgENIYPAEIEQFLHTHPKILEAQV 531
Cdd:cd17646 350 GRPALTAERFVPDpfgpgsRMYRTGDLArwrpdgALE---FL---GRSDDQVkIRG-FRVEPGEIEAALAAHPAVTHAVV 422
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 218563680 532 VGVKDERMGEEVCACIRLKEGQEC-TVEEIKAYCKGKIAHYKVPRYILFVQDYPLTITGKI 591
Cdd:cd17646 423 VARAAPAGAARLVGYVVPAAGAAGpDTAALRAHLAERLPEYMVPAAFVVLDALPLTANGKL 483
|
|
| A_NRPS_Ta1_like |
cd12116 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including salinosporamide A ... |
80-596 |
6.37e-27 |
|
The adenylation domain of nonribosomal peptide synthetases (NRPS), including salinosporamide A polyketide synthase; The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions. This family includes the myxovirescin (TA) antibiotic biosynthetic gene in Myxococcus xanthus; TA production plays a role in predation. It also includes the salinosporamide A polyketide synthase which is involved in the biosynthesis of salinosporamide A, a marine microbial metabolite whose chlorine atom is crucial for potent proteasome inhibition and anticancer activity.
Pssm-ID: 341281 [Multi-domain] Cd Length: 470 Bit Score: 114.31 E-value: 6.37e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218563680 80 PDREAMVFvqDGIRKTFAEFYQDVEKAAAGLLAAGLKRGDRLGMWGPNIYEWVLMQFATAKAGIILVAVNPAYQLQEVEF 159
Cdd:cd12116 1 PDATAVRD--DDRSLSYAELDERANRLAARLRARGVGPGDRVAVYLPRSARLVAAMLAVLKAGAAYVPLDPDYPADRLRY 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218563680 160 ALRKVQCNAVVCptkfksqhycdmlkqlcpemETASPggiksSRLPDLHTVIVTDSQQPGSfllkdlmqAGSSQHYQQLQ 239
Cdd:cd12116 79 ILEDAEPALVLT--------------------DDALP-----DRLPAGLPVLLLALAAAAA--------APAAPRTPVSP 125
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218563680 240 DlqkklvcdDPINIQFTSGTTGKPKGATLSHHNIVNnaYFTGMRIGYNWRKNVRIcLPVPLYhCFG----------SVGG 309
Cdd:cd12116 126 D--------DLAYVIYTSGSTGRPKGVVVSHRNLVN--FLHSMRERLGLGPGDRL-LAVTTY-AFDisllelllplLAGA 193
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218563680 310 GVIMALYGTTvifpstgYDGRANLRAIEKEKCTFVYGTPTMYIDML--GQPDLAKFDLssvrggIAAGSPCPPEVMRKIL 387
Cdd:cd12116 194 RVVIAPRETQ-------RDPEALARLIEAHSITVMQATPATWRMLLdaGWQGRAGLTA------LCGGEALPPDLAARLL 260
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218563680 388 -------NVmgikemvigYGTTEN---SPVTfcgfPVDSAERKIeTVGCISPHTEAKVVDPTtGEIVPLGAQGELMIRGY 457
Cdd:cd12116 261 srvgslwNL---------YGPTETtiwSTAA----RVTAAAGPI-PIGRPLANTQVYVLDAA-LRPVPPGVPGELYIGGD 325
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218563680 458 CVMLEYWQDEEKTRECITKD-------RWYKTGDIASLDQFAYCKIEGRIKDLI-IRgGENIYPAEIEQFLHTHPKILEA 529
Cdd:cd12116 326 GVAQGYLGRPALTAERFVPDpfagpgsRLYRTGDLVRRRADGRLEYLGRADGQVkIR-GHRIELGEIEAALAAHPGVAQA 404
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 218563680 530 QVVgVKDERMGEEVCACIRLKEGQECTVEEIKAYCKGKIAHYKVPRYILFVQDYPLTITGKIQKHKL 596
Cdd:cd12116 405 AVV-VREDGGDRRLVAYVVLKAGAAPDAAALRAHLRATLPAYMVPSAFVRLDALPLTANGKLDRKAL 470
|
|
| LC-FACS_euk |
cd05927 |
Eukaryotic long-chain fatty acid CoA synthetase (LC-FACS); The members of this family are ... |
118-604 |
8.44e-27 |
|
Eukaryotic long-chain fatty acid CoA synthetase (LC-FACS); The members of this family are eukaryotic fatty acid CoA synthetases that activate fatty acids with chain lengths of 12 to 20. LC-FACS catalyzes the formation of fatty acyl-CoA in a two-step reaction: the formation of a fatty acyl-AMP molecule as an intermediate, and the formation of a fatty acyl-CoA. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions. Organisms tend to have multiple isoforms of LC-FACS genes with multiple splice variants. For example, nine genes are found in Arabidopsis and six genes are expressed in mammalian cells.
Pssm-ID: 341250 [Multi-domain] Cd Length: 545 Bit Score: 114.62 E-value: 8.44e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218563680 118 GDRLGMWGPNIYEWVLMQFATAKAGIILVavnPAYQ---LQEVEFALRKVQCNAVVCPTKFKSqhycdmlkqlcpemeta 194
Cdd:cd05927 32 ASFVGIYSINRPEWIISELACYAYSLVTV---PLYDtlgPEAIEYILNHAEISIVFCDAGVKV----------------- 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218563680 195 spggikssrlpdlhtvivtdsqqpgsFLLKDLMQAGSSQHYQQLQdlqKKLvcDDPINIQFTSGTTGKPKGATLSHHNIV 274
Cdd:cd05927 92 --------------------------YSLEEFEKLGKKNKVPPPP---PKP--EDLATICYTSGTTGNPKGVMLTHGNIV 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218563680 275 NN--AYFTGMRIGYNWRKN-VRICLpVPLYHCFGSVgggVIMALY--GTTVIFpstgYDG--RANLRAIEKEKCTFVYGT 347
Cdd:cd05927 141 SNvaGVFKILEILNKINPTdVYISY-LPLAHIFERV---VEALFLyhGAKIGF----YSGdiRLLLDDIKALKPTVFPGV 212
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218563680 348 PTMY------I--DMLGQPDLAKF-----------DLSS------------------------VRGGIAAGSPCPPEVMR 384
Cdd:cd05927 213 PRVLnriydkIfnKVQAKGPLKRKlfnfalnyklaELRSgvvraspfwdklvfnkikqalggnVRLMLTGSAPLSPEVLE 292
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218563680 385 KILNVMGIkEMVIGYGTTENSPVTFCGFPVDSAerkIETVGCISPHTEAKVVDpttgeiVP-LG-------AQGELMIRG 456
Cdd:cd05927 293 FLRVALGC-PVLEGYGQTECTAGATLTLPGDTS---VGHVGGPLPCAEVKLVD------VPeMNydakdpnPRGEVCIRG 362
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218563680 457 YCVMLEYWQDEEKTRECITKDRWYKTGDIASLDQFAYCKIEGRIKDLI-IRGGENIYPAEIEQFLHTHPKI--------- 526
Cdd:cd05927 363 PNVFSGYYKDPEKTAEALDEDGWLHTGDIGEWLPNGTLKIIDRKKNIFkLSQGEYVAPEKIENIYARSPFVaqifvygds 442
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218563680 527 LEAQVVGV------------KDERMG----EEVCaciRLKEGQECTVEEIKAYCK-GKIAHYKVPRYI-----LF-VQDY 583
Cdd:cd05927 443 LKSFLVAIvvpdpdvlkewaASKGGGtgsfEELC---KNPEVKKAILEDLVRLGKeNGLKGFEQVKAIhlepePFsVENG 519
|
570 580
....*....|....*....|.
gi 218563680 584 PLTITGKIQKHKLRERTEKQL 604
Cdd:cd05927 520 LLTPTFKLKRPQLKKYYKKQI 540
|
|
| A_NRPS_LgrA-like |
cd17645 |
adenylation (A) domain of linear gramicidin synthetase (LgrA) and similar proteins; This ... |
238-596 |
2.58e-26 |
|
adenylation (A) domain of linear gramicidin synthetase (LgrA) and similar proteins; This family of the adenylation (A) domain of nonribosomal peptide synthases (NRPS) includes linear gramicidin synthetase (LgrA) in Brevibacillus brevis. LgrA has a formylation domain fused to the N-terminal end that formylates its substrate for linear gramicidin synthesis to proceed. This formyl group is essential for the clinically important antibacterial activity of gramicidin by enabling head-to-head gramicidin dimers to make a beta-helical pore in gram-positive bacterial membranes, allowing free passage of monovalent cations, destroying the ion gradient and killing bacteria. This family also includes bacitracin synthetase 1 (known as ATP-dependent cysteine adenylase or BA1); it activates cysteine, incorporates two D-amino acids, releases and cyclizes the mature bacitracin, an antibiotic that is a mixture of related cyclic peptides that disrupt gram positive bacteria by interfering with cell wall and peptidoglycan synthesis. Also included is surfactin synthetase which activates and polymerizes the amino acids Leu, Glu, Asp, and Val to form the antibiotic surfactin.
Pssm-ID: 341300 [Multi-domain] Cd Length: 440 Bit Score: 111.88 E-value: 2.58e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218563680 238 LQDLQKKLVCDDPIN---IQFTSGTTGKPKGATLSHHNIVN-----NAYFtGMRIGYNWRKNVRICLPVPLYHCFGSVGG 309
Cdd:cd17645 91 LADSSAKILLTNPDDlayVIYTSGSTGLPKGVMIEHHNLVNlcewhRPYF-GVTPADKSLVYASFSFDASAWEIFPHLTA 169
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218563680 310 GVimALYgttVIFPSTGYDGRANLRAIEKEKCTFVYgTPTMYIDMLGQpdlakFDLSSVRGGIAAGspcppEVMRKIlnV 389
Cdd:cd17645 170 GA--ALH---VVPSERRLDLDALNDYFNQEGITISF-LPTGAAEQFMQ-----LDNQSLRVLLTGG-----DKLKKI--E 231
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218563680 390 MGIKEMVIGYGTTENSpVTFCGFPVDSAERKIeTVGCISPHTEAKVVDPTTgEIVPLGAQGELMIRGYCVMLEYWQDEEK 469
Cdd:cd17645 232 RKGYKLVNNYGPTENT-VVATSFEIDKPYANI-PIGKPIDNTRVYILDEAL-QLQPIGVAGELCIAGEGLARGYLNRPEL 308
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218563680 470 TRE------CITKDRWYKTGDIASLDQFAYCKIEGRIKDLIIRGGENIYPAEIEQFLHTHPKILEAQVVGVKDERMGEEV 543
Cdd:cd17645 309 TAEkfivhpFVPGERMYRTGDLAKFLPDGNIEFLGRLDQQVKIRGYRIEPGEIEPFLMNHPLIELAAVLAKEDADGRKYL 388
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|...
gi 218563680 544 CACIRLKEgqECTVEEIKAYCKGKIAHYKVPRYILFVQDYPLTITGKIQKHKL 596
Cdd:cd17645 389 VAYVTAPE--EIPHEELREWLKNDLPDYMIPTYFVHLKALPLTANGKVDRKAL 439
|
|
| FATP_FACS |
cd05940 |
Fatty acid transport proteins (FATP) play dual roles as fatty acid transporters and its ... |
238-598 |
3.13e-26 |
|
Fatty acid transport proteins (FATP) play dual roles as fatty acid transporters and its activation enzymes; Fatty acid transport protein (FATP) transports long-chain or very-long-chain fatty acids across the plasma membrane. FATPs also have fatty acid CoA synthetase activity, thus playing dual roles as fatty acid transporters and its activation enzymes. At least five copies of FATPs are identified in mammalian cells. This family also includes prokaryotic FATPs. FATPs are the key players in the trafficking of exogenous fatty acids into the cell and in intracellular fatty acid homeostasis.
Pssm-ID: 341263 [Multi-domain] Cd Length: 449 Bit Score: 112.06 E-value: 3.13e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218563680 238 LQDLQKKLVCDDPINIQFTSGTTGKPKGATLSHHNIVNNAYFtGMRIGYNWRKNV-RICLPvpLYHCFGSVGGGVIMALY 316
Cdd:cd05940 71 LNVSSAKHLVVDAALYIYTSGTTGLPKAAIISHRRAWRGGAF-FAGSGGALPSDVlYTCLP--LYHSTALIVGWSACLAS 147
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218563680 317 GTTVIFPSTgYDGRANLRAIEKEKCT-FVY-GTPTMYidMLGQPDLAKFDLSSVRggIAAGSPCPPEVMRKILNVMGIKE 394
Cdd:cd05940 148 GATLVIRKK-FSASNFWDDIRKYQATiFQYiGELCRY--LLNQPPKPTERKHKVR--MIFGNGLRPDIWEEFKERFGVPR 222
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218563680 395 MVIGYGTTENSpvtfCGFPvdSAERKIETVGcISPHTEAKV-------VDPTTGEI----------VPLGAQGELMIR-- 455
Cdd:cd05940 223 IAEFYAATEGN----SGFI--NFFGKPGAIG-RNPSLLRKVaplalvkYDLESGEPirdaegrcikVPRGEPGLLISRin 295
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218563680 456 ------GYCVMLEywQDEEKTRECITK-DRWYKTGDIASLDQFAYCKIEGRIKDLIIRGGENIYPAEIEQFLHTHPKILE 528
Cdd:cd05940 296 plepfdGYTDPAA--TEKKILRDVFKKgDAWFNTGDLMRLDGEGFWYFVDRLGDTFRWKGENVSTTEVAAVLGAFPGVEE 373
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 218563680 529 AQVVGVK----DERMGeevCACIRLKEGQECTVEEIKAYCKGKIAHYKVPRYILFVQDYPLTITGKIQKHKLRE 598
Cdd:cd05940 374 ANVYGVQvpgtDGRAG---MAAIVLQPNEEFDLSALAAHLEKNLPGYARPLFLRLQPEMEITGTFKQQKVDLRN 444
|
|
| PrpE |
cd05967 |
Propionyl-CoA synthetase (PrpE); EC 6.2.1.17: propanoate:CoA ligase (AMP-forming) or ... |
248-597 |
3.29e-26 |
|
Propionyl-CoA synthetase (PrpE); EC 6.2.1.17: propanoate:CoA ligase (AMP-forming) or propionate#CoA ligase (PrpE) catalyzes the first step of the 2-methylcitric acid cycle for propionate catabolism. It activates propionate to propionyl-CoA in a two-step reaction, which proceeds through a propionyl-AMP intermediate and requires ATP and Mg2+. In Salmonella enterica, the PrpE protein is required for growth of Salmonella enterica on propionate and can substitute for the acetyl-CoA synthetase (Acs) enzyme during growth on acetate. PrpE can also activate acetate, 3HP, and butyrate to their corresponding CoA-thioesters, although with less efficiency.
Pssm-ID: 341271 [Multi-domain] Cd Length: 617 Bit Score: 113.56 E-value: 3.29e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218563680 248 DDPINIQFTSGTTGKPKGatlshhnIVNNayfTGmriGY----NWrkNVRICLPVPLYHCF--GS-----VGGGVImaLY 316
Cdd:cd05967 230 TDPLYILYTSGTTGKPKG-------VVRD---NG---GHavalNW--SMRNIYGIKPGDVWwaASdvgwvVGHSYI--VY 292
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218563680 317 G------TTVIF---PSTGYDGRANLRAIEKEKCTFVYGTPTMyIDMLGQPDLA-----KFDLSSVRGGIAAGSPCPPEV 382
Cdd:cd05967 293 GpllhgaTTVLYegkPVGTPDPGAFWRVIEKYQVNALFTAPTA-IRAIRKEDPDgkyikKYDLSSLRTLFLAGERLDPPT 371
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218563680 383 MRKILNVMGiKEMVIGYGTTEN-SPVTFCGFPVDSAERKIETVGCISPHTEAKVVDPTtGEIVPLGAQGELMIRGYC--- 458
Cdd:cd05967 372 LEWAENTLG-VPVIDHWWQTETgWPITANPVGLEPLPIKAGSPGKPVPGYQVQVLDED-GEPVGPNELGNIVIKLPLppg 449
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218563680 459 VMLEYWQDEEKTREC-ITKDR-WYKTGDIASLDQFAYCKIEGRIKDLIIRGGENIYPAEIEQFLHTHPKILEAQVVGVKD 536
Cdd:cd05967 450 CLLTLWKNDERFKKLyLSKFPgYYDTGDAGYKDEDGYLFIMGRTDDVINVAGHRLSTGEMEESVLSHPAVAECAVVGVRD 529
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 218563680 537 ERMGEEVCACIRLKEG----QECTVEEIKAYCKGKIAHYKVPRYILFVQDYPLTITGKIQKHKLR 597
Cdd:cd05967 530 ELKGQVPLGLVVLKEGvkitAEELEKELVALVREQIGPVAAFRLVIFVKRLPKTRSGKILRRTLR 594
|
|
| PRK13388 |
PRK13388 |
acyl-CoA synthetase; Provisional |
127-598 |
6.62e-26 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 237374 [Multi-domain] Cd Length: 540 Bit Score: 112.04 E-value: 6.62e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218563680 127 NIYEWVLMQFATAKAGIILVAVNPAYQLQEVEFALRKVQCNAVVcptkfksqhycdmlkqlcpeMETASPGGIKSSRLPD 206
Cdd:PRK13388 61 NTPEMLFWLAAAALGGYVLVGLNTTRRGAALAADIRRADCQLLV--------------------TDAEHRPLLDGLDLPG 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218563680 207 LhTVIVTDSQQpgsflLKDLMQAGSSQHYQqlqdlqKKLVCDDPINIQFTSGTTGKPKGATLSHHNIVNNAYFTGMRIGY 286
Cdd:PRK13388 121 V-RVLDVDTPA-----YAELVAAAGALTPH------REVDAMDPFMLIFTSGTTGAPKAVRCSHGRLAFAGRALTERFGL 188
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218563680 287 NwRKNVRIClPVPLYHcfgsvgGGVIMALY------GTTVIFPSTgYDGRANLRAIEKEKCTFV-Y-GTPTMYIdmLGQP 358
Cdd:PRK13388 189 T-RDDVCYV-SMPLFH------SNAVMAGWapavasGAAVALPAK-FSASGFLDDVRRYGATYFnYvGKPLAYI--LATP 257
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218563680 359 DLAKFDLSSVRggIAAGSPCPPEVMRKILNVMGIkEMVIGYGTTEN--SPVTFCGFPVDSAERKIETVGCISPHT----E 432
Cdd:PRK13388 258 ERPDDADNPLR--VAFGNEASPRDIAEFSRRFGC-QVEDGYGSSEGavIVVREPGTPPGSIGRGAPGVAIYNPETltecA 334
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218563680 433 AKVVDPTTGEIVPLGAQGELMIRGYCVMLE-YWQDEEKTRECItKDRWYKTGDIASLDQFAYCKIEGRIKDLIIRGGENI 511
Cdd:PRK13388 335 VARFDAHGALLNADEAIGELVNTAGAGFFEgYYNNPEATAERM-RHGMYWSGDLAYRDADGWIYFAGRTADWMRVDGENL 413
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218563680 512 YPAEIEQFLHTHPKILEAQVVGVKDERMGEEVCACIRLKEGQECTVEEIKAYCKG------KIAhykvPRYILFVQDYPL 585
Cdd:PRK13388 414 SAAPIERILLRHPAINRVAVYAVPDERVGDQVMAALVLRDGATFDPDAFAAFLAAqpdlgtKAW----PRYVRIAADLPS 489
|
490
....*....|...
gi 218563680 586 TITGKIQKHKLRE 598
Cdd:PRK13388 490 TATNKVLKRELIA 502
|
|
| A_NRPS_SidN3_like |
cd05918 |
The adenylation (A) domain of siderophore-synthesizing nonribosomal peptide synthetases (NRPS); ... |
238-598 |
7.36e-26 |
|
The adenylation (A) domain of siderophore-synthesizing nonribosomal peptide synthetases (NRPS); The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. This family of siderophore-synthesizing NRPS includes the third adenylation domain of SidN from the endophytic fungus Neotyphodium lolii, ferrichrome siderophore synthetase, HC-toxin synthetase, and enniatin synthase. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.
Pssm-ID: 341242 [Multi-domain] Cd Length: 481 Bit Score: 111.10 E-value: 7.36e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218563680 238 LQDLQKKLV-CDDPIN---IQFTSGTTGKPKGATLSHHNIVNNAYFTGMRIGYNwrKNVRI------CLPVPLYHCFG-- 305
Cdd:cd05918 92 LQDTGAKVVlTSSPSDaayVIFTSGSTGKPKGVVIEHRALSTSALAHGRALGLT--SESRVlqfasyTFDVSILEIFTtl 169
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218563680 306 SVGGgvimalygtTVIFPSTgYDGRANL-RAIEKEKCTFVYGTPTMyIDMLgQPDlakfDLSSVRGGIAAGSPCPPEVMR 384
Cdd:cd05918 170 AAGG---------CLCIPSE-EDRLNDLaGFINRLRVTWAFLTPSV-ARLL-DPE----DVPSLRTLVLGGEALTQSDVD 233
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218563680 385 K-ILNVmgikEMVIGYGTTENSPVTFCGFPVDSAERKI--ETVGCIsphteAKVVDP-TTGEIVPLGAQGELMIRGYCVM 460
Cdd:cd05918 234 TwADRV----RLINAYGPAECTIAATVSPVVPSTDPRNigRPLGAT-----CWVVDPdNHDRLVPIGAVGELLIEGPILA 304
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218563680 461 LEYWQDEEKTREC-ITKDRW------------YKTGDIASLDQ---FAYCkieGRIKDLI-IRGgENIYPAEIEQFLHTH 523
Cdd:cd05918 305 RGYLNDPEKTAAAfIEDPAWlkqegsgrgrrlYRTGDLVRYNPdgsLEYV---GRKDTQVkIRG-QRVELGEIEHHLRQS 380
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218563680 524 P---KILEAQVVGVKDERMGEEVCACIRLKEGQECT-----------------VEEIKAYCKGKIAHYKVPRYILFVQDY 583
Cdd:cd05918 381 LpgaKEVVVEVVKPKDGSSSPQLVAFVVLDGSSSGSgdgdslflepsdefralVAELRSKLRQRLPSYMVPSVFLPLSHL 460
|
410
....*....|....*
gi 218563680 584 PLTITGKIQKHKLRE 598
Cdd:cd05918 461 PLTASGKIDRRALRE 475
|
|
| A_NRPS_ACVS-like |
cd17648 |
N-(5-amino-5-carboxypentanoyl)-L-cysteinyl-D-valine synthase; This family contains ACV ... |
238-596 |
1.67e-25 |
|
N-(5-amino-5-carboxypentanoyl)-L-cysteinyl-D-valine synthase; This family contains ACV synthetase (ACVS, EC 6.3.2.26; also known as N-(5-amino-5-carboxypentanoyl)-L-cysteinyl-D-valine synthase or delta-(L-alpha-aminoadipyl)-L-cysteinyl-D-valine synthetase) is involved in medically important antibiotic biosynthesis. ACV synthetase is active in an early step in the penicillin G biosynthesis pathway which involves the formation of the tripeptide 6-(L-alpha-aminoadipyl)-L-cysteinyl-D-valine (ACV); each of the constituent amino acids of the tripeptide ACV are activated as aminoacyl-adenylates with peptide bonds formed through the participation of amino acid thioester intermediates. ACV is then cyclized by the action of isopenicillin N synthase.
Pssm-ID: 341303 [Multi-domain] Cd Length: 453 Bit Score: 109.80 E-value: 1.67e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218563680 238 LQDLQKKLVCDDPIN---IQFTSGTTGKPKGATLSHHNIVNnaYFTGMRIGYNWRKN-VRICLPVPLYHCFGSVGGGVIM 313
Cdd:cd17648 81 LEDTGARVVITNSTDlayAIYTSGTTGKPKGVLVEHGSVVN--LRTSLSERYFGRDNgDEAVLFFSNYVFDFFVEQMTLA 158
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218563680 314 ALYGTTVIFP--STGYDGRANLRAIEKEKCTFVYGTPTMyidmLGQPDLAKfdLSSVRGGIAAGSPCPPEVMRKILNvmG 391
Cdd:cd17648 159 LLNGQKLVVPpdEMRFDPDRFYAYINREKVTYLSGTPSV----LQQYDLAR--LPHLKRVDAAGEEFTAPVFEKLRS--R 230
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218563680 392 IKEMVI-GYGTTENSpVTFCGFPVDSAERKIETVGCISPHTEAKVVDPTTgEIVPLGAQGELMIRGYCVMLEYWQDEEKT 470
Cdd:cd17648 231 FAGLIInAYGPTETT-VTNHKRFFPGDQRFDKSLGRPVRNTKCYVLNDAM-KRVPVGAVGELYLGGDGVARGYLNRPELT 308
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218563680 471 RECI--------------TKDRWYKTGDIASLDQFAYCKIEGRiKDLIIR-GGENIYPAEIEQFLHTHPKILEAQVVGVK 535
Cdd:cd17648 309 AERFlpnpfqteqerargRNARLYKTGDLVRWLPSGELEYLGR-NDFQVKiRGQRIEPGEVEAALASYPGVRECAVVAKE 387
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 218563680 536 DERMGEEVCA----CIRLKEGQECTVEEIKAYCKGKIAHYKVPRYILFVQDYPLTITGKIQKHKL 596
Cdd:cd17648 388 DASQAQSRIQkylvGYYLPEPGHVPESDLLSFLRAKLPRYMVPARLVRLEGIPVTINGKLDVRAL 452
|
|
| A_NRPS_VisG_like |
cd17651 |
similar to adenylation domain of virginiamycin S synthetase; This family of the adenylation (A) ... |
76-597 |
2.47e-25 |
|
similar to adenylation domain of virginiamycin S synthetase; This family of the adenylation (A) domain of nonribosomal peptide synthases (NRPS) includes virginiamycin S synthetase (VisG) in Streptomyces virginiae; VisG is involved in virginiamycin S (VS) biosynthesis as the provider of an L-pheGly molecule, a highly specific substrate for the last condensation step by VisF. This family also includes linear gramicidin synthetase B (LgrB) in Brevibacillus brevis. Substrate specificity analysis using residues of the substrate-binding pockets of all 16 adenylation domains has shown good agreement of the substrate amino acids predicted with the sequence of linear gramicidin. The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester bond to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.
Pssm-ID: 341306 [Multi-domain] Cd Length: 491 Bit Score: 109.74 E-value: 2.47e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218563680 76 VERYPDREAMVFvqDGIRKTFAEFYQDVEKAAAGLLAAGLKRGDRLGMWGPNIYEWVLMQFATAKAGIILVAVNPAYQLQ 155
Cdd:cd17651 5 AARTPDAPALVA--EGRRLTYAELDRRANRLAHRLRARGVGPGDLVALCARRSAELVVALLAILKAGAAYVPLDPAYPAE 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218563680 156 EVEFALRKVQCNAVVcptkfksqhycdmlkqLCPEMETASPggikssrlPDLHTVIVTDSQQpgsfllkdLMQAGSSQHY 235
Cdd:cd17651 83 RLAFMLADAGPVLVL----------------THPALAGELA--------VELVAVTLLDQPG--------AAAGADAEPD 130
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218563680 236 QQLQdlqkklvCDDPINIQFTSGTTGKPKGATLSHHNIVN-----NAYF---TGMR------IGYNwrknvriclpVPLY 301
Cdd:cd17651 131 PALD-------ADDLAYVIYTSGSTGRPKGVVMPHRSLANlvawqARASslgPGARtlqfagLGFD----------VSVQ 193
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218563680 302 HCFGSVGGGvimalyGTTVIFP-STGYDGRANLRAIEKEKCTFVYgTPTMYIDMLGQ-PDLAKFDLSSVRGGIAAGSPCP 379
Cdd:cd17651 194 EIFSTLCAG------ATLVLPPeEVRTDPPALAAWLDEQRISRVF-LPTVALRALAEhGRPLGVRLAALRYLLTGGEQLV 266
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218563680 380 P-EVMRKILNVMGIKEMVIGYGTTENSPVTFCGFPVDSAER-KIETVGCISPHTEAKVVDPTtGEIVPLGAQGELMIRGY 457
Cdd:cd17651 267 LtEDLREFCAGLPGLRLHNHYGPTETHVVTALSLPGDPAAWpAPPPIGRPIDNTRVYVLDAA-LRPVPPGVPGELYIGGA 345
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218563680 458 CVMLEYWQDEEKTRECITKD------RWYKTGDIASLD-----QFAyckieGRIKDLI-IRGgENIYPAEIEQFLHTHPK 525
Cdd:cd17651 346 GLARGYLNRPELTAERFVPDpfvpgaRMYRTGDLARWLpdgelEFL-----GRADDQVkIRG-FRIELGEIEAALARHPG 419
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 218563680 526 ILEAQVVGVKDERMGEEVCACIRLKEGQECTVEEIKAYCKGKIAHYKVPRYILFVQDYPLTITGKIQKHKLR 597
Cdd:cd17651 420 VREAVVLAREDRPGEKRLVAYVVGDPEAPVDAAELRAALATHLPEYMVPSAFVLLDALPLTPNGKLDRRALP 491
|
|
| LC_FACS_bac |
cd05932 |
Bacterial long-chain fatty acid CoA synthetase (LC-FACS), including Marinobacter ... |
118-533 |
3.16e-25 |
|
Bacterial long-chain fatty acid CoA synthetase (LC-FACS), including Marinobacter hydrocarbonoclasticus isoprenoid Coenzyme A synthetase; The members of this family are bacterial long-chain fatty acid CoA synthetase. Marinobacter hydrocarbonoclasticus isoprenoid Coenzyme A synthetase in this family is involved in the synthesis of isoprenoid wax ester storage compounds when grown on phytol as the sole carbon source. LC-FACS catalyzes the formation of fatty acyl-CoA in a two-step reaction: the formation of a fatty acyl-AMP molecule as an intermediate, and the formation of a fatty acyl-CoA. Free fatty acids must be "activated" to their CoA thioesters before participating in most catabolic and anabolic reactions.
Pssm-ID: 341255 [Multi-domain] Cd Length: 508 Bit Score: 109.48 E-value: 3.16e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218563680 118 GDRLGMWGPNIYEWVLMQFATAKAGIILVAVNPAYQLQEVEFALRKVQCNAVVCPtkfKSQHYcdmlkqlcPEMETASPG 197
Cdd:cd05932 31 GSKIALISKNCAEWFITDLAIWMAGHISVPLYPTLNPDTIRYVLEHSESKALFVG---KLDDW--------KAMAPGVPE 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218563680 198 GIKSSRLPDLHTvivtdsqqpgsflLKDlmQAGSSQHYQQLQDLQKKLVCDDP--INIQFTSGTTGKPKGATLSHHNIVN 275
Cdd:cd05932 100 GLISISLPPPSA-------------ANC--QYQWDDLIAQHPPLEERPTRFPEqlATLIYTSGTTGQPKGVMLTFGSFAW 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218563680 276 NAYFTGMRIGYNwrKNVRICLPVPLYHCF-------GSVGGGVIMALYGTTVIFPSTgydgranlraIEKEKCTFVYGTP 348
Cdd:cd05932 165 AAQAGIEHIGTE--ENDRMLSYLPLAHVTervfvegGSLYGGVLVAFAESLDTFVED----------VQRARPTLFFSVP 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218563680 349 TMY-------IDMLGQpdlAKFDL--------SSVRGGIAAG-------------SPCPPEVM---RKI-LNVMGikemv 396
Cdd:cd05932 233 RLWtkfqqgvQDKIPQ---QKLNLllkipvvnSLVKRKVLKGlgldqcrlagcgsAPVPPALLewyRSLgLNILE----- 304
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218563680 397 iGYGTTENSPVTFCGFPVDsaeRKIETVGCISPHTEAKVVDpttgeivplgaQGELMIRGYCVMLEYWQDEEKTRECITK 476
Cdd:cd05932 305 -AYGMTENFAYSHLNYPGR---DKIGTVGNAGPGVEVRISE-----------DGEILVRSPALMMGYYKDPEATAEAFTA 369
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*...
gi 218563680 477 DRWYKTGDIASLDQFAYCKIEGRIKDLI-IRGGENIYPAEIEQFLHTHPKILEAQVVG 533
Cdd:cd05932 370 DGFLRTGDKGELDADGNLTITGRVKDIFkTSKGKYVAPAPIENKLAEHDRVEMVCVIG 427
|
|
| A_NRPS_MycA_like |
cd05908 |
The adenylation domain of nonribosomal peptide synthetases (NRPS) similar to mycosubtilin ... |
253-601 |
4.85e-25 |
|
The adenylation domain of nonribosomal peptide synthetases (NRPS) similar to mycosubtilin synthase subunit A (MycA); The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as (amino)-acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms thioester to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. This family includes NRPS similar to mycosubtilin synthase subunit A (MycA). Mycosubtilin, which is characterized by a beta-amino fatty acid moiety linked to the circular heptapeptide Asn-Tyr-Asn-Gln-Pro-Ser-Asn, belongs to the iturin family of lipopeptide antibiotics. The mycosubtilin synthase subunit A (MycA) combines functional domains derived from peptide synthetases, amino transferases, and fatty acid synthases. Nonribosomal peptide synthetases are large multifunction enzymes that synthesize many therapeutically useful peptides. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and, in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.
Pssm-ID: 341234 [Multi-domain] Cd Length: 499 Bit Score: 109.11 E-value: 4.85e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218563680 253 IQFTSGTTGKPKGATLSHHNIVNNAYftGMRIGYNWRKNVRICLPVPLYHCFGSVGGGVIMALYGTT-VIFPSTGYDGRA 331
Cdd:cd05908 111 IQFSSGSTGDPKGVMLTHENLVHNMF--AILNSTEWKTKDRILSWMPLTHDMGLIAFHLAPLIAGMNqYLMPTRLFIRRP 188
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218563680 332 N--LRAIEKEKCTFVyGTPT----MYIDMLGQPDLAKFDLSSVRGGIAAGSPCPPEVMRKILNVM---GIKE--MVIGYG 400
Cdd:cd05908 189 IlwLKKASEHKATIV-SSPNfgykYFLKTLKPEKANDWDLSSIRMILNGAEPIDYELCHEFLDHMskyGLKRnaILPVYG 267
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218563680 401 TTENSpVTFCGFPVDS--------------AERKIET------------VGCISPHTEAKVVDpTTGEIVPLGAQGELMI 454
Cdd:cd05908 268 LAEAS-VGASLPKAQSpfktitlgrrhvthGEPEPEVdkkdsecltfveVGKPIDETDIRICD-EDNKILPDGYIGHIQI 345
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218563680 455 RGYCVMLEYWQDEEKTRECITKDRWYKTGDIASL-DQFAYckIEGRIKDLIIRGGENIYPAEIEQFLHTHPKILEAQVV- 532
Cdd:cd05908 346 RGKNVTPGYYNNPEATAKVFTDDGWLKTGDLGFIrNGRLV--ITGREKDIIFVNGQNVYPHDIERIAEELEGVELGRVVa 423
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 218563680 533 -GVKDERMGEEVCACIRLKEGqecTVEEIKAYCKG--KIAHYKVPRYI---LFVQDYPLTITGKIQKHKLRERTE 601
Cdd:cd05908 424 cGVNNSNTRNEEIFCFIEHRK---SEDDFYPLGKKikKHLNKRGGWQInevLPIRRIPKTTSGKVKRYELAQRYQ 495
|
|
| FATP_chFAT1_like |
cd05937 |
Uncharacterized subfamily of bifunctional fatty acid transporter/very-long-chain acyl-CoA ... |
248-598 |
2.20e-24 |
|
Uncharacterized subfamily of bifunctional fatty acid transporter/very-long-chain acyl-CoA synthetase in fungi; Fatty acid transport protein (FATP) transports long-chain or very-long-chain fatty acids across the plasma membrane. FATPs also have fatty acid CoA synthetase activity, thus playing dual roles as fatty acid transporters and its activation enzymes. FATPs are the key players in the trafficking of exogenous fatty acids into the cell and in intracellular fatty acid homeostasis. Members of this family are fungal FATPs, including FAT1 from Cochliobolus heterostrophus.
Pssm-ID: 341260 [Multi-domain] Cd Length: 468 Bit Score: 106.75 E-value: 2.20e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218563680 248 DDPINIQFTSGTTGKPKGATLShhniVNNAYFTGMRIG--YNWRKNVRICLPVPLYHCFGSVGGGVIMALYGTTVI---- 321
Cdd:cd05937 87 DDPAILIYTSGTTGLPKAAAIS----WRRTLVTSNLLShdLNLKNGDRTYTCMPLYHGTAAFLGACNCLMSGGTLAlsrk 162
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218563680 322 -----FPSTGYDGRANLRAIEKEKCTFVYGTPTmyidmlgQPDLAKfdlSSVRggIAAGSPCPPEV---MRKILNVMGIK 393
Cdd:cd05937 163 fsasqFWKDVRDSGATIIQYVGELCRYLLSTPP-------SPYDRD---HKVR--VAWGNGLRPDIwerFRERFNVPEIG 230
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218563680 394 EMvigYGTTENSPVTF-----------CGFPVDSAERKIE---TVGCISPHTEAKVVDPTTG--EIVPLGAQGELMIRGY 457
Cdd:cd05937 231 EF---YAATEGVFALTnhnvgdfgagaIGHHGLIRRWKFEnqvVLVKMDPETDDPIRDPKTGfcVRAPVGEPGEMLGRVP 307
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218563680 458 CVMLE----YWQDEEKT-----RECITK-DRWYKTGDIASLDQFAYCKIEGRIKDLIIRGGENIYPAEIEQFLHTHPKIL 527
Cdd:cd05937 308 FKNREafqgYLHNEDATesklvRDVFRKgDIYFRTGDLLRQDADGRWYFLDRLGDTFRWKSENVSTTEVADVLGAHPDIA 387
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 218563680 528 EAQVVGVK----DERMGeevCACIRLKEGQECTVEEIKA----YCKGKIAHYKVPRYILFVQDYPLTITGKIQKHKLRE 598
Cdd:cd05937 388 EANVYGVKvpghDGRAG---CAAITLEESSAVPTEFTKSllasLARKNLPSYAVPLFLRLTEEVATTDNHKQQKGVLRD 463
|
|
| A_NRPS_PvdJ-like |
cd17649 |
non-ribosomal peptide synthetase; This family of the adenylation (A) domain of nonribosomal ... |
255-597 |
3.46e-24 |
|
non-ribosomal peptide synthetase; This family of the adenylation (A) domain of nonribosomal peptide synthases (NRPS) includes pyoverdine biosynthesis protein PvdJ involved in the synthesis of pyoverdine, which consists of a chromophore group attached to a variable peptide chain and comprises around 6-12 amino acids that are specific for each Pseudomonas species, and for which the peptide might be first synthesized before the chromophore assembly. Also included is ornibactin biosynthesis protein OrbI; ornibactin is a tetrapeptide siderophore with an l-ornithine-d-hydroxyaspartate-l-serine-l-ornithine backbone. The adenylation domain at the N-terminal of OrbI possibly initiates the ornibactin with the binding of N5-hydroxyornithine. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.
Pssm-ID: 341304 [Multi-domain] Cd Length: 450 Bit Score: 105.91 E-value: 3.46e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218563680 255 FTSGTTGKPKGATLSHHNIVNNAYFTGMRigYNWRKNVRIcLPvplyhcFGSVG--GGV--IMA--LYGTTVIFPSTG-- 326
Cdd:cd17649 101 YTSGSTGTPKGVAVSHGPLAAHCQATAER--YGLTPGDRE-LQ------FASFNfdGAHeqLLPplICGACVVLRPDElw 171
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218563680 327 YDGRANLRAIEKEKCTfVYGTPTMYIDMLGQPDLAKFDLS--SVRGGIAAGSPCPPEVMRKILnvMGIKEMVIGYGTTEN 404
Cdd:cd17649 172 ASADELAEMVRELGVT-VLDLPPAYLQQLAEEADRTGDGRppSLRLYIFGGEALSPELLRRWL--KAPVRLFNAYGPTEA 248
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218563680 405 SpVTFCGFPVDSAERKIET---VGCISPHTEAKVVDPTTGEiVPLGAQGELMIRGYCVMLEYWQDEEKTRECITKD---- 477
Cdd:cd17649 249 T-VTPLVWKCEAGAARAGAsmpIGRPLGGRSAYILDADLNP-VPVGVTGELYIGGEGLARGYLGRPELTAERFVPDpfga 326
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218563680 478 ---RWYKTGDIASL---DQFAYCkieGRIKDLIIRGGENIYPAEIEQFLHTHPKILEAQVVGVkDERMGEEVCACIRLKE 551
Cdd:cd17649 327 pgsRLYRTGDLARWrddGVIEYL---GRVDHQVKIRGFRIELGEIEAALLEHPGVREAAVVAL-DGAGGKQLVAYVVLRA 402
|
330 340 350 360
....*....|....*....|....*....|....*....|....*...
gi 218563680 552 G--QECTVEEIKAYCKGKIAHYKVPRYILFVQDYPLTITGKIQKHKLR 597
Cdd:cd17649 403 AaaQPELRAQLRTALRASLPDYMVPAHLVFLARLPLTPNGKLDRKALP 450
|
|
| LC_FACS_euk1 |
cd17639 |
Eukaryotic long-chain fatty acid CoA synthetase (LC-FACS), including fungal proteins; The ... |
247-524 |
5.30e-24 |
|
Eukaryotic long-chain fatty acid CoA synthetase (LC-FACS), including fungal proteins; The members of this family are eukaryotic fatty acid CoA synthetases (EC 6.2.1.3) that activate fatty acids with chain lengths of 12 to 20 and includes fungal proteins. They act on a wide range of long-chain saturated and unsaturated fatty acids, but the enzymes from different tissues show some variation in specificity. LC-FACS catalyzes the formation of fatty acyl-CoA in a two-step reaction: the formation of a fatty acyl-AMP molecule as an intermediate, and the formation of a fatty acyl-CoA. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions. Organisms tend to have multiple isoforms of LC-FACS genes with multiple splice variants. For example, nine genes are found in Arabidopsis and six genes are expressed in mammalian cells. In Schizosaccharomyces pombe, lcf1 gene encodes a new fatty acyl-CoA synthetase that preferentially recognizes myristic acid as a substrate.
Pssm-ID: 341294 [Multi-domain] Cd Length: 507 Bit Score: 105.76 E-value: 5.30e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218563680 247 CDDPINIQFTSGTTGKPKGATLSHHNIVnnAYFTGM--RIGYNWRKNVRICLPVPLYHCF------------GSVGGGVI 312
Cdd:cd17639 87 PDDLACIMYTSGSTGNPKGVMLTHGNLV--AGIAGLgdRVPELLGPDDRYLAYLPLAHIFelaaenvclyrgGTIGYGSP 164
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218563680 313 MALYGTTV------------------------------------------IFpSTGYDGRanLRAIEKEKCTF-----VY 345
Cdd:cd17639 165 RTLTDKSKrgckgdltefkptlmvgvpaiwdtirkgvlaklnpmgglkrtLF-WTAYQSK--LKALKEGPGTPlldelVF 241
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218563680 346 GTPTMyidMLGqpdlakfdlSSVRGGIAAGSPCPPEVMRkILNVMgIKEMVIGYGTTEnspvTFCGFPV-DSAERKIETV 424
Cdd:cd17639 242 KKVRA---ALG---------GRLRYMLSGGAPLSADTQE-FLNIV-LCPVIQGYGLTE----TCAGGTVqDPGDLETGRV 303
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218563680 425 GCISPHTEAKVVD-------PTTGEivPlgaQGELMIRGYCVMLEYWQDEEKTRECITKDRWYKTGDIASLDQFAYCKIE 497
Cdd:cd17639 304 GPPLPCCEIKLVDweeggysTDKPP--P---RGEILIRGPNVFKGYYKNPEKTKEAFDGDGWFHTGDIGEFHPDGTLKII 378
|
330 340
....*....|....*....|....*...
gi 218563680 498 GRIKDLI-IRGGENIYPAEIEQFLHTHP 524
Cdd:cd17639 379 DRKKDLVkLQNGEYIALEKLESIYRSNP 406
|
|
| A_NRPS_ApnA-like |
cd17644 |
similar to adenylation domain of anabaenopeptin synthetase (ApnA); This family of the ... |
238-596 |
6.91e-24 |
|
similar to adenylation domain of anabaenopeptin synthetase (ApnA); This family of the adenylation (A) domain of nonribosomal peptide synthases (NRPS) includes Planktothrix agardhii anabaenopeptin synthetase (ApnA A1), which is capable of activating two chemically distinct amino acids (Arg and Tyr). Structural studies show that the architecture of the active site forces Arg to adopt a Tyr-like conformation, thus explaining the bispecificity. The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester bond to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.
Pssm-ID: 341299 [Multi-domain] Cd Length: 465 Bit Score: 105.21 E-value: 6.91e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218563680 238 LQDLQKKLVCDDPIN---IQFTSGTTGKPKGATLSHHNIVNNAYftGMRIGYNWRKNVRICLPVPLyhCFGSVGGGVIMA 314
Cdd:cd17644 93 LEDAQISVLLTQPENlayVIYTSGSTGKPKGVMIEHQSLVNLSH--GLIKEYGITSSDRVLQFASI--AFDVAAEEIYVT 168
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218563680 315 LY--GTTVIFPSTGY-DGRANLRAIEKEKCTfVYGTPTMYIDML---GQPDLAKFDlSSVRGGIAAGSPCPPEVMRKILN 388
Cdd:cd17644 169 LLsgATLVLRPEEMRsSLEDFVQYIQQWQLT-VLSLPPAYWHLLvleLLLSTIDLP-SSLRLVIVGGEAVQPELVRQWQK 246
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218563680 389 VMGIK-EMVIGYGTTENSPVTFCGFPVDSAERKIE--TVGCISPHTEAKVVDPTTgEIVPLGAQGELMIRGYCVMLEYWQ 465
Cdd:cd17644 247 NVGNFiQLINVYGPTEATIAATVCRLTQLTERNITsvPIGRPIANTQVYILDENL-QPVPVGVPGELHIGGVGLARGYLN 325
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218563680 466 DEEKTRECITKD--------RWYKTGDIASLdqFAYCKIE--GRIKDLI-IRGGEnIYPAEIEQFLHTHPKILEAQVVGV 534
Cdd:cd17644 326 RPELTAEKFISHpfnsseseRLYKTGDLARY--LPDGNIEylGRIDNQVkIRGFR-IELGEIEAVLSQHNDVKTAVVIVR 402
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 218563680 535 KDERMGEEVCACIRLKEGQECTVEEIKAYCKGKIAHYKVPRYILFVQDYPLTITGKIQKHKL 596
Cdd:cd17644 403 EDQPGNKRLVAYIVPHYEESPSTVELRQFLKAKLPDYMIPSAFVVLEELPLTPNGKIDRRAL 464
|
|
| A_NRPS_Cytc1-like |
cd17643 |
similar to adenylation domain of cytotrienin synthetase CytC1; This family of the adenylation ... |
238-596 |
7.04e-24 |
|
similar to adenylation domain of cytotrienin synthetase CytC1; This family of the adenylation (A) domain of nonribosomal peptide synthases (NRPS) includes Streptomyces sp. cytotrienin synthetase (CytC1), a relatively promiscuous adenylation enzyme that installs the aminoacyl moieties on the phosphopantetheinyl arm of the holo carrier protein CytC2. Also included are Streptomyces sp Thr1, involved in the biosynthesis of 4-chlorothreonine, Pseudomonas aeruginosa pyoverdine synthetase D (PvdD), involved in the biosynthesis of the siderophore pyoverdine and Pseudomonas syringae syringopeptin synthetase, where syringpeptin is a necrosis-inducing phytotoxin that functions as a virulence determinant in the plant-pathogen interaction. The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester bond to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.
Pssm-ID: 341298 [Multi-domain] Cd Length: 450 Bit Score: 104.70 E-value: 7.04e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218563680 238 LQDLQKKLVCDDPIN---IQFTSGTTGKPKGATLSHHNIVnnAYFTGMRIGYNW-RKNVriclpVPLYHCFG---SVGG- 309
Cdd:cd17643 80 LADSGPSLLLTDPDDlayVIYTSGSTGRPKGVVVSHANVL--ALFAATQRWFGFnEDDV-----WTLFHSYAfdfSVWEi 152
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218563680 310 -GVImaLYGTTVIFPS--TGYDGRANLRAIEKEKCTFVYGTPTMYIDMLGQPDLAKFDLSSVRGGIAAGSPCPPEVMRKI 386
Cdd:cd17643 153 wGAL--LHGGRLVVVPyeVARSPEDFARLLRDEGVTVLNQTPSAFYQLVEAADRDGRDPLALRYVIFGGEALEAAMLRPW 230
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218563680 387 LNVMGIK--EMVIGYGTTENSP-VTFCGF-PVDSAERKIETVGCISPHTEAKVVDpTTGEIVPLGAQGELMIRGYCVMLE 462
Cdd:cd17643 231 AGRFGLDrpQLVNMYGITETTVhVTFRPLdAADLPAAAASPIGRPLPGLRVYVLD-ADGRPVPPGVVGELYVSGAGVARG 309
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218563680 463 YWQDEEKTRECITKD-------RWYKTGDIASL---DQFAYckiEGRIKDLI-IRGgENIYPAEIEQFLHTHPKILEAQV 531
Cdd:cd17643 310 YLGRPELTAERFVANpfggpgsRMYRTGDLARRlpdGELEY---LGRADEQVkIRG-FRIELGEIEAALATHPSVRDAAV 385
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 218563680 532 VGVKDERMGEEVCACIRLKEGQECTVEEIKAYCKGKIAHYKVPRYILFVQDYPLTITGKIQKHKL 596
Cdd:cd17643 386 IVREDEPGDTRLVAYVVADDGAAADIAELRALLKELLPDYMVPARYVPLDALPLTVNGKLDRAAL 450
|
|
| PRK09274 |
PRK09274 |
peptide synthase; Provisional |
78-556 |
7.33e-24 |
|
peptide synthase; Provisional
Pssm-ID: 236443 [Multi-domain] Cd Length: 552 Bit Score: 105.75 E-value: 7.33e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218563680 78 RYPDREAmVFVQDGIRK---------TFAEFYQDVEKAAAGLLAAGLKRGDR-LGMWGPNIyEWVLMQFATAKAGIILVA 147
Cdd:PRK09274 18 ERPDQLA-VAVPGGRGAdgklaydelSFAELDARSDAIAHGLNAAGIGRGMRaVLMVTPSL-EFFALTFALFKAGAVPVL 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218563680 148 VNPAYQLQevefalRKVQCNAVVCPTKFKSQHYCDMLKQLCPemetaspGGIKSSRlpdlHTVIVTDSQQPGSFLLKDLM 227
Cdd:PRK09274 96 VDPGMGIK------NLKQCLAEAQPDAFIGIPKAHLARRLFG-------WGKPSVR----RLVTVGGRLLWGGTTLATLL 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218563680 228 QAGSSQHYQqLQDLQkklvCDDPINIQFTSGTTGKPKGATLSHHNIVnnAYFTGMRIGYNWRKNvRICLPV-PLYHCFGs 306
Cdd:PRK09274 159 RDGAAAPFP-MADLA----PDDMAAILFTSGSTGTPKGVVYTHGMFE--AQIEALREDYGIEPG-EIDLPTfPLFALFG- 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218563680 307 vgggviMALYGTTVI------FPSTgYDGRANLRAIEKEKCTFVYGTPTmYIDMLGQPDLAK-FDLSSVRGGIAAGSPCP 379
Cdd:PRK09274 230 ------PALGMTSVIpdmdptRPAT-VDPAKLFAAIERYGVTNLFGSPA-LLERLGRYGEANgIKLPSLRRVISAGAPVP 301
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218563680 380 PEVMRKILNVMG-IKEMVIGYGTTENSPVTFcgfpVDSAERKIET-----------VGCISPHTEAKVVDPTTGEI---- 443
Cdd:PRK09274 302 IAVIERFRAMLPpDAEILTPYGATEALPISS----IESREILFATraatdngagicVGRPVDGVEVRIIAISDAPIpewd 377
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218563680 444 ----VPLGAQGELMIRGYCVMLEYWQDEEKTRECITKDR----WYKTGDIASLD---QFAYCkieGRIKDLIIRGGENIY 512
Cdd:PRK09274 378 dalrLATGEIGEIVVAGPMVTRSYYNRPEATRLAKIPDGqgdvWHRMGDLGYLDaqgRLWFC---GRKAHRVETAGGTLY 454
|
490 500 510 520
....*....|....*....|....*....|....*....|....*
gi 218563680 513 PAEIEQFLHTHPKILEAQVVGVKdeRMGEEVCA-CIRLKEGQECT 556
Cdd:PRK09274 455 TIPCERIFNTHPGVKRSALVGVG--VPGAQRPVlCVELEPGVACS 497
|
|
| A_NRPS_PpsD_like |
cd17650 |
similar to adenylation domain of plipastatin synthase (PpsD); This family of the adenylation ... |
248-596 |
1.02e-23 |
|
similar to adenylation domain of plipastatin synthase (PpsD); This family of the adenylation (A) domain of nonribosomal peptide synthases (NRPS) includes bacitracin synthetase 1 (BacA) in Bacillus licheniformis, tyrocidine synthetase in Brevibacillus brevis, plipastatin synthase (PpsD, an important antifungal protein) in Bacillus subtilis and mannopeptimycin peptide synthetase (MppB) in Streptomyces hygroscopicus. Plipastatin has strong fungitoxic activity and is involved in inhibition of phospholipase A2 and biofilm formation. Bacitracin, a mixture of related cyclic peptides, is used as a polypeptide antibiotic while function of tyrocidine is thought to be regulation of sporulation. MppB is involved in biosynthetic pathway of mannopeptimycin, a novel class of mannosylated lipoglycopeptides. The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester bond to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.
Pssm-ID: 341305 [Multi-domain] Cd Length: 447 Bit Score: 104.47 E-value: 1.02e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218563680 248 DDPINIQFTSGTTGKPKGATLSHHNIVnNAYFTgmrigynWRKNVRI-CLPVPLYH----CFGSVGGGVIMALY--GTTV 320
Cdd:cd17650 93 EDLAYVIYTSGTTGKPKGVMVEHRNVA-HAAHA-------WRREYELdSFPVRLLQmasfSFDVFAGDFARSLLngGTLV 164
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218563680 321 IFPS-TGYDGRANLRAIEKEKCTFVYGTPTMYIDMLGQPDLAKFDLSSVRGGIAAGSPCPPEVMRKILNVMGIKEMVI-G 398
Cdd:cd17650 165 ICPDeVKLDPAALYDLILKSRITLMESTPALIRPVMAYVYRNGLDLSAMRLLIVGSDGCKAQDFKTLAARFGQGMRIInS 244
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218563680 399 YGTTENS-PVTFCGFPVDSAERKIET-VGCISPHTEAKVVDPTTgEIVPLGAQGELMIRGYCVMLEYWQDEEKTRECITK 476
Cdd:cd17650 245 YGVTEATiDSTYYEEGRDPLGDSANVpIGRPLPNTAMYVLDERL-QPQPVGVAGELYIGGAGVARGYLNRPELTAERFVE 323
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218563680 477 D------RWYKTGDIASLDQFAYCKIEGRIKDLIIRGGENIYPAEIEQFLHTHPKILEAQVVGVKDERMGEEVCACIRLK 550
Cdd:cd17650 324 NpfapgeRMYRTGDLARWRADGNVELLGRVDHQVKIRGFRIELGEIESQLARHPAIDEAVVAVREDKGGEARLCAYVVAA 403
|
330 340 350 360
....*....|....*....|....*....|....*....|....*.
gi 218563680 551 EgqECTVEEIKAYCKGKIAHYKVPRYILFVQDYPLTITGKIQKHKL 596
Cdd:cd17650 404 A--TLNTAELRAFLAKELPSYMIPSYYVQLDALPLTPNGKVDRRAL 447
|
|
| PRK07768 |
PRK07768 |
long-chain-fatty-acid--CoA ligase; Validated |
248-517 |
1.25e-23 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236091 [Multi-domain] Cd Length: 545 Bit Score: 105.08 E-value: 1.25e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218563680 248 DDPINIQFTSGTTGKPKGATLSHHNIVNNAYftGMRIGYNWRKNVRICLP-VPLYHCFGSVGGGVIMALYGTTVIFPS-T 325
Cdd:PRK07768 152 DDLALMQLTSGSTGSPKAVQITHGNLYANAE--AMFVAAEFDVETDVMVSwLPLFHDMGMVGFLTVPMYFGAELVKVTpM 229
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218563680 326 GYDGRANLRA--IEKEKCTFVYGtPTMYIDMLG-----QPDLAKFDLSSVRGGIAAGSPCPPEVMRKILNV---MGIKEM 395
Cdd:PRK07768 230 DFLRDPLLWAelISKYRGTMTAA-PNFAYALLArrlrrQAKPGAFDLSSLRFALNGAEPIDPADVEDLLDAgarFGLRPE 308
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218563680 396 VIG--YGTTENS-----PVTFCGFPVDSAE------------------RKIETVGCISPHTEAKVVDpTTGEIVPLGAQG 450
Cdd:PRK07768 309 AILpaYGMAEATlavsfSPCGAGLVVDEVDadllaalrravpatkgntRRLATLGPPLPGLEVRVVD-EDGQVLPPRGVG 387
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 218563680 451 ELMIRGYCVMlEYWQDEEKTRECITKDRWYKTGDIASLDQFAYCKIEGRIKDLIIRGGENIYPAEIE 517
Cdd:PRK07768 388 VIELRGESVT-PGYLTMDGFIPAQDADGWLDTGDLGYLTEEGEVVVCGRVKDVIIMAGRNIYPTDIE 453
|
|
| AMP-binding_C |
pfam13193 |
AMP-binding enzyme C-terminal domain; This is a small domain that is found C terminal to ... |
515-590 |
2.77e-23 |
|
AMP-binding enzyme C-terminal domain; This is a small domain that is found C terminal to pfam00501. It has a central beta sheet core that is flanked by alpha helices.
Pssm-ID: 463804 [Multi-domain] Cd Length: 76 Bit Score: 93.76 E-value: 2.77e-23
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 218563680 515 EIEQFLHTHPKILEAQVVGVKDERMGEEVCACIRLKEGQECTVEEIKAYCKGKIAHYKVPRYILFVQDYPLTITGK 590
Cdd:pfam13193 1 EVESALVSHPAVAEAAVVGVPDELKGEAPVAFVVLKPGVELLEEELVAHVREELGPYAVPKEVVFVDELPKTRSGK 76
|
|
| ACSBG_like |
cd05933 |
Bubblegum-like very long-chain fatty acid CoA synthetase (VL-FACS); This family of very ... |
95-538 |
7.62e-23 |
|
Bubblegum-like very long-chain fatty acid CoA synthetase (VL-FACS); This family of very long-chain fatty acid CoA synthetase is named bubblegum because Drosophila melanogaster mutant bubblegum (BGM) has elevated levels of very-long-chain fatty acids (VLCFA) caused by a defective gene of this family. The human homolog (hsBG) has been characterized as a very long chain fatty acid CoA synthetase that functions specifically in the brain; hsBG may play a central role in brain VLCFA metabolism and myelinogenesis. VL-FACS is involved in the first reaction step of very long chain fatty acid degradation. It catalyzes the formation of fatty acyl-CoA in a two-step reaction: the formation of a fatty acyl-AMP molecule as an intermediate, and the formation of a fatty acyl-CoA. Free fatty acids must be "activated" to their CoA thioesters before participating in most catabolic and anabolic reactions.
Pssm-ID: 341256 [Multi-domain] Cd Length: 596 Bit Score: 102.82 E-value: 7.62e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218563680 95 TFAEFYQDVEKAAAGLLAAGLKRGDRLGMWGPNIYEWVLMQFATAKAGIILVAVNPAYQLQEVEFALRKVQCNAVVCptk 174
Cdd:cd05933 10 TYKEYYEACRQAAKAFLKLGLERFHGVGILGFNSPEWFIAAVGAIFAGGIAVGIYTTNSPEACQYVAETSEANILVV--- 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218563680 175 fksqhycDMLKQLCPEMEtaspggIKSsRLPDLHTVIV----TDSQQPGSFLLKDLMQAGSSQHYQQLQDLQKKLVCDDP 250
Cdd:cd05933 87 -------ENQKQLQKILQ------IQD-KLPHLKAIIQykepLKEKEPNLYSWDEFMELGRSIPDEQLDAIISSQKPNQC 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218563680 251 INIQFTSGTTGKPKGATLSHHNIVnnayFTGMRIGYNWRknvRICLPV---------PLYHCFG---------SVGGGVI 312
Cdd:cd05933 153 CTLIYTSGTTGMPKGVMLSHDNIT----WTAKAASQHMD---LRPATVgqesvvsylPLSHIAAqildiwlpiKVGGQVY 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218563680 313 M----ALYGT----------------------------TVIFPSTGYDGR-----------ANLRAIEKEKCTFVYGTPT 349
Cdd:cd05933 226 FaqpdALKGTlvktlrevrptafmgvprvwekiqekmkAVGAKSGTLKRKiaswakgvgleTNLKLMGGESPSPLFYRLA 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218563680 350 MYIDMlgQPDLAKFDLSSVRGGIAAGSPCPPEVMRKILNV-MGIKEmviGYGTTENS-PVTFCgfpVDSAERkIETVGCI 427
Cdd:cd05933 306 KKLVF--KKVRKALGLDRCQKFFTGAAPISRETLEFFLSLnIPIME---LYGMSETSgPHTIS---NPQAYR-LLSCGKA 376
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218563680 428 SPHTEAKVVDPTTGEIvplgaqGELMIRGYCVMLEYWQDEEKTRECITKDRWYKTGDIASLDQFAYCKIEGRIKDLIIR- 506
Cdd:cd05933 377 LPGCKTKIHNPDADGI------GEICFWGRHVFMGYLNMEDKTEEAIDEDGWLHSGDLGKLDEDGFLYITGRIKELIITa 450
|
490 500 510
....*....|....*....|....*....|...
gi 218563680 507 GGENIYPAEIEQFLHTH-PKILEAQVVGvkDER 538
Cdd:cd05933 451 GGENVPPVPIEDAVKKElPIISNAMLIG--DKR 481
|
|
| PRK05857 |
PRK05857 |
fatty acid--CoA ligase; |
194-596 |
8.20e-23 |
|
fatty acid--CoA ligase;
Pssm-ID: 180293 [Multi-domain] Cd Length: 540 Bit Score: 102.39 E-value: 8.20e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218563680 194 ASPGGIKSSRLPDLHTVIVTDSQQPGSfllkdlmQAGSSQHYQQLQDL--QKKLVCDDPINIQFTSGTTGKPKGATLShh 271
Cdd:PRK05857 120 APGSKMASSAVPEALHSIPVIAVDIAA-------VTRESEHSLDAASLagNADQGSEDPLAMIFTSGTTGEPKAVLLA-- 190
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218563680 272 nivNNAYFT--------GMRiGYNWRKNVRICLPVPLYHCfgsvgGGVIMAL----YGTTVIfpsTGYDGRANLRAI-EK 338
Cdd:PRK05857 191 ---NRTFFAvpdilqkeGLN-WVTWVVGETTYSPLPATHI-----GGLWWILtclmHGGLCV---TGGENTTSLLEIlTT 258
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218563680 339 EKCTFVYGTPTMYIDMLGQPDLAKFDLSSVRGGIAAGSPCPPEVMRKIlNVMGIKEMVIgYGTTENSPVTFCgFPVDSAE 418
Cdd:PRK05857 259 NAVATTCLVPTLLSKLVSELKSANATVPSLRLVGYGGSRAIAADVRFI-EATGVRTAQV-YGLSETGCTALC-LPTDDGS 335
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218563680 419 -RKIE--TVGCISPHTEAKVV-----DPTTGEIVPLGAQGELMIRGYCVMLEYWQDEEKTREcITKDRWYKTGDIASLDQ 490
Cdd:PRK05857 336 iVKIEagAVGRPYPGVDVYLAatdgiGPTAPGAGPSASFGTLWIKSPANMLGYWNNPERTAE-VLIDGWVNTGDLLERRE 414
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218563680 491 FAYCKIEGRIKDLIIRGGENIYPAEIEQFLHTHPKILEAQVVGVKDERMGEEV-CACIRLKEGQECTVEEIKAYCKgkiA 569
Cdd:PRK05857 415 DGFFYIKGRSSEMIICGGVNIAPDEVDRIAEGVSGVREAACYEIPDEEFGALVgLAVVASAELDESAARALKHTIA---A 491
|
410 420 430
....*....|....*....|....*....|....
gi 218563680 570 HYK-------VPRYILFVQDYPLTITGKIQKHKL 596
Cdd:PRK05857 492 RFRresepmaRPSTIVIVTDIPRTQSGKVMRASL 525
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
255-596 |
1.02e-22 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 103.88 E-value: 1.02e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218563680 255 FTSGTTGKPKGATLSHHNIVNNAYFTGMRIGYNWRKNVricLPVPLYHCFGSVGGGVIMALYGTTVIFPSTGY-DGRANL 333
Cdd:PRK12316 4701 YTSGSTGRPKGVAVSHGSLVNHLHATGERYELTPDDRV---LQFMSFSFDGSHEGLYHPLINGASVVIRDDSLwDPERLY 4777
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218563680 334 RAIEKEKCTFVYGTPTmYIDMLGQPDLAKFDLSSVRGGIAAGSPCPPEVMRKILNVMGIKEMVIGYGTTENS--PVTFCG 411
Cdd:PRK12316 4778 AEIHEHRVTVLVFPPV-YLQQLAEHAERDGEPPSLRVYCFGGEAVAQASYDLAWRALKPVYLFNGYGPTETTvtVLLWKA 4856
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218563680 412 FPVDSAERKIETVGCISPHTEAKVVDpTTGEIVPLGAQGELMIRGYCVMLEYWQDEEKTRECITKD-------RWYKTGD 484
Cdd:PRK12316 4857 RDGDACGAAYMPIGTPLGNRSGYVLD-GQLNPLPVGVAGELYLGGEGVARGYLERPALTAERFVPDpfgapggRLYRTGD 4935
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218563680 485 IASLDQFAYCKIEGRIKDLI-IRGGEnIYPAEIEQFLHTHPKILEAQVVGVK----DERMGEEVCACIRLKEGQECTVE- 558
Cdd:PRK12316 4936 LARYRADGVIDYLGRVDHQVkIRGFR-IELGEIEARLREHPAVREAVVIAQEgavgKQLVGYVVPQDPALADADEAQAEl 5014
|
330 340 350 360
....*....|....*....|....*....|....*....|
gi 218563680 559 --EIKAYCKGKIAHYKVPRYILFVQDYPLTITGKIQKHKL 596
Cdd:PRK12316 5015 rdELKAALRERLPEYMVPAHLVFLARMPLTPNGKLDRKAL 5054
|
|
| AACS |
cd05943 |
Acetoacetyl-CoA synthetase (acetoacetate-CoA ligase, AACS); AACS is a cytosolic ligase that ... |
80-592 |
1.78e-22 |
|
Acetoacetyl-CoA synthetase (acetoacetate-CoA ligase, AACS); AACS is a cytosolic ligase that specifically activates acetoacetate to its coenzyme A ester by a two-step reaction. Acetoacetate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This is the first step of the mevalonate pathway of isoprenoid biosynthesis via isopentenyl diphosphate. Isoprenoids are a large class of compounds found in all living organisms. AACS is widely distributed in bacteria, archaea and eukaryotes. In bacteria, AACS is known to exhibit an important role in the metabolism of poly-b-hydroxybutyrate, an intracellular reserve of organic carbon and chemical energy by some microorganisms. In mammals, AACS influences the rate of ketone body utilization for the formation of physiologically important fatty acids and cholesterol.
Pssm-ID: 341265 [Multi-domain] Cd Length: 629 Bit Score: 101.96 E-value: 1.78e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218563680 80 PDREAMVFVQDGIRK--TFAEFYQDVEKAAAGLLAAGLKRGDRLGMWGPNIYEWVLMQFATAKAGIILVAVNPAYQLQEV 157
Cdd:cd05943 83 DDPAAIYAAEDGERTevTWAELRRRVARLAAALRALGVKPGDRVAGYLPNIPEAVVAMLATASIGAIWSSCSPDFGVPGV 162
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218563680 158 EFALRKVQ------CNAVVcpTKFKSQHYCDMLKQLCPEmetaspggikssrLPDL-HTVIVTDSQQPG---------SF 221
Cdd:cd05943 163 LDRFGQIEpkvlfaVDAYT--YNGKRHDVREKVAELVKG-------------LPSLlAVVVVPYTVAAGqpdlskiakAL 227
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218563680 222 LLKDLMQAGSSQ--HYQQLQdlqkklvCDDPINIQFTSGTTGKPK-------GATLSH---HNIVNNA--------YFTG 281
Cdd:cd05943 228 TLEDFLATGAAGelEFEPLP-------FDHPLYILYSSGTTGLPKcivhgagGTLLQHlkeHILHCDLrpgdrlfyYTTC 300
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218563680 282 MRIGYNWRknvriclpvplyhcFGSVGGGVIMALYGTTVIFPSTGydgrANLRAIEKEKCTfVYGTPTMYIDMLGQPDL- 360
Cdd:cd05943 301 GWMMWNWL--------------VSGLAVGATIVLYDGSPFYPDTN----ALWDLADEEGIT-VFGTSAKYLDALEKAGLk 361
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218563680 361 --AKFDLSSVRGGIAAGSPCPPEVMRKILNvmGIKEMV----IGYGTTENSpvTFCG----FPVDSAErkietVGCISPH 430
Cdd:cd05943 362 paETHDLSSLRTILSTGSPLKPESFDYVYD--HIKPDVllasISGGTDIIS--CFVGgnplLPVYRGE-----IQCRGLG 432
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218563680 431 TEAKVVDPTTGEIVplGAQGELMIRGY--CVMLEYWQDEEKTReciTKDRWYKT-------GDIASLDQFAYCKIEGRIK 501
Cdd:cd05943 433 MAVEAFDEEGKPVW--GEKGELVCTKPfpSMPVGFWNDPDGSR---YRAAYFAKypgvwahGDWIEITPRGGVVILGRSD 507
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218563680 502 DLIIRGGENIYPAEIEQFLHTHPKILEAQVVGVKDERMGEEVCACIRLKEGQECT---VEEIKAYCKGKIAHYKVPRYIL 578
Cdd:cd05943 508 GTLNPGGVRIGTAEIYRVVEKIPEVEDSLVVGQEWKDGDERVILFVKLREGVELDdelRKRIRSTIRSALSPRHVPAKII 587
|
570
....*....|....
gi 218563680 579 FVQDYPLTITGKIQ 592
Cdd:cd05943 588 AVPDIPRTLSGKKV 601
|
|
| PRK08279 |
PRK08279 |
long-chain-acyl-CoA synthetase; Validated |
44-598 |
3.19e-22 |
|
long-chain-acyl-CoA synthetase; Validated
Pssm-ID: 236217 [Multi-domain] Cd Length: 600 Bit Score: 100.72 E-value: 3.19e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218563680 44 PPSIPTLTTSYVHGLSSHPLQSSTVDQCLQATVERYPDREAMVFvqDGIRKTFAEFYQDVEKAAAGLLAAGLKRGDRLGM 123
Cdd:PRK08279 15 LPDLPGILRGLKRTALITPDSKRSLGDVFEEAAARHPDRPALLF--EDQSISYAELNARANRYAHWAAARGVGKGDVVAL 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218563680 124 WGPNIYEWVLMQFATAKAGIILVAVNpaYQLQ-EV-EFALRKVQCNAVVCPTKfksqhycdmlkqlCPEMETASPGGIKS 201
Cdd:PRK08279 93 LMENRPEYLAAWLGLAKLGAVVALLN--TQQRgAVlAHSLNLVDAKHLIVGEE-------------LVEAFEEARADLAR 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218563680 202 SRLPDLHTVIVTDSQQpgsfLLKDLMQAgSSQHYQQLQDLQKKLVCDDPINIQFTSGTTGKPKGATLSHHNIVNnaYFTG 281
Cdd:PRK08279 158 PPRLWVAGGDTLDDPE----GYEDLAAA-AAGAPTTNPASRSGVTAKDTAFYIYTSGTTGLPKAAVMSHMRWLK--AMGG 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218563680 282 MRIGYNWRKNVRICLPVPLYH------CFGSV--GGGvimalygTTVIFPStgYDGRANLRAIEKEKCT-FVY-GTPTMY 351
Cdd:PRK08279 231 FGGLLRLTPDDVLYCCLPLYHntggtvAWSSVlaAGA-------TLALRRK--FSASRFWDDVRRYRATaFQYiGELCRY 301
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218563680 352 IdmLGQPDLAKFDLSSVRggIAAGSPCPPEVMRKILNVMGIKEMVIGYGTTEnSPVTFCGFpvdsaERKIETVGcISPHT 431
Cdd:PRK08279 302 L--LNQPPKPTDRDHRLR--LMIGNGLRPDIWDEFQQRFGIPRILEFYAASE-GNVGFINV-----FNFDGTVG-RVPLW 370
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218563680 432 EAK---VV--DPTTGEI----------VPLGAQGELMIR--------GYcvmleywQDEEKT-----RECITK-DRWYKT 482
Cdd:PRK08279 371 LAHpyaIVkyDVDTGEPvrdadgrcikVKPGEVGLLIGRitdrgpfdGY-------TDPEASekkilRDVFKKgDAWFNT 443
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218563680 483 GDIASLDQFAYCKIEGRIKDLIIRGGENIYPAEIEQFLHTHPKILEAQVVGVK----DERMGeevCACIRLKEGQECTVE 558
Cdd:PRK08279 444 GDLMRDDGFGHAQFVDRLGDTFRWKGENVATTEVENALSGFPGVEEAVVYGVEvpgtDGRAG---MAAIVLADGAEFDLA 520
|
570 580 590 600
....*....|....*....|....*....|....*....|
gi 218563680 559 EIKAYCKGKIAHYKVPRYILFVQDYPLTITGKIQKHKLRE 598
Cdd:PRK08279 521 ALAAHLYERLPAYAVPLFVRLVPELETTGTFKYRKVDLRK 560
|
|
| PRK07824 |
PRK07824 |
o-succinylbenzoate--CoA ligase; |
232-599 |
5.49e-22 |
|
o-succinylbenzoate--CoA ligase;
Pssm-ID: 236108 [Multi-domain] Cd Length: 358 Bit Score: 97.81 E-value: 5.49e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218563680 232 SQHYQQLQDLQKKLVCDDPIN-----IQFTSGTTGKPKGATLSHHNIVNNAYFTGMRIG--YNWrknvriCLPVPLYHCF 304
Cdd:PRK07824 14 AQDERRAALLRDALRVGEPIDddvalVVATSGTTGTPKGAMLTAAALTASADATHDRLGgpGQW------LLALPAHHIA 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218563680 305 G-SVGGGVIMALYGTTVIFPSTGYDGRANLRAIEKEKCTFVYG--TPTMYIDMLGQPD----LAKFDLSSVRGGiaagsP 377
Cdd:PRK07824 88 GlQVLVRSVIAGSEPVELDVSAGFDPTALPRAVAELGGGRRYTslVPMQLAKALDDPAataaLAELDAVLVGGG-----P 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218563680 378 CPPEVMRKILNvMGIKeMVIGYGTTENSP-VTFCGFPVDSAERKIEtvgcisphteakvvdpttGEIVPLGaqGELMIRG 456
Cdd:PRK07824 163 APAPVLDAAAA-AGIN-VVRTYGMSETSGgCVYDGVPLDGVRVRVE------------------DGRIALG--GPTLAKG 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218563680 457 YcvmleywqdeektRECITKD-----RWYKTGDIASLDQfAYCKIEGRIKDLIIRGGENIYPAEIEQFLHTHPKILEAQV 531
Cdd:PRK07824 221 Y-------------RNPVDPDpfaepGWFRTDDLGALDD-GVLTVLGRADDAISTGGLTVLPQVVEAALATHPAVADCAV 286
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 218563680 532 VGVKDERMGEEVCACIRLKEGQECTVEEIKAYCKGKIAHYKVPRYILFVQDYPLTITGKIQKHKLRER 599
Cdd:PRK07824 287 FGLPDDRLGQRVVAAVVGDGGPAPTLEALRAHVARTLDRTAAPRELHVVDELPRRGIGKVDRRALVRR 354
|
|
| PRK06060 |
PRK06060 |
p-hydroxybenzoic acid--AMP ligase FadD22; |
117-600 |
5.86e-22 |
|
p-hydroxybenzoic acid--AMP ligase FadD22;
Pssm-ID: 180374 [Multi-domain] Cd Length: 705 Bit Score: 100.49 E-value: 5.86e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218563680 117 RGDRLGMWGPNIYEWVLMQFATAKAGIILVAVNPAYQLQEVEFalrkvqcnavvcptkfksqhycdmlkqlcPEMETASP 196
Cdd:PRK06060 54 SGDRVLLCLPDSPDLVQLLLACLARGVMAFLANPELHRDDHAL-----------------------------AARNTEPA 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218563680 197 GGIKSSRLPD-LHTVIVTDSQQpgsfLLKDLMQAGSSQHyqqlqdlqKKLVCDDPINIQFTSGTTGKPKGATLSHHNIVn 275
Cdd:PRK06060 105 LVVTSDALRDrFQPSRVAEAAE----LMSEAARVAPGGY--------EPMGGDALAYATYTSGTTGPPKAAIHRHADPL- 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218563680 276 nAYFTGMrigynWRKNVRIC------LPVPLYHCFGsVGGGVI--MALYGTTVIFP-STGYDGRANLRAieKEKCTFVYG 346
Cdd:PRK06060 172 -TFVDAM-----CRKALRLTpedtglCSARMYFAYG-LGNSVWfpLATGGSAVINSaPVTPEAAAILSA--RFGPSVLYG 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218563680 347 TPTMYIDMLG--QPDlakfDLSSVRGGIAAGSPCPPEVMRKILNVMGIKEMVIGYGTTENSPvTFCGFPVDsaERKIETV 424
Cdd:PRK06060 243 VPNFFARVIDscSPD----SFRSLRCVVSAGEALELGLAERLMEFFGGIPILDGIGSTEVGQ-TFVSNRVD--EWRLGTL 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218563680 425 GCISPHTEAKVVDPTtGEIVPLGAQGELMIRGYCVMLEYWQDEEKTrecITKDRWYKTGDIASLDQFAYCKIEGRIKDLI 504
Cdd:PRK06060 316 GRVLPPYEIRVVAPD-GTTAGPGVEGDLWVRGPAIAKGYWNRPDSP---VANEGWLDTRDRVCIDSDGWVTYRCRADDTE 391
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218563680 505 IRGGENIYPAEIEQFLHTHPKILEAQVVGVKDERMGEEVCACIRLKEGQ---ECTVEEIKAYCKGKIAHYKVPRYILFVQ 581
Cdd:PRK06060 392 VIGGVNVDPREVERLIIEDEAVAEAAVVAVRESTGASTLQAFLVATSGAtidGSVMRDLHRGLLNRLSAFKVPHRFAVVD 471
|
490
....*....|....*....
gi 218563680 582 DYPLTITGKIQKHKLRERT 600
Cdd:PRK06060 472 RLPRTPNGKLVRGALRKQS 490
|
|
| PRK07867 |
PRK07867 |
acyl-CoA synthetase; Validated |
248-598 |
1.13e-21 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236120 [Multi-domain] Cd Length: 529 Bit Score: 98.98 E-value: 1.13e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218563680 248 DDPINIQFTSGTTGKPKGATLSHHNIVNNAYFTGMRIGYNWRKNVRICLPvpLYHCfGSVGGGVIMALYGTTVI-----F 322
Cdd:PRK07867 152 DDLFMLIFTSGTSGDPKAVRCTHRKVASAGVMLAQRFGLGPDDVCYVSMP--LFHS-NAVMAGWAVALAAGASIalrrkF 228
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218563680 323 PSTGYdgRANLRAIEKEKCTFVyGTPTMYIdmLG---QPDLAKFDLSSVRGGIAAgspcPPEVMRkILNVMGIKeMVIGY 399
Cdd:PRK07867 229 SASGF--LPDVRRYGATYANYV-GKPLSYV--LAtpeRPDDADNPLRIVYGNEGA----PGDIAR-FARRFGCV-VVDGF 297
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218563680 400 GTTENSpVTFCGFPVDSAerkietvGCISPHTEA-KVVDPTTGEIVPLG------------AQGELM-IRGYCVMLEYWQ 465
Cdd:PRK07867 298 GSTEGG-VAITRTPDTPP-------GALGPLPPGvAIVDPDTGTECPPAedadgrllnadeAIGELVnTAGPGGFEGYYN 369
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218563680 466 DEEKTRECItKDRWYKTGDIASLDQFAYCKIEGRIKDLIIRGGENIYPAEIEQFLHTHPKILEAQVVGVKDERMGEEVCA 545
Cdd:PRK07867 370 DPEADAERM-RGGVYWSGDLAYRDADGYAYFAGRLGDWMRVDGENLGTAPIERILLRYPDATEVAVYAVPDPVVGDQVMA 448
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*
gi 218563680 546 CIRLKEGQECTVEEIKAYCKGK--IAHYKVPRYILFVQDYPLTITGKIQKHKLRE 598
Cdd:PRK07867 449 ALVLAPGAKFDPDAFAEFLAAQpdLGPKQWPSYVRVCAELPRTATFKVLKRQLSA 503
|
|
| PRK08043 |
PRK08043 |
bifunctional acyl-ACP--phospholipid O-acyltransferase/long-chain-fatty-acid--ACP ligase; |
248-603 |
4.47e-21 |
|
bifunctional acyl-ACP--phospholipid O-acyltransferase/long-chain-fatty-acid--ACP ligase;
Pssm-ID: 181207 [Multi-domain] Cd Length: 718 Bit Score: 97.86 E-value: 4.47e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218563680 248 DDPINIQFTSGTTGKPKGATLSHHNIVNN-------AYFTgmrigynwrKNVRICLPVPLYHCFG-SVG------GGVIM 313
Cdd:PRK08043 365 EDAALILFTSGSEGHPKGVVHSHKSLLANveqiktiADFT---------PNDRFMSALPLFHSFGlTVGlftpllTGAEV 435
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218563680 314 ALYGTTV---IFPSTGYDgranlraiekEKCTFVYGTPTMyidmLGqpDLAKF----DLSSVRGGIAAGSPCPPEVMRKI 386
Cdd:PRK08043 436 FLYPSPLhyrIVPELVYD----------RNCTVLFGTSTF----LG--NYARFanpyDFARLRYVVAGAEKLQESTKQLW 499
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218563680 387 LNVMGIKeMVIGYGTTENSPVTFCGFPVDSaerKIETVGCISPHTEAKVVDpttgeiVPLGAQG-ELMIRGYCVMLEYWQ 465
Cdd:PRK08043 500 QDKFGLR-ILEGYGVTECAPVVSINVPMAA---KPGTVGRILPGMDARLLS------VPGIEQGgRLQLKGPNIMNGYLR 569
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218563680 466 DEE---------KTRECITKDRWYKTGDIASLDQFAYCKIEGRIKDLIIRGGENIYPAEIEQF-LHTHPKILEAQVVgVK 535
Cdd:PRK08043 570 VEKpgvlevptaENARGEMERGWYDTGDIVRFDEQGFVQIQGRAKRFAKIAGEMVSLEMVEQLaLGVSPDKQHATAI-KS 648
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 218563680 536 DERMGEevcACIRLKEGQECTVEEIKAYCKGK-IAHYKVPRYILFVQDYPLTITGKIQKHKLRERTEKQ 603
Cdd:PRK08043 649 DASKGE---ALVLFTTDSELTREKLQQYAREHgVPELAVPRDIRYLKQLPLLGSGKPDFVTLKSMVDEP 714
|
|
| A_NRPS_CmdD_like |
cd17652 |
similar to adenylation domain of chondramide synthase cmdD; This family of the adenylation (A) ... |
237-596 |
5.42e-21 |
|
similar to adenylation domain of chondramide synthase cmdD; This family of the adenylation (A) domain of nonribosomal peptide synthases (NRPS) includes phosphinothricin tripeptide (PTT, phosphinothricylalanylalanine) synthetase, where PTT is a natural-product antibiotic and potent herbicide that is produced by Streptomyces hygroscopicus. This adenylation domain has been confirmed to directly activate beta-tyrosine, and fluorinated chondramides are produced through precursor-directed biosynthesis. Also included in this family is chondramide synthase D (also known as ATP-dependent phenylalanine adenylase or phenylalanine activase or tyrosine activase). Chondramides A-D are depsipeptide antitumor and antifungal antibiotics produced by C. crocatus, are a class of mixed peptide/polyketide depsipeptides comprised of three amino acids (alanine, N-methyltryptophan, plus the unusual amino acid beta-tyrosine or alpha-methoxy-beta-tyrosine) and a polyketide chain ([E]-7-hydroxy-2,4,6-trimethyloct-4-enoic acid).
Pssm-ID: 341307 [Multi-domain] Cd Length: 436 Bit Score: 95.78 E-value: 5.42e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218563680 237 QLQDLQKKLVC---DDPINIQFTSGTTGKPKGATLSHHNIVN--NAYFTGMRIGYNWRknvriclpVPLYHCFgSVGGGV 311
Cdd:cd17652 79 MLADARPALLLttpDNLAYVIYTSGSTGRPKGVVVTHRGLANlaAAQIAAFDVGPGSR--------VLQFASP-SFDASV 149
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218563680 312 ---IMALY--GTTVIFPS----TGYDGRANLRAiekEKCTFVYGTPTMyIDMLgQPDlakfDLSSVRGGIAAGSPCPPEV 382
Cdd:cd17652 150 welLMALLagATLVLAPAeellPGEPLADLLRE---HRITHVTLPPAA-LAAL-PPD----DLPDLRTLVVAGEACPAEL 220
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218563680 383 M------RKILNvmgikemviGYGTTEnspVTFCG--FPVDSAERKIeTVGCISPHTEAKVVDPTTgEIVPLGAQGELMI 454
Cdd:cd17652 221 VdrwapgRRMIN---------AYGPTE---TTVCAtmAGPLPGGGVP-PIGRPVPGTRVYVLDARL-RPVPPGVPGELYI 286
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218563680 455 RGYCVMLEYWQDEEKTRECITKD-------RWYKTGDIASLDQFAYCKIEGRIKDLI-IRGgENIYPAEIEQFLHTHPKI 526
Cdd:cd17652 287 AGAGLARGYLNRPGLTAERFVADpfgapgsRMYRTGDLARWRADGQLEFLGRADDQVkIRG-FRIELGEVEAALTEHPGV 365
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 218563680 527 LEAqVVGVKDERMGEE-VCACIRLKEGQECTVEEIKAYCKGKIAHYKVPRYILFVQDYPLTITGKIQKHKL 596
Cdd:cd17652 366 AEA-VVVVRDDRPGDKrLVAYVVPAPGAAPTAAELRAHLAERLPGYMVPAAFVVLDALPLTPNGKLDRRAL 435
|
|
| PRK09192 |
PRK09192 |
fatty acyl-AMP ligase; |
248-558 |
6.02e-21 |
|
fatty acyl-AMP ligase;
Pssm-ID: 236403 [Multi-domain] Cd Length: 579 Bit Score: 97.00 E-value: 6.02e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218563680 248 DDPINIQFTSGTTGKPKGATLSHHNIVNNAyfTGM-RIGYNWRKNVRICLPVPLYHCFGSVGggVIMALYGT--TVIFPS 324
Cdd:PRK09192 176 DDIAYLQYSSGSTRFPRGVIITHRALMANL--RAIsHDGLKVRPGDRCVSWLPFYHDMGLVG--FLLTPVATqlSVDYLP 251
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218563680 325 TGYDGR---ANLRAIEKEKCTFVYgTPTMYIDM----LGQPDLAKFDLSSVRGGIAAGSPCPPEVMRKILNVMG-----I 392
Cdd:PRK09192 252 TRDFARrplQWLDLISRNRGTISY-SPPFGYELcarrVNSKDLAELDLSCWRVAGIGADMIRPDVLHQFAEAFApagfdD 330
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218563680 393 KEMVIGYGTTENS-PVTF----CGFPVDSAERKI------------------ETVGC--ISPHTEAKVVDPTtGEIVPLG 447
Cdd:PRK09192 331 KAFMPSYGLAEATlAVSFsplgSGIVVEEVDRDRleyqgkavapgaetrrvrTFVNCgkALPGHEIEIRNEA-GMPLPER 409
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218563680 448 AQGELMIRGYCVMLEYWQDEEKTRECITkDRWYKTGDIASLDQfAYCKIEGRIKDLIIRGGENIYPAEIEQFLHTHPKIL 527
Cdd:PRK09192 410 VVGHICVRGPSLMSGYFRDEESQDVLAA-DGWLDTGDLGYLLD-GYLYITGRAKDLIIINGRNIWPQDIEWIAEQEPELR 487
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|...
gi 218563680 528 --EAQVVGVKDE-----------RMG---------EEVCACIRLKEGQECTVE 558
Cdd:PRK09192 488 sgDAAAFSIAQEngekivllvqcRISdeerrgqliHALAALVRSEFGVEAAVE 540
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
245-596 |
8.55e-21 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 97.72 E-value: 8.55e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218563680 245 LVCDDPINIQFTSGTTGKPKGATLSHHNIVN------NAYftGMRIGYNWRKNVRICLPVPLYHCFGSVGGGvimalyGT 318
Cdd:PRK12316 652 LNPENLAYVIYTSGSTGKPKGAGNRHRALSNrlcwmqQAY--GLGVGDTVLQKTPFSFDVSVWEFFWPLMSG------AR 723
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218563680 319 TVIFPSTGYDGRANLRA-IEKEKCTFVYGTPTMYIDMLGQPDLAkfDLSSVRGGIAAGSPCPPEVMRKILNVMGIKEMVI 397
Cdd:PRK12316 724 LVVAAPGDHRDPAKLVElINREGVDTLHFVPSMLQAFLQDEDVA--SCTSLRRIVCSGEALPADAQEQVFAKLPQAGLYN 801
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218563680 398 GYGTTENSPVTFCGFPVDSAERKIeTVGCISPHTEAKVVDpTTGEIVPLGAQGELMIRGYCVMLEYWQDEEKTRECITKD 477
Cdd:PRK12316 802 LYGPTEAAIDVTHWTCVEEGGDSV-PIGRPIANLACYILD-ANLEPVPVGVLGELYLAGRGLARGYHGRPGLTAERFVPS 879
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218563680 478 ------RWYKTGDIASLDQFAYCKIEGRIKDLIIRGGENIYPAEIEQFLHTHPKILEAQVVGVKdermGEEVCACIRLKE 551
Cdd:PRK12316 880 pfvageRMYRTGDLARYRADGVIEYAGRIDHQVKLRGLRIELGEIEARLLEHPWVREAAVLAVD----GKQLVGYVVLES 955
|
330 340 350 360
....*....|....*....|....*....|....*....|....*
gi 218563680 552 GQECTVEEIKAYCKGKIAHYKVPRYILFVQDYPLTITGKIQKHKL 596
Cdd:PRK12316 956 EGGDWREALKAHLAASLPEYMVPAQWLALERLPLTPNGKLDRKAL 1000
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
68-596 |
1.14e-20 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 97.34 E-value: 1.14e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218563680 68 VDQCLQATVERYPDREAMVFvqDGIRKTFAEFYQDVEKAAAGLLAAGLKRGDRLGMWGPNIYEWVLMQFATAKAGIILVA 147
Cdd:PRK12316 3059 VHRLFEEQVERTPDAVALAF--GEQRLSYAELNRRANRLAHRLIERGVGPDVLVGVAVERSLEMVVGLLAILKAGGAYVP 3136
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218563680 148 VNPAYQLQEVEFalrkvqcnavvcptkfksqhycdMLKQLCPEMETASPggikSSRLPDLHTVIVtdsqqpgsfLLKDLM 227
Cdd:PRK12316 3137 LDPEYPEERLAY-----------------------MLEDSGAQLLLSQS----HLRLPLAQGVQV---------LDLDRG 3180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218563680 228 QAGSSQHyqqlqDLQKKLVCDDPINIQFTSGTTGKPKGATLSHHNIVNNAYFTGMRIGYNWRKNVricLPVPLYHCFGSV 307
Cdd:PRK12316 3181 DENYAEA-----NPAIRTMPENLAYVIYTSGSTGKPKGVGIRHSALSNHLCWMQQAYGLGVGDRV---LQFTTFSFDVFV 3252
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218563680 308 GGGVIMALYGTTVIFPSTGY--DGRANLRAIEKEKCTFVYGTPTMYIDMLGQPDLAkfDLSSVRGGIAAGSPCPPEVMRK 385
Cdd:PRK12316 3253 EELFWPLMSGARVVLAGPEDwrDPALLVELINSEGVDVLHAYPSMLQAFLEEEDAH--RCTSLKRIVCGGEALPADLQQQ 3330
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218563680 386 ILNVMGIKEMvigYGTTEnSPVTFCGFPVDSAERKIETVGCISPHTEAKVVDpTTGEIVPLGAQGELMIRGYCVMLEYWQ 465
Cdd:PRK12316 3331 VFAGLPLYNL---YGPTE-ATITVTHWQCVEEGKDAVPIGRPIANRACYILD-GSLEPVPVGALGELYLGGEGLARGYHN 3405
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218563680 466 DEEKTRECITKD------RWYKTGDIASLDQFAYCKIEGRIKDLIIRGGENIYPAEIEQFLHTHPKILEAQVVGVKderm 539
Cdd:PRK12316 3406 RPGLTAERFVPDpfvpgeRLYRTGDLARYRADGVIEYIGRVDHQVKIRGFRIELGEIEARLLEHPWVREAVVLAVD---- 3481
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*..
gi 218563680 540 GEEVCACIRLKEGQECTVEEIKAYCKGKIAHYKVPRYILFVQDYPLTITGKIQKHKL 596
Cdd:PRK12316 3482 GRQLVAYVVPEDEAGDLREALKAHLKASLPEYMVPAHLLFLERMPLTPNGKLDRKAL 3538
|
|
| PRK07445 |
PRK07445 |
O-succinylbenzoic acid--CoA ligase; Reviewed |
424-606 |
3.47e-20 |
|
O-succinylbenzoic acid--CoA ligase; Reviewed
Pssm-ID: 236019 [Multi-domain] Cd Length: 452 Bit Score: 93.52 E-value: 3.47e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218563680 424 VGCISPHTEAKVVDPTTGEIVplgaqgelmIRGYCVMLEYWQDEEKTRECITkdrwykTGDIASLDQFAYCKIEGRIKDL 503
Cdd:PRK07445 285 SGQVLPHAQITIPANQTGNIT---------IQAQSLALGYYPQILDSQGIFE------TDDLGYLDAQGYLHILGRNSQK 349
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218563680 504 IIRGGENIYPAEIEQFLHTHPKILEAQVVGVKDERMGEEVCACIRLKEGQECtVEEIKAYCKGKIAHYKVPRYILFVQDY 583
Cdd:PRK07445 350 IITGGENVYPAEVEAAILATGLVQDVCVLGLPDPHWGEVVTAIYVPKDPSIS-LEELKTAIKDQLSPFKQPKHWIPVPQL 428
|
170 180
....*....|....*....|...
gi 218563680 584 PLTITGKIQKHKLRERTEKQLGL 606
Cdd:PRK07445 429 PRNPQGKINRQQLQQIAVQRLGL 451
|
|
| A_NRPS_TlmIV_like |
cd12114 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including ... |
116-591 |
4.58e-20 |
|
The adenylation domain of nonribosomal peptide synthetases (NRPS), including Streptoalloteichus tallysomycin biosynthesis genes; The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions. This family includes the TLM biosynthetic gene cluster from Streptoalloteichus that consists of nine NRPS genes; the N-terminal module of TlmVI (NRPS-5) and the starter module of BlmVI (NRPS-5) are comprised of the acyl CoA ligase (AL) and acyl carrier protein (ACP)-like domains, which are thought to be involved in the biosynthesis of the beta-aminoalaninamide moiety.
Pssm-ID: 341279 [Multi-domain] Cd Length: 477 Bit Score: 93.49 E-value: 4.58e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218563680 116 KRGDRLGMWGPNIYEWVLMQFATAKAGIILVAVNPAYQLQEVEFALRKVQCNAVVcptkfkSQHYCDmlkQLCPEMETAS 195
Cdd:cd12114 35 RPGDLVAVTLPKGPEQVVAVLGILAAGAAYVPVDIDQPAARREAILADAGARLVL------TDGPDA---QLDVAVFDVL 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218563680 196 PGGIKSSRLPDLHTVIVTDSqqpgsfllkdlmqagssqhyqqlqdlqkklvcDDPINIQFTSGTTGKPKGATLSHHNIVN 275
Cdd:cd12114 106 ILDLDALAAPAPPPPVDVAP--------------------------------DDLAYVIFTSGSTGTPKGVMISHRAALN 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218563680 276 NAYFTGMRigYNWRKNVRICLPVPL------YHCFG--SVGGgvimalygtTVIFPSTGYDGRAN--LRAIEKEKCTFVY 345
Cdd:cd12114 154 TILDINRR--FAVGPDDRVLALSSLsfdlsvYDIFGalSAGA---------TLVLPDEARRRDPAhwAELIERHGVTLWN 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218563680 346 GTPT---MYIDMLGQPDLakfDLSSVRGGIAAGSPCPPEVMRKI--------LNVMGikemvigyGTTENS------PVT 408
Cdd:cd12114 223 SVPAlleMLLDVLEAAQA---LLPSLRLVLLSGDWIPLDLPARLralapdarLISLG--------GATEASiwsiyhPID 291
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218563680 409 fcgfPVDSAERKIeTVGCISPHTEAKVVDPTtGEIVPLGAQGELMIRGYCVMLEYWQDEEKTRECITKD----RWYKTGD 484
Cdd:cd12114 292 ----EVPPDWRSI-PYGRPLANQRYRVLDPR-GRDCPDWVPGELWIGGRGVALGYLGDPELTAARFVTHpdgeRLYRTGD 365
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218563680 485 IASLDQFAYCKIEGRIKDLIIRGGENIYPAEIEQFLHTHPKILEAQVVGVkDERMGEEVCACIRLK-EGQECTVEEIKAY 563
Cdd:cd12114 366 LGRYRPDGTLEFLGRRDGQVKVRGYRIELGEIEAALQAHPGVARAVVVVL-GDPGGKRLAAFVVPDnDGTPIAPDALRAF 444
|
490 500
....*....|....*....|....*...
gi 218563680 564 CKGKIAHYKVPRYILFVQDYPLTITGKI 591
Cdd:cd12114 445 LAQTLPAYMIPSRVIALEALPLTANGKV 472
|
|
| A_NRPS_ProA |
cd17656 |
gramicidin S synthase 2, also known as ATP-dependent proline adenylase; This family of the ... |
248-596 |
9.03e-20 |
|
gramicidin S synthase 2, also known as ATP-dependent proline adenylase; This family of the adenylation (A) domain of nonribosomal peptide synthases (NRPS) contains gramicidin S synthase 2 (also known as ATP-dependent proline adenylase or proline activase or ProA). ProA is a multifunctional enzyme involved in synthesis of the cyclic peptide antibiotic gramicidin S and able to activate and polymerize the amino acids proline, valine, ornithine and leucine. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.
Pssm-ID: 341311 [Multi-domain] Cd Length: 479 Bit Score: 92.54 E-value: 9.03e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218563680 248 DDPINIQFTSGTTGKPKGATLSHHNIVNNAYFTGMRIGYNWRKNV--------RIClpvplYH------CFGsvgggvim 313
Cdd:cd17656 128 DDLLYIIYTSGTTGKPKGVQLEHKNMVNLLHFEREKTNINFSDKVlqfatcsfDVC-----YQeifstlLSG-------- 194
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218563680 314 alyGTTVIFP-STGYDGRANLRAIEKEKCTFVYgTPTMYIDMLGQPDLAKFDL-SSVRGGIAAGSPCP-PEVMRKILNVM 390
Cdd:cd17656 195 ---GTLYIIReETKRDVEQLFDLVKRHNIEVVF-LPVAFLKFIFSEREFINRFpTCVKHIITAGEQLViTNEFKEMLHEH 270
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218563680 391 GIkEMVIGYGTTENSPVTFCGFPVDSAERKIETVGCISPHTEAKVVDpTTGEIVPLGAQGELMIRGYCVMLEYWQDEEKT 470
Cdd:cd17656 271 NV-HLHNHYGPSETHVVTTYTINPEAEIPELPPIGKPISNTWIYILD-QEQQLQPQGIVGELYISGASVARGYLNRQELT 348
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218563680 471 RECITKD------RWYKTGDIASLDQFAYCKIEGRIKDLIIRGGENIYPAEIEQFLHTHPKILEAQVVGVKDERMGEEVC 544
Cdd:cd17656 349 AEKFFPDpfdpneRMYRTGDLARYLPDGNIEFLGRADHQVKIRGYRIELGEIEAQLLNHPGVSEAVVLDKADDKGEKYLC 428
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|..
gi 218563680 545 ACIRLKegQECTVEEIKAYCKGKIAHYKVPRYILFVQDYPLTITGKIQKHKL 596
Cdd:cd17656 429 AYFVME--QELNISQLREYLAKQLPEYMIPSFFVPLDQLPLTPNGKVDRKAL 478
|
|
| A_NRPS_GliP_like |
cd17653 |
nonribosomal peptide synthase GliP-like; This family includes the adenylation (A) domain of ... |
238-598 |
4.41e-19 |
|
nonribosomal peptide synthase GliP-like; This family includes the adenylation (A) domain of nonribosomal peptide synthases (NRPS) gliotoxin biosynthesis protein P (GliP), thioclapurine biosynthesis protein P (tcpP) and Sirodesmin biosynthesis protein P (SirP). In the filamentous fungus Aspergillus fumigatus, NRPS GliP is involved in the biosynthesis of gliotoxin, which is initiated by the condensation of serine and phenylalanine. Studies show that GliP is not required for invasive aspergillosis, suggesting that the principal targets of gliotoxin are neutrophils or other phagocytes. SirP is a phytotoxin produced by the fungus Leptosphaeria maculans, which causes blackleg disease of canola (Brassica napus). In the fungus Claviceps purpurea, NRPS tcpP catalyzes condensation of tyrosine and glycine, part of biosynthesis of an unusual class of epipolythiodioxopiperazines (ETPs) that lacks the reactive thiol group for toxicity. The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester bond to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.
Pssm-ID: 341308 [Multi-domain] Cd Length: 433 Bit Score: 90.06 E-value: 4.41e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218563680 238 LQDLQKKL-VC----DDPINIQFTSGTTGKPKGATLSHHNIVNNAYFT--GMRIGYNwRKNVRICLPvplyhCFgSVGGG 310
Cdd:cd17653 90 LRTSGATLlLTtdspDDLAYIIFTSGSTGIPKGVMVPHRGVLNYVSQPpaRLDVGPG-SRVAQVLSI-----AF-DACIG 162
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218563680 311 VIMA--LYGTTVIFPstgyDGRANLRAIEKEkCTFVYGTPTmyidMLGQPDLAKFDlsSVRGGIAAGSPCPPEVMRKILn 388
Cdd:cd17653 163 EIFStlCNGGTLVLA----DPSDPFAHVART-VDALMSTPS----ILSTLSPQDFP--NLKTIFLGGEAVPPSLLDRWS- 230
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218563680 389 vmGIKEMVIGYGTTENSPVTFcgFPVDSAERKIeTVGCISPHTEAKVVDPTTGEiVPLGAQGELMIRGYCVMLEYWQDEE 468
Cdd:cd17653 231 --PGRRLYNAYGPTECTISST--MTELLPGQPV-TIGKPIPNSTCYILDADLQP-VPEGVVGEICISGVQVARGYLGNPA 304
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218563680 469 KTRECITKDRW------YKTGDIASLDQFAYCKIEGRIKDLIIRGGENIYPAEIEQFLHTHPKILEAQVVGVKDERMgee 542
Cdd:cd17653 305 LTASKFVPDPFwpgsrmYRTGDYGRWTEDGGLEFLGREDNQVKVRGFRINLEEIEEVVLQSQPEVTQAAAIVVNGRL--- 381
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*.
gi 218563680 543 vcacIRLKEGQECTVEEIKAYCKGKIAHYKVPRYILFVQDYPLTITGKIQKHKLRE 598
Cdd:cd17653 382 ----VAFVTPETVDVDGLRSELAKHLPSYAVPDRIIALDSFPLTANGKVDRKALRE 433
|
|
| LC_FACS_bac1 |
cd17641 |
bacterial long-chain fatty acid CoA synthetase; The members of this family are bacterial ... |
95-544 |
5.10e-19 |
|
bacterial long-chain fatty acid CoA synthetase; The members of this family are bacterial long-chain fatty acid CoA synthetase, most of which are as yet uncharacterized. LC-FACS catalyzes the formation of fatty acyl-CoA in a two-step reaction: the formation of a fatty acyl-AMP molecule as an intermediate, and the formation of a fatty acyl-CoA. Free fatty acids must be "activated" to their CoA thioesters before participating in most catabolic and anabolic reactions.
Pssm-ID: 341296 [Multi-domain] Cd Length: 569 Bit Score: 90.95 E-value: 5.10e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218563680 95 TFAEFYQDVEKAAAGLLAAGLKRGDRLGMWGPNIYEWVLMQFATAKAGIILVAVnpaYQ---LQEVEFALRKVQCNAVVC 171
Cdd:cd17641 13 TWADYADRVRAFALGLLALGVGRGDVVAILGDNRPEWVWAELAAQAIGALSLGI---YQdsmAEEVAYLLNYTGARVVIA 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218563680 172 ptkfKSQHYCDMLKQLCPemetaspggikssRLPDLHTVIVTDS------QQPGSFLLKDLMQAGSSQHYQQLQDLQKKL 245
Cdd:cd17641 90 ----EDEEQVDKLLEIAD-------------RIPSVRYVIYCDPrgmrkyDDPRLISFEDVVALGRALDRRDPGLYEREV 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218563680 246 VCDDPINIQF---TSGTTGKPKGATLSHHNIVNN--AY--FTGMRIGynwrKNVRICLPVP-----LYhcfgSVGGGVIM 313
Cdd:cd17641 153 AAGKGEDVAVlctTSGTTGKPKLAMLSHGNFLGHcaAYlaADPLGPG----DEYVSVLPLPwigeqMY----SVGQALVC 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218563680 314 alyGTTVIFPSTGYDGRANLRAIEKekcTFVYGTPTMYIDMLGQ-----------------------------------P 358
Cdd:cd17641 225 ---GFIVNFPEEPETMMEDLREIGP---TFVLLPPRVWEGIAADvrarmmdatpfkrfmfelgmklglraldrgkrgrpV 298
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218563680 359 DLA------------------KFDLSSVRGGIAAGSPCPPEVMRkILNVMGI--KEMvigYGTTEnspvtFCGFPVDSAE 418
Cdd:cd17641 299 SLWlrlaswladallfrplrdRLGFSRLRSAATGGAALGPDTFR-FFHAIGVplKQL---YGQTE-----LAGAYTVHRD 369
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218563680 419 RKI--ETVGCISPHTEAKVVDptTGEIVplgaqgelmIRGYCVMLEYWQDEEKTRECITKDRWYKTGDIASLDQFAYCKI 496
Cdd:cd17641 370 GDVdpDTVGVPFPGTEVRIDE--VGEIL---------VRSPGVFVGYYKNPEATAEDFDEDGWLHTGDAGYFKENGHLVV 438
|
490 500 510 520
....*....|....*....|....*....|....*....|....*....
gi 218563680 497 EGRIKDL-IIRGGENIYPAEIEQFLHTHPKILEAQVVGVKDERMGEEVC 544
Cdd:cd17641 439 IDRAKDVgTTSDGTRFSPQFIENKLKFSPYIAEAVVLGAGRPYLTAFIC 487
|
|
| PRK00174 |
PRK00174 |
acetyl-CoA synthetase; Provisional |
249-606 |
1.36e-18 |
|
acetyl-CoA synthetase; Provisional
Pssm-ID: 234677 [Multi-domain] Cd Length: 637 Bit Score: 89.81 E-value: 1.36e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218563680 249 DPINIQFTSGTTGKPKG-----------ATLSHHNIvnnayftgmrigYNWRknvriclPVPLYHCFGSVG--GGVIMAL 315
Cdd:PRK00174 246 DPLFILYTSGSTGKPKGvlhttggylvyAAMTMKYV------------FDYK-------DGDVYWCTADVGwvTGHSYIV 306
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218563680 316 YG------TTVIF---PSTGYDGRAnLRAIEKEKCTFVYGTPTMyIDML---GQPDLAKFDLSSVR--GGIaaGSPCPPE 381
Cdd:PRK00174 307 YGplangaTTLMFegvPNYPDPGRF-WEVIDKHKVTIFYTAPTA-IRALmkeGDEHPKKYDLSSLRllGSV--GEPINPE 382
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218563680 382 VMRKILNVMGIKEMVIG----------------YGTTENSPVTfCGFPVdsaerkietvgcisPHTEAKVVDpTTGEIVP 445
Cdd:PRK00174 383 AWEWYYKVVGGERCPIVdtwwqtetggimitplPGATPLKPGS-ATRPL--------------PGIQPAVVD-EEGNPLE 446
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218563680 446 LGAQGEL--------MIRGYcvmleyWQDEEKTRECI--TKDRWYKTGDIASLDQFAYCKIEGRIKDLIIRGGENIYPAE 515
Cdd:PRK00174 447 GGEGGNLvikdpwpgMMRTI------YGDHERFVKTYfsTFKGMYFTGDGARRDEDGYYWITGRVDDVLNVSGHRLGTAE 520
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218563680 516 IEQFLHTHPKILEAQVVGVKDERMGEEVCACIRLKEGQECTVE---EIKAYCK---GKIAhykVPRYILFVQDYPLTITG 589
Cdd:PRK00174 521 IESALVAHPKVAEAAVVGRPDDIKGQGIYAFVTLKGGEEPSDElrkELRNWVRkeiGPIA---KPDVIQFAPGLPKTRSG 597
|
410
....*....|....*..
gi 218563680 590 KIQKHKLRERTEKQLGL 606
Cdd:PRK00174 598 KIMRRILRKIAEGEEIL 614
|
|
| PaaK |
COG1541 |
Phenylacetate-coenzyme A ligase PaaK, adenylate-forming domain family [Coenzyme transport and ... |
256-532 |
1.65e-18 |
|
Phenylacetate-coenzyme A ligase PaaK, adenylate-forming domain family [Coenzyme transport and metabolism];
Pssm-ID: 441150 [Multi-domain] Cd Length: 423 Bit Score: 88.28 E-value: 1.65e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218563680 256 TSGTTGKPKGATLSHHNIVNNAY-----FTGMRIGYNWRknVRICLPvplYHCFgsVGG-GVIMAL--YGTTVIfPSTGY 327
Cdd:COG1541 91 SSGTTGKPTVVGYTRKDLDRWAElfarsLRAAGVRPGDR--VQNAFG---YGLF--TGGlGLHYGAerLGATVI-PAGGG 162
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218563680 328 DGRANLRAIEKEKCTFVYGTPTMYIDMLGQPDLAKFDL--SSVRGGIAAGSPCPPEvMRK-ILNVMGIKEMVIgYGTTEN 404
Cdd:COG1541 163 NTERQLRLMQDFGPTVLVGTPSYLLYLAEVAEEEGIDPrdLSLKKGIFGGEPWSEE-MRKeIEERWGIKAYDI-YGLTEV 240
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218563680 405 SPVTFCgfpvDSAERKietvGC-ISP---HTEakVVDPTTGEIVPLGAQGELMIrgycvmleywqdeekTreCITKD--- 477
Cdd:COG1541 241 GPGVAY----ECEAQD----GLhIWEdhfLVE--IIDPETGEPVPEGEEGELVV---------------T--TLTKEamp 293
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 218563680 478 --RwYKTGDIASLDQfAYC----------KIEGRIKD-LIIRGGeNIYPAEIEQFLHTHPKIL-EAQVV 532
Cdd:COG1541 294 liR-YRTGDLTRLLP-EPCpcgrthprigRILGRADDmLIIRGV-NVFPSQIEEVLLRIPEVGpEYQIV 359
|
|
| PRK05691 |
PRK05691 |
peptide synthase; Validated |
66-601 |
4.62e-18 |
|
peptide synthase; Validated
Pssm-ID: 235564 [Multi-domain] Cd Length: 4334 Bit Score: 89.07 E-value: 4.62e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218563680 66 STVDQCLQATVERYPDREAMVFVQDGIRKTFAEFYQDVEKAAAGLLAAGLKR---GDRLGMWGPNIYEWVLMQFATAKAG 142
Cdd:PRK05691 9 LTLVQALQRRAAQTPDRLALRFLADDPGEGVVLSYRDLDLRARTIAAALQARasfGDRAVLLFPSGPDYVAAFFGCLYAG 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218563680 143 IILVavnPAYQlqevefalrkvqcnavvcPTKFKSQHycdmLKQLCPEMETASPGGI--KSSRLPDLHTVIVTDSQQPGS 220
Cdd:PRK05691 89 VIAV---PAYP------------------PESARRHH----QERLLSIIADAEPRLLltVADLRDSLLQMEELAAANAPE 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218563680 221 FLLKDLMQAGSSQHYQQLQdlqkkLVCDDPINIQFTSGTTGKPKGATLSHHNIVNNAYFTGMRIGYNWRKNVRICLPVPL 300
Cdd:PRK05691 144 LLCVDTLDPALAEAWQEPA-----LQPDDIAFLQYTSGSTALPKGVQVSHGNLVANEQLIRHGFGIDLNPDDVIVSWLPL 218
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218563680 301 YHCFGSVGGGVIMALYGTTVIFPSTGYDGRANLR---AIEKEKCTFVYGTPTMY---IDMLGQPDLAKFDLSSVRGGIAA 374
Cdd:PRK05691 219 YHDMGLIGGLLQPIFSGVPCVLMSPAYFLERPLRwleAISEYGGTISGGPDFAYrlcSERVSESALERLDLSRWRVAYSG 298
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218563680 375 GSPCPPEVMR--------------KILNVMGIKEMVI-------GYGTT-----------------ENSPVTFCGFPvds 416
Cdd:PRK05691 299 SEPIRQDSLErfaekfaacgfdpdSFFASYGLAEATLfvsggrrGQGIPaleldaealarnraepgTGSVLMSCGRS--- 375
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218563680 417 aerkietvgciSPHTEAKVVDPTTGEIVPLGAQGELMIRGYCVMLEYWQDEEKT-RECITKD--RWYKTGDIASLdQFAY 493
Cdd:PRK05691 376 -----------QPGHAVLIVDPQSLEVLGDNRVGEIWASGPSIAHGYWRNPEASaKTFVEHDgrTWLRTGDLGFL-RDGE 443
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218563680 494 CKIEGRIKDLIIRGGENIYPAEIEqflhthpKILEAQVVGVKDERM--------GEE---VCACIRLKEGQECTVEEIKA 562
Cdd:PRK05691 444 LFVTGRLKDMLIVRGHNLYPQDIE-------KTVEREVEVVRKGRVaafavnhqGEEgigIAAEISRSVQKILPPQALIK 516
|
570 580 590 600
....*....|....*....|....*....|....*....|...
gi 218563680 563 YCKGKIA--HYKVPRYILFVQD--YPLTITGKIQKHKLRERTE 601
Cdd:PRK05691 517 SIRQAVAeaCQEAPSVVLLLNPgaLPKTSSGKLQRSACRLRLA 559
|
|
| PRK12467 |
PRK12467 |
peptide synthase; Provisional |
255-596 |
1.74e-17 |
|
peptide synthase; Provisional
Pssm-ID: 237108 [Multi-domain] Cd Length: 3956 Bit Score: 87.14 E-value: 1.74e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218563680 255 FTSGTTGKPKGATLSHHNIVNnaYFTGMRIGYNWRKNVRICLPVPLyhCFGSVGGGVIMALY--GTTVIFPSTGYDGRAN 332
Cdd:PRK12467 3244 YTSGSTGKPKGVGVRHGALAN--HLCWIAEAYELDANDRVLLFMSF--SFDGAQERFLWTLIcgGCLVVRDNDLWDPEEL 3319
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218563680 333 LRAIEKEKCTFVYGTPTMYIDMLGQPDLAkfDLSSVRGGIAAGSPCPPEVMRKILNVMGIKEMVIGYGTTENS-PVTFCG 411
Cdd:PRK12467 3320 WQAIHAHRISIACFPPAYLQQFAEDAGGA--DCASLDIYVFGGEAVPPAAFEQVKRKLKPRGLTNGYGPTEAVvTVTLWK 3397
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218563680 412 FPVDS-AERKIETVGCISPHTEAKVVDpTTGEIVPLGAQGELMIRGYCVMLEYWQDEEKTRECITKD-------RWYKTG 483
Cdd:PRK12467 3398 CGGDAvCEAPYAPIGRPVAGRSIYVLD-GQLNPVPVGVAGELYIGGVGLARGYHQRPSLTAERFVADpfsgsggRLYRTG 3476
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218563680 484 DIASLDQFAYCKIEGRIKDLIIRGGENIYPAEIEQFLHTHPKILEAQVVGVkDERMGEEVCACIRLKEGQECTVEEIKAY 563
Cdd:PRK12467 3477 DLARYRADGVIEYLGRIDHQVKIRGFRIELGEIEARLLQHPSVREAVVLAR-DGAGGKQLVAYVVPADPQGDWRETLRDH 3555
|
330 340 350
....*....|....*....|....*....|...
gi 218563680 564 CKGKIAHYKVPRYILFVQDYPLTITGKIQKHKL 596
Cdd:PRK12467 3556 LAASLPDYMVPAQLLVLAAMPLGPNGKVDRKAL 3588
|
|
| PRK12467 |
PRK12467 |
peptide synthase; Provisional |
255-596 |
2.89e-17 |
|
peptide synthase; Provisional
Pssm-ID: 237108 [Multi-domain] Cd Length: 3956 Bit Score: 86.37 E-value: 2.89e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218563680 255 FTSGTTGKPKGATLSHHNIVNNAYFTGMRIGY----NWRKNVRICLPVPLYHCFGSV--GGGVIMALYGTTvifpstgYD 328
Cdd:PRK12467 1725 YTSGSTGRPKGAGNRHGALVNRLCATQEAYQLsaadVVLQFTSFAFDVSVWELFWPLinGARLVIAPPGAH-------RD 1797
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218563680 329 GRANLRAIEKEKCTFVYGTPTMyIDMLGQPDLAKFDLSSVRGGIAAGSPCPPEVMRKILNVMGIKEMVIGYGTTENS-PV 407
Cdd:PRK12467 1798 PEQLIQLIERQQVTTLHFVPSM-LQQLLQMDEQVEHPLSLRRVVCGGEALEVEALRPWLERLPDTGLFNLYGPTETAvDV 1876
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218563680 408 TF--CGFpVDSAERKIETVGCISPHTEAKVVDPTTgEIVPLGAQGELMIRGYCVMLEYWQDEEKTRECITKD-------R 478
Cdd:PRK12467 1877 THwtCRR-KDLEGRDSVPIGQPIANLSTYILDASL-NPVPIGVAGELYLGGVGLARGYLNRPALTAERFVADpfgtvgsR 1954
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218563680 479 WYKTGDIASLDQFAYCKIEGRIKDLI-IRGGEnIYPAEIEQFLHTHPKILEAQVVgVKDERMGEEVCA--------CIRL 549
Cdd:PRK12467 1955 LYRTGDLARYRADGVIEYLGRIDHQVkIRGFR-IELGEIEARLREQGGVREAVVI-AQDGANGKQLVAyvvptdpgLVDD 2032
|
330 340 350 360
....*....|....*....|....*....|....*....|....*..
gi 218563680 550 KEGQECTVEEIKAYCKGKIAHYKVPRYILFVQDYPLTITGKIQKHKL 596
Cdd:PRK12467 2033 DEAQVALRAILKNHLKASLPEYMVPAHLVFLARMPLTPNGKLDRKAL 2079
|
|
| PRK12467 |
PRK12467 |
peptide synthase; Provisional |
56-596 |
1.24e-16 |
|
peptide synthase; Provisional
Pssm-ID: 237108 [Multi-domain] Cd Length: 3956 Bit Score: 84.44 E-value: 1.24e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218563680 56 HGLSSHPLQSSTVDQCLQATVERYPDREAMVFvqDGIRKTFAEFYQDVEKAAAGLLAAGLKRGDRLGMWGPNIYEWVLMQ 135
Cdd:PRK12467 502 WNAPATEYAPDCVHQLIEAQARQHPERPALVF--GEQVLSYAELNRQANRLAHVLIAAGVGPDVLVGIAVERSIEMVVGL 579
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218563680 136 FATAKAGIILVAVNPAYQLQEVEFALRKVQCNAVVcptkfksqHYCDMLKQLcpemetaspggikssRLPDLHTVIVTDs 215
Cdd:PRK12467 580 LAVLKAGGAYVPLDPEYPQDRLAYMLDDSGVRLLL--------TQSHLLAQL---------------PVPAGLRSLCLD- 635
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218563680 216 qQPGSFLlkdlmqAGSSQHYQQLQDlqkklvcdDPIN---IQFTSGTTGKPKGATLSHHNIVNNAYFTGMRIGYNWRKNV 292
Cdd:PRK12467 636 -EPADLL------CGYSGHNPEVAL--------DPDNlayVIYTSGSTGQPKGVAISHGALANYVCVIAERLQLAADDSM 700
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218563680 293 RICLPvPLYHCFGSVGGGVIMAlyGTTVIF--PSTGYDGRANLRAIEKEKCTFVYGTPTMYIDML--GQPDLakfdLSSV 368
Cdd:PRK12467 701 LMVST-FAFDLGVTELFGALAS--GATLHLlpPDCARDAEAFAALMADQGVTVLKIVPSHLQALLqaSRVAL----PRPQ 773
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218563680 369 RGGIAAGSPCPPEVMR---------KILNVMGIKEMVIG--YGTTENSPVTFCGFPVDSAerkIETVG------CISPht 431
Cdd:PRK12467 774 RALVCGGEALQVDLLArvralgpgaRLINHYGPTETTVGvsTYELSDEERDFGNVPIGQP---LANLGlyildhYLNP-- 848
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218563680 432 eakvvdpttgeiVPLGAQGELMIRGYCVMLEYWQDEEKTRECITKD-------RWYKTGDIASLDQFAYCKIEGRIKDLI 504
Cdd:PRK12467 849 ------------VPVGVVGELYIGGAGLARGYHRRPALTAERFVPDpfgadggRLYRTGDLARYRADGVIEYLGRMDHQV 916
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218563680 505 -IRgGENIYPAEIEQFLHTHPKILEAQVVGVKDERMGEEVCACI--RLKEGQE--CTVEEIKAYCKGKIAHYKVPRYILF 579
Cdd:PRK12467 917 kIR-GFRIELGEIEARLLAQPGVREAVVLAQPGDAGLQLVAYLVpaAVADGAEhqATRDELKAQLRQVLPDYMVPAHLLL 995
|
570
....*....|....*..
gi 218563680 580 VQDYPLTITGKIQKHKL 596
Cdd:PRK12467 996 LDSLPLTPNGKLDRKAL 1012
|
|
| PLN02736 |
PLN02736 |
long-chain acyl-CoA synthetase |
248-517 |
1.43e-16 |
|
long-chain acyl-CoA synthetase
Pssm-ID: 178337 [Multi-domain] Cd Length: 651 Bit Score: 83.22 E-value: 1.43e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218563680 248 DDPINIQFTSGTTGKPKGATLSHHNIVNNAYFTGMRIGYNwRKNVRICLpVPLYHCFGSVGGgVIMALYGTTV------- 320
Cdd:PLN02736 221 EDVATICYTSGTTGTPKGVVLTHGNLIANVAGSSLSTKFY-PSDVHISY-LPLAHIYERVNQ-IVMLHYGVAVgfyqgdn 297
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218563680 321 -------------IFPSTG------YDGRAN-------LR------AIEKEKCTFVYGTPTMYI----------DMLGqp 358
Cdd:PLN02736 298 lklmddlaalrptIFCSVPrlynriYDGITNavkesggLKerlfnaAYNAKKQALENGKNPSPMwdrlvfnkikAKLG-- 375
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218563680 359 dlakfdlSSVRGGIAAGSPCPPEVMrKILNVMGIKEMVIGYGTTENSPVTFcgfPVDSAERKIETVGCISPHTEAKVVDP 438
Cdd:PLN02736 376 -------GRVRFMSSGASPLSPDVM-EFLRICFGGRVLEGYGMTETSCVIS---GMDEGDNLSGHVGSPNPACEVKLVDV 444
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218563680 439 T----TGEIVPLgAQGELMIRGYCVMLEYWQDEEKTRECITKDRWYKTGDIASLDQFAYCKIEGRIKDLI-IRGGENIYP 513
Cdd:PLN02736 445 PemnyTSEDQPY-PRGEICVRGPIIFKGYYKDEVQTREVIDEDGWLHTGDIGLWLPGGRLKIIDRKKNIFkLAQGEYIAP 523
|
....
gi 218563680 514 AEIE 517
Cdd:PLN02736 524 EKIE 527
|
|
| PLN02654 |
PLN02654 |
acetate-CoA ligase |
248-604 |
1.89e-16 |
|
acetate-CoA ligase
Pssm-ID: 215353 [Multi-domain] Cd Length: 666 Bit Score: 83.02 E-value: 1.89e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218563680 248 DDPINIQFTSGTTGKPKGATlshHNIVNNAYFTGMRIGYNWRKNvriclPVPLYHCFGSVG--GGVIMALYG------TT 319
Cdd:PLN02654 275 EDPLFLLYTSGSTGKPKGVL---HTTGGYMVYTATTFKYAFDYK-----PTDVYWCTADCGwiTGHSYVTYGpmlngaTV 346
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218563680 320 VIF---PSTGYDGRAnLRAIEKEKCTFVYGTPTMYIDML--GQPDLAKFDLSSVRGGIAAGSPCPPEVMRKILNVMGIKE 394
Cdd:PLN02654 347 LVFegaPNYPDSGRC-WDIVDKYKVTIFYTAPTLVRSLMrdGDEYVTRHSRKSLRVLGSVGEPINPSAWRWFFNVVGDSR 425
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218563680 395 MVIG--YGTTEN-----SPVTFCgFPVDSAERKIETVGcisphTEAKVVDPTTGEIvplgaQGElmIRGYCVMLEYWQ-- 465
Cdd:PLN02654 426 CPISdtWWQTETggfmiTPLPGA-WPQKPGSATFPFFG-----VQPVIVDEKGKEI-----EGE--CSGYLCVKKSWPga 492
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218563680 466 ------DEEKTRECITK--DRWYKTGDIASLDQFAYCKIEGRIKDLIIRGGENIYPAEIEQFLHTHPKILEAQVVGVKDE 537
Cdd:PLN02654 493 frtlygDHERYETTYFKpfAGYYFSGDGCSRDKDGYYWLTGRVDDVINVSGHRIGTAEVESALVSHPQCAEAAVVGIEHE 572
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218563680 538 RMGEEVCACIRLKEGQECTVEEIKAY---CKGKIAHYKVPRYILFVQDYPLTITGKIQKHKLRERTEKQL 604
Cdd:PLN02654 573 VKGQGIYAFVTLVEGVPYSEELRKSLiltVRNQIGAFAAPDKIHWAPGLPKTRSGKIMRRILRKIASRQL 642
|
|
| PRK05691 |
PRK05691 |
peptide synthase; Validated |
255-596 |
5.80e-16 |
|
peptide synthase; Validated
Pssm-ID: 235564 [Multi-domain] Cd Length: 4334 Bit Score: 82.14 E-value: 5.80e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218563680 255 FTSGTTGKPKGATLSHHNIVNNAYftgMRIGYnWRKNVRICLPVPLYHCFG-SVGGGVIMALYGTTV-IFPST-GYDGRA 331
Cdd:PRK05691 3876 YTSGSTGLPKGVMVEQRGMLNNQL---SKVPY-LALSEADVIAQTASQSFDiSVWQFLAAPLFGARVeIVPNAiAHDPQG 3951
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218563680 332 NLRAIEKEKCTFVYGTPTMYIDMLGQPDLAkfdLSSVRGGIAAGSPCPPEVMRKILNVMGIKEMVIGYGTTENSP-VTFc 410
Cdd:PRK05691 3952 LLAHVQAQGITVLESVPSLIQGMLAEDRQA---LDGLRWMLPTGEAMPPELARQWLQRYPQIGLVNAYGPAECSDdVAF- 4027
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218563680 411 gFPVDSAErkieTVGCISPhteakVVDPTTG----------EIVPLGAQGELMIRGYCVMLEYWQDEEKTRECITK---- 476
Cdd:PRK05691 4028 -FRVDLAS----TRGSYLP-----IGSPTDNnrlylldealELVPLGAVGELCVAGTGVGRGYVGDPLRTALAFVPhpfg 4097
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218563680 477 ---DRWYKTGDIASLDQFAYCKIEGRIKDLIIRGGENIYPAEIEQFLHTHPKILEAqVVGVKDERMGEEVCACIRLKEG- 552
Cdd:PRK05691 4098 apgERLYRTGDLARRRSDGVLEYVGRIDHQVKIRGYRIELGEIEARLHEQAEVREA-AVAVQEGVNGKHLVGYLVPHQTv 4176
|
330 340 350 360
....*....|....*....|....*....|....*....|....*.
gi 218563680 553 --QECTVEEIKAYCKGKIAHYKVPRYILFVQDYPLTITGKIQKHKL 596
Cdd:PRK05691 4177 laQGALLERIKQRLRAELPDYMVPLHWLWLDRLPLNANGKLDRKAL 4222
|
|
| FACL_like_1 |
cd05910 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
248-534 |
7.85e-16 |
|
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ATP-dependent activation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions.
Pssm-ID: 341236 [Multi-domain] Cd Length: 457 Bit Score: 80.20 E-value: 7.85e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218563680 248 DDPINIQFTSGTTGKPKGATLSHHNIVnnAYFTGMRIGYNWRKNVRICLPVPLYHCFGsvgggvimALYGTTVIFPSTGY 327
Cdd:cd05910 85 DEPAAILFTSGSTGTPKGVVYRHGTFA--AQIDALRQLYGIRPGEVDLATFPLFALFG--------PALGLTSVIPDMDP 154
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218563680 328 ------DGRANLRAIEKEKCTFVYGTPTMyIDMLGQPDLAK-FDLSSVRGGIAAGSPCPPEVM---RKILNVMGikEMVI 397
Cdd:cd05910 155 trparaDPQKLVGAIRQYGVSIVFGSPAL-LERVARYCAQHgITLPSLRRVLSAGAPVPIALAarlRKMLSDEA--EILT 231
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218563680 398 GYGTTENSPVTFCGFPVDSAERKIET-------VGCISPHTEAKVVDPTTGEI--------VPLGAQGELMIRGYCVMLE 462
Cdd:cd05910 232 PYGATEALPVSSIGSRELLATTTAATsggagtcVGRPIPGVRVRIIEIDDEPIaewddtleLPRGEIGEITVTGPTVTPT 311
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 218563680 463 YWQDEEKTRECITKDR----WYKTGDIASLD---QFAYCkieGRIKDLIIRGGENIYPAEIEQFLHTHPKILEAQVVGV 534
Cdd:cd05910 312 YVNRPVATALAKIDDNsegfWHRMGDLGYLDdegRLWFC---GRKAHRVITTGGTLYTEPVERVFNTHPGVRRSALVGV 387
|
|
| PRK04813 |
PRK04813 |
D-alanine--poly(phosphoribitol) ligase subunit DltA; |
248-596 |
1.21e-15 |
|
D-alanine--poly(phosphoribitol) ligase subunit DltA;
Pssm-ID: 235313 [Multi-domain] Cd Length: 503 Bit Score: 79.94 E-value: 1.21e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218563680 248 DDPINIQFTSGTTGKPKGATLSHHNIVNnayFTgmrigyNWRKNV------RICLPVPLYHCFGSVgggviMALY----- 316
Cdd:PRK04813 143 DDNYYIIFTSGTTGKPKGVQISHDNLVS---FT------NWMLEDfalpegPQFLNQAPYSFDLSV-----MDLYptlas 208
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218563680 317 -GTTVIFPSTGYDGRANL-RAIEKEKCTFVYGTPTmYIDM-LGQPDLAKFDLSSVRGGIAAGSPCPPEVMRKILNVMGIK 393
Cdd:PRK04813 209 gGTLVALPKDMTANFKQLfETLPQLPINVWVSTPS-FADMcLLDPSFNEEHLPNLTHFLFCGEELPHKTAKKLLERFPSA 287
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218563680 394 EMVIGYGTTENS-PVTfcgfPVDSAERKIET-----VGCISPHTEAKVVDpTTGEIVPLGAQGELMIRGYCVMLEYWQDE 467
Cdd:PRK04813 288 TIYNTYGPTEATvAVT----SIEITDEMLDQykrlpIGYAKPDSPLLIID-EEGTKLPDGEQGEIVISGPSVSKGYLNNP 362
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218563680 468 EKTREC-ITKD--RWYKTGDIASLD--QFAYckiEGRIkDLIIR-GGENIYPAEIEQFLHTHPKILEAQVVGVKDERMGE 541
Cdd:PRK04813 363 EKTAEAfFTFDgqPAYHTGDAGYLEdgLLFY---QGRI-DFQIKlNGYRIELEEIEQNLRQSSYVESAVVVPYNKDHKVQ 438
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|
gi 218563680 542 EVCACIRLKEGQ-----ECTvEEIKAYCKGKIAHYKVPRYILFVQDYPLTITGKIQKHKL 596
Cdd:PRK04813 439 YLIAYVVPKEEDferefELT-KAIKKELKERLMEYMIPRKFIYRDSLPLTPNGKIDRKAL 497
|
|
| prpE |
PRK10524 |
propionyl-CoA synthetase; Provisional |
80-591 |
1.34e-15 |
|
propionyl-CoA synthetase; Provisional
Pssm-ID: 182517 [Multi-domain] Cd Length: 629 Bit Score: 79.99 E-value: 1.34e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218563680 80 PDREAMVFV--QDGIRK--TFAEFYQDVEKAAAGLLAAGLKRGDRLGMWGPNIYEWVLMQFATAKAGII-------LVAV 148
Cdd:PRK10524 67 PEQLALIAVstETDEERtyTFRQLHDEVNRMAAMLRSLGVQRGDRVLIYMPMIAEAAFAMLACARIGAIhsvvfggFASH 146
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218563680 149 NPAYQLQEVEfalrkvqcnavvcptkfksqhycdmlkqlcPEMETASPGGIKSSRL----PDLHTVIVTDSQQPGSFLLK 224
Cdd:PRK10524 147 SLAARIDDAK------------------------------PVLIVSADAGSRGGKVvpykPLLDEAIALAQHKPRHVLLV 196
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218563680 225 D------LMQAGSSQHYQQL--QDLQKKLVCD-----DPINIQFTSGTTGKPKG------------ATLSHHNIVNNA-- 277
Cdd:PRK10524 197 DrglapmARVAGRDVDYATLraQHLGARVPVEwlesnEPSYILYTSGTTGKPKGvqrdtggyavalATSMDTIFGGKAge 276
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218563680 278 -YFTGMRIGynWrknvriclpV--PLYHCFGSVGGGVIMALYGTTVIFPstgyDGRANLRAIEKEKCTFVYGTPTMyIDM 354
Cdd:PRK10524 277 tFFCASDIG--W---------VvgHSYIVYAPLLAGMATIMYEGLPTRP----DAGIWWRIVEKYKVNRMFSAPTA-IRV 340
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218563680 355 LGQPD---LAKFDLSSVRGGIAAGSPCPPEVMRKILNVMGiKEMVIGYGTTENspvtfcGFPVDSAERKIETvgciSPHT 431
Cdd:PRK10524 341 LKKQDpalLRKHDLSSLRALFLAGEPLDEPTASWISEALG-VPVIDNYWQTET------GWPILAIARGVED----RPTR 409
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218563680 432 -----------EAKVVDPTTGEIVPLGAQGELMIRGY----CvMLEYWQDEEKtrecITKDRW-------YKTGDIASLD 489
Cdd:PRK10524 410 lgspgvpmygyNVKLLNEVTGEPCGPNEKGVLVIEGPlppgC-MQTVWGDDDR----FVKTYWslfgrqvYSTFDWGIRD 484
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218563680 490 QFAYCKIEGRIKDLIIRGGENIYPAEIEQFLHTHPKILEAQVVGVKDERMGEEVCACIRLKEGQECTVE--------EIK 561
Cdd:PRK10524 485 ADGYYFILGRTDDVINVAGHRLGTREIEESISSHPAVAEVAVVGVKDALKGQVAVAFVVPKDSDSLADRearlalekEIM 564
|
570 580 590
....*....|....*....|....*....|
gi 218563680 562 AYCKGKIAHYKVPRYILFVQDYPLTITGKI 591
Cdd:PRK10524 565 ALVDSQLGAVARPARVWFVSALPKTRSGKL 594
|
|
| PTZ00237 |
PTZ00237 |
acetyl-CoA synthetase; Provisional |
250-594 |
1.91e-15 |
|
acetyl-CoA synthetase; Provisional
Pssm-ID: 240325 [Multi-domain] Cd Length: 647 Bit Score: 79.79 E-value: 1.91e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218563680 250 PINIQFTSGTTGKPKGATLShhnivNNAYFTGMRIGYNWRKNVRICLpVPLYHC-----------FGSVGGGVIMALYGT 318
Cdd:PTZ00237 256 PLYILYTSGTTGNSKAVVRS-----NGPHLVGLKYYWRSIIEKDIPT-VVFSHSsigwvsfhgflYGSLSLGNTFVMFEG 329
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218563680 319 TVIFPSTGYDGRANlrAIEKEKCTFVYGTP-TMYIDMLGQPDL----AKFDLSSVRGGIAAGSPCPPEVMRKILNVMGIK 393
Cdd:PTZ00237 330 GIIKNKHIEDDLWN--TIEKHKVTHTLTLPkTIRYLIKTDPEAtiirSKYDLSNLKEIWCGGEVIEESIPEYIENKLKIK 407
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218563680 394 EmVIGYGTTENSPVTFcgFPVDSAERKIETVGCISPHTEAKVVDPTtGEIVPLGAQGELMIR-----GYCVMleYWQDEE 468
Cdd:PTZ00237 408 S-SRGYGQTEIGITYL--YCYGHINIPYNATGVPSIFIKPSILSED-GKELNVNEIGEVAFKlpmppSFATT--FYKNDE 481
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218563680 469 KTRECITK-DRWYKTGDIASLDQFAYCKIEGRIKDLIIRGGENIYPAEIEQFLHTHPKILEAQVVGVKDERMGEEVCACI 547
Cdd:PTZ00237 482 KFKQLFSKfPGYYNSGDLGFKDENGYYTIVSRSDDQIKISGNKVQLNTIETSILKHPLVLECCSIGIYDPDCYNVPIGLL 561
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....
gi 218563680 548 RLKEGQECTV-------EEIKAYCKGKIAHYKVPRYILFVQDYPLTITGKIQKH 594
Cdd:PTZ00237 562 VLKQDQSNQSidlnklkNEINNIITQDIESLAVLRKIIIVNQLPKTKTGKIPRQ 615
|
|
| PRK05851 |
PRK05851 |
long-chain-fatty acid--ACP ligase MbtM; |
249-536 |
2.09e-15 |
|
long-chain-fatty acid--ACP ligase MbtM;
Pssm-ID: 180289 [Multi-domain] Cd Length: 525 Bit Score: 79.04 E-value: 2.09e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218563680 249 DPINIQFTSGTTGKPKGATLSHHNIVNNAYFTGMRIGYNWRKNVrICLPVPLYHCFG------SVGGGVIMALYGTTViF 322
Cdd:PRK05851 153 GPAVLQGTAGSTGTPRTAILSPGAVLSNLRGLNARVGLDAATDV-GCSWLPLYHDMGlaflltAALAGAPLWLAPTTA-F 230
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218563680 323 PSTGY-------DGRANLRAiekekctfvygTPTMYIDMLGQ--PDLAKFDLSSVRGGIAAGSPCPPEVMRKILNVM--- 390
Cdd:PRK05851 231 SASPFrwlswlsDSRATLTA-----------APNFAYNLIGKyaRRVSDVDLGALRVALNGGEPVDCDGFERFATAMapf 299
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218563680 391 GIK--EMVIGYGTTENS-----PVTFCGFPVD-------SAERKIETVGCISPHTEAKVvDPTTGEiVPLGAQ--GELMI 454
Cdd:PRK05851 300 GFDagAAAPSYGLAESTcavtvPVPGIGLRVDevttddgSGARRHAVLGNPIPGMEVRI-SPGDGA-AGVAGReiGEIEI 377
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218563680 455 RGYCVMLEYWQDEEktrecITKDRWYKTGDIASL--DQFAYCkieGRIKDLIIRGGENIYPAEIEQflhthpkiLEAQVV 532
Cdd:PRK05851 378 RGASMMSGYLGQAP-----IDPDDWFPTGDLGYLvdGGLVVC---GRAKELITVAGRNIFPTEIER--------VAAQVR 441
|
....
gi 218563680 533 GVKD 536
Cdd:PRK05851 442 GVRE 445
|
|
| A_NRPS_acs4 |
cd17654 |
acyl-CoA synthetase family member 4; This family of the adenylation (A) domain of nonribosomal ... |
255-596 |
3.06e-15 |
|
acyl-CoA synthetase family member 4; This family of the adenylation (A) domain of nonribosomal peptide synthases (NRPS) contains acyl-CoA synthethase family member 4, also known as 2-aminoadipic 6-semialdehyde dehydrogenase or aminoadipate-semialdehyde dehydrogenase, most of which are uncharacterized. Acyl-CoA synthetase catalyzes the initial reaction in fatty acid metabolism, by forming a thioester with CoA. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.
Pssm-ID: 341309 [Multi-domain] Cd Length: 449 Bit Score: 78.28 E-value: 3.06e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218563680 255 FTSGTTGKPKGATLSHHNIVNNayFTGMRIGYNWRKNvRICLPVPLYHCFGSVgGGVIMALY--GTTVIFPSTGYDGRAN 332
Cdd:cd17654 125 HTSGTTGTPKIVAVPHKCILPN--IQHFRSLFNITSE-DILFLTSPLTFDPSV-VEIFLSLSsgATLLIVPTSVKVLPSK 200
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218563680 333 LRAI--EKEKCTFVYGTPTMYiDMLGQPDLAKFDLS---SVRGGIAAGSPCP---------PEVMR-KILNVMGIKEmVI 397
Cdd:cd17654 201 LADIlfKRHRITVLQATPTLF-RRFGSQSIKSTVLSatsSLRVLALGGEPFPslvilsswrGKGNRtRIFNIYGITE-VS 278
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218563680 398 GYGTT-----ENSPVTFcGFPVDSAerKIEtvgcisphteakVVDPTTGEivplgAQGELmirgycvmleywQDEEKTRE 472
Cdd:cd17654 279 CWALAykvpeEDSPVQL-GSPLLGT--VIE------------VRDQNGSE-----GTGQV------------FLGGLNRV 326
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218563680 473 CITKD-------RWYKTGDIASLDQfAYCKIEGRIKDLIIRGGENIYPAEIEQFLHTHPKILEAQVVGVKDERMgeevCA 545
Cdd:cd17654 327 CILDDevtvpkgTMRATGDFVTVKD-GELFFLGRKDSQIKRRGKRINLDLIQQVIESCLGVESCAVTLSDQQRL----IA 401
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|.
gi 218563680 546 CIRLKEGQECTVEEIKaycKGKIAHYKVPRYILFVQDYPLTITGKIQKHKL 596
Cdd:cd17654 402 FIVGESSSSRIHKELQ---LTLLSSHAIPDTFVQIDKLPLTSHGKVDKSEL 449
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
68-596 |
3.11e-15 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 80.00 E-value: 3.11e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218563680 68 VDQCLQATVERYPDREAMVFvqDGIRKTFAEFYQDVEKAAAGLLAAGLKRGDRLGMWGPNIYEWVLMQFATAKAGIILVA 147
Cdd:PRK12316 2005 VHQRIAEQAARAPEAIAVVF--GDQHLSYAELDSRANRLAHRLRARGVGPEVRVAIAAERSFELVVALLAVLKAGGAYVP 2082
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218563680 148 VNPAYQLQEVEFALRKVQCNAVVCPTkfksqhycDMLKQLCPemetasPGGIKssRLPdlhtvivtdsqqpgsfLLKDLM 227
Cdd:PRK12316 2083 LDPNYPAERLAYMLEDSGAALLLTQR--------HLLERLPL------PAGVA--RLP----------------LDRDAE 2130
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218563680 228 QAGSSQHYQQLQdlqkkLVCDDPINIQFTSGTTGKPKGATLSHHNIVNNAYFTGMRigynWRKNVRICLPVPLYHCF-GS 306
Cdd:PRK12316 2131 WADYPDTAPAVQ-----LAGENLAYVIYTSGSTGLPKGVAVSHGALVAHCQAAGER----YELSPADCELQFMSFSFdGA 2201
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218563680 307 VGGGVIMALYGTTVIF-PSTGYDGRANLRAIEKEKCTFVYgTPTMYIDMLGQPDLAKFDLSSVRGGIAAGSPCPPEVMRK 385
Cdd:PRK12316 2202 HEQWFHPLLNGARVLIrDDELWDPEQLYDEMERHGVTILD-FPPVYLQQLAEHAERDGRPPAVRVYCFGGEAVPAASLRL 2280
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218563680 386 ILNVMGIKEMVIGYGTTEN--SPVTFCGFPVDSAERKIETVGCISPHTEAKVVDPTTgEIVPLGAQGELMIRGYCVMLEY 463
Cdd:PRK12316 2281 AWEALRPVYLFNGYGPTEAvvTPLLWKCRPQDPCGAAYVPIGRALGNRRAYILDADL-NLLAPGMAGELYLGGEGLARGY 2359
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218563680 464 WQDEEKTRECITKD-------RWYKTGDIASLDQFAYCKIEGRIKDLI-IRGGEnIYPAEIEQFLHTHPKILEAQVVGvK 535
Cdd:PRK12316 2360 LNRPGLTAERFVPDpfsasgeRLYRTGDLARYRADGVVEYLGRIDHQVkIRGFR-IELGEIEARLQAHPAVREAVVVA-Q 2437
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 218563680 536 DERMGEEVCACIRLKEGQECTVEEIKAYCKGKIAHYKVPRYILFVQDYPLTITGKIQKHKL 596
Cdd:PRK12316 2438 DGASGKQLVAYVVPDDAAEDLLAELRAWLAARLPAYMVPAHWVVLERLPLNPNGKLDRKAL 2498
|
|
| PRK06334 |
PRK06334 |
long chain fatty acid--[acyl-carrier-protein] ligase; Validated |
248-523 |
3.31e-15 |
|
long chain fatty acid--[acyl-carrier-protein] ligase; Validated
Pssm-ID: 180533 [Multi-domain] Cd Length: 539 Bit Score: 78.70 E-value: 3.31e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218563680 248 DDPINIQFTSGTTGKPKGATLSHHNIVNNAyftgmrigynwrknvRICLP-------------VPLYHCFGSVGGGVIMA 314
Cdd:PRK06334 183 EDVAVILFTSGTEKLPKGVPLTHANLLANQ---------------RACLKffspkeddvmmsfLPPFHAYGFNSCTLFPL 247
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218563680 315 LYGTTVIFPSTGYDGRANLRAIEKEKCTFVYGTPTMYIDMLGQPDLAKFDLSSVRGGIAAGSPCPPEVMRKILNVMGIKE 394
Cdd:PRK06334 248 LSGVPVVFAYNPLYPKKIVEMIDEAKVTFLGSTPVFFDYILKTAKKQESCLPSLRFVVIGGDAFKDSLYQEALKTFPHIQ 327
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218563680 395 MVIGYGTTENSPVTfcGFPVDSAERKIETVGCISPHTEAKVVDPTTGEIVPLGAQGELMIRGYCVMLEYW-QDEEKTREC 473
Cdd:PRK06334 328 LRQGYGTTECSPVI--TINTVNSPKHESCVGMPIRGMDVLIVSEETKVPVSSGETGLVLTRGTSLFSGYLgEDFGQGFVE 405
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|
gi 218563680 474 ITKDRWYKTGDIASLDQFAYCKIEGRIKDLIIRGGENIYPAEIEQFLHTH 523
Cdd:PRK06334 406 LGGETWYVTGDLGYVDRHGELFLKGRLSRFVKIGAEMVSLEALESILMEG 455
|
|
| PRK08308 |
PRK08308 |
acyl-CoA synthetase; Validated |
253-598 |
3.44e-15 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236231 [Multi-domain] Cd Length: 414 Bit Score: 77.77 E-value: 3.44e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218563680 253 IQFTSGTTGKPKGATLSHHNIVN--NAYFTGMRIgynwrknVRICLPV---PLYHCFGSVGGgVIMAL-YGTTVIFPSTg 326
Cdd:PRK08308 106 LQYSSGTTGEPKLIRRSWTEIDReiEAYNEALNC-------EQDETPIvacPVTHSYGLICG-VLAALtRGSKPVIITN- 176
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218563680 327 ydgrANLR-AIEKEKCT---FVYGTPTMYiDMLGQPDLAKFDLSSVrggIAAGSPCPPEVMRKILNVMgiKEMVIGYGTT 402
Cdd:PRK08308 177 ----KNPKfALNILRNTpqhILYAVPLML-HILGRLLPGTFQFHAV---MTSGTPLPEAWFYKLRERT--TYMMQQYGCS 246
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218563680 403 ENSPVTFCGfPVDSAERkietVGCISPHteakvVDPTTGEivPLGAQGELMIRgycvmleywqdeEKTRECITKDRWYKT 482
Cdd:PRK08308 247 EAGCVSICP-DMKSHLD----LGNPLPH-----VSVSAGS--DENAPEEIVVK------------MGDKEIFTKDLGYKS 302
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218563680 483 GDIASldQFAyckieGRIKDLIIRGGENIYPAEIEQFLHTHPKILEAQVVGVKDERMGEEVCAciRLKEGQECTVEEIKA 562
Cdd:PRK08308 303 ERGTL--HFM-----GRMDDVINVSGLNVYPIEVEDVMLRLPGVQEAVVYRGKDPVAGERVKA--KVISHEEIDPVQLRE 373
|
330 340 350
....*....|....*....|....*....|....*...
gi 218563680 563 YCKGKIAHYKVPRYILFVQDYPLTITGKIQK--HKLRE 598
Cdd:PRK08308 374 WCIQHLAPYQVPHEIESVTEIPKNANGKVSRklLELGE 411
|
|
| PRK09029 |
PRK09029 |
O-succinylbenzoic acid--CoA ligase; Provisional |
135-605 |
4.58e-15 |
|
O-succinylbenzoic acid--CoA ligase; Provisional
Pssm-ID: 236363 [Multi-domain] Cd Length: 458 Bit Score: 77.99 E-value: 4.58e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218563680 135 QFATAKAGIILVAVNpayQLQEVEFALRKVQCNAVVCPTKfksqhycdmlKQLcPEMETASpggikssRLPDLHTVIVTD 214
Cdd:PRK09029 48 QGVVEGSGVALRGKN---SPETLLAYLALLQCGARVLPLN----------PQL-PQPLLEE-------LLPSLTLDFALV 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218563680 215 SQQPGSFLLKDLMQAGSSQHYQQLQDLQKKLVcddpiNIQFTSGTTGKPKGATLSHHNIVNNAyfTG----MRIGYN--W 288
Cdd:PRK09029 107 LEGENTFSALTSLHLQLVEGAHAVAWQPQRLA-----TMTLTSGSTGLPKAAVHTAQAHLASA--EGvlslMPFTAQdsW 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218563680 289 rknvriCLPVPLYHcfgsVGGGVIM---ALYGTTVIFPSTG--YDgranlrAIEKekCTFVYGTPTM---YIDMLGQPdL 360
Cdd:PRK09029 180 ------LLSLPLFH----VSGQGIVwrwLYAGATLVVRDKQplEQ------ALAG--CTHASLVPTQlwrLLDNRSEP-L 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218563680 361 AkfdLSSVRGGiaaGSPCPPEVMRKiLNVMGIkEMVIGYGTTE-NSpvTFCGFPVDSaerkIETVGCISPHTEAKVVDpt 439
Cdd:PRK09029 241 S---LKAVLLG---GAAIPVELTEQ-AEQQGI-RCWCGYGLTEmAS--TVCAKRADG----LAGVGSPLPGREVKLVD-- 304
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218563680 440 tgeivplgaqGELMIRGYCVMLEYWQDEEktrecIT----KDRWYKTGDIASLDQfAYCKIEGRIKDLIIRGGENIYPAE 515
Cdd:PRK09029 305 ----------GEIWLRGASLALGYWRQGQ-----LVplvnDEGWFATRDRGEWQN-GELTILGRLDNLFFSGGEGIQPEE 368
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218563680 516 IEQFLHTHPKILEAQVVGVKDERMGEEVCACIRLKegQECTVEEIKAYCKGKIAHYKVPryilfVQDYPLTIT----G-K 590
Cdd:PRK09029 369 IERVINQHPLVQQVFVVPVADAEFGQRPVAVVESD--SEAAVVNLAEWLQDKLARFQQP-----VAYYLLPPElkngGiK 441
|
490
....*....|....*
gi 218563680 591 IQKHKLRERTEKQLG 605
Cdd:PRK09029 442 ISRQALKEWVAQQLG 456
|
|
| PaaK |
cd05913 |
Phenylacetate-CoA ligase (also known as PaaK); PaaK catalyzes the first step in the aromatic ... |
248-541 |
6.74e-15 |
|
Phenylacetate-CoA ligase (also known as PaaK); PaaK catalyzes the first step in the aromatic degradation pathway, by converting phenylacetic acid (PA) into phenylacetyl-CoA (PA-CoA). Phenylacetate-CoA ligase has been found in proteobacteria as well as gram positive prokaryotes. The enzyme is specifically induced after aerobic growth in a chemically defined medium containing PA or phenylalanine (Phe) as the sole carbon source. PaaKs are members of the adenylate-forming enzyme (AFE) family. However, sequence comparison reveals divergent features of PaaK with respect to the superfamily, including a novel N-terminal sequence.
Pssm-ID: 341239 [Multi-domain] Cd Length: 425 Bit Score: 76.89 E-value: 6.74e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218563680 248 DDPINIQFTSGTTGKPKGATLSHHNIvnnayftgmrigYNWRKNVRICLpvplyHCFGSVGGGVIMALY----------- 316
Cdd:cd05913 78 EKVVRIHASSGTTGKPTVVGYTKNDL------------DVWAELVARCL-----DAAGVTPGDRVQNAYgyglftgglgf 140
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218563680 317 -------GTTVIFPSTGYDGRaNLRAIEKEKCTFVYGTPTM------YIDMLGqpdlAKFDLSSVRGGIAAGSPCPPEVM 383
Cdd:cd05913 141 hygaerlGALVIPAGGGNTER-QLQLIKDFGPTVLCCTPSYalylaeEAEEEG----IDPRELSLKVGIFGAEPWTEEMR 215
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218563680 384 RKILNVMGIKEMVIgYGTTEnspVTFCGFPVDSAERKIETVgcISPHTEAKVVDPTTGEIVPLGAQGELMIRGYcvmley 463
Cdd:cd05913 216 KRIERRLGIKAYDI-YGLTE---IIGPGVAFECEEKDGLHI--WEDHFIPEIIDPETGEPVPPGEVGELVFTTL------ 283
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218563680 464 wqdeekTRECITKDRwYKTGDIASLDqFAYC----------KIEGRIKDLIIRGGENIYPAEIEQFLHTHPKIL-EAQVV 532
Cdd:cd05913 284 ------TKEAMPLIR-YRTRDITRLL-PGPCpcgrthrridRITGRSDDMLIIRGVNVFPSQIEDVLLKIPGLGpHYQLI 355
|
....*....
gi 218563680 533 GVKDERMGE 541
Cdd:cd05913 356 LTRQEHLDE 364
|
|
| PLN02614 |
PLN02614 |
long-chain acyl-CoA synthetase |
42-512 |
1.94e-14 |
|
long-chain acyl-CoA synthetase
Pssm-ID: 166255 [Multi-domain] Cd Length: 666 Bit Score: 76.60 E-value: 1.94e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218563680 42 DNPPSI-PTLTTSYVHGLSSHPLQSstVDQC---LQATVERYPD-----REAMVFVQDG--IRKTFAEFYQDVEKAAAGL 110
Cdd:PLN02614 19 DGRPSVgPVYRSIFAKDGFPNPIEG--MDSCwdvFRMSVEKYPNnpmlgRREIVDGKPGkyVWQTYQEVYDIVIKLGNSL 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218563680 111 LAAGLKRGDRLGMWGPNIYEWVLMQFATAKAGIILVAVNPAYQLQEVEFALRKVQCNAVVCPTKFKSQhycdmLKQLCPE 190
Cdd:PLN02614 97 RSVGVKDEAKCGIYGANSPEWIISMEACNAHGLYCVPLYDTLGAGAVEFIISHSEVSIVFVEEKKISE-----LFKTCPN 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218563680 191 ----MET-ASPGGIKSSRLPDLHTV-IVTDSQQpgsfllkDLMQAGSSQHYqQLQDLQKKLVCddpiNIQFTSGTTGKPK 264
Cdd:PLN02614 172 steyMKTvVSFGGVSREQKEEAETFgLVIYAWD-------EFLKLGEGKQY-DLPIKKKSDIC----TIMYTSGTTGDPK 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218563680 265 GATLSHHNIVnnAYFTGMrigYNWRKNVRICLPV--------PLYHCF------------GSVG---GGVIMALYGTTVI 321
Cdd:PLN02614 240 GVMISNESIV--TLIAGV---IRLLKSANAALTVkdvylsylPLAHIFdrvieecfiqhgAAIGfwrGDVKLLIEDLGEL 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218563680 322 FPS-------------TGYDGRANLRAIEKEK---CTFVYGTPTM---YIDMLGQPDLAKFDLSSVRGG-------IAAG 375
Cdd:PLN02614 315 KPTifcavprvldrvySGLQKKLSDGGFLKKFvfdSAFSYKFGNMkkgQSHVEASPLCDKLVFNKVKQGlggnvriILSG 394
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218563680 376 SPCPPEVMRKILNVMGIKEMVIGYGTTENSPVTFCGFPVDSAerKIETVGCISPHTEAKVVDPTTGEIVPLG--AQGELM 453
Cdd:PLN02614 395 AAPLASHVESFLRVVACCHVLQGYGLTESCAGTFVSLPDELD--MLGTVGPPVPNVDIRLESVPEMEYDALAstPRGEIC 472
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 218563680 454 IRGYCVMLEYWQDEEKTRECITkDRWYKTGDIASLDQFAYCKIEGRIKDLI---------IRGGENIY 512
Cdd:PLN02614 473 IRGKTLFSGYYKREDLTKEVLI-DGWLHTGDVGEWQPNGSMKIIDRKKNIFklsqgeyvaVENIENIY 539
|
|
| PLN02430 |
PLN02430 |
long-chain-fatty-acid-CoA ligase |
44-533 |
2.07e-14 |
|
long-chain-fatty-acid-CoA ligase
Pssm-ID: 178049 [Multi-domain] Cd Length: 660 Bit Score: 76.39 E-value: 2.07e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218563680 44 PPSIPTLTTSYvhglsshplqsstvdQCLQATVERYPDREAMVF--VQDG-----IRKTFAEFYQDVEKAAAGLLAAGLK 116
Cdd:PLN02430 35 PPIDSDITTAW---------------DIFSKSVEKYPDNKMLGWrrIVDGkvgpyMWKTYKEVYEEVLQIGSALRASGAE 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218563680 117 RGDRLGMWGPNIYEWVLMQFATAKAGIILV---------AVNPAYQLQEVEFAL---RKVQ------C------NAVVCP 172
Cdd:PLN02430 100 PGSRVGIYGSNCPQWIVAMEACAAHSLICVplydtlgpgAVDYIVDHAEIDFVFvqdKKIKellepdCksakrlKAIVSF 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218563680 173 TKFKSQhycdmlkqlcpEMETASPGGIKSsrlpdlhtvivtdsqqpgsFLLKDLMQAGSsQHYQQLQDLQKKLVCddpiN 252
Cdd:PLN02430 180 TSVTEE-----------ESDKASQIGVKT-------------------YSWIDFLHMGK-ENPSETNPPKPLDIC----T 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218563680 253 IQFTSGTTGKPKGATLSHHNIVnnAYFTGMRIGYNW------RKNVRICLpVPLYHCFGSvgggvIMALY----GTTVIF 322
Cdd:PLN02430 225 IMYTSGTSGDPKGVVLTHEAVA--TFVRGVDLFMEQfedkmtHDDVYLSF-LPLAHILDR-----MIEEYffrkGASVGY 296
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218563680 323 pstgYDGRAN-LRA-IEKEKCTFVYGTPTMY---------------------IDMLGQPDLAKF-------------DLS 366
Cdd:PLN02430 297 ----YHGDLNaLRDdLMELKPTLLAGVPRVFerihegiqkalqelnprrrliFNALYKYKLAWMnrgyshkkaspmaDFL 372
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218563680 367 SVR------GG-----IAAGSPCPPEVmRKILNVMGIKEMVIGYGTTENSPVTFCGFPVDSAerKIETVGCISPHTEAKV 435
Cdd:PLN02430 373 AFRkvkaklGGrlrllISGGAPLSTEI-EEFLRVTSCAFVVQGYGLTETLGPTTLGFPDEMC--MLGTVGAPAVYNELRL 449
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218563680 436 VDPTTGEIVPLG--AQGELMIRGYCVMLEYWQDEEKTRECItKDRWYKTGDIASLDQFAYCKIEGRIKDLI-IRGGENIY 512
Cdd:PLN02430 450 EEVPEMGYDPLGepPRGEICVRGKCLFSGYYKNPELTEEVM-KDGWFHTGDIGEILPNGVLKIIDRKKNLIkLSQGEYVA 528
|
570 580
....*....|....*....|.
gi 218563680 513 PAEIEQFLHTHPKILEAQVVG 533
Cdd:PLN02430 529 LEYLENVYGQNPIVEDIWVYG 549
|
|
| PRK08180 |
PRK08180 |
feruloyl-CoA synthase; Reviewed |
133-488 |
9.78e-14 |
|
feruloyl-CoA synthase; Reviewed
Pssm-ID: 236175 [Multi-domain] Cd Length: 614 Bit Score: 74.14 E-value: 9.78e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218563680 133 LMQFATAKAGIILVAVNPAYQLQEVEFAlrkvqcnavvcptkfKSQHYCDMLKqlcPEMETASPGG-----IKSSRLPDL 207
Cdd:PRK08180 109 LLALAAMYAGVPYAPVSPAYSLVSQDFG---------------KLRHVLELLT---PGLVFADDGAafaraLAAVVPADV 170
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218563680 208 hTVIVTDSQQPG----SF--LLKDLMQAGSSQHYQQLQDlqkklvcDDPINIQFTSGTTGKPKGATLSHHNIVNNAyftg 281
Cdd:PRK08180 171 -EVVAVRGAVPGraatPFaaLLATPPTAAVDAAHAAVGP-------DTIAKFLFTSGSTGLPKAVINTHRMLCANQ---- 238
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218563680 282 MRIGYNWRKnVRICLPV-----PLYHCFGS---VGggviMALY--GTTVIfpstgYDGR----------ANLRAIekekc 341
Cdd:PRK08180 239 QMLAQTFPF-LAEEPPVlvdwlPWNHTFGGnhnLG----IVLYngGTLYI-----DDGKptpggfdetlRNLREI----- 303
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218563680 342 tfvygTPTMYI------DMLGQ-----PDLAKFDLSSVRGGIAAGSPCPPEVMRKiLNVMGIKE------MVIGYGTTEN 404
Cdd:PRK08180 304 -----SPTVYFnvpkgwEMLVPalerdAALRRRFFSRLKLLFYAGAALSQDVWDR-LDRVAEATcgerirMMTGLGMTET 377
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218563680 405 SPV-TFCGFPVDSAerkietvGCI---SPHTEAKvvdpttgeIVPLGAQGELMIRGYCVMLEYWQDEEKTRECITKDRWY 480
Cdd:PRK08180 378 APSaTFTTGPLSRA-------GNIglpAPGCEVK--------LVPVGGKLEVRVKGPNVTPGYWRAPELTAEAFDEEGYY 442
|
....*...
gi 218563680 481 KTGDIASL 488
Cdd:PRK08180 443 RSGDAVRF 450
|
|
| PRK03584 |
PRK03584 |
acetoacetate--CoA ligase; |
80-592 |
1.42e-13 |
|
acetoacetate--CoA ligase;
Pssm-ID: 235134 [Multi-domain] Cd Length: 655 Bit Score: 73.68 E-value: 1.42e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218563680 80 PDREAMVFV-QDGIRK--TFAEFYQDVEKAAAGLLAAGLKRGDRLGMWGPNIYEWVLMQFATAKAGIILVAVNPayqlqe 156
Cdd:PRK03584 98 DDRPAIIFRgEDGPRRelSWAELRRQVAALAAALRALGVGPGDRVAAYLPNIPETVVAMLATASLGAIWSSCSP------ 171
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218563680 157 vEFALRkvqcnAVVcptkfksqhycDMLKQLCPEMETASPG---GIKS-----------SRLPDL-HTVIV-------TD 214
Cdd:PRK03584 172 -DFGVQ-----GVL-----------DRFGQIEPKVLIAVDGyryGGKAfdrrakvaelrAALPSLeHVVVVpylgpaaAA 234
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218563680 215 SQQPGSFLLKDLMQAGSSQ--HYQQLQdlqkklvCDDPINIQFTSGTTGKPK-------GATLSH---HNIVNNA----- 277
Cdd:PRK03584 235 AALPGALLWEDFLAPAEAAelEFEPVP-------FDHPLWILYSSGTTGLPKcivhghgGILLEHlkeLGLHCDLgpgdr 307
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218563680 278 --YFT--G--MrigYNWRknvriclpvplyhcfgsVGGgviMALYGTTVIFP-STGY-DGRANLRAIEKEKCTfVYGTPT 349
Cdd:PRK03584 308 ffWYTtcGwmM---WNWL-----------------VSG---LLVGATLVLYDgSPFYpDPNVLWDLAAEEGVT-VFGTSA 363
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218563680 350 MYIDMLGQPDL---AKFDLSSVRGGIAAGSPCPPEVMRKILNvmGIKEMV----IGYGTtenspvTFCG-F-------PV 414
Cdd:PRK03584 364 KYLDACEKAGLvpgETHDLSALRTIGSTGSPLPPEGFDWVYE--HVKADVwlasISGGT------DICScFvggnpllPV 435
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218563680 415 DSAErkietVGCISPHTEAKVVDPtTGEIVpLGAQGELMIRGY--CVMLEYWQDEEKTReciTKDRWYKT-------GDI 485
Cdd:PRK03584 436 YRGE-----IQCRGLGMAVEAWDE-DGRPV-VGEVGELVCTKPfpSMPLGFWNDPDGSR---YRDAYFDTfpgvwrhGDW 505
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218563680 486 ASLDQFAYCKIEGRIKDLIIRGGENIYPAEIEQFLHTHPKILEAQVVGVKDERMGEEVCACIRLKEGQECT---VEEIKA 562
Cdd:PRK03584 506 IEITEHGGVVIYGRSDATLNRGGVRIGTAEIYRQVEALPEVLDSLVIGQEWPDGDVRMPLFVVLAEGVTLDdalRARIRT 585
|
570 580 590
....*....|....*....|....*....|
gi 218563680 563 YCKGKIAHYKVPRYILFVQDYPLTITGKIQ 592
Cdd:PRK03584 586 TIRTNLSPRHVPDKIIAVPDIPRTLSGKKV 615
|
|
| PRK07769 |
PRK07769 |
long-chain-fatty-acid--CoA ligase; Validated |
248-517 |
1.62e-13 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 181109 [Multi-domain] Cd Length: 631 Bit Score: 73.61 E-value: 1.62e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218563680 248 DDPINIQFTSGTTGKPKGATLSHHNIVNNAYFTGMRIGYNWrkNVRICLPVPLYHCFG-------SVGGGVI-------- 312
Cdd:PRK07769 180 DTIAYLQYTSGSTRIPAGVQITHLNLPTNVLQVIDALEGQE--GDRGVSWLPFFHDMGlitvllpALLGHYItfmspaaf 257
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218563680 313 ----------MA-----LYGTTVIFPSTGYDgRANLRAIEKEkctfvygtptmyidmlGQPDLakfDLSSVRGGIAAGSP 377
Cdd:PRK07769 258 vrrpgrwireLArkpggTGGTFSAAPNFAFE-HAAARGLPKD----------------GEPPL---DLSNVKGLLNGSEP 317
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218563680 378 CPPEVMRKILNVM---GIKEMVI--GYGTTE-----------NSPV------------TFCGFPVDsAERKIETVGC--I 427
Cdd:PRK07769 318 VSPASMRKFNEAFapyGLPPTAIkpSYGMAEatlfvsttpmdEEPTviyvdrdelnagRFVEVPAD-APNAVAQVSAgkV 396
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218563680 428 SPHTEAKVVDPTTGEIVPLGAQGELMIRGYCVMLEYWQDEEKTRECI-----------------TKDRWYKTGDI-ASLD 489
Cdd:PRK07769 397 GVSEWAVIVDPETASELPDGQIGEIWLHGNNIGTGYWGKPEETAATFqnilksrlseshaegapDDALWVRTGDYgVYFD 476
|
330 340
....*....|....*....|....*...
gi 218563680 490 QFAYckIEGRIKDLIIRGGENIYPAEIE 517
Cdd:PRK07769 477 GELY--ITGRVKDLVIIDGRNHYPQDLE 502
|
|
| PRK12582 |
PRK12582 |
acyl-CoA synthetase; Provisional |
118-488 |
5.08e-13 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 237144 [Multi-domain] Cd Length: 624 Bit Score: 72.00 E-value: 5.08e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218563680 118 GDRLGMWGPNIYEWVLMQFATAKAGIILVAVNPAYQLQEVEFALRKvQCNAVVCPTKFKSQH---YCDMLKQLC---PEM 191
Cdd:PRK12582 105 GRPVMILSGNSIEHALMTLAAMQAGVPAAPVSPAYSLMSHDHAKLK-HLFDLVKPRVVFAQSgapFARALAALDlldVTV 183
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218563680 192 --ETASPGGIKSSRLPDLHTVIVTDsqqpgsfllkDLMQAGSSqhyqqlqdlqkkLVCDDPINIQFTSGTTGKPKGATLS 269
Cdd:PRK12582 184 vhVTGPGEGIASIAFADLAATPPTA----------AVAAAIAA------------ITPDTVAKYLFTSGSTGMPKAVINT 241
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218563680 270 HHNIVNNAyftGMRIGynwrknVRICLP----------VPLYHCFGS--------VGGGVIM--------ALYGTTVifp 323
Cdd:PRK12582 242 QRMMCANI---AMQEQ------LRPREPdppppvsldwMPWNHTMGGnanfngllWGGGTLYiddgkplpGMFEETI--- 309
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218563680 324 stgydgrANLRAIEKEkctfVYG-TP---TMYIDMLGQ-PDLAKFDLSSVRGGIAAGSPCPPEVMRKI--LNVMGIKEMV 396
Cdd:PRK12582 310 -------RNLREISPT----VYGnVPagyAMLAEAMEKdDALRRSFFKNLRLMAYGGATLSDDLYERMqaLAVRTTGHRI 378
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218563680 397 I---GYGTTENSPVTFcgfPVDSAERKIETVGCISPHTEAKVVdpttgeivPLGAQGELMIRGYCVMLEYWQDEEKTREC 473
Cdd:PRK12582 379 PfytGYGATETAPTTT---GTHWDTERVGLIGLPLPGVELKLA--------PVGDKYEVRVKGPNVTPGYHKDPELTAAA 447
|
410
....*....|....*
gi 218563680 474 ITKDRWYKTGDIASL 488
Cdd:PRK12582 448 FDEEGFYRLGDAARF 462
|
|
| hsFATP4_like |
cd05939 |
Fatty acid transport proteins (FATP), including FATP4 and FATP1, and similar proteins; Fatty ... |
255-597 |
2.17e-12 |
|
Fatty acid transport proteins (FATP), including FATP4 and FATP1, and similar proteins; Fatty acid transport protein (FATP) transports long-chain or very-long-chain fatty acids across the plasma membrane. At least five copies of FATPs are identified in mammalian cells. This family includes FATP4, FATP1, and homologous proteins. Each FATP has unique patterns of tissue distribution. FATP4 is mainly expressed in the brain, testis, colon and kidney. FATPs also have fatty acid CoA synthetase activity, thus playing dual roles as fatty acid transporters and its activation enzymes. FATPs are the key players in the trafficking of exogenous fatty acids into the cell and in intracellular fatty acid homeostasis.
Pssm-ID: 341262 [Multi-domain] Cd Length: 474 Bit Score: 69.38 E-value: 2.17e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218563680 255 FTSGTTGKPKGATLSHHNIvnnaYFTGMRIGYNWR--KNVRICLPVPLYHCFGSVGGGVIMALYGTTVI----FPSTGYd 328
Cdd:cd05939 111 YTSGTTGLPKAAVIVHSRY----YRIAAGAYYAFGmrPEDVVYDCLPLYHSAGGIMGVGQALLHGSTVVirkkFSASNF- 185
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218563680 329 granLRAIEKEKCTFVygtptMYID-----MLGQPDLAKFDLSSVRggIAAGSPCPPEVMRKILNVMGIKEMVIGYGTTE 403
Cdd:cd05939 186 ----WDDCVKYNCTIV-----QYIGeicryLLAQPPSEEEQKHNVR--LAVGNGLRPQIWEQFVRRFGIPQIGEFYGATE 254
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218563680 404 --------NSPVTFCGFpVDSAERKIETVGCISphteakvVDPTTGEIV-----------PlGAQGELM--IRGYCVMLE 462
Cdd:cd05939 255 gnsslvniDNHVGACGF-NSRILPSVYPIRLIK-------VDEDTGELIrdsdglcipcqP-GEPGLLVgkIIQNDPLRR 325
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218563680 463 Y--WQDEEKTRECITK------DRWYKTGDIASLDQFAYCKIEGRIKDLIIRGGENIYPAEIEQFLHTHPKILEAQVVGV 534
Cdd:cd05939 326 FdgYVNEGATNKKIARdvfkkgDSAFLSGDVLVMDELGYLYFKDRTGDTFRWKGENVSTTEVEGILSNVLGLEDVVVYGV 405
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 218563680 535 KDERM-GEEVCACIRLKEGqECTVEEIKAYCKGKIAHYKVPRYILFVQDYPLTITGKIQKHKLR 597
Cdd:cd05939 406 EVPGVeGRAGMAAIVDPER-KVDLDRFSAVLAKSLPPYARPQFIRLLPEVDKTGTFKLQKTDLQ 468
|
|
| PTZ00216 |
PTZ00216 |
acyl-CoA synthetase; Provisional |
159-503 |
4.27e-12 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 240316 [Multi-domain] Cd Length: 700 Bit Score: 69.23 E-value: 4.27e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218563680 159 FALRKVQCNAVVCPTKfksqhycdMLKQLCPEMetaspggiKSSRLPdlHTVIVTDSQQPGSFLL--------KDLMQAG 230
Cdd:PTZ00216 187 YALRETECKAIVCNGK--------NVPNLLRLM--------KSGGMP--NTTIIYLDSLPASVDTegcrlvawTDVVAKG 248
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218563680 231 SSQHYQQLQDLQKKlvCDDPINIQFTSGTTGKPKGATLSHHNIVNNAYFTGMR----IGyNWRKNVRICLPVPLYHC--F 304
Cdd:PTZ00216 249 HSAGSHHPLNIPEN--NDDLALIMYTSGTTGDPKGVMHTHGSLTAGILALEDRlndlIG-PPEEDETYCSYLPLAHImeF 325
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218563680 305 GSVgggVIMALYGTTVIF--PST---------------------------------------------------GYDGRa 331
Cdd:PTZ00216 326 GVT---NIFLARGALIGFgsPRTltdtfarphgdltefrpvfligvprifdtikkaveaklppvgslkrrvfdhAYQSR- 401
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218563680 332 nLRAIEKEKCT-----FVYGTPTmyiDMLGqpdlakfdlSSVRGGIAAGSPCPPEVMRKILNVMGIkeMVIGYGTTE--- 403
Cdd:PTZ00216 402 -LRALKEGKDTpywneKVFSAPR---AVLG---------GRVRAMLSGGGPLSAATQEFVNVVFGM--VIQGWGLTEtvc 466
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218563680 404 NSPVTFCGfpvdsaERKIETVGCISPHTEAKVVDPT----TGEIVPlgaQGELMIRGYCVMLEYWQDEEKTRECITKDRW 479
Cdd:PTZ00216 467 CGGIQRTG------DLEPNAVGQLLKGVEMKLLDTEeykhTDTPEP---RGEILLRGPFLFKGYYKQEELTREVLDEDGW 537
|
410 420
....*....|....*....|....
gi 218563680 480 YKTGDIASLDQFAYCKIEGRIKDL 503
Cdd:PTZ00216 538 FHTGDVGSIAANGTLRIIGRVKAL 561
|
|
| PRK12476 |
PRK12476 |
putative fatty-acid--CoA ligase; Provisional |
116-517 |
6.69e-12 |
|
putative fatty-acid--CoA ligase; Provisional
Pssm-ID: 171527 [Multi-domain] Cd Length: 612 Bit Score: 68.23 E-value: 6.69e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218563680 116 KRGDRLGMWGPNIYEWVLMQFATAKAGIILVAVNpAYQLQ----EVEFALRKVQcNAVVCPTKFKSQHYCDMLKqlcpem 191
Cdd:PRK12476 90 GPGDRVAILAPQGIDYVAGFFAAIKAGTIAVPLF-APELPghaeRLDTALRDAE-PTVVLTTTAAAEAVEGFLR------ 161
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218563680 192 etaspggikssRLPDLH--TVIVTDsQQPGSfllkdlmqAGSSQHYQQLQDlqkklvcDDPINIQFTSGTTGKPKGATLS 269
Cdd:PRK12476 162 -----------NLPRLRrpRVIAID-AIPDS--------AGESFVPVELDT-------DDVSHLQYTSGSTRPPVGVEIT 214
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218563680 270 HHNIVNNAYFTGMRIGY-NWrkNVRICLPVPLYHcfgSVGGGVIM--ALYG--TTVIFPSTGYdgRANLRAIEK--EKCT 342
Cdd:PRK12476 215 HRAVGTNLVQMILSIDLlDR--NTHGVSWLPLYH---DMGLSMIGfpAVYGghSTLMSPTAFV--RRPQRWIKAlsEGSR 287
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218563680 343 F---VYGTPTMYIDMLGQ----PDLAKFDLS--------------SVRGGIAAGSP--CPPEVMRKilnVMGIKEMVIGY 399
Cdd:PRK12476 288 TgrvVTAAPNFAYEWAAQrglpAEGDDIDLSnvvliigsepvsidAVTTFNKAFAPygLPRTAFKP---SYGIAEATLFV 364
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218563680 400 GTT----ENSPVTF--------CGFPVDS-AERKIETVGC--ISPHTEAKVVDPTTGEIVPLGAQGELMIRGYCVMLEYW 464
Cdd:PRK12476 365 ATIapdaEPSVVYLdreqlgagRAVRVAAdAPNAVAHVSCgqVARSQWAVIVDPDTGAELPDGEVGEIWLHGDNIGRGYW 444
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 218563680 465 QDEEKTRECI------------------TKDRWYKTGDIAS-LDQFAYckIEGRIKDLIIRGGENIYPAEIE 517
Cdd:PRK12476 445 GRPEETERTFgaklqsrlaegshadgaaDDGTWLRTGDLGVyLDGELY--ITGRIADLIVIDGRNHYPQDIE 514
|
|
| PRK05691 |
PRK05691 |
peptide synthase; Validated |
255-596 |
2.00e-11 |
|
peptide synthase; Validated
Pssm-ID: 235564 [Multi-domain] Cd Length: 4334 Bit Score: 67.50 E-value: 2.00e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218563680 255 FTSGTTGKPKGATLSHHNI------VNNAYftGMR----------IGYNWRKNVricLPVPLyhcfgsvgggvimaLYGT 318
Cdd:PRK05691 2340 YTSGSTGKPKGVVVSHGEIamhcqaVIERF--GMRaddcelhfysINFDAASER---LLVPL--------------LCGA 2400
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218563680 319 TVIFPSTG-YDGRANLRAIEKEKCTFVYGTPTmYIDMLGQPDLAKFDLSSVRGGIAAGSPCPPEVMRKILNVMGIKEMVI 397
Cdd:PRK05691 2401 RVVLRAQGqWGAEEICQLIREQQVSILGFTPS-YGSQLAQWLAGQGEQLPVRMCITGGEALTGEHLQRIRQAFAPQLFFN 2479
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218563680 398 GYGTTENSPVTFCGFPVDSAERKIETV--GCISPHTEAKVVDPTTGeIVPLGAQGELMIRGYCVMLEYWQDEEKTRECIT 475
Cdd:PRK05691 2480 AYGPTETVVMPLACLAPEQLEEGAASVpiGRVVGARVAYILDADLA-LVPQGATGELYVGGAGLAQGYHDRPGLTAERFV 2558
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218563680 476 KD-------RWYKTGDIASLDQFAYCKIEGRIKDLI-IRGGEnIYPAEIEQFLHTHPKILEAQVVGVKDER----MGEEV 543
Cdd:PRK05691 2559 ADpfaadggRLYRTGDLVRLRADGLVEYVGRIDHQVkIRGFR-IELGEIESRLLEHPAVREAVVLALDTPSgkqlAGYLV 2637
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....
gi 218563680 544 CACIRLKEGQECTVEE-IKAYCKGKIAHYKVPRYILFVQDYPLTITGKIQKHKL 596
Cdd:PRK05691 2638 SAVAGQDDEAQAALREaLKAHLKQQLPDYMVPAHLILLDSLPLTANGKLDRRAL 2691
|
|
| hsFATP2a_ACSVL_like |
cd05938 |
Fatty acid transport proteins (FATP) including hsFATP2, hsFATP5, and hsFATP6, and similar ... |
255-598 |
4.39e-11 |
|
Fatty acid transport proteins (FATP) including hsFATP2, hsFATP5, and hsFATP6, and similar proteins; Fatty acid transport proteins (FATP) of this family transport long-chain or very-long-chain fatty acids across the plasma membrane. At least five copies of FATPs are identified in mammalian cells. This family includes hsFATP2, hsFATP5, and hsFATP6, and similar proteins. Each FATP has unique patterns of tissue distribution. These FATPs also have fatty acid CoA synthetase activity, thus playing dual roles as fatty acid transporters and its activation enzymes. The hsFATP proteins exist in two splice variants; the b variant, lacking exon 3, has no acyl-CoA synthetase activity. FATPs are key players in the trafficking of exogenous fatty acids into the cell and in intracellular fatty acid homeostasis.
Pssm-ID: 341261 [Multi-domain] Cd Length: 537 Bit Score: 65.39 E-value: 4.39e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218563680 255 FTSGTTGKPKGATLSHHNIVNNAYFTGMRiGYNWRKNVRICLpvPLYHCFGSVGG-------GVIMAL------------ 315
Cdd:cd05938 151 YTSGTTGLPKAARISHLRVLQCSGFLSLC-GVTADDVIYITL--PLYHSSGFLLGiggcielGATCVLkpkfsasqfwdd 227
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218563680 316 ---YGTTVIFpstgYDGranlraiekEKCTFVYGTPtmyidmlgqPDLAKFDlSSVRggIAAGSPCPPEVMRKILNVMG- 391
Cdd:cd05938 228 crkHNVTVIQ----YIG---------ELLRYLCNQP---------QSPNDRD-HKVR--LAIGNGLRADVWREFLRRFGp 282
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218563680 392 --IKEMvigYGTTENSpVTFCGFPvdsaeRKIETVG-------CISPHTEAKvVDPTTGE----------IVPLGAQGEL 452
Cdd:cd05938 283 irIREF---YGSTEGN-IGFFNYT-----GKIGAVGrvsylykLLFPFELIK-FDVEKEEpvrdaqgfciPVAKGEPGLL 352
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218563680 453 M--IRGYCVMLEYWQDEEKTRECITK------DRWYKTGDIASLDQFAYCKIEGRIKDLIIRGGENIYPAEIEQFLHTHP 524
Cdd:cd05938 353 VakITQQSPFLGYAGDKEQTEKKLLRdvfkkgDVYFNTGDLLVQDQQNFLYFHDRVGDTFRWKGENVATTEVADVLGLLD 432
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 218563680 525 KILEAQVVGVK----DERMGeevCACIRLKEGQECTVEEIKAYCKGKIAHYKVPRYILFVQDYPLTITGKIQKHKLRE 598
Cdd:cd05938 433 FLQEVNVYGVTvpghEGRIG---MAAVKLKPGHEFDGKKLYQHVREYLPAYARPRFLRIQDSLEITGTFKQQKVRLVE 507
|
|
| FCS |
cd05921 |
Feruloyl-CoA synthetase (FCS); Feruloyl-CoA synthetase is an essential enzyme in the feruloyl ... |
93-488 |
4.56e-11 |
|
Feruloyl-CoA synthetase (FCS); Feruloyl-CoA synthetase is an essential enzyme in the feruloyl acid degradation pathway and enables some proteobacteria to grow on media containing feruloyl acid as the sole carbon source. It catalyzes the transfer of CoA to the carboxyl group of ferulic acid, which then forms feruloyl-CoA in the presence of ATP and Mg2. The resulting feruloyl-CoA is further degraded to vanillin and acetyl-CoA. Feruloyl-CoA synthetase (FCS) is a subfamily of the adenylate-forming enzymes superfamily.
Pssm-ID: 341245 [Multi-domain] Cd Length: 561 Bit Score: 65.53 E-value: 4.56e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218563680 93 RKTFAEFYQDVEKAAAGLLAAGLKRGDRLGMWGPNIYEWVLMQFATAKAGIILVAVNPAYQLQEVEFAlrkvqcnavvcp 172
Cdd:cd05921 25 RVTYAEALRQVRAIAQGLLDLGLSAERPLLILSGNSIEHALMALAAMYAGVPAAPVSPAYSLMSQDLA------------ 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218563680 173 tkfKSQHYCDMLKQLCPEMETASP--GGIKSSRLPDLhTVIVTDSQQPG--SFLLKDLMqagssqHYQQLQDLQKKLVCD 248
Cdd:cd05921 93 ---KLKHLFELLKPGLVFAQDAAPfaRALAAIFPLGT-PLVVSRNAVAGrgAISFAELA------ATPPTAAVDAAFAAV 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218563680 249 DPINIQ---FTSGTTGKPKGATLSHHNIVNN--------AYFTG-MRIGYNWrknvriclpVPLYHCFGSvGGGVIMALY 316
Cdd:cd05921 163 GPDTVAkflFTSGSTGLPKAVINTQRMLCANqamleqtyPFFGEePPVLVDW---------LPWNHTFGG-NHNFNLVLY 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218563680 317 --GTTVI---FPSTGYDGR--ANLRAIEkekcTFVYGTPTMYIDML-----GQPDLAKFDLSSVRGGIAAGSPCPPEVMR 384
Cdd:cd05921 233 ngGTLYIddgKPMPGGFEEtlRNLREIS----PTVYFNVPAGWEMLvaaleKDEALRRRFFKRLKLMFYAGAGLSQDVWD 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218563680 385 KI--LNVMGIKE---MVIGYGTTENSPV-TFCGFPVDsaerKIETVGCISPHTEAKvvdpttgeIVPLGAQGELMIRGYC 458
Cdd:cd05921 309 RLqaLAVATVGEripMMAGLGATETAPTaTFTHWPTE----RSGLIGLPAPGTELK--------LVPSGGKYEVRVKGPN 376
|
410 420 430
....*....|....*....|....*....|
gi 218563680 459 VMLEYWQDEEKTRECITKDRWYKTGDIASL 488
Cdd:cd05921 377 VTPGYWRQPELTAQAFDEEGFYCLGDAAKL 406
|
|
| PRK05691 |
PRK05691 |
peptide synthase; Validated |
255-598 |
7.54e-10 |
|
peptide synthase; Validated
Pssm-ID: 235564 [Multi-domain] Cd Length: 4334 Bit Score: 62.49 E-value: 7.54e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218563680 255 FTSGTTGKPKGATLSHHNIVNNAYFtgMRIGYNWRKN------VRICLPVPLYHCFGSVGGGVIMALYGttvifPSTGYD 328
Cdd:PRK05691 1280 YTSGSTGQPKGVGNTHAALAERLQW--MQATYALDDSdvlmqkAPISFDVSVWECFWPLITGCRLVLAG-----PGEHRD 1352
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218563680 329 GRANLRAIEKEKCTFVYGTPTMYIDMLGQPDLAkfDLSSVRGGIAAGSPCPPEVMRKILNVMGIKEMVIGYGTTENS-PV 407
Cdd:PRK05691 1353 PQRIAELVQQYGVTTLHFVPPLLQLFIDEPLAA--ACTSLRRLFSGGEALPAELRNRVLQRLPQVQLHNRYGPTETAiNV 1430
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218563680 408 TFCGFPVDSAERkiETVGCISPHTEAKVVDPTTgEIVPLGAQGELMIRGYCVMLEYWQDEEKTRECITKD-------RWY 480
Cdd:PRK05691 1431 THWQCQAEDGER--SPIGRPLGNVLCRVLDAEL-NLLPPGVAGELCIGGAGLARGYLGRPALTAERFVPDplgedgaRLY 1507
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218563680 481 KTGDIASLDQFAYCKIEGRIKDLIIRGGENIYPAEIEQFLHTHPKILEAQVVgVKDERMGEEVCACIRLKEGQECTVEEI 560
Cdd:PRK05691 1508 RTGDRARWNADGALEYLGRLDQQVKLRGFRVEPEEIQARLLAQPGVAQAAVL-VREGAAGAQLVGYYTGEAGQEAEAERL 1586
|
330 340 350
....*....|....*....|....*....|....*...
gi 218563680 561 KAYCKGKIAHYKVPRYILFVQDYPLTITGKIQKHKLRE 598
Cdd:PRK05691 1587 KAALAAELPEYMVPAQLIRLDQMPLGPSGKLDRRALPE 1624
|
|
| PTZ00342 |
PTZ00342 |
acyl-CoA synthetase; Provisional |
248-511 |
1.61e-09 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 240370 [Multi-domain] Cd Length: 746 Bit Score: 60.89 E-value: 1.61e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218563680 248 DDP---INIQFTSGTTGKPKGATLSHHNIVN--------------------------------NAY---FTGMRIGYnWR 289
Cdd:PTZ00342 301 EDPdfiTSIVYTSGTSGKPKGVMLSNKNLYNtvvplckhsifkkynpkthlsylpishiyervIAYlsfMLGGTINI-WS 379
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218563680 290 KNVRiCLPVPLYHCFGSVGGGV---IMALYgTTVI-----FPSTGydgRANLRAIEKEKCTFVYGTPTMYIDMLgqpdla 361
Cdd:PTZ00342 380 KDIN-YFSKDIYNSKGNILAGVpkvFNRIY-TNIMteinnLPPLK---RFLVKKILSLRKSNNNGGFSKFLEGI------ 448
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218563680 362 kFDLSS-VRGGI--------AAGSPCPPEVMRKILNVMGIKeMVIGYGTTE-NSPVtfcgFPVDSAERKIETVGC-ISPH 430
Cdd:PTZ00342 449 -THISSkIKDKVnpnlevilNGGGKLSPKIAEELSVLLNVN-YYQGYGLTEtTGPI----FVQHADDNNTESIGGpISPN 522
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218563680 431 TEAKVVDPTTGEIVPLGAQGELMIRGYCVMLEYWQDEEKTRECITKDRWYKTGDIASLDQFAYCKIEGRIKDLI-IRGGE 509
Cdd:PTZ00342 523 TKYKVRTWETYKATDTLPKGELLIKSDSIFSGYFLEKEQTKNAFTEDGYFKTGDIVQINKNGSLTFLDRSKGLVkLSQGE 602
|
..
gi 218563680 510 NI 511
Cdd:PTZ00342 603 YI 604
|
|
| PRK05850 |
PRK05850 |
acyl-CoA synthetase; Validated |
254-517 |
3.00e-09 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 235624 [Multi-domain] Cd Length: 578 Bit Score: 59.96 E-value: 3.00e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218563680 254 QFTSGTTGKPKGATLSHHNIVNNayFTGMRIGYNWRKNVRICLP------VPLYHCFGSVGGGVIMALYGTTVIFPSTgy 327
Cdd:PRK05850 166 QYTSGSTRTPAGVMVSHRNVIAN--FEQLMSDYFGDTGGVPPPDttvvswLPFYHDMGLVLGVCAPILGGCPAVLTSP-- 241
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218563680 328 dgRANLRaiekekctfvygTPTMYIDMLGQ--------P--------------DLAKFDLSSVRGgIAAGSP-------- 377
Cdd:PRK05850 242 --VAFLQ------------RPARWMQLLASnphafsaaPnfafelavrktsddDMAGLDLGGVLG-IISGSErvhpatlk 306
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218563680 378 ----------CPPEVMRKilnVMGIKEMVIGYGTTE--NSPVTFCgFPVDS-----AERK-----IETVGCISPHTEA-K 434
Cdd:PRK05850 307 rfadrfapfnLRETAIRP---SYGLAEATVYVATREpgQPPESVR-FDYEKlsaghAKRCetgggTPLVSYGSPRSPTvR 382
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218563680 435 VVDPTTGEIVPLGAQGELMIRGYCVMLEYWQDEEKTREC-----------ITKDRWYKTGDIA--SLDQFAyckIEGRIK 501
Cdd:PRK05850 383 IVDPDTCIECPAGTVGEIWVHGDNVAAGYWQKPEETERTfgatlvdpspgTPEGPWLRTGDLGfiSEGELF---IVGRIK 459
|
330
....*....|....*.
gi 218563680 502 DLIIRGGENIYPAEIE 517
Cdd:PRK05850 460 DLLIVDGRNHYPDDIE 475
|
|
| entF |
PRK10252 |
enterobactin non-ribosomal peptide synthetase EntF; |
61-596 |
1.20e-08 |
|
enterobactin non-ribosomal peptide synthetase EntF;
Pssm-ID: 236668 [Multi-domain] Cd Length: 1296 Bit Score: 58.13 E-value: 1.20e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218563680 61 HPLQSSTVDQCLQATVERYPDREAMVFvqDGIRKTFAEFYQDVEKAAAGLLAAGLKRGDRLGMWGPNIYEWVLMQFATAK 140
Cdd:PRK10252 453 VEIPETTLSALVAQQAAKTPDAPALAD--ARYQFSYREMREQVVALANLLRERGVKPGDSVAVALPRSVFLTLALHAIVE 530
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218563680 141 AGIILVAVNPAYqlqevefalrkvqcnavvcPTkfksqhycDMLKQLcpeMETASPggikssRLpdlhtVIVTDSQQP-- 218
Cdd:PRK10252 531 AGAAWLPLDTGY-------------------PD--------DRLKMM---LEDARP------SL-----LITTADQLPrf 569
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218563680 219 -----GSFLLKDLMQAGSsqhyqQLQDLQKKLvCDDPINIQFTSGTTGKPKGATLSHHNIVNNAYFtgMRIGYNWRKNVR 293
Cdd:PRK10252 570 advpdLTSLCYNAPLAPQ-----GAAPLQLSQ-PHHTAYIIFTSGSTGRPKGVMVGQTAIVNRLLW--MQNHYPLTADDV 641
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218563680 294 ICLPVPlyhC-FG-SV---------GGGVIMALygttvifPSTGYDGRANLRAIEKEKCTFVYGTPTMYIDMLGQ--PDL 360
Cdd:PRK10252 642 VLQKTP---CsFDvSVweffwpfiaGAKLVMAE-------PEAHRDPLAMQQFFAEYGVTTTHFVPSMLAAFVASltPEG 711
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218563680 361 AKFDLSSVRGGIAAGSPCPPEVMRKILNVMGIkEMVIGYGTTEnSPVTFCGFPVdSAERKIETVGCISP------HTEAK 434
Cdd:PRK10252 712 ARQSCASLRQVFCSGEALPADLCREWQQLTGA-PLHNLYGPTE-AAVDVSWYPA-FGEELAAVRGSSVPigypvwNTGLR 788
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218563680 435 VVDpTTGEIVPLGAQGELMIRGYCVMLEYWQDEEKTRECITKD------RWYKTGDIAS-LDQFA--YCkieGRIKDLI- 504
Cdd:PRK10252 789 ILD-ARMRPVPPGVAGDLYLTGIQLAQGYLGRPDLTASRFIADpfapgeRMYRTGDVARwLDDGAveYL---GRSDDQLk 864
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218563680 505 IRgGENIYPAEIEQFLHTHPKILE----AQVVGVKDERMGEE--VCACIRLKEGQECTVEEIKAYCKGKIAHYKVPRYIL 578
Cdd:PRK10252 865 IR-GQRIELGEIDRAMQALPDVEQavthACVINQAAATGGDArqLVGYLVSQSGLPLDTSALQAQLRERLPPHMVPVVLL 943
|
570
....*....|....*...
gi 218563680 579 FVQDYPLTITGKIQKHKL 596
Cdd:PRK10252 944 QLDQLPLSANGKLDRKAL 961
|
|
| PLN02387 |
PLN02387 |
long-chain-fatty-acid-CoA ligase family protein |
94-524 |
3.61e-08 |
|
long-chain-fatty-acid-CoA ligase family protein
Pssm-ID: 215217 [Multi-domain] Cd Length: 696 Bit Score: 56.66 E-value: 3.61e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218563680 94 KTFAEFYQDVEKAAAGLLAAGLKRGDRLGMWGPNIYEWVLMQFATAKAGIILVAVNPAYQLQEVEFALRKVQCNAVVCPT 173
Cdd:PLN02387 107 ITYGQVFERVCNFASGLVALGHNKEERVAIFADTRAEWLIALQGCFRQNITVVTIYASLGEEALCHSLNETEVTTVICDS 186
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218563680 174 KfksqhycdMLKQLcPEMetaspggikSSRLPDLHTVIVTDSQQPGSFLLKDLMQAGSSQHYQQLQDLQKKLVCD----- 248
Cdd:PLN02387 187 K--------QLKKL-IDI---------SSQLETVKRVIYMDDEGVDSDSSLSGSSNWTVSSFSEVEKLGKENPVDpdlps 248
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218563680 249 --DPINIQFTSGTTGKPKGATLSHHNIVnnAYFTG-MRIGYNWRKNVRICLPVPLYHCFGSVGGGVIMAL-----YGTTV 320
Cdd:PLN02387 249 pnDIAVIMYTSGSTGLPKGVMMTHGNIV--ATVAGvMTVVPKLGKNDVYLAYLPLAHILELAAESVMAAVgaaigYGSPL 326
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218563680 321 IFPST------GYDGRANLRaiekeKCTFVYGTPTMY----------IDMLGqpDLAK--FDLS---------------- 366
Cdd:PLN02387 327 TLTDTsnkikkGTKGDASAL-----KPTLMTAVPAILdrvrdgvrkkVDAKG--GLAKklFDIAykrrlaaiegswfgaw 399
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218563680 367 ---------------------SVRGGIAAGSPCPPEVMRKILNVMGIKeMVIGYGTTEN-SPVTFCGFPVDSAERkietV 424
Cdd:PLN02387 400 glekllwdalvfkkiravlggRIRFMLSGGAPLSGDTQRFINICLGAP-IGQGYGLTETcAGATFSEWDDTSVGR----V 474
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218563680 425 GCISPHTEAKVVD-PTTGEIV---PLgAQGELMIRGYCVMLEYWQDEEKTRECITKD----RWYKTGDIASLDQFAYCKI 496
Cdd:PLN02387 475 GPPLPCCYVKLVSwEEGGYLIsdkPM-PRGEIVIGGPSVTLGYFKNQEKTDEVYKVDergmRWFYTGDIGQFHPDGCLEI 553
|
490 500
....*....|....*....|....*....
gi 218563680 497 EGRIKDLI-IRGGENIYPAEIEQFLHTHP 524
Cdd:PLN02387 554 IDRKKDIVkLQHGEYVSLGKVEAALSVSP 582
|
|
| PLN02861 |
PLN02861 |
long-chain-fatty-acid-CoA ligase |
95-503 |
1.40e-07 |
|
long-chain-fatty-acid-CoA ligase
Pssm-ID: 178452 [Multi-domain] Cd Length: 660 Bit Score: 54.46 E-value: 1.40e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218563680 95 TFAEFYQDVEKAAAGLLAAGLKRGDRLGMWGPNIYEWVLMQFATAKAGIILVAVNPAYQLQEVEFALRKVQCN-AVVCPT 173
Cdd:PLN02861 79 TYKEVYDAAIRIGSAIRSRGVNPGDRCGIYGSNCPEWIIAMEACNSQGITYVPLYDTLGANAVEFIINHAEVSiAFVQES 158
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218563680 174 KFKSQHYCdmLKQLCPEMET-ASPGGIKSSRLPDlhtvivTDSQQPGSFLLKDLMQAGSSQHyqQLQDLQKKLVCddpiN 252
Cdd:PLN02861 159 KISSILSC--LPKCSSNLKTiVSFGDVSSEQKEE------AEELGVSCFSWEEFSLMGSLDC--ELPPKQKTDIC----T 224
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218563680 253 IQFTSGTTGKPKGATLSHHNIVNNAyftgMRIGYNWRKNVRICLP-------VPLYHCFGSVgggviMALY----GTTVI 321
Cdd:PLN02861 225 IMYTSGTTGEPKGVILTNRAIIAEV----LSTDHLLKVTDRVATEedsyfsyLPLAHVYDQV-----IETYciskGASIG 295
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218563680 322 FpsTGYDGRANLRAIEKEKCTFVYGTPTMYIDMLG-------------------------------------QPDLAKFD 364
Cdd:PLN02861 296 F--WQGDIRYLMEDVQALKPTIFCGVPRVYDRIYTgimqkissggmlrkklfdfaynyklgnlrkglkqeeaSPRLDRLV 373
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218563680 365 LSSVRGG--------IAAGSPCPPEVmRKILNVMGIKEMVIGYGTTENSPVTFCG----FPVdsaerkIETVGCISPHTE 432
Cdd:PLN02861 374 FDKIKEGlggrvrllLSGAAPLPRHV-EEFLRVTSCSVLSQGYGLTESCGGCFTSianvFSM------VGTVGVPMTTIE 446
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 218563680 433 AKVVD-PTTG----EIVPlgaQGELMIRGYCVMLEYWQDEEKTRECITkDRWYKTGDIASLDQFAYCKIEGRIKDL 503
Cdd:PLN02861 447 ARLESvPEMGydalSDVP---RGEICLRGNTLFSGYHKRQDLTEEVLI-DGWFHTGDIGEWQPNGAMKIIDRKKNI 518
|
|
| |
