|
Name |
Accession |
Description |
Interval |
E-value |
| hsFATP2a_ACSVL_like |
cd05938 |
Fatty acid transport proteins (FATP) including hsFATP2, hsFATP5, and hsFATP6, and similar ... |
75-609 |
0e+00 |
|
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: 1005.28 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966209822 75 YEGDIYTYQDVDKRSSRVAHVFLNHSSLKKGDTVALLMSNEPDFVHVWFGLAKLGCVVAFLNTNIRSNSLLNCIRACGPR 154
Cdd:cd05938 1 FEGETYTYRDVDRRSNQAARALLAHAGLRPGDTVALLLGNEPAFLWIWLGLAKLGCPVAFLNTNIRSKSLLHCFRCCGAK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966209822 155 ALVVGADLLGTVEEILPSLSE-NISVWGM-KDSVPQGVISLKEKLSTSPDEPVPRSHHVVSLLKSTCLYIFTSGTTGLPK 232
Cdd:cd05938 81 VLVVAPELQEAVEEVLPALRAdGVSVWYLsHTSNTEGVISLLDKVDAASDEPVPASLRAHVTIKSPALYIYTSGTTGLPK 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966209822 233 AAVISQLQVLRGSAVLWAFGCTAHDIVYITLPLYHSSAAILGISGCVELGATCVLKKKFSASQFWSDCKKYDVTVFQYIG 312
Cdd:cd05938 161 AARISHLRVLQCSGFLSLCGVTADDVIYITLPLYHSSGFLLGIGGCIELGATCVLKPKFSASQFWDDCRKHNVTVIQYIG 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966209822 313 ELCRYLCKQSKREGEKDHKVRLAIGNGIRSDVWREFLDRFGNIKVCELYAATESSISFMNYTGRIGAIGRTNLFYKLLST 392
Cdd:cd05938 241 ELLRYLCNQPQSPNDRDHKVRLAIGNGLRADVWREFLRRFGPIRIREFYGSTEGNIGFFNYTGKIGAVGRVSYLYKLLFP 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966209822 393 FDLIKYDFQKDEPMRNEQGWCIHVKKGEPGLLISRVNAKNPFFGYAGPYKHTKDKLLCDVFKKGDVYLNTGDLIVQDQDN 472
Cdd:cd05938 321 FELIKFDVEKEEPVRDAQGFCIPVAKGEPGLLVAKITQQSPFLGYAGDKEQTEKKLLRDVFKKGDVYFNTGDLLVQDQQN 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966209822 473 FLYFWDRTGDTFRWKGENVATTEVADVIGMLDFIQEANVYGVAISGYEGRAGMASIILKPNTSLDLEKVYEQVVTFLPAY 552
Cdd:cd05938 401 FLYFHDRVGDTFRWKGENVATTEVADVLGLLDFLQEVNVYGVTVPGHEGRIGMAAVKLKPGHEFDGKKLYQHVREYLPAY 480
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*..
gi 966209822 553 ACPRFLRIQEKMEATGTFKLLKHQLVEDGFNPLKISEPLYFMDNLKKSYVLLTRELY 609
Cdd:cd05938 481 ARPRFLRIQDSLEITGTFKQQKVRLVEEGFNPSIISDPLYFLDETQKTYVPLTPDIY 537
|
|
| PRK08279 |
PRK08279 |
long-chain-acyl-CoA synthetase; Validated |
16-619 |
0e+00 |
|
long-chain-acyl-CoA synthetase; Validated
Pssm-ID: 236217 [Multi-domain] Cd Length: 600 Bit Score: 681.60 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966209822 16 LHFLQKLlfPYFWDDFWFVLKVVLIIIRLKKYEKRgelvTVLDKFLSHAKRQPRKPFIIYEGDIYTYQDVDKRSSRVAHV 95
Cdd:PRK08279 5 MDLAARL--PRRLPDLPGILRGLKRTALITPDSKR----SLGDVFEEAAARHPDRPALLFEDQSISYAELNARANRYAHW 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966209822 96 FLNHSsLKKGDTVALLMSNEPDFVHVWFGLAKLGCVVAFLNTNIRSNSLLNCIRACGPRALVVGADLLGTVEEILPSLSE 175
Cdd:PRK08279 79 AAARG-VGKGDVVALLMENRPEYLAAWLGLAKLGAVVALLNTQQRGAVLAHSLNLVDAKHLIVGEELVEAFEEARADLAR 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966209822 176 NISVW---GMKDSVPQGVISLKEKLSTSPDEPVPRSHHVVslLKSTCLYIFTSGTTGLPKAAVISQLQVLR---GSAVLW 249
Cdd:PRK08279 158 PPRLWvagGDTLDDPEGYEDLAAAAAGAPTTNPASRSGVT--AKDTAFYIYTSGTTGLPKAAVMSHMRWLKamgGFGGLL 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966209822 250 AFgcTAHDIVYITLPLYHSSAAILGISGCVELGATCVLKKKFSASQFWSDCKKYDVTVFQYIGELCRYLCKQSKREGEKD 329
Cdd:PRK08279 236 RL--TPDDVLYCCLPLYHNTGGTVAWSSVLAAGATLALRRKFSASRFWDDVRRYRATAFQYIGELCRYLLNQPPKPTDRD 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966209822 330 HKVRLAIGNGIRSDVWREFLDRFGNIKVCELYAATESSISFMNYTGRIGAIGRTNLFykLLSTFDLIKYDFQKDEPMRNE 409
Cdd:PRK08279 314 HRLRLMIGNGLRPDIWDEFQQRFGIPRILEFYAASEGNVGFINVFNFDGTVGRVPLW--LAHPYAIVKYDVDTGEPVRDA 391
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966209822 410 QGWCIHVKKGEPGLLISRVNAKNPFFGYAGPYKhTKDKLLCDVFKKGDVYLNTGDLIVQDQDNFLYFWDRTGDTFRWKGE 489
Cdd:PRK08279 392 DGRCIKVKPGEVGLLIGRITDRGPFDGYTDPEA-SEKKILRDVFKKGDAWFNTGDLMRDDGFGHAQFVDRLGDTFRWKGE 470
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966209822 490 NVATTEVADVIGMLDFIQEANVYGVAISGYEGRAGMASIILKPNTSLDLEKVYEQVVTFLPAYACPRFLRIQEKMEATGT 569
Cdd:PRK08279 471 NVATTEVENALSGFPGVEEAVVYGVEVPGTDGRAGMAAIVLADGAEFDLAALAAHLYERLPAYAVPLFVRLVPELETTGT 550
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|
gi 966209822 570 FKLLKHQLVEDGFNPLKISEPLYFMDNLKKSYVLLTRELYDQIMLGEIKL 619
Cdd:PRK08279 551 FKYRKVDLRKEGFDPSKVDDPLYVLDPGSGGYVPLTAELYAEIAAGKFRL 600
|
|
| FATP_FACS |
cd05940 |
Fatty acid transport proteins (FATP) play dual roles as fatty acid transporters and its ... |
81-584 |
0e+00 |
|
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: 584.70 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966209822 81 TYQDVDKRSSRVAHVFLNHSsLKKGDTVALLMSNEPDFVHVWFGLAKLGCVVAFLNTNIRSNSLLNCIRACGPRALVVga 160
Cdd:cd05940 5 TYAELDAMANRYARWLKSLG-LKPGDVVALFMENRPEYVLLWLGLVKIGAVAALINYNLRGESLAHCLNVSSAKHLVV-- 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966209822 161 dllgtveeilpslsenisvwgmkdsvpqgvislkeklstspdepvprshhvvsllkSTCLYIFTSGTTGLPKAAVISQLQ 240
Cdd:cd05940 82 --------------------------------------------------------DAALYIYTSGTTGLPKAAIISHRR 105
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966209822 241 VLRGSA-VLWAFGCTAHDIVYITLPLYHSSAAILGISGCVELGATCVLKKKFSASQFWSDCKKYDVTVFQYIGELCRYLC 319
Cdd:cd05940 106 AWRGGAfFAGSGGALPSDVLYTCLPLYHSTALIVGWSACLASGATLVIRKKFSASNFWDDIRKYQATIFQYIGELCRYLL 185
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966209822 320 KQSKREGEKDHKVRLAIGNGIRSDVWREFLDRFGNIKVCELYAATESSISFMNYTGRIGAIGRTNLFYKLLSTFDLIKYD 399
Cdd:cd05940 186 NQPPKPTERKHKVRMIFGNGLRPDIWEEFKERFGVPRIAEFYAATEGNSGFINFFGKPGAIGRNPSLLRKVAPLALVKYD 265
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966209822 400 FQKDEPMRNEQGWCIHVKKGEPGLLISRVNAKNPFFGYAGPYKHTKdKLLCDVFKKGDVYLNTGDLIVQDQDNFLYFWDR 479
Cdd:cd05940 266 LESGEPIRDAEGRCIKVPRGEPGLLISRINPLEPFDGYTDPAATEK-KILRDVFKKGDAWFNTGDLMRLDGEGFWYFVDR 344
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966209822 480 TGDTFRWKGENVATTEVADVIGMLDFIQEANVYGVAISGYEGRAGMASIILKPNTSLDLEKVYEQVVTFLPAYACPRFLR 559
Cdd:cd05940 345 LGDTFRWKGENVSTTEVAAVLGAFPGVEEANVYGVQVPGTDGRAGMAAIVLQPNEEFDLSALAAHLEKNLPGYARPLFLR 424
|
490 500
....*....|....*....|....*
gi 966209822 560 IQEKMEATGTFKLLKHQLVEDGFNP 584
Cdd:cd05940 425 LQPEMEITGTFKQQKVDLRNEGFDP 449
|
|
| hsFATP4_like |
cd05939 |
Fatty acid transport proteins (FATP), including FATP4 and FATP1, and similar proteins; Fatty ... |
80-584 |
1.34e-168 |
|
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: 488.86 E-value: 1.34e-168
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966209822 80 YTYQDVDKRSSRVAHVFLNHSsLKKGDTVALLMSNEPDFVHVWFGLAKLGCVVAFLNTNIRSNSLLNCIRACGPRALVVG 159
Cdd:cd05939 4 WTFRELNEYSNKVANFFQAQG-YRSGDVVALFMENRLEFVALWLGLAKIGVETALINSNLRLESLLHCITVSKAKALIFN 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966209822 160 --ADLLGTVEEILPSLsenisvwgmkdsvpqgvislkeklstspdepVPRSHHvvsllkSTCLYIFTSGTTGLPKAAVIS 237
Cdd:cd05939 83 llDPLLTQSSTEPPSQ-------------------------------DDVNFR------DKLFYIYTSGTTGLPKAAVIV 125
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966209822 238 QLQVLRGSA-VLWAFGCTAHDIVYITLPLYHSSAAILGISGCVELGATCVLKKKFSASQFWSDCKKYDVTVFQYIGELCR 316
Cdd:cd05939 126 HSRYYRIAAgAYYAFGMRPEDVVYDCLPLYHSAGGIMGVGQALLHGSTVVIRKKFSASNFWDDCVKYNCTIVQYIGEICR 205
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966209822 317 YLCKQSKREGEKDHKVRLAIGNGIRSDVWREFLDRFGNIKVCELYAATESSISFMNYTGRIGAIGRTNLFYKLLSTFDLI 396
Cdd:cd05939 206 YLLAQPPSEEEQKHNVRLAVGNGLRPQIWEQFVRRFGIPQIGEFYGATEGNSSLVNIDNHVGACGFNSRILPSVYPIRLI 285
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966209822 397 KYDFQKDEPMRNEQGWCIHVKKGEPGLLISRVNAKNP---FFGYAGPyKHTKDKLLCDVFKKGDVYLNTGDLIVQDQDNF 473
Cdd:cd05939 286 KVDEDTGELIRDSDGLCIPCQPGEPGLLVGKIIQNDPlrrFDGYVNE-GATNKKIARDVFKKGDSAFLSGDVLVMDELGY 364
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966209822 474 LYFWDRTGDTFRWKGENVATTEVADVIGMLDFIQEANVYGVAISGYEGRAGMASIIlKPNTSLDLEKVYEQVVTFLPAYA 553
Cdd:cd05939 365 LYFKDRTGDTFRWKGENVSTTEVEGILSNVLGLEDVVVYGVEVPGVEGRAGMAAIV-DPERKVDLDRFSAVLAKSLPPYA 443
|
490 500 510
....*....|....*....|....*....|.
gi 966209822 554 CPRFLRIQEKMEATGTFKLLKHQLVEDGFNP 584
Cdd:cd05939 444 RPQFIRLLPEVDKTGTFKLQKTDLQKEGYDP 474
|
|
| FATP_chFAT1_like |
cd05937 |
Uncharacterized subfamily of bifunctional fatty acid transporter/very-long-chain acyl-CoA ... |
75-584 |
1.44e-144 |
|
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: 427.23 E-value: 1.44e-144
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966209822 75 YEGDIYTYQDVDKRSSRVAHVFLNHSSLKKGDTVALLMSNEPDFVHVWFGLAKLGCVVAFLNTNIRSNSLLNCIRACGPR 154
Cdd:cd05937 1 FEGKTWTYSETYDLVLRYAHWLHDDLGVQAGDFVAIDLTNSPEFVFLWLGLWSIGAAPAFINYNLSGDPLIHCLKLSGSR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966209822 155 ALVVgadllgtveeilpslsenisvwgmkdsvpqgvislkeklstSPDEPvprshhvvsllkstCLYIFTSGTTGLPKAA 234
Cdd:cd05937 81 FVIV-----------------------------------------DPDDP--------------AILIYTSGTTGLPKAA 105
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966209822 235 VISQLQVLRGSAVL-WAFGCTAHDIVYITLPLYHSSAAILGISGCVELGATCVLKKKFSASQFWSDCKKYDVTVFQYIGE 313
Cdd:cd05937 106 AISWRRTLVTSNLLsHDLNLKNGDRTYTCMPLYHGTAAFLGACNCLMSGGTLALSRKFSASQFWKDVRDSGATIIQYVGE 185
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966209822 314 LCRYLCKQSKREGEKDHKVRLAIGNGIRSDVWREFLDRFGNIKVCELYAATESSISFMNY-TG--RIGAIGRTNLFYKLL 390
Cdd:cd05937 186 LCRYLLSTPPSPYDRDHKVRVAWGNGLRPDIWERFRERFNVPEIGEFYAATEGVFALTNHnVGdfGAGAIGHHGLIRRWK 265
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966209822 391 STFD--LIKYDFQKDEP-MRNEQGWCIHVKKGEPGLLISRVNAKN--PFFGYAGPYKHTKDKLLCDVFKKGDVYLNTGDL 465
Cdd:cd05937 266 FENQvvLVKMDPETDDPiRDPKTGFCVRAPVGEPGEMLGRVPFKNreAFQGYLHNEDATESKLVRDVFRKGDIYFRTGDL 345
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966209822 466 IVQDQDNFLYFWDRTGDTFRWKGENVATTEVADVIGMLDFIQEANVYGVAISGYEGRAGMASIILKPNTSLDLEKVYEQV 545
Cdd:cd05937 346 LRQDADGRWYFLDRLGDTFRWKSENVSTTEVADVLGAHPDIAEANVYGVKVPGHDGRAGCAAITLEESSAVPTEFTKSLL 425
|
490 500 510 520
....*....|....*....|....*....|....*....|...
gi 966209822 546 VTF----LPAYACPRFLRIQEKMEATGTFKLLKHQLVEDGFNP 584
Cdd:cd05937 426 ASLarknLPSYAVPLFLRLTEEVATTDNHKQQKGVLRDEGVDP 468
|
|
| FACL_DitJ_like |
cd05934 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
77-577 |
6.17e-82 |
|
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: 264.15 E-value: 6.17e-82
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966209822 77 GDIYTYQDVDKRSSRVAHVFLNHSsLKKGDTVALLMSNEPDFVHVWFGLAKLGCVVAFLNTNIRSNSLLNCIRACGPRAL 156
Cdd:cd05934 1 GRRWTYAELLRESARIAAALAALG-IRPGDRVALMLDNCPEFLFAWFALAKLGAVLVPINTALRGDELAYIIDHSGAQLV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966209822 157 VVgadllgtveeilpslsenisvwgmkdsvpqgvislkeklstspdepvprshhvvsllkSTCLYIFTSGTTGLPKAAVI 236
Cdd:cd05934 80 VV----------------------------------------------------------DPASILYTSGTTGPPKGVVI 101
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966209822 237 SQLQVLRGSAVL-WAFGCTAHDIVYITLPLYHSSAAILGISGCVELGATCVLKKKFSASQFWSDCKKYDVTVFQYIGELC 315
Cdd:cd05934 102 THANLTFAGYYSaRRFGLGEDDVYLTVLPLFHINAQAVSVLAALSVGATLVLLPRFSASRFWSDVRRYGATVTNYLGAML 181
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966209822 316 RYLCKQSKREGEKDHKVRLAIGNGIRSDVWREFLDRFGnIKVCELYAATESSISFMN---YTGRIGAIGRtnlfykLLST 392
Cdd:cd05934 182 SYLLAQPPSPDDRAHRLRAAYGAPNPPELHEEFEERFG-VRLLEGYGMTETIVGVIGprdEPRRPGSIGR------PAPG 254
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966209822 393 FDLIKYDFQkDEPMRNeqgwcihvkkGEPG-LLISRVNAKNPFFGYagpYKHTKDKLlcDVFKKGdvYLNTGDLIVQDQD 471
Cdd:cd05934 255 YEVRIVDDD-GQELPA----------GEPGeLVIRGLRGWGFFKGY---YNMPEATA--EAMRNG--WFHTGDLGYRDAD 316
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966209822 472 NFLYFWDRTGDTFRWKGENVATTEVADVIGMLDFIQEANVYGVAiSGYEGRAGMASIILKPNTSLDLEKVYEQVVTFLPA 551
Cdd:cd05934 317 GFFYFVDRKKDMIRRRGENISSAEVERAILRHPAVREAAVVAVP-DEVGEDEVKAVVVLRPGETLDPEELFAFCEGQLAY 395
|
490 500
....*....|....*....|....*.
gi 966209822 552 YACPRFLRIQEKMEATGTFKLLKHQL 577
Cdd:cd05934 396 FKVPRYIRFVDDLPKTPTEKVAKAQL 421
|
|
| MenE/FadK |
COG0318 |
O-succinylbenzoic acid-CoA ligase MenE or related acyl-CoA synthetase (AMP-forming) [Lipid ... |
56-579 |
1.17e-77 |
|
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: 253.58 E-value: 1.17e-77
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966209822 56 VLDKFLSHAKRQPRKPFIIYEGDIYTYQDVDKRSSRVAHVFLNHSsLKKGDTVALLMSNEPDFVHVWFGLAKLGCVVAFL 135
Cdd:COG0318 1 LADLLRRAAARHPDRPALVFGGRRLTYAELDARARRLAAALRALG-VGPGDRVALLLPNSPEFVVAFLAALRAGAVVVPL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966209822 136 NTNIRSNSLLNCIRACGPRALVvgadllgtveeilpslsenisvwgmkdsvpqgvislkeklstspdepvprshhvvsll 215
Cdd:COG0318 80 NPRLTAEELAYILEDSGARALV---------------------------------------------------------- 101
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966209822 216 ksTCLYIFTSGTTGLPKAAVISQLQVLR-GSAVLWAFGCTAHDIVYITLPLYHSSAAILGISGCVELGATCVLKKKFSAS 294
Cdd:COG0318 102 --TALILYTSGTTGRPKGVMLTHRNLLAnAAAIAAALGLTPGDVVLVALPLFHVFGLTVGLLAPLLAGATLVLLPRFDPE 179
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966209822 295 QFWSDCKKYDVTVFQYIGELCRYLCKQSKREGEKDHKVRLAI--GNGIRSDVWREFLDRFGnIKVCELYAATESS-ISFM 371
Cdd:COG0318 180 RVLELIERERVTVLFGVPTMLARLLRHPEFARYDLSSLRLVVsgGAPLPPELLERFEERFG-VRIVEGYGLTETSpVVTV 258
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966209822 372 N----YTGRIGAIGRtnlfykllstfdlikydfqkdePM-------RNEQGwcIHVKKGEPGLLISRvnAKNPFFGYAGp 440
Cdd:COG0318 259 NpedpGERRPGSVGR----------------------PLpgvevriVDEDG--RELPPGEVGEIVVR--GPNVMKGYWN- 311
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966209822 441 ykhtKDKLLCDVFKKGdvYLNTGDLIVQDQDNFLYFWDRTGDTFRWKGENVATTEVADVIGMLDFIQEANVYGVAiSGYE 520
Cdd:COG0318 312 ----DPEATAEAFRDG--WLRTGDLGRLDEDGYLYIVGRKKDMIISGGENVYPAEVEEVLAAHPGVAEAAVVGVP-DEKW 384
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*....
gi 966209822 521 GRAGMASIILKPNTSLDLEKVYEQVVTFLPAYACPRFLRIQEKMEATGTFKLLKHQLVE 579
Cdd:COG0318 385 GERVVAFVVLRPGAELDAEELRAFLRERLARYKVPRRVEFVDELPRTASGKIDRRALRE 443
|
|
| PRK06155 |
PRK06155 |
crotonobetaine/carnitine-CoA ligase; Provisional |
64-584 |
2.01e-73 |
|
crotonobetaine/carnitine-CoA ligase; Provisional
Pssm-ID: 235719 [Multi-domain] Cd Length: 542 Bit Score: 245.44 E-value: 2.01e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966209822 64 AKRQPRKPFIIYEGDIYTYQDVDKRSSRVAHVfLNHSSLKKGDTVALLMSNEPDFVHVWFGLAKLGCVVAFLNTNIRSNS 143
Cdd:PRK06155 31 AERYPDRPLLVFGGTRWTYAEAARAAAAAAHA-LAAAGVKRGDRVALMCGNRIEFLDVFLGCAWLGAIAVPINTALRGPQ 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966209822 144 LLNCIRACGPRALVVGADLLGTVEEILPSLSENISVWgMKDSVPQGviSLKEKLSTSP----DEPVP----RSHHVVSLL 215
Cdd:PRK06155 110 LEHILRNSGARLLVVEAALLAALEAADPGDLPLPAVW-LLDAPASV--SVPAGWSTAPlpplDAPAPaaavQPGDTAAIL 186
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966209822 216 kstclyiFTSGTTGLPKAAVISQLQVL-RGSAVLWAFGCTAHDIVYITLPLYHSSAAILGISGCVElGATCVLKKKFSAS 294
Cdd:PRK06155 187 -------YTSGTTGPSKGVCCPHAQFYwWGRNSAEDLEIGADDVLYTTLPLFHTNALNAFFQALLA-GATYVLEPRFSAS 258
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966209822 295 QFWSDCKKYDVTVFQYIGELCRYLCKQSKREGEKDHKVRLAIGNGIRSDVWREFLDRFGnIKVCELYAATESSISFMNYT 374
Cdd:PRK06155 259 GFWPAVRRHGATVTYLLGAMVSILLSQPARESDRAHRVRVALGPGVPAALHAAFRERFG-VDLLDGYGSTETNFVIAVTH 337
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966209822 375 G--RIGAIGRtnlfykLLSTFDLIKYDFQKDEpmrneqgwcihVKKGEPGLLISRvnAKNPFF---GYAGPYKHTkdkll 449
Cdd:PRK06155 338 GsqRPGSMGR------LAPGFEARVVDEHDQE-----------LPDGEPGELLLR--ADEPFAfatGYFGMPEKT----- 393
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966209822 450 cdVFKKGDVYLNTGDLIVQDQDNFLYFWDRTGDTFRWKGENVATTEVADVIGMLDFIQEANVYGVAiSGYEGRAGMASII 529
Cdd:PRK06155 394 --VEAWRNLWFHTGDRVVRDADGWFRFVDRIKDAIRRRGENISSFEVEQVLLSHPAVAAAAVFPVP-SELGEDEVMAAVV 470
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*
gi 966209822 530 LKPNTSLDLEKVYEQVVTFLPAYACPRFLRIQEKMEATGTFKLLKHQLVEDGFNP 584
Cdd:PRK06155 471 LRDGTALEPVALVRHCEPRLAYFAVPRYVEFVAALPKTENGKVQKFVLREQGVTA 525
|
|
| AMP-binding |
pfam00501 |
AMP-binding enzyme; |
63-487 |
3.27e-54 |
|
AMP-binding enzyme;
Pssm-ID: 459834 [Multi-domain] Cd Length: 417 Bit Score: 190.22 E-value: 3.27e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966209822 63 HAKRQPRKP-FIIYEGDIYTYQDVDKRSSRVAHvFLNHSSLKKGDTVALLMSNEPDFVHVWFGLAKLGCVVAFLNTNIRS 141
Cdd:pfam00501 4 QAARTPDKTaLEVGEGRRLTYRELDERANRLAA-GLRALGVGKGDRVAILLPNSPEWVVAFLACLKAGAVYVPLNPRLPA 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966209822 142 NSLLNCIRACGPRALVV----GADLLGTVEEILPSLSENISVWGMKDSVPQGVISLKEKLSTSPDEPVPRSHHvvsllkS 217
Cdd:pfam00501 83 EELAYILEDSGAKVLITddalKLEELLEALGKLEVVKLVLVLDRDPVLKEEPLPEEAKPADVPPPPPPPPDPD------D 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966209822 218 TCLYIFTSGTTGLPKAAVISQLQVLRGSAVLW-----AFGCTAHDIVYITLPLYHSSAAILGISGCVELGATCVLKKKFS 292
Cdd:pfam00501 157 LAYIIYTSGTTGKPKGVMLTHRNLVANVLSIKrvrprGFGLGPDDRVLSTLPLFHDFGLSLGLLGPLLAGATVVLPPGFP 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966209822 293 A---SQFWSDCKKYDVTVFQYIGELCRYLCKQSKREGEKDHKVRLAI--GNGIRSDVWREFLDRFGNiKVCELYAATESS 367
Cdd:pfam00501 237 AldpAALLELIERYKVTVLYGVPTLLNMLLEAGAPKRALLSSLRLVLsgGAPLPPELARRFRELFGG-ALVNGYGLTETT 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966209822 368 ISFMNY------TGRIGAIGR--TNLFYKLLstfdlikydfqkDEPMRNEqgwcihVKKGEPG-LLISRVN-AKnpffGY 437
Cdd:pfam00501 316 GVVTTPlpldedLRSLGSVGRplPGTEVKIV------------DDETGEP------VPPGEPGeLCVRGPGvMK----GY 373
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|
gi 966209822 438 agpYKHtkDKLLCDVFKKGDvYLNTGDLIVQDQDNFLYFWDRTGDTFRWK 487
Cdd:pfam00501 374 ---LND--PELTAEAFDEDG-WYRTGDLGRRDEDGYLEIVGRKKDQIKLG 417
|
|
| PRK07867 |
PRK07867 |
acyl-CoA synthetase; Validated |
108-583 |
2.25e-53 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236120 [Multi-domain] Cd Length: 529 Bit Score: 191.05 E-value: 2.25e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966209822 108 VALLMSNEPDFVhVWFGLAKL-GCVVAFLNTNIRSNSLLNCIRACGPRALVVGADLLGTVEEILPSLsENISVwgmkDSV 186
Cdd:PRK07867 57 VGVLLDNTPEFS-LLLGAAALsGIVPVGLNPTRRGAALARDIAHADCQLVLTESAHAELLDGLDPGV-RVINV----DSP 130
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966209822 187 PqgvisLKEKLSTSPDEPVPRShhvVSLLKSTCLYIFTSGTTGLPKAAVISQLQV-LRGSAVLWAFGCTAHDIVYITLPL 265
Cdd:PRK07867 131 A-----WADELAAHRDAEPPFR---VADPDDLFMLIFTSGTSGDPKAVRCTHRKVaSAGVMLAQRFGLGPDDVCYVSMPL 202
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966209822 266 YHSSAAILGISGCVELGATCVLKKKFSASQFWSDCKKYDVTVFQYIGELCRYLCKQSKREGEKDHKVRLAIGN-GIRSDV 344
Cdd:PRK07867 203 FHSNAVMAGWAVALAAGASIALRRKFSASGFLPDVRRYGATYANYVGKPLSYVLATPERPDDADNPLRIVYGNeGAPGDI 282
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966209822 345 wREFLDRFGnIKVCELYAATESSISFMNYTG-RIGAIGRtnlfykllSTFDLIKYDFQKDEPM-RNEQGWCIHVKKGEP- 421
Cdd:PRK07867 283 -ARFARRFG-CVVVDGFGSTEGGVAITRTPDtPPGALGP--------LPPGVAIVDPDTGTECpPAEDADGRLLNADEAi 352
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966209822 422 GLLISrVNAKNPFFGYagpYKH---TKDKLlcdvfkKGDVYlNTGDLIVQDQDNFLYFWDRTGDTFRWKGENVATTEVAD 498
Cdd:PRK07867 353 GELVN-TAGPGGFEGY---YNDpeaDAERM------RGGVY-WSGDLAYRDADGYAYFAGRLGDWMRVDGENLGTAPIER 421
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966209822 499 VIGMLDFIQEANVYGV---AIsgyeGRAGMASIILKPNTSLDLEKVYEqvvtFLPAYA------CPRFLRIQEKMEATGT 569
Cdd:PRK07867 422 ILLRYPDATEVAVYAVpdpVV----GDQVMAALVLAPGAKFDPDAFAE----FLAAQPdlgpkqWPSYVRVCAELPRTAT 493
|
490
....*....|....
gi 966209822 570 FKLLKHQLVEDGFN 583
Cdd:PRK07867 494 FKVLKRQLSAEGVD 507
|
|
| caiC |
PRK08008 |
putative crotonobetaine/carnitine-CoA ligase; Validated |
64-577 |
1.86e-50 |
|
putative crotonobetaine/carnitine-CoA ligase; Validated
Pssm-ID: 181195 [Multi-domain] Cd Length: 517 Bit Score: 182.57 E-value: 1.86e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966209822 64 AKRQPRKPFIIYE---GDI--YTYQDVDKRSSRVAHVFLNhSSLKKGDTVALLMSNEPDFVHVWFGLAKLGCVVAFLNTN 138
Cdd:PRK08008 17 ADVYGHKTALIFEssgGVVrrYSYLELNEEINRTANLFYS-LGIRKGDKVALHLDNCPEFIFCWFGLAKIGAIMVPINAR 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966209822 139 IRSNSLLNCIRACGPRALVVGADLLGTVEEILPSLS---ENISVWGMKDSVPQGVISLKEKLSTSPDEpvpRSHHVVSLL 215
Cdd:PRK08008 96 LLREESAWILQNSQASLLVTSAQFYPMYRQIQQEDAtplRHICLTRVALPADDGVSSFTQLKAQQPAT---LCYAPPLST 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966209822 216 KSTCLYIFTSGTTGLPKAAVISQLQVL-RGSAVLWAFGCTAHDIVYITLPLYHS----SAAILGISgcveLGATCVLKKK 290
Cdd:PRK08008 173 DDTAEILFTSGTTSRPKGVVITHYNLRfAGYYSAWQCALRDDDVYLTVMPAFHIdcqcTAAMAAFS----AGATFVLLEK 248
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966209822 291 FSASQFWSDCKKYDVTVFQYIGELCRYLCKQSKREGEKDHKVR-----LAIGNGIRSDvwreFLDRFGnIKVCELYAATE 365
Cdd:PRK08008 249 YSARAFWGQVCKYRATITECIPMMIRTLMVQPPSANDRQHCLRevmfyLNLSDQEKDA----FEERFG-VRLLTSYGMTE 323
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966209822 366 SSIsfmnytGRIG----------AIGRTNLFYKLLSTfdlikyDFQKDEPMRNEQG-WCIhvkKGEPGllisrvnaKNPF 434
Cdd:PRK08008 324 TIV------GIIGdrpgdkrrwpSIGRPGFCYEAEIR------DDHNRPLPAGEIGeICI---KGVPG--------KTIF 380
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966209822 435 FGYAGPYKHTKDKLlcdvfkKGDVYLNTGDLIVQDQDNFLYFWDRTGDTFRWKGENVATTEVADVIGMLDFIQEANVYGV 514
Cdd:PRK08008 381 KEYYLDPKATAKVL------EADGWLHTGDTGYVDEEGFFYFVDRRCNMIKRGGENVSCVELENIIATHPKIQDIVVVGI 454
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 966209822 515 AISgYEGRAGMASIILKPNTSLDLEKVYEQVVTFLPAYACPRFLRIQEKMEATGTFKLLKHQL 577
Cdd:PRK08008 455 KDS-IRDEAIKAFVVLNEGETLSEEEFFAFCEQNMAKFKVPSYLEIRKDLPRNCSGKIIKKNL 516
|
|
| PRK13388 |
PRK13388 |
acyl-CoA synthetase; Provisional |
64-581 |
7.77e-48 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 237374 [Multi-domain] Cd Length: 540 Bit Score: 175.99 E-value: 7.77e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966209822 64 AKRQPRKPFIIYEGDIYTYQDVDKRSSRVAHVFlnhSSLKKGDT---VALLMSNEPDFVhVWFGLAKL-GCVVAFLNTNI 139
Cdd:PRK13388 11 DRAGDDTIAVRYGDRTWTWREVLAEAAARAAAL---IALADPDRplhVGVLLGNTPEML-FWLAAAALgGYVLVGLNTTR 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966209822 140 RSNSLLNCIRACGPRALVV---GADLLGTVEeiLPSLSENISvwgmkdSVPQGVISLKEKLSTSPDEPVPRSHhvvsllk 216
Cdd:PRK13388 87 RGAALAADIRRADCQLLVTdaeHRPLLDGLD--LPGVRVLDV------DTPAYAELVAAAGALTPHREVDAMD------- 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966209822 217 sTCLYIFTSGTTGLPKAAVISQLQVLR-GSAVLWAFGCTAHDIVYITLPLYHSSAAILGISGCVELGATCVLKKKFSASQ 295
Cdd:PRK13388 152 -PFMLIFTSGTTGAPKAVRCSHGRLAFaGRALTERFGLTRDDVCYVSMPLFHSNAVMAGWAPAVASGAAVALPAKFSASG 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966209822 296 FWSDCKKYDVTVFQYIGELCRYLCKQSKREGEKDHKVRLAIGNGIRSDVWREFLDRFGnIKVCELYAATESSISFMNYTG 375
Cdd:PRK13388 231 FLDDVRRYGATYFNYVGKPLAYILATPERPDDADNPLRVAFGNEASPRDIAEFSRRFG-CQVEDGYGSSEGAVIVVREPG 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966209822 376 R-IGAIGRtnlfykllSTFDLIKYDFQKDEPmrneqgwCIHVKKGEPGLLISR-------VNAKNP--FFGYagpYKHtk 445
Cdd:PRK13388 310 TpPGSIGR--------GAPGVAIYNPETLTE-------CAVARFDAHGALLNAdeaigelVNTAGAgfFEGY---YNN-- 369
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966209822 446 DKLLCDVFKKGDVYlnTGDLIVQDQDNFLYFWDRTGDTFRWKGENVATTEVADVIGMLDFIQEANVYGVAiSGYEGRAGM 525
Cdd:PRK13388 370 PEATAERMRHGMYW--SGDLAYRDADGWIYFAGRTADWMRVDGENLSAAPIERILLRHPAINRVAVYAVP-DERVGDQVM 446
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 966209822 526 ASIILKPNTSLDLekvyEQVVTFLPAY------ACPRFLRIQEKMEATGTFKLLKHQLVEDG 581
Cdd:PRK13388 447 AALVLRDGATFDP----DAFAAFLAAQpdlgtkAWPRYVRIAADLPSTATNKVLKRELIAQG 504
|
|
| AFD_class_I |
cd04433 |
Adenylate forming domain, Class I, also known as the ANL superfamily; This family is known as ... |
218-573 |
8.57e-47 |
|
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: 167.85 E-value: 8.57e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966209822 218 TCLYIFTSGTTGLPKAAVISQLQVLRGSA-VLWAFGCTAHDIVYITLPLYHsSAAILGISGCVELGATCVLKKKFSASQF 296
Cdd:cd04433 2 PALILYTSGTTGKPKGVVLSHRNLLAAAAaLAASGGLTEGDVFLSTLPLFH-IGGLFGLLGALLAGGTVVLLPKFDPEAA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966209822 297 WSDCKKYDVTVFQYIGELCRYLCKQSKREGEKDHKVRLAIGNG--IRSDVWREFLDRFGnIKVCELYAATESSISFMNYT 374
Cdd:cd04433 81 LELIEREKVTILLGVPTLLARLLKAPESAGYDLSSLRALVSGGapLPPELLERFEEAPG-IKLVNGYGLTETGGTVATGP 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966209822 375 G-----RIGAIGRtnlfykllstfdlikydfqkdePM-------RNEQGwcIHVKKGEPGLLisRVNAKNPFFGYAGPYK 442
Cdd:cd04433 160 PdddarKPGSVGR----------------------PVpgvevriVDPDG--GELPPGEIGEL--VVRGPSVMKGYWNNPE 213
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966209822 443 HTKdkllcdvFKKGDVYLNTGDLIVQDQDNFLYFWDRTGDTFRWKGENVATTEVADVIGMLDFIQEANVYGVAiSGYEGR 522
Cdd:cd04433 214 ATA-------AVDEDGWYRTGDLGRLDEDGYLYIVGRLKDMIKSGGENVYPAEVEAVLLGHPGVAEAAVVGVP-DPEWGE 285
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|.
gi 966209822 523 AGMASIILKPNTSLDLEKVYEQVVTFLPAYACPRFLRIQEKMEATGTFKLL 573
Cdd:cd04433 286 RVVAVVVLRPGADLDAEELRAHVRERLAPYKVPRRVVFVDALPRTASGKID 336
|
|
| FC-FACS_FadD_like |
cd05936 |
Prokaryotic long-chain fatty acid CoA synthetases similar to Escherichia coli FadD; This ... |
56-578 |
4.18e-44 |
|
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: 163.89 E-value: 4.18e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966209822 56 VLDKFLSHAKRQPRKPFIIYEGDIYTYQDVDKRSSRVAhVFLNHSSLKKGDTVALLMSNEPDFVHVWFGLAKLGCVVAFL 135
Cdd:cd05936 1 LADLLEEAARRFPDKTALIFMGRKLTYRELDALAEAFA-AGLQNLGVQPGDRVALMLPNCPQFPIAYFGALKAGAVVVPL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966209822 136 NTNIRSNSLLNCIRACGPRALVVgadllgtveeilpslsenisvwgmkdsvpqgVISLKEKLST--SPDEPVPRSHHVVS 213
Cdd:cd05936 80 NPLYTPRELEHILNDSGAKALIV-------------------------------AVSFTDLLAAgaPLGERVALTPEDVA 128
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966209822 214 LLkstcLYifTSGTTGLPKAAVISQ-------LQVLRgsavlWAFGC-TAHDIVYITLPLYHSSAAILGISGCVELGATC 285
Cdd:cd05936 129 VL----QY--TSGTTGVPKGAMLTHrnlvanaLQIKA-----WLEDLlEGDDVVLAALPLFHVFGLTVALLLPLALGATI 197
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966209822 286 VLKKKFSASQFWSDCKKYDVTVF-----QYIGelcryLCKQSKREGEKDHKVRLAIGNG--IRSDVWREFLDRFGNiKVC 358
Cdd:cd05936 198 VLIPRFRPIGVLKEIRKHRVTIFpgvptMYIA-----LLNAPEFKKRDFSSLRLCISGGapLPVEVAERFEELTGV-PIV 271
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966209822 359 ELYAATESS--ISFMNYTG--RIGAIGrtnlfYKLLSTfdlikydfqkDEPMRNEQGwcIHVKKGEPGLLIsrVNAKNPF 434
Cdd:cd05936 272 EGYGLTETSpvVAVNPLDGprKPGSIG-----IPLPGT----------EVKIVDDDG--EELPPGEVGELW--VRGPQVM 332
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966209822 435 FGYAGPYKHTKdkllcDVFKKGdvYLNTGDLIVQDQDNFLYFWDRTGDTFRWKGENVATTEVADVIGMLDFIQEANVYGV 514
Cdd:cd05936 333 KGYWNRPEETA-----EAFVDG--WLRTGDIGYMDEDGYFFIVDRKKDMIIVGGFNVYPREVEEVLYEHPAVAEAAVVGV 405
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 966209822 515 AiSGYEGRAGMASIILKPNTSLDLEKVYEQVVTFLPAYACPRFLRIQEKMEATGTFKLLKHQLV 578
Cdd:cd05936 406 P-DPYSGEAVKAFVVLKEGASLTEEEIIAFCREQLAGYKVPRQVEFRDELPKSAVGKILRRELR 468
|
|
| FACL_FadD13-like |
cd17631 |
fatty acyl-CoA synthetase, including FadD13; This family contains fatty acyl-CoA synthetases, ... |
63-574 |
4.76e-43 |
|
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: 160.08 E-value: 4.76e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966209822 63 HAKRQPRKPFIIYEGDIYTYQDVDKRSSRVAHVfLNHSSLKKGDTVALLMSNEPDFVHVWFGLAKLGCVVAFLNTNIRSN 142
Cdd:cd17631 4 RARRHPDRTALVFGGRSLTYAELDERVNRLAHA-LRALGVAKGDRVAVLSKNSPEFLELLFAAARLGAVFVPLNFRLTPP 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966209822 143 SLLNCIRACGPRALVvgadllgtveeilpslsenisvwgmkdsvpqgvislkeklstspDEPvprshhvvsllkstCLYI 222
Cdd:cd17631 83 EVAYILADSGAKVLF--------------------------------------------DDL--------------ALLM 104
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966209822 223 FTSGTTGLPKAAVISQLQVL-RGSAVLWAFGCTAHDIVYITLPLYHSSAAILGISGCVELGATCVLKKKFSASQFWSDCK 301
Cdd:cd17631 105 YTSGTTGRPKGAMLTHRNLLwNAVNALAALDLGPDDVLLVVAPLFHIGGLGVFTLPTLLRGGTVVILRKFDPETVLDLIE 184
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966209822 302 KYDVTVFQYIGELCRYLCKQSKREGEKDHKVRLAIGNG--IRSDVWREFLDRfgNIKVCELYAATESS--ISFM---NYT 374
Cdd:cd17631 185 RHRVTSFFLVPTMIQALLQHPRFATTDLSSLRAVIYGGapMPERLLRALQAR--GVKFVQGYGMTETSpgVTFLspeDHR 262
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966209822 375 GRIGAIGRTNLF--YKLLstfdlikydfqkDEPMRNeqgwcihVKKGEPGLLISRvnAKNPFFGYagpykHTKDKLLCDV 452
Cdd:cd17631 263 RKLGSAGRPVFFveVRIV------------DPDGRE-------VPPGEVGEIVVR--GPHVMAGY-----WNRPEATAAA 316
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966209822 453 FKKGdvYLNTGDLIVQDQDNFLYFWDRTGDTFRWKGENVATTEVADVIGMLDFIQEANVYGVAiSGYEGRAGMASIILKP 532
Cdd:cd17631 317 FRDG--WFHTGDLGRLDEDGYLYIVDRKKDMIISGGENVYPAEVEDVLYEHPAVAEVAVIGVP-DEKWGEAVVAVVVPRP 393
|
490 500 510 520
....*....|....*....|....*....|....*....|..
gi 966209822 533 NTSLDLEKVYEQVVTFLPAYACPRFLRIQEKMEATGTFKLLK 574
Cdd:cd17631 394 GAELDEDELIAHCRERLARYKIPKSVEFVDALPRNATGKILK 435
|
|
| PRK06839 |
PRK06839 |
o-succinylbenzoate--CoA ligase; |
64-579 |
1.19e-39 |
|
o-succinylbenzoate--CoA ligase;
Pssm-ID: 168698 [Multi-domain] Cd Length: 496 Bit Score: 151.94 E-value: 1.19e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966209822 64 AKRQPRKPFIIYEGDIYTYQDVDKRSSRVAHVFLNHSSLKKGDTVALLMSNEPDFVHVWFGLAKLGCVVAFLNTNIRSNS 143
Cdd:PRK06839 12 AYLHPDRIAIITEEEEMTYKQLHEYVSKVAAYLIYELNVKKGERIAILSQNSLEYIVLLFAIAKVECIAVPLNIRLTENE 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966209822 144 LLNCIRACGPRALVVGADLLGTVEEILPSLSENISVWgmkdsvpqgVISLKEKLSTSPDEPVPRSHhvvsllKSTCLYIF 223
Cdd:PRK06839 92 LIFQLKDSGTTVLFVEKTFQNMALSMQKVSYVQRVIS---------ITSLKEIEDRKIDNFVEKNE------SASFIICY 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966209822 224 TSGTTGLPKAAVISQLQVLRGSA-VLWAFGCTAHDIVYITLPLYHSSAAILGISGCVELGATCVLKKKFSASQFWSDCKK 302
Cdd:PRK06839 157 TSGTTGKPKGAVLTQENMFWNALnNTFAIDLTMHDRSIVLLPLFHIGGIGLFAFPTLFAGGVIIVPRKFEPTKALSMIEK 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966209822 303 YDVTVFQYIGELCRYLCKQSKREGEKDHKVRLAIGNGIRS--DVWREFLDR---FGnikvcELYAATESSIS-FM----N 372
Cdd:PRK06839 237 HKVTVVMGVPTIHQALINCSKFETTNLQSVRWFYNGGAPCpeELMREFIDRgflFG-----QGFGMTETSPTvFMlseeD 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966209822 373 YTGRIGAIGRTNLFykllSTFDLIKYDFQKDEPmrneqgwcihvkkGEPGLLIsrVNAKNPFFGYAGPYKHTKDKLlcdv 452
Cdd:PRK06839 312 ARRKVGSIGKPVLF----CDYELIDENKNKVEV-------------GEVGELL--IRGPNVMKEYWNRPDATEETI---- 368
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966209822 453 fkkGDVYLNTGDLIVQDQDNFLYFWDRTGDTFRWKGENVATTEVADVIGMLDFIQEANVYGVAISGYeGRAGMASIILKP 532
Cdd:PRK06839 369 ---QDGWLCTGDLARVDEDGFVYIVGRKKEMIISGGENIYPLEVEQVINKLSDVYEVAVVGRQHVKW-GEIPIAFIVKKS 444
|
490 500 510 520
....*....|....*....|....*....|....*....|....*..
gi 966209822 533 NTSLDLEKVYEQVVTFLPAYACPRFLRIQEKMEATGTFKLLKHQLVE 579
Cdd:PRK06839 445 SSVLIEKDVIEHCRLFLAKYKIPKEIVFLKELPKNATGKIQKAQLVN 491
|
|
| PRK06187 |
PRK06187 |
long-chain-fatty-acid--CoA ligase; Validated |
55-580 |
1.82e-36 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 235730 [Multi-domain] Cd Length: 521 Bit Score: 143.02 E-value: 1.82e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966209822 55 TVLDKFLSHAKRQPRKPFIIYEGDIYTYQDVDKRSSRVAHVFLNhSSLKKGDTVALLMSNEPDFVHVWFGLAKLGCVVAF 134
Cdd:PRK06187 7 TIGRILRHGARKHPDKEAVYFDGRRTTYAELDERVNRLANALRA-LGVKKGDRVAVFDWNSHEYLEAYFAVPKIGAVLHP 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966209822 135 LNTNIRSNSLLNCIRACGPRALVVGADLLGTVEEILPSLsENISVW-----GMKDSVPQGVISLKEKLSTSPDEPVprsH 209
Cdd:PRK06187 86 INIRLKPEEIAYILNDAEDRVVLVDSEFVPLLAAILPQL-PTVRTVivegdGPAAPLAPEVGEYEELLAAASDTFD---F 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966209822 210 HVVSlLKSTCLYIFTSGTTGLPKAAVISQLQVLRGS-AVLWAFGCTAHDIVYITLPLYHSSAAILGISGcVELGATCVLK 288
Cdd:PRK06187 162 PDID-ENDAAAMLYTSGTTGHPKGVVLSHRNLFLHSlAVCAWLKLSRDDVYLVIVPMFHVHAWGLPYLA-LMAGAKQVIP 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966209822 289 KKFSASQFWSDCKKYDVTVF-------QYIGelcrylckQSKREGEKD-HKVRLAI--GNGIRSDVWREFLDRFGnIKVC 358
Cdd:PRK06187 240 RRFDPENLLDLIETERVTFFfavptiwQMLL--------KAPRAYFVDfSSLRLVIygGAALPPALLREFKEKFG-IDLV 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966209822 359 ELYAATESS--ISF-------MNYTGRIGAIGRTNLFYKLlstfDLIKYDfqkdepmRNEQGWCIhvkkGEPGLLISRvn 429
Cdd:PRK06187 311 QGYGMTETSpvVSVlppedqlPGQWTKRRSAGRPLPGVEA----RIVDDD-------GDELPPDG----GEVGEIIVR-- 373
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966209822 430 AKNPFFGYAGPYKHTKDKllcdvFKKGdvYLNTGDLIVQDQDNFLYFWDRTGDTFRWKGENVATTEVADVIGMLDFIQEA 509
Cdd:PRK06187 374 GPWLMQGYWNRPEATAET-----IDGG--WLHTGDVGYIDEDGYLYITDRIKDVIISGGENIYPRELEDALYGHPAVAEV 446
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 966209822 510 NVYGVAiSGYEGRAGMASIILKPNTSLDLEKVYEQVVTFLPAYACPRFLRIQEKMEATGTFKLLKHQLVED 580
Cdd:PRK06187 447 AVIGVP-DEKWGERPVAVVVLKPGATLDAKELRAFLRGRLAKFKLPKRIAFVDELPRTSVGKILKRVLREQ 516
|
|
| FACL_fum10p_like |
cd05926 |
Subfamily of fatty acid CoA ligase (FACL) similar to Fum10p of Gibberella moniliformis; FACL ... |
80-579 |
2.57e-36 |
|
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: 142.45 E-value: 2.57e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966209822 80 YTYQDVDKRSSRVAHvFLNHSSLKKGDTVALLMSNEPDFVHVWFGLAKLGCVVAFLNTNIRSNSLLNCIRACGPRALVVG 159
Cdd:cd05926 15 LTYADLAELVDDLAR-QLAALGIKKGDRVAIALPNGLEFVVAFLAAARAGAVVAPLNPAYKKAEFEFYLADLGSKLVLTP 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966209822 160 ADLLGTVEEILPSLSENISVWGMKDSVPQGVISlKEKLSTSPDEPVPRSHHVVSLLKSTCLYIFTSGTTGLPKAAVISQL 239
Cdd:cd05926 94 KGELGPASRAASKLGLAILELALDVGVLIRAPS-AESLSNLLADKKNAKSEGVPLPDDLALILHTSGTTGRPKGVPLTHR 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966209822 240 QVLR-GSAVLWAFGCTAHDIVYITLPLYHSSAAILGISGCVELGATCVLKKKFSASQFWSDCKKYDVTVFQYIGELCRYL 318
Cdd:cd05926 173 NLAAsATNITNTYKLTPDDRTLVVMPLFHVHGLVASLLSTLAAGGSVVLPPRFSASTFWPDVRDYNATWYTAVPTIHQIL 252
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966209822 319 CKQSKREGEK-DHKVRLaigngIRS-------DVWREFLDRFGnIKVCELYAATE-SSISFMN----YTGRIGAIGRTNl 385
Cdd:cd05926 253 LNRPEPNPESpPPKLRF-----IRScsaslppAVLEALEATFG-APVLEAYGMTEaAHQMTSNplppGPRKPGSVGKPV- 325
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966209822 386 fykllsTFDLIKYDfQKDEPMRNEQgwcihvkKGEpgllISrVNAKNPFFGYAGPYKHTKDKllcdvFKKGDvYLNTGDL 465
Cdd:cd05926 326 ------GVEVRILD-EDGEILPPGV-------VGE----IC-LRGPNVTRGYLNNPEANAEA-----AFKDG-WFRTGDL 380
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966209822 466 IVQDQDNFLYFWDRTGDTFRWKGENVATTEVADVIGMLDFIQEANVYGVAISGYeGRAGMASIILKPNTSLDLEKVYEQV 545
Cdd:cd05926 381 GYLDADGYLFLTGRIKELINRGGEKISPLEVDGVLLSHPAVLEAVAFGVPDEKY-GEEVAAAVVLREGASVTEEELRAFC 459
|
490 500 510
....*....|....*....|....*....|....
gi 966209822 546 VTFLPAYACPRFLRIQEKMEATGTFKLLKHQLVE 579
Cdd:cd05926 460 RKHLAAFKVPKKVYFVDELPKTATGKIQRRKVAE 493
|
|
| PRK07656 |
PRK07656 |
long-chain-fatty-acid--CoA ligase; Validated |
55-579 |
2.93e-35 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236072 [Multi-domain] Cd Length: 513 Bit Score: 139.65 E-value: 2.93e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966209822 55 TVLDKFLSHAKRQPRKPFIIYEGDIYTYQDVDKRSSRVAHVFLNHSsLKKGDTVALLMSNEPDFVHVWFGLAKLGCVVAF 134
Cdd:PRK07656 6 TLPELLARAARRFGDKEAYVFGDQRLTYAELNARVRRAAAALAALG-IGKGDRVAIWAPNSPHWVIAALGALKAGAVVVP 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966209822 135 LNTNIRSNSLLNCIRACGPRALVVGADLLGTVEEI---LPSLSENISV-WGMKDSVPQGVISLKEKLSTSPDEPVPRSHH 210
Cdd:PRK07656 85 LNTRYTADEAAYILARGDAKALFVLGLFLGVDYSAttrLPALEHVVICeTEEDDPHTEKMKTFTDFLAAGDPAERAPEVD 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966209822 211 V--VSLLkstclyIFTSGTTGLPKAAVISQLQVLRGSAVlWA--FGCTAHDIVYITLPLYHSSAAILGISGCVELGATCV 286
Cdd:PRK07656 165 PddVADI------LFTSGTTGRPKGAMLTHRQLLSNAAD-WAeyLGLTEGDRYLAANPFFHVFGYKAGVNAPLMRGATIL 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966209822 287 LKKKFSASQFWSDCKKYDVTVFQYIGELCRYLCKQSKREGEKDHKVRLAIGNG--IRSDVWREFLDRFGNIKVCELYAAT 364
Cdd:PRK07656 238 PLPVFDPDEVFRLIETERITVLPGPPTMYNSLLQHPDRSAEDLSSLRLAVTGAasMPVALLERFESELGVDIVLTGYGLS 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966209822 365 ESS-ISFMNYTGR-----IGAIGRTnlfykllstfdlIKyDFQkdepMR--NEQGWciHVKKGEPGLLIsrVNAKNPFFG 436
Cdd:PRK07656 318 EASgVTTFNRLDDdrktvAGTIGTA------------IA-GVE----NKivNELGE--EVPVGEVGELL--VRGPNVMKG 376
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966209822 437 YAGPYKHTKDKLlcdvfkKGDVYLNTGDLIVQDQDNFLYFWDRTGDTFRWKGENVATTEVADVIGMLDFIQEANVYGVAI 516
Cdd:PRK07656 377 YYDDPEATAAAI------DADGWLHTGDLGRLDEEGYLYIVDRKKDMFIVGGFNVYPAEVEEVLYEHPAVAEAAVIGVPD 450
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 966209822 517 SGYeGRAGMASIILKPNTSLDLEKVYEQVVTFLPAYACPRFLRIQEKM--EATGtfKLLKHQLVE 579
Cdd:PRK07656 451 ERL-GEVGKAYVVLKPGAELTEEELIAYCREHLAKYKVPRSIEFLDELpkNATG--KVLKRALRE 512
|
|
| Firefly_Luc_like |
cd05911 |
Firefly luciferase of light emitting insects and 4-Coumarate-CoA Ligase (4CL); This family ... |
76-552 |
5.15e-34 |
|
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: 135.42 E-value: 5.15e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966209822 76 EGDIYTYQDVDKRSSRVAHVFLNHSsLKKGDTVALLMSNEPDFVHVWFGLAKLGCVVAFLNTNIRSNSLLNCIRACGPRA 155
Cdd:cd05911 7 TGKELTYAQLRTLSRRLAAGLRKLG-LKKGDVVGIISPNSTYYPPVFLGCLFAGGIFSAANPIYTADELAHQLKISKPKV 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966209822 156 LVVGADLLGTVEEILPSLSENISVWGMKDSvPQGVISLKEKL---STSPDEPVPRshhVVSLLKSTCLYI-FTSGTTGLP 231
Cdd:cd05911 86 IFTDPDGLEKVKEAAKELGPKDKIIVLDDK-PDGVLSIEDLLsptLGEEDEDLPP---PLKDGKDDTAAIlYSSGTTGLP 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966209822 232 KAAVIS---QLQVLRGSAVLWAFGCTAHDIVYITLPLYHSSAAILGISGCVeLGATCVLKKKFSASQFWSDCKKYDVTVF 308
Cdd:cd05911 162 KGVCLShrnLIANLSQVQTFLYGNDGSNDVILGFLPLYHIYGLFTTLASLL-NGATVIIMPKFDSELFLDLIEKYKITFL 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966209822 309 QYIGELCRYLCKQSKREGEKDHKVRLAIGNGirSDVWREFLD----RFGNIKVCELYAATESS-ISFMNYTG--RIGAIG 381
Cdd:cd05911 241 YLVPPIAAALAKSPLLDKYDLSSLRVILSGG--APLSKELQEllakRFPNATIKQGYGMTETGgILTVNPDGddKPGSVG 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966209822 382 RtnlfykLLSTFdLIKYdfqKDEPMRNEQGwcihvkKGEPGLLIsrVNAKNPFFGYAGPYKHTKDKLlcdvFKKGdvYLN 461
Cdd:cd05911 319 R------LLPNV-EAKI---VDDDGKDSLG------PNEPGEIC--VRGPQVMKGYYNNPEATKETF----DEDG--WLH 374
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966209822 462 TGDLIVQDQDNFLYFWDRTGDTFRWKGENVATTEVADVIGMLDFIQEANVYGVAiSGYEGRAGMASIILKPNTSLDLEKV 541
Cdd:cd05911 375 TGDIGYFDEDGYLYIVDRKKELIKYKGFQVAPAELEAVLLEHPGVADAAVIGIP-DEVSGELPRAYVVRKPGEKLTEKEV 453
|
490
....*....|.
gi 966209822 542 YEQVVTFLPAY 552
Cdd:cd05911 454 KDYVAKKVASY 464
|
|
| Acs |
COG0365 |
Acyl-coenzyme A synthetase/AMP-(fatty) acid ligase [Lipid transport and metabolism]; |
56-556 |
1.78e-33 |
|
Acyl-coenzyme A synthetase/AMP-(fatty) acid ligase [Lipid transport and metabolism];
Pssm-ID: 440134 [Multi-domain] Cd Length: 565 Bit Score: 134.85 E-value: 1.78e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966209822 56 VLDKflsHAKRQPRKPFIIYEGD-----IYTYQDVDKRSSRVAHVFLNHSsLKKGDTVALLMSNEPDFVHVWFGLAKLGC 130
Cdd:COG0365 14 CLDR---HAEGRGDKVALIWEGEdgeerTLTYAELRREVNRFANALRALG-VKKGDRVAIYLPNIPEAVIAMLACARIGA 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966209822 131 VVAFLNTNIRSNSLLNCIRACGPRALVVGA---------DLLGTVEEILPSLS--ENISVWG--MKDSVPQGVISLKEKL 197
Cdd:COG0365 90 VHSPVFPGFGAEALADRIEDAEAKVLITADgglrggkviDLKEKVDEALEELPslEHVIVVGrtGADVPMEGDLDWDELL 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966209822 198 STSPD----EPVPRSHhvvsllksTCLYIFTSGTTGLPKAAVISQ---LQVLRGSAVLWaFGCTAHDIVYitlplyhsSA 270
Cdd:COG0365 170 AAASAefepEPTDADD--------PLFILYTSGTTGKPKGVVHTHggyLVHAATTAKYV-LDLKPGDVFW--------CT 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966209822 271 A----ILGISGCV----ELGATCVL---KKKF-SASQFWSDCKKYDVTVFqyigelcrY-------LCKQSKREGEKDH- 330
Cdd:COG0365 233 AdigwATGHSYIVygplLNGATVVLyegRPDFpDPGRLWELIEKYGVTVF--------FtaptairALMKAGDEPLKKYd 304
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966209822 331 --KVRLAIGNG--IRSDVWREFLDRFGnIKVCELYAATESSISFMNYTG----RIGAIGRTNLFYKLlstfDLIkydfqk 402
Cdd:COG0365 305 lsSLRLLGSAGepLNPEVWEWWYEAVG-VPIVDGWGQTETGGIFISNLPglpvKPGSMGKPVPGYDV----AVV------ 373
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966209822 403 depmrNEQGwcIHVKKGEPGLLIsrVNAKNP--FFGYAGPYKHTKDKLLcDVFKkgDVYLnTGDLIVQDQDNFLYFWDRT 480
Cdd:COG0365 374 -----DEDG--NPVPPGEEGELV--IKGPWPgmFRGYWNDPERYRETYF-GRFP--GWYR-TGDGARRDEDGYFWILGRS 440
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966209822 481 GDTFRWKGENVATTEVADVIGMLDFIQEANVYGVAisgYEGRaGM---ASIILKPNTSLD--LEK-VYEQVVTFLPAYAC 554
Cdd:COG0365 441 DDVINVSGHRIGTAEIESALVSHPAVAEAAVVGVP---DEIR-GQvvkAFVVLKPGVEPSdeLAKeLQAHVREELGPYAY 516
|
..
gi 966209822 555 PR 556
Cdd:COG0365 517 PR 518
|
|
| PRK08316 |
PRK08316 |
acyl-CoA synthetase; Validated |
64-580 |
6.27e-32 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 181381 [Multi-domain] Cd Length: 523 Bit Score: 130.05 E-value: 6.27e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966209822 64 AKRQPRKPFIIYEGDIYTYQDVDKRSSRVAHVFLNhSSLKKGDTVALLMSNEPDFVHVWFGLAKLGCVVAFLNTNIRSNS 143
Cdd:PRK08316 21 ARRYPDKTALVFGDRSWTYAELDAAVNRVAAALLD-LGLKKGDRVAALGHNSDAYALLWLACARAGAVHVPVNFMLTGEE 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966209822 144 LLNCIRACGPRALVVGADLLGTVEEILPSLSENISVW---GMKDSVPQGVISLKEKLSTSPD---EPVPRSHHVVSLLks 217
Cdd:PRK08316 100 LAYILDHSGARAFLVDPALAPTAEAALALLPVDTLILslvLGGREAPGGWLDFADWAEAGSVaepDVELADDDLAQIL-- 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966209822 218 tclyiFTSGTTGLPKAAVISQlqvlrgSAVLW-------AFGCTAHDIVYITLPLYHSSAAILGISGCVELGATCVLKKK 290
Cdd:PRK08316 178 -----YTSGTESLPKGAMLTH------RALIAeyvscivAGDMSADDIPLHALPLYHCAQLDVFLGPYLYVGATNVILDA 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966209822 291 FSASQFWSDCKKYDVTVF-----QYIGELcrylckqskREGEKDhKVRLA------IGNGIRS-DVWREFLDRFGNIKVC 358
Cdd:PRK08316 247 PDPELILRTIEAERITSFfapptVWISLL---------RHPDFD-TRDLSslrkgyYGASIMPvEVLKELRERLPGLRFY 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966209822 359 ELYAATE-----SSISFMNYTGRIGAIGRTNLFY--KLLstfdlikydfqkDEPMRNeqgwcihVKKGEPGLLISRvnak 431
Cdd:PRK08316 317 NCYGQTEiaplaTVLGPEEHLRRPGSAGRPVLNVetRVV------------DDDGND-------VAPGEVGEIVHR---- 373
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966209822 432 NP--FFGYAGPYKHTKdkllcDVFKKGdvYLNTGDLIVQDQDNFLYFWDRTGDTFRWKGENVATTEVADVIGMLDFIQEA 509
Cdd:PRK08316 374 SPqlMLGYWDDPEKTA-----EAFRGG--WFHSGDLGVMDEEGYITVVDRKKDMIKTGGENVASREVEEALYTHPAVAEV 446
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 966209822 510 NVYGV-------AISgyegragmASIILKPNTSLDLEKVYEQVVTFLPAYACPRFLRIQEKMEATGTFKLLKHQLVED 580
Cdd:PRK08316 447 AVIGLpdpkwieAVT--------AVVVPKAGATVTEDELIAHCRARLAGFKVPKRVIFVDELPRNPSGKILKRELRER 516
|
|
| PRK07868 |
PRK07868 |
acyl-CoA synthetase; Validated |
64-613 |
2.00e-31 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236121 [Multi-domain] Cd Length: 994 Bit Score: 130.61 E-value: 2.00e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966209822 64 AKRQPRKPFIIYEGDIYTYQDVDKRSSRVAHVFLNhSSLKKGDTVALLMSNEPDFVHVWFGLAKLGCVVAFLNtnirsns 143
Cdd:PRK07868 457 ARDAPKGEFLLFDGRVHTYEAVNRRINNVVRGLIA-VGVRQGDRVGVLMETRPSALVAIAALSRLGAVAVLMP------- 528
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966209822 144 llnciracgPRALVVGADLLGTVEEIL--PSLSENISVWGMKDSVPQGvislkeklSTSPDEPVPRSHHVVSL------- 214
Cdd:PRK07868 529 ---------PDTDLAAAVRLGGVTEIItdPTNLEAARQLPGRVLVLGG--------GESRDLDLPDDADVIDMekidpda 591
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966209822 215 ------------LKSTCLYIFTSGTTG--LPKaavisqlQVLRGSAVLWAFGcTA-------HDIVYITLPLYHSSAAIL 273
Cdd:PRK07868 592 velpgwyrpnpgLARDLAFIAFSTAGGelVAK-------QITNYRWALSAFG-TAsaaaldrRDTVYCLTPLHHESGLLV 663
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966209822 274 GISGCVELGATCVLKKKFSASQFWSDCKKYDVTVFQYIGELCRYLCKQSKREGEKDHKVRLAIGNGIRSDVWREFLDRFG 353
Cdd:PRK07868 664 SLGGAVVGGSRIALSRGLDPDRFVQEVRQYGVTVVSYTWAMLREVVDDPAFVLHGNHPVRLFIGSGMPTGLWERVVEAFA 743
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966209822 354 NIKVCELYAATESSISFMNYTG-RIGAIGRtnlfyKLLST--FDLIKYDFQKDEPMRNEQGWCIHVKKGEPGLLISRvna 430
Cdd:PRK07868 744 PAHVVEFFATTDGQAVLANVSGaKIGSKGR-----PLPGAgrVELAAYDPEHDLILEDDRGFVRRAEVNEVGVLLAR--- 815
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966209822 431 knpffgyAGPYKHTKDKLLCDVFKKGDVYLNTGDLIVQDQDNFLYFWDRTGDTFRWKGENVATTEVADVIGMLDFIQEAN 510
Cdd:PRK07868 816 -------ARGPIDPTASVKRGVFAPADTWISTEYLFRRDDDGDYWLVDRRGSVIRTARGPVYTEPVTDALGRIGGVDLAV 888
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966209822 511 VYGVAISGYEgrAGMASIILKPNTSLDLEKVYEqVVTFLPAYACPRFLRIQEKMEATGTFKLLKHQLVEDGFnPlKISEP 590
Cdd:PRK07868 889 TYGVEVGGRQ--LAVAAVTLRPGAAITAADLTE-ALASLPVGLGPDIVHVVPEIPLSATYRPTVSALRAAGI-P-KPGRQ 963
|
570 580
....*....|....*....|...
gi 966209822 591 LYFMDNLKKSYVLLTRELYDQIM 613
Cdd:PRK07868 964 AWYFDPETNRYRRLTPAVRAELT 986
|
|
| PRK07786 |
PRK07786 |
long-chain-fatty-acid--CoA ligase; Validated |
62-580 |
1.59e-26 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 169098 [Multi-domain] Cd Length: 542 Bit Score: 114.10 E-value: 1.59e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966209822 62 SHAKRQPRKPFIIYEGDIYTYQDVDKRSSRVAHVfLNHSSLKKGDTVALLMSNEPDFVHVWFGLAKLGCVVAFLNTNIRS 141
Cdd:PRK07786 25 RHALMQPDAPALRFLGNTTTWRELDDRVAALAGA-LSRRGVGFGDRVLILMLNRTEFVESVLAANMLGAIAVPVNFRLTP 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966209822 142 NSLLNCIRACGPRALVVG---ADLLGTVEEILPSLSENISVWGMKDSvpqGVISLkEKLSTSPDEPvprsHHVVSLLKST 218
Cdd:PRK07786 104 PEIAFLVSDCGAHVVVTEaalAPVATAVRDIVPLLSTVVVAGGSSDD---SVLGY-EDLLAEAGPA----HAPVDIPNDS 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966209822 219 -CLYIFTSGTTGLPKAAVISQLQvLRGSAV--LWAFGC-TAHDIVYITLPLYHsSAAILGISGCVELGATCVLK--KKFS 292
Cdd:PRK07786 176 pALIMYTSGTTGRPKGAVLTHAN-LTGQAMtcLRTNGAdINSDVGFVGVPLFH-IAGIGSMLPGLLLGAPTVIYplGAFD 253
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966209822 293 ASQFWSDCKKYDVTVFQYIGELCRYLCKQSKREGeKDHKVR-LAIGNGIRSD-VWREFLDRFGNIKVCELYAATE-SSIS 369
Cdd:PRK07786 254 PGQLLDVLEAEKVTGIFLVPAQWQAVCAEQQARP-RDLALRvLSWGAAPASDtLLRQMAATFPEAQILAAFGQTEmSPVT 332
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966209822 370 FM----NYTGRIGAIGrtnlfyKLLSTFDLIKYdfqkDEPMRNeqgwcihVKKGEPGLLISRvnAKNPFFGYAGPYKHTk 445
Cdd:PRK07786 333 CMllgeDAIRKLGSVG------KVIPTVAARVV----DENMND-------VPVGEVGEIVYR--APTLMSGYWNNPEAT- 392
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966209822 446 dkllCDVFKKGdvYLNTGDLIVQDQDNFLYFWDRTGDTFRWKGENVATTEVADVIGMLDFIQEANVYGVAISGYeGRAGM 525
Cdd:PRK07786 393 ----AEAFAGG--WFHSGDLVRQDEEGYVWVVDRKKDMIISGGENIYCAEVENVLASHPDIVEVAVIGRADEKW-GEVPV 465
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*.
gi 966209822 526 ASIILKP-NTSLDLEKVYEQVVTFLPAYACPRFLRIQEKMEATGTFKLLKHQLVED 580
Cdd:PRK07786 466 AVAAVRNdDAALTLEDLAEFLTDRLARYKHPKALEIVDALPRNPAGKVLKTELRER 521
|
|
| PRK06145 |
PRK06145 |
acyl-CoA synthetase; Validated |
63-577 |
3.47e-26 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 102207 [Multi-domain] Cd Length: 497 Bit Score: 112.29 E-value: 3.47e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966209822 63 HAKRQPRKPFIIYEGDIYTYQDVDKRSSRVAhVFLNHSSLKKGDTVALLMSNEPDFVHVWFGLAKLGCVVAFLNTNIRSN 142
Cdd:PRK06145 11 HARRTPDRAALVYRDQEISYAEFHQRILQAA-GMLHARGIGQGDVVALLMKNSAAFLELAFAASYLGAVFLPINYRLAAD 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966209822 143 SLLNCIRACGPRALVVGADLlgtveEILPSLSENISVWGMKDSVPQGVISlkeklstSPDEPVPRSHHVvsllKSTCLY- 221
Cdd:PRK06145 90 EVAYILGDAGAKLLLVDEEF-----DAIVALETPKIVIDAAAQADSRRLA-------QGGLEIPPQAAV----APTDLVr 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966209822 222 -IFTSGTTGLPKAAVISQLQVLRGSA-VLWAFGCTAHDIVYITLPLYHSSAAILGISGCVELGATCVLKKKFSASQFWSD 299
Cdd:PRK06145 154 lMYTSGTTDRPKGVMHSYGNLHWKSIdHVIALGLTASERLLVVGPLYHVGAFDLPGIAVLWVGGTLRIHREFDPEAVLAA 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966209822 300 CKKYDVTVFQYIGELCRYLCKQSKREGEKDHKVRLAIGNGIRSDVW--REFLDRFGNIKVCELYAATE--SSISFMNYTG 375
Cdd:PRK06145 234 IERHRLTCAWMAPVMLSRVLTVPDRDRFDLDSLAWCIGGGEKTPESriRDFTRVFTRARYIDAYGLTEtcSGDTLMEAGR 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966209822 376 RIGAIGRTNlfyKLLSTFDLikydfqkdEPMRNEQGWCIHVKKGEPGLLISRVNAknpffGYAGPYKHTKDKLLCDVFKK 455
Cdd:PRK06145 314 EIEKIGSTG---RALAHVEI--------RIADGAGRWLPPNMKGEICMRGPKVTK-----GYWKDPEKTAEAFYGDWFRS 377
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966209822 456 GDV-YLntgdlivqDQDNFLYFWDRTGDTFRWKGENVATTEVADVIGMLDFIQEANVYGVAISGYeGRAGMASIILKPNT 534
Cdd:PRK06145 378 GDVgYL--------DEEGFLYLTDRKKDMIISGGENIASSEVERVIYELPEVAEAAVIGVHDDRW-GERITAVVVLNPGA 448
|
490 500 510 520
....*....|....*....|....*....|....*....|...
gi 966209822 535 SLDLEKVYEQVVTFLPAYACPRFLRIQEKMEATGTFKLLKHQL 577
Cdd:PRK06145 449 TLTLEALDRHCRQRLASFKVPRQLKVRDELPRNPSGKVLKRVL 491
|
|
| PRK12406 |
PRK12406 |
long-chain-fatty-acid--CoA ligase; Provisional |
82-579 |
3.50e-26 |
|
long-chain-fatty-acid--CoA ligase; Provisional
Pssm-ID: 183506 [Multi-domain] Cd Length: 509 Bit Score: 112.48 E-value: 3.50e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966209822 82 YQDVDKRSSRVAHVfLNHSSLKKGDTVALLMSNEPDFVHVWFGLAKLGCVVAFLNTNIRSNSLLNCIRACGPRALVVGAD 161
Cdd:PRK12406 14 FDELAQRAARAAGG-LAALGVRPGDCVALLMRNDFAFFEAAYAAMRLGAYAVPVNWHFKPEEIAYILEDSGARVLIAHAD 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966209822 162 LLGTVEEILPS----LS-----ENISVWGMKD---SVPQGVISLKEKLSTSPDEPVPRSHHVVSLlkstclyIFTSGTTG 229
Cdd:PRK12406 93 LLHGLASALPAgvtvLSvptppEIAAAYRISPallTPPAGAIDWEGWLAQQEPYDGPPVPQPQSM-------IYTSGTTG 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966209822 230 LPK----AAVISQLQVLRGSAVLWAFGCTAHDIVYITLPLYHSSAAILGISGcVELGATCVLKKKFSASQFWSDCKKYDV 305
Cdd:PRK12406 166 HPKgvrrAAPTPEQAAAAEQMRALIYGLKPGIRALLTGPLYHSAPNAYGLRA-GRLGGVLVLQPRFDPEELLQLIERHRI 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966209822 306 TVFQYIGELCRYLCK--QSKREGEKDHKVRLAIGNGIR--SDVWREFLDRFGNIkVCELYAATESS-ISFMN---YTGRI 377
Cdd:PRK12406 245 THMHMVPTMFIRLLKlpEEVRAKYDVSSLRHVIHAAAPcpADVKRAMIEWWGPV-IYEYYGSTESGaVTFATsedALSHP 323
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966209822 378 GAIGrtnlfyKLLSTFDLIKYDfqkdepmrnEQGWciHVKKGEPGLLISRVnAKNPFFGYagpykHTKDKLLCDVFKKGd 457
Cdd:PRK12406 324 GTVG------KAAPGAELRFVD---------EDGR--PLPQGEIGEIYSRI-AGNPDFTY-----HNKPEKRAEIDRGG- 379
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966209822 458 vYLNTGDLIVQDQDNFLYFWDRTGDTFRWKGENVATTEVADVIGMLDFIQEANVYGVAISGYeGRAGMASIILKPNTSLD 537
Cdd:PRK12406 380 -FITSGDVGYLDADGYLFLCDRKRDMVISGGVNIYPAEIEAVLHAVPGVHDCAVFGIPDAEF-GEALMAVVEPQPGATLD 457
|
490 500 510 520
....*....|....*....|....*....|....*....|..
gi 966209822 538 LEKVYEQVVTFLPAYACPRFLRIQEKMEATGTFKLLKHQLVE 579
Cdd:PRK12406 458 EADIRAQLKARLAGYKVPKHIEIMAELPREDSGKIFKRRLRD 499
|
|
| PRK13391 |
PRK13391 |
acyl-CoA synthetase; Provisional |
63-579 |
3.51e-26 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 184022 [Multi-domain] Cd Length: 511 Bit Score: 112.48 E-value: 3.51e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966209822 63 HAKRQPRKP-FIIYE-GDIYTYQDVDKRSSRVAHVFLNHSsLKKGDTVALLMSNEPDFVHVWFGLAKLGCVVAFLNTNIR 140
Cdd:PRK13391 6 HAQTTPDKPaVIMAStGEVVTYRELDERSNRLAHLFRSLG-LKRGDHVAIFMENNLRYLEVCWAAERSGLYYTCVNSHLT 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966209822 141 SNSLLNCIRACGPRALVVGADLLGTVEEIL---PSLSENISVWGMKDSvpQGVISLKEKLSTSPDEPVPRSHHVVSLLKS 217
Cdd:PRK13391 85 PAEAAYIVDDSGARALITSAAKLDVARALLkqcPGVRHRLVLDGDGEL--EGFVGYAEAVAGLPATPIADESLGTDMLYS 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966209822 218 tclyiftSGTTGLPKA--------AVISQLQVLRGSAVLWAFGctaHDIVYI-TLPLYHS---SAAILGISgcveLGATC 285
Cdd:PRK13391 163 -------SGTTGRPKGikrplpeqPPDTPLPLTAFLQRLWGFR---SDMVYLsPAPLYHSapqRAVMLVIR----LGGTV 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966209822 286 VLKKKFSASQFWSDCKKYDVTVFQYIGEL-CRYLCKQSKREGEKDHK-VRLAIGNG--IRSDVWREFLDRFGNIkVCELY 361
Cdd:PRK13391 229 IVMEHFDAEQYLALIEEYGVTHTQLVPTMfSRMLKLPEEVRDKYDLSsLEVAIHAAapCPPQVKEQMIDWWGPI-IHEYY 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966209822 362 AATE----SSISFMNYTGRIGAIGRTnLFYKLLSTfdlikydfqkDEPMRNeqgwcihVKKGEPGLLisrvnaknpFFGY 437
Cdd:PRK13391 308 AATEglgfTACDSEEWLAHPGTVGRA-MFGDLHIL----------DDDGAE-------LPPGEPGTI---------WFEG 360
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966209822 438 AGPYKHTKDKLLCDVFKKGDVYLNT-GDLIVQDQDNFLYFWDRTGDTFRWKG--------ENVATT--EVAD--VIGML- 503
Cdd:PRK13391 361 GRPFEYLNDPAKTAEARHPDGTWSTvGDIGYVDEDGYLYLTDRAAFMIISGGvniypqeaENLLIThpKVADaaVFGVPn 440
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 966209822 504 -DFIQEANVYGVAISGYEGRAGMAsiilkpntsldlEKVYEQVVTFLPAYACPRFLRIQEKMEATGTFKLLKHQLVE 579
Cdd:PRK13391 441 eDLGEEVKAVVQPVDGVDPGPALA------------AELIAFCRQRLSRQKCPRSIDFEDELPRLPTGKLYKRLLRD 505
|
|
| PRK07788 |
PRK07788 |
acyl-CoA synthetase; Validated |
63-580 |
2.05e-24 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236097 [Multi-domain] Cd Length: 549 Bit Score: 107.32 E-value: 2.05e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966209822 63 HAKRQPRKPFIIYEGDIYTYQDVDKRSSRVAHVFLNHSsLKKGDTVALLMSNEPDFVHVWFGLAKLGCVVAFLNTNIRSN 142
Cdd:PRK07788 58 AARRAPDRAALIDERGTLTYAELDEQSNALARGLLALG-VRAGDGVAVLARNHRGFVLALYAAGKVGARIILLNTGFSGP 136
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966209822 143 SLLNCIRACGPRALVVGADLLGTVEEILPSLSEnISVWGM-KDSVPQ---GVISLKEKLSTSPDEPVP---RSHHVVsll 215
Cdd:PRK07788 137 QLAEVAAREGVKALVYDDEFTDLLSALPPDLGR-LRAWGGnPDDDEPsgsTDETLDDLIAGSSTAPLPkppKPGGIV--- 212
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966209822 216 kstclyIFTSGTTGLPKAAVISQ---LQVLRG--SAVLWafgcTAHDIVYITLPLYHS---SAAILGISgcveLGATCVL 287
Cdd:PRK07788 213 ------ILTSGTTGTPKGAPRPEpspLAPLAGllSRVPF----RAGETTLLPAPMFHAtgwAHLTLAMA----LGSTVVL 278
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966209822 288 KKKFSASQFWSDCKKYDVT------VFqyigeLCRYLCKQSKREGEKDH---KVRLAIGNGIRSDVWREFLDRFGNIkVC 358
Cdd:PRK07788 279 RRRFDPEATLEDIAKHKATalvvvpVM-----LSRILDLGPEVLAKYDTsslKIIFVSGSALSPELATRALEAFGPV-LY 352
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966209822 359 ELYAATESSISFM--------NYT--GRIgAIGRTnlfYKLLstfdlikydfqkDEPmRNEqgwcihVKKGEPGllisRV 428
Cdd:PRK07788 353 NLYGSTEVAFATIatpedlaeAPGtvGRP-PKGVT---VKIL------------DEN-GNE------VPRGVVG----RI 405
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966209822 429 NAKN--PFFGYAGPykhtKDKllcdvfKKGDVYLNTGDLIVQDQDNFLYFWDRTGDTFRWKGENVATTEVADVIGMLDFI 506
Cdd:PRK07788 406 FVGNgfPFEGYTDG----RDK------QIIDGLLSSGDVGYFDEDGLLFVDGRDDDMIVSGGENVFPAEVEDLLAGHPDV 475
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 966209822 507 QEANVYGVAISGYEGRAGmASIILKPNTSLDLEKVYEQVVTFLPAYACPR---FLriqEKMEATGTFKLLKHQLVED 580
Cdd:PRK07788 476 VEAAVIGVDDEEFGQRLR-AFVVKAPGAALDEDAIKDYVRDNLARYKVPRdvvFL---DELPRNPTGKVLKRELREM 548
|
|
| MACS_AAE_MA_like |
cd05970 |
Medium-chain acyl-CoA synthetase (MACS) of AAE_MA like; MACS catalyzes the two-step activation ... |
56-567 |
2.69e-24 |
|
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: 107.20 E-value: 2.69e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966209822 56 VLDKFlshAKRQPRKPFIIYEGD-----IYTYQDVDKRSSRVAHVFLNHSsLKKGDTVALLMSNEPDFVHVWFGLAKLGC 130
Cdd:cd05970 22 VVDAM---AKEYPDKLALVWCDDageerIFTFAELADYSDKTANFFKAMG-IGKGDTVMLTLKRRYEFWYSLLALHKLGA 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966209822 131 VVAFLNTNIRSNSLLNCIRACGPRALVV--GADLLGTVEEILPSL-SENISVWgMKDSVPQGVISLKEKLSTSPDEPVPR 207
Cdd:cd05970 98 IAIPATHQLTAKDIVYRIESADIKMIVAiaEDNIPEEIEKAAPECpSKPKLVW-VGDPVPEGWIDFRKLIKNASPDFERP 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966209822 208 SHHVVSLLKSTCLYIFTSGTTGLPKAavisqlqvlrgsavlwafgcTAHDIVY----ITLPLY---------HSSAAILG 274
Cdd:cd05970 177 TANSYPCGEDILLVYFSSGTTGMPKM--------------------VEHDFTYplghIVTAKYwqnvregglHLTVADTG 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966209822 275 ISGCV------ELGATCVL----KKKFSASQFWSDCKKYDVTVFQYIGELCRYLCKQsKREGEKDHKVRLAI--GNGIRS 342
Cdd:cd05970 237 WGKAVwgkiygQWIAGAAVfvydYDKFDPKALLEKLSKYGVTTFCAPPTIYRFLIRE-DLSRYDLSSLRYCTtaGEALNP 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966209822 343 DVWREFLDRFGnIKVCELYAATESSISFMNYTG---RIGAIGRTNLFYKLlstfDLIKYDFQKdepmrneqgwcihVKKG 419
Cdd:cd05970 316 EVFNTFKEKTG-IKLMEGFGQTETTLTIATFPWmepKPGSMGKPAPGYEI----DLIDREGRS-------------CEAG 377
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966209822 420 EPGLLISRVNAKNPFFGYAGPYKHTKDKllCDVFKKGdvYLNTGDLIVQDQDNFLYFWDRTGDTFRWKGENVATTEVADV 499
Cdd:cd05970 378 EEGEIVIRTSKGKPVGLFGGYYKDAEKT--AEVWHDG--YYHTGDAAWMDEDGYLWFVGRTDDLIKSSGYRIGPFEVESA 453
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 966209822 500 IgmldfIQEANVYGVAISGY----EGRAGMASIIL----KPNTSLDLEkVYEQVVTFLPAYACPRFLRIQEKMEAT 567
Cdd:cd05970 454 L-----IQHPAVLECAVTGVpdpiRGQVVKATIVLakgyEPSEELKKE-LQDHVKKVTAPYKYPRIVEFVDELPKT 523
|
|
| 4CL |
cd05904 |
4-Coumarate-CoA Ligase (4CL); 4-Coumarate:coenzyme A ligase is a key enzyme in the ... |
77-536 |
5.09e-24 |
|
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: 105.78 E-value: 5.09e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966209822 77 GDIYTYQDVDKRSSRVAHVfLNHSSLKKGDTVALLMSNEPDFVHVWFGLAKLGCVVAFLNTNIRSNSLLNCIRACGPRAL 156
Cdd:cd05904 30 GRALTYAELERRVRRLAAG-LAKRGGRKGDVVLLLSPNSIEFPVAFLAVLSLGAVVTTANPLSTPAEIAKQVKDSGAKLA 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966209822 157 VVGADLLgtveEILPSLSENISVWGMKDSVPQGVIS-LKEKLSTSPDEPVPRSHHVVSLLkstclyiFTSGTTGLPKAAV 235
Cdd:cd05904 109 FTTAELA----EKLASLALPVVLLDSAEFDSLSFSDlLFEADEAEPPVVVIKQDDVAALL-------YSSGTTGRSKGVM 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966209822 236 ------ISQLQVLRgsavlWAFGCT-AHDIVYI-TLPLYHssaaILGISGCV----ELGATCVLKKKFSASQFWSDCKKY 303
Cdd:cd05904 178 lthrnlIAMVAQFV-----AGEGSNsDSEDVFLcVLPMFH----IYGLSSFAlgllRLGATVVVMPRFDLEELLAAIERY 248
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966209822 304 DVTVFQYIGELCRYLCKQSKREGEKDHKVRlAIGNG---IRSDVWREFLDRFGNIKVCELYAATESS-ISFMNYT----- 374
Cdd:cd05904 249 KVTHLPVVPPIVLALVKSPIVDKYDLSSLR-QIMSGaapLGKELIEAFRAKFPNVDLGQGYGMTESTgVVAMCFApekdr 327
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966209822 375 GRIGAIGRT--NLFYKLLSTfdlikyDFQKDEPmRNEQG-WCIH---VKKGepgllisrvnaknpFFGYAGPYKHTKDKl 448
Cdd:cd05904 328 AKYGSVGRLvpNVEAKIVDP------ETGESLP-PNQTGeLWIRgpsIMKG--------------YLNNPEATAATIDK- 385
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966209822 449 lcdvfkkgDVYLNTGDLIVQDQDNFLYFWDRTGDTFRWKGENVATTE----------VAD--VIGMLDfiQEAnvygvai 516
Cdd:cd05904 386 --------EGWLHTGDLCYIDEDGYLFIVDRLKELIKYKGFQVAPAElealllshpeILDaaVIPYPD--EEA------- 448
|
490 500
....*....|....*....|
gi 966209822 517 sgyeGRAGMASIILKPNTSL 536
Cdd:cd05904 449 ----GEVPMAFVVRKPGSSL 464
|
|
| MCS |
cd05941 |
Malonyl-CoA synthetase (MCS); MCS catalyzes the formation of malonyl-CoA in a two-step ... |
70-579 |
1.55e-23 |
|
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: 103.91 E-value: 1.55e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966209822 70 KPFIIYEGDIYTYQDVDKRSSRVAHVFLNHSSLKKGDTVALLMSNEPDFVHVWFGLAKLGCVVAFLNTNIRSNSLLNCIR 149
Cdd:cd05941 2 RIAIVDDGDSITYADLVARAARLANRLLALGKDLRGDRVAFLAPPSAEYVVAQLAIWRAGGVAVPLNPSYPLAELEYVIT 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966209822 150 ACGPRALVVGAdllgtveeilpslsenisvwgmkdsvpqgvislkeklstspdepvprshhvvsllkstcLYIFTSGTTG 229
Cdd:cd05941 82 DSEPSLVLDPA-----------------------------------------------------------LILYTSGTTG 102
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966209822 230 LPKAAVISQLQVLRGSAVL---WAFgcTAHDIVYITLPLYHSSAAILGISGCVELGATCVLKKKFSASQFWSDCKKYDVT 306
Cdd:cd05941 103 RPKGVVLTHANLAANVRALvdaWRW--TEDDVLLHVLPLHHVHGLVNALLCPLFAGASVEFLPKFDPKEVAISRLMPSIT 180
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966209822 307 VF-----------QYIGELCRYLCKQSKregEKDHKVRLAI-GNG-IRSDVWREFLDRFGNiKVCELYAATESSISFMN- 372
Cdd:cd05941 181 VFmgvptiytrllQYYEAHFTDPQFARA---AAAERLRLMVsGSAaLPVPTLEEWEAITGH-TLLERYGMTEIGMALSNp 256
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966209822 373 YTG--RIGAIGRTnlfyklLSTFDL-IKYDFQKDEPMRNEQGWcIHVKKgePGLlisrvnaknpFFGYAGPYKHTKDKLL 449
Cdd:cd05941 257 LDGerRPGTVGMP------LPGVQArIVDEETGEPLPRGEVGE-IQVRG--PSV----------FKEYWNKPEATKEEFT 317
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966209822 450 CDVFKKgdvylnTGDLIVQDQDNFLYFWDRTG-DTFRWKGENVATTEVADVIGMLDFIQEANVYGVAISGYeGRAGMASI 528
Cdd:cd05941 318 DDGWFK------TGDLGVVDEDGYYWILGRSSvDIIKSGGYKVSALEIERVLLAHPGVSECAVIGVPDPDW-GERVVAVV 390
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|..
gi 966209822 529 ILKPN-TSLDLEKVYEQVVTFLPAYACPRFLRIQEKMEATGTFKLLKHQLVE 579
Cdd:cd05941 391 VLRAGaAALSLEELKEWAKQRLAPYKRPRRLILVDELPRNAMGKVNKKELRK 442
|
|
| MACS_like |
cd05972 |
Medium-chain acyl-CoA synthetase (MACS or ACSM); MACS catalyzes the two-step activation of ... |
80-577 |
2.52e-23 |
|
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: 102.80 E-value: 2.52e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966209822 80 YTYQDVDKRSSRVAHVFLNHSsLKKGDTVALLMSNEPDFVHVWFGLAKLGCVVAFLNTNIRSNSLLNCIRACGPRALVVG 159
Cdd:cd05972 1 WSFRELKRESAKAANVLAKLG-LRKGDRVAVLLPRVPELWAVILAVIKLGAVYVPLTTLLGPKDIEYRLEAAGAKAIVTD 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966209822 160 ADllgtveeilpslsenisvwgmkdsvpqgvislkeklstspdepvprshhvvsllkSTCLYIFTSGTTGLPKAavisql 239
Cdd:cd05972 80 AE-------------------------------------------------------DPALIYFTSGTTGLPKG------ 98
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966209822 240 qVLRGSAVLWAFGCTAH--------DIVYIT------LPLYHSSAAILGisgcveLGATCVL--KKKFSASQFWSDCKKY 303
Cdd:cd05972 99 -VLHTHSYPLGHIPTAAywlglrpdDIHWNIadpgwaKGAWSSFFGPWL------LGATVFVyeGPRFDAERILELLERY 171
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966209822 304 DVTVFQYIGELCRYLCKQSKREGEKDHkVRLAIGNG-------IrsDVWREFLdrfgNIKVCELYAATESSISFMNYTG- 375
Cdd:cd05972 172 GVTSFCGPPTAYRMLIKQDLSSYKFSH-LRLVVSAGeplnpevI--EWWRAAT----GLPIRDGYGQTETGLTVGNFPDm 244
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966209822 376 --RIGAIGRTNLFYKLlstfDLIKYDFQKDEPmrneqgwcihvkkGEPGLLISRVNAKNPFFGYAGPYKHTKDKLlcdvf 453
Cdd:cd05972 245 pvKPGSMGRPTPGYDV----AIIDDDGRELPP-------------GEEGDIAIKLPPPGLFLGYVGDPEKTEASI----- 302
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966209822 454 kKGDVYLnTGDLIVQDQDNFLYFWDRTGDTFRWKGENVATTEVADVIgmldfIQEANVYGVAISGY--EGRAGM--ASII 529
Cdd:cd05972 303 -RGDYYL-TGDRAYRDEDGYFWFVGRADDIIKSSGYRIGPFEVESAL-----LEHPAVAEAAVVGSpdPVRGEVvkAFVV 375
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|.
gi 966209822 530 LKPN---TSLDLEKVYEQVVTFLPAYACPRFLRIQEKMEATGTFKLLKHQL 577
Cdd:cd05972 376 LTSGyepSEELAEELQGHVKKVLAPYKYPREIEFVEELPKTISGKIRRVEL 426
|
|
| BCL_like |
cd05919 |
Benzoate CoA ligase (BCL) and similar adenylate forming enzymes; This family contains benzoate ... |
72-577 |
2.00e-22 |
|
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: 100.23 E-value: 2.00e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966209822 72 FIIYEGDIyTYQDVDKRSSRVAHVFLNHSsLKKGDTVALLMSNEPDFVHVWFGLAKLGCVVAFLNTNIRSNSLLNCIRAC 151
Cdd:cd05919 4 FYAADRSV-TYGQLHDGANRLGSALRNLG-VSSGDRVLLLMLDSPELVQLFLGCLARGAIAVVINPLLHPDDYAYIARDC 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966209822 152 GPRALVVGADLLgtveeilpslsenisvwgmkdsvpqgvislkeklstspdepvprshhvvsllkstCLYIFTSGTTGLP 231
Cdd:cd05919 82 EARLVVTSADDI-------------------------------------------------------AYLLYSSGTTGPP 106
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966209822 232 KaAVISQLQVLRGSAVLWA---FGCTAHDIVYITLPLYHSSAAILGISGCVELGATCVLKKKF-SASQFWSDCKKYDVTV 307
Cdd:cd05919 107 K-GVMHAHRDPLLFADAMAreaLGLTPGDRVFSSAKMFFGYGLGNSLWFPLAVGASAVLNPGWpTAERVLATLARFRPTV 185
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966209822 308 FQYIGELCRYLCKQSKREGEKDHKVRLAI--GNGIRSDVWREFLDRFGnIKVCELYAATESSISFM-NYTG--RIGAIGR 382
Cdd:cd05919 186 LYGVPTFYANLLDSCAGSPDALRSLRLCVsaGEALPRGLGERWMEHFG-GPILDGIGATEVGHIFLsNRPGawRLGSTGR 264
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966209822 383 TNLFYKLlstfdlikydfqkdePMRNEQGWCIhvKKGEPGLLISRVNAKNPffGYAGPYKHTKDKLLcdvfkkgDVYLNT 462
Cdd:cd05919 265 PVPGYEI---------------RLVDEEGHTI--PPGEEGDLLVRGPSAAV--GYWNNPEKSRATFN-------GGWYRT 318
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966209822 463 GDLIVQDQDNFLYFWDRTGDTFRWKGENVATTEVADVIGMLDFIQEANVYGVAiSGYEGRAGMASIILKPNTSLDlEKVY 542
Cdd:cd05919 319 GDKFCRDADGWYTHAGRADDMLKVGGQWVSPVEVESLIIQHPAVAEAAVVAVP-ESTGLSRLTAFVVLKSPAAPQ-ESLA 396
|
490 500 510
....*....|....*....|....*....|....*....
gi 966209822 543 EQVVTF----LPAYACPRFLRIQEKMEATGTFKLLKHQL 577
Cdd:cd05919 397 RDIHRHllerLSAHKVPRRIAFVDELPRTATGKLQRFKL 435
|
|
| PRK08276 |
PRK08276 |
long-chain-fatty-acid--CoA ligase; Validated |
73-579 |
8.23e-22 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236215 [Multi-domain] Cd Length: 502 Bit Score: 99.21 E-value: 8.23e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966209822 73 IIYEGDIYTYQDVDKRSSRVAHVFLNHSsLKKGDTVALLMSNEPDFVHVWFGLAKLGCVVAFLNTNIRSNSLLNCIRACG 152
Cdd:PRK08276 5 MAPSGEVVTYGELEARSNRLAHGLRALG-LREGDVVAILLENNPEFFEVYWAARRSGLYYTPINWHLTAAEIAYIVDDSG 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966209822 153 PRALVVGADLLGTVEEILPSLSENISVWGMKDSVPQGVISLKEKLSTSPDEPVPRshhvvSLLKSTCLYifTSGTTGLPK 232
Cdd:PRK08276 84 AKVLIVSAALADTAAELAAELPAGVPLLLVVAGPVPGFRSYEEALAAQPDTPIAD-----ETAGADMLY--SSGTTGRPK 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966209822 233 AAVISQLQV------LRGSAVLWAFGCTAHDIVYI-TLPLYHssAAILGISGCV-ELGATCVLKKKFSASQFWSDCKKYD 304
Cdd:PRK08276 157 GIKRPLPGLdpdeapGMMLALLGFGMYGGPDSVYLsPAPLYH--TAPLRFGMSAlALGGTVVVMEKFDAEEALALIERYR 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966209822 305 VTVFQYIGELCRYLCK--QSKREGEKDHKVRLAIGNG--IRSDVWREFLDRFGNIkVCELYAATESS-ISFMN---YTGR 376
Cdd:PRK08276 235 VTHSQLVPTMFVRMLKlpEEVRARYDVSSLRVAIHAAapCPVEVKRAMIDWWGPI-IHEYYASSEGGgVTVITsedWLAH 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966209822 377 IGAIGRTnlfykLLSTfdlIK-YDFQKDEpmrneqgwcihVKKGEPGLLISRVNAknPFFGYAG-PYKHTKDKLLCDVFK 454
Cdd:PRK08276 314 PGSVGKA-----VLGE---VRiLDEDGNE-----------LPPGEIGTVYFEMDG--YPFEYHNdPEKTAAARNPHGWVT 372
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966209822 455 KGDV-YLntgdlivqDQDNFLYFWDRTGDTFRWKGENVATTEVADVIGMLDFIQEANVYGVAISGYeGRAGMASIILKPN 533
Cdd:PRK08276 373 VGDVgYL--------DEDGYLYLTDRKSDMIISGGVNIYPQEIENLLVTHPKVADVAVFGVPDEEM-GERVKAVVQPADG 443
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|
gi 966209822 534 TSLDlEKVYEQVVTF----LPAYACPRFLRIQEKMEATGTFKLLKHQLVE 579
Cdd:PRK08276 444 ADAG-DALAAELIAWlrgrLAHYKCPRSIDFEDELPRTPTGKLYKRRLRD 492
|
|
| PRK08314 |
PRK08314 |
long-chain-fatty-acid--CoA ligase; Validated |
64-287 |
1.46e-21 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236235 [Multi-domain] Cd Length: 546 Bit Score: 98.49 E-value: 1.46e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966209822 64 AKRQPRKPFIIYEGDIYTYQDVDKRSSRVAHVFLNHSSLKKGDTVALLMSNEPDFVHVWFGLAKLGCVVAFLNTNIRSNS 143
Cdd:PRK08314 20 ARRYPDKTAIVFYGRAISYRELLEEAERLAGYLQQECGVRKGDRVLLYMQNSPQFVIAYYAILRANAVVVPVNPMNREEE 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966209822 144 LLNCIRACGPRALVVGADLLGTVEEILPSLS-ENISVWGMKDSVP-QGVISLKEKLSTSPDEPVPRSHHVVSLLKST--- 218
Cdd:PRK08314 100 LAHYVTDSGARVAIVGSELAPKVAPAVGNLRlRHVIVAQYSDYLPaEPEIAVPAWLRAEPPLQALAPGGVVAWKEALaag 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966209822 219 -------------CLYIFTSGTTGLPKAAVISQLQVLRG--SAVLWaFGCTAHDIVYITLPLYHSSAAILGISGCVELGA 283
Cdd:PRK08314 180 lappphtagpddlAVLPYTSGTTGVPKGCMHTHRTVMANavGSVLW-SNSTPESVVLAVLPLFHVTGMVHSMNAPIYAGA 258
|
....
gi 966209822 284 TCVL 287
Cdd:PRK08314 259 TVVL 262
|
|
| menE |
TIGR01923 |
O-succinylbenzoate-CoA ligase; This model represents an enzyme, O-succinylbenzoate-CoA ligase, ... |
81-514 |
2.84e-21 |
|
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: 96.75 E-value: 2.84e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966209822 81 TYQDVDKRSSRVAHVFLNHSsLKKGDTVALLMSNEPDFVHVWFGLAKLGCVVAFLNTNIRSNSLLNCIRACGPrALVVGA 160
Cdd:TIGR01923 1 TWQDLDCEAAHLAKALKAQG-IRSGSRVALVGQNSIEMVLLLHACLLLGAEIAMLNTRLTENERTNQLEDLDV-QLLLTD 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966209822 161 DLLGtvEEILPSlsenisvwgmkDSVPQGVISLKEKLSTSPDEPVPRshhVVSLlkstclyIFTSGTTGLPKAAVISQLQ 240
Cdd:TIGR01923 79 SLLE--EKDFQA-----------DSLDRIEAAGRYETSLSASFNMDQ---IATL-------MFTSGTTGKPKAVPHTFRN 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966209822 241 VL---RGSAVLWAFgcTAHDIVYITLPLYHssaailgISG------CVELGATCVLKKKFSasQFWSDCKKYDVTVFQYI 311
Cdd:TIGR01923 136 HYasaVGSKENLGF--TEDDNWLLSLPLYH-------ISGlsilfrWLIEGATLRIVDKFN--QLLEMIANERVTHISLV 204
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966209822 312 -GELCRYLCKQSKREGEKdhKVRLAiGNGIRSDVWREFLDRfgNIKVCELYAATESSISFMNYTGRI----GAIGRTnLF 386
Cdd:TIGR01923 205 pTQLNRLLDEGGHNENLR--KILLG-GSAIPAPLIEEAQQY--GLPIYLSYGMTETCSQVTTATPEMlharPDVGRP-LA 278
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966209822 387 YKLLStfdlIKYDfqkDEPMRNEqgwcIHVKkgepgllisrvnAKNPFFGY--AGPYKHTkdkllcdVFKKGdvYLNTGD 464
Cdd:TIGR01923 279 GREIK----IKVD---NKEGHGE----IMVK------------GANLMKGYlyQGELTPA-------FEQQG--WFNTGD 326
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|
gi 966209822 465 LIVQDQDNFLYFWDRTGDTFRWKGENVATTEVADVIGMLDFIQEANVYGV 514
Cdd:TIGR01923 327 IGELDGEGFLYVLGRRDDLIISGGENIYPEEIETVLYQHPGIQEAVVVPK 376
|
|
| ABCL |
cd05958 |
2-aminobenzoate-CoA ligase (ABCL); ABCL catalyzes the initial step in the 2-aminobenzoate ... |
80-577 |
4.46e-21 |
|
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: 96.39 E-value: 4.46e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966209822 80 YTYQDVDKRSSRVAHVFLNHSSLKKGDTVALLMSNEPDFVHVWFGLAKLGCVVAFLNTNIRSNSLLNCIRACGP-RALVV 158
Cdd:cd05958 11 WTYRDLLALANRIANVLVGELGIVPGNRVLLRGSNSPELVACWFGIQKAGAIAVATMPLLRPKELAYILDKARItVALCA 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966209822 159 GAdllgtveeilpslsenisvwgmkdsvpqgvislkekLSTSPDepvprshhvvsllksTCLYIFTSGTTGLPKAAViSQ 238
Cdd:cd05958 91 HA------------------------------------LTASDD---------------ICILAFTSGTTGAPKATM-HF 118
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966209822 239 LQVLRGSAVLWA---FGCTAHDIVYITLPLYHSSAAILGISGCVELGATCVLKKKFSASQFWSDCKKYDVTVFQYIGELC 315
Cdd:cd05958 119 HRDPLASADRYAvnvLRLREDDRFVGSPPLAFTFGLGGVLLFPFGVGASGVLLEEATPDLLLSAIARYKPTVLFTAPTAY 198
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966209822 316 RYLCkQSKREGEKD-HKVRLAI--GNGIRSDVWREFLDRFGnIKVCELYAATESSISFMNYTG---RIGAIGRTNLFYKL 389
Cdd:cd05958 199 RAML-AHPDAAGPDlSSLRKCVsaGEALPAALHRAWKEATG-IPIIDGIGSTEMFHIFISARPgdaRPGATGKPVPGYEA 276
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966209822 390 lstfdLIKYDFQKDEPmrneqgwcihvkKGEPGLLISRvnaknpffgyaGP--YKHTKDKLLCDVFKKGdvYLNTGDLIV 467
Cdd:cd05958 277 -----KVVDDEGNPVP------------DGTIGRLAVR-----------GPtgCRYLADKRQRTYVQGG--WNITGDTYS 326
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966209822 468 QDQDNFLYFWDRTGDTFRWKGENVATTEVADVIgmldfIQEANVYGVAISGYEGRAGM----ASIILKPNTSLD---LEK 540
Cdd:cd05958 327 RDPDGYFRHQGRSDDMIVSGGYNIAPPEVEDVL-----LQHPAVAECAVVGHPDESRGvvvkAFVVLRPGVIPGpvlARE 401
|
490 500 510
....*....|....*....|....*....|....*..
gi 966209822 541 VYEQVVTFLPAYACPRFLRIQEKMEATGTFKLLKHQL 577
Cdd:cd05958 402 LQDHAKAHIAPYKYPRAIEFVTELPRTATGKLQRFAL 438
|
|
| OSB_CoA_lg |
cd05912 |
O-succinylbenzoate-CoA ligase (also known as O-succinylbenzoate-CoA synthase, OSB-CoA ... |
80-577 |
7.60e-21 |
|
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: 95.11 E-value: 7.60e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966209822 80 YTYQDVDKRSSRVAHVfLNHSSLKKGDTVALLMSNEPDFVHVWFGLAKLGCVVAFLNTNIRSNSLLnciracgpralvvg 159
Cdd:cd05912 2 YTFAELFEEVSRLAEH-LAALGVRKGDRVALLSKNSIEMILLIHALWLLGAEAVLLNTRLTPNELA-------------- 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966209822 160 adllgtveeilpslsenisvWGMKDSVPQgvislKEKLSTspdepvprshhvvsllkstclYIFTSGTTGLPKAAVIS-- 237
Cdd:cd05912 67 --------------------FQLKDSDVK-----LDDIAT---------------------IMYTSGTTGKPKGVQQTfg 100
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966209822 238 -QLQVLRGSAVlwAFGCTAHDIVYITLPLYHssaailgISGC------VELGATCVLKKKFSASQFWSDCKKYDVTVFQY 310
Cdd:cd05912 101 nHWWSAIGSAL--NLGLTEDDNWLCALPLFH-------ISGLsilmrsVIYGMTVYLVDKFDAEQVLHLINSGKVTIISV 171
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966209822 311 IGELCRYLCKQSKREGEKDHKVRLAIGNGIRSDVWREFLDRfgNIKVCELYAATESS-----ISFMNYTGRIGAIGRTnL 385
Cdd:cd05912 172 VPTMLQRLLEILGEGYPNNLRCILLGGGPAPKPLLEQCKEK--GIPVYQSYGMTETCsqivtLSPEDALNKIGSAGKP-L 248
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966209822 386 FYKLLStfdlIKYDFQkdepmrneqgwcihvKKGEPGLLIsrVNAKNPFFGYAGPYKHTKdkllcDVFKKGdvYLNTGDL 465
Cdd:cd05912 249 FPVELK----IEDDGQ---------------PPYEVGEIL--LKGPNVTKGYLNRPDATE-----ESFENG--WFKTGDI 300
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966209822 466 IVQDQDNFLYFWDRTGDTFRWKGENVATTEVADVIGMLDFIQEANVYGVAISGYeGRAGMASIILkpNTSLDLEKVYEQV 545
Cdd:cd05912 301 GYLDEEGFLYVLDRRSDLIISGGENIYPAEIEEVLLSHPAIKEAGVVGIPDDKW-GQVPVAFVVS--ERPISEEELIAYC 377
|
490 500 510
....*....|....*....|....*....|..
gi 966209822 546 VTFLPAYACPRFLRIQEKMEATGTFKLLKHQL 577
Cdd:cd05912 378 SEKLAKYKVPKKIYFVDELPRTASGKLLRHEL 409
|
|
| PRK08751 |
PRK08751 |
long-chain fatty acid--CoA ligase; |
55-577 |
9.26e-21 |
|
long-chain fatty acid--CoA ligase;
Pssm-ID: 181546 [Multi-domain] Cd Length: 560 Bit Score: 96.10 E-value: 9.26e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966209822 55 TVLDKFLSHAKRQPRKPFIIYEGDIYTYQDVDKRSSRVAHVFLNHSSLKKGDTVALLMSNEPDFVHVWFGLAKLGCVVAF 134
Cdd:PRK08751 26 TVAEVFATSVAKFADRPAYHSFGKTITYREADQLVEQFAAYLLGELQLKKGDRVALMMPNCLQYPIATFGVLRAGLTVVN 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966209822 135 LNTNIRSNSLLNCIRACGPRALVVGADLLGTVEEILPS----------LSE----------NISVWGMKDSVPQ----GV 190
Cdd:PRK08751 106 VNPLYTPRELKHQLIDSGASVLVVIDNFGTTVQQVIADtpvkqvittgLGDmlgfpkaalvNFVVKYVKKLVPEyrinGA 185
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966209822 191 ISLKEKLSTSPDEPVPR---SHHVVSLLKstclyiFTSGTTGLPKAAVISQLQVLRG--SAVLWAFGC----TAHDIVYI 261
Cdd:PRK08751 186 IRFREALALGRKHSMPTlqiEPDDIAFLQ------YTGGTTGVAKGAMLTHRNLVANmqQAHQWLAGTgkleEGCEVVIT 259
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966209822 262 TLPLYH------SSAAILGISGCVELgatcvLKKKFSASQFWSDCKKYDVTVFQYIGELCRYLCKQSKREGEKDHKVRLA 335
Cdd:PRK08751 260 ALPLYHifaltaNGLVFMKIGGCNHL-----ISNPRDMPGFVKELKKTRFTAFTGVNTLFNGLLNTPGFDQIDFSSLKMT 334
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966209822 336 IGNGIRsdVWREFLDRFGNIK---VCELYAATESS-------ISFMNYTGRIGaigrtnlfYKLLSTFDLIKYDFQKDEP 405
Cdd:PRK08751 335 LGGGMA--VQRSVAERWKQVTgltLVEAYGLTETSpaacinpLTLKEYNGSIG--------LPIPSTDACIKDDAGTVLA 404
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966209822 406 MrneqgwcihvkkGEPGLLIsrVNAKNPFFGYAGPYKHTKDKLlcdvfkKGDVYLNTGDLIVQDQDNFLYFWDRTGDTFR 485
Cdd:PRK08751 405 I------------GEIGELC--IKGPQVMKGYWKRPEETAKVM------DADGWLHTGDIARMDEQGFVYIVDRKKDMIL 464
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966209822 486 WKGENVATTEVADVIGMLDFIQEANVYGVAisgyEGRAG--MASIILKPNTSLDLEKVYEQVVTFLPAYACPRFLRIQEK 563
Cdd:PRK08751 465 VSGFNVYPNEIEDVIAMMPGVLEVAAVGVP----DEKSGeiVKVVIVKKDPALTAEDVKAHARANLTGYKQPRIIEFRKE 540
|
570
....*....|....
gi 966209822 564 MEATGTFKLLKHQL 577
Cdd:PRK08751 541 LPKTNVGKILRREL 554
|
|
| PRK12583 |
PRK12583 |
acyl-CoA synthetase; Provisional |
55-579 |
9.96e-21 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 237145 [Multi-domain] Cd Length: 558 Bit Score: 96.00 E-value: 9.96e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966209822 55 TVLDKFLSHAKRQPRKPFIIY--EGDIYTYQDVDKRSSRVAHVFLNhSSLKKGDTVALLMSNEPDFVHVWFGLAKLGCVV 132
Cdd:PRK12583 19 TIGDAFDATVARFPDREALVVrhQALRYTWRQLADAVDRLARGLLA-LGVQPGDRVGIWAPNCAEWLLTQFATARIGAIL 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966209822 133 AFLNTNIRSNSLLNCIRACGPRALVV-----GADLLGTVEEILPSLSENISVWGMKDSVP--QGVISLKEKLS---TSPD 202
Cdd:PRK12583 98 VNINPAYRASELEYALGQSGVRWVICadafkTSDYHAMLQELLPGLAEGQPGALACERLPelRGVVSLAPAPPpgfLAWH 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966209822 203 EPVPRSHHVV---------SLLKSTCLYI-FTSGTTGLPKAAVISQLQVLR-GSAVLWAFGCTAHDIVYITLPLYHSSAA 271
Cdd:PRK12583 178 ELQARGETVSrealaerqaSLDRDDPINIqYTSGTTGFPKGATLSHHNILNnGYFVAESLGLTEHDRLCVPVPLYHCFGM 257
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966209822 272 ILGISGCVELGATCVL-KKKFSASQFWSDCKKYDVTVFQ-----YIGELcrylckQSKREGEKD-HKVRLAI--GNGIRS 342
Cdd:PRK12583 258 VLANLGCMTVGACLVYpNEAFDPLATLQAVEEERCTALYgvptmFIAEL------DHPQRGNFDlSSLRTGImaGAPCPI 331
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966209822 343 DVWREFLDRFGNIKVCELYAATESS-ISFMNYTG-----RIGAIGRT--NLFYKLLstfdlikydfqkdEPMRNEqgwci 414
Cdd:PRK12583 332 EVMRRVMDEMHMAEVQIAYGMTETSpVSLQTTAAddlerRVETVGRTqpHLEVKVV-------------DPDGAT----- 393
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966209822 415 hVKKGEPGLLISRvnAKNPFFGYAGPYKHTKDKLlcdvfkKGDVYLNTGDLIVQDQDNFLYFWDRTGDTFRWKGENVATT 494
Cdd:PRK12583 394 -VPRGEIGELCTR--GYSVMKGYWNNPEATAESI------DEDGWMHTGDLATMDEQGYVRIVGRSKDMIIRGGENIYPR 464
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966209822 495 EVADVIGMLDFIQEANVYGVAISGYeGRAGMASIILKPNTSLDLEKVYEQVVTFLPAYACPRFLRIQEKMEATGTFKLLK 574
Cdd:PRK12583 465 EIEEFLFTHPAVADVQVFGVPDEKY-GEEIVAWVRLHPGHAASEEELREFCKARIAHFKVPRYFRFVDEFPMTVTGKVQK 543
|
....*
gi 966209822 575 HQLVE 579
Cdd:PRK12583 544 FRMRE 548
|
|
| PRK13382 |
PRK13382 |
bile acid CoA ligase; |
60-577 |
1.09e-20 |
|
bile acid CoA ligase;
Pssm-ID: 172019 [Multi-domain] Cd Length: 537 Bit Score: 95.98 E-value: 1.09e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966209822 60 FLSHAKRQPRKPFIIYEGDIYTYQDVDKRSSRVAhVFLNHSSLKKGDTVALLMSNEPDFVHVWFGLAKLGCVVAFLNTNI 139
Cdd:PRK13382 49 FAIAAQRCPDRPGLIDELGTLTWRELDERSDALA-AALQALPIGEPRVVGIMCRNHRGFVEALLAANRIGADILLLNTSF 127
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966209822 140 RSNSLLNCIRACGPRALVVGADLLGTVEEILPSLSENISVWGMKDSVPQgviSLKEKLSTSP--DEPVPRShhvvsllKS 217
Cdd:PRK13382 128 AGPALAEVVTREGVDTVIYDEEFSATVDRALADCPQATRIVAWTDEDHD---LTVEVLIAAHagQRPEPTG-------RK 197
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966209822 218 TCLYIFTSGTTGLPKAAVISQLQ-VLRGSAVLWAFGCTAHDIVYITLPLYHS---SAAILGISgcveLGATCVLKKKFSA 293
Cdd:PRK13382 198 GRVILLTSGTTGTPKGARRSGPGgIGTLKAILDRTPWRAEEPTVIVAPMFHAwgfSQLVLAAS----LACTIVTRRRFDP 273
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966209822 294 SQFWSDCKKYDVT-------VFQYIGELC-----RYLCKQSkregekdhKVRLAIGNGIRSDVWREFLDRFGNIkVCELY 361
Cdd:PRK13382 274 EATLDLIDRHRATglavvpvMFDRIMDLPaevrnRYSGRSL--------RFAAASGSRMRPDVVIAFMDQFGDV-IYNNY 344
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966209822 362 AATESSI----------SFMNYTGRiGAIGrtnlfykllSTFDLIKYDFQKdepmrneqgwcihVKKGEPGLLISRVNAK 431
Cdd:PRK13382 345 NATEAGMiatatpadlrAAPDTAGR-PAEG---------TEIRILDQDFRE-------------VPTGEVGTIFVRNDTQ 401
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966209822 432 npFFGYAGpyKHTKDkllcdvFKKGdvYLNTGDLIVQDQDNFLYFWDRTGDTFRWKGENVATTEVADVIGMLDFIQEANV 511
Cdd:PRK13382 402 --FDGYTS--GSTKD------FHDG--FMASGDVGYLDENGRLFVVGRDDEMIVSGGENVYPIEVEKTLATHPDVAEAAV 469
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 966209822 512 YGVAISGYeGRAGMASIILKPNTSLDLEKVYEQVVTFLPAYACPRFLRIQEKMEATGTFKLLKHQL 577
Cdd:PRK13382 470 IGVDDEQY-GQRLAAFVVLKPGASATPETLKQHVRDNLANYKVPRDIVVLDELPRGATGKILRREL 534
|
|
| PRK06087 |
PRK06087 |
medium-chain fatty-acid--CoA ligase; |
43-580 |
1.92e-20 |
|
medium-chain fatty-acid--CoA ligase;
Pssm-ID: 180393 [Multi-domain] Cd Length: 547 Bit Score: 95.20 E-value: 1.92e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966209822 43 RLKKYEKRGEL--VTVLDKFLSHAKRQPRKPFIIYE-GDIYTYQDVDKRSSRVAHVFLNhSSLKKGDTVALLMSNEPDFV 119
Cdd:PRK06087 10 RRAAYRQQGYWgdASLADYWQQTARAMPDKIAVVDNhGASYTYSALDHAASRLANWLLA-KGIEPGDRVAFQLPGWCEFT 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966209822 120 HVWFGLAKLGCVVAFLNTNIRSNSLLNCIRACGPRALVVGA--------DLLGTVEEILPSLSENISVWGMKDSVPQgvI 191
Cdd:PRK06087 89 IIYLACLKVGAVSVPLLPSWREAELVWVLNKCQAKMFFAPTlfkqtrpvDLILPLQNQLPQLQQIVGVDKLAPATSS--L 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966209822 192 SLKEKLSTSP---DEPVPRSHHVVSLLkstclyiFTSGTTGLPKAAVISQLQVLRGS-AVLWAFGCTAHDIVYITLPLYH 267
Cdd:PRK06087 167 SLSQIIADYEpltTAITTHGDELAAVL-------FTSGTEGLPKGVMLTHNNILASErAYCARLNLTWQDVFMMPAPLGH 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966209822 268 SSAAILGISGCVELGATCVLKKKFSASQ----------FWS--------------DCKKYDVTVFQYigelcrYLCKqsk 323
Cdd:PRK06087 240 ATGFLHGVTAPFLIGARSVLLDIFTPDAclalleqqrcTCMlgatpfiydllnllEKQPADLSALRF------FLCG--- 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966209822 324 regekdhkvrlaiGNGIRSDVWREFLDRfgNIKVCELYAATESS----------ISFMNYTGRIGAIGrtnLFYKLLstf 393
Cdd:PRK06087 311 -------------GTTIPKKVARECQQR--GIKLLSVYGSTESSphavvnlddpLSRFMHTDGYAAAG---VEIKVV--- 369
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966209822 394 dlikydfqkDEpMRNEqgwcihVKKGEPGLLISRvnAKNPFFGYAGPYKHTkDKLLCDvfkkgDVYLNTGDLIVQDQDNF 473
Cdd:PRK06087 370 ---------DE-ARKT------LPPGCEGEEASR--GPNVFMGYLDEPELT-ARALDE-----EGWYYSGDLCRMDEAGY 425
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966209822 474 LYFWDRTGDTFRWKGENVATTEVADVIGMLDFIQEANVYGVAisgyEGRAG---MASIILKPNT-SLDLEKVYEQVVT-F 548
Cdd:PRK06087 426 IKITGRKKDIIVRGGENISSREVEDILLQHPKIHDACVVAMP----DERLGersCAYVVLKAPHhSLTLEEVVAFFSRkR 501
|
570 580 590
....*....|....*....|....*....|..
gi 966209822 549 LPAYACPRFLRIQEKMEATGTFKLLKHQLVED 580
Cdd:PRK06087 502 VAKYKYPEHIVVIDKLPRTASGKIQKFLLRKD 533
|
|
| PRK13390 |
PRK13390 |
acyl-CoA synthetase; Provisional |
62-577 |
2.68e-20 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 139538 [Multi-domain] Cd Length: 501 Bit Score: 94.31 E-value: 2.68e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966209822 62 SHAKRQPRKPFIIYE--GDIYTYQDVDKRSSRVAHVfLNHSSLKKGDTVALLMSNEPDFVHVWFGLAKLGCVVAFLNTNI 139
Cdd:PRK13390 5 THAQIAPDRPAVIVAetGEQVSYRQLDDDSAALARV-LYDAGLRTGDVVALLSDNSPEALVVLWAALRSGLYITAINHHL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966209822 140 RSNSLLNCIRACGPRALVVGADLLGTVEEILPSLSENISVWGMKDsvpqGVISLKEKLSTSPdepvPRshhvvsLLKSTC 219
Cdd:PRK13390 84 TAPEADYIVGDSGARVLVASAALDGLAAKVGADLPLRLSFGGEID----GFGSFEAALAGAG----PR------LTEQPC 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966209822 220 --LYIFTSGTTGLPKAA-------VISQ-----LQVLRGsavlwAFGCTAHDIVYITLPLYHssAAILGISGCVE-LGAT 284
Cdd:PRK13390 150 gaVMLYSSGTTGFPKGIqpdlpgrDVDApgdpiVAIARA-----FYDISESDIYYSSAPIYH--AAPLRWCSMVHaLGGT 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966209822 285 CVLKKKFSASQFWSDCKKYDVTVFQYIGELCRYLCKQskregEKDHKVRLAIGNgIRS----------DVWREFLDRFGN 354
Cdd:PRK13390 223 VVLAKRFDAQATLGHVERYRITVTQMVPTMFVRLLKL-----DADVRTRYDVSS-LRAvihaaapcpvDVKHAMIDWLGP 296
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966209822 355 IkVCELYAATES-SISFMN---YTGRIGAIGRTnlfykLLSTFDLIKYDfQKDEPmrneqgwcihvkKGEPGLLISRVNA 430
Cdd:PRK13390 297 I-VYEYYSSTEAhGMTFIDspdWLAHPGSVGRS-----VLGDLHICDDD-GNELP------------AGRIGTVYFERDR 357
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966209822 431 KnPFFGYAGPYKHTKDKLLCDVFkkgdvYLNTGDLIVQDQDNFLYFWDRTGDTFRWKGENVATTEVADVIGMLDFIQEAN 510
Cdd:PRK13390 358 L-PFRYLNDPEKTAAAQHPAHPF-----WTTVGDLGSVDEDGYLYLADRKSFMIISGGVNIYPQETENALTMHPAVHDVA 431
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 966209822 511 VYGVAiSGYEGRAGMASIIL----KPNTSLDLEKVyEQVVTFLPAYACPRFLRIQEKMEATGTFKLLKHQL 577
Cdd:PRK13390 432 VIGVP-DPEMGEQVKAVIQLvegiRGSDELARELI-DYTRSRIAHYKAPRSVEFVDELPRTPTGKLVKGLL 500
|
|
| PRK06710 |
PRK06710 |
long-chain-fatty-acid--CoA ligase; Validated |
57-580 |
3.56e-20 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 180666 [Multi-domain] Cd Length: 563 Bit Score: 94.33 E-value: 3.56e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966209822 57 LDKFLSH-AKRQPRKPFIIYEGDIYTYQDVDKRSSRVAHvFLNHSSLKKGDTVALLMSNEPDFVHVWFGLAKLGCVVAFL 135
Cdd:PRK06710 26 LHKYVEQmASRYPEKKALHFLGKDITFSVFHDKVKRFAN-YLQKLGVEKGDRVAIMLPNCPQAVIGYYGTLLAGGIVVQT 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966209822 136 NTNIRSNSL-----------LNCIRACGPRALVVGAD------LLGTVEEILP---------------------SLSENI 177
Cdd:PRK06710 105 NPLYTERELeyqlhdsgakvILCLDLVFPRVTNVQSAtkiehvIVTRIADFLPfpknllypfvqkkqsnlvvkvSESETI 184
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966209822 178 SVWGmkdsvpqgviSLKEKLSTSPDEPVPRSHHVvSLLKstclyiFTSGTTGLPKAAVISQLQVLRGS--AVLWAFGCT- 254
Cdd:PRK06710 185 HLWN----------SVEKEVNTGVEVPCDPENDL-ALLQ------YTGGTTGFPKGVMLTHKNLVSNTlmGVQWLYNCKe 247
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966209822 255 AHDIVYITLPLYH--SSAAILGISgcVELGATCVLKKKFSASQFWSDCKKYDVTVFQ-----YIGELCRYLCKqskregE 327
Cdd:PRK06710 248 GEEVVLGVLPFFHvyGMTAVMNLS--IMQGYKMVLIPKFDMKMVFEAIKKHKVTLFPgaptiYIALLNSPLLK------E 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966209822 328 KD-HKVRLAIGNGIRSDVwrEFLDRFGNI---KVCELYAATESS-ISFMNY--TGRI-GAIGrtnlfykllstfdlikyd 399
Cdd:PRK06710 320 YDiSSIRACISGSAPLPV--EVQEKFETVtggKLVEGYGLTESSpVTHSNFlwEKRVpGSIG------------------ 379
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966209822 400 fqkdEPMRNEQGWCIHVKKGE---PGLlISRVNAKNP--FFGYAGPYKHTKDKLlcdvfkkGDVYLNTGDLIVQDQDNFL 474
Cdd:PRK06710 380 ----VPWPDTEAMIMSLETGEalpPGE-IGEIVVKGPqiMKGYWNKPEETAAVL-------QDGWLHTGDVGYMDEDGFF 447
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966209822 475 YFWDRTGDTFRWKGENVATTEVADVIGMLDFIQEANVYGVAiSGYEGRAGMASIILKPNTSLDLEKVYEQVVTFLPAYAC 554
Cdd:PRK06710 448 YVKDRKKDMIVASGFNVYPREVEEVLYEHEKVQEVVTIGVP-DPYRGETVKAFVVLKEGTECSEEELNQFARKYLAAYKV 526
|
570 580
....*....|....*....|....*.
gi 966209822 555 PRFLRIQEKMEATGTFKLLKHQLVED 580
Cdd:PRK06710 527 PKVYEFRDELPKTTVGKILRRVLIEE 552
|
|
| PRK08974 |
PRK08974 |
long-chain-fatty-acid--CoA ligase FadD; |
55-580 |
6.58e-20 |
|
long-chain-fatty-acid--CoA ligase FadD;
Pssm-ID: 236359 [Multi-domain] Cd Length: 560 Bit Score: 93.58 E-value: 6.58e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966209822 55 TVLDKFLSHAKRQPRKPFIIYEGDIYTYQDVDKRSSRVAHVFLNHSSLKKGDTVALLMSNEPDFVHVWFGLAKLGCVVAF 134
Cdd:PRK08974 24 SLVDMFEQAVARYADQPAFINMGEVMTFRKLEERSRAFAAYLQNGLGLKKGDRVALMMPNLLQYPIALFGILRAGMIVVN 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966209822 135 LNTNIRSNSLLNCIRACGPRALVVGADLLGTVEE----------ILPSLSENIS----------VWGMKDSVPQ----GV 190
Cdd:PRK08974 104 VNPLYTPRELEHQLNDSGAKAIVIVSNFAHTLEKvvfktpvkhvILTRMGDQLStakgtlvnfvVKYIKRLVPKyhlpDA 183
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966209822 191 ISLKEKLSTSPdepvpRSHHVVSLLKSTCLYI--FTSGTTGLPKAAVISQLQVLrgSAVL---WAFGCTAHD---IVYIT 262
Cdd:PRK08974 184 ISFRSALHKGR-----RMQYVKPELVPEDLAFlqYTGGTTGVAKGAMLTHRNML--ANLEqakAAYGPLLHPgkeLVVTA 256
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966209822 263 LPLYHSSAAILGISGCVELGATCVL-KKKFSASQFWSDCKKYDVTVFQYIGELCRYLCkQSKREGEKD-HKVRLAIGNGI 340
Cdd:PRK08974 257 LPLYHIFALTVNCLLFIELGGQNLLiTNPRDIPGFVKELKKYPFTAITGVNTLFNALL-NNEEFQELDfSSLKLSVGGGM 335
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966209822 341 rsDVWREFLDRFGNIKVCEL---YAATESS-------ISFMNYTGRIGaigrtnlfYKLLSTFDLIKYDFQKDEPMrneq 410
Cdd:PRK08974 336 --AVQQAVAERWVKLTGQYLlegYGLTECSplvsvnpYDLDYYSGSIG--------LPVPSTEIKLVDDDGNEVPP---- 401
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966209822 411 gwcihvkkGEPGLLIsrvnAKNP--FFGYAGPYKHTKdkllcDVFKKGdvYLNTGDLIVQDQDNFLYFWDRTGDTFRWKG 488
Cdd:PRK08974 402 --------GEPGELW----VKGPqvMLGYWQRPEATD-----EVIKDG--WLATGDIAVMDEEGFLRIVDRKKDMILVSG 462
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966209822 489 ENVATTEVADVIGMLDFIQEANVYGVAiSGYEGRAgMASIILKPNTSLDLEKVYEQVVTFLPAYACPRFLRIQEKMEATG 568
Cdd:PRK08974 463 FNVYPNEIEDVVMLHPKVLEVAAVGVP-SEVSGEA-VKIFVVKKDPSLTEEELITHCRRHLTGYKVPKLVEFRDELPKSN 540
|
570
....*....|..
gi 966209822 569 TFKLLKHQLVED 580
Cdd:PRK08974 541 VGKILRRELRDE 552
|
|
| PRK09088 |
PRK09088 |
acyl-CoA synthetase; Validated |
63-577 |
8.25e-20 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 181644 [Multi-domain] Cd Length: 488 Bit Score: 92.95 E-value: 8.25e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966209822 63 HAKRQPRKPFI--IYEGDIYTYQDVDKRSSRVAHVfLNHSSLKKGDTVALLMSNEPDFVHVWFGLAKLGCVVAFLNTNIR 140
Cdd:PRK09088 4 HARLQPQRLAAvdLALGRRWTYAELDALVGRLAAV-LRRRGCVDGERLAVLARNSVWLVALHFACARVGAIYVPLNWRLS 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966209822 141 SNSLLNCIRACGPRaLVVGADLLGTVEEILPSLSenisvwgmkdsvpqGVISLKEKLSTSPDEPVPRSHhvVSLLkstcl 220
Cdd:PRK09088 83 ASELDALLQDAEPR-LLLGDDAVAAGRTDVEDLA--------------AFIASADALEPADTPSIPPER--VSLI----- 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966209822 221 yIFTSGTTGLPKAAVISQlQVLRGSAVlwAFGCT----AHDIVYITLPLYHSSAAILGISGCVELGATCVLKKKFSASQF 296
Cdd:PRK09088 141 -LFTSGTSGQPKGVMLSE-RNLQQTAH--NFGVLgrvdAHSSFLCDAPMFHIIGLITSVRPVLAVGGSILVSNGFEPKRT 216
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966209822 297 WSDCKKYDVTVFQYIG--ELCRYLCKQSKREGEK-DHKVRLAIGNGIR-SDVWREFLDRfgNIKVCELYAATESSISF-M 371
Cdd:PRK09088 217 LGRLGDPALGITHYFCvpQMAQAFRAQPGFDAAAlRHLTALFTGGAPHaAEDILGWLDD--GIPMVDGFGMSEAGTVFgM 294
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966209822 372 NY-----TGRIGAIG--RTNLFYKLLstfdlikydfqkDEPMRNeqgwcihVKKGEPGLLISRvnAKNPFFGYAGPYKHT 444
Cdd:PRK09088 295 SVdcdviRAKAGAAGipTPTVQTRVV------------DDQGND-------CPAGVPGELLLR--GPNLSPGYWRRPQAT 353
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966209822 445 KDKLlcdvfkKGDVYLNTGDLIVQDQDNFLYFWDRTGDTFRWKGENVATTEVADVIGMLDFIQEANVYGVAISGYeGRAG 524
Cdd:PRK09088 354 ARAF------TGDGWFRTGDIARRDADGFFWVVDRKKDMFISGGENVYPAEIEAVLADHPGIRECAVVGMADAQW-GEVG 426
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|...
gi 966209822 525 MASIILKPNTSLDLEKVYEQVVTFLPAYACPRFLRIQEKMEATGTFKLLKHQL 577
Cdd:PRK09088 427 YLAIVPADGAPLDLERIRSHLSTRLAKYKVPKHLRLVDALPRTASGKLQKARL 479
|
|
| PRK06178 |
PRK06178 |
acyl-CoA synthetase; Validated |
57-307 |
1.15e-19 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 235724 [Multi-domain] Cd Length: 567 Bit Score: 92.80 E-value: 1.15e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966209822 57 LDKFLSH-AKRQPRKPFIIYEGDIYTYQDVDKRSSRVAHVFLNHSsLKKGDTVALLMSNEPDFVHVWFGLAKLGCVVAFL 135
Cdd:PRK06178 35 LTEYLRAwARERPQRPAIIFYGHVITYAELDELSDRFAALLRQRG-VGAGDRVAVFLPNCPQFHIVFFGILKLGAVHVPV 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966209822 136 NTNIRSNSLLNCIRACGPRALVVGADLLGTVEEILPSLS-ENISVWGMKDSVP------------------QGVISLkek 196
Cdd:PRK06178 114 SPLFREHELSYELNDAGAEVLLALDQLAPVVEQVRAETSlRHVIVTSLADVLPaeptlplpdslraprlaaAGAIDL--- 190
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966209822 197 LSTSPDEPVPRSHHVVSLLKSTCLYiFTSGTTGLPKAAVISQLQVL--RGSAVLWAFGCTAHDIVYITLPLYHSSAAILG 274
Cdd:PRK06178 191 LPALRACTAPVPLPPPALDALAALN-YTGGTTGMPKGCEHTQRDMVytAAAAYAVAVVGGEDSVFLSFLPEFWIAGENFG 269
|
250 260 270
....*....|....*....|....*....|...
gi 966209822 275 ISGCVELGATCVLKKKFSASQFWSDCKKYDVTV 307
Cdd:PRK06178 270 LLFPLFSGATLVLLARWDAVAFMAAVERYRVTR 302
|
|
| PRK03640 |
PRK03640 |
o-succinylbenzoate--CoA ligase; |
68-583 |
3.44e-19 |
|
o-succinylbenzoate--CoA ligase;
Pssm-ID: 235146 [Multi-domain] Cd Length: 483 Bit Score: 90.79 E-value: 3.44e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966209822 68 PRKPFIIYEGDIYTYQDVDKRSSRVAHVfLNHSSLKKGDTVALLMSNEPDFVHVWFGLAKLGCVVAFLNTNIRSNSLLNC 147
Cdd:PRK03640 16 PDRTAIEFEEKKVTFMELHEAVVSVAGK-LAALGVKKGDRVALLMKNGMEMILVIHALQQLGAVAVLLNTRLSREELLWQ 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966209822 148 IRAcgpralvVGADLLGTVEEILPSLSENISVwgMKDSVPQGVISLKEKLSTSPDEPVprshhvvsllkSTCLYifTSGT 227
Cdd:PRK03640 95 LDD-------AEVKCLITDDDFEAKLIPGISV--KFAELMNGPKEEAEIQEEFDLDEV-----------ATIMY--TSGT 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966209822 228 TGLPKaAVISQLQVLRGSAVLWA--FGCTAHDIVYITLPLYHssaailgISG------CVELGATCVLKKKFSASQFWSD 299
Cdd:PRK03640 153 TGKPK-GVIQTYGNHWWSAVGSAlnLGLTEDDCWLAAVPIFH-------ISGlsilmrSVIYGMRVVLVEKFDAEKINKL 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966209822 300 CKKYDVTVFQYIGELCRYLCKQSKREGEKDHKVRLAIGNG-IRSDVWREFLDRfgNIKVCELYAATESS-----ISFMNY 373
Cdd:PRK03640 225 LQTGGVTIISVVSTMLQRLLERLGEGTYPSSFRCMLLGGGpAPKPLLEQCKEK--GIPVYQSYGMTETAsqivtLSPEDA 302
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966209822 374 TGRIGAIGRTnLFYKLLStfdlIKYDFQKDEPmrNEQGWcIHVKkgepgllisrvnaknpffgyaGP-----YKHTKDKL 448
Cdd:PRK03640 303 LTKLGSAGKP-LFPCELK----IEKDGVVVPP--FEEGE-IVVK---------------------GPnvtkgYLNREDAT 353
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966209822 449 LcDVFKKGdvYLNTGDLIVQDQDNFLYFWDRTGDTFRWKGENVATTEVADVIGMLDFIQEANVYGVAISGYeGRAGMASI 528
Cdd:PRK03640 354 R-ETFQDG--WFKTGDIGYLDEEGFLYVLDRRSDLIISGGENIYPAEIEEVLLSHPGVAEAGVVGVPDDKW-GQVPVAFV 429
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*
gi 966209822 529 ILkpNTSLDLEKVYEQVVTFLPAYACPRFLRIQEKMEATGTFKLLKHQLVEDGFN 583
Cdd:PRK03640 430 VK--SGEVTEEELRHFCEEKLAKYKVPKRFYFVEELPRNASGKLLRHELKQLVEE 482
|
|
| FAA1 |
COG1022 |
Long-chain acyl-CoA synthetase (AMP-forming) [Lipid transport and metabolism]; |
55-513 |
1.00e-18 |
|
Long-chain acyl-CoA synthetase (AMP-forming) [Lipid transport and metabolism];
Pssm-ID: 440645 [Multi-domain] Cd Length: 603 Bit Score: 90.16 E-value: 1.00e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966209822 55 TVLDKFLSHAKRQPRKPFIIY-EGDIY---TYQDVDKRSSRVAHVFLNHSsLKKGDTVALLMSNEPDFVHVWFGLAKLGC 130
Cdd:COG1022 12 TLPDLLRRRAARFPDRVALREkEDGIWqslTWAEFAERVRALAAGLLALG-VKPGDRVAILSDNRPEWVIADLAILAAGA 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966209822 131 VVAFLNTNIRSNSLLNCIRACGPRALVVG-ADLLGTVEEILPSLSENISVWGMKDSVPQG---VISLKE-----KLSTSP 201
Cdd:COG1022 91 VTVPIYPTSSAEEVAYILNDSGAKVLFVEdQEQLDKLLEVRDELPSLRHIVVLDPRGLRDdprLLSLDEllalgREVADP 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966209822 202 DEPVPRSHHVVslLKSTCLYIFTSGTTGLPKAAVISQLQVL-RGSAVLWAFGCTAHDIVYITLPLYHSSAAILGIsGCVE 280
Cdd:COG1022 171 AELEARRAAVK--PDDLATIIYTSGTTGRPKGVMLTHRNLLsNARALLERLPLGPGDRTLSFLPLAHVFERTVSY-YALA 247
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966209822 281 LGATCVlkkkFSAS--QFWSDCKKYDVTVF-------------------------QYIGELCRYLCKQ---SKREGEK-- 328
Cdd:COG1022 248 AGATVA----FAESpdTLAEDLREVKPTFMlavprvwekvyagiqakaeeagglkRKLFRWALAVGRRyarARLAGKSps 323
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966209822 329 ----------D----HKVRLAIGNGIRS----------DVWReFLDRFGnIKVCELYAATESS-ISFMNYTG--RIGAIG 381
Cdd:COG1022 324 lllrlkhalaDklvfSKLREALGGRLRFavsggaalgpELAR-FFRALG-IPVLEGYGLTETSpVITVNRPGdnRIGTVG 401
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966209822 382 RtnlfykllstfdlikydfqkdePMRNeqgwcIHVKKGEPGLLISRvnAKNPFFGYagpYK---HTKdkllcDVFKKgDV 458
Cdd:COG1022 402 P----------------------PLPG-----VEVKIAEDGEILVR--GPNVMKGY---YKnpeATA-----EAFDA-DG 443
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*...
gi 966209822 459 YLNTGDLIVQDQDNFLYFWDRTGDTFrwK---GENVATTEVADVIGMLDFIQEANVYG 513
Cdd:COG1022 444 WLHTGDIGELDEDGFLRITGRKKDLI--VtsgGKNVAPQPIENALKASPLIEQAVVVG 499
|
|
| LC_FACS_like |
cd05935 |
Putative long-chain fatty acid CoA ligase; The members of this family are putative long-chain ... |
81-577 |
1.44e-18 |
|
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: 88.69 E-value: 1.44e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966209822 81 TYQDVDKRSSRVAHvFLNHSSLKKGDTVALLMSNEPDFVHVWFGLAKLGCVVAFLNTNIRSNSLLNCIRACGPRALVVGA 160
Cdd:cd05935 3 TYLELLEVVKKLAS-FLSNKGVRKGDRVGICLQNSPQYVIAYFAIWRANAVVVPINPMLKERELEYILNDSGAKVAVVGS 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966209822 161 DLlgtveeilpslsenisvwgmkdsvpqgvislkEKLSTSPdepvprshhvvsllkstclyiFTSGTTGLPKAAVISQLQ 240
Cdd:cd05935 82 EL--------------------------------DDLALIP---------------------YTSGTTGLPKGCMHTHFS 108
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966209822 241 VLRGSAVL-WAFGCTAHDIVYITLPLYHSSAAILGISGCVELGATCVLKKKFSASQFWSDCKKYDVTVFQYIGELCRYLC 319
Cdd:cd05935 109 AAANALQSaVWTGLTPSDVILACLPLFHVTGFVGSLNTAVYVGGTYVLMARWDRETALELIEKYKVTFWTNIPTMLVDLL 188
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966209822 320 kQSKREGEKDHKVRLAIGNG---IRSDVWREFLDRFGnIKVCELYAATES-SISFMNYTGRIG----AIGRTNLFYKLLS 391
Cdd:cd05935 189 -ATPEFKTRDLSSLKVLTGGgapMPPAVAEKLLKLTG-LRFVEGYGLTETmSQTHTNPPLRPKlqclGIP*FGVDARVID 266
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966209822 392 TFDLIKYDfqkdepmrneqgwcihvkKGEPGLLIsrVNAKNPFFGYagpYKHTKDKLLCDVFKKGDVYLNTGDLIVQDQD 471
Cdd:cd05935 267 IETGRELP------------------PNEVGEIV--VRGPQIFKGY---WNRPEETEESFIEIKGRRFFRTGDLGYMDEE 323
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966209822 472 NFLYFWDRTGDTFRWKGENVATTEVADVIGMLDFIQEANVYGVAiSGYEGRAGMASIILKP--NTSLDLEKVYEQVVTFL 549
Cdd:cd05935 324 GYFFFVDRVKRMINVSGFKVWPAEVEAKLYKHPAI*EVCVISVP-DERVGEEVKAFIVLRPeyRGKVTEEDIIEWAREQM 402
|
490 500
....*....|....*....|....*...
gi 966209822 550 PAYACPRFLRIQEKMEATGTFKLLKHQL 577
Cdd:cd05935 403 AAYKYPREVEFVDELPRSASGKILWRLL 430
|
|
| CHC_CoA_lg |
cd05903 |
Cyclohexanecarboxylate-CoA ligase (also called cyclohex-1-ene-1-carboxylate:CoA ligase); ... |
80-579 |
2.27e-18 |
|
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: 87.82 E-value: 2.27e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966209822 80 YTYQDVDKRSSRVAHVfLNHSSLKKGDTVALLMSNEPDFVHVWFGLAKLGCVVAFLNTNIRSNSLLNCIRACGPRALVVg 159
Cdd:cd05903 2 LTYSELDTRADRLAAG-LAALGVGPGDVVAFQLPNWWEFAVLYLACLRIGAVTNPILPFFREHELAFILRRAKAKVFVV- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966209822 160 adllgtveeilpslsenISVWGMKDSVPQgvislkeklstsPDEPvprshhvvsllkstCLYIFTSGTTGLPKAAVISQl 239
Cdd:cd05903 80 -----------------PERFRQFDPAAM------------PDAV--------------ALLLFTSGTTGEPKGVMHSH- 115
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966209822 240 QVLRGSAVLWA--FGCTAHDIVYITLPLYHSSAAILGISGCVELGATCVLKKKFSASQFWSDCKKYDVTVFQYIGELCRY 317
Cdd:cd05903 116 NTLSASIRQYAerLGLGPGDVFLVASPMAHQTGFVYGFTLPLLLGAPVVLQDIWDPDKALALMREHGVTFMMGATPFLTD 195
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966209822 318 LCKQSKREGEK--DHKVRLAIGNGIRSDVWREFLDRFGnIKVCELYAATESSISFMNYT-GRIGAIGRTNLFYKLLSTFD 394
Cdd:cd05903 196 LLNAVEEAGEPlsRLRTFVCGGATVPRSLARRAAELLG-AKVCSAYGSTECPGAVTSITpAPEDRRLYTDGRPLPGVEIK 274
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966209822 395 LIKYDFQKDEPmrneqgwcihvkkGEPGLLISRvnAKNPFFGYagpykhTKDKLLCDVFKKGDVYlNTGDLIVQDQDNFL 474
Cdd:cd05903 275 VVDDTGATLAP-------------GVEGELLSR--GPSVFLGY------LDRPDLTADAAPEGWF-RTGDLARLDEDGYL 332
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966209822 475 YFWDRTGDTFRWKGENVATTEVADVIgmldfIQEANVYGVAISGYE----GRAGMASIILKPNTSLDLekvyEQVVTFLP 550
Cdd:cd05903 333 RITGRSKDIIIRGGENIPVLEVEDLL-----LGHPGVIEAAVVALPderlGERACAVVVTKSGALLTF----DELVAYLD 403
|
490 500 510
....*....|....*....|....*....|....
gi 966209822 551 A-----YACPRFLRIQEKMEATGTFKLLKHQLVE 579
Cdd:cd05903 404 RqgvakQYWPERLVHVDDLPRTPSGKVQKFRLRE 437
|
|
| FACL_like_2 |
cd05917 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
223-577 |
2.92e-18 |
|
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: 86.56 E-value: 2.92e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966209822 223 FTSGTTGLPKAAVISQLQVL-RGSAVLWAFGCTAHDIVYITLPLYHSSAAILGISGCVELGATCVL-KKKFSASQFWSDC 300
Cdd:cd05917 9 FTSGTTGSPKGATLTHHNIVnNGYFIGERLGLTEQDRLCIPVPLFHCFGSVLGVLACLTHGATMVFpSPSFDPLAVLEAI 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966209822 301 KKYDVTVFQ-----YIGELcrylcKQSKREGEKDHKVRLAI--GNGIRSDVWREFLDRFGNIKVCELYAATESS-ISFMN 372
Cdd:cd05917 89 EKEKCTALHgvptmFIAEL-----EHPDFDKFDLSSLRTGImaGAPCPPELMKRVIEVMNMKDVTIAYGMTETSpVSTQT 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966209822 373 YTG-----RIGAIGRT--NLFYKLLSTFDlikydfqkdepmrneqgwCIHVKKGEPGLLISRvnaknpffGY---AGPYK 442
Cdd:cd05917 164 RTDdsiekRVNTVGRImpHTEAKIVDPEG------------------GIVPPVGVPGELCIR--------GYsvmKGYWN 217
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966209822 443 -HTKDKLLCDvfkkGDVYLNTGDLIVQDQDNFLYFWDRTGDTFRWKGENVATTEVADVIGMLDFIQEANVYGVAISGYeG 521
Cdd:cd05917 218 dPEKTAEAID----GDGWLHTGDLAVMDEDGYCRIVGRIKDMIIRGGENIYPREIEEFLHTHPKVSDVQVVGVPDERY-G 292
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*.
gi 966209822 522 RAGMASIILKPNTSLDLEKVYEQVVTFLPAYACPRFLRIQEKMEATGTFKLLKHQL 577
Cdd:cd05917 293 EEVCAWIRLKEGAELTEEDIKAYCKGKIAHYKVPRYVFFVDEFPLTVSGKIQKFKL 348
|
|
| BCL_4HBCL |
cd05959 |
Benzoate CoA ligase (BCL) and 4-Hydroxybenzoate-Coenzyme A Ligase (4-HBA-CoA ligase); Benzoate ... |
60-577 |
3.25e-18 |
|
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: 88.19 E-value: 3.25e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966209822 60 FLSHAKRQPRKPFIIYEGDIYTYQDVDKRSSRVAHVFLNhSSLKKGDTVALLMSNEPDFVHVWFGLAKLGCVVAFLNTNI 139
Cdd:cd05959 10 DLNLNEGRGDKTAFIDDAGSLTYAELEAEARRVAGALRA-LGVKREERVLLIMLDTVDFPTAFLGAIRAGIVPVPVNTLL 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966209822 140 RSNSLLNCIRACGPRALVVGADLLGTVEEIL----PSLSENISVWG---------MKDSVPQGVISLKEKlSTSPDEPvp 206
Cdd:cd05959 89 TPDDYAYYLEDSRARVVVVSGELAPVLAAALtkseHTLVVLIVSGGagpeagallLAELVAAEAEQLKPA-ATHADDP-- 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966209822 207 rshhvvsllkstCLYIFTSGTTGLPKAAVISQLQvLRGSAVLWA---FGCTAHDIVYITLPLYHssAAILGISGCVEL-- 281
Cdd:cd05959 166 ------------AFWLYSSGSTGRPKGVVHLHAD-IYWTAELYArnvLGIREDDVCFSAAKLFF--AYGLGNSLTFPLsv 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966209822 282 GATCVLKKKF-SASQFWSDCKKYDVTVFQYIGELCRYLCKQSKREGEKDHKVRLAI--GNGIRSDVWREFLDRFGnIKVC 358
Cdd:cd05959 231 GATTVLMPERpTPAAVFKRIRRYRPTVFFGVPTLYAAMLAAPNLPSRDLSSLRLCVsaGEALPAEVGERWKARFG-LDIL 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966209822 359 ELYAATES-SISFMNYTGRI--GAIGRTNLFYKLlstfdlikydfqkdePMRNEQGwcIHVKKGEPGLLIsrVNAKNPFF 435
Cdd:cd05959 310 DGIGSTEMlHIFLSNRPGRVryGTTGKPVPGYEV---------------ELRDEDG--GDVADGEPGELY--VRGPSSAT 370
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966209822 436 GYAGPYKHTKdkllcDVFKKGdvYLNTGDLIVQDQDNFLYFWDRTGDTFRWKGENVATTEVADVIgmldfIQEANVYGVA 515
Cdd:cd05959 371 MYWNNRDKTR-----DTFQGE--WTRTGDKYVRDDDGFYTYAGRADDMLKVSGIWVSPFEVESAL-----VQHPAVLEAA 438
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966209822 516 ISGYEGRAGM----ASIILKPNTSlDLEKVYEQVVTF----LPAYACPRFLRIQEKMEATGTFKLLKHQL 577
Cdd:cd05959 439 VVGVEDEDGLtkpkAFVVLRPGYE-DSEALEEELKEFvkdrLAPYKYPRWIVFVDELPKTATGKIQRFKL 507
|
|
| PRK07638 |
PRK07638 |
acyl-CoA synthetase; Validated |
55-556 |
8.07e-18 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236071 [Multi-domain] Cd Length: 487 Bit Score: 86.76 E-value: 8.07e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966209822 55 TVLDKFLSHAKRQPRKPFIIYEGDIYTYQDVDKRSSRVAHVFlnHSSLKKGDTVALLMSNEPDFVHVWFGLAKLGCVVAF 134
Cdd:PRK07638 2 GITKEYKKHASLQPNKIAIKENDRVLTYKDWFESVCKVANWL--NEKESKNKTIAILLENRIEFLQLFAGAAMAGWTCVP 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966209822 135 LNTNIRSNSLLNciracgpRALVVGADLLGTVEEILPSLSEnisvwgmkdsVPQGVISL---KEKLSTSPDEPVPrshhv 211
Cdd:PRK07638 80 LDIKWKQDELKE-------RLAISNADMIVTERYKLNDLPD----------EEGRVIEIdewKRMIEKYLPTYAP----- 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966209822 212 VSLLKSTCLYI-FTSGTTGLPKAAVISQLQvlrgsavlW--AFGCTAHDI-------VYITLPLYHSSAAILGISgCVEL 281
Cdd:PRK07638 138 IENVQNAPFYMgFTSGSTGKPKAFLRAQQS--------WlhSFDCNVHDFhmkredsVLIAGTLVHSLFLYGAIS-TLYV 208
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966209822 282 GATCVLKKKFSASQFWSDCKKYDVTVFQYIGELCRYLCKQskrEGEKDHKVRLaIGNGIRsdvW-----REFLDRFGNIK 356
Cdd:PRK07638 209 GQTVHLMRKFIPNQVLDKLETENISVMYTVPTMLESLYKE---NRVIENKMKI-ISSGAK---WeaeakEKIKNIFPYAK 281
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966209822 357 VCELYAATEssISFMNY------TGRIGAIGRtnlfykllsTFDLIKYDfqkdepMRNEQGwcIHVKKGEPGllisRVNA 430
Cdd:PRK07638 282 LYEFYGASE--LSFVTAlvdeesERRPNSVGR---------PFHNVQVR------ICNEAG--EEVQKGEIG----TVYV 338
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966209822 431 KNP--FFGYAGPYKHTKDkllcdvfKKGDVYLNTGDLIVQDQDNFLYFWDRTGDTFRWKGENVATTEVADVIGMLDFIQE 508
Cdd:PRK07638 339 KSPqfFMGYIIGGVLARE-------LNADGWMTVRDVGYEDEEGFIYIVGREKNMILFGGINIFPEEIESVLHEHPAVDE 411
|
490 500 510 520
....*....|....*....|....*....|....*....|....*...
gi 966209822 509 ANVYGVAISgYEGRAGMAsiILKPNTslDLEKVYEQVVTFLPAYACPR 556
Cdd:PRK07638 412 IVVIGVPDS-YWGEKPVA--IIKGSA--TKQQLKSFCLQRLSSFKIPK 454
|
|
| PRK07798 |
PRK07798 |
acyl-CoA synthetase; Validated |
68-366 |
1.33e-17 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236100 [Multi-domain] Cd Length: 533 Bit Score: 86.09 E-value: 1.33e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966209822 68 PRKPFIIYEGDIYTYQDVDKRSSRVAHvFLNHSSLKKGDTVALLMSNEPDFVHVWFGLAKLGCVVAFLNTNIRSNSLLNC 147
Cdd:PRK07798 17 PDRVALVCGDRRLTYAELEERANRLAH-YLIAQGLGPGDHVGIYARNRIEYVEAMLGAFKARAVPVNVNYRYVEDELRYL 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966209822 148 IRACGPRALVVGADLLGTVEEILPSLsENISVW-----GMKDSVPQGVISLKEKLSTSPDEP--VPRShhvvsllkSTCL 220
Cdd:PRK07798 96 LDDSDAVALVYEREFAPRVAEVLPRL-PKLRTLvvvedGSGNDLLPGAVDYEDALAAGSPERdfGERS--------PDDL 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966209822 221 Y-IFTSGTTGLPKAAVISQLQVLRGS--AVLWAFGCTAHD--------------IVYITLPLYHsSAAILGISGCVELGA 283
Cdd:PRK07798 167 YlLYTGGTTGMPKGVMWRQEDIFRVLlgGRDFATGEPIEDeeelakraaagpgmRRFPAPPLMH-GAGQWAAFAALFSGQ 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966209822 284 TCVL--KKKFSASQFWSDCKKYDVTVFQYIGE-LCRYLCKQSKREGEKDHKVRLAIGNG---IRSDVWREFLDRFGNIKV 357
Cdd:PRK07798 246 TVVLlpDVRFDADEVWRTIEREKVNVITIVGDaMARPLLDALEARGPYDLSSLFAIASGgalFSPSVKEALLELLPNVVL 325
|
....*....
gi 966209822 358 CELYAATES 366
Cdd:PRK07798 326 TDSIGSSET 334
|
|
| PRK05605 |
PRK05605 |
long-chain-fatty-acid--CoA ligase; Validated |
51-556 |
2.33e-17 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 235531 [Multi-domain] Cd Length: 573 Bit Score: 85.44 E-value: 2.33e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966209822 51 GELVTVLDKFLShakRQPRKPFIIYEGDIYTYQDVDKRSSRVAHVfLNHSSLKKGDTVALLMSNEPDFVHVWFGLAKLGC 130
Cdd:PRK05605 32 TTLVDLYDNAVA---RFGDRPALDFFGATTTYAELGKQVRRAAAG-LRALGVRPGDRVAIVLPNCPQHIVAFYAVLRLGA 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966209822 131 VVAFLNTNIRSNSLLNCIRACGPRALVVGADLLGTVEEILPSLS-ENI-SV-----------WGMKDSVPQgVISLKEKL 197
Cdd:PRK05605 108 VVVEHNPLYTAHELEHPFEDHGARVAIVWDKVAPTVERLRRTTPlETIvSVnmiaampllqrLALRLPIPA-LRKARAAL 186
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966209822 198 STSPDEPVPRSHHVVSLL--------------KSTCLYIFTSGTTGLPKAAVISQL----QVLRGSAvlWAFGCTAHD-I 258
Cdd:PRK05605 187 TGPAPGTVPWETLVDAAIggdgsdvshprptpDDVALILYTSGTTGKPKGAQLTHRnlfaNAAQGKA--WVPGLGDGPeR 264
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966209822 259 VYITLPLYHSSAAILGISGCVELGATCVLKKKFSASQFWSDCKKYDVTVFQYIGELCRYLCKQSKREGEKDHKVRLAIgN 338
Cdd:PRK05605 265 VLAALPMFHAYGLTLCLTLAVSIGGELVLLPAPDIDLILDAMKKHPPTWLPGVPPLYEKIAEAAEERGVDLSGVRNAF-S 343
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966209822 339 GIRS---DVWREFLDRFGNIKVcELYAATESS-ISF---MNYTGRIGAIGrtnlfYKLLSTFDLI--KYDFQKDEPmrne 409
Cdd:PRK05605 344 GAMAlpvSTVELWEKLTGGLLV-EGYGLTETSpIIVgnpMSDDRRPGYVG-----VPFPDTEVRIvdPEDPDETMP---- 413
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966209822 410 qgwcihvkKGEPGLLIsrvnAKNP--FFGYAGPYKHTKDKLLCDVFKkgdvylnTGDLIVQDQDNFLYFWDR------TG 481
Cdd:PRK05605 414 --------DGEEGELL----VRGPqvFKGYWNRPEETAKSFLDGWFR-------TGDVVVMEEDGFIRIVDRikeliiTG 474
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 966209822 482 dtfrwkGENVATTEVADVIGMLDFIQEANVYGVAIS-GYEGRAgmASIILKPNTSLDLEKVYEQVVTFLPAYACPR 556
Cdd:PRK05605 475 ------GFNVYPAEVEEVLREHPGVEDAAVVGLPREdGSEEVV--AAVVLEPGAALDPEGLRAYCREHLTRYKVPR 542
|
|
| PRK06164 |
PRK06164 |
acyl-CoA synthetase; Validated |
53-579 |
2.38e-17 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 235722 [Multi-domain] Cd Length: 540 Bit Score: 85.57 E-value: 2.38e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966209822 53 LVTVLDkflSHAKRQPRKPFIIYEGDIYTYQDVDKRSSRVAhVFLNHSSLKKGDTVALLMSNEPDFVHVWFGLAKLGCVV 132
Cdd:PRK06164 12 LASLLD---AHARARPDAVALIDEDRPLSRAELRALVDRLA-AWLAAQGVRRGDRVAVWLPNCIEWVVLFLACARLGATV 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966209822 133 AFLNTNIRSNSLLNCIRACGPRALVV-----GADLLGTVEEI----LPSLSENISVWGMKDSVPQGVISLKEKLSTSPDE 203
Cdd:PRK06164 88 IAVNTRYRSHEVAHILGRGRARWLVVwpgfkGIDFAAILAAVppdaLPPLRAIAVVDDAADATPAPAPGARVQLFALPDP 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966209822 204 PVPRSHHVVSLLKSTCLYIF-TSGTTGLPKAAVISQLQVLR-GSAVLWAFGCTAHDIVYITLPL---YHSSAAILGISGc 278
Cdd:PRK06164 168 APPAAAGERAADPDAGALLFtTSGTTSGPKLVLHRQATLLRhARAIARAYGYDPGAVLLAALPFcgvFGFSTLLGALAG- 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966209822 279 velGATCVLKKKFSASQFWSDCKKYDVTVFQYIGELCRYLCKQSKREGEKDHKVRLAIGNgirsdvwreFLDRFGNIkvc 358
Cdd:PRK06164 247 ---GAPLVCEPVFDAARTARALRRHRVTHTFGNDEMLRRILDTAGERADFPSARLFGFAS---------FAPALGEL--- 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966209822 359 elyaATESSISFMNYTGRIGAIGRTNLFykLLSTFDLikydfqkDEPMRNEQ-GWCIH---------------VKKGEPG 422
Cdd:PRK06164 312 ----AALARARGVPLTGLYGSSEVQALV--ALQPATD-------PVSVRIEGgGRPASpearvrardpqdgalLPDGESG 378
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966209822 423 LLisRVNAKNPFFGYAGPYKHTKDKLlcdvfkKGDVYLNTGDLIVQDQDNFLYFWDRTGDTFRWKGENVATTEVADVIGM 502
Cdd:PRK06164 379 EI--EIRAPSLMRGYLDNPDATARAL------TDDGYFRTGDLGYTRGDGQFVYQTRMGDSLRLGGFLVNPAEIEHALEA 450
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966209822 503 LDFIQEANVYGVAISGYEgRAgMASIILKPNTSLDLEKVYEQVVTFLPAYACP-RFLRIQE--KMEATGTFKLLKHQLVE 579
Cdd:PRK06164 451 LPGVAAAQVVGATRDGKT-VP-VAFVIPTDGASPDEAGLMAACREALAGFKVPaRVQVVEAfpVTESANGAKIQKHRLRE 528
|
|
| FACL_like_6 |
cd05922 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
88-578 |
2.95e-17 |
|
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: 84.80 E-value: 2.95e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966209822 88 RSSRVAHVFLNHSsLKKGDTVALLMSNEPDFVHVWFGLAKLGCVVAF----LNTNIRSNSLLNCIRACGPR-ALVV--GA 160
Cdd:cd05922 2 GVSAAASALLEAG-GVRGERVVLILPNRFTYIELSFAVAYAGGRLGLvfvpLNPTLKESVLRYLVADAGGRiVLADagAA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966209822 161 DLLGTVEEILPSLSENISV---WGMKDSVPqGVISLKEKLStspdepvprshhvvsllkstcLYIFTSGTTGLPKAAVIS 237
Cdd:cd05922 81 DRLRDALPASPDPGTVLDAdgiRAARASAP-AHEVSHEDLA---------------------LLLYTSGSTGSPKLVRLS 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966209822 238 QLQVLRG-SAVLWAFGCTAHDIVYITLPLYHSSA-AILGISgcVELGATCVLKKKFSASQ-FWSDCKKYDVTVFQ---YI 311
Cdd:cd05922 139 HQNLLANaRSIAEYLGITADDRALTVLPLSYDYGlSVLNTH--LLRGATLVLTNDGVLDDaFWEDLREHGATGLAgvpST 216
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966209822 312 GELCRYLckqsKREGEKDHKVRL--AIGNGIRSDVWREFLDRFGNIKVCELYAATESS--ISFM------NYTGRIG-AI 380
Cdd:cd05922 217 YAMLTRL----GFDPAKLPSLRYltQAGGRLPQETIARLRELLPGAQVYVMYGQTEATrrMTYLpperilEKPGSIGlAI 292
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966209822 381 GRTNLFykllstfdlikydfqkdepMRNEQGWCIHVkkGEPGLLISRVNakNPFFGYAGPYKHTKDKLLcdvfkKGDVyL 460
Cdd:cd05922 293 PGGEFE-------------------ILDDDGTPTPP--GEPGEIVHRGP--NVMKGYWNDPPYRRKEGR-----GGGV-L 343
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966209822 461 NTGDLIVQDQDNFLYFWDRTGDTFRWKGENVATTEVADVIGMLDFIQEANVYGVAISGYEGRAGMASIILKPNTSLDLEK 540
Cdd:cd05922 344 HTGDLARRDEDGFLFIVGRRDRMIKLFGNRISPTEIEAAARSIGLIIEAAAVGLPDPLGEKLALFVTAPDKIDPKDVLRS 423
|
490 500 510
....*....|....*....|....*....|....*...
gi 966209822 541 VYEQvvtfLPAYACPRFLRIQEKMEATGTFKLLKHQLV 578
Cdd:cd05922 424 LAER----LPPYKVPATVRVVDELPLTASGKVDYAALR 457
|
|
| PRK05677 |
PRK05677 |
long-chain-fatty-acid--CoA ligase; Validated |
51-577 |
7.30e-17 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 168170 [Multi-domain] Cd Length: 562 Bit Score: 84.04 E-value: 7.30e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966209822 51 GELVTVLDKFLSHAKRQPRKPFIIYEGDIYTYQDVDKRSSRVAHVFLNHSSLKKGDTVALLMSNEPDFVHVWFGLAKLGC 130
Cdd:PRK05677 21 DEYPNIQAVLKQSCQRFADKPAFSNLGKTLTYGELYKLSGAFAAWLQQHTDLKPGDRIAVQLPNVLQYPVAVFGAMRAGL 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966209822 131 VVafLNTN--IRSNSLLNCIRACGPRALVVGADLLGTVEEILPS--------------------LSENISVWGMKDSVPQ 188
Cdd:PRK05677 101 IV--VNTNplYTAREMEHQFNDSGAKALVCLANMAHLAEKVLPKtgvkhvivtevadmlpplkrLLINAVVKHVKKMVPA 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966209822 189 ----GVISLKEKLSTSPDEPV----PRSHHVVSLLkstclyiFTSGTTGLPKAAVISQ-------LQVLRGSAVLWAFGC 253
Cdd:PRK05677 179 yhlpQAVKFNDALAKGAGQPVteanPQADDVAVLQ-------YTGGTTGVAKGAMLTHrnlvanmLQCRALMGSNLNEGC 251
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966209822 254 tahDIVYITLPLYHSSAAILGISGCVELGATCVL---KKKFSAsqFWSDCKKYDVTVFQYIGELCRYLCKqskREGEKDH 330
Cdd:PRK05677 252 ---EILIAPLPLYHIYAFTFHCMAMMLIGNHNILisnPRDLPA--MVKELGKWKFSGFVGLNTLFVALCN---NEAFRKL 323
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966209822 331 -----KVRLAIGNGIRSDV---WREFLdrfgNIKVCELYAATESS--ISFMNYTG-RIGAIGrtnlfYKLLSTFDLIKYD 399
Cdd:PRK05677 324 dfsalKLTLSGGMALQLATaerWKEVT----GCAICEGYGMTETSpvVSVNPSQAiQVGTIG-----IPVPSTLCKVIDD 394
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966209822 400 FQKDEPMrneqgwcihvkkGEPGLLIsrVNAKNPFFGYAGPYKHTkDKLLCDvfkkgDVYLNTGDLIVQDQDNFLYFWDR 479
Cdd:PRK05677 395 DGNELPL------------GEVGELC--VKGPQVMKGYWQRPEAT-DEILDS-----DGWLKTGDIALIQEDGYMRIVDR 454
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966209822 480 TGDTFRWKGENVATTEVADVIGMLDFIQEANVYGVAiSGYEGRAGMASIILKPNTSLDLEKVYEQVVTFLPAYACPRFLR 559
Cdd:PRK05677 455 KKDMILVSGFNVYPNELEDVLAALPGVLQCAAIGVP-DEKSGEAIKVFVVVKPGETLTKEQVMEHMRANLTGYKVPKAVE 533
|
570
....*....|....*...
gi 966209822 560 IQEKMEATGTFKLLKHQL 577
Cdd:PRK05677 534 FRDELPTTNVGKILRREL 551
|
|
| CBAL |
cd05923 |
4-Chlorobenzoate-CoA ligase (CBAL); CBAL catalyzes the conversion of 4-chlorobenzoate (4-CB) ... |
81-515 |
7.84e-17 |
|
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: 83.71 E-value: 7.84e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966209822 81 TYQDVDKRSSRVAHVFLNhSSLKKGDTVALLMSNEPDFVHVWFGLAKLGCVVAFLNTNIRSNSLLNCIR---ACG----P 153
Cdd:cd05923 30 TYSELRARIEAVAARLHA-RGLRPGQRVAVVLPNSVEAVIALLALHRLGAVPALINPRLKAAELAELIErgeMTAaviaV 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966209822 154 RALVVGADLLGTVEEI----LPSLSENisvwgmkdsvpqgvislkEKLSTSPDEPVPRShhvvsllKSTCLYIFTSGTTG 229
Cdd:cd05923 109 DAQVMDAIFQSGVRVLalsdLVGLGEP------------------ESAGPLIEDPPREP-------EQPAFVFYTSGTTG 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966209822 230 LPKAAVISQlqvlRGSAVLWAFGCT-------AHDIVYITLPLYHSSAAILGISGCVELGATCVLKKKFSASQFWSDCKK 302
Cdd:cd05923 164 LPKGAVIPQ----RAAESRVLFMSTqaglrhgRHNVVLGLMPLYHVIGFFAVLVAALALDGTYVVVEEFDPADALKLIEQ 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966209822 303 YDVTVFQYIGELCRYLCKQSKREGEKDHKVR-LAIGNGIRSDVWREFLDRFGNIKVCELYAATESSISFMNYTGRIGAIG 381
Cdd:cd05923 240 ERVTSLFATPTHLDALAAAAEFAGLKLSSLRhVTFAGATMPDAVLERVNQHLPGEKVNIYGTTEAMNSLYMRDARTGTEM 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966209822 382 RTNLFykllSTFDLIKYDFQKDEPMRNeqgwcihvkkGEPGLLISRVNAKNPFFGYAGPYKHTKDKLLcdvfkkgDVYLN 461
Cdd:cd05923 320 RPGFF----SEVRIVRIGGSPDEALAN----------GEEGELIVAAAADAAFTGYLNQPEATAKKLQ-------DGWYR 378
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....
gi 966209822 462 TGDLIVQDQDNFLYFWDRTGDTFRWKGENVATTEVADVIGMLDFIQEANVYGVA 515
Cdd:cd05923 379 TGDVGYVDPSGDVRILGRVDDMIISGGENIHPSEIERVLSRHPGVTEVVVIGVA 432
|
|
| PLN03102 |
PLN03102 |
acyl-activating enzyme; Provisional |
60-577 |
1.10e-16 |
|
acyl-activating enzyme; Provisional
Pssm-ID: 215576 [Multi-domain] Cd Length: 579 Bit Score: 83.53 E-value: 1.10e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966209822 60 FLSHAKR-QPRKPFIIYEGDIYTYQDVDKRSSRVAHVFLNhSSLKKGDTVALLMSNEPDFVHVWFGLAKLGCVVAFLNTN 138
Cdd:PLN03102 19 FLKRASEcYPNRTSIIYGKTRFTWPQTYDRCCRLAASLIS-LNITKNDVVSVLAPNTPAMYEMHFAVPMAGAVLNPINTR 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966209822 139 IRSNSLLNCIRACGPRALVVGADLLGTVEEILPSLSENISVWGMKDSVPQGVISLKEKLSTSPD--------EPVPRS-- 208
Cdd:PLN03102 98 LDATSIAAILRHAKPKILFVDRSFEPLAREVLHLLSSEDSNLNLPVIFIHEIDFPKRPSSEELDyecliqrgEPTPSLva 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966209822 209 --------HHVVSLlkstclyIFTSGTTGLPKAAVISQlqvlRG------SAVL-WAFGCTAhdiVYI-TLPLYHSSAAI 272
Cdd:PLN03102 178 rmfriqdeHDPISL-------NYTSGTTADPKGVVISH----RGaylstlSAIIgWEMGTCP---VYLwTLPMFHCNGWT 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966209822 273 LgISGCVELGATCVLKKKFSASQFWSDCKKYDVTVFQYIGELCRYLCKQSKRE-GEKDHKVRLAIGNGIRSDVWREFLDR 351
Cdd:PLN03102 244 F-TWGTAARGGTSVCMRHVTAPEIYKNIEMHNVTHMCCVPTVFNILLKGNSLDlSPRSGPVHVLTGGSPPPAALVKKVQR 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966209822 352 FGnIKVCELYAATESS--ISFMNYTG---------RIGAIGRTNLFYKLLSTFDLIKYDFQKDEPMRNEQGWCIHVKkge 420
Cdd:PLN03102 323 LG-FQVMHAYGLTEATgpVLFCEWQDewnrlpenqQMELKARQGVSILGLADVDVKNKETQESVPRDGKTMGEIVIK--- 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966209822 421 pGLLISRVNAKNPffgyagpykhtkdKLLCDVFKKGdvYLNTGDLIVQDQDNFLYFWDRTGDTFRWKGENVATTEVADVI 500
Cdd:PLN03102 399 -GSSIMKGYLKNP-------------KATSEAFKHG--WLNTGDVGVIHPDGHVEIKDRSKDIIISGGENISSVEVENVL 462
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966209822 501 GMLDFIQEANVYGVAISGYeGRAGMASIILKpNTSLDLEKVYEQVVTF-----------LPAYACPRFLRIQEKMEATGT 569
Cdd:PLN03102 463 YKYPKVLETAVVAMPHPTW-GETPCAFVVLE-KGETTKEDRVDKLVTRerdlieycrenLPHFMCPRKVVFLQELPKNGN 540
|
....*...
gi 966209822 570 FKLLKHQL 577
Cdd:PLN03102 541 GKILKPKL 548
|
|
| PRK05852 |
PRK05852 |
fatty acid--CoA ligase family protein; |
63-567 |
1.64e-16 |
|
fatty acid--CoA ligase family protein;
Pssm-ID: 235625 [Multi-domain] Cd Length: 534 Bit Score: 82.63 E-value: 1.64e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966209822 63 HAKRQPRKPFIIYEGD--IYTYQDVDKRSSRVAhVFLNHSSLKKGDTVALLMSNEPDFVHVWFGLAKLGCVVAFLNTNIR 140
Cdd:PRK05852 25 AATRLPEAPALVVTADriAISYRDLARLVDDLA-GQLTRSGLLPGDRVALRMGSNAEFVVALLAASRADLVVVPLDPALP 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966209822 141 SNSLLNCIRACGPRALVVgaDLLGTVEEILPSLSE-NISVWGMKDSVPQGVISLKEKLSTSpdEPVPRSHHVVSLLKSTC 219
Cdd:PRK05852 104 IAEQRVRSQAAGARVVLI--DADGPHDRAEPTTRWwPLTVNVGGDSGPSGGTLSVHLDAAT--EPTPATSTPEGLRPDDA 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966209822 220 LYIFTSGTTGLPKAAVISQLQVLRG-SAVLWAFGCTAHDIVYITLPLYHSSAAILGISGCVELGATCVL--KKKFSASQF 296
Cdd:PRK05852 180 MIMFTGGTTGLPKMVPWTHANIASSvRAIITGYRLSPRDATVAVMPLYHGHGLIAALLATLASGGAVLLpaRGRFSAHTF 259
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966209822 297 WSDCKKYDVTVFQYIGELCRYLCKQSKRE--GEKDHKVRLaigngIRS-------DVWREFLDRFGNIKVCElYAATESS 367
Cdd:PRK05852 260 WDDIKAVGATWYTAVPTIHQILLERAATEpsGRKPAALRF-----IRScsapltaETAQALQTEFAAPVVCA-FGMTEAT 333
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966209822 368 ISFMnyTGRIGAIGRTNlfYKLLSTFDLIKYDFQKDEPMRNEQGWCIHVKKGEPGLLISRVnaknpFFGYAGPYKHTKDK 447
Cdd:PRK05852 334 HQVT--TTQIEGIGQTE--NPVVSTGLVGRSTGAQIRIVGSDGLPLPAGAVGEVWLRGTTV-----VRGYLGDPTITAAN 404
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966209822 448 llcdvFKKGdvYLNTGDLIVQDQDNFLYFWDRTGDTFRWKGENVATTEVADVIGMLDFIQEANVYGVAISGYeGRAGMAS 527
Cdd:PRK05852 405 -----FTDG--WLRTGDLGSLSAAGDLSIRGRIKELINRGGEKISPERVEGVLASHPNVMEAAVFGVPDQLY-GEAVAAV 476
|
490 500 510 520
....*....|....*....|....*....|....*....|
gi 966209822 528 IILKPNTSLDLEKVYEQVVTFLPAYACPRFLRIQEKMEAT 567
Cdd:PRK05852 477 IVPRESAPPTAEELVQFCRERLAAFEIPASFQEASGLPHT 516
|
|
| AAS_C |
cd05909 |
C-terminal domain of the acyl-acyl carrier protein synthetase (also called ... |
103-572 |
4.72e-16 |
|
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: 81.22 E-value: 4.72e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966209822 103 KKGDTVALLMSNEPDFVHVWFGLAKLGCVVAFLNTNIRSNSLLNCIRACGPRALVVGADLL--GTVEEiLPSLSENISVW 180
Cdd:cd05909 29 KEGENVGVMLPPSAGGALANFALALSGKVPVMLNYTAGLRELRACIKLAGIKTVLTSKQFIekLKLHH-LFDVEYDARIV 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966209822 181 GMKDSvpQGVISLKEKLST------SPDEPVPRSHHVVSLLKSTCLYIFTSGTTGLPKAAVISQLQVLRG-SAVLWAFGC 253
Cdd:cd05909 108 YLEDL--RAKISKADKCKAflagkfPPKWLLRIFGVAPVQPDDPAVILFTSGSEGLPKGVVLSHKNLLANvEQITAIFDP 185
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966209822 254 TAHDIVYITLPLYHSsaaiLGISGCVELGATCVLKKKFSASQFWSD-----CKKYDVTVFQYIGELCRYLCKQSKREGEK 328
Cdd:cd05909 186 NPEDVVFGALPFFHS----FGLTGCLWLPLLSGIKVVFHPNPLDYKkipelIYDKKATILLGTPTFLRGYARAAHPEDFS 261
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966209822 329 dhKVRLAI--GNGIRSDVWREFLDRFGnIKVCELYAATESS----ISFMNYTGRIGAIGRT--NLFYKLLSTFDLIKydf 400
Cdd:cd05909 262 --SLRLVVagAEKLKDTLRQEFQEKFG-IRILEGYGTTECSpvisVNTPQSPNKEGTVGRPlpGMEVKIVSVETHEE--- 335
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966209822 401 qkdepmrneqgwcihVKKGEPGLLISRVNakNPFFGYAGPYKHTkdkllcdVFKKGDVYLNTGDLIVQDQDNFLYFWDRT 480
Cdd:cd05909 336 ---------------VPIGEGGLLLVRGP--NVMLGYLNEPELT-------SFAFGDGWYDTGDIGKIDGEGFLTITGRL 391
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966209822 481 GDTFRWKGENVATTEVADVIGMLDFIQeANVYGVAISgyEGRAGMASIILKPNTSLDLEKVYEQVVTF-LPAYACPRFLR 559
Cdd:cd05909 392 SRFAKIAGEMVSLEAIEDILSEILPED-NEVAVVSVP--DGRKGEKIVLLTTTTDTDPSSLNDILKNAgISNLAKPSYIH 468
|
490
....*....|...
gi 966209822 560 IQEKMEATGTFKL 572
Cdd:cd05909 469 QVEEIPLLGTGKP 481
|
|
| ttLC_FACS_AEE21_like |
cd12118 |
Fatty acyl-CoA synthetases similar to LC-FACS from Thermus thermophiles and Arabidopsis; This ... |
64-577 |
1.49e-15 |
|
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: 79.65 E-value: 1.49e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966209822 64 AKRQPRKPFIIYEGDIYTYQDVDKRSSRVAHVfLNHSSLKKGDTVALLMSNEPDFVHVWFGLAKLGCVVAFLNTNIRSNS 143
Cdd:cd12118 14 AAVYPDRTSIVYGDRRYTWRQTYDRCRRLASA-LAALGISRGDTVAVLAPNTPAMYELHFGVPMAGAVLNALNTRLDAEE 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966209822 144 LLNCIRACGPRALVV-----GADLLGTVE---EILPSLSEnisvWGMkdsvpqgvISLKeklstspdepvprshhvvsll 215
Cdd:cd12118 93 IAFILRHSEAKVLFVdrefeYEDLLAEGDpdfEWIPPADE----WDP--------IALN--------------------- 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966209822 216 kstclyiFTSGTTGLPKAAVISQ----LQVLrGSAVLWAFGctaHDIVYI-TLPLYHSSA--AILGISGcveLGATCVLK 288
Cdd:cd12118 140 -------YTSGTTGRPKGVVYHHrgayLNAL-ANILEWEMK---QHPVYLwTLPMFHCNGwcFPWTVAA---VGGTNVCL 205
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966209822 289 KKFSASQFWSDCKKYDVTVFQYIGELCRYLCKQSKREGEK-DHKVRLAIGNGIRSDVWREFLDRFGnIKVCELYAATESS 367
Cdd:cd12118 206 RKVDAKAIYDLIEKHKVTHFCGAPTVLNMLANAPPSDARPlPHRVHVMTAGAPPPAAVLAKMEELG-FDVTHVYGLTETY 284
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966209822 368 --ISFMNY---------TGRIGAIGRTNLFYKLLSTFDLIKYDFQKDEPMRNEQgwcihvkKGEpglLISRVNA------ 430
Cdd:cd12118 285 gpATVCAWkpewdelptEERARLKARQGVRYVGLEEVDVLDPETMKPVPRDGKT-------IGE---IVFRGNIvmkgyl 354
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966209822 431 KNPffgyagpyKHTKdkllcDVFKKGdvYLNTGDLIVQDQDNFLYFWDRTGDTFRWKGENVATTEVADVIGMLDFIQEAN 510
Cdd:cd12118 355 KNP--------EATA-----EAFRGG--WFHSGDLAVIHPDGYIEIKDRSKDIIISGGENISSVEVEGVLYKHPAVLEAA 419
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 966209822 511 VYGVAISGYeGRAGMASIILKPNTSLDLEKVYEQVVTFLPAYACPRFLRIQEkMEATGTFKLLKHQL 577
Cdd:cd12118 420 VVARPDEKW-GEVPCAFVELKEGAKVTEEEIIAFCREHLAGFMVPKTVVFGE-LPKTSTGKIQKFVL 484
|
|
| PLN02246 |
PLN02246 |
4-coumarate--CoA ligase |
77-307 |
1.81e-15 |
|
4-coumarate--CoA ligase
Pssm-ID: 215137 [Multi-domain] Cd Length: 537 Bit Score: 79.64 E-value: 1.81e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966209822 77 GDIYTYQDVDKRSSRVAhVFLNHSSLKKGDTVALLMSNEPDFVHVWFGLAKLGCVVAFLNTNIRSNSLLNCIRACGPRAL 156
Cdd:PLN02246 48 GRVYTYADVELLSRRVA-AGLHKLGIRQGDVVMLLLPNCPEFVLAFLGASRRGAVTTTANPFYTPAEIAKQAKASGAKLI 126
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966209822 157 VVGADLLGTVEEIlpSLSENISVWGMkDSVPQGVISLKEkLSTSPDEPVP----RSHHVVSLlkstclyIFTSGTTGLPK 232
Cdd:PLN02246 127 ITQSCYVDKLKGL--AEDDGVTVVTI-DDPPEGCLHFSE-LTQADENELPeveiSPDDVVAL-------PYSSGTTGLPK 195
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966209822 233 AA-------VISQLQVLRGSAVlwAFGCTAHDIVYITLPLYH--SSAAILGISgcVELGATCVLKKKFSASQFWSDCKKY 303
Cdd:PLN02246 196 GVmlthkglVTSVAQQVDGENP--NLYFHSDDVILCVLPMFHiySLNSVLLCG--LRVGAAILIMPKFEIGALLELIQRH 271
|
....
gi 966209822 304 DVTV 307
Cdd:PLN02246 272 KVTI 275
|
|
| ttLC_FACS_AlkK_like |
cd12119 |
Fatty acyl-CoA synthetases similar to LC-FACS from Thermus thermophiles; This family includes ... |
76-574 |
1.83e-15 |
|
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: 79.60 E-value: 1.83e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966209822 76 EGDIYTYQDVDKRSSRVAHVfLNHSSLKKGDTVALLMSNEPDFVHVWFGLAKLGCVvafLNT-NIR--SNSLLNCIRACG 152
Cdd:cd12119 22 EVHRYTYAEVAERARRLANA-LRRLGVKPGDRVATLAWNTHRHLELYYAVPGMGAV---LHTiNPRlfPEQIAYIINHAE 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966209822 153 PRALVVGADLLGTVEEILPSLsENISVW-------GMKDSVPQGVISLKEKLST-SPDEPVPR-SHHVVSllkSTClyiF 223
Cdd:cd12119 98 DRVVFVDRDFLPLLEAIAPRL-PTVEHVvvmtddaAMPEPAGVGVLAYEELLAAeSPEYDWPDfDENTAA---AIC---Y 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966209822 224 TSGTTGLPKAAVISQ----LQVLRGSAVLwAFGCTAHDIVYITLPLYHSSAAILGISgCVELGATCVLKKKF----SASQ 295
Cdd:cd12119 171 TSGTTGNPKGVVYSHrslvLHAMAALLTD-GLGLSESDVVLPVVPMFHVNAWGLPYA-AAMVGAKLVLPGPYldpaSLAE 248
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966209822 296 FWsdcKKYDVT-----------VFQYigelcrylckQSKREGEKDHKVRLAIGNGI--RSdVWREFLDRFgnIKVCELYA 362
Cdd:cd12119 249 LI---EREGVTfaagvptvwqgLLDH----------LEANGRDLSSLRRVVIGGSAvpRS-LIEAFEERG--VRVIHAWG 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966209822 363 ATEssisfmnyTGRIGAIGRTNLfykllstfDLIKYDFQKDEPMRNEQGWCIhvkkgePGLLISRVNAKNPF-------F 435
Cdd:cd12119 313 MTE--------TSPLGTVARPPS--------EHSNLSEDEQLALRAKQGRPV------PGVELRIVDDDGRElpwdgkaV 370
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966209822 436 G---YAGP------YKHTKDKLLCDVfkkgDVYLNTGDLIVQDQDNFLYFWDRTGDTFRWKGENVATTEVADVIGMLDFI 506
Cdd:cd12119 371 GelqVRGPwvtksyYKNDEESEALTE----DGWLRTGDVATIDEDGYLTITDRSKDVIKSGGEWISSVELENAIMAHPAV 446
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 966209822 507 QEANVYGVAISGYEGRAgMASIILKPNTSLDLEKVYEQVVTFLPAYACPRFLRIQEKMEATGTFKLLK 574
Cdd:cd12119 447 AEAAVIGVPHPKWGERP-LAVVVLKEGATVTAEELLEFLADKVAKWWLPDDVVFVDEIPKTSTGKIDK 513
|
|
| EntE |
COG1021 |
EntE, 2,3-dihydroxybenzoate-AMP synthase component of non-ribosomal peptide synthetase ... |
57-287 |
6.32e-15 |
|
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: 77.88 E-value: 6.32e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966209822 57 LDKFLS-HAKRQPRKPFIIYEGDIYTYQDVDKRSSRVAHVFLNHSsLKKGDTVALLMSNEPDFVHVWFGLAKLGCVVAFL 135
Cdd:COG1021 27 LGDLLRrRAERHPDRIAVVDGERRLSYAELDRRADRLAAGLLALG-LRPGDRVVVQLPNVAEFVIVFFALFRAGAIPVFA 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966209822 136 NTNIRSNSLLNCIRACGPRALVV-----GADLLGTVEEI---LPSLsENISVWGmkDsvPQGVISLkEKLSTSP---DEP 204
Cdd:COG1021 106 LPAHRRAEISHFAEQSEAVAYIIpdrhrGFDYRALARELqaeVPSL-RHVLVVG--D--AGEFTSL-DALLAAPadlSEP 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966209822 205 VPRSHHVVSLLKStclyiftSGTTGLPKaaVISQ-----LQVLRGSAVLWAFgcTAHDIVYITLPLYH----SSAAILgi 275
Cdd:COG1021 180 RPDPDDVAFFQLS-------GGTTGLPK--LIPRthddyLYSVRASAEICGL--DADTVYLAALPAAHnfplSSPGVL-- 246
|
250
....*....|..
gi 966209822 276 sGCVELGATCVL 287
Cdd:COG1021 247 -GVLYAGGTVVL 257
|
|
| EntF |
COG1020 |
EntF, seryl-AMP synthase component of non-ribosomal peptide synthetase [Secondary metabolites ... |
54-368 |
6.41e-15 |
|
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: 78.75 E-value: 6.41e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966209822 54 VTVLDKFLSHAKRQPRKPFIIYEGDIYTYQDVDKRSSRVAHvFLNHSSLKKGDTVALLMSNEPDFVHVWFGLAKLGCV-- 131
Cdd:COG1020 476 ATLHELFEAQAARTPDAVAVVFGDQSLTYAELNARANRLAH-HLRALGVGPGDLVGVCLERSLEMVVALLAVLKAGAAyv 554
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966209822 132 ----------VAFLntnirsnsllncIRACGPRALVVGADLLGTveeiLPSLSENisvwgmkdsvpqgVISL-KEKLSTS 200
Cdd:COG1020 555 pldpaypaerLAYM------------LEDAGARLVLTQSALAAR----LPELGVP-------------VLALdALALAAE 605
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966209822 201 PDEPVPRSHHVVSLlkstcLY-IFTSGTTGLPKAAVISQLQVLRgsAVLW---AFGCTAHDIVyitlpLYHSS----AAI 272
Cdd:COG1020 606 PATNPPVPVTPDDL-----AYvIYTSGSTGRPKGVMVEHRALVN--LLAWmqrRYGLGPGDRV-----LQFASlsfdASV 673
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966209822 273 LGISGCVELGATCVL---KKKFSASQFWSDCKKYDVTVFQ----YIGELCRYLckqskreGEKDHKVRLAI--GNGIRSD 343
Cdd:COG1020 674 WEIFGALLSGATLVLappEARRDPAALAELLARHRVTVLNltpsLLRALLDAA-------PEALPSLRLVLvgGEALPPE 746
|
330 340
....*....|....*....|....*
gi 966209822 344 VWREFLDRFGNIKVCELYAATESSI 368
Cdd:COG1020 747 LVRRWRARLPGARLVNLYGPTETTV 771
|
|
| PRK07529 |
PRK07529 |
AMP-binding domain protein; Validated |
64-580 |
1.87e-14 |
|
AMP-binding domain protein; Validated
Pssm-ID: 236043 [Multi-domain] Cd Length: 632 Bit Score: 76.53 E-value: 1.87e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966209822 64 AKRQPRKPFIIY--------EGDIYTYQDVDKRSSRVAHVFlnHS-SLKKGDTVALLMSNEPDFVHVWFGLAKLGCVVAf 134
Cdd:PRK07529 35 AARHPDAPALSFlldadpldRPETWTYAELLADVTRTANLL--HSlGVGPGDVVAFLLPNLPETHFALWGGEAAGIANP- 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966209822 135 LNTNIRSNSLLNCIRACGPRALVV-----GADLLGTVEEI---LPSLSENISVWGMKDSVPQ--------------GVIS 192
Cdd:PRK07529 112 INPLLEPEQIAELLRAAGAKVLVTlgpfpGTDIWQKVAEVlaaLPELRTVVEVDLARYLPGPkrlavplirrkahaRILD 191
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966209822 193 LKEKLSTSPDE-----PVPRSHHVVSllkstclYIFTSGTTGLPKAAVISQL-QVLRGSAVLWAFGCTAHDIVYITLPLY 266
Cdd:PRK07529 192 FDAELARQPGDrlfsgRPIGPDDVAA-------YFHTGGTTGMPKLAQHTHGnEVANAWLGALLLGLGPGDTVFCGLPLF 264
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966209822 267 HSSAAILGISGCVELGATCVL------KKKFSASQFWSDCKKYDVTVFQ-----YIGELcrylckQSKREGEKDHKVRLA 335
Cdd:PRK07529 265 HVNALLVTGLAPLARGAHVVLatpqgyRGPGVIANFWKIVERYRINFLSgvptvYAALL------QVPVDGHDISSLRYA 338
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966209822 336 IGNG--IRSDVWREFLDRFGnIKVCELYAATE-SSISFMNYTG---RIGAIGrtnlfykllstfdlIKYDFQKdepMR-- 407
Cdd:PRK07529 339 LCGAapLPVEVFRRFEAATG-VRIVEGYGLTEaTCVSSVNPPDgerRIGSVG--------------LRLPYQR---VRvv 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966209822 408 --NEQGWCIH-VKKGEPGLLIsrVNAKNPFFGYAGPyKHTKDKLLcdvfkkGDVYLNTGDLIVQDQDNFLYFWDRTGDTF 484
Cdd:PRK07529 401 ilDDAGRYLRdCAVDEVGVLC--IAGPNVFSGYLEA-AHNKGLWL------EDGWLNTGDLGRIDADGYFWLTGRAKDLI 471
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966209822 485 RWKGENVATTEVADVIGMLDFIQEANVYGVAiSGYEGRAGMASIILKPNTSLDLEKVYEQVVTFLP--AyACPRFLRIQE 562
Cdd:PRK07529 472 IRGGHNIDPAAIEEALLRHPAVALAAAVGRP-DAHAGELPVAYVQLKPGASATEAELLAFARDHIAerA-AVPKHVRILD 549
|
570
....*....|....*...
gi 966209822 563 KMEATGTFKLLKHQLVED 580
Cdd:PRK07529 550 ALPKTAVGKIFKPALRRD 567
|
|
| FAAL |
cd05931 |
Fatty acyl-AMP ligase (FAAL); FAAL belongs to the class I adenylate forming enzyme family and ... |
63-353 |
2.32e-14 |
|
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: 76.12 E-value: 2.32e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966209822 63 HAKRQPRKP---FIIYEGDI---YTYQDVDKRSSRVAHVFLnhSSLKKGDTVALLMSNEPDFVHVWFG--LAKLGCVVAF 134
Cdd:cd05931 2 RAAARPDRPaytFLDDEGGReetLTYAELDRRARAIAARLQ--AVGKPGDRVLLLAPPGLDFVAAFLGclYAGAIAVPLP 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966209822 135 LNTNIRSNS-LLNCIRACGPRALVVGADLLGTVEEILPSLSENISVWGMkdsvpqgVISLKEKLSTSPDEPVPRSHHVVS 213
Cdd:cd05931 80 PPTPGRHAErLAAILADAGPRVVLTTAAALAAVRAFAASRPAAGTPRLL-------VVDLLPDTSAADWPPPSPDPDDIA 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966209822 214 LLKstclyiFTSGTTGLPKAAVISQLQVLRG-SAVLWAFGCTAHDIVYITLPLYHSSAAILGISGCVELGATCVLkkkFS 292
Cdd:cd05931 153 YLQ------YTSGSTGTPKGVVVTHRNLLANvRQIRRAYGLDPGDVVVSWLPLYHDMGLIGGLLTPLYSGGPSVL---MS 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966209822 293 ASQF------W----SdckKYDVTV-----FQYigELC-RYLcKQSKREGEKDHKVRLAIgNG---IRSDVWREFLDRFG 353
Cdd:cd05931 224 PAAFlrrplrWlrliS---RYRATIsaapnFAY--DLCvRRV-RDEDLEGLDLSSWRVAL-NGaepVRPATLRRFAEAFA 296
|
|
| FADD10 |
cd17635 |
adenylate forming domain, fatty acid CoA ligase (FadD10); This family contains long chain ... |
218-572 |
2.88e-14 |
|
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: 74.22 E-value: 2.88e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966209822 218 TCLYIFTSGTTGLPKAAVISQLQVLRGSAVLWAFG--CTAHDIVYITLPLYHsSAAILGISGCVELGATCVLKKKF-SAS 294
Cdd:cd17635 3 PLAVIFTSGTTGEPKAVLLANKTFFAVPDILQKEGlnWVVGDVTYLPLPATH-IGGLWWILTCLIHGGLCVTGGENtTYK 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966209822 295 QFWSDCKKYDVTVFQYIGELCRYLCKQSKREGEKDHKVRLAIGNG---IRSDVwrEFLDRFGNIKVCELYAATESS---- 367
Cdd:cd17635 82 SLFKILTTNAVTTTCLVPTLLSKLVSELKSANATVPSLRLIGYGGsraIAADV--RFIEATGLTNTAQVYGLSETGtalc 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966209822 368 ISFMNYTGRIGAIGRTnlfykllstfdLIKYDFQkdepMRNEQGwcIHVKKGEPGLLISRVNAKnpFFGYAGPYKHTKDK 447
Cdd:cd17635 160 LPTDDDSIEINAVGRP-----------YPGVDVY----LAATDG--IAGPSASFGTIWIKSPAN--MLGYWNNPERTAEV 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966209822 448 LLcdvfkkgDVYLNTGDLIVQDQDNFLYFWDRTGDTFRWKGENVATTEVADVIGMLDFIQEA-------NVYG------V 514
Cdd:cd17635 221 LI-------DGWVNTGDLGERREDGFLFITGRSSESINCGGVKIAPDEVERIAEGVSGVQECacyeisdEEFGelvglaV 293
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*...
gi 966209822 515 AISGYEGRAGMASIILKPNTSldlekvyeqvvtfLPAYACPRFLRIQEKMEATGTFKL 572
Cdd:cd17635 294 VASAELDENAIRALKHTIRRE-------------LEPYARPSTIVIVTDIPRTQSGKV 338
|
|
| PRK08315 |
PRK08315 |
AMP-binding domain protein; Validated |
59-579 |
3.10e-13 |
|
AMP-binding domain protein; Validated
Pssm-ID: 236236 [Multi-domain] Cd Length: 559 Bit Score: 72.54 E-value: 3.10e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966209822 59 KFLSH-AKRQPRKPFIIY-EGDI-YTYQDVDKRSSRVAHVFLNHSsLKKGDTVALLMSNEPDFVHVWFGLAKLGCVVAFL 135
Cdd:PRK08315 20 QLLDRtAARYPDREALVYrDQGLrWTYREFNEEVDALAKGLLALG-IEKGDRVGIWAPNVPEWVLTQFATAKIGAILVTI 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966209822 136 NTNIRSNSLLNCIRACGPRALVV-----GADLLGTVEEILPSLSENI-------------SVWGMKDSVPQGVISLKEKL 197
Cdd:PRK08315 99 NPAYRLSELEYALNQSGCKALIAadgfkDSDYVAMLYELAPELATCEpgqlqsarlpelrRVIFLGDEKHPGMLNFDELL 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966209822 198 STSPDEPVPRSHHVVSLLKST-CLYI-FTSGTTGLPKAAVISQLQVL-RGSAVLWAFGCTAHDIVYITLPLYHSSAAILG 274
Cdd:PRK08315 179 ALGRAVDDAELAARQATLDPDdPINIqYTSGTTGFPKGATLTHRNILnNGYFIGEAMKLTEEDRLCIPVPLYHCFGMVLG 258
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966209822 275 ISGCVELGATCVlkkkFSASQFwsDCKK-------------YDV-TVFqyIGELcrylckqskregekDHK--------- 331
Cdd:PRK08315 259 NLACVTHGATMV----YPGEGF--DPLAtlaaveeerctalYGVpTMF--IAEL--------------DHPdfarfdlss 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966209822 332 VRLAIGNGirS----DVWREFLDRFGNIKVCELYAATESS-ISFMNYTG-----RIGAIGRT--NLFYKLLstfdlikyd 399
Cdd:PRK08315 317 LRTGIMAG--SpcpiEVMKRVIDKMHMSEVTIAYGMTETSpVSTQTRTDdplekRVTTVGRAlpHLEVKIV--------- 385
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966209822 400 fqkdEPMRNEQgwcihVKKGEPGLLISRvnaknpffGYA---GPYK---HTKDKLlcdvfkKGDVYLNTGDLIVQDQDNF 473
Cdd:PRK08315 386 ----DPETGET-----VPRGEQGELCTR--------GYSvmkGYWNdpeKTAEAI------DADGWMHTGDLAVMDEEGY 442
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966209822 474 LYFwdrTGdtfRWK------GENVATTEVADVIGMLDFIQEANVYGVAISGYeGRAGMASIILKPNTSLDLEKVYEQVVT 547
Cdd:PRK08315 443 VNI---VG---RIKdmiirgGENIYPREIEEFLYTHPKIQDVQVVGVPDEKY-GEEVCAWIILRPGATLTEEDVRDFCRG 515
|
570 580 590
....*....|....*....|....*....|..
gi 966209822 548 FLPAYACPRFLRIQEKMEATGTFKLLKHQLVE 579
Cdd:PRK08315 516 KIAHYKIPRYIRFVDEFPMTVTGKIQKFKMRE 547
|
|
| MACS_like_4 |
cd05969 |
Uncharacterized subfamily of Acetyl-CoA synthetase like family (ACS); This family is most ... |
80-577 |
3.13e-13 |
|
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: 72.15 E-value: 3.13e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966209822 80 YTYQDVDKRSSRVAHVfLNHSSLKKGDTVALLMSNEPDFVHVWFGLAKLGCVV-----AFLNTNIRSnsllnciracgpR 154
Cdd:cd05969 1 YTFAQLKVLSARFANV-LKSLGVGKGDRVFVLSPRSPELYFSMLGIGKIGAVIcplfsAFGPEAIRD------------R 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966209822 155 ALVVGADLLGTVEEilpslsenisvwgmkdsvpqgvisLKEKlsTSPDEPVprshhvvsllkstcLYIFTSGTTGLPKA- 233
Cdd:cd05969 68 LENSEAKVLITTEE------------------------LYER--TDPEDPT--------------LLHYTSGTTGTPKGv 107
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966209822 234 -----AVISQLQV------LRGSAVLWafgCTAhDIVYITLPLYHSSAAIL-GISGCVELGatcvlkkKFSASQFWSDCK 301
Cdd:cd05969 108 lhvhdAMIFYYFTgkyvldLHPDDIYW---CTA-DPGWVTGTVYGIWAPWLnGVTNVVYEG-------RFDAESWYGIIE 176
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966209822 302 KYDVTVF----QYIGELCRYLCKQSKREGEKDHKVRLAIGNGIRSDVWREFLDRFgNIKVCELYAATES-SISFMNYTG- 375
Cdd:cd05969 177 RVKVTVWytapTAIRMLMKEGDELARKYDLSSLRFIHSVGEPLNPEAIRWGMEVF-GVPIHDTWWQTETgSIMIANYPCm 255
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966209822 376 --RIGAIGRTnlfyklLSTFDLIKYDFQKDEPMRNEQGwCIHVKKGEPGLLisrvnakNPFFGYAGPYKHTkdkllcdvF 453
Cdd:cd05969 256 piKPGSMGKP------LPGVKAAVVDENGNELPPGTKG-ILALKPGWPSMF-------RGIWNDEERYKNS--------F 313
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966209822 454 KKGdvYLNTGDLIVQDQDNFLYFWDRTGDTFRWKGENVATTEVADVIGMLDFIQEANVYGVAiSGYEGRAGMASIILKPN 533
Cdd:cd05969 314 IDG--WYLTGDLAYRDEDGYFWFVGRADDIIKTSGHRVGPFEVESALMEHPAVAEAGVIGKP-DPLRGEIIKAFISLKEG 390
|
490 500 510 520
....*....|....*....|....*....|....*....|....*...
gi 966209822 534 TSLDlEKVYEQVVTF----LPAYACPRFLRIQEKMEATGTFKLLKHQL 577
Cdd:cd05969 391 FEPS-DELKEEIINFvrqkLGAHVAPREIEFVDNLPKTRSGKIMRRVL 437
|
|
| PLN02860 |
PLN02860 |
o-succinylbenzoate-CoA ligase |
97-518 |
3.54e-13 |
|
o-succinylbenzoate-CoA ligase
Pssm-ID: 215464 [Multi-domain] Cd Length: 563 Bit Score: 72.52 E-value: 3.54e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966209822 97 LNHSSLKKGDTVALLMSNEPDFVHVWFGLAKLGCVVAFLNTNIRSNSLLNCIRACGPRALVVG------ADLLGTVEeiL 170
Cdd:PLN02860 49 LLRLGLRNGDVVAIAALNSDLYLEWLLAVACAGGIVAPLNYRWSFEEAKSAMLLVRPVMLVTDetcsswYEELQNDR--L 126
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966209822 171 PSLSENISvwgMKDSVPQGVISLKEKLSTSPdepvPRSHHVVSLLKSTC-------LYIFTSGTTGLPKAAVISQLQVLR 243
Cdd:PLN02860 127 PSLMWQVF---LESPSSSVFIFLNSFLTTEM----LKQRALGTTELDYAwapddavLICFTSGTTGRPKGVTISHSALIV 199
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966209822 244 GSAVLWAFGCTAHDIVYI-TLPLYHssaaILGISGC---VELGATCVLKKKFSASQFWSDCKKYDVTVF----QYIGELC 315
Cdd:PLN02860 200 QSLAKIAIVGYGEDDVYLhTAPLCH----IGGLSSAlamLMVGACHVLLPKFDAKAALQAIKQHNVTSMitvpAMMADLI 275
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966209822 316 RYLCKQSKREGEKDHKVRLAIGNGIRSDVWREFLDRFGNIKVCELYAATE--SSISFMnytgrigaigrtNLFYKLLSTF 393
Cdd:PLN02860 276 SLTRKSMTWKVFPSVRKILNGGGSLSSRLLPDAKKLFPNAKLFSAYGMTEacSSLTFM------------TLHDPTLESP 343
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966209822 394 D--LIKYDFQKDEPMRNEQGWCI-----HVK---KGEPGLLISRVNAKNP--FFGYAGPYKHTKDKLlcdvfkKGDVYLN 461
Cdd:PLN02860 344 KqtLQTVNQTKSSSVHQPQGVCVgkpapHVElkiGLDESSRVGRILTRGPhvMLGYWGQNSETASVL------SNDGWLD 417
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*..
gi 966209822 462 TGDLIVQDQDNFLYFWDRTGDTFRWKGENVATTEVADVIgmldfIQEANVYGVAISG 518
Cdd:PLN02860 418 TGDIGWIDKAGNLWLIGRSNDRIKTGGENVYPEEVEAVL-----SQHPGVASVVVVG 469
|
|
| PRK07470 |
PRK07470 |
acyl-CoA synthetase; Validated |
54-585 |
5.43e-13 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 180988 [Multi-domain] Cd Length: 528 Bit Score: 71.61 E-value: 5.43e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966209822 54 VTVLDKFLSH-AKRQPRKPFIIYEGDIYTYQDVDKRSSRVAHVfLNHSSLKKGDTVALLMSNEPDFVHVWFGLAKLGCVv 132
Cdd:PRK07470 6 VMNLAHFLRQaARRFPDRIALVWGDRSWTWREIDARVDALAAA-LAARGVRKGDRILVHSRNCNQMFESMFAAFRLGAV- 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966209822 133 aFLNTNIRS--NSLLNCIRACGPRALVVGADLLGTVE---EILPSLSENISVWGmkdsvPQGVISLKEKLSTSPDEPVPR 207
Cdd:PRK07470 84 -WVPTNFRQtpDEVAYLAEASGARAMICHADFPEHAAavrAASPDLTHVVAIGG-----ARAGLDYEALVARHLGARVAN 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966209822 208 ShhVVSLlKSTCLYIFTSGTTGLPKAAVISQLQVlrgsavlwAF-----------GCTAHDIVYITLPLYHSSaailGIS 276
Cdd:PRK07470 158 A--AVDH-DDPCWFFFTSGTTGRPKAAVLTHGQM--------AFvitnhladlmpGTTEQDASLVVAPLSHGA----GIH 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966209822 277 GCVEL--GATCVL--KKKFSASQFWSDCKKYDVTVFQYIGELCRYLCKQSKREGEKDHKVRLAIGNG---IRSDVWREfL 349
Cdd:PRK07470 223 QLCQVarGAATVLlpSERFDPAEVWALVERHRVTNLFTVPTILKMLVEHPAVDRYDHSSLRYVIYAGapmYRADQKRA-L 301
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966209822 350 DRFGNIKVcELYAATE--SSISFM---------NYTGRIGAIG--RTNLFYKLLstfdlikydfqkDEPMRneqgwciHV 416
Cdd:PRK07470 302 AKLGKVLV-QYFGLGEvtGNITVLppalhdaedGPDARIGTCGfeRTGMEVQIQ------------DDEGR-------EL 361
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966209822 417 KKGEPGLLISRVNAKnpFFGYagpykHTKDKLLCDVFKKGdvYLNTGDLIVQDQDNFLYFWDRTGDTFRWKGENVATTEV 496
Cdd:PRK07470 362 PPGETGEICVIGPAV--FAGY-----YNNPEANAKAFRDG--WFRTGDLGHLDARGFLYITGRASDMYISGGSNVYPREI 432
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966209822 497 ADVIGMLDFIQEANVYGVAiSGYEGRAGMASIILKPNTSLDLEKVYEQVVTFLPAYACPRFLRIQEKMEATG----TFKL 572
Cdd:PRK07470 433 EEKLLTHPAVSEVAVLGVP-DPVWGEVGVAVCVARDGAPVDEAELLAWLDGKVARYKLPKRFFFWDALPKSGygkiTKKM 511
|
570
....*....|...
gi 966209822 573 LKHQLVEDGFNPL 585
Cdd:PRK07470 512 VREELEERGLLDL 524
|
|
| AFD_YhfT-like |
cd17633 |
fatty acid-CoA ligase VraA; This family of acyl-CoA ligases includes Bacillus subtilis YhfT, ... |
220-514 |
9.24e-13 |
|
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: 69.74 E-value: 9.24e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966209822 220 LYI-FTSGTTGLPKAAVISQLQvlrgsavlWA--FGCTAH-------DIVYITLPLYHSsaaiLGISGCVE---LGATCV 286
Cdd:cd17633 3 FYIgFTSGTTGLPKAYYRSERS--------WIesFVCNEDlfnisgeDAILAPGPLSHS----LFLYGAISalyLGGTFI 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966209822 287 LKKKFSASQFWSDCKKYDVTVFQYIGELCRYLCkqskREGEKDHKVR--LAIGNGIRSDVWREFLDRFGNIKVCELYAAT 364
Cdd:cd17633 71 GQRKFNPKSWIRKINQYNATVIYLVPTMLQALA----RTLEPESKIKsiFSSGQKLFESTKKKLKNIFPKANLIEFYGTS 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966209822 365 ESS-ISFMNY--TGRIGAIGRtnLFYKLlstfdlikydfqkDEPMRNEQGwcihvkkGEPGLLisRVNAKNPFFGYAGPY 441
Cdd:cd17633 147 ELSfITYNFNqeSRPPNSVGR--PFPNV-------------EIEIRNADG-------GEIGKI--FVKSEMVFSGYVRGG 202
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 966209822 442 KHTKDKllcdvfkkgdvYLNTGDLIVQDQDNFLYFWDRTGDTFRWKGENVATTEVADVIGMLDFIQEANVYGV 514
Cdd:cd17633 203 FSNPDG-----------WMSVGDIGYVDEEGYLYLVGRESDMIIIGGINIFPTEIESVLKAIPGIEEAIVVGI 264
|
|
| PLN02574 |
PLN02574 |
4-coumarate--CoA ligase-like |
81-577 |
1.27e-12 |
|
4-coumarate--CoA ligase-like
Pssm-ID: 215312 [Multi-domain] Cd Length: 560 Bit Score: 70.64 E-value: 1.27e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966209822 81 TYQDVDKRSSRVAHVFLNHSSLKKGDTVALLMSNEPDFVHVWFGLAKLGCVVAFLNTNIRSNSLLNCIRACGPrALVVGA 160
Cdd:PLN02574 68 SYSELQPLVKSMAAGLYHVMGVRQGDVVLLLLPNSVYFPVIFLAVLSLGGIVTTMNPSSSLGEIKKRVVDCSV-GLAFTS 146
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966209822 161 dlLGTVEEiLPSLSenISVWGMKDSVPQGVIS-----LKEKLSTSPD---EPVPRSHHVVSLLkstclyiFTSGTTGLPK 232
Cdd:PLN02574 147 --PENVEK-LSPLG--VPVIGVPENYDFDSKRiefpkFYELIKEDFDfvpKPVIKQDDVAAIM-------YSSGTTGASK 214
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966209822 233 AAV------ISQLQV-LRGSAVLWAFgcTAHDIVYIT-LPLYHSSAAILGISGCVELGATCVLKKKFSASQFWSDCKKYD 304
Cdd:PLN02574 215 GVVlthrnlIAMVELfVRFEASQYEY--PGSDNVYLAaLPMFHIYGLSLFVVGLLSLGSTIVVMRRFDASDMVKVIDRFK 292
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966209822 305 VTVFQYIGELCRYLCKQSKREGEKDHKVRLAIGNG---IRSDVWREFLDRFGNIKVCELYAATESSisfmnytgrigAIG 381
Cdd:PLN02574 293 VTHFPVVPPILMALTKKAKGVCGEVLKSLKQVSCGaapLSGKFIQDFVQTLPHVDFIQGYGMTEST-----------AVG 361
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966209822 382 RTNLFYKLLSTFDLIKYdfqkdePMRNEQGWCIHVKKGE---PG----LLISRVNAKNPFFGYAGPYKHTKDKllcdvfk 454
Cdd:PLN02574 362 TRGFNTEKLSKYSSVGL------LAPNMQAKVVDWSTGCllpPGncgeLWIQGPGVMKGYLNNPKATQSTIDK------- 428
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966209822 455 kgDVYLNTGDLIVQDQDNFLYFWDRTGDTFRWKGENVATTEVADVIgmldfIQEANVYGVAISGYE----GRAGMASIIL 530
Cdd:PLN02574 429 --DGWLRTGDIAYFDEDGYLYIVDRLKEIIKYKGFQIAPADLEAVL-----ISHPEIIDAAVTAVPdkecGEIPVAFVVR 501
|
490 500 510 520
....*....|....*....|....*....|....*....|....*..
gi 966209822 531 KPNTSLDLEKVYEQVVTFLPAYACPRFLRIQEKMEATGTFKLLKHQL 577
Cdd:PLN02574 502 RQGSTLSQEAVINYVAKQVAPYKKVRKVVFVQSIPKSPAGKILRREL 548
|
|
| MACS_like_2 |
cd05973 |
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the ... |
80-577 |
3.46e-12 |
|
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: 68.70 E-value: 3.46e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966209822 80 YTYQDVDKRSSRVAHvFLNHSSLKKGDTVALLMSNEPDFVHVWFGLAKLGCVVAFLNTNIRSNSLLNCIRACGPRALVVG 159
Cdd:cd05973 1 LTFGELRALSARFAN-ALQELGVGPGDVVAGLLPRTPELVVTILGIWRLGAVYQPLFTAFGPKAIEHRLRTSGARLVVTD 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966209822 160 ADLLgtveeilpslsenisvwgmkdsvpqgvislkEKLSTSPdepvprshhvvsllkstCLYIFTSGTTGLPKaAVISQL 239
Cdd:cd05973 80 AANR-------------------------------HKLDSDP-----------------FVMMFTSGTTGLPK-GVPVPL 110
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966209822 240 QVLR--GSAVLWAFGCTAHDIVY-ITLP-----LYHSsaailgISGCVELG-ATCVLKKKFSASQFWSDCKKYDVTVFQY 310
Cdd:cd05973 111 RALAafGAYLRDAVDLRPEDSFWnAADPgwaygLYYA------ITGPLALGhPTILLEGGFSVESTWRVIERLGVTNLAG 184
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966209822 311 IGELCRYLcKQSKREGEKDHKVRL----AIGNGIRSDVWREFLDRFGnIKVCELYAATESSISFMNYTG-----RIGAIG 381
Cdd:cd05973 185 SPTAYRLL-MAAGAEVPARPKGRLrrvsSAGEPLTPEVIRWFDAALG-VPIHDHYGQTELGMVLANHHAlehpvHAGSAG 262
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966209822 382 RTnlfyklLSTFDLIKYDFQKDEPMrneqgwcihvkKGEPGLLISRVnAKNP---FFGYAGPYKHTKDkllcdvfkkGDV 458
Cdd:cd05973 263 RA------MPGWRVAVLDDDGDELG-----------PGEPGRLAIDI-ANSPlmwFRGYQLPDTPAID---------GGY 315
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966209822 459 YLnTGDLIVQDQDNFLYFWDRTGDTFRWKGENVATTEVADVIGMLDFIQEANVYGVAiSGYEGRAGMASIILKPNT--SL 536
Cdd:cd05973 316 YL-TGDTVEFDPDGSFSFIGRADDVITMSGYRIGPFDVESALIEHPAVAEAAVIGVP-DPERTEVVKAFVVLRGGHegTP 393
|
490 500 510 520
....*....|....*....|....*....|....*....|..
gi 966209822 537 DLEKVYEQVV-TFLPAYACPRFLRIQEKMEATGTFKLLKHQL 577
Cdd:cd05973 394 ALADELQLHVkKRLSAHAYPRTIHFVDELPKTPSGKIQRFLL 435
|
|
| AMP-binding_C |
pfam13193 |
AMP-binding enzyme C-terminal domain; This is a small domain that is found C terminal to ... |
495-571 |
9.88e-12 |
|
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: 60.64 E-value: 9.88e-12
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 966209822 495 EVADVIGMLDFIQEANVYGVAISgYEGRAGMASIILKPNTSLDLEKVYEQVVTFLPAYACPRFLRIQEKMEATGTFK 571
Cdd:pfam13193 1 EVESALVSHPAVAEAAVVGVPDE-LKGEAPVAFVVLKPGVELLEEELVAHVREELGPYAVPKEVVFVDELPKTRSGK 76
|
|
| PRK06188 |
PRK06188 |
acyl-CoA synthetase; Validated |
65-545 |
1.53e-11 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 235731 [Multi-domain] Cd Length: 524 Bit Score: 66.93 E-value: 1.53e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966209822 65 KRQPRKPFIIYEGDIYTYQDVDKRSSRVAHVFlnHS-SLKKGDTVALLMSNEPDfvhVWFGLAKlGCVVAFlntniRSNS 143
Cdd:PRK06188 23 KRYPDRPALVLGDTRLTYGQLADRISRYIQAF--EAlGLGTGDAVALLSLNRPE---VLMAIGA-AQLAGL-----RRTA 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966209822 144 L---------LNCIRACGPRALVV--------GADLLGTVeeilPSLSENISVwgmkDSVPQGV--ISLKEKLSTSPDEP 204
Cdd:PRK06188 92 LhplgslddhAYVLEDAGISTLIVdpapfverALALLARV----PSLKHVLTL----GPVPDGVdlLAAAAKFGPAPLVA 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966209822 205 VPRSHHVVSLlkstclyIFTSGTTGLPKAAVISQLQVLRGSAVLWA-FGCTAHDIVYITLPLYHSSAAIlgISGCVELGA 283
Cdd:PRK06188 164 AALPPDIAGL-------AYTGGTTGKPKGVMGTHRSIATMAQIQLAeWEWPADPRFLMCTPLSHAGGAF--FLPTLLRGG 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966209822 284 TCVLKKKFSASQFWSDCKKYDVT-VFQYIGELCRYLckqskregekDHK----------------------VRLAigngi 340
Cdd:PRK06188 235 TVIVLAKFDPAEVLRAIEEQRITaTFLVPTMIYALL----------DHPdlrtrdlssletvyygaspmspVRLA----- 299
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966209822 341 rsdvwrEFLDRFGNIKVcELYAATE--SSISFM-------NYTGRIGAIGRTNLF--YKLLstfdlikydfqkDEPMRne 409
Cdd:PRK06188 300 ------EAIERFGPIFA-QYYGQTEapMVITYLrkrdhdpDDPKRLTSCGRPTPGlrVALL------------DEDGR-- 358
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966209822 410 qgwciHVKKGEPGLLISRvnakNPFF--GYagpykHTKDKLLCDVFKKGdvYLNTGDLIVQDQDNFLYFWDRTGDTFRWK 487
Cdd:PRK06188 359 -----EVAQGEVGEICVR----GPLVmdGY-----WNRPEETAEAFRDG--WLHTGDVAREDEDGFYYIVDRKKDMIVTG 422
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*...
gi 966209822 488 GENVATTEVADVIGMLDFIQEANVYGVAISGYeGRAGMASIILKPNTSLDLEKVYEQV 545
Cdd:PRK06188 423 GFNVFPREVEDVLAEHPAVAQVAVIGVPDEKW-GEAVTAVVVLRPGAAVDAAELQAHV 479
|
|
| AACS_like |
cd05968 |
Uncharacterized acyl-CoA synthetase subfamily similar to Acetoacetyl-CoA synthetase; This ... |
26-574 |
2.91e-11 |
|
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: 66.36 E-value: 2.91e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966209822 26 YFWDDFwfvLKVVLIIiRLKKYEK--------------RGELVTVLDKFLSHAKR-QPRKPFIIYEGD-----IYTYQDV 85
Cdd:cd05968 22 WFWGEF---VKDVGIE-WYEPPYQtldlsggkpwaawfVGGRMNIVEQLLDKWLAdTRTRPALRWEGEdgtsrTLTYGEL 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966209822 86 DKRSSRVAHvFLNHSSLKKGDTVALLMSNEPDFVHVWFGLAKLGCVVAFLNTNIRSNSLLNCIRACGPRALVVG------ 159
Cdd:cd05968 98 LYEVKRLAN-GLRALGVGKGDRVGIYLPMIPEIVPAFLAVARIGGIVVPIFSGFGKEAAATRLQDAEAKALITAdgftrr 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966209822 160 ---ADLLGTVEEIL---PSLSENISVWGMKDSVPQ---GVISLKEKLSTSPDEpVPRSHHvvsllKSTCLYIFTSGTTGL 230
Cdd:cd05968 177 greVNLKEEADKACaqcPTVEKVVVVRHLGNDFTPakgRDLSYDEEKETAGDG-AERTES-----EDPLMIIYTSGTTGK 250
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966209822 231 PKAAVIS--------------QLQVLRGSAVLWafgctAHDIVYITLPLYhssaailgISGCVELGATCVLKKKF----S 292
Cdd:cd05968 251 PKGTVHVhagfplkaaqdmyfQFDLKPGDLLTW-----FTDLGWMMGPWL--------IFGGLILGATMVLYDGApdhpK 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966209822 293 ASQFWSDCKKYDVTVFQYIGELCRYLCKQSKREGEKDHK--VRLAIGNG--IRSDVWREFLDRFG--NIKVCELYAATEs 366
Cdd:cd05968 318 ADRLWRMVEDHEITHLGLSPTLIRALKPRGDAPVNAHDLssLRVLGSTGepWNPEPWNWLFETVGkgRNPIINYSGGTE- 396
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966209822 367 sIS---FMNYTGR-IGAIGrtnlFYKLLSTFDLIKYDfqkdepmrnEQGWCIHVKKGEPGLLisrvnakNPFFGYAGPYK 442
Cdd:cd05968 397 -ISggiLGNVLIKpIKPSS----FNGPVPGMKADVLD---------ESGKPARPEVGELVLL-------APWPGMTRGFW 455
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966209822 443 HTKDKLLCDVFKKGDVYLNTGDLIVQDQDNFLYFWDRTGDTFRWKGENVATTEVADVIGMLDFIQEANVYGVAiSGYEGR 522
Cdd:cd05968 456 RDEDRYLETYWSRFDNVWVHGDFAYYDEEGYFYILGRSDDTINVAGKRVGPAEIESVLNAHPAVLESAAIGVP-HPVKGE 534
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|....*
gi 966209822 523 AGMASIILKPN---TSLDLEKVYEQVVTFLPAYACPRFLRIQEKMEATGTFKLLK 574
Cdd:cd05968 535 AIVCFVVLKPGvtpTEALAEELMERVADELGKPLSPERILFVKDLPKTRNAKVMR 589
|
|
| PRK07059 |
PRK07059 |
Long-chain-fatty-acid--CoA ligase; Validated |
53-577 |
3.21e-11 |
|
Long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 235923 [Multi-domain] Cd Length: 557 Bit Score: 66.20 E-value: 3.21e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966209822 53 LVTVLDKflSHAKRQPRKPFIIYEGDIyTYQDVDKRSSRVAhVFLNHSSLKKGDTVALLMSNEPDFVHVWFGLAKLGCVV 132
Cdd:PRK07059 25 LADLLEE--SFRQYADRPAFICMGKAI-TYGELDELSRALA-AWLQSRGLAKGARVAIMMPNVLQYPVAIAAVLRAGYVV 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966209822 133 AFLNTNIRSNSLLNCIRACGPRALVVGADLLGTVEEILPSLS-ENISVWGMKD-----------------------SVPq 188
Cdd:PRK07059 101 VNVNPLYTPRELEHQLKDSGAEAIVVLENFATTVQQVLAKTAvKHVVVASMGDllgfkghivnfvvrrvkkmvpawSLP- 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966209822 189 GVISLKEKLSTSPD---EPVPRSHHVVSLLKstclyiFTSGTTGLPKAAVISQLQVLrgSAVL----W---AFGCTAHDI 258
Cdd:PRK07059 180 GHVRFNDALAEGARqtfKPVKLGPDDVAFLQ------YTGGTTGVSKGATLLHRNIV--ANVLqmeaWlqpAFEKKPRPD 251
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966209822 259 VYIT---LPLYHSSA----AILGISgcveLGATCVL-KKKFSASQFWSDCKKYDVTVFQYIGELCRYLCKQSKREGEKDH 330
Cdd:PRK07059 252 QLNFvcaLPLYHIFAltvcGLLGMR----TGGRNILiPNPRDIPGFIKELKKYQVHIFPAVNTLYNALLNNPDFDKLDFS 327
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966209822 331 KVRLAIGNG--IRSDVWREFLDRFGnIKVCELYAATESS-------ISFMNYTGRIGaigrtnlfYKLLSTFDLIKYDFQ 401
Cdd:PRK07059 328 KLIVANGGGmaVQRPVAERWLEMTG-CPITEGYGLSETSpvatcnpVDATEFSGTIG--------LPLPSTEVSIRDDDG 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966209822 402 KDEPMrneqgwcihvkkGEPGLLISR---VNAknpffGYAGPYKHTKDKLLCDVFKKgdvylnTGDLIVQDQDNFLYFWD 478
Cdd:PRK07059 399 NDLPL------------GEPGEICIRgpqVMA-----GYWNRPDETAKVMTADGFFR------TGDVGVMDERGYTKIVD 455
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966209822 479 RTGDTFRWKGENVATTEVADVIGMLDFIQEANVYGVAisgyEGRAGMA--SIILKPNTSLDLEKVYEQVVTFLPAYACPR 556
Cdd:PRK07059 456 RKKDMILVSGFNVYPNEIEEVVASHPGVLEVAAVGVP----DEHSGEAvkLFVVKKDPALTEEDVKAFCKERLTNYKRPK 531
|
570 580
....*....|....*....|.
gi 966209822 557 FLRIQEKMEATGTFKLLKHQL 577
Cdd:PRK07059 532 FVEFRTELPKTNVGKILRREL 552
|
|
| PRK13295 |
PRK13295 |
cyclohexanecarboxylate-CoA ligase; Reviewed |
55-579 |
6.53e-11 |
|
cyclohexanecarboxylate-CoA ligase; Reviewed
Pssm-ID: 171961 [Multi-domain] Cd Length: 547 Bit Score: 65.07 E-value: 6.53e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966209822 55 TVLDKFLSHAKRQPRKP-FIIYEGDI-----YTYQDVDKRSSRVAhVFLNHSSLKKGDTVALLMSNEPDFVHVWFGLAKL 128
Cdd:PRK13295 25 TINDDLDACVASCPDKTaVTAVRLGTgaprrFTYRELAALVDRVA-VGLARLGVGRGDVVSCQLPNWWEFTVLYLACSRI 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966209822 129 GCVVAFLNTNIRSNSLLNCIRACGPRALVV-----GADLLGTVEEI---LPSLSENISVWGmkdsvpQGVISLKEKLSTS 200
Cdd:PRK13295 104 GAVLNPLMPIFRERELSFMLKHAESKVLVVpktfrGFDHAAMARRLrpeLPALRHVVVVGG------DGADSFEALLITP 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966209822 201 PDEPVPRSHHVVSLLK----STCLYIFTSGTTGLPKAavisqlqVLRGSAVLWA--------FGCTAHDIVYITLPLYHS 268
Cdd:PRK13295 178 AWEQEPDAPAILARLRpgpdDVTQLIYTSGTTGEPKG-------VMHTANTLMAnivpyaerLGLGADDVILMASPMAHQ 250
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966209822 269 SAAILGISGCVELGATCVLKKKFSASQFWSDCKKYDVTvFQ-----YIGELCRylckqSKREGEKDH---KVRLAIGNGI 340
Cdd:PRK13295 251 TGFMYGLMMPVMLGATAVLQDIWDPARAAELIRTEGVT-FTmastpFLTDLTR-----AVKESGRPVsslRTFLCAGAPI 324
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966209822 341 RSDVWREFLDRFGnIKVCELYAATESsisfmnytgriGAIGRTNL--FYKLLSTFD----------LIKYDFQKdepmrn 408
Cdd:PRK13295 325 PGALVERARAALG-AKIVSAWGMTEN-----------GAVTLTKLddPDERASTTDgcplpgvevrVVDADGAP------ 386
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966209822 409 eqgwcihVKKGEPGLLISRvnAKNPFFGYAGPYKHTKDkllcdvfkKGDVYLNTGDLIVQDQDNFLYFWDRTGDTFRWKG 488
Cdd:PRK13295 387 -------LPAGQIGRLQVR--GCSNFGGYLKRPQLNGT--------DADGWFDTGDLARIDADGYIRISGRSKDVIIRGG 449
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966209822 489 ENVATTEVADVIGMLDFIQEanvygVAISGYE----GRAGMASIILKPNTSLDLekvyEQVVTFLPAYAC-----PRFLR 559
Cdd:PRK13295 450 ENIPVVEIEALLYRHPAIAQ-----VAIVAYPderlGERACAFVVPRPGQSLDF----EEMVEFLKAQKVakqyiPERLV 520
|
570 580
....*....|....*....|
gi 966209822 560 IQEKMEATGTFKLLKHQLVE 579
Cdd:PRK13295 521 VRDALPRTPSGKIQKFRLRE 540
|
|
| PRK05857 |
PRK05857 |
fatty acid--CoA ligase; |
45-537 |
1.10e-10 |
|
fatty acid--CoA ligase;
Pssm-ID: 180293 [Multi-domain] Cd Length: 540 Bit Score: 64.26 E-value: 1.10e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966209822 45 KKYEKRGEL-VTVLDKFLSHAKRQPrKPFIIYEGD---IYTYQDVDKRSSRVAHVfLNHSSLKKGDTVALLMSNEPDFVH 120
Cdd:PRK05857 4 KKFQAMPQLpSTVLDRVFEQARQQP-EAIALRRCDgtsALRYRELVAEVGGLAAD-LRAQSVSRGSRVLVISDNGPETYL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966209822 121 VWFGLAKLGCVVAFLNTNIRSNSLLNCIRACGPRALV------VGADLLGTVEEILPSLSENISVWGMKDSVPQGVISLK 194
Cdd:PRK05857 82 SVLACAKLGAIAVMADGNLPIAAIERFCQITDPAAALvapgskMASSAVPEALHSIPVIAVDIAAVTRESEHSLDAASLA 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966209822 195 EKLSTSPDEPVPrshhvvsllkstclYIFTSGTTGLPKAAVISQL------QVLRGSAVLWaFGCTAHDIVYITLPLYHs 268
Cdd:PRK05857 162 GNADQGSEDPLA--------------MIFTSGTTGEPKAVLLANRtffavpDILQKEGLNW-VTWVVGETTYSPLPATH- 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966209822 269 SAAILGISGCVELGATCVLKKKFSAS--QFWSDCKkydVTVFQYIGELCRYLCKQSKREGEKDHKVRLAIGNGIR---SD 343
Cdd:PRK05857 226 IGGLWWILTCLMHGGLCVTGGENTTSllEILTTNA---VATTCLVPTLLSKLVSELKSANATVPSLRLVGYGGSRaiaAD 302
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966209822 344 VwrEFLDRFGnIKVCELYAATE---SSISFMNYTGRI-----GAIGRTnlfYKLLSTFdlikydfqkdepMRNEQGWCIH 415
Cdd:PRK05857 303 V--RFIEATG-VRTAQVYGLSEtgcTALCLPTDDGSIvkieaGAVGRP---YPGVDVY------------LAATDGIGPT 364
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966209822 416 VKKGEPGLLISRVNAKNP--FFGYAGPYKHTKDKLLcdvfkkgDVYLNTGDLIVQDQDNFLYFWDRTGDTFRWKGENVAT 493
Cdd:PRK05857 365 APGAGPSASFGTLWIKSPanMLGYWNNPERTAEVLI-------DGWVNTGDLLERREDGFFYIKGRSSEMIICGGVNIAP 437
|
490 500 510 520
....*....|....*....|....*....|....*....|....
gi 966209822 494 TEVADVIGMLDFIQEANVYGVAISGYEGRAGMASIilkPNTSLD 537
Cdd:PRK05857 438 DEVDRIAEGVSGVREAACYEIPDEEFGALVGLAVV---ASAELD 478
|
|
| MACS_euk |
cd05928 |
Eukaryotic Medium-chain acyl-CoA synthetase (MACS or ACSM); MACS catalyzes the two-step ... |
80-496 |
1.27e-10 |
|
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: 64.02 E-value: 1.27e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966209822 80 YTYQDVDKRSSRVAHVFLNHSSLKKGDTVALLMSNEPDFVHVWFGLAKLGCVVAFLNTNIRSNSLLNCIRACGPRALVVG 159
Cdd:cd05928 42 WSFRELGSLSRKAANVLSGACGLQRGDRVAVILPRVPEWWLVNVACIRTGLVFIPGTIQLTAKDILYRLQASKAKCIVTS 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966209822 160 ADLLGTVEEIL---PSLSENISVwgmKDSVPQGVISLKEKLSTSPDEpvprsHHVVSLLKSTCLYI-FTSGTTGLPKAAV 235
Cdd:cd05928 122 DELAPEVDSVAsecPSLKTKLLV---SEKSRDGWLNFKELLNEASTE-----HHCVETGSQEPMAIyFTSGTTGSPKMAE 193
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966209822 236 ISQLQVLRGSAV---LWaFGCTAHDIVYITLPLYHSSAAILGISGCVELGAtCV---LKKKFSASQFWSDCKKYDVTVFQ 309
Cdd:cd05928 194 HSHSSLGLGLKVngrYW-LDLTASDIMWNTSDTGWIKSAWSSLFEPWIQGA-CVfvhHLPRFDPLVILKTLSSYPITTFC 271
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966209822 310 YIGELCRYLCKQS-KREGEKDHKVRLAIGNGIRSDVWREFLDRFGnIKVCELYAATESSISFMNYTG---RIGAIGRTNL 385
Cdd:cd05928 272 GAPTVYRMLVQQDlSSYKFPSLQHCVTGGEPLNPEVLEKWKAQTG-LDIYEGYGQTETGLICANFKGmkiKPGSMGKASP 350
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966209822 386 fykllstfdliKYDFQkdepMRNEQGWCihVKKGEPGLLISRVNAKNPFFGYAGpYKHTKDKllCDVFKKGDVYLnTGDL 465
Cdd:cd05928 351 -----------PYDVQ----IIDDNGNV--LPPGTEGDIGIRVKPIRPFGLFSG-YVDNPEK--TAATIRGDFYL-TGDR 409
|
410 420 430
....*....|....*....|....*....|.
gi 966209822 466 IVQDQDNFLYFWDRTGDTFRWKGENVATTEV 496
Cdd:cd05928 410 GIMDEDGYFWFMGRADDVINSSGYRIGPFEV 440
|
|
| PRK04319 |
PRK04319 |
acetyl-CoA synthetase; Provisional |
80-307 |
1.33e-10 |
|
acetyl-CoA synthetase; Provisional
Pssm-ID: 235279 [Multi-domain] Cd Length: 570 Bit Score: 64.15 E-value: 1.33e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966209822 80 YTYQDVDKRSSRVAHVFLNHSsLKKGDTVALLMSNEPDFVHVWFGLAKLGCVV-----AFLNTNIRSNsllncIRACGPR 154
Cdd:PRK04319 74 YTYKELKELSNKFANVLKELG-VEKGDRVFIFMPRIPELYFALLGALKNGAIVgplfeAFMEEAVRDR-----LEDSEAK 147
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966209822 155 ALVVGADLLG-TVEEILPSLsENISVWGMKDSVPQGVISLKEKLSTSPD--EPVPRSHHVVSLLKstclyiFTSGTTGLP 231
Cdd:PRK04319 148 VLITTPALLErKPADDLPSL-KHVLLVGEDVEEGPGTLDFNALMEQASDefDIEWTDREDGAILH------YTSGSTGKP 220
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966209822 232 KA------AVISQLQV------LRGSAVLWafgCTAhDIVYITLPLYhssaailGISGCVELGAT-CVLKKKFSASQFWS 298
Cdd:PRK04319 221 KGvlhvhnAMLQHYQTgkyvldLHEDDVYW---CTA-DPGWVTGTSY-------GIFAPWLNGATnVIDGGRFSPERWYR 289
|
....*....
gi 966209822 299 DCKKYDVTV 307
Cdd:PRK04319 290 ILEDYKVTV 298
|
|
| ACS |
cd05966 |
Acetyl-CoA synthetase (also known as acetate-CoA ligase and acetyl-activating enzyme); ... |
63-308 |
1.34e-10 |
|
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: 64.12 E-value: 1.34e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966209822 63 HAKRQPRKPFIIYEGD------IYTYQDVDKRSSRVAHVFLNHsSLKKGDTVALLMSNEPDFVHVWFGLAKLGCV--VAF 134
Cdd:cd05966 62 HLKERGDKVAIIWEGDepdqsrTITYRELLREVCRFANVLKSL-GVKKGDRVAIYMPMIPELVIAMLACARIGAVhsVVF 140
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966209822 135 lnTNIRSNSLLNCIRACGPRaLVVGAD----------LLGTVEEIL---PSLsENISVWGMKDsvpqGVISLKEKLstsp 201
Cdd:cd05966 141 --AGFSAESLADRINDAQCK-LVITADggyrggkvipLKEIVDEALekcPSV-EKVLVVKRTG----GEVPMTEGR---- 208
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966209822 202 DEPVprsHHVVSLLKSTC----------LYI-FTSGTTGLPKAAVISQlqvlrGSAVLWA---------------FGCTA 255
Cdd:cd05966 209 DLWW---HDLMAKQSPECepewmdsedpLFIlYTSGSTGKPKGVVHTT-----GGYLLYAattfkyvfdyhpddiYWCTA 280
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|
gi 966209822 256 hDIVYITlplYHSsaaiLGISGCVELGATCVLkkkF-------SASQFWSDCKKYDVTVF 308
Cdd:cd05966 281 -DIGWIT---GHS----YIVYGPLANGATTVM---FegtptypDPGRYWDIVEKHKVTIF 329
|
|
| VL_LC_FACS_like |
cd05907 |
Long-chain fatty acid CoA synthetases and Bubblegum-like very long-chain fatty acid CoA ... |
80-513 |
1.72e-10 |
|
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: 63.38 E-value: 1.72e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966209822 80 YTYQDVDKRSSRVAHVFLNHSsLKKGDTVALLMSNEPDfvhvWFgLAKLGCVVAflntnirsnsllnciracgpRALVVG 159
Cdd:cd05907 6 ITWAEFAEEVRALAKGLIALG-VEPGDRVAILSRNRPE----WT-IADLAILAI--------------------GAVPVP 59
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966209822 160 adllgtveeILPSLSENISVWGMKDSVPQGVIslkeklstspdepvprshhvVSLLKSTCLYIFTSGTTGLPKAAVISQ- 238
Cdd:cd05907 60 ---------IYPTSSAEQIAYILNDSEAKALF--------------------VEDPDDLATIIYTSGTTGRPKGVMLSHr 110
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966209822 239 --LQVLRGSAVLWAFGCTAHDIVYitLPLYHSSAAILGISGCVELGATCVLkkKFSASQFWSDCKKYDVTVFQYIGELCR 316
Cdd:cd05907 111 niLSNALALAERLPATEGDRHLSF--LPLAHVFERRAGLYVPLLAGARIYF--ASSAETLLDDLSEVRPTVFLAVPRVWE 186
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966209822 317 YLCKQSKREGEKDHK---VRLAIGNGIRS----------DVWReFLDRFGnIKVCELYAATESS-ISFMNY--TGRIGAI 380
Cdd:cd05907 187 KVYAAIKVKAVPGLKrklFDLAVGGRLRFaasggaplpaELLH-FFRALG-IPVYEGYGLTETSaVVTLNPpgDNRIGTV 264
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966209822 381 GRtnlfykllstfdlikydfqkdePMRneqgwCIHVKKGEPGLLIsrVNAKNPFFGYAGPYKHTKDKLLCDvfkkGdvYL 460
Cdd:cd05907 265 GK----------------------PLP-----GVEVRIADDGEIL--VRGPNVMLGYYKNPEATAEALDAD----G--WL 309
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....
gi 966209822 461 NTGDLIVQDQDNFLYFWDRTGDTFRW-KGENVATTEVADVIGMLDFIQEANVYG 513
Cdd:cd05907 310 HTGDLGEIDEDGFLHITGRKKDLIITsGGKNISPEPIENALKASPLISQAVVIG 363
|
|
| MACS_like_3 |
cd05971 |
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the ... |
80-578 |
1.75e-10 |
|
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: 63.22 E-value: 1.75e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966209822 80 YTYQDVDKRSSRVAHVFLNhSSLKKGDTVALLMSNEPDFVHVWFGLAKLGCVVAFLNTNIRSNSLLNCIRACGPRALVvg 159
Cdd:cd05971 7 VTFKELKTASNRFANVLKE-IGLEKGDRVGVFLSQGPECAIAHIAILRSGAIAVPLFALFGPEALEYRLSNSGASALV-- 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966209822 160 ADLlgtveeilpslsenisvwgmkdsvpqgvislkeklstsPDEPVprshhvvsllkstcLYIFTSGTTGLPKAAVISQl 239
Cdd:cd05971 84 TDG--------------------------------------SDDPA--------------LIIYTSGTTGPPKGALHAH- 110
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966209822 240 QVLRGSAVLWAFgctAHDIVYITLPLYHSSAAILGISGCVEL-------GATCVLKK--KFSASQFWSDCKKYDVT-VFq 309
Cdd:cd05971 111 RVLLGHLPGVQF---PFNLFPRDGDLYWTPADWAWIGGLLDVllpslyfGVPVLAHRmtKFDPKAALDLMSRYGVTtAF- 186
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966209822 310 yigeLCRYLCKQSKREGE--KDHKVRL-AIGNGIRSdVWREFL----DRFGnIKVCELYAATESSISFMN----YTGRIG 378
Cdd:cd05971 187 ----LPPTALKMMRQQGEqlKHAQVKLrAIATGGES-LGEELLgwarEQFG-VEVNEFYGQTECNLVIGNcsalFPIKPG 260
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966209822 379 AIGrtnlfyKLLSTFDLIKYDFQKDEPMRNEQGWcIHVKKGEPgllisrvnakNPFFGYAGPYKHTKDKLLCDVFKkgdv 458
Cdd:cd05971 261 SMG------KPIPGHRVAIVDDNGTPLPPGEVGE-IAVELPDP----------VAFLGYWNNPSATEKKMAGDWLL---- 319
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966209822 459 ylnTGDLIVQDQDNFLYFWDRTGDTFRWKGENVATTEVADVIGMLDFIQEANVYGV--AISGYEGRagmASIILKPN--T 534
Cdd:cd05971 320 ---TGDLGRKDSDGYFWYVGRDDDVITSSGYRIGPAEIEECLLKHPAVLMAAVVGIpdPIRGEIVK---AFVVLNPGetP 393
|
490 500 510 520
....*....|....*....|....*....|....*....|....*
gi 966209822 535 SLDLEK-VYEQVVTFLPAYACPRFLRIQEKMEATGTFKLLKHQLV 578
Cdd:cd05971 394 SDALAReIQELVKTRLAAHEYPREIEFVNELPRTATGKIRRRELR 438
|
|
| AA-adenyl-dom |
TIGR01733 |
amino acid adenylation domain; This model represents a domain responsible for the specific ... |
81-374 |
2.03e-10 |
|
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: 63.05 E-value: 2.03e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966209822 81 TYQDVDKRSSRVAHVFLNHSSLKKGDTVALLMSNEPDFVHVWFGLAKLGCV------------VAFLntnirsnsllncI 148
Cdd:TIGR01733 1 TYRELDERANRLARHLRAAGGVGPGDRVAVLLERSAELVVAILAVLKAGAAyvpldpaypaerLAFI------------L 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966209822 149 RACGPRALVVGADLLGTVEEILPSLSENISVWgmkdsvpqgvislkekLSTSPDEPVPRSHHVVSLLKSTCLYIFTSGTT 228
Cdd:TIGR01733 69 EDAGARLLLTDSALASRLAGLVLPVILLDPLE----------------LAALDDAPAPPPPDAPSGPDDLAYVIYTSGST 132
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966209822 229 GLPKAAVISQ-------------LQVLRGSAVLwAFGCTAHDI-VY-ITLPLYHSSAAILGISGcvelgatcVLKKKFSA 293
Cdd:TIGR01733 133 GRPKGVVVTHrslvnllawlarrYGLDPDDRVL-QFASLSFDAsVEeIFGALLAGATLVVPPED--------EERDDAAL 203
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966209822 294 SQFWSDckKYDVTVFQYIGELCRyLCKQSKREGEKDHKVRLAIGNGIRSDVWREFLDRFGNIKVCELYAATESSISFMNY 373
Cdd:TIGR01733 204 LAALIA--EHPVTVLNLTPSLLA-LLAAALPPALASLRLVILGGEALTPALVDRWRARGPGARLINLYGPTETTVWSTAT 280
|
.
gi 966209822 374 T 374
Cdd:TIGR01733 281 L 281
|
|
| Firefly_Luc |
cd17642 |
insect luciferase, similar to plant 4-coumarate: CoA ligases; This family contains insect ... |
80-514 |
2.04e-10 |
|
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: 63.31 E-value: 2.04e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966209822 80 YTYQDVDKRSSRVAHVFLNHSsLKKGDTVALLMSNEPDFVHVWFGLAKLGCVVAFLNTNIRSNSLLNCIRACGPRALVV- 158
Cdd:cd17642 45 YSYAEYLEMSVRLAEALKKYG-LKQNDRIAVCSENSLQFFLPVIAGLFIGVGVAPTNDIYNERELDHSLNISKPTIVFCs 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966209822 159 --GADLLGTVEEILPSLSENISVWGMKDSvpQGVISLkEKLSTSPDEPVPRSHHVVSLL----KSTCLYIFTSGTTGLPK 232
Cdd:cd17642 124 kkGLQKVLNVQKKLKIIKTIIILDSKEDY--KGYQCL-YTFITQNLPPGFNEYDFKPPSfdrdEQVALIMNSSGSTGLPK 200
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966209822 233 AAVISQLQVLR--GSAVLWAFGCT-AHDIVYITLPLYHSSAAILGISGCVELGATCVLKKKFSASQFWSDCKKYDVTVFQ 309
Cdd:cd17642 201 GVQLTHKNIVArfSHARDPIFGNQiIPDTAILTVIPFHHGFGMFTTLGYLICGFRVVLMYKFEEELFLRSLQDYKVQSAL 280
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966209822 310 YIGELCRYLCKQSKREG-EKDHKVRLAIGNG-IRSDVWREFLDRFGNIKVCELYAATESSISFM---NYTGRIGAIGRTN 384
Cdd:cd17642 281 LVPTLFAFFAKSTLVDKyDLSNLHEIASGGApLSKEVGEAVAKRFKLPGIRQGYGLTETTSAILitpEGDDKPGAVGKVV 360
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966209822 385 LFYKLlstfDLIKYDFQKDEPMrNEQG-WCIhvkKGePGLLISRVNakNPffgyagpyKHTK---DKllcdvfkkgDVYL 460
Cdd:cd17642 361 PFFYA----KVVDLDTGKTLGP-NERGeLCV---KG-PMIMKGYVN--NP--------EATKaliDK---------DGWL 412
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....
gi 966209822 461 NTGDLIVQDQDNFLYFWDRTGDTFRWKGENVATTEVADVIGMLDFIQEANVYGV 514
Cdd:cd17642 413 HSGDIAYYDEDGHFFIVDRLKSLIKYKGYQVPPAELESILLQHPKIFDAGVAGI 466
|
|
| PRK09192 |
PRK09192 |
fatty acyl-AMP ligase; |
78-353 |
2.13e-10 |
|
fatty acyl-AMP ligase;
Pssm-ID: 236403 [Multi-domain] Cd Length: 579 Bit Score: 63.49 E-value: 2.13e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966209822 78 DIYTYQDVDKRSSRVAHVFLNHSsLKKGDTVALLMSNEPDFVHVWFGLAKLGCV-------VAFLNTNIRSNSLLNCIRA 150
Cdd:PRK09192 48 EALPYQTLRARAEAGARRLLALG-LKPGDRVALIAETDGDFVEAFFACQYAGLVpvplplpMGFGGRESYIAQLRGMLAS 126
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966209822 151 CGPRALVVGADLLGTVEEILPSLSENISV-WGMKDSVPQGVISLKEklsTSPDEPvprshhvvsllkstCLYIFTSGTTG 229
Cdd:PRK09192 127 AQPAAIITPDELLPWVNEATHGNPLLHVLsHAWFKALPEADVALPR---PTPDDI--------------AYLQYSSGSTR 189
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966209822 230 LPKAAVISQ--------------LQVLRGS-AVLWafgctahdivyitLPLYHSsaaiLGISGCVELGATCVLKKKFSAS 294
Cdd:PRK09192 190 FPRGVIITHralmanlraishdgLKVRPGDrCVSW-------------LPFYHD----MGLVGFLLTPVATQLSVDYLPT 252
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966209822 295 Q-F------WSD-CKKYDVTV-----FQYigELCrylckqSKREGEKDHKV------RLAiGNG---IRSDVWREFLDRF 352
Cdd:PRK09192 253 RdFarrplqWLDlISRNRGTIsysppFGY--ELC------ARRVNSKDLAEldlscwRVA-GIGadmIRPDVLHQFAEAF 323
|
.
gi 966209822 353 G 353
Cdd:PRK09192 324 A 324
|
|
| A_NRPS_VisG_like |
cd17651 |
similar to adenylation domain of virginiamycin S synthetase; This family of the adenylation (A) ... |
60-237 |
2.32e-10 |
|
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: 63.13 E-value: 2.32e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966209822 60 FLSHAKRQPRKPFIIYEGDIYTYQDVDKRSSRVAHvFLNHSSLKKGDTVALLMSNEPDFVHVWFGLAKLGCVVAFLNTNI 139
Cdd:cd17651 1 FERQAARTPDAPALVAEGRRLTYAELDRRANRLAH-RLRARGVGPGDLVALCARRSAELVVALLAILKAGAAYVPLDPAY 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966209822 140 RSNSLLNCIRACGPRALVVGADLLGtveeilpsLSENISVWGMKDSVPQGVislkeklSTSPDEPVPRSHhvvsllKSTC 219
Cdd:cd17651 80 PAERLAFMLADAGPVLVLTHPALAG--------ELAVELVAVTLLDQPGAA-------AGADAEPDPALD------ADDL 138
|
170
....*....|....*....
gi 966209822 220 LY-IFTSGTTGLPKAAVIS 237
Cdd:cd17651 139 AYvIYTSGSTGRPKGVVMP 157
|
|
| PRK07514 |
PRK07514 |
malonyl-CoA synthase; Validated |
68-560 |
3.31e-10 |
|
malonyl-CoA synthase; Validated
Pssm-ID: 181011 [Multi-domain] Cd Length: 504 Bit Score: 62.59 E-value: 3.31e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966209822 68 PRKPFI-IYEGDIYTYQDVDKRSSRVAHVfLNHSSLKKGDTVALLMSNEPDFVHVWFGLAKLGCVVAFLNTNIRSNSLLN 146
Cdd:PRK07514 16 RDAPFIeTPDGLRYTYGDLDAASARLANL-LVALGVKPGDRVAVQVEKSPEALALYLATLRAGAVFLPLNTAYTLAELDY 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966209822 147 CIRACGPRALVVGADLLGTVEEILPSLSEnISVWGMKDsvpQGVISLKEKLSTSPD--EPVPRSHHVVSLLkstcLYifT 224
Cdd:PRK07514 95 FIGDAEPALVVCDPANFAWLSKIAAAAGA-PHVETLDA---DGTGSLLEAAAAAPDdfETVPRGADDLAAI----LY--T 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966209822 225 SGTTGLPKAAVISQLQVLRGSAVL---WAFgcTAHDIVYITLPLYHSSAAILGISGCVELGATCVLKKKFSASQFWSDCK 301
Cdd:PRK07514 165 SGTTGRSKGAMLSHGNLLSNALTLvdyWRF--TPDDVLIHALPIFHTHGLFVATNVALLAGASMIFLPKFDPDAVLALMP 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966209822 302 KydVTVFQ-----YIgelcRYLckQSKREG-EKDHKVRLAI-GNG-IRSDVWREFLDRFGNiKVCELYAATESSISFMN- 372
Cdd:PRK07514 243 R--ATVMMgvptfYT----RLL--QEPRLTrEAAAHMRLFIsGSApLLAETHREFQERTGH-AILERYGMTETNMNTSNp 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966209822 373 YTG-RI-GAIGRTnlfyklLSTFDLIKYDFQKDEPmrneqgwcihVKKGEPGLLisRVNAKNPFFGY-AGPYKhTKDKLL 449
Cdd:PRK07514 314 YDGeRRaGTVGFP------LPGVSLRVTDPETGAE----------LPPGEIGMI--EVKGPNVFKGYwRMPEK-TAEEFR 374
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966209822 450 CDVFKKgdvylnTGDLIVQDQDNFLYFWDRTGDTFRWKGENVATTEVADVIGMLDFIQEANVYGVAISGYeGRAGMASII 529
Cdd:PRK07514 375 ADGFFI------TGDLGKIDERGYVHIVGRGKDLIISGGYNVYPKEVEGEIDELPGVVESAVIGVPHPDF-GEGVTAVVV 447
|
490 500 510
....*....|....*....|....*....|.
gi 966209822 530 LKPNTSLDLEKVYEQVVTFLPAYACPRFLRI 560
Cdd:PRK07514 448 PKPGAALDEAAILAALKGRLARFKQPKRVFF 478
|
|
| ACLS-CaiC |
cd17637 |
acyl-CoA synthetase (AMP-forming)/AMP-acid ligase II; This family contains fatty acid CoA ... |
222-558 |
3.31e-10 |
|
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: 61.90 E-value: 3.31e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966209822 222 IFTSGTTGLPKAAVISQLQVLRGSA-VLWAFGCTAHDIVYITLPLYHSSAAILGISgCVELGATCVLKKKFSASQFWSDC 300
Cdd:cd17637 6 IHTAAVAGRPRGAVLSHGNLIAANLqLIHAMGLTEADVYLNMLPLFHIAGLNLALA-TFHAGGANVVMEKFDPAEALELI 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966209822 301 KKYDVTVFqyiGELCRYLCKQSKREGEKDHKVR-LAIGNGIRS-DVWREFLdRFGNIKVCELYAATESS--ISFMNYTGR 376
Cdd:cd17637 85 EEEKVTLM---GSFPPILSNLLDAAEKSGVDLSsLRHVLGLDApETIQRFE-ETTGATFWSLYGQTETSglVTLSPYRER 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966209822 377 IGAIGRTNLfyklLSTFDLIKydfQKDEPmrneqgwcihVKKGEPGLLIsrVNAKNPFFGYAGpykhtKDKLLCDVFKKG 456
Cdd:cd17637 161 PGSAGRPGP----LVRVRIVD---DNDRP----------VPAGETGEIV--VRGPLVFQGYWN-----LPELTAYTFRNG 216
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966209822 457 dvYLNTGDLIVQDQDNFLYFWDRTGDTFRWK--GENVATTEVADVIGMLDFIQEANVYGVAISGYeGRAGMASIILKPNT 534
Cdd:cd17637 217 --WHHTGDLGRFDEDGYLWYAGRKPEKELIKpgGENVYPAEVEKVILEHPAIAEVCVIGVPDPKW-GEGIKAVCVLKPGA 293
|
330 340
....*....|....*....|....
gi 966209822 535 SLDLEKVYEQVVTFLPAYACPRFL 558
Cdd:cd17637 294 TLTADELIEFVGSRIARYKKPRYV 317
|
|
| PRK09029 |
PRK09029 |
O-succinylbenzoic acid--CoA ligase; Provisional |
64-275 |
3.54e-10 |
|
O-succinylbenzoic acid--CoA ligase; Provisional
Pssm-ID: 236363 [Multi-domain] Cd Length: 458 Bit Score: 62.58 E-value: 3.54e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966209822 64 AKRQPRKPFIIYEGDIYTYQDVDKRSSRVAHvFLNHSSLKKGDTVALLMSNEPDFVHVWFGLAKLGCVVAFLNTNIrsns 143
Cdd:PRK09029 13 AQVRPQAIALRLNDEVLTWQQLCARIDQLAA-GFAQQGVVEGSGVALRGKNSPETLLAYLALLQCGARVLPLNPQL---- 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966209822 144 llnciracgPRALVvgadllgtvEEILPSLSENISVWGMKDSVPQGVISLKEKLSTSPDEPVPRSHHVVSLlkstclyIF 223
Cdd:PRK09029 88 ---------PQPLL---------EELLPSLTLDFALVLEGENTFSALTSLHLQLVEGAHAVAWQPQRLATM-------TL 142
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 966209822 224 TSGTTGLPKAAVISQLQVLrGSA--VLWAFGCTAHDIVYITLPLYHSSAaiLGI 275
Cdd:PRK09029 143 TSGSTGLPKAAVHTAQAHL-ASAegVLSLMPFTAQDSWLLSLPLFHVSG--QGI 193
|
|
| PRK09274 |
PRK09274 |
peptide synthase; Provisional |
81-287 |
7.01e-10 |
|
peptide synthase; Provisional
Pssm-ID: 236443 [Multi-domain] Cd Length: 552 Bit Score: 61.84 E-value: 7.01e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966209822 81 TYQDVDKRSSRVAHVfLNHSSLKKGDTVALLMSNEPDFVHVWFGLAKLGCVVAFLNTNIRSNSLLNCIRACGPRALV--- 157
Cdd:PRK09274 43 SFAELDARSDAIAHG-LNAAGIGRGMRAVLMVTPSLEFFALTFALFKAGAVPVLVDPGMGIKNLKQCLAEAQPDAFIgip 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966209822 158 ---VGADLLGTVEeilPSLSENISV-----WGMKDSVpqgviSLKEKLSTSPDEPVPRSHHvvsllkSTCLYIFTSGTTG 229
Cdd:PRK09274 122 kahLARRLFGWGK---PSVRRLVTVggrllWGGTTLA-----TLLRDGAAAPFPMADLAPD------DMAAILFTSGSTG 187
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 966209822 230 LPKAAVIS------QLQVLRGsavlwAFGCTAHDIVYITLPLYhssaAILGISgcveLGATCVL 287
Cdd:PRK09274 188 TPKGVVYThgmfeaQIEALRE-----DYGIEPGEIDLPTFPLF----ALFGPA----LGMTSVI 238
|
|
| A_NRPS_Srf_like |
cd12117 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including Bacillus subtilis ... |
64-287 |
7.63e-10 |
|
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: 61.45 E-value: 7.63e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966209822 64 AKRQPRKPFIIYEGDIYTYQDVDKRSSRVAHVfLNHSSLKKGDTVALLMSNEPDFVHVWFGLAKLGCVVAFLNTNI---R 140
Cdd:cd12117 7 AARTPDAVAVVYGDRSLTYAELNERANRLARR-LRAAGVGPGDVVGVLAERSPELVVALLAVLKAGAAYVPLDPELpaeR 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966209822 141 SNSLLnciRACGPRALVVGADLLGTVEEILPSlsenisvwgmkdsvpqgVISLKEKLSTSPDEPVPRSHhvvsllKSTCL 220
Cdd:cd12117 86 LAFML---ADAGAKVLLTDRSLAGRAGGLEVA-----------------VVIDEALDAGPAGNPAVPVS------PDDLA 139
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 966209822 221 YI-FTSGTTGLPKAAVISQLQVLRgsavlwafgcTAHDIVYITLP-----LYHSS----AAILGISGCVELGATCVL 287
Cdd:cd12117 140 YVmYTSGSTGRPKGVAVTHRGVVR----------LVKNTNYVTLGpddrvLQTSPlafdASTFEIWGALLNGARLVL 206
|
|
| FadD3 |
cd17638 |
acyl-CoA synthetase FadD3 and similar proteins; This family contains long chain fatty acid CoA ... |
222-574 |
1.35e-09 |
|
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: 59.82 E-value: 1.35e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966209822 222 IFTSGTTGLPKAAVISQLQVLRGSAVlWA--FGCTAHDIVYITLPLYHSSAAILGISGCVELGATCVLKKKFSASQFWSD 299
Cdd:cd17638 6 MFTSGTTGRSKGVMCAHRQTLRAAAA-WAdcADLTEDDRYLIINPFFHTFGYKAGIVACLLTGATVVPVAVFDVDAILEA 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966209822 300 CKKYDVTVFQYIGELCRYLCKQSKREGEKDHKVRLAIGNGirSDVWREFLDR----FGNIKVCELYAATESSISFMNYTG 375
Cdd:cd17638 85 IERERITVLPGPPTLFQSLLDHPGRKKFDLSSLRAAVTGA--ATVPVELVRRmrseLGFETVLTAYGLTEAGVATMCRPG 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966209822 376 rigaigrtNLFYKLLSTFDLIKYDFQkdepmrneqgwcihVKKGEPGLLISRvnAKNPFFGYAGPYKHTKDKLlcdvfkK 455
Cdd:cd17638 163 --------DDAETVATTCGRACPGFE--------------VRIADDGEVLVR--GYNVMQGYLDDPEATAEAI------D 212
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966209822 456 GDVYLNTGDLIVQDQDNFLYFWDRTGDTFRWKGENVATTEVADVIGMLDFIQEANVYGVAiSGYEGRAGMASIILKPNTS 535
Cdd:cd17638 213 ADGWLHTGDVGELDERGYLRITDRLKDMYIVGGFNVYPAEVEGALAEHPGVAQVAVIGVP-DERMGEVGKAFVVARPGVT 291
|
330 340 350
....*....|....*....|....*....|....*....
gi 966209822 536 LDLEKVYEQVVTFLPAYACPRFLRIQEKMEATGTFKLLK 574
Cdd:cd17638 292 LTEEDVIAWCRERLANYKVPRFVRFLDELPRNASGKVMK 330
|
|
| A_NRPS_TubE_like |
cd05906 |
The adenylation domain (A domain) of a family of nonribosomal peptide synthetases (NRPSs) ... |
64-267 |
1.37e-09 |
|
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: 60.76 E-value: 1.37e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966209822 64 AKRQPRKpFIIYEGD-----IYTYQDVDKRSSRVAHvFLNHSSLKKGDTVALLMSNEPDFVhVWFGLAKL-GCVVAFLNT 137
Cdd:cd05906 20 AERGPTK-GITYIDAdgseeFQSYQDLLEDARRLAA-GLRQLGLRPGDSVILQFDDNEDFI-PAFWACVLaGFVPAPLTV 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966209822 138 -------NIRSNSLLNCIRACGPRALVVGADLlgtVEEILPSLSEnisvWGMKDSVpqgVISLKEKLSTSPDEPVP--RS 208
Cdd:cd05906 97 pptydepNARLRKLRHIWQLLGSPVVLTDAEL---VAEFAGLETL----SGLPGIR---VLSIEELLDTAADHDLPqsRP 166
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 966209822 209 HHVVSLLkstclyiFTSGTTGLPKAAVISQLQVL-RGSAVLWAFGCTAHDIVYITLPLYH 267
Cdd:cd05906 167 DDLALLM-------LTSGSTGFPKAVPLTHRNILaRSAGKIQHNGLTPQDVFLNWVPLDH 219
|
|
| FACL_like_4 |
cd05944 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
221-580 |
1.50e-09 |
|
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: 60.19 E-value: 1.50e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966209822 221 YIFTSGTTGLPKAAvisQLQVLRGSAVLWAFGC----TAHDIVYITLPLYHSSAAILGISGCVELGATCVL------KKK 290
Cdd:cd05944 7 YFHTGGTTGTPKLA---QHTHSNEVYNAWMLALnslfDPDDVLLCGLPLFHVNGSVVTLLTPLASGAHVVLagpagyRNP 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966209822 291 FSASQFWSDCKKYDVTVFQYIGELCRYLckqSKREGEKD-HKVRLAIGNG--IRSDVWREFLDRFGnIKVCELYAATE-- 365
Cdd:cd05944 84 GLFDNFWKLVERYRITSLSTVPTVYAAL---LQVPVNADiSSLRFAMSGAapLPVELRARFEDATG-LPVVEGYGLTEat 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966209822 366 --SSISFMNYTGRIGAIGRTnlfykllstfdlIKYDFQKdepMRNEQGWCIHVKKGEPGlLISRVNAKNPffGYAGPYKH 443
Cdd:cd05944 160 clVAVNPPDGPKRPGSVGLR------------LPYARVR---IKVLDGVGRLLRDCAPD-EVGEICVAGP--GVFGGYLY 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966209822 444 TKDKLLCDVfkkGDVYLNTGDLIVQDQDNFLYFWDRTGDTFRWKGENVATTEVADVIgmldfIQEANVYGVAISG----Y 519
Cdd:cd05944 222 TEGNKNAFV---ADGWLNTGDLGRLDADGYLFITGRAKDLIIRGGHNIDPALIEEAL-----LRHPAVAFAGAVGqpdaH 293
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 966209822 520 EGRAGMASIILKPNTSLDLEKVYEQVVTFLPAYAC-PRFLRIQEKMEATGTFKLLKHQLVED 580
Cdd:cd05944 294 AGELPVAYVQLKPGAVVEEEELLAWARDHVPERAAvPKHIEVLEELPVTAVGKVFKPALRAD 355
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
56-577 |
1.76e-09 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 61.13 E-value: 1.76e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966209822 56 VLDKFLSHAKRQPRKPFIIYEGDIYTYQDVDKRSSRVAHVfLNHSSLKKGDTVALLMSNEPDFVHVWFGLAKLGCVVAFL 135
Cdd:PRK12316 2005 VHQRIAEQAARAPEAIAVVFGDQHLSYAELDSRANRLAHR-LRARGVGPEVRVAIAAERSFELVVALLAVLKAGGAYVPL 2083
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966209822 136 NTNIRSNSLLNCIRACGPRALVVGADLLgtveEILPslsenisvwgmkdsVPQGVISLkekLSTSPDE--PVPRSHHVVS 213
Cdd:PRK12316 2084 DPNYPAERLAYMLEDSGAALLLTQRHLL----ERLP--------------LPAGVARL---PLDRDAEwaDYPDTAPAVQ 2142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966209822 214 LLKSTCLY-IFTSGTTGLPKAAVISQLQ-VLRGSAVLWAFGCTAHDIVYITLPL-YHSSAAILGISGCVelGATCVLK-- 288
Cdd:PRK12316 2143 LAGENLAYvIYTSGSTGLPKGVAVSHGAlVAHCQAAGERYELSPADCELQFMSFsFDGAHEQWFHPLLN--GARVLIRdd 2220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966209822 289 KKFSASQFWSDCKKYDVTVFQYIGELCRYLCKQSKREGEKDhKVRLAI--GNGIRSDVWREFLDRFGNIKVCELYAATES 366
Cdd:PRK12316 2221 ELWDPEQLYDEMERHGVTILDFPPVYLQQLAEHAERDGRPP-AVRVYCfgGEAVPAASLRLAWEALRPVYLFNGYGPTEA 2299
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966209822 367 SISFMNYTGR-----------IG-AIGRTNLfYKLLSTFDLIKydfqkdepmrneQGWCIHVKKGEPGLliSRvnaknpf 434
Cdd:PRK12316 2300 VVTPLLWKCRpqdpcgaayvpIGrALGNRRA-YILDADLNLLA------------PGMAGELYLGGEGL--AR------- 2357
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966209822 435 fGYAGPYKHTKDKLLCDVF-KKGDVYLNTGDLIVQDQDNFLYFWDRTGDTFRWKGENVATTEVADVIGMLDFIQEANVyg 513
Cdd:PRK12316 2358 -GYLNRPGLTAERFVPDPFsASGERLYRTGDLARYRADGVVEYLGRIDHQVKIRGFRIELGEIEARLQAHPAVREAVV-- 2434
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 966209822 514 VAISGYEGRAGMASIILKPNTSLDLEKVYEQVVTFLPAYACPRFLRIQEKMEATGTFKLLKHQL 577
Cdd:PRK12316 2435 VAQDGASGKQLVAYVVPDDAAEDLLAELRAWLAARLPAYMVPAHWVVLERLPLNPNGKLDRKAL 2498
|
|
| PRK12492 |
PRK12492 |
long-chain-fatty-acid--CoA ligase; Provisional |
55-577 |
3.12e-09 |
|
long-chain-fatty-acid--CoA ligase; Provisional
Pssm-ID: 171539 [Multi-domain] Cd Length: 562 Bit Score: 59.84 E-value: 3.12e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966209822 55 TVLDKFLSHAKRQPRKPFIIYEGDIYTYQDVDKRSSRVAHVFLNHSSLKKGDTVALLMSNEPDFVHVWFGLAKLGCVVAF 134
Cdd:PRK12492 25 SVVEVFERSCKKFADRPAFSNLGVTLSYAELERHSAAFAAYLQQHTDLVPGDRIAVQMPNVLQYPIAVFGALRAGLIVVN 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966209822 135 LNTNIRSNSLLNCIRACGPRALVVgADLLGT-VEEILPS-----LSE---------------NISVWGMKDSVPQ----G 189
Cdd:PRK12492 105 TNPLYTAREMRHQFKDSGARALVY-LNMFGKlVQEVLPDtgieyLIEakmgdllpaakgwlvNTVVDKVKKMVPAyhlpQ 183
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966209822 190 VISLKEKLSTSPD---EPVPRSHHVVSLLKstclyiFTSGTTGLPKAA-------VISQLQVLrgsAVLWAFGCTAH--- 256
Cdd:PRK12492 184 AVPFKQALRQGRGlslKPVPVGLDDIAVLQ------YTGGTTGLAKGAmlthgnlVANMLQVR---ACLSQLGPDGQplm 254
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966209822 257 ----DIVYITLPLYHSSAAILGISGCVELGATCVL-KKKFSASQFWSDCKKYDVTVFqyIGELCRYLCKQSKREGEKDHK 331
Cdd:PRK12492 255 kegqEVMIAPLPLYHIYAFTANCMCMMVSGNHNVLiTNPRDIPGFIKELGKWRFSAL--LGLNTLFVALMDHPGFKDLDF 332
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966209822 332 VRLAIGNGIRSDVWREFLDRFGNIKVC---ELYAATESS-ISFMNYTG---RIGAIGrtnlFYKLLSTFDLIkyDFQKDE 404
Cdd:PRK12492 333 SALKLTNSGGTALVKATAERWEQLTGCtivEGYGLTETSpVASTNPYGelaRLGTVG----IPVPGTALKVI--DDDGNE 406
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966209822 405 PMRNEQG-WCIhvkKGePGLLIsrvnaknpffGYAGPYKHTKDKLlcdvfkKGDVYLNTGDLIVQDQDNFLYFWDRTGDT 483
Cdd:PRK12492 407 LPLGERGeLCI---KG-PQVMK----------GYWQQPEATAEAL------DAEGWFKTGDIAVIDPDGFVRIVDRKKDL 466
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966209822 484 FRWKGENVATTEVADVIGMLDFIQEANVYGVAisgyEGRAGMAS--IILKPNTSLDLEKVYEQVVTFLPAYACPRFLRIQ 561
Cdd:PRK12492 467 IIVSGFNVYPNEIEDVVMAHPKVANCAAIGVP----DERSGEAVklFVVARDPGLSVEELKAYCKENFTGYKVPKHIVLR 542
|
570
....*....|....*.
gi 966209822 562 EKMEATGTFKLLKHQL 577
Cdd:PRK12492 543 DSLPMTPVGKILRREL 558
|
|
| PRK04813 |
PRK04813 |
D-alanine--poly(phosphoribitol) ligase subunit DltA; |
56-238 |
3.51e-09 |
|
D-alanine--poly(phosphoribitol) ligase subunit DltA;
Pssm-ID: 235313 [Multi-domain] Cd Length: 503 Bit Score: 59.52 E-value: 3.51e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966209822 56 VLDKFLSHAKRQPRKPFIIYEGDIYTYQDVDKRSSRVAHvFLNHSSLKKGDTVALLMSNEPDFVHVWFGLAKLGCVVAFL 135
Cdd:PRK04813 4 IIETIEEFAQTQPDFPAYDYLGEKLTYGQLKEDSDALAA-FIDSLKLPDKSPIIVFGHMSPEMLATFLGAVKAGHAYIPV 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966209822 136 NTNIRSNSLLNCIRACGPRALVVGADLLGTVEEIlPSLSENIsvwgmkdsvpqgvisLKEklSTSPDEPVPRSHHVvsll 215
Cdd:PRK04813 83 DVSSPAERIEMIIEVAKPSLIIATEELPLEILGI-PVITLDE---------------LKD--IFATGNPYDFDHAV---- 140
|
170 180
....*....|....*....|....*
gi 966209822 216 KSTCLY--IFTSGTTGLPKAAVISQ 238
Cdd:PRK04813 141 KGDDNYyiIFTSGTTGKPKGVQISH 165
|
|
| ttLC_FACS_like |
cd05915 |
Fatty acyl-CoA synthetases similar to LC-FACS from Thermus thermophiles; This family includes ... |
77-270 |
4.57e-09 |
|
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: 58.98 E-value: 4.57e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966209822 77 GDI-YTYQDVDKRSSRVAHVfLNHSSLKKGDTVALLMSNEPDFVHVWFGLAKLGCVVAFLNTNIRSNSLLNCIRACGPRA 155
Cdd:cd05915 21 EVHrTTYAEVYQRARRLMGG-LRALGVGVGDRVATLGFNHFRHLEAYFAVPGMGAVLHTANPRLSPKEIAYILNHAEDKV 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966209822 156 LVVGADLLGTVEEILpSLSENISVWGMKDSVPQgviSLKEKLST-----SPDEPVPRSHHVVsllkstclYIFTSGTTGL 230
Cdd:cd05915 100 LLFDPNLLPLVEAIR-GELKTVQHFVVMDEKAP---EGYLAYEEalgeeADPVRVPERAACG--------MAYTTGTTGL 167
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 966209822 231 PKAAVISQlqvlRGS-------AVLWAFGCTAHDIVYITLPLYHSSA 270
Cdd:cd05915 168 PKGVVYSH----RALvlhslaaSLVDGTALSEKDVVLPVVPMFHVNA 210
|
|
| PRK07787 |
PRK07787 |
acyl-CoA synthetase; Validated |
184-292 |
8.37e-09 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236096 [Multi-domain] Cd Length: 471 Bit Score: 58.08 E-value: 8.37e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966209822 184 DSVPQGVislkekLSTSPDEPVPRSHHVVSLL------------KSTCLYIFTSGTTGLPKAAVISQLQV---LRGSAVL 248
Cdd:PRK07787 90 DSGAQAW------LGPAPDDPAGLPHVPVRLHarswhrypepdpDAPALIVYTSGTTGPPKGVVLSRRAIaadLDALAEA 163
|
90 100 110 120
....*....|....*....|....*....|....*....|....
gi 966209822 249 WAFgcTAHDIVYITLPLYHSSAAILGISGCVELGATCVLKKKFS 292
Cdd:PRK07787 164 WQW--TADDVLVHGLPLFHVHGLVLGVLGPLRIGNRFVHTGRPT 205
|
|
| PRK07008 |
PRK07008 |
long-chain-fatty-acid--CoA ligase; Validated |
76-270 |
1.35e-08 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 235908 [Multi-domain] Cd Length: 539 Bit Score: 57.79 E-value: 1.35e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966209822 76 EGDI--YTYQDVDKRSSRVAHVfLNHSSLKKGDTVALLMSNEPDFVHVWFGLAKLGCVVAFLNTNIRSNSLLNCIRACGP 153
Cdd:PRK07008 34 EGDIhrYTYRDCERRAKQLAQA-LAALGVEPGDRVGTLAWNGYRHLEAYYGVSGSGAVCHTINPRLFPEQIAYIVNHAED 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966209822 154 RALVVGADLLGTVEEILPSLsENISVWGM---KDSVPQGVISLK--EKL--STSPDEPVPR-SHHVVSllkSTClyiFTS 225
Cdd:PRK07008 113 RYVLFDLTFLPLVDALAPQC-PNVKGWVAmtdAAHLPAGSTPLLcyETLvgAQDGDYDWPRfDENQAS---SLC---YTS 185
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 966209822 226 GTTGLPKAAVISQLQ-VLR--GSAVLWAFGCTAHDIVYITLPLYHSSA 270
Cdd:PRK07008 186 GTTGNPKGALYSHRStVLHayGAALPDAMGLSARDAVLPVVPMFHVNA 233
|
|
| A_NRPS |
cd05930 |
The adenylation domain of nonribosomal peptide synthetases (NRPS); The adenylation (A) domain ... |
68-564 |
2.91e-08 |
|
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: 56.38 E-value: 2.91e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966209822 68 PRKPFIIYEGDIYTYQDVDKRSSRVAHvFLNHSSLKKGDTVALLMSNEPDFVHVWFGLAKLGCvvAF--LNTNI---RSN 142
Cdd:cd05930 1 PDAVAVVDGDQSLTYAELDARANRLAR-YLRERGVGPGDLVAVLLERSLEMVVAILAVLKAGA--AYvpLDPSYpaeRLA 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966209822 143 SLLnciRACGPRALVVGADLLGTVeeilpslsenisvwgmkdsvpqgvislkeklstspdepvprshhvvsllkstclyI 222
Cdd:cd05930 78 YIL---EDSGAKLVLTDPDDLAYV-------------------------------------------------------I 99
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966209822 223 FTSGTTGLPKAAVISQLQVLRGSAVLW-AFGCTAHDIVyitlpLYHSS----AAILGISGCVELGATCVL---KKKFSAS 294
Cdd:cd05930 100 YTSGSTGKPKGVMVEHRGLVNLLLWMQeAYPLTPGDRV-----LQFTSfsfdVSVWEIFGALLAGATLVVlpeEVRKDPE 174
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966209822 295 QFWSDCKKYDVTVFQ----YIGELCRYLckqskrEGEKDHKVRLAI--GNGIRSDVWREFLDRFGNIKVCELYAATESSI 368
Cdd:cd05930 175 ALADLLAEEGITVLHltpsLLRLLLQEL------ELAALPSLRLVLvgGEALPPDLVRRWRELLPGARLVNLYGPTEATV 248
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966209822 369 SfmnytgrigaigrtnlfykllSTFDLIKYDFQKDE------PMRN-------EQGWCihVKKGEPG-LLISRVN-AKnp 433
Cdd:cd05930 249 D---------------------ATYYRVPPDDEEDGrvpigrPIPNtrvyvldENLRP--VPPGVPGeLYIGGAGlAR-- 303
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966209822 434 ffGYAGPYKHTKDKLLCDVFKKGDVYLNTGDLIVQDQDNFLYFWDRTgDT------FRwkgenVATTEVADVIGMLDFIQ 507
Cdd:cd05930 304 --GYLNRPELTAERFVPNPFGPGERMYRTGDLVRWLPDGNLEFLGRI-DDqvkirgYR-----IELGEIEAALLAHPGVR 375
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 966209822 508 EAnvygvAISGYEGRAG----MASIILKPNTSLDLEKVYEQVVTFLPAYACPRFLRIQEKM 564
Cdd:cd05930 376 EA-----AVVAREDGDGekrlVAYVVPDEGGELDEEELRAHLAERLPDYMVPSAFVVLDAL 431
|
|
| 23DHB-AMP_lg |
cd05920 |
2,3-dihydroxybenzoate-AMP ligase; 2,3-dihydroxybenzoate-AMP ligase activates 2, ... |
47-284 |
3.52e-08 |
|
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: 56.18 E-value: 3.52e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966209822 47 YEKRG--ELVTVLDKFLSHAKRQPRKPFIIYEGDIYTYQDVDKRSSRVAhVFLNHSSLKKGDTVALLMSNEPDFVHVWFG 124
Cdd:cd05920 6 YRAAGywQDEPLGDLLARSAARHPDRIAVVDGDRRLTYRELDRRADRLA-AGLRGLGIRPGDRVVVQLPNVAEFVVLFFA 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966209822 125 LAKLGCVVAFLNTNIRSNSLLNCIRACGPRALVVgADllgtveeilpslsenisVWGMKDSVPQGvislKEKLSTSPDep 204
Cdd:cd05920 85 LLRLGAVPVLALPSHRRSELSAFCAHAEAVAYIV-PD-----------------RHAGFDHRALA----RELAESIPE-- 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966209822 205 vprshhvvsllksTCLYIFTSGTTGLPKAavISQ-----LQVLRGSAVLWAFGctaHDIVYIT-LPLYH----SSAAILG 274
Cdd:cd05920 141 -------------VALFLLSGGTTGTPKL--IPRthndyAYNVRASAEVCGLD---QDTVYLAvLPAAHnfplACPGVLG 202
|
250
....*....|...
gi 966209822 275 I---SGCVELGAT 284
Cdd:cd05920 203 TllaGGRVVLAPD 215
|
|
| PLN02479 |
PLN02479 |
acetate-CoA ligase |
67-577 |
4.52e-08 |
|
acetate-CoA ligase
Pssm-ID: 178097 [Multi-domain] Cd Length: 567 Bit Score: 56.01 E-value: 4.52e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966209822 67 QPRKPFIIYEGDIYTYQDVDKRSSRVAHVFLNHSsLKKGDTVALLMSNEPDFVHVWFGLAKLGCVVaflNT-NIRSNS-- 143
Cdd:PLN02479 33 HPTRKSVVHGSVRYTWAQTYQRCRRLASALAKRS-IGPGSTVAVIAPNIPAMYEAHFGVPMAGAVV---NCvNIRLNApt 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966209822 144 ---LLNCIRAcgpRALVVGADLLGTVEEILPSLSEN---------ISVWG--------MKDSVPQGVISLKEKLSTSPDE 203
Cdd:PLN02479 109 iafLLEHSKS---EVVMVDQEFFTLAEEALKILAEKkkssfkpplLIVIGdptcdpksLQYALGKGAIEYEKFLETGDPE 185
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966209822 204 PV---PRSHhvvslLKSTCLYiFTSGTTGLPKAAVISQlqvlRGS-------AVLWAFGCTAhdiVYI-TLPLYH----- 267
Cdd:PLN02479 186 FAwkpPADE-----WQSIALG-YTSGTTASPKGVVLHH----RGAylmalsnALIWGMNEGA---VYLwTLPMFHcngwc 252
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966209822 268 ---SSAAILGISGCVelgatcvlkKKFSASQFWSDCKKYDVTVFQYIGELCRYLCKQSKRE--------------GEKDH 330
Cdd:PLN02479 253 ftwTLAALCGTNICL---------RQVTAKAIYSAIANYGVTHFCAAPVVLNTIVNAPKSEtilplprvvhvmtaGAAPP 323
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966209822 331 KVRLAIGN--GIRSDVWREFLDRFGNIKVC-------ELYAATESsisfmnytgRIGAigRTNLFYKLLSTFDLIkyDFQ 401
Cdd:PLN02479 324 PSVLFAMSekGFRVTHTYGLSETYGPSTVCawkpewdSLPPEEQA---------RLNA--RQGVRYIGLEGLDVV--DTK 390
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966209822 402 KDEPMRNEqGWCIhvkkgepGLLISRVNA------KNPffgyagpykhtkdKLLCDVFKKGdvYLNTGDLIVQDQDNFLY 475
Cdd:PLN02479 391 TMKPVPAD-GKTM-------GEIVMRGNMvmkgylKNP-------------KANEEAFANG--WFHSGDLGVKHPDGYIE 447
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966209822 476 FWDRTGDTFRWKGENVATTEVADVIGMLDFIQEANVYGVAISGYeGRAGMASIILKPNT-SLDLEKVYEQVVTF----LP 550
Cdd:PLN02479 448 IKDRSKDIIISGGENISSLEVENVVYTHPAVLEASVVARPDERW-GESPCAFVTLKPGVdKSDEAALAEDIMKFcrerLP 526
|
570 580
....*....|....*....|....*..
gi 966209822 551 AYACPRFLrIQEKMEATGTFKLLKHQL 577
Cdd:PLN02479 527 AYWVPKSV-VFGPLPKTATGKIQKHVL 552
|
|
| PLN02330 |
PLN02330 |
4-coumarate--CoA ligase-like 1 |
77-579 |
1.17e-07 |
|
4-coumarate--CoA ligase-like 1
Pssm-ID: 215189 [Multi-domain] Cd Length: 546 Bit Score: 54.60 E-value: 1.17e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966209822 77 GDIYTYQDVDKRSSRVAHVfLNHSSLKKGDTVALLMSNEPDFVHVWFGLAKLGCVVAFLNTNIRSNSLLNCIRACGPRAL 156
Cdd:PLN02330 53 GKAVTYGEVVRDTRRFAKA-LRSLGLRKGQVVVVVLPNVAEYGIVALGIMAAGGVFSGANPTALESEIKKQAEAAGAKLI 131
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966209822 157 VVGADLLGTVEeilpSLSENISVWGmkDSVPQGVISLKEKLSTSpDEPVPRSHHVVSLLKSTCLYIFTSGTTGLPKAAVI 236
Cdd:PLN02330 132 VTNDTNYGKVK----GLGLPVIVLG--EEKIEGAVNWKELLEAA-DRAGDTSDNEEILQTDLCALPFSSGTTGISKGVML 204
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966209822 237 SQlQVLRGSAVLWAFGCTAHDIVYIT----LPLYHssaaILGISG--CVEL--GATCVLKKKFSASQFWSDCKKYDVTVF 308
Cdd:PLN02330 205 TH-RNLVANLCSSLFSVGPEMIGQVVtlglIPFFH----IYGITGicCATLrnKGKVVVMSRFELRTFLNALITQEVSFA 279
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966209822 309 QYIGELCRYLCKQSKREGEKDHKVRL-AIGNG---IRSDVWREFLDRFGNIKVCELYAATE-SSISFMNYTGRIG-AIGR 382
Cdd:PLN02330 280 PIVPPIILNLVKNPIVEEFDLSKLKLqAIMTAaapLAPELLTAFEAKFPGVQVQEAYGLTEhSCITLTHGDPEKGhGIAK 359
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966209822 383 TNLFYKLLSTFDlIKYdfqkdepMRNEQGwcIHVKKGEPGLLISRvnAKNPFFGYAGPYKHTKDKLlcdvfkKGDVYLNT 462
Cdd:PLN02330 360 KNSVGFILPNLE-VKF-------IDPDTG--RSLPKNTPGELCVR--SQCVMQGYYNNKEETDRTI------DEDGWLHT 421
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966209822 463 GDLIVQDQDNFLYFWDRTGDTFRWKGENVATTEVADVIGMLDFIQEANVygVAISGYE-GRAGMASIILKPNTSLDLEKV 541
Cdd:PLN02330 422 GDIGYIDDDGDIFIVDRIKELIKYKGFQVAPAELEAILLTHPSVEDAAV--VPLPDEEaGEIPAACVVINPKAKESEEDI 499
|
490 500 510
....*....|....*....|....*....|....*...
gi 966209822 542 YEQVVTFLPAYACPRFLRIQEKMEATGTFKLLKHQLVE 579
Cdd:PLN02330 500 LNFVAANVAHYKKVRVVQFVDSIPKSLSGKIMRRLLKE 537
|
|
| PRK08162 |
PRK08162 |
acyl-CoA synthetase; Validated |
68-306 |
1.38e-07 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236169 [Multi-domain] Cd Length: 545 Bit Score: 54.57 E-value: 1.38e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966209822 68 PRKPFIIYEGDIYTYQDVDKRSSRVAHvFLNHSSLKKGDTVALLMSNEPDFVHVWFGLAKLGCVVAFLNTNIRSNSLLNC 147
Cdd:PRK08162 32 PDRPAVIHGDRRRTWAETYARCRRLAS-ALARRGIGRGDTVAVLLPNIPAMVEAHFGVPMAGAVLNTLNTRLDAASIAFM 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966209822 148 IRACGPRALVVGADLLGTVEEILPSLSE-NISVWGMKDSVPQGVISLKEK------LSTSPD---EPVPRSHHVVSLlks 217
Cdd:PRK08162 111 LRHGEAKVLIVDTEFAEVAREALALLPGpKPLVIDVDDPEYPGGRFIGALdyeaflASGDPDfawTLPADEWDAIAL--- 187
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966209822 218 tclyIFTSGTTGLPKAAVISQlqvlRGSAVL-------WAFGctaHDIVYI-TLPLYH--------SSAAILGISGCVel 281
Cdd:PRK08162 188 ----NYTSGTTGNPKGVVYHH----RGAYLNalsnilaWGMP---KHPVYLwTLPMFHcngwcfpwTVAARAGTNVCL-- 254
|
250 260
....*....|....*....|....*
gi 966209822 282 gatcvlkKKFSASQFWSDCKKYDVT 306
Cdd:PRK08162 255 -------RKVDPKLIFDLIREHGVT 272
|
|
| PRK05691 |
PRK05691 |
peptide synthase; Validated |
76-287 |
1.43e-07 |
|
peptide synthase; Validated
Pssm-ID: 235564 [Multi-domain] Cd Length: 4334 Bit Score: 55.17 E-value: 1.43e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966209822 76 EGDIYTYQDVDKRSSRVAHVFLNHSSLkkGDTVALLMSNEPDFVHVWFG--LAKLGCVVAFLNTNIRSN---SLLNCIRA 150
Cdd:PRK05691 37 EGVVLSYRDLDLRARTIAAALQARASF--GDRAVLLFPSGPDYVAAFFGclYAGVIAVPAYPPESARRHhqeRLLSIIAD 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966209822 151 CGPRALVVGADLLGTVEEILPSLSenisvwgmkDSVPQ--GVISLKEKLSTSPDEPVPRSHHVVSLLkstclyiFTSGTT 228
Cdd:PRK05691 115 AEPRLLLTVADLRDSLLQMEELAA---------ANAPEllCVDTLDPALAEAWQEPALQPDDIAFLQ-------YTSGST 178
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 966209822 229 GLPKAavisqLQVLRGSAVL--W----AFGCTAH--DIVYITLPLYHSSAAILGISGCVELGATCVL 287
Cdd:PRK05691 179 ALPKG-----VQVSHGNLVAneQlirhGFGIDLNpdDVIVSWLPLYHDMGLIGGLLQPIFSGVPCVL 240
|
|
| OSB_MenE-like |
cd17630 |
O-succinylbenzoic acid-CoA ligase; This family contains O-succinylbenzoyl-CoA (OSB-CoA) ... |
219-562 |
1.70e-07 |
|
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: 53.49 E-value: 1.70e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966209822 219 CLYIFTSGTTGLPKAAVISQLQVL-RGSAVLWAFGCTAHDIVYITLPLYHssaailgISG------CVELGATCVLKKKF 291
Cdd:cd17630 3 ATVILTSGSTGTPKAVVHTAANLLaSAAGLHSRLGFGGGDSWLLSLPLYH-------VGGlailvrSLLAGAELVLLERN 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966209822 292 SASQfwSDCKKYDVTVFQYI-GELCRYLckQSKREGEKDHKVRLAIGNGirSDVWREFLDRFGN--IKVCELYAATE--S 366
Cdd:cd17630 76 QALA--EDLAPPGVTHVSLVpTQLQRLL--DSGQGPAALKSLRAVLLGG--APIPPELLERAADrgIPLYTTYGMTEtaS 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966209822 367 SIsfmnYTGRIGAIGRTNLfYKLLstfDLIKYDFQKDEpmrneqgwCIHVKKgePGLlisrvnaknpFFGYAGPYKHTkd 446
Cdd:cd17630 150 QV----ATKRPDGFGRGGV-GVLL---PGRELRIVEDG--------EIWVGG--ASL----------AMGYLRGQLVP-- 199
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966209822 447 kllcDVFKKGDVYlnTGDLIVQDQDNFLYFWDRTGDTFRWKGENVATTEVADVIGMLDFIQEANVYGVAisgyEGRAGMA 526
Cdd:cd17630 200 ----EFNEDGWFT--TKDLGELHADGRLTVLGRADNMIISGGENIQPEEIEAALAAHPAVRDAFVVGVP----DEELGQR 269
|
330 340 350
....*....|....*....|....*....|....*...
gi 966209822 527 SI-ILKPNTSLDLEKVYEQVVTFLPAYACP-RFLRIQE 562
Cdd:cd17630 270 PVaVIVGRGPADPAELRAWLKDKLARFKLPkRIYPVPE 307
|
|
| PrpE |
cd05967 |
Propionyl-CoA synthetase (PrpE); EC 6.2.1.17: propanoate:CoA ligase (AMP-forming) or ... |
62-235 |
3.78e-06 |
|
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: 50.01 E-value: 3.78e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966209822 62 SHAKR-QPRKPFIIYEG------DIYTYQDVDKRSSRVAHVFLNHSsLKKGDTVALLMSNEPDFVHVWFGLAKLGCVVAF 134
Cdd:cd05967 58 RHVEAgRGDQIALIYDSpvtgteRTYTYAELLDEVSRLAGVLRKLG-VVKGDRVIIYMPMIPEAAIAMLACARIGAIHSV 136
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966209822 135 LNTNIRSNSLLNCIRACGPrALVVGADL---LGTVEEILPSLSENISVWGMKdsvPQGVIsLKEKLSTSPDEPVP----- 206
Cdd:cd05967 137 VFGGFAAKELASRIDDAKP-KLIVTASCgiePGKVVPYKPLLDKALELSGHK---PHHVL-VLNRPQVPADLTKPgrdld 211
|
170 180 190
....*....|....*....|....*....|....*...
gi 966209822 207 --------RSHHVVSLLKSTCLYI-FTSGTTGLPKAAV 235
Cdd:cd05967 212 wsellakaEPVDCVPVAATDPLYIlYTSGTTGKPKGVV 249
|
|
| Dip2 |
cd05905 |
Disco-interacting protein 2 (Dip2); Dip2 proteins show sequence similarity to other members of ... |
76-132 |
9.37e-06 |
|
Disco-interacting protein 2 (Dip2); Dip2 proteins show sequence similarity to other members of the adenylate forming enzyme family, including insect luciferase, acetyl CoA ligases and the adenylation domain of nonribosomal peptide synthetases (NRPS). However, its function may have diverged from other members of the superfamily. In mouse embryo, Dip2 homolog A plays an important role in the development of both vertebrate and invertebrate nervous systems. Dip2A appears to regulate cell growth and the arrangement of cells in organs. Biochemically, Dip2A functions as a receptor of FSTL1, an extracellular glycoprotein, and may play a role as a cardiovascular protective agent.
Pssm-ID: 341231 [Multi-domain] Cd Length: 571 Bit Score: 48.50 E-value: 9.37e-06
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*..
gi 966209822 76 EGDIYTYQDVDKRSSRVAHVFLNHSSLKKGDTVALLMSNEPDFVHVWFGLAKLGCVV 132
Cdd:cd05905 11 EATTLTWGKLLSRAEKIAAVLQKKVGLKPGDRVALMYPDPLDFVAAFYGCLYAGVVP 67
|
|
| PRK06814 |
PRK06814 |
acyl-[ACP]--phospholipid O-acyltransferase; |
105-268 |
2.44e-05 |
|
acyl-[ACP]--phospholipid O-acyltransferase;
Pssm-ID: 235865 [Multi-domain] Cd Length: 1140 Bit Score: 47.65 E-value: 2.44e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966209822 105 GDTVALLMSNEPDFVHVWFGLAKLGCVVAFLNTNIRSNSLLNCIRACG------PRALVVGADLLGTVEEI--------L 170
Cdd:PRK06814 682 GENVGVMLPNANGAAVTFFALQSAGRVPAMINFSAGIANILSACKAAQvktvltSRAFIEKARLGPLIEALefgiriiyL 761
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966209822 171 PSLSENISVWGMKDSVPQGVISLKEKLSTSPDEPVprshhVVsllkstclyIFTSGTTGLPKAAVISQLQVLRGSAVLWA 250
Cdd:PRK06814 762 EDVRAQIGLADKIKGLLAGRFPLVYFCNRDPDDPA-----VI---------LFTSGSEGTPKGVVLSHRNLLANRAQVAA 827
|
170
....*....|....*....
gi 966209822 251 -FGCTAHDIVYITLPLYHS 268
Cdd:PRK06814 828 rIDFSPEDKVFNALPVFHS 846
|
|
| FACL_like_5 |
cd05924 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
220-556 |
2.72e-05 |
|
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: 46.61 E-value: 2.72e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966209822 220 LYI-FTSGTTGLPKAAVISQLQVLRGSavlwaFGCTAHD--------------------IVYITLPLYHSSAAILGISGC 278
Cdd:cd05924 6 LYIlYTGGTTGMPKGVMWRQEDIFRML-----MGGADFGtgeftpsedahkaaaaaagtVMFPAPPLMHGTGSWTAFGGL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966209822 279 VELGATCVLKKKFSASQFWSDCKKYDVTVFQYIGE-LCRYLCKQSKREGEKDHKVRLAIGNG---IRSDVWREFLDRFGN 354
Cdd:cd05924 81 LGGQTVVLPDDRFDPEEVWRTIEKHKVTSMTIVGDaMARPLIDALRDAGPYDLSSLFAISSGgalLSPEVKQGLLELVPN 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966209822 355 IKVCELYAATESsiSFMNYTGRIGAIGRTNLFYKLLSTFDLIKYDFQKDEPMRNEQGWCihVKKGEPGLlisrvnaknpf 434
Cdd:cd05924 161 ITLVDAFGSSET--GFTGSGHSAGSGPETGPFTRANPDTVVLDDDGRVVPPGSGGVGWI--ARRGHIPL----------- 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966209822 435 fGYAGPYKHTKDKLlcdvFKKGDV-YLNTGDLIVQDQDNFLYFWDRTGDTFRWKGENVATTEVADVIGmldfiQEANVYG 513
Cdd:cd05924 226 -GYYGDEAKTAETF----PEVDGVrYAVPGDRATVEADGTVTLLGRGSVCINTGGEKVFPEEVEEALK-----SHPAVYD 295
|
330 340 350 360
....*....|....*....|....*....|....*....|....*..
gi 966209822 514 VAISGYE----GRAGMASIILKPNTSLDLEKVYEQVVTFLPAYACPR 556
Cdd:cd05924 296 VLVVGRPderwGQEVVAVVQLREGAGVDLEELREHCRTRIARYKLPK 342
|
|
| PLN02736 |
PLN02736 |
long-chain acyl-CoA synthetase |
125-267 |
3.46e-05 |
|
long-chain acyl-CoA synthetase
Pssm-ID: 178337 [Multi-domain] Cd Length: 651 Bit Score: 47.02 E-value: 3.46e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966209822 125 LAKLGCVVAFLNTnirsnsLLNCIRAC-GPRALVVgadlLGTVEEILPSLSENISVwgmkdsvpqGVISLKEKLS---TS 200
Cdd:PLN02736 151 VAAIFCVPQTLNT------LLSCLSEIpSVRLIVV----VGGADEPLPSLPSGTGV---------EIVTYSKLLAqgrSS 211
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 966209822 201 PDEPVPRSHHVVSLLkstClyiFTSGTTGLPKAAVISQLQVLR---GSAVLWAFGCTAhdiVYIT-LPLYH 267
Cdd:PLN02736 212 PQPFRPPKPEDVATI---C---YTSGTTGTPKGVVLTHGNLIAnvaGSSLSTKFYPSD---VHISyLPLAH 273
|
|
| A_NRPS_Cytc1-like |
cd17643 |
similar to adenylation domain of cytotrienin synthetase CytC1; This family of the adenylation ... |
68-368 |
5.88e-05 |
|
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: 45.76 E-value: 5.88e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966209822 68 PRKPFIIYEGDIYTYQDVDKRSSRVAHVfLNHSSLKKGDTVALLMSNEPDFVhvwfglaklgcvVAFLNtnirsnsllnc 147
Cdd:cd17643 1 PEAVAVVDEDRRLTYGELDARANRLART-LRAEGVGPGDRVALALPRSAELI------------VALLA----------- 56
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966209822 148 IRACGprALVVGADLLGTVEEILPSLsenisvwgmKDSVPQGVIslkeklsTSPDEPVprshhvvsllkstclY-IFTSG 226
Cdd:cd17643 57 ILKAG--GAYVPIDPAYPVERIAFIL---------ADSGPSLLL-------TDPDDLA---------------YvIYTSG 103
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966209822 227 TTGLPKAAVISQLQVLR-GSAVLWAFGCTAHDIVYitlpLYHSSA---AILGISGCVELGATCVLKKKF---SASQFWSD 299
Cdd:cd17643 104 STGRPKGVVVSHANVLAlFAATQRWFGFNEDDVWT----LFHSYAfdfSVWEIWGALLHGGRLVVVPYEvarSPEDFARL 179
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 966209822 300 CKKYDVTVFQYIGELCRYLCKQSKREGEKDHKVRLAI--GNGIRSDVWREFLDRFGNIK--VCELYAATESSI 368
Cdd:cd17643 180 LRDEGVTVLNQTPSAFYQLVEAADRDGRDPLALRYVIfgGEALEAAMLRPWAGRFGLDRpqLVNMYGITETTV 252
|
|
| FACL_like_1 |
cd05910 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
81-285 |
5.97e-05 |
|
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: 45.91 E-value: 5.97e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966209822 81 TYQDVDKRSSRVAHVfLNHSSLKKGDTVALLMSNEPDFVHVWFGLAKLGCVVAFLNTNIRSNSLLNCIracgpralvvga 160
Cdd:cd05910 4 SFRELDERSDRIAQG-LTAYGIRRGMRAVLMVPPGPDFFALTFALFKAGAVPVLIDPGMGRKNLKQCL------------ 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966209822 161 dllgtveeilpslsenisvwgmKDSVPQGVISlkeklstspdepVPRSHHVVSLLkstclyiFTSGTTGLPKAAVIS--- 237
Cdd:cd05910 71 ----------------------QEAEPDAFIG------------IPKADEPAAIL-------FTSGSTGTPKGVVYRhgt 109
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 966209822 238 ---QLQVLRGSavlwaFGCTAHDIVYITLPLYHSSAAILGISGCV-ELGATC 285
Cdd:cd05910 110 faaQIDALRQL-----YGIRPGEVDLATFPLFALFGPALGLTSVIpDMDPTR 156
|
|
| PRK05620 |
PRK05620 |
long-chain fatty-acid--CoA ligase; |
81-283 |
7.06e-05 |
|
long-chain fatty-acid--CoA ligase;
Pssm-ID: 180167 [Multi-domain] Cd Length: 576 Bit Score: 45.93 E-value: 7.06e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966209822 81 TYQDVDKRSSRVAHVFLNHSSLKKGDTVALLMSNEPDFVHVWFGLAKLGCVVAFLNTNIRSNSLLNCIRACGPRALVVGA 160
Cdd:PRK05620 40 TFAAIGARAAALAHALHDELGITGDQRVGSMMYNCAEHLEVLFAVACMGAVFNPLNKQLMNDQIVHIINHAEDEVIVADP 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966209822 161 DLLGTVEEILPSLS--ENISVWGMKDS------VPQGVI-----SLKEKLSTSPDEPVPRSHHVVSLLKSTclyiftsGT 227
Cdd:PRK05620 120 RLAEQLGEILKECPcvRAVVFIGPSDAdsaaahMPEGIKvysyeALLDGRSTVYDWPELDETTAAAICYST-------GT 192
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 966209822 228 TGLPKAAVIS------QLQVLRGSAVLwafgCTAHDIVYIT-LPLYHSsaailgISGCVELGA 283
Cdd:PRK05620 193 TGAPKGVVYShrslylQSLSLRTTDSL----AVTHGESFLCcVPIYHV------LSWGVPLAA 245
|
|
| A_NRPS_GliP_like |
cd17653 |
nonribosomal peptide synthase GliP-like; This family includes the adenylation (A) domain of ... |
58-243 |
3.01e-04 |
|
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: 43.45 E-value: 3.01e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966209822 58 DKFLSHAKRQPRKPFIIYEGDIYTYQDVDKRSSRVAHvFLNHSSLKKGDTVALLMSNEPDFVHVWFGLAKLGCVVAFLNT 137
Cdd:cd17653 1 DAFERIAAAHPDAVAVESLGGSLTYGELDAASNALAN-RLLQLGVVPGDVVPLLSDRSLEMLVAILAILKAGAAYVPLDA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966209822 138 NIRSNSLLNCIRACGPRALVVgadllgtveeilpslsenisvwgmkdsvpqgvislkeklSTSPDEPVprshhvvsllks 217
Cdd:cd17653 80 KLPSARIQAILRTSGATLLLT---------------------------------------TDSPDDLA------------ 108
|
170 180
....*....|....*....|....*.
gi 966209822 218 tcLYIFTSGTTGLPKAAVISQLQVLR 243
Cdd:cd17653 109 --YIIFTSGSTGIPKGVMVPHRGVLN 132
|
|
| PaaK |
COG1541 |
Phenylacetate-coenzyme A ligase PaaK, adenylate-forming domain family [Coenzyme transport and ... |
224-365 |
3.47e-04 |
|
Phenylacetate-coenzyme A ligase PaaK, adenylate-forming domain family [Coenzyme transport and metabolism];
Pssm-ID: 441150 [Multi-domain] Cd Length: 423 Bit Score: 43.21 E-value: 3.47e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966209822 224 TSGTTGLPKAAVISQ--LQVL--RGSAVLWAFGCTAHDIVYITLPlYHSSAAILGI-SGCVELGATCVlkkkfSASQFWS 298
Cdd:COG1541 91 SSGTTGKPTVVGYTRkdLDRWaeLFARSLRAAGVRPGDRVQNAFG-YGLFTGGLGLhYGAERLGATVI-----PAGGGNT 164
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966209822 299 D-----CKKYDVTVFqyigeLC-----RYLCKQSKREGE--KDHKVRLAI------GNGIRsdvwREFLDRFGnIKVCEL 360
Cdd:COG1541 165 ErqlrlMQDFGPTVL-----VGtpsylLYLAEVAEEEGIdpRDLSLKKGIfggepwSEEMR----KEIEERWG-IKAYDI 234
|
....*
gi 966209822 361 YAATE 365
Cdd:COG1541 235 YGLTE 239
|
|
| ACSBG_like |
cd05933 |
Bubblegum-like very long-chain fatty acid CoA synthetase (VL-FACS); This family of very ... |
81-284 |
3.66e-04 |
|
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: 43.50 E-value: 3.66e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966209822 81 TYQDVDKRSSRVAHVFLnHSSLKKGDTVALLMSNEPDFVHVWFGLAKLGCVVAFLNTNIRSNSLLNCIRACGPRALVVG- 159
Cdd:cd05933 10 TYKEYYEACRQAAKAFL-KLGLERFHGVGILGFNSPEWFIAAVGAIFAGGIAVGIYTTNSPEACQYVAETSEANILVVEn 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966209822 160 ---ADLLGTVEEILPSLSENISVWG-MKDSVPqGVISLKEKLSTSPDEPVPRSHHVVSLLKST--CLYIFTSGTTGLPKA 233
Cdd:cd05933 89 qkqLQKILQIQDKLPHLKAIIQYKEpLKEKEP-NLYSWDEFMELGRSIPDEQLDAIISSQKPNqcCTLIYTSGTTGMPKG 167
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 966209822 234 AVISQlqvlrgSAVLWAFGCTA-----------HDIVYITLPLYHSSAAILGISGCVELGAT 284
Cdd:cd05933 168 VMLSH------DNITWTAKAASqhmdlrpatvgQESVVSYLPLSHIAAQILDIWLPIKVGGQ 223
|
|
| PTZ00237 |
PTZ00237 |
acetyl-CoA synthetase; Provisional |
49-373 |
3.69e-04 |
|
acetyl-CoA synthetase; Provisional
Pssm-ID: 240325 [Multi-domain] Cd Length: 647 Bit Score: 43.58 E-value: 3.69e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966209822 49 KRGELVT---VLDKFLSH-AKRQprKPFIIYEGDI------YTYQDVDKRSSRVAHVFLNhSSLKKGDTVALLMSNEPDF 118
Cdd:PTZ00237 54 KGGELNTcynVLDIHVKNpLKRD--QDALIYECPYlkktikLTYYQLYEKVCEFSRVLLN-LNISKNDNVLIYMANTLEP 130
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966209822 119 VHVWFGLAKLGCVVAFLNTNIRSNSLLNCIRACGPRaLVVGAD---LLGTVEEILPSLSENISVWGMKdsvPQGVISLKE 195
Cdd:PTZ00237 131 LIAMLSCARIGATHCVLFDGYSVKSLIDRIETITPK-LIITTNygiLNDEIITFTPNLKEAIELSTFK---PSNVITLFR 206
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966209822 196 KLSTSPDE--------PVPRS------------------HHVVSLLKSTCLYI-FTSGTTGLPKAAVISQLQVLRGSAVL 248
Cdd:PTZ00237 207 NDITSESDlkkietipTIPNTlswydeikkikennqspfYEYVPVESSHPLYIlYTSGTTGNSKAVVRSNGPHLVGLKYY 286
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966209822 249 WAFgCTAHDIVYItlplYHSSAAILGIS------GCVELGATCVL------KKKFSASQFWSDCKKYDVTVFQYIGELCR 316
Cdd:PTZ00237 287 WRS-IIEKDIPTV----VFSHSSIGWVSfhgflyGSLSLGNTFVMfeggiiKNKHIEDDLWNTIEKHKVTHTLTLPKTIR 361
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 966209822 317 YLCKQSKrEGEKDHK-------VRLAIGNGIRSDVWREFLDRFGNIKVCELYAATESSI-SFMNY 373
Cdd:PTZ00237 362 YLIKTDP-EATIIRSkydlsnlKEIWCGGEVIEESIPEYIENKLKIKSSRGYGQTEIGItYLYCY 425
|
|
| A_NRPS_Sfm_like |
cd12115 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including Saframycin A gene ... |
436-562 |
3.79e-04 |
|
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: 43.46 E-value: 3.79e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966209822 436 GYAGPYKHTKDKLLCDVFKKGDVYLNTGDLIVQDQDNFLYFWDRTGDTFRWKGENVATTEVADVIGMLDFIQEAnVYGVA 515
Cdd:cd12115 307 GYLGRPGLTAERFLPDPFGPGARLYRTGDLVRWRPDGLLEFLGRADNQVKVRGFRIELGEIEAALRSIPGVREA-VVVAI 385
|
90 100 110 120
....*....|....*....|....*....|....*....|....*...
gi 966209822 516 ISGYEGRAGMASIILKPNTSLDLEKVYEQVVTFLPAYACP-RFLRIQE 562
Cdd:cd12115 386 GDAAGERRLVAYIVAEPGAAGLVEDLRRHLGTRLPAYMVPsRFVRLDA 433
|
|
| PRK07768 |
PRK07768 |
long-chain-fatty-acid--CoA ligase; Validated |
81-237 |
8.17e-04 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236091 [Multi-domain] Cd Length: 545 Bit Score: 42.29 E-value: 8.17e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966209822 81 TYQDVDKRSSRVAHVfLNHSSLKKGDTVALL--MSNE--PDFVHVWFglakLGCVVAFLNTNIRSNSL-------LNCIR 149
Cdd:PRK07768 31 TWGEVHERARRIAGG-LAAAGVGPGDAVAVLagAPVEiaPTAQGLWM----RGASLTMLHQPTPRTDLavwaedtLRVIG 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966209822 150 ACGPRALVVGADLlgtvEEILPSLSENisvwGMKdsvpqgVISLKEKLSTSPDEPVPRSHHVVSLLKstclyiFTSGTTG 229
Cdd:PRK07768 106 MIGAKAVVVGEPF----LAAAPVLEEK----GIR------VLTVADLLAADPIDPVETGEDDLALMQ------LTSGSTG 165
|
....*...
gi 966209822 230 LPKAAVIS 237
Cdd:PRK07768 166 SPKAVQIT 173
|
|
| LC-FACS_euk |
cd05927 |
Eukaryotic long-chain fatty acid CoA synthetase (LC-FACS); The members of this family are ... |
216-267 |
2.93e-03 |
|
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: 40.66 E-value: 2.93e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*..
gi 966209822 216 KSTCLYIFTSGTTGLPKAAVISQLQVLRGSAVLWAFG----CTAHDIVYIT-LPLYH 267
Cdd:cd05927 114 EDLATICYTSGTTGNPKGVMLTHGNIVSNVAGVFKILeilnKINPTDVYISyLPLAH 170
|
|
| A_NRPS_LgrA-like |
cd17645 |
adenylation (A) domain of linear gramicidin synthetase (LgrA) and similar proteins; This ... |
60-129 |
4.36e-03 |
|
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: 39.85 E-value: 4.36e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966209822 60 FLSHAKRQPRKPFIIYEGDIYTYQDVDKRSSRVAHVfLNHSSLKKGDTVALLMSNEPDFVHVWFGLAKLG 129
Cdd:cd17645 4 FEEQVERTPDHVAVVDRGQSLTYKQLNEKANQLARH-LRGKGVKPDDQVGIMLDKSLDMIAAILGVLKAG 72
|
|
| A_NRPS_acs4 |
cd17654 |
acyl-CoA synthetase family member 4; This family of the adenylation (A) domain of nonribosomal ... |
142-368 |
4.74e-03 |
|
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: 39.76 E-value: 4.74e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966209822 142 NSLLNCIrACgpraLVVGADLLgtveEILPSLSENISVWGMKDSVPQGVISLKEKLSTSPDEPVPRSHHVVSLLKSTCLY 221
Cdd:cd17654 53 ESPVAIL-AI----LFLGAAYA----PIDPASPEQRSLTVMKKCHVSYLLQNKELDNAPLSFTPEHRHFNIRTDECLAYV 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966209822 222 IFTSGTTGLPK------AAVISQLQVLRGSavlwaFGCTAHDIVYITLPLyHSSAAILGISGCVELGAT--------CVL 287
Cdd:cd17654 124 IHTSGTTGTPKivavphKCILPNIQHFRSL-----FNITSEDILFLTSPL-TFDPSVVEIFLSLSSGATllivptsvKVL 197
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966209822 288 KKKFSASQFwsdcKKYDVTVFQYIGELCRYLCKQSKREG--EKDHKVR-LAI-GNGIRSDV----WREFLDRfgnIKVCE 359
Cdd:cd17654 198 PSKLADILF----KRHRITVLQATPTLFRRFGSQSIKSTvlSATSSLRvLALgGEPFPSLVilssWRGKGNR---TRIFN 270
|
....*....
gi 966209822 360 LYAATESSI 368
Cdd:cd17654 271 IYGITEVSC 279
|
|
| |
