|
Name |
Accession |
Description |
Interval |
E-value |
| MACS_euk |
cd05928 |
Eukaryotic Medium-chain acyl-CoA synthetase (MACS or ACSM); MACS catalyzes the two-step ... |
54-409 |
0e+00 |
|
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: 735.43 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544134 54 IPEYFNFAKDVLDQWTDKEKAGKKPSNPAFWWINRNGEEMRWSFEELGSLSRKFANILSEACSLQRGDRVILILPRVPEW 133
Cdd:cd05928 1 VPEYFNFASDVLDQWADKEKAGKRPPNPALWWVNGKGDEVKWSFRELGSLSRKAANVLSGACGLQRGDRVAVILPRVPEW 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544134 134 WLANVACLRTGTVLIPGTTQLTQKDILYRLQSSKANCIITNDVLAPAVDAVASKCENLHSKLIVSENSREGWGNLKELMK 213
Cdd:cd05928 81 WLVNVACIRTGLVFIPGTIQLTAKDILYRLQASKAKCIVTSDELAPEVDSVASECPSLKTKLLVSEKSRDGWLNFKELLN 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544134 214 HASDSHTCVKTKHNEIMAIFFTSGTSGYPKMTAHTHSSFGLGLSVNGRFWLDLTPSDVMWNTSDTGWAKSAWSSVFSPWI 293
Cdd:cd05928 161 EASTEHHCVETGSQEPMAIYFTSGTTGSPKMAEHSHSSLGLGLKVNGRYWLDLTASDIMWNTSDTGWIKSAWSSLFEPWI 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544134 294 QGACVFTHHLPRFEPTSILQTLSKYPITVFCSAPTVYRMLVQNDITSYKFKSLKHCVSAGEPITPDVTEKWRNKTGLDIY 373
Cdd:cd05928 241 QGACVFVHHLPRFDPLVILKTLSSYPITTFCGAPTVYRMLVQQDLSSYKFPSLQHCVTGGEPLNPEVLEKWKAQTGLDIY 320
|
330 340 350
....*....|....*....|....*....|....*.
gi 42544134 374 EGYGQTETVLICGNFKGMKIKPGSMGKPSPAFDVKV 409
Cdd:cd05928 321 EGYGQTETGLICANFKGMKIKPGSMGKASPPYDVQI 356
|
|
| MACS_like |
cd05972 |
Medium-chain acyl-CoA synthetase (MACS or ACSM); MACS catalyzes the two-step activation of ... |
95-409 |
1.17e-118 |
|
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: 352.79 E-value: 1.17e-118
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544134 95 WSFEELGSLSRKFANILSEACsLQRGDRVILILPRVPEWWLANVACLRTGTVLIPGTTQLTQKDILYRLQSSKANCIITN 174
Cdd:cd05972 1 WSFRELKRESAKAANVLAKLG-LRKGDRVAVLLPRVPELWAVILAVIKLGAVYVPLTTLLGPKDIEYRLEAAGAKAIVTD 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544134 175 DvlapavdavaskcenlhsklivsensregwgnlkelmkhasdshtcvktkhNEIMAIFFTSGTSGYPKMTAHTHSsFGL 254
Cdd:cd05972 80 A---------------------------------------------------EDPALIYFTSGTTGLPKGVLHTHS-YPL 107
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544134 255 GLSVNGRFWLDLTPSDVMWNTSDTGWAKSAWSSVFSPWIQGACVFTHHLPRFEPTSILQTLSKYPITVFCSAPTVYRMLV 334
Cdd:cd05972 108 GHIPTAAYWLGLRPDDIHWNIADPGWAKGAWSSFFGPWLLGATVFVYEGPRFDAERILELLERYGVTSFCGPPTAYRMLI 187
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 42544134 335 QNDITSYKFKSLKHCVSAGEPITPDVTEKWRNKTGLDIYEGYGQTETVLICGNFKGMKIKPGSMGKPSPAFDVKV 409
Cdd:cd05972 188 KQDLSSYKFSHLRLVVSAGEPLNPEVIEWWRAATGLPIRDGYGQTETGLTVGNFPDMPVKPGSMGRPTPGYDVAI 262
|
|
| MACS_AAE_MA_like |
cd05970 |
Medium-chain acyl-CoA synthetase (MACS) of AAE_MA like; MACS catalyzes the two-step activation ... |
43-407 |
1.52e-115 |
|
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: 348.72 E-value: 1.52e-115
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544134 43 YESMKQDFKLGIPEYFNFAKDVLDQWtdkekAGKKPSNPAFWWINRNGEEMRWSFEELGSLSRKFANILsEACSLQRGDR 122
Cdd:cd05970 1 YEDFHNNFSINVPENFNFAYDVVDAM-----AKEYPDKLALVWCDDAGEERIFTFAELADYSDKTANFF-KAMGIGKGDT 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544134 123 VILILPRVPEWWLANVACLRTGTVLIPGTTQLTQKDILYRLQSS--KANCIITNDVLAPAVDAVASKCENLHSKLIVSEN 200
Cdd:cd05970 75 VMLTLKRRYEFWYSLLALHKLGAIAIPATHQLTAKDIVYRIESAdiKMIVAIAEDNIPEEIEKAAPECPSKPKLVWVGDP 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544134 201 SREGWGNLKELMKHASDS----HTCVKTKHNEIMAIFFTSGTSGYPKMTAHTHSsFGLGLSVNGRFWLDLTPSDVMWNTS 276
Cdd:cd05970 155 VPEGWIDFRKLIKNASPDferpTANSYPCGEDILLVYFSSGTTGMPKMVEHDFT-YPLGHIVTAKYWQNVREGGLHLTVA 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544134 277 DTGWAKSAWSSVFSPWIQGACVFTHHLPRFEPTSILQTLSKYPITVFCSAPTVYRMLVQNDITSYKFKSLKHCVSAGEPI 356
Cdd:cd05970 234 DTGWGKAVWGKIYGQWIAGAAVFVYDYDKFDPKALLEKLSKYGVTTFCAPPTIYRFLIREDLSRYDLSSLRYCTTAGEAL 313
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|.
gi 42544134 357 TPDVTEKWRNKTGLDIYEGYGQTETVLICGNFKGMKIKPGSMGKPSPAFDV 407
Cdd:cd05970 314 NPEVFNTFKEKTGIKLMEGFGQTETTLTIATFPWMEPKPGSMGKPAPGYEI 364
|
|
| Acs |
COG0365 |
Acyl-coenzyme A synthetase/AMP-(fatty) acid ligase [Lipid transport and metabolism]; |
54-409 |
2.32e-115 |
|
Acyl-coenzyme A synthetase/AMP-(fatty) acid ligase [Lipid transport and metabolism];
Pssm-ID: 440134 [Multi-domain] Cd Length: 565 Bit Score: 349.03 E-value: 2.32e-115
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544134 54 IPEYFNFAKDVLDQWtdkekAGKKPSNPAFWWINRNGEEMRWSFEELGSLSRKFANILsEACSLQRGDRVILILPRVPEW 133
Cdd:COG0365 4 VGGRLNIAYNCLDRH-----AEGRGDKVALIWEGEDGEERTLTYAELRREVNRFANAL-RALGVKKGDRVAIYLPNIPEA 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544134 134 WLANVACLRTGTVLIPGTTQLTQKDILYRLQSSKANCIITNDV---------LAPAVDAVASKCENLHSKLIV----SEN 200
Cdd:COG0365 78 VIAMLACARIGAVHSPVFPGFGAEALADRIEDAEAKVLITADGglrggkvidLKEKVDEALEELPSLEHVIVVgrtgADV 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544134 201 SREGWGNLKELMKHASDSHTCVKTKHNEIMAIFFTSGTSGYPKMTAHTHSSFGLGLSVNGRFWLDLTPSDVMWNTSDTGW 280
Cdd:COG0365 158 PMEGDLDWDELLAAASAEFEPEPTDADDPLFILYTSGTTGKPKGVVHTHGGYLVHAATTAKYVLDLKPGDVFWCTADIGW 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544134 281 AKSAWSSVFSPWIQGACVFTHH-LPRF-EPTSILQTLSKYPITVFCSAPTVYRMLVQND---ITSYKFKSLKHCVSAGEP 355
Cdd:COG0365 238 ATGHSYIVYGPLLNGATVVLYEgRPDFpDPGRLWELIEKYGVTVFFTAPTAIRALMKAGdepLKKYDLSSLRLLGSAGEP 317
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*
gi 42544134 356 ITPDVTEKWRNKTGLDIYEGYGQTETV-LICGNFKGMKIKPGSMGKPSPAFDVKV 409
Cdd:COG0365 318 LNPEVWEWWYEAVGVPIVDGWGQTETGgIFISNLPGLPVKPGSMGKPVPGYDVAV 372
|
|
| MACS_like_1 |
cd05974 |
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the ... |
96-409 |
1.24e-78 |
|
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the two-step activation of medium chain fatty acids (containing 4-12 carbons). The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. MACS enzymes are localized to mitochondria.
Pssm-ID: 341278 [Multi-domain] Cd Length: 432 Bit Score: 250.18 E-value: 1.24e-78
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544134 96 SFEELGSLSRKFANILsEACSLQRGDRVILILPRVPEWWLANVACLRTGTVLIPGTTQLTQKDILYRLQSSKAnciitnd 175
Cdd:cd05974 2 SFAEMSARSSRVANFL-RSIGVGRGDRILLMLGNVVELWEAMLAAMKLGAVVIPATTLLTPDDLRDRVDRGGA------- 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544134 176 VLAPAVDAVaskcenlhsklivsensregwgnlkelmkHASDShtcvktkhneiMAIFFTSGTSGYPKMTAHTHSSFGLG 255
Cdd:cd05974 74 VYAAVDENT-----------------------------HADDP-----------MLLYFTSGTTSKPKLVEHTHRSYPVG 113
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544134 256 lSVNGRFWLDLTPSDVMWNTSDTGWAKSAWSSVFSPWIQGACVFTHHLPRFEPTSILQTLSKYPITVFCSAPTVYRMLVQ 335
Cdd:cd05974 114 -HLSTMYWIGLKPGDVHWNISSPGWAKHAWSCFFAPWNAGATVFLFNYARFDAKRVLAALVRYGVTTLCAPPTVWRMLIQ 192
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 42544134 336 NDITSYKFKsLKHCVSAGEPITPDVTEKWRNKTGLDIYEGYGQTETVLICGNFKGMKIKPGSMGKPSPAFDVKV 409
Cdd:cd05974 193 QDLASFDVK-LREVVGAGEPLNPEVIEQVRRAWGLTIRDGYGQTETTALVGNSPGQPVKAGSMGRPLPGYRVAL 265
|
|
| PRK04319 |
PRK04319 |
acetyl-CoA synthetase; Provisional |
35-403 |
5.11e-63 |
|
acetyl-CoA synthetase; Provisional
Pssm-ID: 235279 [Multi-domain] Cd Length: 570 Bit Score: 213.22 E-value: 5.11e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544134 35 ATPQNFSnYESMKQDFKLGIPEYFNFAKDVLDQWTDKEKAGKkpsnPAFWWINRNGEEmRWSFEELGSLSRKFANILSEA 114
Cdd:PRK04319 20 ETYATFS-WEEVEKEFSWLETGKVNIAYEAIDRHADGGRKDK----VALRYLDASRKE-KYTYKELKELSNKFANVLKEL 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544134 115 cSLQRGDRVILILPRVPEWWLANVACLRTGTVLIPGTTQLTQKDILYRLQSSKANCIITNDVLAPAVdaVASKCENLHSK 194
Cdd:PRK04319 94 -GVEKGDRVFIFMPRIPELYFALLGALKNGAIVGPLFEAFMEEAVRDRLEDSEAKVLITTPALLERK--PADDLPSLKHV 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544134 195 LIVSENSREGWG--NLKELMKHASDSHTCVKTKHNEIMAIFFTSGTSGYPKMTAHTHSSFgLGLSVNGRFWLDLTPSDVM 272
Cdd:PRK04319 171 LLVGEDVEEGPGtlDFNALMEQASDEFDIEWTDREDGAILHYTSGSTGKPKGVLHVHNAM-LQHYQTGKYVLDLHEDDVY 249
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544134 273 WNTSDTGWAKSAWSSVFSPWIQGA--CVFThhlPRFEPTSILQTLSKYPITVFCSAPTVYRMLVQND---ITSYKFKSLK 347
Cdd:PRK04319 250 WCTADPGWVTGTSYGIFAPWLNGAtnVIDG---GRFSPERWYRILEDYKVTVWYTAPTAIRMLMGAGddlVKKYDLSSLR 326
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*....
gi 42544134 348 HCVSAGEPITPDVTeKWRNKT-GLDIYEGYGQTET--VLICgNFKGMKIKPGSMGKPSP 403
Cdd:PRK04319 327 HILSVGEPLNPEVV-RWGMKVfGLPIHDNWWMTETggIMIA-NYPAMDIKPGSMGKPLP 383
|
|
| AMP-binding |
pfam00501 |
AMP-binding enzyme; |
72-409 |
1.04e-55 |
|
AMP-binding enzyme;
Pssm-ID: 459834 [Multi-domain] Cd Length: 417 Bit Score: 189.83 E-value: 1.04e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544134 72 EKAGKKPSNPAFwwinRNGEEMRWSFEELGSLSRKFANILsEACSLQRGDRVILILPRVPEWWLANVACLRTGTVLIPGT 151
Cdd:pfam00501 3 RQAARTPDKTAL----EVGEGRRLTYRELDERANRLAAGL-RALGVGKGDRVAILLPNSPEWVVAFLACLKAGAVYVPLN 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544134 152 TQLTQKDILYRLQSSKANCIITNDVL-APAVDAVASKCENLHSKLIVS-ENSREGWGNLKELMKHASDSHTCVKTKHNEI 229
Cdd:pfam00501 78 PRLPAEELAYILEDSGAKVLITDDALkLEELLEALGKLEVVKLVLVLDrDPVLKEEPLPEEAKPADVPPPPPPPPDPDDL 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544134 230 MAIFFTSGTSGYPKMTAHTH---SSFGLGLSVNGRFWLDLTPSDVMWNTSDTGWAKSAWSSVFSPWIQGA-CVFTHHLPR 305
Cdd:pfam00501 158 AYIIYTSGTTGKPKGVMLTHrnlVANVLSIKRVRPRGFGLGPDDRVLSTLPLFHDFGLSLGLLGPLLAGAtVVLPPGFPA 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544134 306 FEPTSILQTLSKYPITVFCSAPTVYRMLVQN-DITSYKFKSLKHCVSAGEPITPDVTEKWRNKTGLDIYEGYGQTET--- 381
Cdd:pfam00501 238 LDPAALLELIERYKVTVLYGVPTLLNMLLEAgAPKRALLSSLRLVLSGGAPLPPELARRFRELFGGALVNGYGLTETtgv 317
|
330 340
....*....|....*....|....*...
gi 42544134 382 VLICGNFKGMKIKPGSMGKPSPAFDVKV 409
Cdd:pfam00501 318 VTTPLPLDEDLRSLGSVGRPLPGTEVKI 345
|
|
| MACS_like_4 |
cd05969 |
Uncharacterized subfamily of Acetyl-CoA synthetase like family (ACS); This family is most ... |
95-403 |
2.61e-52 |
|
Uncharacterized subfamily of Acetyl-CoA synthetase like family (ACS); This family is most similar to acetyl-CoA synthetase. Acetyl-CoA synthetase (ACS) catalyzes the formation of acetyl-CoA from acetate, CoA, and ATP. Synthesis of acetyl-CoA is carried out in a two-step reaction. In the first step, the enzyme catalyzes the synthesis of acetyl-AMP intermediate from acetate and ATP. In the second step, acetyl-AMP reacts with CoA to produce acetyl-CoA. This enzyme is only present in bacteria.
Pssm-ID: 341273 [Multi-domain] Cd Length: 442 Bit Score: 181.55 E-value: 2.61e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544134 95 WSFEELGSLSRKFANILsEACSLQRGDRVILILPRVPEWWLANVACLRTGTVLIPGTTQLTQKDILYRLQSSKANCIITN 174
Cdd:cd05969 1 YTFAQLKVLSARFANVL-KSLGVGKGDRVFVLSPRSPELYFSMLGIGKIGAVICPLFSAFGPEAIRDRLENSEAKVLITT 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544134 175 DVLAPavdavaskcenlhsklivsensregwgnlkelmkhasdshtcvKTKHNEIMAIFFTSGTSGYPKMTAHTHSSFgL 254
Cdd:cd05969 80 EELYE-------------------------------------------RTDPEDPTLLHYTSGTTGTPKGVLHVHDAM-I 115
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544134 255 GLSVNGRFWLDLTPSDVMWNTSDTGWAKSAWSSVFSPWIQGACVFTHHlPRFEPTSILQTLSKYPITVFCSAPTVYRMLV 334
Cdd:cd05969 116 FYYFTGKYVLDLHPDDIYWCTADPGWVTGTVYGIWAPWLNGVTNVVYE-GRFDAESWYGIIERVKVTVWYTAPTAIRMLM 194
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 42544134 335 QNDI---TSYKFKSLKHCVSAGEPITPDVTEKWRNKTGLDIYEGYGQTET--VLICgNFKGMKIKPGSMGKPSP 403
Cdd:cd05969 195 KEGDelaRKYDLSSLRFIHSVGEPLNPEAIRWGMEVFGVPIHDTWWQTETgsIMIA-NYPCMPIKPGSMGKPLP 267
|
|
| MenE/FadK |
COG0318 |
O-succinylbenzoic acid-CoA ligase MenE or related acyl-CoA synthetase (AMP-forming) [Lipid ... |
63-410 |
5.15e-50 |
|
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: 175.77 E-value: 5.15e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544134 63 DVLDQWtdkekAGKKPSNPAFWWINRngeemRWSFEELGSLSRKFANILSEACsLQRGDRVILILPRVPEWWLANVACLR 142
Cdd:COG0318 3 DLLRRA-----AARHPDRPALVFGGR-----RLTYAELDARARRLAAALRALG-VGPGDRVALLLPNSPEFVVAFLAALR 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544134 143 TGTVLIPGTTQLTQKDILYRLQSSKANCIITndvlapavdavaskcenlhsklivsensregwgnlkelmkhasdshtcv 222
Cdd:COG0318 72 AGAVVVPLNPRLTAEELAYILEDSGARALVT------------------------------------------------- 102
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544134 223 ktkhneiMAIFFTSGTSGYPKMTAHTHSSFgLGLSVNGRFWLDLTPSDVMWNTS----DTGWaksaWSSVFSPWIQGACV 298
Cdd:COG0318 103 -------ALILYTSGTTGRPKGVMLTHRNL-LANAAAIAAALGLTPGDVVLVALplfhVFGL----TVGLLAPLLAGATL 170
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544134 299 ftHHLPRFEPTSILQTLSKYPITVFCSAPTVYRMLVQN-DITSYKFKSLKHCVSAGEPITPDVTEKWRNKTGLDIYEGYG 377
Cdd:COG0318 171 --VLLPRFDPERVLELIERERVTVLFGVPTMLARLLRHpEFARYDLSSLRLVVSGGAPLPPELLERFEERFGVRIVEGYG 248
|
330 340 350
....*....|....*....|....*....|....*
gi 42544134 378 QTET-VLICGNFKGMK-IKPGSMGKPSPAFDVKVC 410
Cdd:COG0318 249 LTETsPVVTVNPEDPGeRRPGSVGRPLPGVEVRIV 283
|
|
| BCL_4HBCL |
cd05959 |
Benzoate CoA ligase (BCL) and 4-Hydroxybenzoate-Coenzyme A Ligase (4-HBA-CoA ligase); Benzoate ... |
56-408 |
1.60e-47 |
|
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: 170.24 E-value: 1.60e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544134 56 EYFNFAKDVLDQwTDKEKAGKkpsnPAFwwINRNGEemrWSFEELGSLSRKFANILSEAcSLQRGDRVILILPRVPEWWL 135
Cdd:cd05959 1 EKYNAATLVDLN-LNEGRGDK----TAF--IDDAGS---LTYAELEAEARRVAGALRAL-GVKREERVLLIMLDTVDFPT 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544134 136 ANVACLRTGTVLIPGTTQLTQKDILYRLQSSKANCIITNDVLAPAVDAVASKCENLHSKLIVSENSRE--GWGNLKELMK 213
Cdd:cd05959 70 AFLGAIRAGIVPVPVNTLLTPDDYAYYLEDSRARVVVVSGELAPVLAAALTKSEHTLVVLIVSGGAGPeaGALLLAELVA 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544134 214 HASDSHTCVKTKHNEIMAIFFTSGTSGYPKMTAHTHSSFGLGLSVNGRFWLDLTPSDVMWNTSDTGWAKSAWSSVFSP-W 292
Cdd:cd05959 150 AEAEQLKPAATHADDPAFWLYSSGSTGRPKGVVHLHADIYWTAELYARNVLGIREDDVCFSAAKLFFAYGLGNSLTFPlS 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544134 293 IQGACVFthhLP-RFEPTSILQTLSKYPITVFCSAPTVYR-MLVQNDITSYKFKSLKHCVSAGEPITPDVTEKWRNKTGL 370
Cdd:cd05959 230 VGATTVL---MPeRPTPAAVFKRIRRYRPTVFFGVPTLYAaMLAAPNLPSRDLSSLRLCVSAGEALPAEVGERWKARFGL 306
|
330 340 350
....*....|....*....|....*....|....*....
gi 42544134 371 DIYEGYGQTETVLI-CGNFKGmKIKPGSMGKPSPAFDVK 408
Cdd:cd05959 307 DILDGIGSTEMLHIfLSNRPG-RVRYGTTGKPVPGYEVE 344
|
|
| FC-FACS_FadD_like |
cd05936 |
Prokaryotic long-chain fatty acid CoA synthetases similar to Escherichia coli FadD; This ... |
63-410 |
1.12e-43 |
|
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: 158.88 E-value: 1.12e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544134 63 DVLDqwtdkEKAGKKPSNPAFWWINRngeemRWSFEELGSLSRKFANILSEAcSLQRGDRVILILPRVPEWWLANVACLR 142
Cdd:cd05936 3 DLLE-----EAARRFPDKTALIFMGR-----KLTYRELDALAEAFAAGLQNL-GVQPGDRVALMLPNCPQFPIAYFGALK 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544134 143 TGTVLIPGTTQLTQKDILYRLQSSKANCIIT----NDVLAPAvDAVASKCENlhsklivsensregwgnlkelmkHASDs 218
Cdd:cd05936 72 AGAVVVPLNPLYTPRELEHILNDSGAKALIVavsfTDLLAAG-APLGERVAL-----------------------TPED- 126
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544134 219 htcvktkhneIMAIFFTSGTSGYPKMTAHTHSSFGLGLSVNgRFWL--DLTPSDVMWNT-------SDTgwaksawSSVF 289
Cdd:cd05936 127 ----------VAVLQYTSGTTGVPKGAMLTHRNLVANALQI-KAWLedLLEGDDVVLAAlplfhvfGLT-------VALL 188
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544134 290 SPWIQGACVFThhLPRFEPTSILQTLSKYPITVFCSAPTVYRMLVQN-DITSYKFKSLKHCVSAGEPITPDVTEKWRNKT 368
Cdd:cd05936 189 LPLALGATIVL--IPRFRPIGVLKEIRKHRVTIFPGVPTMYIALLNApEFKKRDFSSLRLCISGGAPLPVEVAERFEELT 266
|
330 340 350 360
....*....|....*....|....*....|....*....|...
gi 42544134 369 GLDIYEGYGQTETV-LICGNFKGMKIKPGSMGKPSPAFDVKVC 410
Cdd:cd05936 267 GVPIVEGYGLTETSpVVAVNPLDGPRKPGSIGIPLPGTEVKIV 309
|
|
| MACS_like_3 |
cd05971 |
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the ... |
89-409 |
5.78e-40 |
|
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: 148.35 E-value: 5.78e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544134 89 NGEEMRWSFEELGSLSRKFANILSEAcSLQRGDRVILILPRVPEWWLANVACLRTGTVLIPGTTQLTQKDILYRLQSSKA 168
Cdd:cd05971 1 KGTPEKVTFKELKTASNRFANVLKEI-GLEKGDRVGVFLSQGPECAIAHIAILRSGAIAVPLFALFGPEALEYRLSNSGA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544134 169 NCIITNDVLAPAVdavaskcenlhsklivsensregwgnlkelmkhasdshtcvktkhneimaIFFTSGTSGYPKMTAHT 248
Cdd:cd05971 80 SALVTDGSDDPAL--------------------------------------------------IIYTSGTTGPPKGALHA 109
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544134 249 HSsFGLGLSVNGRFWLDLTP--SDVMWNTSDTGWAKSAWSSVFSPWIQGACVFTHHLPRFEPTSILQTLSKYPITVFCSA 326
Cdd:cd05971 110 HR-VLLGHLPGVQFPFNLFPrdGDLYWTPADWAWIGGLLDVLLPSLYFGVPVLAHRMTKFDPKAALDLMSRYGVTTAFLP 188
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544134 327 PTVYRML-VQNDITSYKFKSLKHCVSAGEPITPDVTEKWRNKTGLDIYEGYGQTETVLICGNFKG-MKIKPGSMGKPSPA 404
Cdd:cd05971 189 PTALKMMrQQGEQLKHAQVKLRAIATGGESLGEELLGWAREQFGVEVNEFYGQTECNLVIGNCSAlFPIKPGSMGKPIPG 268
|
....*
gi 42544134 405 FDVKV 409
Cdd:cd05971 269 HRVAI 273
|
|
| MACS_like_2 |
cd05973 |
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the ... |
96-432 |
1.47e-39 |
|
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: 147.28 E-value: 1.47e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544134 96 SFEELGSLSRKFANILSEAcSLQRGDRVILILPRVPEWWLANVACLRTGTVLIPGTTQLTQKDILYRLQSSKANCIITNd 175
Cdd:cd05973 2 TFGELRALSARFANALQEL-GVGPGDVVAGLLPRTPELVVTILGIWRLGAVYQPLFTAFGPKAIEHRLRTSGARLVVTD- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544134 176 vlapavdavaskCENLHsklivsensregwgnlkelmKHASDshtcvktkhneIMAIFFTSGTSGYPKMTAHTHSSFgLG 255
Cdd:cd05973 80 ------------AANRH--------------------KLDSD-----------PFVMMFTSGTTGLPKGVPVPLRAL-AA 115
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544134 256 LSVNGRFWLDLTPSDVMWNTSDTGWAKSAWSSVFSPWIQGACVFTHHLPrFEPTSILQTLSKYPITVFCSAPTVYRMLVQ 335
Cdd:cd05973 116 FGAYLRDAVDLRPEDSFWNAADPGWAYGLYYAITGPLALGHPTILLEGG-FSVESTWRVIERLGVTNLAGSPTAYRLLMA 194
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544134 336 NDITSYKFK--SLKHCVSAGEPITPDVTEKWRNKTGLDIYEGYGQTETVLICGNFKGMK--IKPGSMGKPSPAFDVKVC- 410
Cdd:cd05973 195 AGAEVPARPkgRLRRVSSAGEPLTPEVIRWFDAALGVPIHDHYGQTELGMVLANHHALEhpVHAGSAGRAMPGWRVAVLd 274
|
330 340 350
....*....|....*....|....*....|...
gi 42544134 411 ----TSPSRRM-------FNNPICTLPTYRLPP 432
Cdd:cd05973 275 ddgdELGPGEPgrlaidiANSPLMWFRGYQLPD 307
|
|
| AFD_class_I |
cd04433 |
Adenylate forming domain, Class I, also known as the ANL superfamily; This family is known as ... |
228-410 |
5.77e-39 |
|
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: 143.19 E-value: 5.77e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544134 228 EIMAIFFTSGTSGYPKMTAHTHSSFgLGLSVNGRFWLDLTPSDVMWNTSDTGWAkSAWSSVFSPWIQGACVFTHhlPRFE 307
Cdd:cd04433 1 DPALILYTSGTTGKPKGVVLSHRNL-LAAAAALAASGGLTEGDVFLSTLPLFHI-GGLFGLLGALLAGGTVVLL--PKFD 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544134 308 PTSILQTLSKYPITVFCSAPTVYRMLVQND-ITSYKFKSLKHCVSAGEPITPDVTEKWRNKTGLDIYEGYGQTET--VLI 384
Cdd:cd04433 77 PEAALELIEREKVTILLGVPTLLARLLKAPeSAGYDLSSLRALVSGGAPLPPELLERFEEAPGIKLVNGYGLTETggTVA 156
|
170 180
....*....|....*....|....*.
gi 42544134 385 CGNFKGMKIKPGSMGKPSPAFDVKVC 410
Cdd:cd04433 157 TGPPDDDARKPGSVGRPVPGVEVRIV 182
|
|
| PRK06187 |
PRK06187 |
long-chain-fatty-acid--CoA ligase; Validated |
62-409 |
1.87e-37 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 235730 [Multi-domain] Cd Length: 521 Bit Score: 143.02 E-value: 1.87e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544134 62 KDVLDQWtdkekAGKKPSNPAFWWinrngEEMRWSFEELGSLSRKFANILsEACSLQRGDRVILILPRVPEWWLANVACL 141
Cdd:PRK06187 9 GRILRHG-----ARKHPDKEAVYF-----DGRRTTYAELDERVNRLANAL-RALGVKKGDRVAVFDWNSHEYLEAYFAVP 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544134 142 RTGTVLIPGTTQLTQKDILYRLQSSKANCIITNDVLAPAVDAVASKCENLHSKLIVSENSREG----WGNLKELMKHASD 217
Cdd:PRK06187 78 KIGAVLHPINIRLKPEEIAYILNDAEDRVVLVDSEFVPLLAAILPQLPTVRTVIVEGDGPAAPlapeVGEYEELLAAASD 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544134 218 SHTCVKTKHNEIMAIFFTSGTSGYPKMTAHTHSSFgLGLSVNGRFWLDLTPSDV------MWNTSDTGWAksawssvFSP 291
Cdd:PRK06187 158 TFDFPDIDENDAAAMLYTSGTTGHPKGVVLSHRNL-FLHSLAVCAWLKLSRDDVylvivpMFHVHAWGLP-------YLA 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544134 292 WIQGAcvfTHHLP-RFEPTSILQTLSKYPITVFCSAPTVYRMLVQNDITS-YKFKSLKHCVSAGEPITPDVTEKWRNKTG 369
Cdd:PRK06187 230 LMAGA---KQVIPrRFDPENLLDLIETERVTFFFAVPTIWQMLLKAPRAYfVDFSSLRLVIYGGAALPPALLREFKEKFG 306
|
330 340 350 360
....*....|....*....|....*....|....*....|....*.
gi 42544134 370 LDIYEGYGQTETV-LICGNF-----KGMKIKPGSMGKPSPAFDVKV 409
Cdd:PRK06187 307 IDLVQGYGMTETSpVVSVLPpedqlPGQWTKRRSAGRPLPGVEARI 352
|
|
| benz_CoA_lig |
TIGR02262 |
benzoate-CoA ligase family; Characterized members of this protein family include benzoate-CoA ... |
80-409 |
3.45e-36 |
|
benzoate-CoA ligase family; Characterized members of this protein family include benzoate-CoA ligase, 4-hydroxybenzoate-CoA ligase, 2-aminobenzoate-CoA ligase, etc. Members are related to fatty acid and acetate CoA ligases.
Pssm-ID: 274059 [Multi-domain] Cd Length: 505 Bit Score: 139.20 E-value: 3.45e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544134 80 NPAFWWINRNGEEMR------------WSFEELGSLSRKFANILSeACSLQRGDRVILILPRVPEWWLANVACLRTGTVL 147
Cdd:TIGR02262 4 NAAEDLLDRNVVEGRggktafiddissLSYGELEAQVRRLAAALR-RLGVKREERVLLLMLDGVDFPIAFLGAIRAGIVP 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544134 148 IPGTTQLTQKDILYRLQSSKANCIITNDVLAPAVDAVASKCENLHSkLIVSENSREGWGNLKELMKHASDSHTCVKTKHN 227
Cdd:TIGR02262 83 VALNTLLTADDYAYMLEDSRARVVFVSGALLPVIKAALGKSPHLEH-RVVVGRPEAGEVQLAELLATESEQFKPAATQAD 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544134 228 EIMAIFFTSGTSGYPKMTAHTHSSFGLGLSVNGRFWLDLTPSDVMWNTSDTGWAKSAWSSVFSPWIQGACVFTHHlPRFE 307
Cdd:TIGR02262 162 DPAFWLYSSGSTGMPKGVVHTHSNPYWTAELYARNTLGIREDDVCFSAAKLFFAYGLGNALTFPMSVGATTVLMG-ERPT 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544134 308 PTSILQTLSKYPITVFCSAPTVYR-MLVQNDITSYKFKSLKHCVSAGEPITPDVTEKWRNKTGLDIYEGYGQTETVLICG 386
Cdd:TIGR02262 241 PDAVFDRLRRHQPTIFYGVPTLYAaMLADPNLPSEDQVRLRLCTSAGEALPAEVGQRWQARFGVDIVDGIGSTEMLHIFL 320
|
330 340
....*....|....*....|...
gi 42544134 387 NFKGMKIKPGSMGKPSPAFDVKV 409
Cdd:TIGR02262 321 SNLPGDVRYGTSGKPVPGYRLRL 343
|
|
| ACS-like |
cd17634 |
acetate-CoA ligase; This family includes acyl- and aryl-CoA ligases, as well as the ... |
95-409 |
3.06e-33 |
|
acetate-CoA ligase; This family includes acyl- and aryl-CoA ligases, as well as the adenylation domain of nonribosomal peptide synthetases and firefly luciferases. The adenylate-forming enzymes catalyze an ATP-dependent two-step reaction to first activate a carboxylate substrate as an adenylate and then transfer the carboxylate to the pantetheine group of either coenzyme A or an acyl-carrier protein. The active site of the domain is located at the interface of a large N-terminal subdomain and a smaller C-terminal subdomain.
Pssm-ID: 341289 [Multi-domain] Cd Length: 587 Bit Score: 131.93 E-value: 3.06e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544134 95 WSFEELGSLSRKFANILsEACSLQRGDRVILILPRVPEWWLANVACLRTGTVLIPGTTQLTQKDILYRLQSSKANCIITN 174
Cdd:cd17634 85 ISYRELHREVCRFAGTL-LDLGVKKGDRVAIYMPMIPEAAVAMLACARIGAVHSVIFGGFAPEAVAGRIIDSSSRLLITA 163
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544134 175 D----------VLAPAVDAVASKCENLHSKLIVSensREG---------WGNLKELMKHASDSHTCVKTKHNEIMAIFFT 235
Cdd:cd17634 164 DggvragrsvpLKKNVDDALNPNVTSVEHVIVLK---RTGsdidwqegrDLWWRDLIAKASPEHQPEAMNAEDPLFILYT 240
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544134 236 SGTSGYPKMTAHTHSSFGLGLSVNGRFWLDLTPSDVMWNTSDTGWAKSAWSSVFSPWIQGACVFTHH-LPRF-EPTSILQ 313
Cdd:cd17634 241 SGTTGKPKGVLHTTGGYLVYAATTMKYVFDYGPGDIYWCTADVGWVTGHSYLLYGPLACGATTLLYEgVPNWpTPARMWQ 320
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544134 314 TLSKYPITVFCSAPTVYRMLVQND---ITSYKFKSLKHCVSAGEPITPDVTE-KWR--NKTGLDIYEGYGQTETV-LICG 386
Cdd:cd17634 321 VVDKHGVNILYTAPTAIRALMAAGddaIEGTDRSSLRILGSVGEPINPEAYEwYWKkiGKEKCPVVDTWWQTETGgFMIT 400
|
330 340
....*....|....*....|....
gi 42544134 387 NFKGM-KIKPGSMGKPSPAFDVKV 409
Cdd:cd17634 401 PLPGAiELKAGSATRPVFGVQPAV 424
|
|
| PRK07656 |
PRK07656 |
long-chain-fatty-acid--CoA ligase; Validated |
74-409 |
5.89e-33 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236072 [Multi-domain] Cd Length: 513 Bit Score: 130.02 E-value: 5.89e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544134 74 AGKKPSNPAFWWinrngEEMRWSFEELGSLSRKFANILsEACSLQRGDRVILILPRVPEWWLANVACLRTGTVLIPGTTQ 153
Cdd:PRK07656 15 ARRFGDKEAYVF-----GDQRLTYAELNARVRRAAAAL-AALGIGKGDRVAIWAPNSPHWVIAALGALKAGAVVVPLNTR 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544134 154 LTQKDILYRLQSSKANCIITNDVLAPAVDAVASKCENLHSKLIV----SENSREGWGNLKELMKHASDSHTCVKTKHNEI 229
Cdd:PRK07656 89 YTADEAAYILARGDAKALFVLGLFLGVDYSATTRLPALEHVVICeteeDDPHTEKMKTFTDFLAAGDPAERAPEVDPDDV 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544134 230 MAIFFTSGTSGYPK--MTAHTHSsfglgLSvNGRFW---LDLTPSD---------------VMWNTsdtgwaksawssvf 289
Cdd:PRK07656 169 ADILFTSGTTGRPKgaMLTHRQL-----LS-NAADWaeyLGLTEGDrylaanpffhvfgykAGVNA-------------- 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544134 290 sPWIQGACVFTHhlPRFEPTSILQTLSKYPITVFCSAPTVYRMLVQN-DITSYKFKSLKHCVSAGEPITPDVTEKWRNKT 368
Cdd:PRK07656 229 -PLMRGATILPL--PVFDPDEVFRLIETERITVLPGPPTMYNSLLQHpDRSAEDLSSLRLAVTGAASMPVALLERFESEL 305
|
330 340 350 360
....*....|....*....|....*....|....*....|....*
gi 42544134 369 GLDIY-EGYGQTE---TVLICGNFKGMKIKPGSMGKPSPAFDVKV 409
Cdd:PRK07656 306 GVDIVlTGYGLSEasgVTTFNRLDDDRKTVAGTIGTAIAGVENKI 350
|
|
| Firefly_Luc_like |
cd05911 |
Firefly luciferase of light emitting insects and 4-Coumarate-CoA Ligase (4CL); This family ... |
95-409 |
5.99e-33 |
|
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: 129.64 E-value: 5.99e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544134 95 WSFEELGSLSRKFANILSEAcSLQRGDRVILILPRVPEWWLANVACLRTGTVLIPGTTQLTQKDILYRLQSSKANCIIT- 173
Cdd:cd05911 11 LTYAQLRTLSRRLAAGLRKL-GLKKGDVVGIISPNSTYYPPVFLGCLFAGGIFSAANPIYTADELAHQLKISKPKVIFTd 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544134 174 NDVLAPAVDAVasKCENLHSKLIVSENSREGWGNLKELMK---HASDSH--TCVKTKHNEIMAIFFTSGTSGYPKMTAHT 248
Cdd:cd05911 90 PDGLEKVKEAA--KELGPKDKIIVLDDKPDGVLSIEDLLSptlGEEDEDlpPPLKDGKDDTAAILYSSGTTGLPKGVCLS 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544134 249 HSSFGLGL-SVNGRFWLDLTPSDVMWNTSDTGWAKSAWSSVFSPWiQGACVFTHhlPRFEPTSILQTLSKYPITVFCSAP 327
Cdd:cd05911 168 HRNLIANLsQVQTFLYGNDGSNDVILGFLPLYHIYGLFTTLASLL-NGATVIIM--PKFDSELFLDLIEKYKITFLYLVP 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544134 328 TVYRMLVQN-DITSYKFKSLKHCVSAGEPITPDVTEKWRNKTGL-DIYEGYGQTETVLICGNFKGMKIKPGSMGKPSPAF 405
Cdd:cd05911 245 PIAAALAKSpLLDKYDLSSLRVILSGGAPLSKELQELLAKRFPNaTIKQGYGMTETGGILTVNPDGDDKPGSVGRLLPNV 324
|
....
gi 42544134 406 DVKV 409
Cdd:cd05911 325 EAKI 328
|
|
| ABCL |
cd05958 |
2-aminobenzoate-CoA ligase (ABCL); ABCL catalyzes the initial step in the 2-aminobenzoate ... |
92-409 |
5.06e-32 |
|
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: 126.44 E-value: 5.06e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544134 92 EMRWSFEELGSLSRKFANILSEACSLQRGDRVILILPRVPEWWLANVACLRTGTVLIPGTTQLTQKDILYRLQsskaNCI 171
Cdd:cd05958 8 EREWTYRDLLALANRIANVLVGELGIVPGNRVLLRGSNSPELVACWFGIQKAGAIAVATMPLLRPKELAYILD----KAR 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544134 172 ITNDVLAPAVDAVaskcenlhsklivsensregwgnlkelmkhasdshtcvktkhNEIMAIFFTSGTSGYPKMTAHTHSS 251
Cdd:cd05958 84 ITVALCAHALTAS------------------------------------------DDICILAFTSGTTGAPKATMHFHRD 121
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544134 252 FGLGLSVNGRFWLDLTPSDVMWNTSDTGWAKSAWSSVFSPWIQGACVFThhLPRFEPTSILQTLSKYPITVFCSAPTVYR 331
Cdd:cd05958 122 PLASADRYAVNVLRLREDDRFVGSPPLAFTFGLGGVLLFPFGVGASGVL--LEEATPDLLLSAIARYKPTVLFTAPTAYR 199
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 42544134 332 -MLVQNDITSYKFKSLKHCVSAGEPITPDVTEKWRNKTGLDIYEGYGQTETVLICGNFKGMKIKPGSMGKPSPAFDVKV 409
Cdd:cd05958 200 aMLAHPDAAGPDLSSLRKCVSAGEALPAALHRAWKEATGIPIIDGIGSTEMFHIFISARPGDARPGATGKPVPGYEAKV 278
|
|
| BCL_like |
cd05919 |
Benzoate CoA ligase (BCL) and similar adenylate forming enzymes; This family contains benzoate ... |
96-409 |
6.17e-32 |
|
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: 126.04 E-value: 6.17e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544134 96 SFEELGSLSRKFANILsEACSLQRGDRVILILPRVPEWWLANVACLRTGTVLIPGTTQLTQKDILYRLQSSKANCIITND 175
Cdd:cd05919 12 TYGQLHDGANRLGSAL-RNLGVSSGDRVLLLMLDSPELVQLFLGCLARGAIAVVINPLLHPDDYAYIARDCEARLVVTSA 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544134 176 vlapavDAVASkcenlhsklivsensregwgnlkelmkhasdshtcvktkhneimaIFFTSGTSGYPKMTAHTHSSFGLG 255
Cdd:cd05919 91 ------DDIAY---------------------------------------------LLYSSGTTGPPKGVMHAHRDPLLF 119
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544134 256 LSVNGRFWLDLTPSDVMWNTSDTGWAKSAWSSVFSPWIQGACVFTHHLPRfEPTSILQTLSKYPITVFCSAPTVY-RMLV 334
Cdd:cd05919 120 ADAMAREALGLTPGDRVFSSAKMFFGYGLGNSLWFPLAVGASAVLNPGWP-TAERVLATLARFRPTVLYGVPTFYaNLLD 198
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 42544134 335 QNDITSYKFKSLKHCVSAGEPITPDVTEKWRNKTGLDIYEGYGQTETVLICGNFKGMKIKPGSMGKPSPAFDVKV 409
Cdd:cd05919 199 SCAGSPDALRSLRLCVSAGEALPRGLGERWMEHFGGPILDGIGATEVGHIFLSNRPGAWRLGSTGRPVPGYEIRL 273
|
|
| AACS_like |
cd05968 |
Uncharacterized acyl-CoA synthetase subfamily similar to Acetoacetyl-CoA synthetase; This ... |
59-409 |
2.16e-30 |
|
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: 123.75 E-value: 2.16e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544134 59 NFAKDVLDQWTdkekaGKKPSNPAFWWINRNGEEMRWSFEELGSLSRKFANILsEACSLQRGDRVILILPRVPEWWLANV 138
Cdd:cd05968 61 NIVEQLLDKWL-----ADTRTRPALRWEGEDGTSRTLTYGELLYEVKRLANGL-RALGVGKGDRVGIYLPMIPEIVPAFL 134
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544134 139 ACLRTGTVLIPGTTQLTQKDILYRLQSSKANCIITNDV---------LAPAVDAVASKCENLHSKLIVSENSRE-GWGNL 208
Cdd:cd05968 135 AVARIGGIVVPIFSGFGKEAAATRLQDAEAKALITADGftrrgrevnLKEEADKACAQCPTVEKVVVVRHLGNDfTPAKG 214
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544134 209 KELMKH---ASDSHTCVKTKHNEIMAIFFTSGTSGYPKMTAHTHSSFGLGLSVNGRFWLDLTPSDVMWNTSDTGWAKSAW 285
Cdd:cd05968 215 RDLSYDeekETAGDGAERTESEDPLMIIYTSGTTGKPKGTVHVHAGFPLKAAQDMYFQFDLKPGDLLTWFTDLGWMMGPW 294
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544134 286 sSVFSPWIQGACVFTHH-LPRF-EPTSILQTLSKYPITVFCSAPTVYRMLV---QNDITSYKFKSLKHCVSAGEPITPdv 360
Cdd:cd05968 295 -LIFGGLILGATMVLYDgAPDHpKADRLWRMVEDHEITHLGLSPTLIRALKprgDAPVNAHDLSSLRVLGSTGEPWNP-- 371
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*.
gi 42544134 361 tEKW------RNKTGLDIYEGYGQTETV-LICGNFKGMKIKPGSMGKPSPAFDVKV 409
Cdd:cd05968 372 -EPWnwlfetVGKGRNPIINYSGGTEISgGILGNVLIKPIKPSSFNGPVPGMKADV 426
|
|
| ACS |
cd05966 |
Acetyl-CoA synthetase (also known as acetate-CoA ligase and acetyl-activating enzyme); ... |
59-409 |
7.18e-30 |
|
Acetyl-CoA synthetase (also known as acetate-CoA ligase and acetyl-activating enzyme); Acetyl-CoA synthetase (ACS, EC 6.2.1.1, acetate#CoA ligase or acetate:CoA ligase (AMP-forming)) catalyzes the formation of acetyl-CoA from acetate, CoA, and ATP. Synthesis of acetyl-CoA is carried out in a two-step reaction. In the first step, the enzyme catalyzes the synthesis of acetyl-AMP intermediate from acetate and ATP. In the second step, acetyl-AMP reacts with CoA to produce acetyl-CoA. This enzyme is widely present in all living organisms. The activity of this enzyme is crucial for maintaining the required levels of acetyl-CoA, a key intermediate in many important biosynthetic and catabolic processes. Acetyl-CoA is used in the biosynthesis of glucose, fatty acids, and cholesterol. It can also be used in the production of energy in the citric acid cycle. Eukaryotes typically have two isoforms of acetyl-CoA synthetase, a cytosolic form involved in biosynthetic processes and a mitochondrial form primarily involved in energy generation.
Pssm-ID: 341270 [Multi-domain] Cd Length: 608 Bit Score: 122.28 E-value: 7.18e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544134 59 NFAKDVLDQWtdkekAGKKPSNPAFWWINRNGEEMR-WSFEELGSLSRKFANILSEAcSLQRGDRVILILPRVPEWWLAN 137
Cdd:cd05966 53 NISYNCLDRH-----LKERGDKVAIIWEGDEPDQSRtITYRELLREVCRFANVLKSL-GVKKGDRVAIYMPMIPELVIAM 126
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544134 138 VACLRTG---TVLIPGttqLTQKDILYRLQSSKANCIITND---------VLAPAVDAVASKCENLHsKLIVSENS---- 201
Cdd:cd05966 127 LACARIGavhSVVFAG---FSAESLADRINDAQCKLVITADggyrggkviPLKEIVDEALEKCPSVE-KVLVVKRTggev 202
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544134 202 -----REGWGNlkELMKHASDSHTCVKTKHNEIMAIFFTSGTSGYPKMTAHTHSSFGLGLSVNGRFWLDLTPSDVMWNTS 276
Cdd:cd05966 203 pmtegRDLWWH--DLMAKQSPECEPEWMDSEDPLFILYTSGSTGKPKGVVHTTGGYLLYAATTFKYVFDYHPDDIYWCTA 280
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544134 277 DTGWAKSAWSSVFSPWIQGACVFThhlprFE--PT--------SILQtlsKYPITVFCSAPTVYRMLVQ---NDITSYKF 343
Cdd:cd05966 281 DIGWITGHSYIVYGPLANGATTVM-----FEgtPTypdpgrywDIVE---KHKVTIFYTAPTAIRALMKfgdEWVKKHDL 352
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 42544134 344 KSLKHCVSAGEPITPdvtEKWR---NKTG---LDIYEGYGQTETVLIC-----GnfkGMKIKPGSMGKPSPAFDVKV 409
Cdd:cd05966 353 SSLRVLGSVGEPINP---EAWMwyyEVIGkerCPIVDTWWQTETGGIMitplpG---ATPLKPGSATRPFFGIEPAI 423
|
|
| FACL_FadD13-like |
cd17631 |
fatty acyl-CoA synthetase, including FadD13; This family contains fatty acyl-CoA synthetases, ... |
74-409 |
6.71e-27 |
|
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: 111.93 E-value: 6.71e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544134 74 AGKKPSNPAFWWINRngeemRWSFEELGSLSRKFANILSEAcSLQRGDRVILILPRVPEWWLANVACLRTGTVLIPGTTQ 153
Cdd:cd17631 5 ARRHPDRTALVFGGR-----SLTYAELDERVNRLAHALRAL-GVAKGDRVAVLSKNSPEFLELLFAAARLGAVFVPLNFR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544134 154 LTQKDILYRLQSSKAnciitndvlapavdavaskcenlhsKLIVSENSRegwgnlkelmkhasdshtcvktkhneimaIF 233
Cdd:cd17631 79 LTPPEVAYILADSGA-------------------------KVLFDDLAL-----------------------------LM 104
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544134 234 FTSGTSGYPKMTAHTHSSFgLGLSVNGRFWLDLTPSDV------MWNTSDTGwaksawssVFSPWIQGACVFTHHLPRFE 307
Cdd:cd17631 105 YTSGTTGRPKGAMLTHRNL-LWNAVNALAALDLGPDDVllvvapLFHIGGLG--------VFTLPTLLRGGTVVILRKFD 175
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544134 308 PTSILQTLSKYPITVFCSAPTVYRMLVQN-DITSYKFKSLKHCVSAGEPITPDVTEKWRnKTGLDIYEGYGQTETV-LIC 385
Cdd:cd17631 176 PETVLDLIERHRVTSFFLVPTMIQALLQHpRFATTDLSSLRAVIYGGAPMPERLLRALQ-ARGVKFVQGYGMTETSpGVT 254
|
330 340
....*....|....*....|....*
gi 42544134 386 GNFKGMKI-KPGSMGKPSPAFDVKV 409
Cdd:cd17631 255 FLSPEDHRrKLGSAGRPVFFVEVRI 279
|
|
| AA-adenyl-dom |
TIGR01733 |
amino acid adenylation domain; This model represents a domain responsible for the specific ... |
96-388 |
3.39e-26 |
|
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: 109.66 E-value: 3.39e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544134 96 SFEELGSLSRKFANILSEACSLQRGDRVILILPRVPEWWLANVACLRTGTVLIPgttqLtqkDILY---RLQS----SKA 168
Cdd:TIGR01733 1 TYRELDERANRLARHLRAAGGVGPGDRVAVLLERSAELVVAILAVLKAGAAYVP----L---DPAYpaeRLAFiledAGA 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544134 169 NCIITNDVLAPAVDAVAskcenlhsKLIVSENSREGWgnlkELMKHASDSHTCVKTKHNEIMAIFFTSGTSGYPKMTAHT 248
Cdd:TIGR01733 74 RLLLTDSALASRLAGLV--------LPVILLDPLELA----ALDDAPAPPPPDAPSGPDDLAYVIYTSGSTGRPKGVVVT 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544134 249 HSSFGLGLSVNGRFWlDLTPSDVMWNTSDTGWAKSAWsSVFSPWIQGACVF--THHLPRFEPTSILQTLSKYPITVFCSA 326
Cdd:TIGR01733 142 HRSLVNLLAWLARRY-GLDPDDRVLQFASLSFDASVE-EIFGALLAGATLVvpPEDEERDDAALLAALIAEHPVTVLNLT 219
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 42544134 327 PTVYRMLVQNDITSykFKSLKHCVSAGEPITPDVTEKWRNKTG-LDIYEGYGQTETVLICGNF 388
Cdd:TIGR01733 220 PSLLALLAAALPPA--LASLRLVILGGEALTPALVDRWRARGPgARLINLYGPTETTVWSTAT 280
|
|
| PrpE |
cd05967 |
Propionyl-CoA synthetase (PrpE); EC 6.2.1.17: propanoate:CoA ligase (AMP-forming) or ... |
90-409 |
1.24e-25 |
|
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: 109.71 E-value: 1.24e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544134 90 GEEMRWSFEELGSLSRKFANILsEACSLQRGDRVILILPRVPEWWLANVACLRTGTV--LIPG---TTQLTQkdilyRLQ 164
Cdd:cd05967 78 GTERTYTYAELLDEVSRLAGVL-RKLGVVKGDRVIIYMPMIPEAAIAMLACARIGAIhsVVFGgfaAKELAS-----RID 151
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544134 165 SSKANCIITNDV---------LAPAVD-AVASKCENLHSKLIVSENSRE-------GWGNLKELMKHASdSHTCVKTKHN 227
Cdd:cd05967 152 DAKPKLIVTASCgiepgkvvpYKPLLDkALELSGHKPHHVLVLNRPQVPadltkpgRDLDWSELLAKAE-PVDCVPVAAT 230
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544134 228 EIMAIFFTSGTSGYPKMTAHTHSSFGLGLSVNGRFWLDLTPSDVMWNTSDTGWAKSAWSSVFSPWIQGA-CVFTHHLPRF 306
Cdd:cd05967 231 DPLYILYTSGTTGKPKGVVRDNGGHAVALNWSMRNIYGIKPGDVWWAASDVGWVVGHSYIVYGPLLHGAtTVLYEGKPVG 310
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544134 307 --EPTSILQTLSKYPITVFCSAPTVYRMLVQND-----ITSYKFKSLKHCVSAGEPITPDVTEKWRNKTGLDIYEGYGQT 379
Cdd:cd05967 311 tpDPGAFWRVIEKYQVNALFTAPTAIRAIRKEDpdgkyIKKYDLSSLRTLFLAGERLDPPTLEWAENTLGVPVIDHWWQT 390
|
330 340 350
....*....|....*....|....*....|....
gi 42544134 380 ET----VLICGNFKGMKIKPGSMGKPSPAFDVKV 409
Cdd:cd05967 391 ETgwpiTANPVGLEPLPIKAGSPGKPVPGYQVQV 424
|
|
| PRK08314 |
PRK08314 |
long-chain-fatty-acid--CoA ligase; Validated |
78-382 |
1.86e-25 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236235 [Multi-domain] Cd Length: 546 Bit Score: 108.89 E-value: 1.86e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544134 78 PSNPAFWWINRngeemRWSFEELGSLSRKFANILSEACSLQRGDRVILILPRVPEWWLANVACLRTGTVLIPGTTQLTQK 157
Cdd:PRK08314 24 PDKTAIVFYGR-----AISYRELLEEAERLAGYLQQECGVRKGDRVLLYMQNSPQFVIAYYAILRANAVVVPVNPMNREE 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544134 158 DILYRLQSSKANCIITNDVLAPAV------------------DAVASKCE-----NLHSKLIVSENSREGWGNLKELMK- 213
Cdd:PRK08314 99 ELAHYVTDSGARVAIVGSELAPKVapavgnlrlrhvivaqysDYLPAEPEiavpaWLRAEPPLQALAPGGVVAWKEALAa 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544134 214 -HASDSHTcvkTKHNEIMAIFFTSGTSGYPKMTAHTHSSFgLGLSVNGRFWLDLTPSDVMWNTSD----TGWAKSAWSSV 288
Cdd:PRK08314 179 gLAPPPHT---AGPDDLAVLPYTSGTTGVPKGCMHTHRTV-MANAVGSVLWSNSTPESVVLAVLPlfhvTGMVHSMNAPI 254
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544134 289 FSpwiqGACVFThhLPRFEPTSILQTLSKYPITVFCSAPTvyrMLV----QNDITSYKFKSLKHCVSAGEPITPDVTEKW 364
Cdd:PRK08314 255 YA----GATVVL--MPRWDREAAARLIERYRVTHWTNIPT---MVVdflaSPGLAERDLSSLRYIGGGGAAMPEAVAERL 325
|
330
....*....|....*...
gi 42544134 365 RNKTGLDIYEGYGQTETV 382
Cdd:PRK08314 326 KELTGLDYVEGYGLTETM 343
|
|
| prpE |
PRK10524 |
propionyl-CoA synthetase; Provisional |
76-409 |
6.53e-24 |
|
propionyl-CoA synthetase; Provisional
Pssm-ID: 182517 [Multi-domain] Cd Length: 629 Bit Score: 104.26 E-value: 6.53e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544134 76 KKPSNPAFWWIN-RNGEEMRWSFEELGSLSRKFANILsEACSLQRGDRVILILPRVPEWWLANVACLRTG---TVLIPG- 150
Cdd:PRK10524 65 KRPEQLALIAVStETDEERTYTFRQLHDEVNRMAAML-RSLGVQRGDRVLIYMPMIAEAAFAMLACARIGaihSVVFGGf 143
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544134 151 -TTQLTQkdilyRLQSSKANCIITND-------VLA--PAVDAVASKCENLHSK-LIVS-----ENSREG----WGNLKE 210
Cdd:PRK10524 144 aSHSLAA-----RIDDAKPVLIVSADagsrggkVVPykPLLDEAIALAQHKPRHvLLVDrglapMARVAGrdvdYATLRA 218
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544134 211 lmKHASDSHTCVKTKHNEIMAIFFTSGTSGYPKMTAHTHSSFGLGLSVNGRFWLDLTPSDVMWNTSDTGWAKSAWSSVFS 290
Cdd:PRK10524 219 --QHLGARVPVEWLESNEPSYILYTSGTTGKPKGVQRDTGGYAVALATSMDTIFGGKAGETFFCASDIGWVVGHSYIVYA 296
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544134 291 PWIQG-ACVFTHHLP-RFEPTSILQTLSKYPITVFCSAPTVYRMLVQND---ITSYKFKSLKHCVSAGEPITpDVTEKWR 365
Cdd:PRK10524 297 PLLAGmATIMYEGLPtRPDAGIWWRIVEKYKVNRMFSAPTAIRVLKKQDpalLRKHDLSSLRALFLAGEPLD-EPTASWI 375
|
330 340 350 360
....*....|....*....|....*....|....*....|....*....
gi 42544134 366 NKT-GLDIYEGYGQTET----VLICGNFKGMKIKPGSMGKPSPAFDVKV 409
Cdd:PRK10524 376 SEAlGVPVIDNYWQTETgwpiLAIARGVEDRPTRLGSPGVPMYGYNVKL 424
|
|
| PRK06710 |
PRK06710 |
long-chain-fatty-acid--CoA ligase; Validated |
96-411 |
1.53e-23 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 180666 [Multi-domain] Cd Length: 563 Bit Score: 103.19 E-value: 1.53e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544134 96 SFEELGSLSRKFANILsEACSLQRGDRVILILPRVPEWWLANVACLRTGTVLIPGTTQLTQKDILYRLQSSKANCIITND 175
Cdd:PRK06710 51 TFSVFHDKVKRFANYL-QKLGVEKGDRVAIMLPNCPQAVIGYYGTLLAGGIVVQTNPLYTERELEYQLHDSGAKVILCLD 129
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544134 176 VLAPAVDAV--ASKCENL-----------------------HSKLIVSENSREG---WGNLKELMKHASDShTCvkTKHN 227
Cdd:PRK06710 130 LVFPRVTNVqsATKIEHVivtriadflpfpknllypfvqkkQSNLVVKVSESETihlWNSVEKEVNTGVEV-PC--DPEN 206
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544134 228 EIMAIFFTSGTSGYPKMTAHTHSSFgLGLSVNGRFWLD--LTPSDVMWNTSDTGWAKSAWSSVFSPWIQGACVFThhLPR 305
Cdd:PRK06710 207 DLALLQYTGGTTGFPKGVMLTHKNL-VSNTLMGVQWLYncKEGEEVVLGVLPFFHVYGMTAVMNLSIMQGYKMVL--IPK 283
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544134 306 FEPTSILQTLSKYPITVFCSAPTVYRMLVQNDI-TSYKFKSLKHCVSAGEPITPDVTEKWRNKTGLDIYEGYGQTETVLI 384
Cdd:PRK06710 284 FDMKMVFEAIKKHKVTLFPGAPTIYIALLNSPLlKEYDISSIRACISGSAPLPVEVQEKFETVTGGKLVEGYGLTESSPV 363
|
330 340
....*....|....*....|....*...
gi 42544134 385 C-GNFKGMKIKPGSMGKPSPAFDVKVCT 411
Cdd:PRK06710 364 ThSNFLWEKRVPGSIGVPWPDTEAMIMS 391
|
|
| LC_FACS_like |
cd05935 |
Putative long-chain fatty acid CoA ligase; The members of this family are putative long-chain ... |
96-382 |
1.97e-23 |
|
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: 101.79 E-value: 1.97e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544134 96 SFEELGSLSRKFANILSeACSLQRGDRVILILPRVPEWWLANVACLRTGTVLIPGTTQLTQKDILYRLQSSKANCIITnd 175
Cdd:cd05935 3 TYLELLEVVKKLASFLS-NKGVRKGDRVGICLQNSPQYVIAYFAIWRANAVVVPINPMLKERELEYILNDSGAKVAVV-- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544134 176 vlapavdavaskcenlHSKLivsensregwgnlkelmkhasdshtcvktkhNEIMAIFFTSGTSGYPKMTAHTHSSFgLG 255
Cdd:cd05935 80 ----------------GSEL-------------------------------DDLALIPYTSGTTGLPKGCMHTHFSA-AA 111
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544134 256 LSVNGRFWLDLTPSDVMWNTSDTGWAKSAWSSVFSPWIQGACVFThhLPRFEPTSILQTLSKYPITVFCSAPTVYRMLVQ 335
Cdd:cd05935 112 NALQSAVWTGLTPSDVILACLPLFHVTGFVGSLNTAVYVGGTYVL--MARWDRETALELIEKYKVTFWTNIPTMLVDLLA 189
|
250 260 270 280
....*....|....*....|....*....|....*....|....*...
gi 42544134 336 N-DITSYKFKSLKHCVSAGEPITPDVTEKWRNKTGLDIYEGYGQTETV 382
Cdd:cd05935 190 TpEFKTRDLSSLKVLTGGGAPMPPAVAEKLLKLTGLRFVEGYGLTETM 237
|
|
| FAA1 |
COG1022 |
Long-chain acyl-CoA synthetase (AMP-forming) [Lipid transport and metabolism]; |
74-409 |
8.61e-22 |
|
Long-chain acyl-CoA synthetase (AMP-forming) [Lipid transport and metabolism];
Pssm-ID: 440645 [Multi-domain] Cd Length: 603 Bit Score: 97.86 E-value: 8.61e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544134 74 AGKKPSNPAFWWiNRNGEEMRWSFEELGSLSRKFANILsEACSLQRGDRVILILPRVPEWWLANVACLRTGTVLIPGTTQ 153
Cdd:COG1022 21 AARFPDRVALRE-KEDGIWQSLTWAEFAERVRALAAGL-LALGVKPGDRVAILSDNRPEWVIADLAILAAGAVTVPIYPT 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544134 154 LTQKDILYRLQSSKANCIIT-NDVLAPAVDAVASKCENLhsKLIVSENSREGWG-----NLKELMKHASDSHT------- 220
Cdd:COG1022 99 SSAEEVAYILNDSGAKVLFVeDQEQLDKLLEVRDELPSL--RHIVVLDPRGLRDdprllSLDELLALGREVADpaelear 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544134 221 CVKTKHNEIMAIFFTSGTSGYPKMTAHTHSSFgLGLSVNGRFWLDLTPSDV------MWNTSDTGWaksawsSVFSpWIQ 294
Cdd:COG1022 177 RAAVKPDDLATIIYTSGTTGRPKGVMLTHRNL-LSNARALLERLPLGPGDRtlsflpLAHVFERTV------SYYA-LAA 248
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544134 295 GACVftHHLPRfePTSILQTLSKYPITVFCSAPTVYRMlVQNDITS---------------------------------- 340
Cdd:COG1022 249 GATV--AFAES--PDTLAEDLREVKPTFMLAVPRVWEK-VYAGIQAkaeeagglkrklfrwalavgrryararlagksps 323
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544134 341 --YKFK------------------SLKHCVSAGEPITPDVTEKWRNkTGLDIYEGYGQTET-VLICGNFKGmKIKPGSMG 399
Cdd:COG1022 324 llLRLKhaladklvfsklrealggRLRFAVSGGAALGPELARFFRA-LGIPVLEGYGLTETsPVITVNRPG-DNRIGTVG 401
|
410
....*....|
gi 42544134 400 KPSPAFDVKV 409
Cdd:COG1022 402 PPLPGVEVKI 411
|
|
| A_NRPS |
cd05930 |
The adenylation domain of nonribosomal peptide synthetases (NRPS); The adenylation (A) domain ... |
78-381 |
3.21e-21 |
|
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: 95.29 E-value: 3.21e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544134 78 PSNPAFWWINRngeemRWSFEELGSLSRKFANILSEACsLQRGDRVILILPRVPEWWLANVACLRTGTVLIPGTTQLTQK 157
Cdd:cd05930 1 PDAVAVVDGDQ-----SLTYAELDARANRLARYLRERG-VGPGDLVAVLLERSLEMVVAILAVLKAGAAYVPLDPSYPAE 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544134 158 DILYRLQSSKANCIITNdvlapavdavaskcenlhsklivsensregwgnlkelmkhasdshtcvktkHNEIMAIFFTSG 237
Cdd:cd05930 75 RLAYILEDSGAKLVLTD---------------------------------------------------PDDLAYVIYTSG 103
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544134 238 TSGYPKMTAHTHSSFglglsVNGRFW----LDLTPSDVMWNTSDTGWAKSAWsSVFSPWIQGACVftHHLP---RFEPTS 310
Cdd:cd05930 104 STGKPKGVMVEHRGL-----VNLLLWmqeaYPLTPGDRVLQFTSFSFDVSVW-EIFGALLAGATL--VVLPeevRKDPEA 175
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 42544134 311 ILQTLSKYPITVFCSAPTVYRMLVQNDITSyKFKSLKHCVSAGEPITPDVTEKWR-NKTGLDIYEGYGQTET 381
Cdd:cd05930 176 LADLLAEEGITVLHLTPSLLRLLLQELELA-ALPSLRLVLVGGEALPPDLVRRWReLLPGARLVNLYGPTEA 246
|
|
| PRK00174 |
PRK00174 |
acetyl-CoA synthetase; Provisional |
106-409 |
1.39e-20 |
|
acetyl-CoA synthetase; Provisional
Pssm-ID: 234677 [Multi-domain] Cd Length: 637 Bit Score: 94.44 E-value: 1.39e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544134 106 KFANILSEAcSLQRGDRVILILPRVPEWWLANVACLRTG---TVLIPGttqLTQKDILYRLQSSKANCIITND------- 175
Cdd:PRK00174 110 RFANALKSL-GVKKGDRVAIYMPMIPEAAVAMLACARIGavhSVVFGG---FSAEALADRIIDAGAKLVITADegvrggk 185
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544134 176 --VLAPAVDAVASKCENLHSKLIVS--------ENSREGWGNlkELMKHASDSHTCVKTKHNEIMAIFFTSGTSGYPKMT 245
Cdd:PRK00174 186 piPLKANVDEALANCPSVEKVIVVRrtggdvdwVEGRDLWWH--ELVAGASDECEPEPMDAEDPLFILYTSGSTGKPKGV 263
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544134 246 AHTHSSFGLGLSVNGRFWLDLTPSDVMWNTSDTGWAKSAWSSVFSPWIQGACVFTHH-LPRF-EPTSILQTLSKYPITVF 323
Cdd:PRK00174 264 LHTTGGYLVYAAMTMKYVFDYKDGDVYWCTADVGWVTGHSYIVYGPLANGATTLMFEgVPNYpDPGRFWEVIDKHKVTIF 343
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544134 324 CSAPTVYRMLVQ---NDITSYKFKSLKHCVSAGEPITPdvtEKWR---NKTGLD---IYEGYGQTET--VLIC---Gnfk 389
Cdd:PRK00174 344 YTAPTAIRALMKegdEHPKKYDLSSLRLLGSVGEPINP---EAWEwyyKVVGGErcpIVDTWWQTETggIMITplpG--- 417
|
330 340
....*....|....*....|
gi 42544134 390 GMKIKPGSMGKPSPAFDVKV 409
Cdd:PRK00174 418 ATPLKPGSATRPLPGIQPAV 437
|
|
| PRK08316 |
PRK08316 |
acyl-CoA synthetase; Validated |
91-401 |
1.44e-20 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 181381 [Multi-domain] Cd Length: 523 Bit Score: 93.84 E-value: 1.44e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544134 91 EEMRWSFEELGSLSRKFANILSEAcSLQRGDRVILILPRVPEWWLANVACLRTGTVLIPGTTQLTQKDILYRLQSSKANC 170
Cdd:PRK08316 33 GDRSWTYAELDAAVNRVAAALLDL-GLKKGDRVAALGHNSDAYALLWLACARAGAVHVPVNFMLTGEELAYILDHSGARA 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544134 171 IITNDVLAPAVDAVASKCENLHSKLIVSENSRE---GWGNLKELMKHASDSHTCVKTKHNEIMAIFFTSGTSGYPKMTAH 247
Cdd:PRK08316 112 FLVDPALAPTAEAALALLPVDTLILSLVLGGREapgGWLDFADWAEAGSVAEPDVELADDDLAQILYTSGTESLPKGAML 191
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544134 248 THSSFgLGLSVNGRFWLDLTPSDVMWNtsdtgwA----KSAWSSVF-SPWIQ-GACvfTHHLPRFEPTSILQTLSKYPIT 321
Cdd:PRK08316 192 THRAL-IAEYVSCIVAGDMSADDIPLH------AlplyHCAQLDVFlGPYLYvGAT--NVILDAPDPELILRTIEAERIT 262
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544134 322 VFCSAPTVY-RMLVQNDITSYKFKSLKHCVSaGEPITP-DVTEKWRNK-TGLDIYEGYGQTE-----TVLicgNFKGMKI 393
Cdd:PRK08316 263 SFFAPPTVWiSLLRHPDFDTRDLSSLRKGYY-GASIMPvEVLKELRERlPGLRFYNCYGQTEiaplaTVL---GPEEHLR 338
|
....*...
gi 42544134 394 KPGSMGKP 401
Cdd:PRK08316 339 RPGSAGRP 346
|
|
| PRK07514 |
PRK07514 |
malonyl-CoA synthase; Validated |
94-409 |
4.08e-20 |
|
malonyl-CoA synthase; Validated
Pssm-ID: 181011 [Multi-domain] Cd Length: 504 Bit Score: 92.63 E-value: 4.08e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544134 94 RWSFEELGSLSRKFANILSeACSLQRGDRVILILPRVPEWWLANVACLRTGTVLIPGTTQLTQKDILYRLQSSKANCIIT 173
Cdd:PRK07514 28 RYTYGDLDAASARLANLLV-ALGVKPGDRVAVQVEKSPEALALYLATLRAGAVFLPLNTAYTLAELDYFIGDAEPALVVC 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544134 174 NDVLAPAVDAVASKCENLHskliVSENSREGWGNLKELMKHASDSHTCVKTKHNEIMAIFFTSGTSGYPK--MTAHTH-S 250
Cdd:PRK07514 107 DPANFAWLSKIAAAAGAPH----VETLDADGTGSLLEAAAAAPDDFETVPRGADDLAAILYTSGTTGRSKgaMLSHGNlL 182
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544134 251 SFGLGLSVNGRFwldlTPSDVMwntsdtgwaksawssvfspwIQGACVFTHH------------------LPRFEPTSIL 312
Cdd:PRK07514 183 SNALTLVDYWRF----TPDDVL--------------------IHALPIFHTHglfvatnvallagasmifLPKFDPDAVL 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544134 313 QTLSKypITVFCSAPTVY-RMLVQNDITSYKFKSLKHCVSAGEPITPDVTEKWRNKTGLDIYEGYGQTETVLICGN-FKG 390
Cdd:PRK07514 239 ALMPR--ATVMMGVPTFYtRLLQEPRLTREAAAHMRLFISGSAPLLAETHREFQERTGHAILERYGMTETNMNTSNpYDG 316
|
330
....*....|....*....
gi 42544134 391 MKIkPGSMGKPSPAFDVKV 409
Cdd:PRK07514 317 ERR-AGTVGFPLPGVSLRV 334
|
|
| AAS_C |
cd05909 |
C-terminal domain of the acyl-acyl carrier protein synthetase (also called ... |
221-409 |
9.43e-20 |
|
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: 91.24 E-value: 9.43e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544134 221 CVKTKHNEIMAIFFTSGTSGYPKMTAHTHSSFGLGL-SVNGRFwlDLTPSDVMWNTSDTGWAKSAWSSVFSPWIQGACVF 299
Cdd:cd05909 141 VAPVQPDDPAVILFTSGSEGLPKGVVLSHKNLLANVeQITAIF--DPNPEDVVFGALPFFHSFGLTGCLWLPLLSGIKVV 218
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544134 300 THHLPrFEPTSILQTLSKYPITVFCSAPTVYRMLVQNdITSYKFKSLKHCVSAGEPITPDVTEKWRNKTGLDIYEGYGQT 379
Cdd:cd05909 219 FHPNP-LDYKKIPELIYDKKATILLGTPTFLRGYARA-AHPEDFSSLRLVVAGAEKLKDTLRQEFQEKFGIRILEGYGTT 296
|
170 180 190
....*....|....*....|....*....|.
gi 42544134 380 ETV-LICGNFKGMKIKPGSMGKPSPAFDVKV 409
Cdd:cd05909 297 ECSpVISVNTPQSPNKEGTVGRPLPGMEVKI 327
|
|
| 4CL |
cd05904 |
4-Coumarate-CoA Ligase (4CL); 4-Coumarate:coenzyme A ligase is a key enzyme in the ... |
72-409 |
1.64e-19 |
|
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: 90.76 E-value: 1.64e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544134 72 EKAGKKPSNPAFwwIN-RNGEEMrwSFEELGSLSRKFANILSeACSLQRGDRVILILPRVPEWWLANVACLRTGTVLIPG 150
Cdd:cd05904 13 LFASAHPSRPAL--IDaATGRAL--TYAELERRVRRLAAGLA-KRGGRKGDVVLLLSPNSIEFPVAFLAVLSLGAVVTTA 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544134 151 TTQLTQKDILYRLQSSKANCIITndvlapaVDAVASKCENLHSKLIVSENSR-EGWGNLKELMKHASDSHTCVKTKHNEI 229
Cdd:cd05904 88 NPLSTPAEIAKQVKDSGAKLAFT-------TAELAEKLASLALPVVLLDSAEfDSLSFSDLLFEADEAEPPVVVIKQDDV 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544134 230 MAIFFTSGTSGYPKMTAHTHSSF-GLGLSVNGRFWLDLTPSDVMWntsdtgwaksawssVFSPW--IQGACVFTHH---- 302
Cdd:cd05904 161 AALLYSSGTTGRSKGVMLTHRNLiAMVAQFVAGEGSNSDSEDVFL--------------CVLPMfhIYGLSSFALGllrl 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544134 303 ------LPRFEPTSILQTLSKYPITVFCSAPTVYRMLVQNDIT-SYKFKSLKHCVSAGEPITPDVTEKWRNK-TGLDIYE 374
Cdd:cd05904 227 gatvvvMPRFDLEELLAAIERYKVTHLPVVPPIVLALVKSPIVdKYDLSSLRQIMSGAAPLGKELIEAFRAKfPNVDLGQ 306
|
330 340 350
....*....|....*....|....*....|....*...
gi 42544134 375 GYGQTET---VLICGNFKGMKIKPGSMGKPSPAFDVKV 409
Cdd:cd05904 307 GYGMTEStgvVAMCFAPEKDRAKYGSVGRLVPNVEAKI 344
|
|
| PLN02654 |
PLN02654 |
acetate-CoA ligase |
83-381 |
2.17e-18 |
|
acetate-CoA ligase
Pssm-ID: 215353 [Multi-domain] Cd Length: 666 Bit Score: 87.65 E-value: 2.17e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544134 83 FWWINRNGEEMRWSFEELGSLSRKFANILsEACSLQRGDRVILILPRVPEWWLANVACLRTGTVLIPGTTQLTQKDILYR 162
Cdd:PLN02654 109 YWEGNEPGFDASLTYSELLDRVCQLANYL-KDVGVKKGDAVVIYLPMLMELPIAMLACARIGAVHSVVFAGFSAESLAQR 187
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544134 163 LQSSKANCIIT-NDV--------LAPAVDAVASKCENLHSKL---IVSENS----REG--WGNLKELMKHasDSHTCVKT 224
Cdd:PLN02654 188 IVDCKPKVVITcNAVkrgpktinLKDIVDAALDESAKNGVSVgicLTYENQlamkREDtkWQEGRDVWWQ--DVVPNYPT 265
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544134 225 K-------HNEIMAIFFTSGTSGYPKMTAHTHSSFGLGLSVNGRFWLDLTPSDVMWNTSDTGWAKSAWSSVFSPWIQGAC 297
Cdd:PLN02654 266 KcevewvdAEDPLFLLYTSGSTGKPKGVLHTTGGYMVYTATTFKYAFDYKPTDVYWCTADCGWITGHSYVTYGPMLNGAT 345
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544134 298 VFTHH-LPRF-EPTSILQTLSKYPITVFCSAPTVYRMLVQND---ITSYKFKSLKHCVSAGEPITPDVTEKWRNKTG--- 369
Cdd:PLN02654 346 VLVFEgAPNYpDSGRCWDIVDKYKVTIFYTAPTLVRSLMRDGdeyVTRHSRKSLRVLGSVGEPINPSAWRWFFNVVGdsr 425
|
330
....*....|..
gi 42544134 370 LDIYEGYGQTET 381
Cdd:PLN02654 426 CPISDTWWQTET 437
|
|
| VL_LC_FACS_like |
cd05907 |
Long-chain fatty acid CoA synthetases and Bubblegum-like very long-chain fatty acid CoA ... |
95-409 |
2.53e-18 |
|
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: 86.88 E-value: 2.53e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544134 95 WSFEELGSLSRKFANILsEACSLQRGDRVILILPRVPEWWLANVACLRTGTVLIPGTTQLTQKDILYRLQSSKAnciitn 174
Cdd:cd05907 6 ITWAEFAEEVRALAKGL-IALGVEPGDRVAILSRNRPEWTIADLAILAIGAVPVPIYPTSSAEQIAYILNDSEA------ 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544134 175 dvlapavdavaskcenlhsKLIVSENSregwgnlkelmkhasdSHTCVktkhneimaIFFTSGTSGYPKMTAHTHSSFgl 254
Cdd:cd05907 79 -------------------KALFVEDP----------------DDLAT---------IIYTSGTTGRPKGVMLSHRNI-- 112
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544134 255 glsvngrfwldltpsdvMWN--TSDTGWAKSAWSSVFS----------------PWIQGACVFthHLPRFEptSILQTLS 316
Cdd:cd05907 113 -----------------LSNalALAERLPATEGDRHLSflplahvferraglyvPLLAGARIY--FASSAE--TLLDDLS 171
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544134 317 KYPITVFCSAPTVYRML----VQNDITSYK--------FKSLKHCVSAGEPITPDVTEKWRnKTGLDIYEGYGQTETV-L 383
Cdd:cd05907 172 EVRPTVFLAVPRVWEKVyaaiKVKAVPGLKrklfdlavGGRLRFAASGGAPLPAELLHFFR-ALGIPVYEGYGLTETSaV 250
|
330 340
....*....|....*....|....*.
gi 42544134 384 ICGNFKGmKIKPGSMGKPSPAFDVKV 409
Cdd:cd05907 251 VTLNPPG-DNRIGTVGKPLPGVEVRI 275
|
|
| MCS |
cd05941 |
Malonyl-CoA synthetase (MCS); MCS catalyzes the formation of malonyl-CoA in a two-step ... |
94-409 |
4.60e-18 |
|
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: 85.80 E-value: 4.60e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544134 94 RWSFEELGSLSRKFANILSEACSLQRGDRVILILPRVPEWWLANVACLRTGTVLIPGTTQLTQKDILYRLQSSKANCiit 173
Cdd:cd05941 11 SITYADLVARAARLANRLLALGKDLRGDRVAFLAPPSAEYVVAQLAIWRAGGVAVPLNPSYPLAELEYVITDSEPSL--- 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544134 174 ndVLAPAVdavaskcenlhsklivsensregwgnlkelmkhasdshtcvktkhneimaIFFTSGTSGYPKMTAHTHSSFG 253
Cdd:cd05941 88 --VLDPAL--------------------------------------------------ILYTSGTTGRPKGVVLTHANLA 115
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544134 254 LGLSVNGRFWlDLTPSDV------------MWNtsdtgwaksawsSVFSPWIQGACVftHHLPRFEPTSILQTLSKYPIT 321
Cdd:cd05941 116 ANVRALVDAW-RWTEDDVllhvlplhhvhgLVN------------ALLCPLFAGASV--EFLPKFDPKEVAISRLMPSIT 180
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544134 322 VFCSAPTVYRMLVQ---------NDITSYKFKSLKHCVSAGEPITPDVTEKWRNKTGLDIYEGYGQTETVLICGN-FKGm 391
Cdd:cd05941 181 VFMGVPTIYTRLLQyyeahftdpQFARAAAAERLRLMVSGSAALPVPTLEEWEAITGHTLLERYGMTEIGMALSNpLDG- 259
|
330
....*....|....*...
gi 42544134 392 KIKPGSMGKPSPAFDVKV 409
Cdd:cd05941 260 ERRPGTVGMPLPGVQARI 277
|
|
| PRK06178 |
PRK06178 |
acyl-CoA synthetase; Validated |
63-410 |
2.07e-17 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 235724 [Multi-domain] Cd Length: 567 Bit Score: 84.32 E-value: 2.07e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544134 63 DVLDQWtdkekAGKKPSNPAFWWINRngeemRWSFEELGSLSRKFANILsEACSLQRGDRVILILPRVPEWWLANVACLR 142
Cdd:PRK06178 37 EYLRAW-----ARERPQRPAIIFYGH-----VITYAELDELSDRFAALL-RQRGVGAGDRVAVFLPNCPQFHIVFFGILK 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544134 143 TGTVLIPGTTQLTQKDILYRLQSSKANCIITNDVLAPAVDAVASKCENLH------SKLIVSENSR-------------E 203
Cdd:PRK06178 106 LGAVHVPVSPLFREHELSYELNDAGAEVLLALDQLAPVVEQVRAETSLRHvivtslADVLPAEPTLplpdslraprlaaA 185
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544134 204 GWGNLKELMKHASDSHTCVKTKHNEIMAIFFTSGTSGYPKMTAHTHSSFGLGLSVNGRFWLDLTPSDVMWNTSDTGWAKS 283
Cdd:PRK06178 186 GAIDLLPALRACTAPVPLPPPALDALAALNYTGGTTGMPKGCEHTQRDMVYTAAAAYAVAVVGGEDSVFLSFLPEFWIAG 265
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544134 284 AWSSVFSPWIQGACVFThhLPRFEPTSILQTLSKYPITVfcsapTVyrMLVQN--------DITSYKFKSLKH--CVSAG 353
Cdd:PRK06178 266 ENFGLLFPLFSGATLVL--LARWDAVAFMAAVERYRVTR-----TV--MLVDNavelmdhpRFAEYDLSSLRQvrVVSFV 336
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 42544134 354 EPITPDVTEKWRNKTGLDIYEG-YGQTETvLICGNF-KGM-------KIKPGSMGKPSPAFDVKVC 410
Cdd:PRK06178 337 KKLNPDYRQRWRALTGSVLAEAaWGMTET-HTCDTFtAGFqdddfdlLSQPVFVGLPVPGTEFKIC 401
|
|
| PRK06060 |
PRK06060 |
p-hydroxybenzoic acid--AMP ligase FadD22; |
117-409 |
2.19e-17 |
|
p-hydroxybenzoic acid--AMP ligase FadD22;
Pssm-ID: 180374 [Multi-domain] Cd Length: 705 Bit Score: 84.70 E-value: 2.19e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544134 117 LQRGDRVILILPRVPEWWLANVACLRTGTVLIPGTTQLTQKDILYRLQSSKANCIITNDVLapavdavaskCENLHSKLI 196
Cdd:PRK06060 52 LSSGDRVLLCLPDSPDLVQLLLACLARGVMAFLANPELHRDDHALAARNTEPALVVTSDAL----------RDRFQPSRV 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544134 197 V------SENSREGWGNLKELMKHASDSHTcvktkhneimaifFTSGTSGYPKMTAHTHSSFGLGLSVNGRFWLDLTPSD 270
Cdd:PRK06060 122 AeaaelmSEAARVAPGGYEPMGGDALAYAT-------------YTSGTTGPPKAAIHRHADPLTFVDAMCRKALRLTPED 188
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544134 271 VMWNTSDTGWAKSAWSSVFSPWIQGACVFTHHLP-RFEPTSILQTlsKYPITVFCSAPTVYRMLVqNDITSYKFKSLKHC 349
Cdd:PRK06060 189 TGLCSARMYFAYGLGNSVWFPLATGGSAVINSAPvTPEAAAILSA--RFGPSVLYGVPNFFARVI-DSCSPDSFRSLRCV 265
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 42544134 350 VSAGEPITPDVTEKWRN-KTGLDIYEGYGQTEtvlICGNFKGMKI---KPGSMGKPSPAFDVKV 409
Cdd:PRK06060 266 VSAGEALELGLAERLMEfFGGIPILDGIGSTE---VGQTFVSNRVdewRLGTLGRVLPPYEIRV 326
|
|
| FACL_DitJ_like |
cd05934 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
94-409 |
2.62e-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. Members of this family include DitJ from Pseudomonas and similar proteins.
Pssm-ID: 341257 [Multi-domain] Cd Length: 422 Bit Score: 83.49 E-value: 2.62e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544134 94 RWSFEELGSLSRKFANILSeACSLQRGDRVILILPRVPEWWLANVACLRTGTVLIPGTTQLTQKDILYRLQSSKANCIIT 173
Cdd:cd05934 3 RWTYAELLRESARIAAALA-ALGIRPGDRVALMLDNCPEFLFAWFALAKLGAVLVPINTALRGDELAYIIDHSGAQLVVV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544134 174 ndvlAPAvdavaskcenlhsklivsensregwgnlkelmkhasdshtcvktkhneimAIFFTSGTSGYPKMTAHTHSSFG 253
Cdd:cd05934 82 ----DPA--------------------------------------------------SILYTSGTTGPPKGVVITHANLT 107
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544134 254 LGLSVNGRfWLDLTPSDVMW--------NTSDTGWAkSAWSSvfspwiQGACVFthhLPRFEPTSILQTLSKYPITVFCS 325
Cdd:cd05934 108 FAGYYSAR-RFGLGEDDVYLtvlplfhiNAQAVSVL-AALSV------GATLVL---LPRFSASRFWSDVRRYGATVTNY 176
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544134 326 APTVYRMLVQNDItsyKFKSLKHCVSA--GEPITPDVTEKWRNKTGLDIYEGYGQTETVLICGNFKGMKIKPGSMGKPSP 403
Cdd:cd05934 177 LGAMLSYLLAQPP---SPDDRAHRLRAayGAPNPPELHEEFEERFGVRLLEGYGMTETIVGVIGPRDEPRRPGSIGRPAP 253
|
....*.
gi 42544134 404 AFDVKV 409
Cdd:cd05934 254 GYEVRI 259
|
|
| PRK06155 |
PRK06155 |
crotonobetaine/carnitine-CoA ligase; Provisional |
92-409 |
2.09e-16 |
|
crotonobetaine/carnitine-CoA ligase; Provisional
Pssm-ID: 235719 [Multi-domain] Cd Length: 542 Bit Score: 81.34 E-value: 2.09e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544134 92 EMRWSFEELGSLSRKFANILSEAcSLQRGDRVILILPRVPEWWLANVACLRTGTVLIPGTTQLTQKDILYRLQSSKANCI 171
Cdd:PRK06155 44 GTRWTYAEAARAAAAAAHALAAA-GVKRGDRVALMCGNRIEFLDVFLGCAWLGAIAVPINTALRGPQLEHILRNSGARLL 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544134 172 ITNDVLAPAVDAVASKCENLHSKLIVSENSRE----GWGNLKelMKHASDSHTCVKTKHNEIMAIFFTSGTSGYPKMTAH 247
Cdd:PRK06155 123 VVEAALLAALEAADPGDLPLPAVWLLDAPASVsvpaGWSTAP--LPPLDAPAPAAAVQPGDTAAILYTSGTTGPSKGVCC 200
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544134 248 THSSFglglsvngrFW--------LDLTPSDVMWNTSDTgWAKSAWSSVFSPWIQGAcvfTHHL-PRFEPTSILQTLSKY 318
Cdd:PRK06155 201 PHAQF---------YWwgrnsaedLEIGADDVLYTTLPL-FHTNALNAFFQALLAGA---TYVLePRFSASGFWPAVRRH 267
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544134 319 PITVFCSAPTVYRMLVQNDIT-SYKFKSLKHCVSAGEPitPDVTEKWRNKTGLDIYEGYGQTETVLICGNFKGMKiKPGS 397
Cdd:PRK06155 268 GATVTYLLGAMVSILLSQPAReSDRAHRVRVALGPGVP--AALHAAFRERFGVDLLDGYGSTETNFVIAVTHGSQ-RPGS 344
|
330
....*....|..
gi 42544134 398 MGKPSPAFDVKV 409
Cdd:PRK06155 345 MGRLAPGFEARV 356
|
|
| PRK07786 |
PRK07786 |
long-chain-fatty-acid--CoA ligase; Validated |
77-409 |
2.22e-16 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 169098 [Multi-domain] Cd Length: 542 Bit Score: 81.36 E-value: 2.22e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544134 77 KPSNPAFWWInrnGEEMRWSfeELGSLSRKFANILSEAcSLQRGDRVILILPRVPEWWLANVACLRTGTVLIPGTTQLTQ 156
Cdd:PRK07786 30 QPDAPALRFL---GNTTTWR--ELDDRVAALAGALSRR-GVGFGDRVLILMLNRTEFVESVLAANMLGAIAVPVNFRLTP 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544134 157 KDILYRLQSSKANCIITNDVLAPAVDAVASKCENLHSKLIVSENSREGWGNLKELMKHASDSHTCVKTKHNEIMAIFFTS 236
Cdd:PRK07786 104 PEIAFLVSDCGAHVVVTEAALAPVATAVRDIVPLLSTVVVAGGSSDDSVLGYEDLLAEAGPAHAPVDIPNDSPALIMYTS 183
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544134 237 GTSGYPKMTAHTHSSFGlGLSVNG-RFWLDLTPSDVMWNTSDTgWAKSAWSSVFSPWIQGACVFTHHLPRFEPTSILQTL 315
Cdd:PRK07786 184 GTTGRPKGAVLTHANLT-GQAMTClRTNGADINSDVGFVGVPL-FHIAGIGSMLPGLLLGAPTVIYPLGAFDPGQLLDVL 261
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544134 316 SKYPIT-VFCsAPTVYRMLVQNDITSYKFKSLKhCVSAGEPITPDVTEKWRNKT--GLDIYEGYGQTE----TVLICGNF 388
Cdd:PRK07786 262 EAEKVTgIFL-VPAQWQAVCAEQQARPRDLALR-VLSWGAAPASDTLLRQMAATfpEAQILAAFGQTEmspvTCMLLGED 339
|
330 340
....*....|....*....|.
gi 42544134 389 KGMKIkpGSMGKPSPAFDVKV 409
Cdd:PRK07786 340 AIRKL--GSVGKVIPTVAARV 358
|
|
| FACL_fum10p_like |
cd05926 |
Subfamily of fatty acid CoA ligase (FACL) similar to Fum10p of Gibberella moniliformis; FACL ... |
95-402 |
4.34e-16 |
|
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: 80.05 E-value: 4.34e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544134 95 WSFEELGSLSRKFANILSEAcSLQRGDRVILILPRVPEWWLANVACLRTGTVLIPGTTQLTQKDILYRLQSSKANCIIT- 173
Cdd:cd05926 15 LTYADLAELVDDLARQLAAL-GIKKGDRVAIALPNGLEFVVAFLAAARAGAVVAPLNPAYKKAEFEFYLADLGSKLVLTp 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544134 174 NDVLAPAVDAvASKCENLHSKLIVSENSREGWGNLKELMKHASDSHTCVKTKH---NEIMAIFFTSGTSGYPKMTAHTHS 250
Cdd:cd05926 94 KGELGPASRA-ASKLGLAILELALDVGVLIRAPSAESLSNLLADKKNAKSEGVplpDDLALILHTSGTTGRPKGVPLTHR 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544134 251 SfgLGLSV-NGRFWLDLTPSD----VMWNTSDTGWAKSAWSSVFSpwiQGACVFThhlPRFEPTSILQTLSKYPITVFCS 325
Cdd:cd05926 173 N--LAASAtNITNTYKLTPDDrtlvVMPLFHVHGLVASLLSTLAA---GGSVVLP---PRFSASTFWPDVRDYNATWYTA 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544134 326 APTVYRMLVQNDITSY--KFKSLKHCVSAGEPITPDVTEKWRNKTGLDIYEGYGQTETV--LICGNFKGMKIKPGSMGKP 401
Cdd:cd05926 245 VPTIHQILLNRPEPNPesPPPKLRFIRSCSASLPPAVLEALEATFGAPVLEAYGMTEAAhqMTSNPLPPGPRKPGSVGKP 324
|
.
gi 42544134 402 S 402
Cdd:cd05926 325 V 325
|
|
| PRK05605 |
PRK05605 |
long-chain-fatty-acid--CoA ligase; Validated |
63-409 |
5.30e-16 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 235531 [Multi-domain] Cd Length: 573 Bit Score: 80.04 E-value: 5.30e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544134 63 DVLDqwtdkEKAGKKPSNPAFWWInrnGEEMrwSFEELGSLSRKFANILsEACSLQRGDRVILILPRVPEWWLANVACLR 142
Cdd:PRK05605 36 DLYD-----NAVARFGDRPALDFF---GATT--TYAELGKQVRRAAAGL-RALGVRPGDRVAIVLPNCPQHIVAFYAVLR 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544134 143 TGTVLIPGTTQLTQKDILYRLQSSKANCIItndvlapAVDAVASKCENLHSKL----IVSEN------------------ 200
Cdd:PRK05605 105 LGAVVVEHNPLYTAHELEHPFEDHGARVAI-------VWDKVAPTVERLRRTTpletIVSVNmiaampllqrlalrlpip 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544134 201 ----SREG----------WgnlKELMKHA----SDSHTCVKTKHNEIMAIFFTSGTSGYPKMTAHTHSsfglGLSVN--- 259
Cdd:PRK05605 178 alrkARAAltgpapgtvpW---ETLVDAAiggdGSDVSHPRPTPDDVALILYTSGTTGKPKGAQLTHR----NLFANaaq 250
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544134 260 GRFWLDLTPSD----------------VMWNTsdtgwaksawssvFSPWIQGACVFthhLPRFEPTSILQTLSKYPITVF 323
Cdd:PRK05605 251 GKAWVPGLGDGpervlaalpmfhayglTLCLT-------------LAVSIGGELVL---LPAPDIDLILDAMKKHPPTWL 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544134 324 CSAPTVYRMLVQN------DITSykfksLKHCVSAGEPITPDVTEKWRNKTGLDIYEGYGQTETV-LICGNFKGMKIKPG 396
Cdd:PRK05605 315 PGVPPLYEKIAEAaeergvDLSG-----VRNAFSGAMALPVSTVELWEKLTGGLLVEGYGLTETSpIIVGNPMSDDRRPG 389
|
410
....*....|...
gi 42544134 397 SMGKPSPAFDVKV 409
Cdd:PRK05605 390 YVGVPFPDTEVRI 402
|
|
| ttLC_FACS_AlkK_like |
cd12119 |
Fatty acyl-CoA synthetases similar to LC-FACS from Thermus thermophiles; This family includes ... |
90-381 |
5.76e-16 |
|
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: 79.98 E-value: 5.76e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544134 90 GEEMRWSFEELGSLSRKFANILSEAcSLQRGDRVILIL---PRVPEWWLAnVAClrTGTVLIPGTTQLTQKDILYRLQSS 166
Cdd:cd12119 21 GEVHRYTYAEVAERARRLANALRRL-GVKPGDRVATLAwntHRHLELYYA-VPG--MGAVLHTINPRLFPEQIAYIINHA 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544134 167 KANCIITNDVLAPAVDAVASKCENLHSKLIVSENSR------EGWGNLKELMKHASDSHTCVKTKHNEIMAIFFTSGTSG 240
Cdd:cd12119 97 EDRVVFVDRDFLPLLEAIAPRLPTVEHVVVMTDDAAmpepagVGVLAYEELLAAESPEYDWPDFDENTAAAICYTSGTTG 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544134 241 YPKMTAHTHSSFGLG-LSVNGRFWLDLTPSDV------MWNTsdtgwakSAWSSVFSPWIQGAC-VFTHhlPRFEPTSIL 312
Cdd:cd12119 177 NPKGVVYSHRSLVLHaMAALLTDGLGLSESDVvlpvvpMFHV-------NAWGLPYAAAMVGAKlVLPG--PYLDPASLA 247
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544134 313 QTLSKYPITVFCSAPTVYRMLVQN-DITSYKFKSLKHCVSAGEPITPDVTEKWRNKtGLDIYEGYGQTET 381
Cdd:cd12119 248 ELIEREGVTFAAGVPTVWQGLLDHlEANGRDLSSLRRVVIGGSAVPRSLIEAFEER-GVRVIHAWGMTET 316
|
|
| PRK06839 |
PRK06839 |
o-succinylbenzoate--CoA ligase; |
90-409 |
6.03e-16 |
|
o-succinylbenzoate--CoA ligase;
Pssm-ID: 168698 [Multi-domain] Cd Length: 496 Bit Score: 79.90 E-value: 6.03e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544134 90 GEEMRWSFEELGSLSRKFANILSEACSLQRGDRVILILPRVPEWWLANVACLRTGTVLIPGTTQLTQKDILYRLQSSKAN 169
Cdd:PRK06839 23 TEEEEMTYKQLHEYVSKVAAYLIYELNVKKGERIAILSQNSLEYIVLLFAIAKVECIAVPLNIRLTENELIFQLKDSGTT 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544134 170 CIITNDVLAPAVDAVASKCENLHSKLIVSensregwgnLKELMKHASDShtCVKTKHNEIMAIFFTSGTSGYPKMTAHTH 249
Cdd:PRK06839 103 VLFVEKTFQNMALSMQKVSYVQRVISITS---------LKEIEDRKIDN--FVEKNESASFIICYTSGTTGKPKGAVLTQ 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544134 250 SSFGLGlSVNGRFWLDLTPSDV------MWNTSDTGWAksawssVFSPWIQGACVFTHHlpRFEPTSILQTLSKYPITVF 323
Cdd:PRK06839 172 ENMFWN-ALNNTFAIDLTMHDRsivllpLFHIGGIGLF------AFPTLFAGGVIIVPR--KFEPTKALSMIEKHKVTVV 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544134 324 CSAPTVYRMLVQN-DITSYKFKSLKHCVSAGEPITPDVTEKWRNKtGLDIYEGYGQTET-----VLICGNFKGmkiKPGS 397
Cdd:PRK06839 243 MGVPTIHQALINCsKFETTNLQSVRWFYNGGAPCPEELMREFIDR-GFLFGQGFGMTETsptvfMLSEEDARR---KVGS 318
|
330
....*....|..
gi 42544134 398 MGKPSPAFDVKV 409
Cdd:PRK06839 319 IGKPVLFCDYEL 330
|
|
| DltA |
cd05945 |
D-alanine:D-alanyl carrier protein ligase (DltA) and similar proteins; This family includes ... |
74-385 |
1.20e-15 |
|
D-alanine:D-alanyl carrier protein ligase (DltA) and similar proteins; This family includes D-alanyl carrier protein ligase DltA and aliphatic beta-amino acid adenylation enzymes IdnL1 and CmiS6. DltA incorporates D-ala in techoic acids in gram-positive bacteria via a two-step process, starting with adenylation of D-alanine that transfers D-alanine to the D-alanyl carrier protein. IdnL1, a short-chain aliphatic beta-amino acid adenylation enzyme, recognizes 3-aminobutanoic acid, and is involved in the synthesis of the macrolactam antibiotic incednine. CmiS6 is a medium-chain beta-amino acid adenylation enzyme that recognizes 3-aminononanoic acid, and is involved in the synthesis of cremimycin, also a macrolactam antibiotic. The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester bond to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.
Pssm-ID: 341267 [Multi-domain] Cd Length: 449 Bit Score: 78.44 E-value: 1.20e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544134 74 AGKKPSNPAFWWINRngeemRWSFEELGSLSRKFANILSEACsLQRGDRVILILPRVPEWWLANVACLRTGTVLIPGTTQ 153
Cdd:cd05945 1 AAANPDRPAVVEGGR-----TLTYRELKERADALAAALASLG-LDAGDPVVVYGHKSPDAIAAFLAALKAGHAYVPLDAS 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544134 154 LTQKdilyRLQSskancIItnDVLAPAVdavaskcenlhskLIVSENsregwgnlkelmkhasdshtcvktkhnEIMAIF 233
Cdd:cd05945 75 SPAE----RIRE-----IL--DAAKPAL-------------LIADGD---------------------------DNAYII 103
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544134 234 FTSGTSGYPKMTAHTHS---SFGLGLsvNGRFwlDLTPSDVMWNTSDtgwaksaWS---SVFS---PWIQGACVFThhLP 304
Cdd:cd05945 104 FTSGSTGRPKGVQISHDnlvSFTNWM--LSDF--PLGPGDVFLNQAP-------FSfdlSVMDlypALASGATLVP--VP 170
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544134 305 RFE---PTSILQTLSKYPITVFCSAPTVYRMLVQN-DITSYKFKSLKHCVSAGEPITPDVTEKWRNKT-GLDIYEGYGQT 379
Cdd:cd05945 171 RDAtadPKQLFRFLAEHGITVWVSTPSFAAMCLLSpTFTPESLPSLRHFLFCGEVLPHKTARALQQRFpDARIYNTYGPT 250
|
....*.
gi 42544134 380 ETVLIC 385
Cdd:cd05945 251 EATVAV 256
|
|
| PRK08276 |
PRK08276 |
long-chain-fatty-acid--CoA ligase; Validated |
90-401 |
1.62e-15 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236215 [Multi-domain] Cd Length: 502 Bit Score: 78.41 E-value: 1.62e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544134 90 GEEMRWSFEELGSLSRKFANILSEAcSLQRGDRVILILPRVPEWWLANVACLRTGTVLIPGTTQLTQKDILYRLQSSKAN 169
Cdd:PRK08276 7 PSGEVVTYGELEARSNRLAHGLRAL-GLREGDVVAILLENNPEFFEVYWAARRSGLYYTPINWHLTAAEIAYIVDDSGAK 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544134 170 CIITNDVLAPAVDAVASKCENLHSKLIVSENSREGWGNLKELMKHASDSHTCVKTKHNEiMAifFTSGTSGYPK------ 243
Cdd:PRK08276 86 VLIVSAALADTAAELAAELPAGVPLLLVVAGPVPGFRSYEEALAAQPDTPIADETAGAD-ML--YSSGTTGRPKgikrpl 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544134 244 MTAHTHSSFGLGLSVNGrFWLDLTPSDV------MWNTSDTGWAKSAwssvfspwiqgacvftHHL-------PRFEPTS 310
Cdd:PRK08276 163 PGLDPDEAPGMMLALLG-FGMYGGPDSVylspapLYHTAPLRFGMSA----------------LALggtvvvmEKFDAEE 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544134 311 ILQTLSKYPITVFCSAPTVY-RML-----VQNditSYKFKSLKHCVSAGEPITPDVTEK----WrnktGLDIYEGYGQTE 380
Cdd:PRK08276 226 ALALIERYRVTHSQLVPTMFvRMLklpeeVRA---RYDVSSLRVAIHAAAPCPVEVKRAmidwW----GPIIHEYYASSE 298
|
330 340
....*....|....*....|....*
gi 42544134 381 ----TVLICGNFKGmkiKPGSMGKP 401
Cdd:PRK08276 299 gggvTVITSEDWLA---HPGSVGKA 320
|
|
| PRK07470 |
PRK07470 |
acyl-CoA synthetase; Validated |
74-383 |
1.98e-15 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 180988 [Multi-domain] Cd Length: 528 Bit Score: 78.16 E-value: 1.98e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544134 74 AGKKPSNPAFWWinrnGEEmRWSFEELGSLSRKFANILsEACSLQRGDRVILILPRVPEWWLANVACLRTGTVLIPGTTQ 153
Cdd:PRK07470 17 ARRFPDRIALVW----GDR-SWTWREIDARVDALAAAL-AARGVRKGDRILVHSRNCNQMFESMFAAFRLGAVWVPTNFR 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544134 154 LTQKDILYRLQSSKANCIITNDVLAPAVDAVASKCENLHSKlIVSENSREGWGNLKELMKHASDSHTCVKTKHNEIMAIF 233
Cdd:PRK07470 91 QTPDEVAYLAEASGARAMICHADFPEHAAAVRAASPDLTHV-VAIGGARAGLDYEALVARHLGARVANAAVDHDDPCWFF 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544134 234 FTSGTSGYPKMTAHTHSSfgLGLSVNGRFwLDLTPsdvmwntsdtGWAKSAWSSVFSPWIQGACVftHHL---------- 303
Cdd:PRK07470 170 FTSGTTGRPKAAVLTHGQ--MAFVITNHL-ADLMP----------GTTEQDASLVVAPLSHGAGI--HQLcqvargaatv 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544134 304 ----PRFEPTSILQTLSKYPITVFCSAPTVYRMLVQN-DITSYKFKSLKHCVSAGEPITPDVTEKWRNKTGLDIYEGYGQ 378
Cdd:PRK07470 235 llpsERFDPAEVWALVERHRVTNLFTVPTILKMLVEHpAVDRYDHSSLRYVIYAGAPMYRADQKRALAKLGKVLVQYFGL 314
|
330
....*....|
gi 42544134 379 TE-----TVL 383
Cdd:PRK07470 315 GEvtgniTVL 324
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
72-382 |
4.98e-15 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 78.08 E-value: 4.98e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544134 72 EKAGKKPSNPAFWWinrngEEMRWSFEELGSLSRKFANILseacsLQRG----DRVILILPRVPEWWLANVACLRTGTVL 147
Cdd:PRK12316 4559 ERARMTPDAVAVVF-----DEEKLTYAELNRRANRLAHAL-----IARGvgpeVLVGIAMERSAEMMVGLLAVLKAGGAY 4628
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544134 148 IPGTTQLTQKDILYRLQSSKANCIITNDVLAPAVDAVASkcenLHSKLIVSENSREGWgnlkelmkhaSDSHTCVKTKHN 227
Cdd:PRK12316 4629 VPLDPEYPRERLAYMMEDSGAALLLTQSHLLQRLPIPDG----LASLALDRDEDWEGF----------PAHDPAVRLHPD 4694
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544134 228 EIMAIFFTSGTSGYPKMTAHTHSSFGLGLSVNGRFWlDLTPSDVMWNTSDTGWAKSAWSsVFSPWIQGACVFTHHLPRFE 307
Cdd:PRK12316 4695 NLAYVIYTSGSTGRPKGVAVSHGSLVNHLHATGERY-ELTPDDRVLQFMSFSFDGSHEG-LYHPLINGASVVIRDDSLWD 4772
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 42544134 308 PTSILQTLSKYPITVFCSAPTVYRMLVQNDITSYKFKSLKHCVSAGEPITPD-VTEKWRNKTGLDIYEGYGQTETV 382
Cdd:PRK12316 4773 PERLYAEIHEHRVTVLVFPPVYLQQLAEHAERDGEPPSLRVYCFGGEAVAQAsYDLAWRALKPVYLFNGYGPTETT 4848
|
|
| ttLC_FACS_AEE21_like |
cd12118 |
Fatty acyl-CoA synthetases similar to LC-FACS from Thermus thermophiles and Arabidopsis; This ... |
92-385 |
1.06e-14 |
|
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: 75.80 E-value: 1.06e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544134 92 EMRWSFEELGSLSRKFANILSEAcSLQRGDRVILILPRVPEWWLANVACLRTGTVLIPGTTQLTQKDILYRLQSSKANCI 171
Cdd:cd12118 27 DRRYTWRQTYDRCRRLASALAAL-GISRGDTVAVLAPNTPAMYELHFGVPMAGAVLNALNTRLDAEEIAFILRHSEAKVL 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544134 172 ItndvlapaVDAvaskcENLHSKLIVSENSREGWgnlkelmkhasdshTCVKTKHNEImAIFFTSGTSGYPKMTAHTHSS 251
Cdd:cd12118 106 F--------VDR-----EFEYEDLLAEGDPDFEW--------------IPPADEWDPI-ALNYTSGTTGRPKGVVYHHRG 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544134 252 FGLGLSVNGRFWlDLTPSDV-MWNTSD---TGWAksawssvfSPWIQGACVFTHH-LPRFEPTSILQTLSKYPITVFCSA 326
Cdd:cd12118 158 AYLNALANILEW-EMKQHPVyLWTLPMfhcNGWC--------FPWTVAAVGGTNVcLRKVDAKAIYDLIEKHKVTHFCGA 228
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 42544134 327 PTVYRMLVqNDITSYKfKSLKHCVS---AGEPITPDVTEKWRNKtGLDIYEGYGQTET---VLIC 385
Cdd:cd12118 229 PTVLNMLA-NAPPSDA-RPLPHRVHvmtAGAPPPAAVLAKMEEL-GFDVTHVYGLTETygpATVC 290
|
|
| PRK07529 |
PRK07529 |
AMP-binding domain protein; Validated |
74-409 |
1.22e-14 |
|
AMP-binding domain protein; Validated
Pssm-ID: 236043 [Multi-domain] Cd Length: 632 Bit Score: 76.15 E-value: 1.22e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544134 74 AGKKPSNPAFWWI---NRNGEEMRWSFEELgsLSR--KFANILSeACSLQRGDRVILILPRVPE----WW---LANVAC- 140
Cdd:PRK07529 35 AARHPDAPALSFLldaDPLDRPETWTYAEL--LADvtRTANLLH-SLGVGPGDVVAFLLPNLPEthfaLWggeAAGIANp 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544134 141 -------------LR-TGT-VLI-----PGTtqltqkDILYRLQSSKAnciitndvLAPAVDAV----ASKCENLHSKLI 196
Cdd:PRK07529 112 inpllepeqiaelLRaAGAkVLVtlgpfPGT------DIWQKVAEVLA--------ALPELRTVvevdLARYLPGPKRLA 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544134 197 VSENSREG----WGNLKELMKHASDSHTCVKTKHNEIMAIFF-TSGTSGYPKMTAHTHSsfglGLSVNGrfW-----LDL 266
Cdd:PRK07529 178 VPLIRRKAhariLDFDAELARQPGDRLFSGRPIGPDDVAAYFhTGGTTGMPKLAQHTHG----NEVANA--WlgallLGL 251
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544134 267 TPSDVMW--------NTSDTGwaksawssVFSPWIQGACVFThhlprfePTS-----------ILQTLSKYPITVFCSAP 327
Cdd:PRK07529 252 GPGDTVFcglplfhvNALLVT--------GLAPLARGAHVVL-------ATPqgyrgpgvianFWKIVERYRINFLSGVP 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544134 328 TVYRMLVQNDITSYKFKSLKHCVSAGEPITPDVTEKWRNKTGLDIYEGYGQTE-TVLICGNFKGMKIKPGSMGKPSPAFD 406
Cdd:PRK07529 317 TVYAALLQVPVDGHDISSLRYALCGAAPLPVEVFRRFEAATGVRIVEGYGLTEaTCVSSVNPPDGERRIGSVGLRLPYQR 396
|
...
gi 42544134 407 VKV 409
Cdd:PRK07529 397 VRV 399
|
|
| PRK06087 |
PRK06087 |
medium-chain fatty-acid--CoA ligase; |
94-382 |
1.56e-14 |
|
medium-chain fatty-acid--CoA ligase;
Pssm-ID: 180393 [Multi-domain] Cd Length: 547 Bit Score: 75.55 E-value: 1.56e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544134 94 RWSFEELGSLSRKFANILSeACSLQRGDRVILILPRVPEWWLANVACLRTGTVLIPGTTQLTQKDILYRLQSSKANCIIT 173
Cdd:PRK06087 49 SYTYSALDHAASRLANWLL-AKGIEPGDRVAFQLPGWCEFTIIYLACLKVGAVSVPLLPSWREAELVWVLNKCQAKMFFA 127
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544134 174 NDVLA-----PAVDAVASKCENLHSKLIVSENSREGWG-NLKELMKHASDSHTCVKTKHNEIMAIFFTSGTSGYPKMTAH 247
Cdd:PRK06087 128 PTLFKqtrpvDLILPLQNQLPQLQQIVGVDKLAPATSSlSLSQIIADYEPLTTAITTHGDELAAVLFTSGTEGLPKGVML 207
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544134 248 THSSFGLG-LSVNGRfwLDLTPSDVMWNTSDTGWAKSAWSSVFSPWIQGACVFThhLPRFEPTSILQTLSKYPITVFCSA 326
Cdd:PRK06087 208 THNNILASeRAYCAR--LNLTWQDVFMMPAPLGHATGFLHGVTAPFLIGARSVL--LDIFTPDACLALLEQQRCTCMLGA 283
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*...
gi 42544134 327 -PTVYRMLVQNDITSYKFKSLKHCVSAGEPITPDVTEK-WRNktGLDIYEGYGQTETV 382
Cdd:PRK06087 284 tPFIYDLLNLLEKQPADLSALRFFLCGGTTIPKKVAREcQQR--GIKLLSVYGSTESS 339
|
|
| PLN02246 |
PLN02246 |
4-coumarate--CoA ligase |
72-399 |
2.24e-14 |
|
4-coumarate--CoA ligase
Pssm-ID: 215137 [Multi-domain] Cd Length: 537 Bit Score: 75.02 E-value: 2.24e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544134 72 EKAGKKPSNPAFwwIN-RNGEEMrwSFEELGSLSRKFANILSeACSLQRGDRVILILPRVPEWWLANVACLRTGTVLIPG 150
Cdd:PLN02246 31 ERLSEFSDRPCL--IDgATGRVY--TYADVELLSRRVAAGLH-KLGIRQGDVVMLLLPNCPEFVLAFLGASRRGAVTTTA 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544134 151 TTQLTQKDILYRLQSSKANCIITndvLAPAVDAVASKCENLHSKLIVSENSREGWGNLKELMKHASDSHTCVKTKHNEIM 230
Cdd:PLN02246 106 NPFYTPAEIAKQAKASGAKLIIT---QSCYVDKLKGLAEDDGVTVVTIDDPPEGCLHFSELTQADENELPEVEISPDDVV 182
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544134 231 AIFFTSGTSGYPKMTAHTHSsfGLGLSV---------NgrfwLDLTPSDVMWNTSDTGWAKSAWSSVFSPWIQGACVFTh 301
Cdd:PLN02246 183 ALPYSSGTTGLPKGVMLTHK--GLVTSVaqqvdgenpN----LYFHSDDVILCVLPMFHIYSLNSVLLCGLRVGAAILI- 255
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544134 302 hLPRFEPTSILQTLSKYPITVFCSAPTVYRMLVQNDIT-SYKFKSLKHCVSAGEPITPDVTEKWRNKTGLDIY-EGYGQT 379
Cdd:PLN02246 256 -MPKFEIGALLELIQRHKVTIAPFVPPIVLAIAKSPVVeKYDLSSIRMVLSGAAPLGKELEDAFRAKLPNAVLgQGYGMT 334
|
330 340
....*....|....*....|....*
gi 42544134 380 E--TVL-ICGNF--KGMKIKPGSMG 399
Cdd:PLN02246 335 EagPVLaMCLAFakEPFPVKSGSCG 359
|
|
| FACL_like_4 |
cd05944 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
226-409 |
2.42e-14 |
|
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: 74.05 E-value: 2.42e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544134 226 HNEIMAIFFTSGTSGYPKMTAHTHSsfglGLSVNGrfW-----LDLTPSDVMWNTSDTGWAKSAWSSVFSPWIQGA-CVF 299
Cdd:cd05944 1 SDDVAAYFHTGGTTGTPKLAQHTHS----NEVYNA--WmlalnSLFDPDDVLLCGLPLFHVNGSVVTLLTPLASGAhVVL 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544134 300 THHLPRFEPT---SILQTLSKYPITVFCSAPTVYRMLVQNDITSyKFKSLKHCVSAGEPITPDVTEKWRNKTGLDIYEGY 376
Cdd:cd05944 75 AGPAGYRNPGlfdNFWKLVERYRITSLSTVPTVYAALLQVPVNA-DISSLRFAMSGAAPLPVELRARFEDATGLPVVEGY 153
|
170 180 190
....*....|....*....|....*....|....
gi 42544134 377 GQTE-TVLICGNFKGMKIKPGSMGKPSPAFDVKV 409
Cdd:cd05944 154 GLTEaTCLVAVNPPDGPKRPGSVGLRLPYARVRI 187
|
|
| LC_FACL_like |
cd05914 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); The members of this family are ... |
90-422 |
2.45e-14 |
|
Uncharacterized subfamily of fatty acid CoA ligase (FACL); The members of this family are bacterial long-chain fatty acid CoA synthetase, most of which are as yet uncharacterized. LC-FACS catalyzes the formation of fatty acyl-CoA in a two-step reaction: the formation of a fatty acyl-AMP molecule as an intermediate, and the formation of a fatty acyl-CoA. Free fatty acids must be "activated" to their CoA thioesters before participating in most catabolic and anabolic reactions.
Pssm-ID: 341240 [Multi-domain] Cd Length: 463 Bit Score: 74.79 E-value: 2.45e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544134 90 GEEMRWSFEELGSLSRKFANILsEACSLQRGDRVILILPRVPEWWLANVACLRTGTVLIPGTTQLTQKDILYRLQSSKAn 169
Cdd:cd05914 3 YGGEPLTYKDLADNIAKFALLL-KINGVGTGDRVALMGENRPEWGIAFFAIWTYGAIAVPILAEFTADEVHHILNHSEA- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544134 170 ciitndvlapavdavaskcenlhSKLIVSENsregwgnlkelmkhasdshtcvktkhNEIMAIFFTSGTSGYPKMTAHTH 249
Cdd:cd05914 81 -----------------------KAIFVSDE--------------------------DDVALINYTSGTTGNSKGVMLTY 111
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544134 250 SSfgLGLSVNGRFWLD-LTPSDVMWNTSDTGWAKSAWSSVFSPWIQGACVftHHLPRFePTSILQTLSKYPITVFCSAPT 328
Cdd:cd05914 112 RN--IVSNVDGVKEVVlLGKGDKILSILPLHHIYPLTFTLLLPLLNGAHV--VFLDKI-PSAKIIALAFAQVTPTLGVPV 186
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544134 329 VYRM--------LVQNDITSYKFK------------------------SLKHCVSAGEPITPDVTEKWRnKTGLDIYEGY 376
Cdd:cd05914 187 PLVIekifkmdiIPKLTLKKFKFKlakkinnrkirklafkkvheafggNIKEFVIGGAKINPDVEEFLR-TIGFPYTIGY 265
|
330 340 350 360
....*....|....*....|....*....|....*....|....*..
gi 42544134 377 GQTETV-LICGNFKGmKIKPGSMGKPSPAFDVKVcTSPSRRMFNNPI 422
Cdd:cd05914 266 GMTETApIISYSPPN-RIRLGSAGKVIDGVEVRI-DSPDPATGEGEI 310
|
|
| A_NRPS_AB3403-like |
cd17646 |
Peptide Synthetase; The adenylation (A) domain of NRPS recognizes a specific amino acid or ... |
72-382 |
2.73e-14 |
|
Peptide Synthetase; The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester bond to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.
Pssm-ID: 341301 [Multi-domain] Cd Length: 488 Bit Score: 74.62 E-value: 2.73e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544134 72 EKAGKKPSNPAFWWinrngEEMRWSFEELGSLSRKFANILSEAcSLQRGDRVILILPRVPEWWLANVACLRTGTVLIPGT 151
Cdd:cd17646 6 EQAARTPDAPAVVD-----EGRTLTYRELDERANRLAHLLRAR-GVGPEDRVAVLLPRSADLVVALLAVLKAGAAYLPLD 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544134 152 TQLTQKDILYRLQSSKANCIITNDVLA---PAVDAVASKCEnlhsklivsensregwgnlkELMKHASDSHTCVKTKHNE 228
Cdd:cd17646 80 PGYPADRLAYMLADAGPAVVLTTADLAarlPAGGDVALLGD--------------------EALAAPPATPPLVPPRPDN 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544134 229 IMAIFFTSGTSGYPKMTAHTHSSFglglsVNGRFWL----DLTPSDVMWNTSDTGWAKSAWSsVFSPWIQGAC-VFTHHL 303
Cdd:cd17646 140 LAYVIYTSGSTGRPKGVMVTHAGI-----VNRLLWMqdeyPLGPGDRVLQKTPLSFDVSVWE-LFWPLVAGARlVVARPG 213
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 42544134 304 PRFEPTSILQTLSKYPITVFCSAPTVYRMLVQnDITSYKFKSLKHCVSAGEPITPDVTEKWRNKTGLDIYEGYGQTETV 382
Cdd:cd17646 214 GHRDPAYLAALIREHGVTTCHFVPSMLRVFLA-EPAAGSCASLRRVFCSGEALPPELAARFLALPGAELHNLYGPTEAA 291
|
|
| PRK03640 |
PRK03640 |
o-succinylbenzoate--CoA ligase; |
91-401 |
3.44e-14 |
|
o-succinylbenzoate--CoA ligase;
Pssm-ID: 235146 [Multi-domain] Cd Length: 483 Bit Score: 74.23 E-value: 3.44e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544134 91 EEMRWSFEELGSLSRKFANILSEACsLQRGDRVILILPRVPEWWLANVACLRTGTVLIPGTTQLTQKDILYRLQSSKANC 170
Cdd:PRK03640 24 EEKKVTFMELHEAVVSVAGKLAALG-VKKGDRVALLMKNGMEMILVIHALQQLGAVAVLLNTRLSREELLWQLDDAEVKC 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544134 171 IITNDVLAPAVDAVASkcenlhskLIVSEnsregwgnlkeLMKHASDSHTCVKTKH-NEIMAIFFTSGTSGYPK---MTA 246
Cdd:PRK03640 103 LITDDDFEAKLIPGIS--------VKFAE-----------LMNGPKEEAEIQEEFDlDEVATIMYTSGTTGKPKgviQTY 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544134 247 HTH------SSFGLGLSVNGRfWLDLTPsdvMWNTsdtgwakSAWSSVFSPWIQGACVFTHhlPRFEPTSILQTLSKYPI 320
Cdd:PRK03640 164 GNHwwsavgSALNLGLTEDDC-WLAAVP---IFHI-------SGLSILMRSVIYGMRVVLV--EKFDAEKINKLLQTGGV 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544134 321 TVFCSAPT-VYRMLVQNDITSYKfKSLKHCVSAGEPITPDVTEKWRNKtGLDIYEGYGQTETV-LICG-NFKGMKIKPGS 397
Cdd:PRK03640 231 TIISVVSTmLQRLLERLGEGTYP-SSFRCMLLGGGPAPKPLLEQCKEK-GIPVYQSYGMTETAsQIVTlSPEDALTKLGS 308
|
....
gi 42544134 398 MGKP 401
Cdd:PRK03640 309 AGKP 312
|
|
| EntF |
COG1020 |
EntF, seryl-AMP synthase component of non-ribosomal peptide synthetase [Secondary metabolites ... |
91-381 |
4.29e-14 |
|
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: 74.89 E-value: 4.29e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544134 91 EEMRWSFEELGSLSRKFANILsEACSLQRGDRVILILPRVPEWWLANVACLRTGTVLIPGTTQLTQKDILYRLQSSKANC 170
Cdd:COG1020 498 GDQSLTYAELNARANRLAHHL-RALGVGPGDLVGVCLERSLEMVVALLAVLKAGAAYVPLDPAYPAERLAYMLEDAGARL 576
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544134 171 IITNDVLAPAVDAVASKCENLHSKLIVSENSregwGNLKElmkHASDSHTCVktkhneimaIFFTSGTSGYPKMTAHTHS 250
Cdd:COG1020 577 VLTQSALAARLPELGVPVLALDALALAAEPA----TNPPV---PVTPDDLAY---------VIYTSGSTGRPKGVMVEHR 640
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544134 251 SFG-LGLSVNGRFwlDLTPSDVM-WNTS---DTgwakSAWSsVFSPWIQGACVfthHLP----RFEPTSILQTLSKYPIT 321
Cdd:COG1020 641 ALVnLLAWMQRRY--GLGPGDRVlQFASlsfDA----SVWE-IFGALLSGATL---VLAppeaRRDPAALAELLARHRVT 710
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 42544134 322 VFCSAPTVYRMLVQNDITSykFKSLKHCVSAGEPITPDVTEKWRNKT-GLDIYEGYGQTET 381
Cdd:COG1020 711 VLNLTPSLLRALLDAAPEA--LPSLRLVLVGGEALPPELVRRWRARLpGARLVNLYGPTET 769
|
|
| PRK08279 |
PRK08279 |
long-chain-acyl-CoA synthetase; Validated |
63-408 |
8.32e-14 |
|
long-chain-acyl-CoA synthetase; Validated
Pssm-ID: 236217 [Multi-domain] Cd Length: 600 Bit Score: 73.37 E-value: 8.32e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544134 63 DVLDQWTDKekagkKPSNPAFwwinrNGEEMRWSFEELGSLSRKFANILSEAcSLQRGDRVILILPRVPEWWLANVACLR 142
Cdd:PRK08279 41 DVFEEAAAR-----HPDRPAL-----LFEDQSISYAELNARANRYAHWAAAR-GVGKGDVVALLMENRPEYLAAWLGLAK 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544134 143 TGTV--LIpgTTQLTQKDILYRLQSSKANCIITNDVLAPAVDAVASKCENLHSKLIVSENSREGWGNLKELMKHASDSHT 220
Cdd:PRK08279 110 LGAVvaLL--NTQQRGAVLAHSLNLVDAKHLIVGEELVEAFEEARADLARPPRLWVAGGDTLDDPEGYEDLAAAAAGAPT 187
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544134 221 CVKTKHNEIMA---IF--FTSGTSGYPKMTAHTH-----SSFGLGLSvngrfwLDLTPSDVMWNT----SDTGwAKSAWS 286
Cdd:PRK08279 188 TNPASRSGVTAkdtAFyiYTSGTTGLPKAAVMSHmrwlkAMGGFGGL------LRLTPDDVLYCClplyHNTG-GTVAWS 260
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544134 287 SVFSPwiqGACV-----FThhLPRFEPTSIlqtlsKYPITVFCSAPTVYRMLVQNDITSY-KFKSLKHCVSAGepITPDV 360
Cdd:PRK08279 261 SVLAA---GATLalrrkFS--ASRFWDDVR-----RYRATAFQYIGELCRYLLNQPPKPTdRDHRLRLMIGNG--LRPDI 328
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|.
gi 42544134 361 TEKWRNKTGLD-IYEGYGQTE--TVLIcgNFKGmkiKPGSMGKpSPAFDVK 408
Cdd:PRK08279 329 WDEFQQRFGIPrILEFYAASEgnVGFI--NVFN---FDGTVGR-VPLWLAH 373
|
|
| OSB_CoA_lg |
cd05912 |
O-succinylbenzoate-CoA ligase (also known as O-succinylbenzoate-CoA synthase, OSB-CoA ... |
95-409 |
9.30e-14 |
|
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: 72.38 E-value: 9.30e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544134 95 WSFEEL----GSLSRKFANIlseacSLQRGDRVILILPRVPEWWLANVACLRTGTVLIPGTTQLTQKDILYRLQSSKANC 170
Cdd:cd05912 2 YTFAELfeevSRLAEHLAAL-----GVRKGDRVALLSKNSIEMILLIHALWLLGAEAVLLNTRLTPNELAFQLKDSDVKL 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544134 171 iitndvlapavdavaskcenlhsklivsensregwgnlkelmkhasdshtcvktkhNEIMAIFFTSGTSGYPK---MTAH 247
Cdd:cd05912 77 --------------------------------------------------------DDIATIMYTSGTTGKPKgvqQTFG 100
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544134 248 TH------SSFGLGLSVNGRfWLDLTPsdvMWNTsdtgwakSAWSSVFSPWIQGACVFTHhlPRFEPTSILQTLSKYPIT 321
Cdd:cd05912 101 NHwwsaigSALNLGLTEDDN-WLCALP---LFHI-------SGLSILMRSVIYGMTVYLV--DKFDAEQVLHLINSGKVT 167
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544134 322 VFCSAPTVYRMLVQNDITSYKfKSLKHCVSAGEPITPDVTEKWRNKtGLDIYEGYGQTETV--LICGNFKGMKIKPGSMG 399
Cdd:cd05912 168 IISVVPTMLQRLLEILGEGYP-NNLRCILLGGGPAPKPLLEQCKEK-GIPVYQSYGMTETCsqIVTLSPEDALNKIGSAG 245
|
330
....*....|
gi 42544134 400 KPSPAFDVKV 409
Cdd:cd05912 246 KPLFPVELKI 255
|
|
| A_NRPS_VisG_like |
cd17651 |
similar to adenylation domain of virginiamycin S synthetase; This family of the adenylation (A) ... |
90-381 |
2.62e-13 |
|
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: 71.61 E-value: 2.62e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544134 90 GEEMRWSFEELGSLSRKFANILsEACSLQRGDRVILILPRVPEWWLANVACLRTGTVLIPGTTQLTQKDILYRLQSSKAN 169
Cdd:cd17651 16 AEGRRLTYAELDRRANRLAHRL-RARGVGPGDLVALCARRSAELVVALLAILKAGAAYVPLDPAYPAERLAFMLADAGPV 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544134 170 CIITNDVLAPAVDAVAskcenlhskLIVSENSREGWGNLkelmkhASDSHTCVKTKHNEIMAIFfTSGTSGYPKMTAHTH 249
Cdd:cd17651 95 LVLTHPALAGELAVEL---------VAVTLLDQPGAAAG------ADAEPDPALDADDLAYVIY-TSGSTGRPKGVVMPH 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544134 250 SSFglglsVNGRFWLD----LTPSDVMWNTSDTGWAKSAWSsVFSPWIQGACVfthHLP----RFEPTSILQTLSKYPIT 321
Cdd:cd17651 159 RSL-----ANLVAWQArassLGPGARTLQFAGLGFDVSVQE-IFSTLCAGATL---VLPpeevRTDPPALAAWLDEQRIS 229
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 42544134 322 VfCSAPTVY--RMLVQNDITSYKFKSLKHCVSAGEP--ITPDVTEKWRNKTGLDIYEGYGQTET 381
Cdd:cd17651 230 R-VFLPTVAlrALAEHGRPLGVRLAALRYLLTGGEQlvLTEDLREFCAGLPGLRLHNHYGPTET 292
|
|
| CHC_CoA_lg |
cd05903 |
Cyclohexanecarboxylate-CoA ligase (also called cyclohex-1-ene-1-carboxylate:CoA ligase); ... |
94-409 |
3.97e-13 |
|
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: 70.87 E-value: 3.97e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544134 94 RWSFEELGSLSRKFANILSEAcSLQRGDRVILILPrvpEWWLANV---ACLRTGTVLIPGTTQLTQKDILYRLQSSKANC 170
Cdd:cd05903 1 RLTYSELDTRADRLAAGLAAL-GVGPGDVVAFQLP---NWWEFAVlylACLRIGAVTNPILPFFREHELAFILRRAKAKV 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544134 171 IITNDVlapavdavaskcenlhsklivsensregWGNlkelMKHASDShtcvktkhNEIMAIFFTSGTSGYPKMTAHTHS 250
Cdd:cd05903 77 FVVPER----------------------------FRQ----FDPAAMP--------DAVALLLFTSGTTGEPKGVMHSHN 116
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544134 251 SfglgLSVNGRFW---LDLTPSDVMWNTSDTGWAKSAWSSVFSPWIQGACVftHHLPRFEPTSILQTLSKYPITVFCSAP 327
Cdd:cd05903 117 T----LSASIRQYaerLGLGPGDVFLVASPMAHQTGFVYGFTLPLLLGAPV--VLQDIWDPDKALALMREHGVTFMMGAT 190
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544134 328 T-VYRMLVQNDITSYKFKSLKHCVSAGEPITPDVTEKWRNKTGLDIYEGYGQTETVLICGNfkgmkIKPG-------SMG 399
Cdd:cd05903 191 PfLTDLLNAVEEAGEPLSRLRTFVCGGATVPRSLARRAAELLGAKVCSAYGSTECPGAVTS-----ITPApedrrlyTDG 265
|
330
....*....|
gi 42544134 400 KPSPAFDVKV 409
Cdd:cd05903 266 RPLPGVEIKV 275
|
|
| PRK08751 |
PRK08751 |
long-chain fatty acid--CoA ligase; |
96-407 |
5.06e-13 |
|
long-chain fatty acid--CoA ligase;
Pssm-ID: 181546 [Multi-domain] Cd Length: 560 Bit Score: 70.68 E-value: 5.06e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544134 96 SFEELGSLSRKFANILSEACSLQRGDRVILILPRVPEWWLANVACLRTGTVLIPGTTQLTQKDILYRLQSSKANCIITND 175
Cdd:PRK08751 52 TYREADQLVEQFAAYLLGELQLKKGDRVALMMPNCLQYPIATFGVLRAGLTVVNVNPLYTPRELKHQLIDSGASVLVVID 131
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544134 176 VLAPAVDAVASKCE---------------------NL---HSKLIVSENSREGWGNLKELMKHASdSHTC--VKTKHNEI 229
Cdd:PRK08751 132 NFGTTVQQVIADTPvkqvittglgdmlgfpkaalvNFvvkYVKKLVPEYRINGAIRFREALALGR-KHSMptLQIEPDDI 210
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544134 230 MAIFFTSGTSGYPKMTAHTHSSFGLGLSVNGRfWLDLTpsdvmwNTSDTG-------------WAKSAWSSVFSPWiqGA 296
Cdd:PRK08751 211 AFLQYTGGTTGVAKGAMLTHRNLVANMQQAHQ-WLAGT------GKLEEGcevvitalplyhiFALTANGLVFMKI--GG 281
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544134 297 CvftHHL---PRFEPTSIlQTLSKYPITVFCSAPTVYRMLVQN-DITSYKFKSLKHCVSAGEPITPDVTEKWRNKTGLDI 372
Cdd:PRK08751 282 C---NHLisnPRDMPGFV-KELKKTRFTAFTGVNTLFNGLLNTpGFDQIDFSSLKMTLGGGMAVQRSVAERWKQVTGLTL 357
|
330 340 350
....*....|....*....|....*....|....*.
gi 42544134 373 YEGYGQTETV-LICGNFKGMKIKPGSMGKPSPAFDV 407
Cdd:PRK08751 358 VEAYGLTETSpAACINPLTLKEYNGSIGLPIPSTDA 393
|
|
| LC_FACS_bac |
cd05932 |
Bacterial long-chain fatty acid CoA synthetase (LC-FACS), including Marinobacter ... |
89-409 |
7.00e-13 |
|
Bacterial long-chain fatty acid CoA synthetase (LC-FACS), including Marinobacter hydrocarbonoclasticus isoprenoid Coenzyme A synthetase; The members of this family are bacterial long-chain fatty acid CoA synthetase. Marinobacter hydrocarbonoclasticus isoprenoid Coenzyme A synthetase in this family is involved in the synthesis of isoprenoid wax ester storage compounds when grown on phytol as the sole carbon source. LC-FACS catalyzes the formation of fatty acyl-CoA in a two-step reaction: the formation of a fatty acyl-AMP molecule as an intermediate, and the formation of a fatty acyl-CoA. Free fatty acids must be "activated" to their CoA thioesters before participating in most catabolic and anabolic reactions.
Pssm-ID: 341255 [Multi-domain] Cd Length: 508 Bit Score: 70.19 E-value: 7.00e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544134 89 NGEEMRWSFEELGSLSRKFANILsEACSLQRGDRVILILPRVPEWWLANVACLRTGTVLIPGTTQLTQKDILYRLQSSKA 168
Cdd:cd05932 1 GGQVVEFTWGEVADKARRLAAAL-RALGLEPGSKIALISKNCAEWFITDLAIWMAGHISVPLYPTLNPDTIRYVLEHSES 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544134 169 NCIIT-----NDVLAPAV-DAVASKCENLHSKLivseNSREGWgnlKELMKHASDSHTCVKTKHNEIMAIFFTSGTSGYP 242
Cdd:cd05932 80 KALFVgklddWKAMAPGVpEGLISISLPPPSAA----NCQYQW---DDLIAQHPPLEERPTRFPEQLATLIYTSGTTGQP 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544134 243 KMTAHTHSSFGLGLSvNGRFWLDLTPSDVMWntSDTGWAKSAWSS-VFSPWIQGACV--FTHHLPRFeptsiLQTLSKYP 319
Cdd:cd05932 153 KGVMLTFGSFAWAAQ-AGIEHIGTEENDRML--SYLPLAHVTERVfVEGGSLYGGVLvaFAESLDTF-----VEDVQRAR 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544134 320 ITVFCSAP---TVYRMLVQNDITSYKFKSL----------KHCVSAG-------------EPITPDVTEkWRNKTGLDIY 373
Cdd:cd05932 225 PTLFFSVPrlwTKFQQGVQDKIPQQKLNLLlkipvvnslvKRKVLKGlgldqcrlagcgsAPVPPALLE-WYRSLGLNIL 303
|
330 340 350
....*....|....*....|....*....|....*.
gi 42544134 374 EGYGQTETVLICGNFKGMKIKPGSMGKPSPAFDVKV 409
Cdd:cd05932 304 EAYGMTENFAYSHLNYPGRDKIGTVGNAGPGVEVRI 339
|
|
| A_NRPS_GliP_like |
cd17653 |
nonribosomal peptide synthase GliP-like; This family includes the adenylation (A) domain of ... |
94-410 |
7.77e-13 |
|
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: 69.65 E-value: 7.77e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544134 94 RWSFEELGSLSRKFANILSEAcSLQRGDRVILILPRVPEWWLANVACLRTGTVLIPGTTQLTQKDILYRLQSSKANCIIT 173
Cdd:cd17653 22 SLTYGELDAASNALANRLLQL-GVVPGDVVPLLSDRSLEMLVAILAILKAGAAYVPLDAKLPSARIQAILRTSGATLLLT 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544134 174 NDvlapAVDAVAskcenlhsklivsensregwgnlkelmkhasdshtcvktkhneimAIFFTSGTSGYPKMTAHTHSSFg 253
Cdd:cd17653 101 TD----SPDDLA---------------------------------------------YIIFTSGSTGIPKGVMVPHRGV- 130
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544134 254 LGLSVNGRFWLDLTPSDVMWNTSDTGWAKSAWsSVFSPWIQGAcvfthHLPRFEPTSILQTLSKyPITVFCSAPTVYRML 333
Cdd:cd17653 131 LNYVSQPPARLDVGPGSRVAQVLSIAFDACIG-EIFSTLCNGG-----TLVLADPSDPFAHVAR-TVDALMSTPSILSTL 203
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 42544134 334 VQNDitsykFKSLKHCVSAGEPITPDVTEKWRNktGLDIYEGYGQTETVLICGNFKGMKIKPGSMGKPSPAFDVKVC 410
Cdd:cd17653 204 SPQD-----FPNLKTIFLGGEAVPPSLLDRWSP--GRRLYNAYGPTECTISSTMTELLPGQPVTIGKPIPNSTCYIL 273
|
|
| PRK13390 |
PRK13390 |
acyl-CoA synthetase; Provisional |
78-410 |
1.07e-12 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 139538 [Multi-domain] Cd Length: 501 Bit Score: 69.65 E-value: 1.07e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544134 78 PSNPAFWwINRNGEEMrwSFEELGSLSRKFANILSEAcSLQRGDRVILILPRVPEWWLANVACLRTGTVLIPGTTQLTQK 157
Cdd:PRK13390 11 PDRPAVI-VAETGEQV--SYRQLDDDSAALARVLYDA-GLRTGDVVALLSDNSPEALVVLWAALRSGLYITAINHHLTAP 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544134 158 DILYRLQSSKANCIitndVLAPAVDAVASKCENLHSKLIVSENSREGWGNLKELMKHASDSHTcvKTKHNEIMaiFFTSG 237
Cdd:PRK13390 87 EADYIVGDSGARVL----VASAALDGLAAKVGADLPLRLSFGGEIDGFGSFEAALAGAGPRLT--EQPCGAVM--LYSSG 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544134 238 TSGYPK-----MTAHTHSSFGLGLSVNGRFWLDLTPSDVMWNTSDTGWAKS-AWSSVFSPwIQGACVFTHhlpRFEPTSI 311
Cdd:PRK13390 159 TTGFPKgiqpdLPGRDVDAPGDPIVAIARAFYDISESDIYYSSAPIYHAAPlRWCSMVHA-LGGTVVLAK---RFDAQAT 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544134 312 LQTLSKYPITVFCSAPTVY-RMLVQND--ITSYKFKSLKHCVSAGEPITPDVTEKWRNKTGLDIYEGYGQTE----TVLI 384
Cdd:PRK13390 235 LGHVERYRITVTQMVPTMFvRLLKLDAdvRTRYDVSSLRAVIHAAAPCPVDVKHAMIDWLGPIVYEYYSSTEahgmTFID 314
|
330 340
....*....|....*....|....*.
gi 42544134 385 CGNFKGmkiKPGSMGKpSPAFDVKVC 410
Cdd:PRK13390 315 SPDWLA---HPGSVGR-SVLGDLHIC 336
|
|
| PRK12583 |
PRK12583 |
acyl-CoA synthetase; Provisional |
91-409 |
1.11e-12 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 237145 [Multi-domain] Cd Length: 558 Bit Score: 69.80 E-value: 1.11e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544134 91 EEMRWSFEELGSLSRKFANILSeACSLQRGDRVILILPRVPEWWLANVACLRTGTVLIPGTTQLTQKDILYRLQSSKANC 170
Cdd:PRK12583 42 QALRYTWRQLADAVDRLARGLL-ALGVQPGDRVGIWAPNCAEWLLTQFATARIGAILVNINPAYRASELEYALGQSGVRW 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544134 171 IITNDV------------LAPAV---DAVASKCENL-HSKLIVS--ENSREGWGNLKELMKHA---SDSHTCVKT---KH 226
Cdd:PRK12583 121 VICADAfktsdyhamlqeLLPGLaegQPGALACERLpELRGVVSlaPAPPPGFLAWHELQARGetvSREALAERQaslDR 200
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544134 227 NEIMAIFFTSGTSGYPKMTAHTHSSfglgLSVNGRF---WLDLTPSDVM------WNTSDTGWAKSAWSSVfspwiqGAC 297
Cdd:PRK12583 201 DDPINIQYTSGTTGFPKGATLSHHN----ILNNGYFvaeSLGLTEHDRLcvpvplYHCFGMVLANLGCMTV------GAC 270
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544134 298 VFthhLPR--FEPTSILQTLSKYPITVFCSAPTVY-RMLVQNDITSYKFKSLKHCVSAGEPITPDVTEKWRNKTGL-DIY 373
Cdd:PRK12583 271 LV---YPNeaFDPLATLQAVEEERCTALYGVPTMFiAELDHPQRGNFDLSSLRTGIMAGAPCPIEVMRRVMDEMHMaEVQ 347
|
330 340 350
....*....|....*....|....*....|....*....
gi 42544134 374 EGYGQTET---VLICGNFKGMKIKPGSMGKPSPAFDVKV 409
Cdd:PRK12583 348 IAYGMTETspvSLQTTAADDLERRVETVGRTQPHLEVKV 386
|
|
| PRK08974 |
PRK08974 |
long-chain-fatty-acid--CoA ligase FadD; |
72-409 |
1.85e-12 |
|
long-chain-fatty-acid--CoA ligase FadD;
Pssm-ID: 236359 [Multi-domain] Cd Length: 560 Bit Score: 68.93 E-value: 1.85e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544134 72 EKAGKK-PSNPAFwwINRnGEEMrwSFEELGSLSRKFANILSEACSLQRGDRVILILPRVPEWWLANVACLRTGTVLIPG 150
Cdd:PRK08974 30 EQAVARyADQPAF--INM-GEVM--TFRKLEERSRAFAAYLQNGLGLKKGDRVALMMPNLLQYPIALFGILRAGMIVVNV 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544134 151 TTQLTQKDILYRLQSSKANCIITNDVLAPAVDAVASKCENLHSKLI-VSENSREGWGNL--------KELMK--HASDSH 219
Cdd:PRK08974 105 NPLYTPRELEHQLNDSGAKAIVIVSNFAHTLEKVVFKTPVKHVILTrMGDQLSTAKGTLvnfvvkyiKRLVPkyHLPDAI 184
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544134 220 TCVKTKH-------------NEIMAIF-FTSGTSGYPKMTAHTHSsfglglsvngrfwldltpsDVMWNTSDTGWAKSAW 285
Cdd:PRK08974 185 SFRSALHkgrrmqyvkpelvPEDLAFLqYTGGTTGVAKGAMLTHR-------------------NMLANLEQAKAAYGPL 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544134 286 SSVFSPWIQGA------------CVFTHHL---------PRFEPTSIlQTLSKYPITVFCSAPTVYRMLVQN-DITSYKF 343
Cdd:PRK08974 246 LHPGKELVVTAlplyhifaltvnCLLFIELggqnllitnPRDIPGFV-KELKKYPFTAITGVNTLFNALLNNeEFQELDF 324
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 42544134 344 KSLKHCVSAGEPITPDVTEKWRNKTGLDIYEGYGQTE-TVLICGNFKGMKIKPGSMGKPSPAFDVKV 409
Cdd:PRK08974 325 SSLKLSVGGGMAVQQAVAERWVKLTGQYLLEGYGLTEcSPLVSVNPYDLDYYSGSIGLPVPSTEIKL 391
|
|
| PRK05677 |
PRK05677 |
long-chain-fatty-acid--CoA ligase; Validated |
96-409 |
5.20e-12 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 168170 [Multi-domain] Cd Length: 562 Bit Score: 67.48 E-value: 5.20e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544134 96 SFEELGSLSRKFANILSEACSLQRGDRVILILPRVPEWWLANVACLRTGTVLIPGTTQLTQKDILYRLQSSKANCIITND 175
Cdd:PRK05677 51 TYGELYKLSGAFAAWLQQHTDLKPGDRIAVQLPNVLQYPVAVFGAMRAGLIVVNTNPLYTAREMEHQFNDSGAKALVCLA 130
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544134 176 VLAPAVDAVASKCENLHskLIVSENSrEGWGNLKELMKHASDSH----------------------------TCVKTKHN 227
Cdd:PRK05677 131 NMAHLAEKVLPKTGVKH--VIVTEVA-DMLPPLKRLLINAVVKHvkkmvpayhlpqavkfndalakgagqpvTEANPQAD 207
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544134 228 EIMAIFFTSGTSGYPKMTAHTHSSfglgLSVNgrfWLDLTP--SDVMWNTSDTGWAKSAWSSVFSpwiqgacvFTHHL-- 303
Cdd:PRK05677 208 DVAVLQYTGGTTGVAKGAMLTHRN----LVAN---MLQCRAlmGSNLNEGCEILIAPLPLYHIYA--------FTFHCma 272
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544134 304 -------------PRFEPtSILQTLSKYPITVFCSAPTVYRMLVQN-DITSYKFKSLKHCVSAGEPITPDVTEKWRNKTG 369
Cdd:PRK05677 273 mmlignhnilisnPRDLP-AMVKELGKWKFSGFVGLNTLFVALCNNeAFRKLDFSALKLTLSGGMALQLATAERWKEVTG 351
|
330 340 350 360
....*....|....*....|....*....|....*....|.
gi 42544134 370 LDIYEGYGQTETV-LICGNFKGmKIKPGSMGKPSPAFDVKV 409
Cdd:PRK05677 352 CAICEGYGMTETSpVVSVNPSQ-AIQVGTIGIPVPSTLCKV 391
|
|
| PRK13391 |
PRK13391 |
acyl-CoA synthetase; Provisional |
78-401 |
6.52e-12 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 184022 [Multi-domain] Cd Length: 511 Bit Score: 67.41 E-value: 6.52e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544134 78 PSNPAFWwINRNGEEMrwSFEELGSLSRKFANILSEAcSLQRGDRVILIL---PRVPEwwlANVACLRTGTVLIPGTTQL 154
Cdd:PRK13391 11 PDKPAVI-MASTGEVV--TYRELDERSNRLAHLFRSL-GLKRGDHVAIFMennLRYLE---VCWAAERSGLYYTCVNSHL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544134 155 TQKDILYRLQSSKANCIITNDVLAPAVDAVASKCENLHSKLIV-SENSREGWGNLKELMKHASDShtcVKTKHNEIMAIF 233
Cdd:PRK13391 84 TPAEAAYIVDDSGARALITSAAKLDVARALLKQCPGVRHRLVLdGDGELEGFVGYAEAVAGLPAT---PIADESLGTDML 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544134 234 FTSGTSGYPK----------------MTAHTHSSFGLGlsvNGRFWLDLTPsdvMWNTsdtgwAKSAWSSVfspwIQ--G 295
Cdd:PRK13391 161 YSSGTTGRPKgikrplpeqppdtplpLTAFLQRLWGFR---SDMVYLSPAP---LYHS-----APQRAVML----VIrlG 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544134 296 ACVFThhLPRFEPTSILQTLSKYPITVFCSAPTVY-RML-VQNDI-TSYKFKSLKHCVSAGEPITPDVTEKWRNKTGLDI 372
Cdd:PRK13391 226 GTVIV--MEHFDAEQYLALIEEYGVTHTQLVPTMFsRMLkLPEEVrDKYDLSSLEVAIHAAAPCPPQVKEQMIDWWGPII 303
|
330 340 350
....*....|....*....|....*....|
gi 42544134 373 YEGYGQTETVLICG-NFKGMKIKPGSMGKP 401
Cdd:PRK13391 304 HEYYAATEGLGFTAcDSEEWLAHPGTVGRA 333
|
|
| PLN02330 |
PLN02330 |
4-coumarate--CoA ligase-like 1 |
95-408 |
2.23e-11 |
|
4-coumarate--CoA ligase-like 1
Pssm-ID: 215189 [Multi-domain] Cd Length: 546 Bit Score: 65.77 E-value: 2.23e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544134 95 WSFEELGSLSRKFANILSeACSLQRGDRVILILPRVPEWWLANVACLRTGTVLIPGTTQLTQKDILYRLQSSKANCIITN 174
Cdd:PLN02330 56 VTYGEVVRDTRRFAKALR-SLGLRKGQVVVVVLPNVAEYGIVALGIMAAGGVFSGANPTALESEIKKQAEAAGAKLIVTN 134
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544134 175 DvlapavdAVASKCENLHSKLIV-SENSREGWGNLKELMK---HASDSHTCVKTKHNEIMAIFFTSGTSGYPKMTAHTH- 249
Cdd:PLN02330 135 D-------TNYGKVKGLGLPVIVlGEEKIEGAVNWKELLEaadRAGDTSDNEEILQTDLCALPFSSGTTGISKGVMLTHr 207
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544134 250 --------SSFGLGLSVNGRF-WLDLTPSDVMWNtsdtgwaksawssvfspwIQGACVFTHH-------LPRFEPTSILQ 313
Cdd:PLN02330 208 nlvanlcsSLFSVGPEMIGQVvTLGLIPFFHIYG------------------ITGICCATLRnkgkvvvMSRFELRTFLN 269
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544134 314 TLSKYPITVFCSAPTVYRMLVQN------DITSYKFKSLkhcVSAGEPITPDVTEKWRNK-TGLDIYEGYGQTETVLICG 386
Cdd:PLN02330 270 ALITQEVSFAPIVPPIILNLVKNpiveefDLSKLKLQAI---MTAAAPLAPELLTAFEAKfPGVQVQEAYGLTEHSCITL 346
|
330 340
....*....|....*....|....*..
gi 42544134 387 NF----KGMKI-KPGSMGKPSPAFDVK 408
Cdd:PLN02330 347 THgdpeKGHGIaKKNSVGFILPNLEVK 373
|
|
| LC_FACS_like |
cd17640 |
Long-chain fatty acid CoA synthetase; This family includes long-chain fatty acid (C12-C20) CoA ... |
94-409 |
4.28e-11 |
|
Long-chain fatty acid CoA synthetase; This family includes long-chain fatty acid (C12-C20) CoA synthetases, including an Arabidopsis gene At4g14070 that plays a role in activation and elongation of exogenous fatty acids. FACS catalyzes the formation of fatty acyl-CoA in a two-step reaction: the formation of a fatty acyl-AMP molecule as an intermediate, and the formation of a fatty acyl-CoA. Eukaryotes generally have multiple isoforms of LC-FACS genes with multiple splice variants. For example, nine genes are found in Arabidopsis and six genes are expressed in mammalian cells. Free fatty acids must be "activated" to their CoA thioesters before participating in most catabolic and anabolic reactions.
Pssm-ID: 341295 [Multi-domain] Cd Length: 468 Bit Score: 64.69 E-value: 4.28e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544134 94 RWSFEELGSLSRKFANILsEACSLQRGDRVILILPRVPEWWLANVACLRTGTVLIPGTTQLTQKDILYRLQSSKanciit 173
Cdd:cd17640 5 RITYKDLYQEILDFAAGL-RSLGVKAGEKVALFADNSPRWLIADQGIMALGAVDVVRGSDSSVEELLYILNHSE------ 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544134 174 ndvlapavdavaskcenlhSKLIVSENSregwgnlkelmkhasdshtcvktkHNEIMAIFFTSGTSGYPKMTAHTHSSF- 252
Cdd:cd17640 78 -------------------SVALVVEND------------------------SDDLATIIYTSGTTGNPKGVMLTHANLl 114
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544134 253 --------GLGLSVNGRFwLDLTPSdvmWNTSDtgwaKSAWSSVFSpwiQG-ACVFThhlprfEPTSILQTLSKYPITVF 323
Cdd:cd17640 115 hqirslsdIVPPQPGDRF-LSILPI---WHSYE----RSAEYFIFA---CGcSQAYT------SIRTLKDDLKRVKPHYI 177
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544134 324 CSAPTVYRMLVQNDITSYKFKS---------------LKHCVSAGEPITPDVtEKWRNKTGLDIYEGYGQTET--VLICG 386
Cdd:cd17640 178 VSVPRLWESLYSGIQKQVSKSSpikqflflfflsggiFKFGISGGGALPPHV-DTFFEAIGIEVLNGYGLTETspVVSAR 256
|
330 340
....*....|....*....|...
gi 42544134 387 NFKGMKIkpGSMGKPSPAFDVKV 409
Cdd:cd17640 257 RLKCNVR--GSVGRPLPGTEIKI 277
|
|
| PRK07788 |
PRK07788 |
acyl-CoA synthetase; Validated |
96-409 |
5.05e-11 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236097 [Multi-domain] Cd Length: 549 Bit Score: 64.56 E-value: 5.05e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544134 96 SFEELGSLSRKFANILSEACSlqRGDRVILILPRVPEWW-LANVACLRTGTVLI-----PGTTQLtqKDILYRLqssKAN 169
Cdd:PRK07788 76 TYAELDEQSNALARGLLALGV--RAGDGVAVLARNHRGFvLALYAAGKVGARIIllntgFSGPQL--AEVAARE---GVK 148
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544134 170 CIITNDVLAPAVDAVASKCENLHSKLIVSEN---SREGWGNLKELMKHASDSHTCVKTKHNEImaIFFTSGTSGYPKMTA 246
Cdd:PRK07788 149 ALVYDDEFTDLLSALPPDLGRLRAWGGNPDDdepSGSTDETLDDLIAGSSTAPLPKPPKPGGI--VILTSGTTGTPKGAP 226
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544134 247 HTHSSfglGLSVNGRFwLDLTP---SDVMWNTS----DTGWAKSAWSSVFspwiqGACVFTHHlpRFEPTSILQTLSKYP 319
Cdd:PRK07788 227 RPEPS---PLAPLAGL-LSRVPfraGETTLLPApmfhATGWAHLTLAMAL-----GSTVVLRR--RFDPEATLEDIAKHK 295
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544134 320 ITVFCSAPT-VYRML--VQNDITSYKFKSLKHCVSAGEPITPDVTEKWRNKTGLDIYEGYGQTE----TVlicGNFKGMK 392
Cdd:PRK07788 296 ATALVVVPVmLSRILdlGPEVLAKYDTSSLKIIFVSGSALSPELATRALEAFGPVLYNLYGSTEvafaTI---ATPEDLA 372
|
330
....*....|....*..
gi 42544134 393 IKPGSMGKPSPAFDVKV 409
Cdd:PRK07788 373 EAPGTVGRPPKGVTVKI 389
|
|
| ACLS-CaiC |
cd17637 |
acyl-CoA synthetase (AMP-forming)/AMP-acid ligase II; This family contains fatty acid CoA ... |
303-409 |
6.51e-11 |
|
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: 63.44 E-value: 6.51e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544134 303 LPRFEPTSILQTLSKYPITVFCS-APTVYRMLVQNDITSYKFKSLKHcVSAGEpiTPDVTEKWRNKTGLDIYEGYGQTET 381
Cdd:cd17637 72 MEKFDPAEALELIEEEKVTLMGSfPPILSNLLDAAEKSGVDLSSLRH-VLGLD--APETIQRFEETTGATFWSLYGQTET 148
|
90 100 110
....*....|....*....|....*....|.
gi 42544134 382 ---VLICGNFKgmkiKPGSMGKPSPAFDVKV 409
Cdd:cd17637 149 sglVTLSPYRE----RPGSAGRPGPLVRVRI 175
|
|
| A_NRPS_Srf_like |
cd12117 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including Bacillus subtilis ... |
91-381 |
7.34e-11 |
|
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: 63.76 E-value: 7.34e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544134 91 EEMRWSFEELGSLSRKFANILSEAcSLQRGDRVILILPRVPEWWLANVACLRTGTVLIPGTTQLTQKDILYRLQSSKANC 170
Cdd:cd12117 19 GDRSLTYAELNERANRLARRLRAA-GVGPGDVVGVLAERSPELVVALLAVLKAGAAYVPLDPELPAERLAFMLADAGAKV 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544134 171 IITNDVLAPAVDavaskcENLHSKLIVSENSREGWGNLKelmkHASDSHTCvktkhneimA-IFFTSGTSGYPKMTAHTH 249
Cdd:cd12117 98 LLTDRSLAGRAG------GLEVAVVIDEALDAGPAGNPA----VPVSPDDL---------AyVMYTSGSTGRPKGVAVTH 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544134 250 SSFgLGLsVNGRFWLDLTPSDVMWNTSDTGWAKSAWsSVFSPWIQGACVF---THHLPRfePTSILQTLSKYPITV-FCS 325
Cdd:cd12117 159 RGV-VRL-VKNTNYVTLGPDDRVLQTSPLAFDASTF-EIWGALLNGARLVlapKGTLLD--PDALGALIAEEGVTVlWLT 233
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*..
gi 42544134 326 APtVYRMLVQNDITSykFKSLKHCVSAGEPITPDVTEKWRNKT-GLDIYEGYGQTET 381
Cdd:cd12117 234 AA-LFNQLADEDPEC--FAGLRELLTGGEVVSPPHVRRVLAACpGLRLVNGYGPTEN 287
|
|
| PRK09274 |
PRK09274 |
peptide synthase; Provisional |
96-385 |
8.86e-11 |
|
peptide synthase; Provisional
Pssm-ID: 236443 [Multi-domain] Cd Length: 552 Bit Score: 63.76 E-value: 8.86e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544134 96 SFEELGSLSRKFANILSEAcSLQRGDRVILILPRVPEWWLANVACLRTG--TVLI-PGttqLTQKDILYRLQSSKANCII 172
Cdd:PRK09274 43 SFAELDARSDAIAHGLNAA-GIGRGMRAVLMVTPSLEFFALTFALFKAGavPVLVdPG---MGIKNLKQCLAEAQPDAFI 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544134 173 TNDvLApavdAVAS-----KCENLHSKLIVSenSREGWGN--LKELMKHASD-SHTCVKTKHNEIMAIFFTSGTSGYPKM 244
Cdd:PRK09274 119 GIP-KA----HLARrlfgwGKPSVRRLVTVG--GRLLWGGttLATLLRDGAAaPFPMADLAPDDMAAILFTSGSTGTPKG 191
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544134 245 TAHTHSSF---------GLGLSVNGRfwlDLTPSDVMwntsdtgwaksawsSVFSPWIQGACVfthhLPRFEPT------ 309
Cdd:PRK09274 192 VVYTHGMFeaqiealreDYGIEPGEI---DLPTFPLF--------------ALFGPALGMTSV----IPDMDPTrpatvd 250
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544134 310 --SILQTLSKYPITVFCSAPTVYRML----VQNDItsyKFKSLKHCVSAGEPITPDVTEKWRN--KTGLDIYEGYGQTET 381
Cdd:PRK09274 251 paKLFAAIERYGVTNLFGSPALLERLgrygEANGI---KLPSLRRVISAGAPVPIAVIERFRAmlPPDAEILTPYGATEA 327
|
....
gi 42544134 382 VLIC 385
Cdd:PRK09274 328 LPIS 331
|
|
| FACL_like_6 |
cd05922 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
117-407 |
1.24e-10 |
|
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: 63.23 E-value: 1.24e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544134 117 LQRGDRVILILPRVPE--WWLANV--ACLRTGTVLIPGTTQLTQKDILYRLQSSKANCIITNDVLAPAVDAVASKCENlh 192
Cdd:cd05922 15 GVRGERVVLILPNRFTyiELSFAVayAGGRLGLVFVPLNPTLKESVLRYLVADAGGRIVLADAGAADRLRDALPASPD-- 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544134 193 SKLIVSEnsrEGWgnlkelmKHASDSHTCVKTKHNEIMAIFFTSGTSGYPKMTAHTHSSFGLGL-SVNGRfwLDLTPSDV 271
Cdd:cd05922 93 PGTVLDA---DGI-------RAARASAPAHEVSHEDLALLLYTSGSTGSPKLVRLSHQNLLANArSIAEY--LGITADDR 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544134 272 MWNTSDTGWAkSAWSSVFSPWIQGACVFTHHLPRFePTSILQTLSKYPITVFCSAPTVYRMLVQNDITSYKFKSLKHCVS 351
Cdd:cd05922 161 ALTVLPLSYD-YGLSVLNTHLLRGATLVLTNDGVL-DDAFWEDLREHGATGLAGVPSTYAMLTRLGFDPAKLPSLRYLTQ 238
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 42544134 352 AGEPITPDVTEKWRNK-TGLDIYEGYGQTETvlicgnFKGMKI--------KPGSMGKPSP--AFDV 407
Cdd:cd05922 239 AGGRLPQETIARLRELlPGAQVYVMYGQTEA------TRRMTYlpperileKPGSIGLAIPggEFEI 299
|
|
| A_NRPS_PvdJ-like |
cd17649 |
non-ribosomal peptide synthetase; This family of the adenylation (A) domain of nonribosomal ... |
217-382 |
1.88e-10 |
|
non-ribosomal peptide synthetase; This family of the adenylation (A) domain of nonribosomal peptide synthases (NRPS) includes pyoverdine biosynthesis protein PvdJ involved in the synthesis of pyoverdine, which consists of a chromophore group attached to a variable peptide chain and comprises around 6-12 amino acids that are specific for each Pseudomonas species, and for which the peptide might be first synthesized before the chromophore assembly. Also included is ornibactin biosynthesis protein OrbI; ornibactin is a tetrapeptide siderophore with an l-ornithine-d-hydroxyaspartate-l-serine-l-ornithine backbone. The adenylation domain at the N-terminal of OrbI possibly initiates the ornibactin with the binding of N5-hydroxyornithine. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.
Pssm-ID: 341304 [Multi-domain] Cd Length: 450 Bit Score: 62.39 E-value: 1.88e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544134 217 DS-HTCVKTKHNEIMA-IFFTSGTSGYPKMTAHTHSSFGLGLSVNGRFwLDLTPSDVMWNTSDTGWaKSAWSSVFSPWIQ 294
Cdd:cd17649 82 DSgAGLLLTHHPRQLAyVIYTSGSTGTPKGVAVSHGPLAAHCQATAER-YGLTPGDRELQFASFNF-DGAHEQLLPPLIC 159
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544134 295 GACVFTHHLPRFEPTSILQTL-SKYPITVFCSAPTVYRMLVQ--NDITSYKFKSLKHCVSAGEPITPDVTEKWRnKTGLD 371
Cdd:cd17649 160 GACVVLRPDELWASADELAEMvRELGVTVLDLPPAYLQQLAEeaDRTGDGRPPSLRLYIFGGEALSPELLRRWL-KAPVR 238
|
170
....*....|.
gi 42544134 372 IYEGYGQTETV 382
Cdd:cd17649 239 LFNAYGPTEAT 249
|
|
| PRK08633 |
PRK08633 |
2-acyl-glycerophospho-ethanolamine acyltransferase; Validated |
221-409 |
6.33e-10 |
|
2-acyl-glycerophospho-ethanolamine acyltransferase; Validated
Pssm-ID: 236315 [Multi-domain] Cd Length: 1146 Bit Score: 61.48 E-value: 6.33e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544134 221 CVKTKHNE-IMAIFFTSGTSGYPK--MTAHT----------------------------HSsfgLGLSVNgrFWLdltps 269
Cdd:PRK08633 775 YGPTFKPDdTATIIFSSGSEGEPKgvMLSHHnilsnieqisdvfnlrnddvilsslpffHS---FGLTVT--LWL----- 844
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544134 270 dvmwntsdtgwaksawssvfsPWIQGACVFTHHLPrFEPTSILQTLSKYPITVFCSAPTVYRMLVQND-ITSYKFKSLKH 348
Cdd:PRK08633 845 ---------------------PLLEGIKVVYHPDP-TDALGIAKLVAKHRATILLGTPTFLRLYLRNKkLHPLMFASLRL 902
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 42544134 349 CVSAGEPITPDVTEKWRNKTGLDIYEGYGQTET----------VLICGNFKGMKIKPGSMGKPSPAFDVKV 409
Cdd:PRK08633 903 VVAGAEKLKPEVADAFEEKFGIRILEGYGATETspvasvnlpdVLAADFKRQTGSKEGSVGMPLPGVAVRI 973
|
|
| PRK08162 |
PRK08162 |
acyl-CoA synthetase; Validated |
91-381 |
1.27e-09 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236169 [Multi-domain] Cd Length: 545 Bit Score: 59.96 E-value: 1.27e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544134 91 EEMRWSFEELGSLSRKFANILSEAcSLQRGDRVILILPRVPEWWLANVACLRTGTVLIPGTTQLTQKDILYRLQSSKANC 170
Cdd:PRK08162 40 GDRRRTWAETYARCRRLASALARR-GIGRGDTVAVLLPNIPAMVEAHFGVPMAGAVLNTLNTRLDAASIAFMLRHGEAKV 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544134 171 IITNDVLAPAVDAVASKCENLhsKLIV--------SENSREGWGNLKELMKHAsDSHTCVKTKHNEIMAIF--FTSGTSG 240
Cdd:PRK08162 119 LIVDTEFAEVAREALALLPGP--KPLVidvddpeyPGGRFIGALDYEAFLASG-DPDFAWTLPADEWDAIAlnYTSGTTG 195
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544134 241 YPKMTAHTHSSFGLGLSVNGRFWlDLTPSDV-MW-------NtsdtGWAksawssvFsPWIQGACVFTH-HLPRFEPTSI 311
Cdd:PRK08162 196 NPKGVVYHHRGAYLNALSNILAW-GMPKHPVyLWtlpmfhcN----GWC-------F-PWTVAARAGTNvCLRKVDPKLI 262
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 42544134 312 LQTLSKYPITVFCSAPTVYRMLVqNDITSYKfKSLKHCVS---AGEPITPDVTEKWRNkTGLDIYEGYGQTET 381
Cdd:PRK08162 263 FDLIREHGVTHYCGAPIVLSALI-NAPAEWR-AGIDHPVHamvAGAAPPAAVIAKMEE-IGFDLTHVYGLTET 332
|
|
| PTZ00237 |
PTZ00237 |
acetyl-CoA synthetase; Provisional |
232-403 |
1.46e-09 |
|
acetyl-CoA synthetase; Provisional
Pssm-ID: 240325 [Multi-domain] Cd Length: 647 Bit Score: 60.14 E-value: 1.46e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544134 232 IFFTSGTSGYPKMTAHTHSSFGLGLSVNGRFWLDLTPSDVMWNTSDTGWAKsawssvFSPWIQGACVFTHHLPRFE---- 307
Cdd:PTZ00237 259 ILYTSGTTGNSKAVVRSNGPHLVGLKYYWRSIIEKDIPTVVFSHSSIGWVS------FHGFLYGSLSLGNTFVMFEggii 332
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544134 308 -----PTSILQTLSKYPITVFCSAPTVYRMLVQND-----ITS-YKFKSLKHCVSAGEPITPDVTEKWRNKTGLDIYEGY 376
Cdd:PTZ00237 333 knkhiEDDLWNTIEKHKVTHTLTLPKTIRYLIKTDpeatiIRSkYDLSNLKEIWCGGEVIEESIPEYIENKLKIKSSRGY 412
|
170 180 190
....*....|....*....|....*....|
gi 42544134 377 GQTE---TVLICgnFKGMKIKPGSMGKPSP 403
Cdd:PTZ00237 413 GQTEigiTYLYC--YGHINIPYNATGVPSI 440
|
|
| AFD_YhfT-like |
cd17633 |
fatty acid-CoA ligase VraA; This family of acyl-CoA ligases includes Bacillus subtilis YhfT, ... |
234-410 |
1.51e-09 |
|
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: 58.96 E-value: 1.51e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544134 234 FTSGTSGYPKMTAHTHSSfglglsvngrfWLDLTPSDVMwntsdtGWAKSAWSSVFSPwiqGACVFTHHL---------- 303
Cdd:cd17633 7 FTSGTTGLPKAYYRSERS-----------WIESFVCNED------LFNISGEDAILAP---GPLSHSLFLygaisalylg 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544134 304 ------PRFEPTSILQTLSKYPITVFCSAPTVYRMLVQNDITSYKFKSLkhcVSAGEPITPDVTEKWRNKT-GLDIYEGY 376
Cdd:cd17633 67 gtfigqRKFNPKSWIRKINQYNATVIYLVPTMLQALARTLEPESKIKSI---FSSGQKLFESTKKKLKNIFpKANLIEFY 143
|
170 180 190
....*....|....*....|....*....|....
gi 42544134 377 GQTETVLICGNFKGMKIKPGSMGKPSPAFDVKVC 410
Cdd:cd17633 144 GTSELSFITYNFNQESRPPNSVGRPFPNVEIEIR 177
|
|
| PRK12406 |
PRK12406 |
long-chain-fatty-acid--CoA ligase; Provisional |
94-409 |
1.76e-09 |
|
long-chain-fatty-acid--CoA ligase; Provisional
Pssm-ID: 183506 [Multi-domain] Cd Length: 509 Bit Score: 59.71 E-value: 1.76e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544134 94 RWSFEELGSLSRKFANILSeACSLQRGDRVILILPRVPEWWLANVACLRTGTVLIPGTTQLTQKDILYRLQSSKANCIIT 173
Cdd:PRK12406 11 RRSFDELAQRAARAAGGLA-ALGVRPGDCVALLMRNDFAFFEAAYAAMRLGAYAVPVNWHFKPEEIAYILEDSGARVLIA 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544134 174 N-DVLAPAVDAVASKCENLH--------SKLIVSENSR---------EGWgnlkeLMKHASDSHTCVKTKHNEImaifFT 235
Cdd:PRK12406 90 HaDLLHGLASALPAGVTVLSvptppeiaAAYRISPALLtppagaidwEGW-----LAQQEPYDGPPVPQPQSMI----YT 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544134 236 SGTSGYPK------MTAHTHSSFGL------GLSVNGRFWLdltpSDVMWNTSDTGWAksawssVFSPWIQGACVFthhL 303
Cdd:PRK12406 161 SGTTGHPKgvrraaPTPEQAAAAEQmraliyGLKPGIRALL----TGPLYHSAPNAYG------LRAGRLGGVLVL---Q 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544134 304 PRFEPTSILQTLSKYPITVFCSAPTVY-RML-----VQNditSYKFKSLKHCVSAGEPITPDVT----EKWrnktGLDIY 373
Cdd:PRK12406 228 PRFDPEELLQLIERHRITHMHMVPTMFiRLLklpeeVRA---KYDVSSLRHVIHAAAPCPADVKramiEWW----GPVIY 300
|
330 340 350
....*....|....*....|....*....|....*...
gi 42544134 374 EGYGQTET--VLICGNFKGMKiKPGSMGKPSPAFDVKV 409
Cdd:PRK12406 301 EYYGSTESgaVTFATSEDALS-HPGTVGKAAPGAELRF 337
|
|
| A_NRPS_SidN3_like |
cd05918 |
The adenylation (A) domain of siderophore-synthesizing nonribosomal peptide synthetases (NRPS); ... |
225-404 |
2.00e-09 |
|
The adenylation (A) domain of siderophore-synthesizing nonribosomal peptide synthetases (NRPS); The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. This family of siderophore-synthesizing NRPS includes the third adenylation domain of SidN from the endophytic fungus Neotyphodium lolii, ferrichrome siderophore synthetase, HC-toxin synthetase, and enniatin synthase. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.
Pssm-ID: 341242 [Multi-domain] Cd Length: 481 Bit Score: 59.48 E-value: 2.00e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544134 225 KHNEIMAIFFTSGTSGYPKMTAHTHSSFGLGLSVNGRFwLDLTPS-----------DVMWNtsdtgwaksawsSVFSPWI 293
Cdd:cd05918 104 SPSDAAYVIFTSGSTGKPKGVVIEHRALSTSALAHGRA-LGLTSEsrvlqfasytfDVSIL------------EIFTTLA 170
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544134 294 QGACVFT-------HHLPRFeptsilqtLSKYPITVFCSAPTVYRMLVQNDITSykfksLKHCVSAGEPITPDVTEKWRN 366
Cdd:cd05918 171 AGGCLCIpseedrlNDLAGF--------INRLRVTWAFLTPSVARLLDPEDVPS-----LRTLVLGGEALTQSDVDTWAD 237
|
170 180 190
....*....|....*....|....*....|....*....
gi 42544134 367 KTGLdiYEGYGQTE-TVLICGNFKGMKIKPGSMGKPSPA 404
Cdd:cd05918 238 RVRL--INAYGPAEcTIAATVSPVVPSTDPRNIGRPLGA 274
|
|
| PRK07059 |
PRK07059 |
Long-chain-fatty-acid--CoA ligase; Validated |
96-407 |
2.26e-09 |
|
Long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 235923 [Multi-domain] Cd Length: 557 Bit Score: 59.26 E-value: 2.26e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544134 96 SFEELGSLSRKFANILsEACSLQRGDRVILILPRVPEWWLANVACLRTGTVLIPGTTQLTQKDILYRLQSSKANCIITND 175
Cdd:PRK07059 50 TYGELDELSRALAAWL-QSRGLAKGARVAIMMPNVLQYPVAIAAVLRAGYVVVNVNPLYTPRELEHQLKDSGAEAIVVLE 128
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544134 176 VLAPAVDAVASKCE--------------------NL---HSKLIVSENSREGWGNLKE-LMKHASDSHTCVKTKHNEIMA 231
Cdd:PRK07059 129 NFATTVQQVLAKTAvkhvvvasmgdllgfkghivNFvvrRVKKMVPAWSLPGHVRFNDaLAEGARQTFKPVKLGPDDVAF 208
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544134 232 IFFTSGTSGYPKMTAHTHSSFglglsvngrfwldltPSDVMWNTSdtgWAKSAWSSvfsPWIQGACVFTHHLP------- 304
Cdd:PRK07059 209 LQYTGGTTGVSKGATLLHRNI---------------VANVLQMEA---WLQPAFEK---KPRPDQLNFVCALPlyhifal 267
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544134 305 --------RFEPTSIL-----------QTLSKYPITVFCSAPTVYRMLVQN-DITSYKFKSLKHCVSAGEPITPDVTEKW 364
Cdd:PRK07059 268 tvcgllgmRTGGRNILipnprdipgfiKELKKYQVHIFPAVNTLYNALLNNpDFDKLDFSKLIVANGGGMAVQRPVAERW 347
|
330 340 350 360
....*....|....*....|....*....|....*....|....*
gi 42544134 365 RNKTGLDIYEGYGQTET--VLICGNFKGMKIKpGSMGKPSPAFDV 407
Cdd:PRK07059 348 LEMTGCPITEGYGLSETspVATCNPVDATEFS-GTIGLPLPSTEV 391
|
|
| PRK13382 |
PRK13382 |
bile acid CoA ligase; |
232-409 |
5.56e-09 |
|
bile acid CoA ligase;
Pssm-ID: 172019 [Multi-domain] Cd Length: 537 Bit Score: 58.23 E-value: 5.56e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544134 232 IFFTSGTSGYPKMTAHTHSSFGLGLSVngrfWLDLTPsdvmWNTSDTGWAKSAwssVFSPWIQGACVFTHHLP------- 304
Cdd:PRK13382 201 ILLTSGTTGTPKGARRSGPGGIGTLKA----ILDRTP----WRAEEPTVIVAP---MFHAWGFSQLVLAASLActivtrr 269
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544134 305 RFEPTSILQTLSKYPITVFCSAPTVYRM---LVQNDITSYKFKSLKHCVSAGEPITPDVTEKWRNKTGLDIYEGYGQTET 381
Cdd:PRK13382 270 RFDPEATLDLIDRHRATGLAVVPVMFDRimdLPAEVRNRYSGRSLRFAAASGSRMRPDVVIAFMDQFGDVIYNNYNATEA 349
|
170 180
....*....|....*....|....*....
gi 42544134 382 VLIC-GNFKGMKIKPGSMGKPSPAFDVKV 409
Cdd:PRK13382 350 GMIAtATPADLRAAPDTAGRPAEGTEIRI 378
|
|
| PRK12492 |
PRK12492 |
long-chain-fatty-acid--CoA ligase; Provisional |
96-409 |
6.83e-09 |
|
long-chain-fatty-acid--CoA ligase; Provisional
Pssm-ID: 171539 [Multi-domain] Cd Length: 562 Bit Score: 57.91 E-value: 6.83e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544134 96 SFEELGSLSRKFANILSEACSLQRGDRVILILPRVPEWWLANVACLRTGTVLIPGTTQLTQKDILYRLQSSKANCIITND 175
Cdd:PRK12492 51 SYAELERHSAAFAAYLQQHTDLVPGDRIAVQMPNVLQYPIAVFGALRAGLIVVNTNPLYTAREMRHQFKDSGARALVYLN 130
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544134 176 VLAPAVDAVASKCENLH---SKLIVSENSREGW---------------------GNLKELMKHASD-SHTCVKTKHNEIM 230
Cdd:PRK12492 131 MFGKLVQEVLPDTGIEYlieAKMGDLLPAAKGWlvntvvdkvkkmvpayhlpqaVPFKQALRQGRGlSLKPVPVGLDDIA 210
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544134 231 AIFFTSGTSGYPKMTAHTHSSfglgLSVN--------GRFWLDLTPsdVMWNTSDTGWAKSAWSSVFSPWIQGACVF--- 299
Cdd:PRK12492 211 VLQYTGGTTGLAKGAMLTHGN----LVANmlqvraclSQLGPDGQP--LMKEGQEVMIAPLPLYHIYAFTANCMCMMvsg 284
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544134 300 THHLPRFEPTSI---LQTLSKYPITVFCSAPTVYRMLVQN-DITSYKFKSLKHCVSAGEPITPDVTEKWRNKTGLDIYEG 375
Cdd:PRK12492 285 NHNVLITNPRDIpgfIKELGKWRFSALLGLNTLFVALMDHpGFKDLDFSALKLTNSGGTALVKATAERWEQLTGCTIVEG 364
|
330 340 350
....*....|....*....|....*....|....*
gi 42544134 376 YGQTETV-LICGNFKGMKIKPGSMGKPSPAFDVKV 409
Cdd:PRK12492 365 YGLTETSpVASTNPYGELARLGTVGIPVPGTALKV 399
|
|
| hsFATP2a_ACSVL_like |
cd05938 |
Fatty acid transport proteins (FATP) including hsFATP2, hsFATP5, and hsFATP6, and similar ... |
91-402 |
8.45e-09 |
|
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: 57.30 E-value: 8.45e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544134 91 EEMRWSFEELGSLSRKFANILSEACSLQRGDRVILILPRVPEW---WLAnVACLRTGTVLIPgtTQLTQKDILYRLQSSK 167
Cdd:cd05938 2 EGETYTYRDVDRRSNQAARALLAHAGLRPGDTVALLLGNEPAFlwiWLG-LAKLGCPVAFLN--TNIRSKSLLHCFRCCG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544134 168 ANCIITNDVLAPAVDAV--ASKCENLHSKLIVSENSREGWGNLKELMKHASD--------SHTCVKTKhneimAIF-FTS 236
Cdd:cd05938 79 AKVLVVAPELQEAVEEVlpALRADGVSVWYLSHTSNTEGVISLLDKVDAASDepvpaslrAHVTIKSP-----ALYiYTS 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544134 237 GTSGYPKMTAHTHSSFglgLSVNGRFWL-DLTPSDVMWNTSDTgWAKSAWSSVFSPWIQ-GA-CVFThhlPRFEPTSILQ 313
Cdd:cd05938 154 GTTGLPKAARISHLRV---LQCSGFLSLcGVTADDVIYITLPL-YHSSGFLLGIGGCIElGAtCVLK---PKFSASQFWD 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544134 314 TLSKYPITVFCSAPTVYRMLVQndiTSYKFKSLKHCV--SAGEPITPDVTEKWRNKTG-LDIYEGYGQTETVLICGNFKG 390
Cdd:cd05938 227 DCRKHNVTVIQYIGELLRYLCN---QPQSPNDRDHKVrlAIGNGLRADVWREFLRRFGpIRIREFYGSTEGNIGFFNYTG 303
|
330
....*....|..
gi 42544134 391 mkiKPGSMGKPS 402
Cdd:cd05938 304 ---KIGAVGRVS 312
|
|
| FadD3 |
cd17638 |
acyl-CoA synthetase FadD3 and similar proteins; This family contains long chain fatty acid CoA ... |
228-409 |
9.91e-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: 56.74 E-value: 9.91e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544134 228 EIMAIFFTSGTSGYPK--MTAHTHSsfgLGLSVNgrfWldltpSDVMWNTSDTGWA-----------KSAWSSVFspwIQ 294
Cdd:cd17638 1 DVSDIMFTSGTTGRSKgvMCAHRQT---LRAAAA---W-----ADCADLTEDDRYLiinpffhtfgyKAGIVACL---LT 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544134 295 GACVFTHHLprFEPTSILQTLSKYPITVFCSAPTVYR-MLVQNDITSYKFKSLKHCVSAGEPITPDVTEKWRNKTGLD-I 372
Cdd:cd17638 67 GATVVPVAV--FDVDAILEAIERERITVLPGPPTLFQsLLDHPGRKKFDLSSLRAAVTGAATVPVELVRRMRSELGFEtV 144
|
170 180 190
....*....|....*....|....*....|....*....
gi 42544134 373 YEGYGQTE--TVLICGNFKGMKIKPGSMGKPSPAFDVKV 409
Cdd:cd17638 145 LTAYGLTEagVATMCRPGDDAETVATTCGRACPGFEVRI 183
|
|
| entF |
PRK10252 |
enterobactin non-ribosomal peptide synthetase EntF; |
96-380 |
1.19e-08 |
|
enterobactin non-ribosomal peptide synthetase EntF;
Pssm-ID: 236668 [Multi-domain] Cd Length: 1296 Bit Score: 57.36 E-value: 1.19e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544134 96 SFEELGSLSRKFANILSEAcSLQRGDRVILILPRVPEWWLANVACLRTGTVLIPGTTQLTQKDILYRLQSSKANCIITND 175
Cdd:PRK10252 485 SYREMREQVVALANLLRER-GVKPGDSVAVALPRSVFLTLALHAIVEAGAAWLPLDTGYPDDRLKMMLEDARPSLLITTA 563
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544134 176 VLA---PAVDAVASKCENlhSKLIVSENSREGWGnlkelmkhaSDSHTCVktkhneimaIFFTSGTSGYPKMTAHTHSSF 252
Cdd:PRK10252 564 DQLprfADVPDLTSLCYN--APLAPQGAAPLQLS---------QPHHTAY---------IIFTSGSTGRPKGVMVGQTAI 623
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544134 253 glglsVNGRFWLD----LTPSDVMWNTSDTGWAKSAWsSVFSPWIQGACVF-----THHlprfEPTSILQTLSKYPITV- 322
Cdd:PRK10252 624 -----VNRLLWMQnhypLTADDVVLQKTPCSFDVSVW-EFFWPFIAGAKLVmaepeAHR----DPLAMQQFFAEYGVTTt 693
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 42544134 323 ---------FCSAPTVyrmlvqnDITSYKFKSLKHCVSAGEPITPDVTEKWRNKTGLDIYEGYGQTE 380
Cdd:PRK10252 694 hfvpsmlaaFVASLTP-------EGARQSCASLRQVFCSGEALPADLCREWQQLTGAPLHNLYGPTE 753
|
|
| PLN03051 |
PLN03051 |
acyl-activating enzyme; Provisional |
127-302 |
2.75e-08 |
|
acyl-activating enzyme; Provisional
Pssm-ID: 215552 [Multi-domain] Cd Length: 499 Bit Score: 55.98 E-value: 2.75e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544134 127 LPRVPEWWLANVACLRTGTVLIPGTTQLTQKDILYRLQSSKANCIITNDVLA------PAVDAVASKCENLHSKLIVSEN 200
Cdd:PLN03051 1 MPMTVDAVIIYLAIVLAGCVVVSVADSFSAKEIATRLDISGAKGVFTQDVVLrggralPLYSKVVEAAPAKAIVLPAAGE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544134 201 S-----REGWGNLKELMKHASDSH-------TCVKTKHNEIMAIFFTSGTSGYPKMTAHTHSSfGLGLSVNGRFWLDLTP 268
Cdd:PLN03051 81 PvavplREQDLSWCDFLGVAAAQGsvggneySPVYAPVESVTNILFSSGTTGEPKAIPWTHLS-PLRCASDGWAHMDIQP 159
|
170 180 190
....*....|....*....|....*....|....*
gi 42544134 269 SDVM-WNTSdTGWAKSAWsSVFSPWIQGACVFTHH 302
Cdd:PLN03051 160 GDVVcWPTN-LGWMMGPW-LLYSAFLNGATLALYG 192
|
|
| PRK08043 |
PRK08043 |
bifunctional acyl-ACP--phospholipid O-acyltransferase/long-chain-fatty-acid--ACP ligase; |
222-413 |
3.59e-08 |
|
bifunctional acyl-ACP--phospholipid O-acyltransferase/long-chain-fatty-acid--ACP ligase;
Pssm-ID: 181207 [Multi-domain] Cd Length: 718 Bit Score: 55.87 E-value: 3.59e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544134 222 VKTKHNEIMAIFFTSGTSGYPKMTAHTHSSFgLGLSVNGRFWLDLTPSDVMWNTSDTGWAKSAWSSVFSPWIQGACVFTh 301
Cdd:PRK08043 360 VKQQPEDAALILFTSGSEGHPKGVVHSHKSL-LANVEQIKTIADFTPNDRFMSALPLFHSFGLTVGLFTPLLTGAEVFL- 437
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544134 302 hlprfeptsilqtlskYPitvfcsAPTVYRM---LV--QNDI----TS------------YKFKSLKHCVSAGEPITPDV 360
Cdd:PRK08043 438 ----------------YP------SPLHYRIvpeLVydRNCTvlfgTStflgnyarfanpYDFARLRYVVAGAEKLQEST 495
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 42544134 361 TEKWRNKTGLDIYEGYGQTETVLICGNFKGMKIKPGSMGKPSPAFDVKVCTSP 413
Cdd:PRK08043 496 KQLWQDKFGLRILEGYGVTECAPVVSINVPMAAKPGTVGRILPGMDARLLSVP 548
|
|
| PRK05852 |
PRK05852 |
fatty acid--CoA ligase family protein; |
96-381 |
5.91e-08 |
|
fatty acid--CoA ligase family protein;
Pssm-ID: 235625 [Multi-domain] Cd Length: 534 Bit Score: 54.89 E-value: 5.91e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544134 96 SFEELGSLSRKFANILSEAcSLQRGDRVILILPRVPEWWLANVACLRTGTVLIPGTTQLTQKDILYRLQSSKANCIITnD 175
Cdd:PRK05852 45 SYRDLARLVDDLAGQLTRS-GLLPGDRVALRMGSNAEFVVALLAASRADLVVVPLDPALPIAEQRVRSQAAGARVVLI-D 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544134 176 VLAPAVDAVAS-KCENLhsKLIVSENSREGWGNLKELMKHASDSHTCVKT----KHNEIMaIFFTSGTSGYPKMTAHTHS 250
Cdd:PRK05852 123 ADGPHDRAEPTtRWWPL--TVNVGGDSGPSGGTLSVHLDAATEPTPATSTpeglRPDDAM-IMFTGGTTGLPKMVPWTHA 199
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544134 251 SfgLGLSVNGRF-WLDLTPSD----VMWNTSDTGWAKSAWSSVFSpwiqGACVFTHHLPRFEPTSILQTLSKYPITVFCS 325
Cdd:PRK05852 200 N--IASSVRAIItGYRLSPRDatvaVMPLYHGHGLIAALLATLAS----GGAVLLPARGRFSAHTFWDDIKAVGATWYTA 273
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*....
gi 42544134 326 APTVYRMLVQNDITSY---KFKSLKHCVSAGEPITPDVTEKWRNKTGLDIYEGYGQTET 381
Cdd:PRK05852 274 VPTIHQILLERAATEPsgrKPAALRFIRSCSAPLTAETAQALQTEFAAPVVCAFGMTEA 332
|
|
| A_NRPS_acs4 |
cd17654 |
acyl-CoA synthetase family member 4; This family of the adenylation (A) domain of nonribosomal ... |
96-381 |
7.41e-08 |
|
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: 54.40 E-value: 7.41e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544134 96 SFEELGSLSRKFANILSEacSLQRGDRVI-LILPRVPEWWLANVACLRTGTVLIPGTTQLTQKDILYRLQSSKANCIITN 174
Cdd:cd17654 18 SYADLAEKISNLSNFLRK--KFQTEERAIgLRCDRGTESPVAILAILFLGAAYAPIDPASPEQRSLTVMKKCHVSYLLQN 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544134 175 dvlapavdavaskCENLHSKLIvsensregwgnlkelmKHASDSHTCVKTKHNEIMAIFfTSGTSGYPKMTAHTHSSFgL 254
Cdd:cd17654 96 -------------KELDNAPLS----------------FTPEHRHFNIRTDECLAYVIH-TSGTTGTPKIVAVPHKCI-L 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544134 255 GLSVNGRFWLDLTPSDVMWNTSDTGWAKSAwSSVFSPWIQGAC-VFTHHLPRFEPTSILQTLSKYP-ITVFCSAPTVYRM 332
Cdd:cd17654 145 PNIQHFRSLFNITSEDILFLTSPLTFDPSV-VEIFLSLSSGATlLIVPTSVKVLPSKLADILFKRHrITVLQATPTLFRR 223
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....
gi 42544134 333 LVQNDITSY---KFKSLKHCVSAGEPITPDVTEK-WRNK-TGLDIYEGYGQTET 381
Cdd:cd17654 224 FGSQSIKSTvlsATSSLRVLALGGEPFPSLVILSsWRGKgNRTRIFNIYGITEV 277
|
|
| Dip2 |
cd05905 |
Disco-interacting protein 2 (Dip2); Dip2 proteins show sequence similarity to other members of ... |
96-364 |
1.11e-07 |
|
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: 53.89 E-value: 1.11e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544134 96 SFEELGSLSRKFANILSEACSLQRGDRVILILPRVPEWWLANVACLRTGTVLIPGTTQLTQKDILYRLQSSKANCIITND 175
Cdd:cd05905 16 TWGKLLSRAEKIAAVLQKKVGLKPGDRVALMYPDPLDFVAAFYGCLYAGVVPIPIEPPDISQQLGFLLGTCKVRVALTVE 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544134 176 VLAP----AVDAVASKCENLHSKLIvsENSREGWGNLKELMKHASDSHTCVKTKHNEIMAIFFTSGTSGYPKMTAHTHSS 251
Cdd:cd05905 96 ACLKglpkKLLKSKTAAEIAKKKGW--PKILDFVKIPKSKRSKLKKWGPHPPTRDGDTAYIEYSFSSDGSLSGVAVSHSS 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544134 252 FgLGLSVNGRFWLDLTPSDVMWN----TSDTGWAKSAWSSVFSpwiqGACVFTHHLPRFE--PTSILQTLSKYPI-TVFC 324
Cdd:cd05905 174 L-LAHCRALKEACELYESRPLVTvldfKSGLGLWHGCLLSVYS----GHHTILIPPELMKtnPLLWLQTLSQYKVrDAYV 248
|
250 260 270 280
....*....|....*....|....*....|....*....|....*...
gi 42544134 325 SAPTVYRMLVQ--NDITSYK-----FKSLKHC-VSAGEPITPDVTEKW 364
Cdd:cd05905 249 KLRTLHWCLKDlsSTLASLKnrdvnLSSLRMCmVPCENRPRISSCDSF 296
|
|
| LC_FACS_bac1 |
cd17641 |
bacterial long-chain fatty acid CoA synthetase; The members of this family are bacterial ... |
95-409 |
1.85e-07 |
|
bacterial long-chain fatty acid CoA synthetase; The members of this family are bacterial long-chain fatty acid CoA synthetase, most of which are as yet uncharacterized. LC-FACS catalyzes the formation of fatty acyl-CoA in a two-step reaction: the formation of a fatty acyl-AMP molecule as an intermediate, and the formation of a fatty acyl-CoA. Free fatty acids must be "activated" to their CoA thioesters before participating in most catabolic and anabolic reactions.
Pssm-ID: 341296 [Multi-domain] Cd Length: 569 Bit Score: 53.20 E-value: 1.85e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544134 95 WSFEELGSLSRKFANILSeACSLQRGDRVILILPRVPEWWLANVACLRTGTVLIPGTTQLTQKDILYRLQSSKANCIITN 174
Cdd:cd17641 12 FTWADYADRVRAFALGLL-ALGVGRGDVVAILGDNRPEWVWAELAAQAIGALSLGIYQDSMAEEVAYLLNYTGARVVIAE 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544134 175 DvlAPAVDAVASKCENLHS--KLIVSE-----NSREGW----GNLKELMKHASDSHTCV------KTKHNEIMAIFFTSG 237
Cdd:cd17641 91 D--EEQVDKLLEIADRIPSvrYVIYCDprgmrKYDDPRlisfEDVVALGRALDRRDPGLyerevaAGKGEDVAVLCTTSG 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544134 238 TSGYPKMTAHTHSSFgLGLSVNGRFWLDLTPSDVMWNTSDTGWAKSAWSSVFSPWIQGACVfthHLPRfEPTSILQTLSK 317
Cdd:cd17641 169 TTGKPKLAMLSHGNF-LGHCAAYLAADPLGPGDEYVSVLPLPWIGEQMYSVGQALVCGFIV---NFPE-EPETMMEDLRE 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544134 318 YPITVFCSAPTVYRMLVQN------DITSYK------------------------------------------------F 343
Cdd:cd17641 244 IGPTFVLLPPRVWEGIAADvrarmmDATPFKrfmfelgmklglraldrgkrgrpvslwlrlaswladallfrplrdrlgF 323
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 42544134 344 KSLKHCVSAGEPITPDVTEKWRnKTGLDIYEGYGQTETVLICGNFKGMKIKPGSMGKPSPAFDVKV 409
Cdd:cd17641 324 SRLRSAATGGAALGPDTFRFFH-AIGVPLKQLYGQTELAGAYTVHRDGDVDPDTVGVPFPGTEVRI 388
|
|
| PLN03052 |
PLN03052 |
acetate--CoA ligase; Provisional |
72-298 |
2.45e-07 |
|
acetate--CoA ligase; Provisional
Pssm-ID: 215553 [Multi-domain] Cd Length: 728 Bit Score: 53.16 E-value: 2.45e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544134 72 EKAGKKPSNPAFWWINRNGEEM---RWSFEELGSLSRKFANILsEACSLQRGDRVILILPRVPEWWLANVACLRTGTVLI 148
Cdd:PLN03052 183 PKPSKTDDSIAIIWRDEGSDDLpvnRMTLSELRSQVSRVANAL-DALGFEKGDAIAIDMPMNVHAVIIYLAIILAGCVVV 261
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544134 149 PGTTQLTQKDILYRLQSSKANCIITNDVL-----------------APAVDAVASKCENLHSKLivsensREG---WGNL 208
Cdd:PLN03052 262 SIADSFAPSEIATRLKISKAKAIFTQDVIvrggksiplysrvveakAPKAIVLPADGKSVRVKL------REGdmsWDDF 335
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544134 209 KELMKHAS--DSHTCVKTKHNEIMAIFFTSGTSGYPKMTAHTHSSfGLGLSVNGRFWLDLTPSDVM-WNTsDTGWAKSAW 285
Cdd:PLN03052 336 LARANGLRrpDEYKAVEQPVEAFTNILFSSGTTGEPKAIPWTQLT-PLRAAADAWAHLDIRKGDIVcWPT-NLGWMMGPW 413
|
250
....*....|...
gi 42544134 286 sSVFSPWIQGACV 298
Cdd:PLN03052 414 -LVYASLLNGATL 425
|
|
| A_NRPS_Cytc1-like |
cd17643 |
similar to adenylation domain of cytotrienin synthetase CytC1; This family of the adenylation ... |
232-381 |
3.43e-07 |
|
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: 52.31 E-value: 3.43e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544134 232 IFFTSGTSGYPKMTAHTHSSFgLGLSVNGRFWLDLTPSDVMWNTSDTGWAKSAWsSVFSPWIQGA--CVFTHHLPRfEPT 309
Cdd:cd17643 98 VIYTSGSTGRPKGVVVSHANV-LALFAATQRWFGFNEDDVWTLFHSYAFDFSVW-EIWGALLHGGrlVVVPYEVAR-SPE 174
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 42544134 310 SILQTLSKYPITVFCSAPTVYRMLVQNDITSYKFK-SLKHCVSAGEPITPDVTEKWRNKTGL---DIYEGYGQTET 381
Cdd:cd17643 175 DFARLLRDEGVTVLNQTPSAFYQLVEAADRDGRDPlALRYVIFGGEALEAAMLRPWAGRFGLdrpQLVNMYGITET 250
|
|
| LC-FACS_euk |
cd05927 |
Eukaryotic long-chain fatty acid CoA synthetase (LC-FACS); The members of this family are ... |
131-409 |
4.21e-07 |
|
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: 52.22 E-value: 4.21e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544134 131 PEWWLANVACLRTGTVLIPGTTQLTQKDILYRLQSSKANCIItndvlapavdavASKCENLHSklivsensregwgnLKE 210
Cdd:cd05927 43 PEWIISELACYAYSLVTVPLYDTLGPEAIEYILNHAEISIVF------------CDAGVKVYS--------------LEE 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544134 211 LMK-HASDSHTCVKTKHNEIMAIFFTSGTSGYPKMTAHTHSSFGLGLSVNGRFWLDLtpsdVMWNTSDTGWAKSAWSSVF 289
Cdd:cd05927 97 FEKlGKKNKVPPPPPKPEDLATICYTSGTTGNPKGVMLTHGNIVSNVAGVFKILEIL----NKINPTDVYISYLPLAHIF 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544134 290 SPWIQ------GACV-FTHHLPRfEPTSILQTLSkyPiTVFCSAPTVY-RML--VQNDI--------------TSYKFKS 345
Cdd:cd05927 173 ERVVEalflyhGAKIgFYSGDIR-LLLDDIKALK--P-TVFPGVPRVLnRIYdkIFNKVqakgplkrklfnfaLNYKLAE 248
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544134 346 LKH---------------------------CVSAGEPITPDVTEKWRNKTGLDIYEGYGQTETV-LICGNFKGMKIkPGS 397
Cdd:cd05927 249 LRSgvvraspfwdklvfnkikqalggnvrlMLTGSAPLSPEVLEFLRVALGCPVLEGYGQTECTaGATLTLPGDTS-VGH 327
|
330
....*....|..
gi 42544134 398 MGKPSPAFDVKV 409
Cdd:cd05927 328 VGGPLPCAEVKL 339
|
|
| FACL_like_2 |
cd05917 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
232-409 |
4.29e-07 |
|
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: 51.51 E-value: 4.29e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544134 232 IFFTSGTSGYPKMTAHTHSSFglgLSvNGRF---WLDLTPSDVM----------------WNTSDTGwaksawssvfspw 292
Cdd:cd05917 7 IQFTSGTTGSPKGATLTHHNI---VN-NGYFigeRLGLTEQDRLcipvplfhcfgsvlgvLACLTHG------------- 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544134 293 iqGACVFTHhlPRFEPTSILQTLSKYPITVFCSAPTVY-RMLVQNDITSYKFKSLKHCVSAGEPITPDVTEKWRNKTGL- 370
Cdd:cd05917 70 --ATMVFPS--PSFDPLAVLEAIEKEKCTALHGVPTMFiAELEHPDFDKFDLSSLRTGIMAGAPCPPELMKRVIEVMNMk 145
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 42544134 371 DIYEGYGQTETVLICgnFKGMKIKP-----GSMGKPSPAFDVKV 409
Cdd:cd05917 146 DVTIAYGMTETSPVS--TQTRTDDSiekrvNTVGRIMPHTEAKI 187
|
|
| PRK06814 |
PRK06814 |
acyl-[ACP]--phospholipid O-acyltransferase; |
231-409 |
5.66e-07 |
|
acyl-[ACP]--phospholipid O-acyltransferase;
Pssm-ID: 235865 [Multi-domain] Cd Length: 1140 Bit Score: 51.89 E-value: 5.66e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544134 231 AIFFTSGTSGYPKMTAHTHSSFglgLS----VNGRfwLDLTPSDVMWNTsdtgwaksawssvfspwiqgacvfthhLPRF 306
Cdd:PRK06814 797 VILFTSGSEGTPKGVVLSHRNL---LAnraqVAAR--IDFSPEDKVFNA---------------------------LPVF 844
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544134 307 EP---TS--ILQTLSKYPITVFCSaPTVYR----MLVQNDIT-----------------SYKFKSLKHCVSAGEPITPDV 360
Cdd:PRK06814 845 HSfglTGglVLPLLSGVKVFLYPS-PLHYRiipeLIYDTNATilfgtdtflngyaryahPYDFRSLRYVFAGAEKVKEET 923
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 42544134 361 TEKWRNKTGLDIYEGYGQTET--VLICGNfkGMKIKPGSMGKPSPAFDVKV 409
Cdd:PRK06814 924 RQTWMEKFGIRILEGYGVTETapVIALNT--PMHNKAGTVGRLLPGIEYRL 972
|
|
| caiC |
PRK08008 |
putative crotonobetaine/carnitine-CoA ligase; Validated |
72-249 |
9.82e-07 |
|
putative crotonobetaine/carnitine-CoA ligase; Validated
Pssm-ID: 181195 [Multi-domain] Cd Length: 517 Bit Score: 50.84 E-value: 9.82e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544134 72 EKAGKKPSNPAFWWINRNGEEMRWSFEELGSLSRKFANiLSEACSLQRGDRVILILPRVPEW---WLAnVACLrtGTVLI 148
Cdd:PRK08008 15 DLADVYGHKTALIFESSGGVVRRYSYLELNEEINRTAN-LFYSLGIRKGDKVALHLDNCPEFifcWFG-LAKI--GAIMV 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544134 149 PGTTQLTQKDILYRLQSSKANCIITNDVLAPAVDAVASKCEN-LHSKLIVSENSRE--GWGNLKELMKHASDSHTCVKTK 225
Cdd:PRK08008 91 PINARLLREESAWILQNSQASLLVTSAQFYPMYRQIQQEDATpLRHICLTRVALPAddGVSSFTQLKAQQPATLCYAPPL 170
|
170 180
....*....|....*....|....*
gi 42544134 226 HNEIMA-IFFTSGTSGYPKMTAHTH 249
Cdd:PRK08008 171 STDDTAeILFTSGTTSRPKGVVITH 195
|
|
| PRK12467 |
PRK12467 |
peptide synthase; Provisional |
91-382 |
1.18e-06 |
|
peptide synthase; Provisional
Pssm-ID: 237108 [Multi-domain] Cd Length: 3956 Bit Score: 51.32 E-value: 1.18e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544134 91 EEMRWSFEELGSLSRKFANILseacsLQRG---DRVI-LILPRVPEWWLANVACLRTGTVLIPGTTQLTQKDILYRLQSS 166
Cdd:PRK12467 3117 GDQQLSYAELNRRANRLAHRL-----IAIGvgpDVLVgVAVERSVEMIVALLAVLKAGGAYVPLDPEYPRERLAYMIEDS 3191
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544134 167 KANCIITNDVLAPAVDAVASkcenLHSKLIvsenSREGWGNLKElmkHASDSHTcvktkHNEIMA-IFFTSGTSGYPKMT 245
Cdd:PRK12467 3192 GVKLLLTQAHLLEQLPAPAG----DTALTL----DRLDLNGYSE---NNPSTRV-----MGENLAyVIYTSGSTGKPKGV 3255
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544134 246 AHTHSSFGLGLSVNGRFWlDLTPSDVMWNTSDTGWAKSAWSsVFSPWIQGACVFTHHLPRFEPTSILQTLSKYPITVFCS 325
Cdd:PRK12467 3256 GVRHGALANHLCWIAEAY-ELDANDRVLLFMSFSFDGAQER-FLWTLICGGCLVVRDNDLWDPEELWQAIHAHRISIACF 3333
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*....
gi 42544134 326 APTVYRMLVQN-DITSYKfkSLKHCVSAGEPITPDVTEKWRNKTG-LDIYEGYGQTETV 382
Cdd:PRK12467 3334 PPAYLQQFAEDaGGADCA--SLDIYVFGGEAVPPAAFEQVKRKLKpRGLTNGYGPTEAV 3390
|
|
| FADD10 |
cd17635 |
adenylate forming domain, fatty acid CoA ligase (FadD10); This family contains long chain ... |
228-409 |
1.55e-06 |
|
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: 49.95 E-value: 1.55e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544134 228 EIMAIFFTSGTSGYPKMTAHTHSSFGLGLSVNGRFWLDLTPSDVMWNTSDTGWAKSAWSSVFSPWIQGACVFTHHlpRFE 307
Cdd:cd17635 2 DPLAVIFTSGTTGEPKAVLLANKTFFAVPDILQKEGLNWVVGDVTYLPLPATHIGGLWWILTCLIHGGLCVTGGE--NTT 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544134 308 PTSILQTLSKYPITVFCSAPTVYRMLVQNDITSYKFKSLKHCVSAG--EPITPDVTEKWRNKTgLDIYEGYGQTET-VLI 384
Cdd:cd17635 80 YKSLFKILTTNAVTTTCLVPTLLSKLVSELKSANATVPSLRLIGYGgsRAIAADVRFIEATGL-TNTAQVYGLSETgTAL 158
|
170 180
....*....|....*....|....*
gi 42544134 385 CGNFKGMKIKPGSMGKPSPAFDVKV 409
Cdd:cd17635 159 CLPTDDDSIEINAVGRPYPGVDVYL 183
|
|
| A_NRPS_TlmIV_like |
cd12114 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including ... |
94-334 |
2.23e-06 |
|
The adenylation domain of nonribosomal peptide synthetases (NRPS), including Streptoalloteichus tallysomycin biosynthesis genes; The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions. This family includes the TLM biosynthetic gene cluster from Streptoalloteichus that consists of nine NRPS genes; the N-terminal module of TlmVI (NRPS-5) and the starter module of BlmVI (NRPS-5) are comprised of the acyl CoA ligase (AL) and acyl carrier protein (ACP)-like domains, which are thought to be involved in the biosynthesis of the beta-aminoalaninamide moiety.
Pssm-ID: 341279 [Multi-domain] Cd Length: 477 Bit Score: 49.58 E-value: 2.23e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544134 94 RWSFEELGSLSRKFANILsEACSLQRGDRVILILPRVPEWWLANVACLRTGTVLIPGTTQLTQKDILYRLQSSKANCIIT 173
Cdd:cd12114 12 TLTYGELAERARRVAGAL-KAAGVRPGDLVAVTLPKGPEQVVAVLGILAAGAAYVPVDIDQPAARREAILADAGARLVLT 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544134 174 NDVLAPAVDAVAskcenlhSKLIVSENSREGWgnlKELMKHASDSHTcvktkhneiMA-IFFTSGTSGYPKMTAHTHSS- 251
Cdd:cd12114 91 DGPDAQLDVAVF-------DVLILDLDALAAP---APPPPVDVAPDD---------LAyVIFTSGSTGTPKGVMISHRAa 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544134 252 FGLGLSVNGRFwlDLTPSDVMWNTSDTGWAKSAWsSVFSPWIQGAC-VFTHHLPRFEPTSILQTLSKYPITVFCSAPTVY 330
Cdd:cd12114 152 LNTILDINRRF--AVGPDDRVLALSSLSFDLSVY-DIFGALSAGATlVLPDEARRRDPAHWAELIERHGVTLWNSVPALL 228
|
....
gi 42544134 331 RMLV 334
Cdd:cd12114 229 EMLL 232
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
71-381 |
2.40e-06 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 50.34 E-value: 2.40e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544134 71 KEKAGKKPSNPAFwwinRNGEEmRWSFEELGSLSRKFANILSEaCSLQRGDRVILILPRVPEWWLANVACLRTGTVLIPG 150
Cdd:PRK12316 518 EEQVERTPEAPAL----AFGEE-TLDYAELNRRANRLAHALIE-RGVGPDVLVGVAMERSIEMVVALLAILKAGGAYVPL 591
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544134 151 TTQLTQKDILYRLQSSKANCIITNDVLAPAVDaVASKCENLHSKLIVSENSREGWGNLKelmkhasdshTCVktkHNEIM 230
Cdd:PRK12316 592 DPEYPAERLAYMLEDSGVQLLLSQSHLGRKLP-LAAGVQVLDLDRPAAWLEGYSEENPG----------TEL---NPENL 657
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544134 231 A-IFFTSGTSGYPKMTAHTHSSFglglsVNGRFW----LDLTPSDVMWNTSDTGWAKSAWsSVFSPWIQGA-CVFTHHLP 304
Cdd:PRK12316 658 AyVIYTSGSTGKPKGAGNRHRAL-----SNRLCWmqqaYGLGVGDTVLQKTPFSFDVSVW-EFFWPLMSGArLVVAAPGD 731
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 42544134 305 RFEPTSILQTLSKYPITVFCSAPTVYRMLVQN-DITSykFKSLKHCVSAGEPITPDVTEK-WRNKTGLDIYEGYGQTET 381
Cdd:PRK12316 732 HRDPAKLVELINREGVDTLHFVPSMLQAFLQDeDVAS--CTSLRRIVCSGEALPADAQEQvFAKLPQAGLYNLYGPTEA 808
|
|
| A_NRPS_ApnA-like |
cd17644 |
similar to adenylation domain of anabaenopeptin synthetase (ApnA); This family of the ... |
224-410 |
2.57e-06 |
|
similar to adenylation domain of anabaenopeptin synthetase (ApnA); This family of the adenylation (A) domain of nonribosomal peptide synthases (NRPS) includes Planktothrix agardhii anabaenopeptin synthetase (ApnA A1), which is capable of activating two chemically distinct amino acids (Arg and Tyr). Structural studies show that the architecture of the active site forces Arg to adopt a Tyr-like conformation, thus explaining the bispecificity. The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester bond to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.
Pssm-ID: 341299 [Multi-domain] Cd Length: 465 Bit Score: 49.36 E-value: 2.57e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544134 224 TKHNEIMAIFFTSGTSGYPKMTAHTHSS---FGLGLSVNgrfwLDLTPSDVMWNTSDTGWAKSAwSSVFSPWIQGAC-VF 299
Cdd:cd17644 103 TQPENLAYVIYTSGSTGKPKGVMIEHQSlvnLSHGLIKE----YGITSSDRVLQFASIAFDVAA-EEIYVTLLSGATlVL 177
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544134 300 THHLPRFEPTSILQTLSKYPITVFCSAPTVYRMLV----QNDITSykFKSLKHCVSAGEPITPDVTEKWRNKTGLDI--Y 373
Cdd:cd17644 178 RPEEMRSSLEDFVQYIQQWQLTVLSLPPAYWHLLVlellLSTIDL--PSSLRLVIVGGEAVQPELVRQWQKNVGNFIqlI 255
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 42544134 374 EGYGQTETVL--ICGNFK---GMKIKPGSMGKPSPAFDVKVC 410
Cdd:cd17644 256 NVYGPTEATIaaTVCRLTqltERNITSVPIGRPIANTQVYIL 297
|
|
| PRK05857 |
PRK05857 |
fatty acid--CoA ligase; |
72-407 |
2.63e-06 |
|
fatty acid--CoA ligase;
Pssm-ID: 180293 [Multi-domain] Cd Length: 540 Bit Score: 49.62 E-value: 2.63e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544134 72 EKAGKKPSNPAfwwINRNGEEMRWSFEELGSLSRKFANILsEACSLQRGDRVILILPRVPEWWLANVACLRTGTVLIPGT 151
Cdd:PRK05857 22 EQARQQPEAIA---LRRCDGTSALRYRELVAEVGGLAADL-RAQSVSRGSRVLVISDNGPETYLSVLACAKLGAIAVMAD 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544134 152 TQLTQKDILYRLQSSKANCIITNDvlAPAVDAvASKCENLHSKLIVSENSREGWGNlkelMKHASDS---HTCVKTKHNE 228
Cdd:PRK05857 98 GNLPIAAIERFCQITDPAAALVAP--GSKMAS-SAVPEALHSIPVIAVDIAAVTRE----SEHSLDAaslAGNADQGSED 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544134 229 IMAIFFTSGTSGYPKMTAHTHSSFGLG---LSVNGRFWLDltpsdvmWNTSDTGWAKSAWSSVFSPW------IQGACVF 299
Cdd:PRK05857 171 PLAMIFTSGTTGEPKAVLLANRTFFAVpdiLQKEGLNWVT-------WVVGETTYSPLPATHIGGLWwiltclMHGGLCV 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544134 300 THHlprfEPT-SILQTLSKYPITVFCSAPTVYRMLVQN-DITSYKFKSLKHCVSAG-EPITPDVteKWRNKTGLDIYEGY 376
Cdd:PRK05857 244 TGG----ENTtSLLEILTTNAVATTCLVPTLLSKLVSElKSANATVPSLRLVGYGGsRAIAADV--RFIEATGVRTAQVY 317
|
330 340 350
....*....|....*....|....*....|....*.
gi 42544134 377 GQTET-----VLICGNFKGMKIKPGSMGKPSPAFDV 407
Cdd:PRK05857 318 GLSETgctalCLPTDDGSIVKIEAGAVGRPYPGVDV 353
|
|
| BACL_like |
cd05929 |
Bacterial Bile acid CoA ligases and similar proteins; Bile acid-Coenzyme A ligase catalyzes ... |
303-401 |
4.05e-06 |
|
Bacterial Bile acid CoA ligases and similar proteins; Bile acid-Coenzyme A ligase catalyzes the formation of bile acid-CoA conjugates in a two-step reaction: the formation of a bile acid-AMP molecule as an intermediate, followed by the formation of a bile acid-CoA. This ligase requires a bile acid with a free carboxyl group, ATP, Mg2+, and CoA for synthesis of the final bile acid-CoA conjugate. The bile acid-CoA ligation is believed to be the initial step in the bile acid 7alpha-dehydroxylation pathway in the intestinal bacterium Eubacterium sp.
Pssm-ID: 341252 [Multi-domain] Cd Length: 473 Bit Score: 48.91 E-value: 4.05e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544134 303 LPRFEPTSILQTLSKYPITVFCSAPTVY-RML-----VQNditSYKFKSLKHCVSAGEPITPDVTEKWRNKTGLDIYEGY 376
Cdd:cd05929 200 MEKFDPEEFLRLIERYRVTFAQFVPTMFvRLLklpeaVRN---AYDLSSLKRVIHAAAPCPPWVKEQWIDWGGPIIWEYY 276
|
90 100
....*....|....*....|....*.
gi 42544134 377 GQTETV-LICGNFKGMKIKPGSMGKP 401
Cdd:cd05929 277 GGTEGQgLTIINGEEWLTHPGSVGRA 302
|
|
| PLN02479 |
PLN02479 |
acetate-CoA ligase |
105-381 |
4.24e-06 |
|
acetate-CoA ligase
Pssm-ID: 178097 [Multi-domain] Cd Length: 567 Bit Score: 49.07 E-value: 4.24e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544134 105 RKFANILSEAcSLQRGDRVILILPRVPEWWLANVACLRTGTVLIPGTTQLTQKDILYRLQSSKANCIITNDVLAP----A 180
Cdd:PLN02479 56 RRLASALAKR-SIGPGSTVAVIAPNIPAMYEAHFGVPMAGAVVNCVNIRLNAPTIAFLLEHSKSEVVMVDQEFFTlaeeA 134
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544134 181 VDAVASKCENLHSK--LIVSENSREGWGNLKE-LMKHASDSHTCVKTKHNEI-----------MAIFFTSGTSGYPKmta 246
Cdd:PLN02479 135 LKILAEKKKSSFKPplLIVIGDPTCDPKSLQYaLGKGAIEYEKFLETGDPEFawkppadewqsIALGYTSGTTASPK--- 211
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544134 247 hthssfGLGLSVNGRFWLDLTpSDVMWNTSD-------------TGWAKSaWSsvfspwIQGACVFTHHLPRFEPTSILQ 313
Cdd:PLN02479 212 ------GVVLHHRGAYLMALS-NALIWGMNEgavylwtlpmfhcNGWCFT-WT------LAALCGTNICLRQVTAKAIYS 277
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 42544134 314 TLSKYPITVFCSAPTVYRMLVqNDITSYKFKSLKHCV---SAGEPITPDVTEKWrNKTGLDIYEGYGQTET 381
Cdd:PLN02479 278 AIANYGVTHFCAAPVVLNTIV-NAPKSETILPLPRVVhvmTAGAAPPPSVLFAM-SEKGFRVTHTYGLSET 346
|
|
| A_NRPS_TubE_like |
cd05906 |
The adenylation domain (A domain) of a family of nonribosomal peptide synthetases (NRPSs) ... |
86-249 |
5.59e-06 |
|
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: 48.43 E-value: 5.59e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544134 86 INRNGEEMRWSFEELGSLSRKFANILSEAcSLQRGDRVILILPR----VPEWWlanvACLRTGTVLIPGTTQLTqkdilY 161
Cdd:cd05906 31 IDADGSEEFQSYQDLLEDARRLAAGLRQL-GLRPGDSVILQFDDnedfIPAFW----ACVLAGFVPAPLTVPPT-----Y 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544134 162 RLQSSKAN------------CIITNDVLAPAVDAVASKCENLHSKLIVSENSREGwgnLKELMKHASDSHTcvktkhneI 229
Cdd:cd05906 101 DEPNARLRklrhiwqllgspVVLTDAELVAEFAGLETLSGLPGIRVLSIEELLDT---AADHDLPQSRPDD--------L 169
|
170 180
....*....|....*....|
gi 42544134 230 MAIFFTSGTSGYPKMTAHTH 249
Cdd:cd05906 170 ALLMLTSGSTGFPKAVPLTH 189
|
|
| OSB_MenE-like |
cd17630 |
O-succinylbenzoic acid-CoA ligase; This family contains O-succinylbenzoyl-CoA (OSB-CoA) ... |
232-382 |
6.59e-06 |
|
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: 47.71 E-value: 6.59e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544134 232 IFFTSGTSGYPKMTAHT-----HSSFG----LGLSVNGRfWLDLTPS------DVMWNtsdtgWAKSAWSSVFSPWIQGA 296
Cdd:cd17630 5 VILTSGSTGTPKAVVHTaanllASAAGlhsrLGFGGGDS-WLLSLPLyhvgglAILVR-----SLLAGAELVLLERNQAL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544134 297 cvfthhlprfeptsiLQTLSKYPITVFCSAPTVYRMLVQNDITSYKFKSLKHCVSAGEPITPDVTEKWRNKtGLDIYEGY 376
Cdd:cd17630 79 ---------------AEDLAPPGVTHVSLVPTQLQRLLDSGQGPAALKSLRAVLLGGAPIPPELLERAADR-GIPLYTTY 142
|
....*.
gi 42544134 377 GQTETV 382
Cdd:cd17630 143 GMTETA 148
|
|
| 23DHB-AMP_lg |
cd05920 |
2,3-dihydroxybenzoate-AMP ligase; 2,3-dihydroxybenzoate-AMP ligase activates 2, ... |
90-249 |
9.99e-06 |
|
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: 47.71 E-value: 9.99e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544134 90 GEEMRWSFEELGSLSRKFANILSEAcSLQRGDRVILILPRVPEWWLANVACLRTGTVLIPGTTQLTQKDILYRLQSSKAN 169
Cdd:cd05920 36 DGDRRLTYRELDRRADRLAAGLRGL-GIRPGDRVVVQLPNVAEFVVLFFALLRLGAVPVLALPSHRRSELSAFCAHAEAV 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544134 170 CIITNDVLAPavdavaskcenlhsklivsensregwgnlkelMKHASDSHTcVKTKHNEIMAIFFTSGTSGYPKMTAHTH 249
Cdd:cd05920 115 AYIVPDRHAG--------------------------------FDHRALARE-LAESIPEVALFLLSGGTTGTPKLIPRTH 161
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
92-383 |
1.41e-05 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 47.64 E-value: 1.41e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544134 92 EMRWSFEELGSLSRKFANILseacsLQRG----DRVILILPRVPEWWLANVACLRTGTVLIPGTTQLTQKDILYRLQSSK 167
Cdd:PRK12316 2026 DQHLSYAELDSRANRLAHRL-----RARGvgpeVRVAIAAERSFELVVALLAVLKAGGAYVPLDPNYPAERLAYMLEDSG 2100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544134 168 ANCIITNDVLAPAVDAVASkcenlhskLIVSENSREGWgnlkelMKHASDSHTCVKTKHNEIMAIFFTSGTSGYPKMTAH 247
Cdd:PRK12316 2101 AALLLTQRHLLERLPLPAG--------VARLPLDRDAE------WADYPDTAPAVQLAGENLAYVIYTSGSTGLPKGVAV 2166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544134 248 THSSFGLGLSVNGRFWlDLTPSDVMWNTSDTGWAKSAWsSVFSPWIQGACVFTHHLPRFEPTSILQTLSKYPITVFCSAP 327
Cdd:PRK12316 2167 SHGALVAHCQAAGERY-ELSPADCELQFMSFSFDGAHE-QWFHPLLNGARVLIRDDELWDPEQLYDEMERHGVTILDFPP 2244
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*..
gi 42544134 328 TVYRMLVQNDITSYKFKSLKHCVSAGEPITPDVTEK-WRNKTGLDIYEGYGQTETVL 383
Cdd:PRK12316 2245 VYLQQLAEHAERDGRPPAVRVYCFGGEAVPAASLRLaWEALRPVYLFNGYGPTEAVV 2301
|
|
| PtmA |
cd17636 |
long-chain fatty acid CoA ligase (FadD); This family contains fatty acid CoA ligases, ... |
295-409 |
1.49e-05 |
|
long-chain fatty acid CoA ligase (FadD); This family contains fatty acid CoA ligases, including acyl-CoA synthetase (AMP-forming)/AMP-acid ligase II, most of which are yet to be characterized. Fatty acyl-CoA ligases catalyze the ATP-dependent activation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions.
Pssm-ID: 341291 [Multi-domain] Cd Length: 331 Bit Score: 46.91 E-value: 1.49e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544134 295 GACVFthhLPRFEPTSILQTLSKYPIT-VFCSAPTVYRMLVQNDITSYKFKSLKHCVSAGE---PITPDVTEkWRNKTGl 370
Cdd:cd17636 67 GTNVF---VRRVDAEEVLELIEAERCThAFLLPPTIDQIVELNADGLYDLSSLRSSPAAPEwndMATVDTSP-WGRKPG- 141
|
90 100 110 120
....*....|....*....|....*....|....*....|
gi 42544134 371 diyeGYGQTETV-LICGNFKGMKIKpGSMGKPSPAFDVKV 409
Cdd:cd17636 142 ----GYGQTEVMgLATFAALGGGAI-GGAGRPSPLVQVRI 176
|
|
| EntE |
COG1021 |
EntE, 2,3-dihydroxybenzoate-AMP synthase component of non-ribosomal peptide synthetase ... |
63-249 |
3.41e-05 |
|
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: 45.91 E-value: 3.41e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544134 63 DVLDQWtdkekAGKKPSNPAFwwInrnGEEMRWSFEELGSLSRKFANILSEAcSLQRGDRVILILPRVPEWWLANVACLR 142
Cdd:COG1021 29 DLLRRR-----AERHPDRIAV--V---DGERRLSYAELDRRADRLAAGLLAL-GLRPGDRVVVQLPNVAEFVIVFFALFR 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544134 143 TGtvLIPGTT--QLTQKDILYRLQSSKANCIITNDV-----LAPAVDAVASKCENLhsKLIVSENSREGWGNLKELMKHA 215
Cdd:COG1021 98 AG--AIPVFAlpAHRRAEISHFAEQSEAVAYIIPDRhrgfdYRALARELQAEVPSL--RHVLVVGDAGEFTSLDALLAAP 173
|
170 180 190
....*....|....*....|....*....|....*
gi 42544134 216 SDSHTCvkTKHNEIMAIFFTS-GTSGYPKMTAHTH 249
Cdd:COG1021 174 ADLSEP--RPDPDDVAFFQLSgGTTGLPKLIPRTH 206
|
|
| PRK03584 |
PRK03584 |
acetoacetate--CoA ligase; |
59-143 |
7.17e-05 |
|
acetoacetate--CoA ligase;
Pssm-ID: 235134 [Multi-domain] Cd Length: 655 Bit Score: 45.17 E-value: 7.17e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544134 59 NFAKDVLDQwtdkekagKKPSNPAFWWINRNGEEMRWSFEELGSLSRKFANILsEACSLQRGDRVILILPRVPEwwlANV 138
Cdd:PRK03584 87 NYAENLLRH--------RRDDRPAIIFRGEDGPRRELSWAELRRQVAALAAAL-RALGVGPGDRVAAYLPNIPE---TVV 154
|
....*
gi 42544134 139 ACLRT 143
Cdd:PRK03584 155 AMLAT 159
|
|
| A_NRPS_CmdD_like |
cd17652 |
similar to adenylation domain of chondramide synthase cmdD; This family of the adenylation (A) ... |
78-381 |
1.07e-04 |
|
similar to adenylation domain of chondramide synthase cmdD; This family of the adenylation (A) domain of nonribosomal peptide synthases (NRPS) includes phosphinothricin tripeptide (PTT, phosphinothricylalanylalanine) synthetase, where PTT is a natural-product antibiotic and potent herbicide that is produced by Streptomyces hygroscopicus. This adenylation domain has been confirmed to directly activate beta-tyrosine, and fluorinated chondramides are produced through precursor-directed biosynthesis. Also included in this family is chondramide synthase D (also known as ATP-dependent phenylalanine adenylase or phenylalanine activase or tyrosine activase). Chondramides A-D are depsipeptide antitumor and antifungal antibiotics produced by C. crocatus, are a class of mixed peptide/polyketide depsipeptides comprised of three amino acids (alanine, N-methyltryptophan, plus the unusual amino acid beta-tyrosine or alpha-methoxy-beta-tyrosine) and a polyketide chain ([E]-7-hydroxy-2,4,6-trimethyloct-4-enoic acid).
Pssm-ID: 341307 [Multi-domain] Cd Length: 436 Bit Score: 44.17 E-value: 1.07e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544134 78 PSNPAfwwINRNGEEMrwSFEELGSLSRKFANILSEaCSLQRGDRVILILPRVPEWWLANVACLRTGTVLIPGTTQLTQK 157
Cdd:cd17652 1 PDAPA---VVFGDETL--TYAELNARANRLARLLAA-RGVGPERLVALALPRSAELVVAILAVLKAGAAYLPLDPAYPAE 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544134 158 DILYRLQSSKANCIITndvlapavdavaskcenlhsklivsensregwgnlkelmkHASDshtcvktkhneIMAIFFTSG 237
Cdd:cd17652 75 RIAYMLADARPALLLT----------------------------------------TPDN-----------LAYVIYTSG 103
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544134 238 TSGYPKMTAHTHSSFGlGLSVNGRFWLDLTPSDVMWNTSDTGWAKSAWsSVFSPWIQGACVfthHLPRFEPTS----ILQ 313
Cdd:cd17652 104 STGRPKGVVVTHRGLA-NLAAAQIAAFDVGPGSRVLQFASPSFDASVW-ELLMALLAGATL---VLAPAEELLpgepLAD 178
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 42544134 314 TLSKYPITVFCSAPTVYRMLVQNDITsykfkSLKHCVSAGEPITPDVTEKWrnKTGLDIYEGYGQTET 381
Cdd:cd17652 179 LLREHRITHVTLPPAALAALPPDDLP-----DLRTLVVAGEACPAELVDRW--APGRRMINAYGPTET 239
|
|
| PRK06018 |
PRK06018 |
putative acyl-CoA synthetase; Provisional |
231-381 |
3.63e-04 |
|
putative acyl-CoA synthetase; Provisional
Pssm-ID: 235673 [Multi-domain] Cd Length: 542 Bit Score: 42.82 E-value: 3.63e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544134 231 AIFFTSGTSGYPKMTAHTHSSFGL-GLSVNGRFWLDLTPSDVMWNTSDTGWAkSAWSSVFSPWIQGACVFthhLP--RFE 307
Cdd:PRK06018 181 GMCYTSGTTGDPKGVLYSHRSNVLhALMANNGDALGTSAADTMLPVVPLFHA-NSWGIAFSAPSMGTKLV---MPgaKLD 256
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 42544134 308 PTSILQTLSKYPITVFCSAPTVYRMLVQN-DITSYKFKSLKHCVSAGEPItPDVTEKWRNKTGLDIYEGYGQTET 381
Cdd:PRK06018 257 GASVYELLDTEKVTFTAGVPTVWLMLLQYmEKEGLKLPHLKMVVCGGSAM-PRSMIKAFEDMGVEVRHAWGMTEM 330
|
|
| PRK05691 |
PRK05691 |
peptide synthase; Validated |
72-381 |
5.24e-04 |
|
peptide synthase; Validated
Pssm-ID: 235564 [Multi-domain] Cd Length: 4334 Bit Score: 42.85 E-value: 5.24e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544134 72 EKAGKKPSNPAFWWinrngEEMRWSFEELGSLSRKFANILSEaCSLQRGDRVILILPRVPEWWLANVACLRTGTVLIPGT 151
Cdd:PRK05691 1139 EQARQTPERIALVW-----DGGSLDYAELHAQANRLAHYLRD-KGVGPDVCVAIAAERSPQLLVGLLAILKAGGAYVPLD 1212
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544134 152 TQLTQKDILYRLQSSKANCIITNDVL---APAVDAVASKC-ENLHSklivsensrEGWGNlkelmkHASDSHTcvktkHN 227
Cdd:PRK05691 1213 PDYPAERLAYMLADSGVELLLTQSHLlerLPQAEGVSAIAlDSLHL---------DSWPS------QAPGLHL-----HG 1272
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544134 228 EIMA-IFFTSGTSGYPKMTAHTHSSFGLGLSvngrfWLD----LTPSDVMWNTSDTGWAKSAWsSVFSPWIQG-----AC 297
Cdd:PRK05691 1273 DNLAyVIYTSGSTGQPKGVGNTHAALAERLQ-----WMQatyaLDDSDVLMQKAPISFDVSVW-ECFWPLITGcrlvlAG 1346
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544134 298 VFTHHlprfEPTSILQTLSKYPITVFCSAPTVYRMLVQNDITSyKFKSLKHCVSAGEPITPDVTEKWRNK-TGLDIYEGY 376
Cdd:PRK05691 1347 PGEHR----DPQRIAELVQQYGVTTLHFVPPLLQLFIDEPLAA-ACTSLRRLFSGGEALPAELRNRVLQRlPQVQLHNRY 1421
|
....*
gi 42544134 377 GQTET 381
Cdd:PRK05691 1422 GPTET 1426
|
|
| A_NRPS_ACVS-like |
cd17648 |
N-(5-amino-5-carboxypentanoyl)-L-cysteinyl-D-valine synthase; This family contains ACV ... |
232-381 |
1.46e-03 |
|
N-(5-amino-5-carboxypentanoyl)-L-cysteinyl-D-valine synthase; This family contains ACV synthetase (ACVS, EC 6.3.2.26; also known as N-(5-amino-5-carboxypentanoyl)-L-cysteinyl-D-valine synthase or delta-(L-alpha-aminoadipyl)-L-cysteinyl-D-valine synthetase) is involved in medically important antibiotic biosynthesis. ACV synthetase is active in an early step in the penicillin G biosynthesis pathway which involves the formation of the tripeptide 6-(L-alpha-aminoadipyl)-L-cysteinyl-D-valine (ACV); each of the constituent amino acids of the tripeptide ACV are activated as aminoacyl-adenylates with peptide bonds formed through the participation of amino acid thioester intermediates. ACV is then cyclized by the action of isopenicillin N synthase.
Pssm-ID: 341303 [Multi-domain] Cd Length: 453 Bit Score: 40.85 E-value: 1.46e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544134 232 IFFTSGTSGYPK--MTAHtHSSFGLGLSVNGRFWLDLTPSDVMWNTSdtgwaksawSSVFSPWIQGAC--VFTHH----L 303
Cdd:cd17648 99 AIYTSGTTGKPKgvLVEH-GSVVNLRTSLSERYFGRDNGDEAVLFFS---------NYVFDFFVEQMTlaLLNGQklvvP 168
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544134 304 P---RFEPTSILQTLSKYPITVFCSAPTVyrmLVQNDITSykFKSLKHCVSAGEPITPDVTEKWRNKTGLDIYEGYGQTE 380
Cdd:cd17648 169 PdemRFDPDRFYAYINREKVTYLSGTPSV---LQQYDLAR--LPHLKRVDAAGEEFTAPVFEKLRSRFAGLIINAYGPTE 243
|
.
gi 42544134 381 T 381
Cdd:cd17648 244 T 244
|
|
| PLN02736 |
PLN02736 |
long-chain acyl-CoA synthetase |
117-413 |
1.53e-03 |
|
long-chain acyl-CoA synthetase
Pssm-ID: 178337 [Multi-domain] Cd Length: 651 Bit Score: 40.85 E-value: 1.53e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544134 117 LQRGDRVILILPRVPEWWLANVACLRTGTVLIPgttqltqkdiLYRLQSSKANCIITNDVLAPAVDAVASKCENLHS--- 193
Cdd:PLN02736 100 IPKGACVGLYFINRPEWLIVDHACSAYSYVSVP----------LYDTLGPDAVKFIVNHAEVAAIFCVPQTLNTLLScls 169
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544134 194 -----KLIVSensregWGNLKELM-------------------KHASDSHTCVKTKHNEIMAIFFTSGTSGYPKMTAHTH 249
Cdd:PLN02736 170 eipsvRLIVV------VGGADEPLpslpsgtgveivtyskllaQGRSSPQPFRPPKPEDVATICYTSGTTGTPKGVVLTH 243
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544134 250 SSfgLGLSVNG-RFWLDLTPSDVmwNTSDTGWAKsawssVFSPWIQGACVFTHHLPRFEPTSILQTLSKYPI---TVFCS 325
Cdd:PLN02736 244 GN--LIANVAGsSLSTKFYPSDV--HISYLPLAH-----IYERVNQIVMLHYGVAVGFYQGDNLKLMDDLAAlrpTIFCS 314
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544134 326 APTVY-------------------RM------------------------LVQNDITSYKFKSLKHCVSAGEPITPDVTE 362
Cdd:PLN02736 315 VPRLYnriydgitnavkesgglkeRLfnaaynakkqalengknpspmwdrLVFNKIKAKLGGRVRFMSSGASPLSPDVME 394
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|..
gi 42544134 363 KWRNKTGLDIYEGYGQTET-VLICGNFKGMKIKpGSMGKPSPAFDVKVCTSP 413
Cdd:PLN02736 395 FLRICFGGRVLEGYGMTETsCVISGMDEGDNLS-GHVGSPNPACEVKLVDVP 445
|
|
| PRK09192 |
PRK09192 |
fatty acyl-AMP ligase; |
117-273 |
3.19e-03 |
|
fatty acyl-AMP ligase;
Pssm-ID: 236403 [Multi-domain] Cd Length: 579 Bit Score: 39.99 E-value: 3.19e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544134 117 LQRGDRVILILPRVPEWWLANVACLRTGTVLIP--GTTQLTQKDILYR-----LQSSKANCIITNDVLAPAVDAVAskce 189
Cdd:PRK09192 71 LKPGDRVALIAETDGDFVEAFFACQYAGLVPVPlpLPMGFGGRESYIAqlrgmLASAQPAAIITPDELLPWVNEAT---- 146
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544134 190 nlhsklivsENSREGW-GNLKELMKHASDSHTCVKTKHNEIMAIFFTSGTSGYPKMTAHTHSSFGLGLSVNGRFWLDLTP 268
Cdd:PRK09192 147 ---------HGNPLLHvLSHAWFKALPEADVALPRPTPDDIAYLQYSSGSTRFPRGVIITHRALMANLRAISHDGLKVRP 217
|
....*..
gi 42544134 269 SD--VMW 273
Cdd:PRK09192 218 GDrcVSW 224
|
|
| ACSBG_like |
cd05933 |
Bubblegum-like very long-chain fatty acid CoA synthetase (VL-FACS); This family of very ... |
131-247 |
4.11e-03 |
|
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: 39.65 E-value: 4.11e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544134 131 PEWWLANVACLRTGTVLIPGTTQLTQKDILYRLQSSKAN-CIITNDVLAPAVDAVASKCENLHSKLIVSENSRE------ 203
Cdd:cd05933 44 PEWFIAAVGAIFAGGIAVGIYTTNSPEACQYVAETSEANiLVVENQKQLQKILQIQDKLPHLKAIIQYKEPLKEkepnly 123
|
90 100 110 120
....*....|....*....|....*....|....*....|....*....
gi 42544134 204 GWGNLKELMKHASDS--HTCVKT-KHNEIMAIFFTSGTSGYPK--MTAH 247
Cdd:cd05933 124 SWDEFMELGRSIPDEqlDAIISSqKPNQCCTLIYTSGTTGMPKgvMLSH 172
|
|
| |
