|
Name |
Accession |
Description |
Interval |
E-value |
| MACS_euk |
cd05928 |
Eukaryotic Medium-chain acyl-CoA synthetase (MACS or ACSM); MACS catalyzes the two-step ... |
22-343 |
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: 637.59 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755522749 22 RRWMALTESDIFWNTTDTGWVKAAW-TLFSAWSNGACIFVHELPRVDAKTILNTLCRFPITTLCCVPTLFRLLVQEDLTR 100
Cdd:cd05928 208 RYWLDLTASDIMWNTSDTGWIKSAWsSLFEPWIQGACVFVHHLPRFDPLVILKTLSSYPITTFCGAPTVYRMLVQQDLSS 287
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755522749 101 YKFQCLRHCLTGGEALNPDVRDKWKSQTGLELHEGYGQSETVVICGNSRNSTIKSGSMGKASPPYDVQIVDEEGNVLPPG 180
Cdd:cd05928 288 YKFPSLQHCVTGGEPLNPEVLEKWKAQTGLDIYEGYGQTETGLICANFKGMKIKPGSMGKASPPYDVQIIDDNGNVLPPG 367
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755522749 181 KEGNIAVRIKPTRPFCFFNCYLDNPEKTAASEQGDFYITGDRAHMDEDGYFWFLGRNDDVINSSSYRIGPVEVESALAEH 260
Cdd:cd05928 368 TEGDIGIRVKPIRPFGLFSGYVDNPEKTAATIRGDFYLTGDRGIMDEDGYFWFMGRADDVINSSGYRIGPFEVESALIEH 447
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755522749 261 PAVLESAVVSSPDPIRGEVVKAFIVLSPAYASHDPEALTRELQEHVKTVTAPYKYPRKVAFISELPKTVSGKILRSKLRN 340
Cdd:cd05928 448 PAVVESAVVSSPDPIRGEVVKAFVVLAPQFLSHDPEQLTKELQQHVKSVTAPYKYPRKVEFVQELPKTVTGKIQRNELRD 527
|
...
gi 755522749 341 QEW 343
Cdd:cd05928 528 KEW 530
|
|
| MACS_like |
cd05972 |
Medium-chain acyl-CoA synthetase (MACS or ACSM); MACS catalyzes the two-step activation of ... |
16-339 |
8.70e-157 |
|
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: 446.40 E-value: 8.70e-157
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755522749 16 LGGLKT-RRWMALTESDIFWNTTDTGWVKAAW-TLFSAWSNGACIFVHELPRVDAKTILNTLCRFPITTLCCVPTLFRLL 93
Cdd:cd05972 107 LGHIPTaAYWLGLRPDDIHWNIADPGWAKGAWsSFFGPWLLGATVFVYEGPRFDAERILELLERYGVTSFCGPPTAYRML 186
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755522749 94 VQEDLTRYKFQCLRHCLTGGEALNPDVRDKWKSQTGLELHEGYGQSETVVICGNSRNSTIKSGSMGKASPPYDVQIVDEE 173
Cdd:cd05972 187 IKQDLSSYKFSHLRLVVSAGEPLNPEVIEWWRAATGLPIRDGYGQTETGLTVGNFPDMPVKPGSMGRPTPGYDVAIIDDD 266
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755522749 174 GNVLPPGKEGNIAVRIKPTRPFCFfncYLDNPEKTAASEQGDFYITGDRAHMDEDGYFWFLGRNDDVINSSSYRIGPVEV 253
Cdd:cd05972 267 GRELPPGEEGDIAIKLPPPGLFLG---YVGDPEKTEASIRGDYYLTGDRAYRDEDGYFWFVGRADDIIKSSGYRIGPFEV 343
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755522749 254 ESALAEHPAVLESAVVSSPDPIRGEVVKAFIVLSPAYAshDPEALTRELQEHVKTVTAPYKYPRKVAFISELPKTVSGKI 333
Cdd:cd05972 344 ESALLEHPAVAEAAVVGSPDPVRGEVVKAFVVLTSGYE--PSEELAEELQGHVKKVLAPYKYPREIEFVEELPKTISGKI 421
|
....*.
gi 755522749 334 LRSKLR 339
Cdd:cd05972 422 RRVELR 427
|
|
| Acs |
COG0365 |
Acyl-coenzyme A synthetase/AMP-(fatty) acid ligase [Lipid transport and metabolism]; |
24-345 |
1.31e-139 |
|
Acyl-coenzyme A synthetase/AMP-(fatty) acid ligase [Lipid transport and metabolism];
Pssm-ID: 440134 [Multi-domain] Cd Length: 565 Bit Score: 407.58 E-value: 1.31e-139
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755522749 24 WMALTESDIFWNTTDTGWVKAAW-TLFSAWSNGACIFVHE--LPRVDAKTILNTLCRFPITTLCCVPTLFRLLVQED--- 97
Cdd:COG0365 220 VLDLKPGDVFWCTADIGWATGHSyIVYGPLLNGATVVLYEgrPDFPDPGRLWELIEKYGVTVFFTAPTAIRALMKAGdep 299
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755522749 98 LTRYKFQCLRHCLTGGEALNPDVRDKWKSQTGLELHEGYGQSETV-VICGNSRNSTIKSGSMGKASPPYDVQIVDEEGNV 176
Cdd:COG0365 300 LKKYDLSSLRLLGSAGEPLNPEVWEWWYEAVGVPIVDGWGQTETGgIFISNLPGLPVKPGSMGKPVPGYDVAVVDEDGNP 379
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755522749 177 LPPGKEGNIAVRikptRPF-CFFNCYLDNPEKTAASEQGDF---YITGDRAHMDEDGYFWFLGRNDDVINSSSYRIGPVE 252
Cdd:COG0365 380 VPPGEEGELVIK----GPWpGMFRGYWNDPERYRETYFGRFpgwYRTGDGARRDEDGYFWILGRSDDVINVSGHRIGTAE 455
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755522749 253 VESALAEHPAVLESAVVSSPDPIRGEVVKAFIVLSPAYAshDPEALTRELQEHVKTVTAPYKYPRKVAFISELPKTVSGK 332
Cdd:COG0365 456 IESALVSHPAVAEAAVVGVPDEIRGQVVKAFVVLKPGVE--PSDELAKELQAHVREELGPYAYPREIEFVDELPKTRSGK 533
|
330
....*....|...
gi 755522749 333 ILRSKLRNQEWGR 345
Cdd:COG0365 534 IMRRLLRKIAEGR 546
|
|
| MACS_AAE_MA_like |
cd05970 |
Medium-chain acyl-CoA synthetase (MACS) of AAE_MA like; MACS catalyzes the two-step activation ... |
16-342 |
2.71e-132 |
|
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: 388.01 E-value: 2.71e-132
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755522749 16 LGGLKTRR-WMALTESDIFWNTTDTGWVKAAW-TLFSAWSNGACIFVHELPRVDAKTILNTLCRFPITTLCCVPTLFRLL 93
Cdd:cd05970 211 LGHIVTAKyWQNVREGGLHLTVADTGWGKAVWgKIYGQWIAGAAVFVYDYDKFDPKALLEKLSKYGVTTFCAPPTIYRFL 290
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755522749 94 VQEDLTRYKFQCLRHCLTGGEALNPDVRDKWKSQTGLELHEGYGQSETVVICGNSRNSTIKSGSMGKASPPYDVQIVDEE 173
Cdd:cd05970 291 IREDLSRYDLSSLRYCTTAGEALNPEVFNTFKEKTGIKLMEGFGQTETTLTIATFPWMEPKPGSMGKPAPGYEIDLIDRE 370
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755522749 174 GNVLPPGKEGNIAVRIKPTRPFCFFNCYLDNPEKTAASEQGDFYITGDRAHMDEDGYFWFLGRNDDVINSSSYRIGPVEV 253
Cdd:cd05970 371 GRSCEAGEEGEIVIRTSKGKPVGLFGGYYKDAEKTAEVWHDGYYHTGDAAWMDEDGYLWFVGRTDDLIKSSGYRIGPFEV 450
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755522749 254 ESALAEHPAVLESAVVSSPDPIRGEVVKAFIVLSPAYAShdPEALTRELQEHVKTVTAPYKYPRKVAFISELPKTVSGKI 333
Cdd:cd05970 451 ESALIQHPAVLECAVTGVPDPIRGQVVKATIVLAKGYEP--SEELKKELQDHVKKVTAPYKYPRIVEFVDELPKTISGKI 528
|
....*....
gi 755522749 334 LRSKLRNQE 342
Cdd:cd05970 529 RRVEIRERD 537
|
|
| MACS_like_1 |
cd05974 |
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the ... |
17-342 |
2.71e-102 |
|
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: 307.57 E-value: 2.71e-102
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755522749 17 GGLKTRRWMALTESDIFWNTTDTGWVKAAWT-LFSAWSNGACIFVHELPRVDAKTILNTLCRFPITTLCCVPTLFRLLVQ 95
Cdd:cd05974 113 GHLSTMYWIGLKPGDVHWNISSPGWAKHAWScFFAPWNAGATVFLFNYARFDAKRVLAALVRYGVTTLCAPPTVWRMLIQ 192
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755522749 96 EDLTRYKFQcLRHCLTGGEALNPDVRDKWKSQTGLELHEGYGQSETVVICGNSRNSTIKSGSMGKASPPYDVQIVDEEGN 175
Cdd:cd05974 193 QDLASFDVK-LREVVGAGEPLNPEVIEQVRRAWGLTIRDGYGQTETTALVGNSPGQPVKAGSMGRPLPGYRVALLDPDGA 271
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755522749 176 vlpPGKEGNIAVRIKPTRPFCFFNCYLDNPEKTAASEQGDFYITGDRAHMDEDGYFWFLGRNDDVINSSSYRIGPVEVES 255
Cdd:cd05974 272 ---PATEGEVALDLGDTRPVGLMKGYAGDPDKTAHAMRGGYYRTGDIAMRDEDGYLTYVGRADDVFKSSDYRISPFELES 348
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755522749 256 ALAEHPAVLESAVVSSPDPIRGEVVKAFIVLSPAYASHDPEALtrELQEHVKTVTAPYKYPRKVAFiSELPKTVSGKILR 335
Cdd:cd05974 349 VLIEHPAVAEAAVVPSPDPVRLSVPKAFIVLRAGYEPSPETAL--EIFRFSRERLAPYKRIRRLEF-AELPKTISGKIRR 425
|
....*..
gi 755522749 336 SKLRNQE 342
Cdd:cd05974 426 VELRRRE 432
|
|
| MenE/FadK |
COG0318 |
O-succinylbenzoic acid-CoA ligase MenE or related acyl-CoA synthetase (AMP-forming) [Lipid ... |
21-345 |
5.62e-102 |
|
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: 307.51 E-value: 5.62e-102
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755522749 21 TRRWMALTESDIFWNTT----DTGWVkaaWTLFSAWSNGACIFVheLPRVDAKTILNTLCRFPITTLCCVPTLF-RLLVQ 95
Cdd:COG0318 132 IAAALGLTPGDVVLVALplfhVFGLT---VGLLAPLLAGATLVL--LPRFDPERVLELIERERVTVLFGVPTMLaRLLRH 206
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755522749 96 EDLTRYKFQCLRHCLTGGEALNPDVRDKWKSQTGLELHEGYGQSET-VVICGNSRNS-TIKSGSMGKASPPYDVQIVDEE 173
Cdd:COG0318 207 PEFARYDLSSLRLVVSGGAPLPPELLERFEERFGVRIVEGYGLTETsPVVTVNPEDPgERRPGSVGRPLPGVEVRIVDED 286
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755522749 174 GNVLPPGKEGNIAVRikptrPFCFFNCYLDNPEKTAASEQGDFYITGDRAHMDEDGYFWFLGRNDDVINSSSYRIGPVEV 253
Cdd:COG0318 287 GRELPPGEVGEIVVR-----GPNVMKGYWNDPEATAEAFRDGWLRTGDLGRLDEDGYLYIVGRKKDMIISGGENVYPAEV 361
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755522749 254 ESALAEHPAVLESAVVSSPDPIRGEVVKAFIVLSPAyASHDPEALTRELQEHVktvtAPYKYPRKVAFISELPKTVSGKI 333
Cdd:COG0318 362 EEVLAAHPGVAEAAVVGVPDEKWGERVVAFVVLRPG-AELDAEELRAFLRERL----ARYKVPRRVEFVDELPRTASGKI 436
|
330
....*....|..
gi 755522749 334 LRSKLRNQEWGR 345
Cdd:COG0318 437 DRRALRERYAAG 448
|
|
| MACS_like_4 |
cd05969 |
Uncharacterized subfamily of Acetyl-CoA synthetase like family (ACS); This family is most ... |
21-342 |
1.47e-96 |
|
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: 293.25 E-value: 1.47e-96
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755522749 21 TRRW-MALTESDIFWNTTDTGWVK-AAWTLFSAWSNGACIFVHElPRVDAKTILNTLCRFPITTLCCVPTLFRLLVQED- 97
Cdd:cd05969 120 TGKYvLDLHPDDIYWCTADPGWVTgTVYGIWAPWLNGVTNVVYE-GRFDAESWYGIIERVKVTVWYTAPTAIRMLMKEGd 198
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755522749 98 --LTRYKFQCLRHCLTGGEALNPDVRdKWKSQT-GLELHEGYGQSET--VVICgNSRNSTIKSGSMGKASPPYDVQIVDE 172
Cdd:cd05969 199 elARKYDLSSLRFIHSVGEPLNPEAI-RWGMEVfGVPIHDTWWQTETgsIMIA-NYPCMPIKPGSMGKPLPGVKAAVVDE 276
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755522749 173 EGNVLPPGKEGNIAvrIKPTRPfCFFNCYLDNPEKTAASEQGDFYITGDRAHMDEDGYFWFLGRNDDVINSSSYRIGPVE 252
Cdd:cd05969 277 NGNELPPGTKGILA--LKPGWP-SMFRGIWNDEERYKNSFIDGWYLTGDLAYRDEDGYFWFVGRADDIIKTSGHRVGPFE 353
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755522749 253 VESALAEHPAVLESAVVSSPDPIRGEVVKAFIVLSPAYASHDpeALTRELQEHVKTVTAPYKYPRKVAFISELPKTVSGK 332
Cdd:cd05969 354 VESALMEHPAVAEAGVIGKPDPLRGEIIKAFISLKEGFEPSD--ELKEEIINFVRQKLGAHVAPREIEFVDNLPKTRSGK 431
|
330
....*....|
gi 755522749 333 ILRSKLRNQE 342
Cdd:cd05969 432 IMRRVLKAKE 441
|
|
| MACS_like_3 |
cd05971 |
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the ... |
13-339 |
4.34e-96 |
|
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: 292.03 E-value: 4.34e-96
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755522749 13 RVCLG---GLKTRRWMALTESDIFWNTTDTGWVKAAW-TLFSAWSNGACIFVHELPRVDAKTILNTLCRFPITTLCCVPT 88
Cdd:cd05971 111 RVLLGhlpGVQFPFNLFPRDGDLYWTPADWAWIGGLLdVLLPSLYFGVPVLAHRMTKFDPKAALDLMSRYGVTTAFLPPT 190
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755522749 89 LFRLLVQEDLTRYKFQC-LRHCLTGGEALNPDVRDKWKSQTGLELHEGYGQSETVVICGNSRN-STIKSGSMGKASPPYD 166
Cdd:cd05971 191 ALKMMRQQGEQLKHAQVkLRAIATGGESLGEELLGWAREQFGVEVNEFYGQTECNLVIGNCSAlFPIKPGSMGKPIPGHR 270
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755522749 167 VQIVDEEGNVLPPGKEGNIAVRiKPTrPFCFFNcYLDNPEKTAASEQGDFYITGDRAHMDEDGYFWFLGRNDDVINSSSY 246
Cdd:cd05971 271 VAIVDDNGTPLPPGEVGEIAVE-LPD-PVAFLG-YWNNPSATEKKMAGDWLLTGDLGRKDSDGYFWYVGRDDDVITSSGY 347
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755522749 247 RIGPVEVESALAEHPAVLESAVVSSPDPIRGEVVKAFIVLSPAYAshDPEALTRELQEHVKTVTAPYKYPRKVAFISELP 326
Cdd:cd05971 348 RIGPAEIEECLLKHPAVLMAAVVGIPDPIRGEIVKAFVVLNPGET--PSDALAREIQELVKTRLAAHEYPREIEFVNELP 425
|
330
....*....|...
gi 755522749 327 KTVSGKILRSKLR 339
Cdd:cd05971 426 RTATGKIRRRELR 438
|
|
| AFD_class_I |
cd04433 |
Adenylate forming domain, Class I, also known as the ANL superfamily; This family is known as ... |
21-334 |
7.60e-94 |
|
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: 282.64 E-value: 7.60e-94
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755522749 21 TRRWMALTESDIFWNTTDTGWVKAAWTLFSAWSNGACIFVHelPRVDAKTILNTLCRFPITTLCCVPTLFRLLVQEDL-T 99
Cdd:cd04433 32 LAASGGLTEGDVFLSTLPLFHIGGLFGLLGALLAGGTVVLL--PKFDPEAALELIEREKVTILLGVPTLLARLLKAPEsA 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755522749 100 RYKFQCLRHCLTGGEALNPDVRDKWKSQTGLELHEGYGQSET--VVICGNSRNSTIKSGSMGKASPPYDVQIVDEEGNVL 177
Cdd:cd04433 110 GYDLSSLRALVSGGAPLPPELLERFEEAPGIKLVNGYGLTETggTVATGPPDDDARKPGSVGRPVPGVEVRIVDPDGGEL 189
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755522749 178 PPGKEGNIAVRIkPTRpfcfFNCYLDNPEKTAASEQGDFYITGDRAHMDEDGYFWFLGRNDDVINSSSYRIGPVEVESAL 257
Cdd:cd04433 190 PPGEIGELVVRG-PSV----MKGYWNNPEATAAVDEDGWYRTGDLGRLDEDGYLYIVGRLKDMIKSGGENVYPAEVEAVL 264
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 755522749 258 AEHPAVLESAVVSSPDPIRGEVVKAFIVLSPAyASHDPEaltrELQEHVKTVTAPYKYPRKVAFISELPKTVSGKIL 334
Cdd:cd04433 265 LGHPGVAEAAVVGVPDPEWGERVVAVVVLRPG-ADLDAE----ELRAHVRERLAPYKVPRRVVFVDALPRTASGKID 336
|
|
| PRK04319 |
PRK04319 |
acetyl-CoA synthetase; Provisional |
21-344 |
2.30e-93 |
|
acetyl-CoA synthetase; Provisional
Pssm-ID: 235279 [Multi-domain] Cd Length: 570 Bit Score: 289.10 E-value: 2.30e-93
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755522749 21 TRRW-MALTESDIFWNTTDTGWVKA-AWTLFSAWSNGACIFVHElPRVDAKTILNTLCRFPITTLCCVPTLFRLLV---Q 95
Cdd:PRK04319 236 TGKYvLDLHEDDVYWCTADPGWVTGtSYGIFAPWLNGATNVIDG-GRFSPERWYRILEDYKVTVWYTAPTAIRMLMgagD 314
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755522749 96 EDLTRYKFQCLRHCLTGGEALNPDVRdKW-KSQTGLELHEGYGQSET--VVICgNSRNSTIKSGSMGKASPPYDVQIVDE 172
Cdd:PRK04319 315 DLVKKYDLSSLRHILSVGEPLNPEVV-RWgMKVFGLPIHDNWWMTETggIMIA-NYPAMDIKPGSMGKPLPGIEAAIVDD 392
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755522749 173 EGNVLPPGKEGNIAvrIKPTRPfCFFNCYLDNPEKTAASEQGDFYITGDRAHMDEDGYFWFLGRNDDVINSSSYRIGPVE 252
Cdd:PRK04319 393 QGNELPPNRMGNLA--IKKGWP-SMMRGIWNNPEKYESYFAGDWYVSGDSAYMDEDGYFWFQGRVDDVIKTSGERVGPFE 469
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755522749 253 VESALAEHPAVLESAVVSSPDPIRGEVVKAFIVLSPAYASHDpeALTRELQEHVKTVTAPYKYPRKVAFISELPKTVSGK 332
Cdd:PRK04319 470 VESKLMEHPAVAEAGVIGKPDPVRGEIIKAFVALRPGYEPSE--ELKEEIRGFVKKGLGAHAAPREIEFKDKLPKTRSGK 547
|
330
....*....|..
gi 755522749 333 ILRSKLRNQEWG 344
Cdd:PRK04319 548 IMRRVLKAWELG 559
|
|
| MACS_like_2 |
cd05973 |
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the ... |
27-340 |
2.24e-84 |
|
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: 262.07 E-value: 2.24e-84
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755522749 27 LTESDIFWNTTDTGWvkaAWTLFSAWSNG-----ACIFVHELPRVDakTILNTLCRFPITTLCCVPTLFRLLVQ---EDL 98
Cdd:cd05973 126 LRPEDSFWNAADPGW---AYGLYYAITGPlalghPTILLEGGFSVE--STWRVIERLGVTNLAGSPTAYRLLMAagaEVP 200
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755522749 99 TRYKFQcLRHCLTGGEALNPDVRDKWKSQTGLELHEGYGQSETVVICGNSRN--STIKSGSMGKASPPYDVQIVDEEGNV 176
Cdd:cd05973 201 ARPKGR-LRRVSSAGEPLTPEVIRWFDAALGVPIHDHYGQTELGMVLANHHAleHPVHAGSAGRAMPGWRVAVLDDDGDE 279
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755522749 177 LPPGKEGNIAVRIKPTrPFCFFNCYLDNPEKTAAseqGDFYITGDRAHMDEDGYFWFLGRNDDVINSSSYRIGPVEVESA 256
Cdd:cd05973 280 LGPGEPGRLAIDIANS-PLMWFRGYQLPDTPAID---GGYYLTGDTVEFDPDGSFSFIGRADDVITMSGYRIGPFDVESA 355
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755522749 257 LAEHPAVLESAVVSSPDPIRGEVVKAFIVLSPAyasHDP-EALTRELQEHVKTVTAPYKYPRKVAFISELPKTVSGKILR 335
Cdd:cd05973 356 LIEHPAVAEAAVIGVPDPERTEVVKAFVVLRGG---HEGtPALADELQLHVKKRLSAHAYPRTIHFVDELPKTPSGKIQR 432
|
....*
gi 755522749 336 SKLRN 340
Cdd:cd05973 433 FLLRR 437
|
|
| ABCL |
cd05958 |
2-aminobenzoate-CoA ligase (ABCL); ABCL catalyzes the initial step in the 2-aminobenzoate ... |
27-339 |
4.54e-81 |
|
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: 253.55 E-value: 4.54e-81
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755522749 27 LTESDIFwnttdTGWVKAAWT------LFSAWSNGACIFVheLPRVDAKTILNTLCRFPITTLCCVPTLFRLLV------ 94
Cdd:cd05958 136 LREDDRF-----VGSPPLAFTfglggvLLFPFGVGASGVL--LEEATPDLLLSAIARYKPTVLFTAPTAYRAMLahpdaa 208
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755522749 95 QEDLTrykfqCLRHCLTGGEALNPDVRDKWKSQTGLELHEGYGQSETVVICGNSRNSTIKSGSMGKASPPYDVQIVDEEG 174
Cdd:cd05958 209 GPDLS-----SLRKCVSAGEALPAALHRAWKEATGIPIIDGIGSTEMFHIFISARPGDARPGATGKPVPGYEAKVVDDEG 283
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755522749 175 NVLPPGKEGNIAVRiKPTrpfcffNCYLDNPEKTAASEQGDFYITGDRAHMDEDGYFWFLGRNDDVINSSSYRIGPVEVE 254
Cdd:cd05958 284 NPVPDGTIGRLAVR-GPT------GCRYLADKRQRTYVQGGWNITGDTYSRDPDGYFRHQGRSDDMIVSGGYNIAPPEVE 356
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755522749 255 SALAEHPAVLESAVVSSPDPIRGEVVKAFIVLSPAYAShdPEALTRELQEHVKTVTAPYKYPRKVAFISELPKTVSGKIL 334
Cdd:cd05958 357 DVLLQHPAVAECAVVGHPDESRGVVVKAFVVLRPGVIP--GPVLARELQDHAKAHIAPYKYPRAIEFVTELPRTATGKLQ 434
|
....*
gi 755522749 335 RSKLR 339
Cdd:cd05958 435 RFALR 439
|
|
| FC-FACS_FadD_like |
cd05936 |
Prokaryotic long-chain fatty acid CoA synthetases similar to Escherichia coli FadD; This ... |
48-339 |
1.96e-79 |
|
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: 250.17 E-value: 1.96e-79
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755522749 48 LFSAWSNGACIFVheLPRVDAKTILNTLCRFPITTLCCVPTLF-RLLVQEDLTRYKFQCLRHCLTGGEALNPDVRDKWKS 126
Cdd:cd05936 187 LLLPLALGATIVL--IPRFRPIGVLKEIRKHRVTIFPGVPTMYiALLNAPEFKKRDFSSLRLCISGGAPLPVEVAERFEE 264
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755522749 127 QTGLELHEGYGQSETV-VICGNSRNSTIKSGSMGKASPPYDVQIVDEEGNVLPPGKEGNIAVRiKPTRpfcfFNCYLDNP 205
Cdd:cd05936 265 LTGVPIVEGYGLTETSpVVAVNPLDGPRKPGSIGIPLPGTEVKIVDDDGEELPPGEVGELWVR-GPQV----MKGYWNRP 339
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755522749 206 EKTAASEQGDFYITGDRAHMDEDGYFWFLGRNDDVINSSSYRIGPVEVESALAEHPAVLESAVVSSPDPIRGEVVKAFIV 285
Cdd:cd05936 340 EETAEAFVDGWLRTGDIGYMDEDGYFFIVDRKKDMIIVGGFNVYPREVEEVLYEHPAVAEAAVVGVPDPYSGEAVKAFVV 419
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*
gi 755522749 286 LspayasHDPEALT-RELQEHVKTVTAPYKYPRKVAFISELPKTVSGKILRSKLR 339
Cdd:cd05936 420 L------KEGASLTeEEIIAFCREQLAGYKVPRQVEFRDELPKSAVGKILRRELR 468
|
|
| BCL_4HBCL |
cd05959 |
Benzoate CoA ligase (BCL) and 4-Hydroxybenzoate-Coenzyme A Ligase (4-HBA-CoA ligase); Benzoate ... |
22-339 |
5.84e-77 |
|
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: 244.97 E-value: 5.84e-77
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755522749 22 RRWMALTESDIFWNTTdtgwvkaawTLFSAWSNG-ACIF--------VHELPRVDAKTILNTLCRFPITTLCCVPTLFR- 91
Cdd:cd05959 197 RNVLGIREDDVCFSAA---------KLFFAYGLGnSLTFplsvgattVLMPERPTPAAVFKRIRRYRPTVFFGVPTLYAa 267
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755522749 92 LLVQEDLTRYKFQCLRHCLTGGEALNPDVRDKWKSQTGLELHEGYGQSETVVICGNSRNSTIKSGSMGKASPPYDVQIVD 171
Cdd:cd05959 268 MLAAPNLPSRDLSSLRLCVSAGEALPAEVGERWKARFGLDILDGIGSTEMLHIFLSNRPGRVRYGTTGKPVPGYEVELRD 347
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755522749 172 EEGNVLPPGKEGNIAVRIKPTRPFcffncYLDNPEKTAASEQGDFYITGDRAHMDEDGYFWFLGRNDDVINSSSYRIGPV 251
Cdd:cd05959 348 EDGGDVADGEPGELYVRGPSSATM-----YWNNRDKTRDTFQGEWTRTGDKYVRDDDGFYTYAGRADDMLKVSGIWVSPF 422
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755522749 252 EVESALAEHPAVLESAVVSSPDPIRGEVVKAFIVLSPAYAshDPEALTRELQEHVKTVTAPYKYPRKVAFISELPKTVSG 331
Cdd:cd05959 423 EVESALVQHPAVLEAAVVGVEDEDGLTKPKAFVVLRPGYE--DSEALEEELKEFVKDRLAPYKYPRWIVFVDELPKTATG 500
|
....*...
gi 755522749 332 KILRSKLR 339
Cdd:cd05959 501 KIQRFKLR 508
|
|
| BCL_like |
cd05919 |
Benzoate CoA ligase (BCL) and similar adenylate forming enzymes; This family contains benzoate ... |
48-339 |
2.19e-69 |
|
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: 223.11 E-value: 2.19e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755522749 48 LFSAWSNGACIFVHELPRvDAKTILNTLCRFPITTLCCVPTLF-RLLVQEDLTRYKFQCLRHCLTGGEALNPDVRDKWKS 126
Cdd:cd05919 152 LWFPLAVGASAVLNPGWP-TAERVLATLARFRPTVLYGVPTFYaNLLDSCAGSPDALRSLRLCVSAGEALPRGLGERWME 230
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755522749 127 QTGLELHEGYGQSETVVICGNSRNSTIKSGSMGKASPPYDVQIVDEEGNVLPPGKEGNIAVRiKPTRpfcfFNCYLDNPE 206
Cdd:cd05919 231 HFGGPILDGIGATEVGHIFLSNRPGAWRLGSTGRPVPGYEIRLVDEEGHTIPPGEEGDLLVR-GPSA----AVGYWNNPE 305
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755522749 207 KTAASEQGDFYITGDRAHMDEDGYFWFLGRNDDVINSSSYRIGPVEVESALAEHPAVLESAVVSSPDPIRGEVVKAFIVL 286
Cdd:cd05919 306 KSRATFNGGWYRTGDKFCRDADGWYTHAGRADDMLKVGGQWVSPVEVESLIIQHPAVAEAAVVAVPESTGLSRLTAFVVL 385
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|...
gi 755522749 287 SPAYASHdpEALTRELQEHVKTVTAPYKYPRKVAFISELPKTVSGKILRSKLR 339
Cdd:cd05919 386 KSPAAPQ--ESLARDIHRHLLERLSAHKVPRRIAFVDELPRTATGKLQRFKLR 436
|
|
| PRK06187 |
PRK06187 |
long-chain-fatty-acid--CoA ligase; Validated |
44-343 |
1.31e-65 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 235730 [Multi-domain] Cd Length: 521 Bit Score: 215.44 E-value: 1.31e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755522749 44 AAWTL-FSAWSNGACIFVHElpRVDAKTILNTLCRFPITTLCCVPTLFRLLVQEDLTR-YKFQCLRHCLTGGEALNPDVR 121
Cdd:PRK06187 221 HAWGLpYLALMAGAKQVIPR--RFDPENLLDLIETERVTFFFAVPTIWQMLLKAPRAYfVDFSSLRLVIYGGAALPPALL 298
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755522749 122 DKWKSQTGLELHEGYGQSETV-VICGN-----SRNSTIKSGSMGKASPPYDVQIVDEEGNVLPP-GKE-GNIAVRiKPtr 193
Cdd:PRK06187 299 REFKEKFGIDLVQGYGMTETSpVVSVLppedqLPGQWTKRRSAGRPLPGVEARIVDDDGDELPPdGGEvGEIIVR-GP-- 375
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755522749 194 pfCFFNCYLDNPEKTAASEQGDFYITGDRAHMDEDGYFWFLGRNDDVINSSSYRIGPVEVESALAEHPAVLESAVVSSPD 273
Cdd:PRK06187 376 --WLMQGYWNRPEATAETIDGGWLHTGDVGYIDEDGYLYITDRIKDVIISGGENIYPRELEDALYGHPAVAEVAVIGVPD 453
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755522749 274 PIRGEVVKAFIVLSPAyASHDPEaltrELQEHVKTVTAPYKYPRKVAFISELPKTVSGKILRSKLRNQEW 343
Cdd:PRK06187 454 EKWGERPVAVVVLKPG-ATLDAK----ELRAFLRGRLAKFKLPKRIAFVDELPRTSVGKILKRVLREQYA 518
|
|
| FACL_FadD13-like |
cd17631 |
fatty acyl-CoA synthetase, including FadD13; This family contains fatty acyl-CoA synthetases, ... |
60-335 |
5.55e-65 |
|
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: 211.70 E-value: 5.55e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755522749 60 VHELPRVDAKTILNTLCRFPITTLCCVPTLFRLLVQ-EDLTRYKFQCLRHCLTGGEALNPDVRDKWKSqTGLELHEGYGQ 138
Cdd:cd17631 168 VVILRKFDPETVLDLIERHRVTSFFLVPTMIQALLQhPRFATTDLSSLRAVIYGGAPMPERLLRALQA-RGVKFVQGYGM 246
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755522749 139 SETV-VICGNSRNSTI-KSGSMGKASPPYDVQIVDEEGNVLPPGKEGNIAVRiKPTRpfcfFNCYLDNPEKTAASEQGDF 216
Cdd:cd17631 247 TETSpGVTFLSPEDHRrKLGSAGRPVFFVEVRIVDPDGREVPPGEVGEIVVR-GPHV----MAGYWNRPEATAAAFRDGW 321
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755522749 217 YITGDRAHMDEDGYFWFLGRNDDVINSSSYRIGPVEVESALAEHPAVLESAVVSSPDPIRGEVVKAFIVLSPayaSHDPE 296
Cdd:cd17631 322 FHTGDLGRLDEDGYLYIVDRKKDMIISGGENVYPAEVEDVLYEHPAVAEVAVIGVPDEKWGEAVVAVVVPRP---GAELD 398
|
250 260 270
....*....|....*....|....*....|....*....
gi 755522749 297 ALtrELQEHVKTVTAPYKYPRKVAFISELPKTVSGKILR 335
Cdd:cd17631 399 ED--ELIAHCRERLARYKIPKSVEFVDALPRNATGKILK 435
|
|
| FACL_DitJ_like |
cd05934 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
14-339 |
3.97e-63 |
|
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: 206.37 E-value: 3.97e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755522749 14 VCLGGLKTRRWMALTESDIFWNTTDTGWVKA-AWTLFSAWSNGACIFVheLPRVDAKTILNTLCRFPITTLCCVPTLFR- 91
Cdd:cd05934 106 LTFAGYYSARRFGLGEDDVYLTVLPLFHINAqAVSVLAALSVGATLVL--LPRFSASRFWSDVRRYGATVTNYLGAMLSy 183
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755522749 92 LLVQEDLTRYKFQCLRhcLTGGEALNPDVRDKWKSQTGLELHEGYGQSETVVICGNSRNSTIKSGSMGKASPPYDVQIVD 171
Cdd:cd05934 184 LLAQPPSPDDRAHRLR--AAYGAPNPPELHEEFEERFGVRLLEGYGMTETIVGVIGPRDEPRRPGSIGRPAPGYEVRIVD 261
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755522749 172 EEGNVLPPGKEGNIAVRikPTRPFCFFNCYLDNPEKTAASEQGDFYITGDRAHMDEDGYFWFLGRNDDVINSSSYRIGPV 251
Cdd:cd05934 262 DDGQELPAGEPGELVIR--GLRGWGFFKGYYNMPEATAEAMRNGWFHTGDLGYRDADGFFYFVDRKKDMIRRRGENISSA 339
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755522749 252 EVESALAEHPAVLESAVVSSPDPIRGEVVKAFIVLSPAyASHDPEALTRELQEHVktvtAPYKYPRKVAFISELPKTVSG 331
Cdd:cd05934 340 EVERAILRHPAVREAAVVAVPDEVGEDEVKAVVVLRPG-ETLDPEELFAFCEGQL----AYFKVPRYIRFVDDLPKTPTE 414
|
....*...
gi 755522749 332 KILRSKLR 339
Cdd:cd05934 415 KVAKAQLR 422
|
|
| MCS |
cd05941 |
Malonyl-CoA synthetase (MCS); MCS catalyzes the formation of malonyl-CoA in a two-step ... |
52-340 |
5.61e-59 |
|
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: 196.36 E-value: 5.61e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755522749 52 WSNGACIFvheLPRVDAKTILNTLCRFPITTLCCVPTLFRLLVQ---------EDLTRYKFQCLRHCLTGGEALNPDVRD 122
Cdd:cd05941 154 FAGASVEF---LPKFDPKEVAISRLMPSITVFMGVPTIYTRLLQyyeahftdpQFARAAAAERLRLMVSGSAALPVPTLE 230
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755522749 123 KWKSQTGLELHEGYGQSETVVICGNSRNSTIKSGSMGKASPPYDVQIVDEEGN-VLPPGKEGNIAVRiKPTrpfcFFNCY 201
Cdd:cd05941 231 EWEAITGHTLLERYGMTEIGMALSNPLDGERRPGTVGMPLPGVQARIVDEETGePLPRGEVGEIQVR-GPS----VFKEY 305
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755522749 202 LDNPEKTAASEQGD-FYITGDRAHMDEDGYFWFLGR-NDDVINSSSYRIGPVEVESALAEHPAVLESAVVSSPDPIRGEV 279
Cdd:cd05941 306 WNKPEATKEEFTDDgWFKTGDLGVVDEDGYYWILGRsSVDIIKSGGYKVSALEIERVLLAHPGVSECAVIGVPDPDWGER 385
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 755522749 280 VKAFIVLSPAYASHDPEaltrELQEHVKTVTAPYKYPRKVAFISELPKTVSGKILRSKLRN 340
Cdd:cd05941 386 VVAVVVLRAGAAALSLE----ELKEWAKQRLAPYKRPRRLILVDELPRNAMGKVNKKELRK 442
|
|
| PrpE |
cd05967 |
Propionyl-CoA synthetase (PrpE); EC 6.2.1.17: propanoate:CoA ligase (AMP-forming) or ... |
31-340 |
8.53e-59 |
|
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: 199.85 E-value: 8.53e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755522749 31 DIFWNTTDTGWVKA-AWTLFSAWSNGACIFVHELPRV---DAKTILNTLCRFPITTLCCVPTLFRLLVQED-----LTRY 101
Cdd:cd05967 273 DVWWAASDVGWVVGhSYIVYGPLLHGATTVLYEGKPVgtpDPGAFWRVIEKYQVNALFTAPTAIRAIRKEDpdgkyIKKY 352
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755522749 102 KFQCLRHCLTGGEALNPDVRDKWKSQTGLELHEGYGQSET-VVICGNSRN---STIKSGSMGKASPPYDVQIVDEEGNVL 177
Cdd:cd05967 353 DLSSLRTLFLAGERLDPPTLEWAENTLGVPVIDHWWQTETgWPITANPVGlepLPIKAGSPGKPVPGYQVQVLDEDGEPV 432
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755522749 178 PPGKEGNIAVRIkPTRPFCFFNCYLDNP--EKTAASEQGDFYITGDRAHMDEDGYFWFLGRNDDVINSSSYRIGPVEVES 255
Cdd:cd05967 433 GPNELGNIVIKL-PLPPGCLLTLWKNDErfKKLYLSKFPGYYDTGDAGYKDEDGYLFIMGRTDDVINVAGHRLSTGEMEE 511
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755522749 256 ALAEHPAVLESAVVSSPDPIRGEVVKAFIVLSPAYaSHDPEALTRELQEHVKTVTAPYKYPRKVAFISELPKTVSGKILR 335
Cdd:cd05967 512 SVLSHPAVAECAVVGVRDELKGQVPLGLVVLKEGV-KITAEELEKELVALVREQIGPVAAFRLVIFVKRLPKTRSGKILR 590
|
....*
gi 755522749 336 SKLRN 340
Cdd:cd05967 591 RTLRK 595
|
|
| Ac_CoA_lig_AcsA |
TIGR02188 |
acetate--CoA ligase; This model describes acetate-CoA ligase (EC 6.2.1.1), also called ... |
29-339 |
2.08e-55 |
|
acetate--CoA ligase; This model describes acetate-CoA ligase (EC 6.2.1.1), also called acetyl-CoA synthetase and acetyl-activating enzyme. It catalyzes the reaction ATP + acetate + CoA = AMP + diphosphate + acetyl-CoA and belongs to the family of AMP-binding enzymes described by pfam00501.
Pssm-ID: 274022 [Multi-domain] Cd Length: 626 Bit Score: 190.92 E-value: 2.08e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755522749 29 ESDIFWNTTDTGWVKA-AWTLFSAWSNGACIFVHE-LPRV-DAKTILNTLCRFPITTLCCVPTLFRLLVQ---EDLTRYK 102
Cdd:TIGR02188 278 DGDIFWCTADVGWITGhSYIVYGPLANGATTVMFEgVPTYpDPGRFWEIIEKHKVTIFYTAPTAIRALMRlgdEWVKKHD 357
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755522749 103 FQCLRHCLTGGEALNPDVRDKWKSQTGLE---LHEGYGQSETVVICGNSRNSTI--KSGSMGKASPPYDVQIVDEEGNVL 177
Cdd:TIGR02188 358 LSSLRLLGSVGEPINPEAWMWYYKVVGKErcpIVDTWWQTETGGIMITPLPGATptKPGSATLPFFGIEPAVVDEEGNPV 437
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755522749 178 PPGKEGNIAVrIKPTRPFCFFNCYLDnPE---KTAASEQGDFYITGDRAHMDEDGYFWFLGRNDDVINSSSYRIGPVEVE 254
Cdd:TIGR02188 438 EGPGEGGYLV-IKQPWPGMLRTIYGD-HErfvDTYFSPFPGYYFTGDGARRDKDGYIWITGRVDDVINVSGHRLGTAEIE 515
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755522749 255 SALAEHPAVLESAVVSSPDPIRGEVVKAFIVLSPAYASHDpeALTRELQEHVKTVTAPYKYPRKVAFISELPKTVSGKIL 334
Cdd:TIGR02188 516 SALVSHPAVAEAAVVGIPDDIKGQAIYAFVTLKDGYEPDD--ELRKELRKHVRKEIGPIAKPDKIRFVPGLPKTRSGKIM 593
|
....*
gi 755522749 335 RSKLR 339
Cdd:TIGR02188 594 RRLLR 598
|
|
| benz_CoA_lig |
TIGR02262 |
benzoate-CoA ligase family; Characterized members of this protein family include benzoate-CoA ... |
19-339 |
6.10e-55 |
|
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: 187.35 E-value: 6.10e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755522749 19 LKTRRWMALTESDIfwnttdtgwVKAAWTLFSAWSNGACIF-----------VHELPRVDAktILNTLCRFPITTLCCVP 87
Cdd:TIGR02262 192 LYARNTLGIREDDV---------CFSAAKLFFAYGLGNALTfpmsvgattvlMGERPTPDA--VFDRLRRHQPTIFYGVP 260
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755522749 88 TLFR-LLVQEDLTRYKFQCLRHCLTGGEALNPDVRDKWKSQTGLELHEGYGQSETVVICGNSRNSTIKSGSMGKASPPYD 166
Cdd:TIGR02262 261 TLYAaMLADPNLPSEDQVRLRLCTSAGEALPAEVGQRWQARFGVDIVDGIGSTEMLHIFLSNLPGDVRYGTSGKPVPGYR 340
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755522749 167 VQIVDEEGNVLPPGKEGNIAVRiKPTRPFCFFNcyldNPEKTAASEQGDFYITGDRAHMDEDGYFWFLGRNDDVINSSSY 246
Cdd:TIGR02262 341 LRLVGDGGQDVADGEPGELLIS-GPSSATMYWN----NRAKSRDTFQGEWTRSGDKYVRNDDGSYTYAGRTDDMLKVSGI 415
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755522749 247 RIGPVEVESALAEHPAVLESAVVSSPDPIRGEVVKAFIVLSPAYashdpEALTRELQEHVKTVTAPYKYPRKVAFISELP 326
Cdd:TIGR02262 416 YVSPFEIESALIQHPAVLEAAVVGVADEDGLIKPKAFVVLRPGQ-----TALETELKEHVKDRLAPYKYPRWIVFVDDLP 490
|
330
....*....|...
gi 755522749 327 KTVSGKILRSKLR 339
Cdd:TIGR02262 491 KTATGKIQRFKLR 503
|
|
| PRK08314 |
PRK08314 |
long-chain-fatty-acid--CoA ligase; Validated |
63-345 |
6.70e-55 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236235 [Multi-domain] Cd Length: 546 Bit Score: 187.86 E-value: 6.70e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755522749 63 LPRVDAKTILNTLCRFPITTLCCVPT-LFRLLVQEDLTRYKFQCLRhCLTGGEALNPD-VRDKWKSQTGLELHEGYGQSE 140
Cdd:PRK08314 263 MPRWDREAAARLIERYRVTHWTNIPTmVVDFLASPGLAERDLSSLR-YIGGGGAAMPEaVAERLKELTGLDYVEGYGLTE 341
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755522749 141 TVV-ICGNSRNSTiKSGSMGKASPPYDVQIVD-EEGNVLPPGKEGNIAVRiKPTrpfcFFNCYLDNPEKTAAS----EQG 214
Cdd:PRK08314 342 TMAqTHSNPPDRP-KLQCLGIPTFGVDARVIDpETLEELPPGEVGEIVVH-GPQ----VFKGYWNRPEATAEAfieiDGK 415
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755522749 215 DFYITGDRAHMDEDGYFWFLGRNDDVINSSSYRIGPVEVESALAEHPAVLESAVVSSPDPIRGEVVKAFIVLSPAYASHD 294
Cdd:PRK08314 416 RFFRTGDLGRMDEEGYFFITDRLKRMINASGFKVWPAEVENLLYKHPAIQEACVIATPDPRRGETVKAVVVLRPEARGKT 495
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|.
gi 755522749 295 PEAltrELQEHVKTVTAPYKYPRKVAFISELPKTVSGKILRSKLRNQEWGR 345
Cdd:PRK08314 496 TEE---EIIAWAREHMAAYKYPRIVEFVDSLPKSGSGKILWRQLQEQEKAR 543
|
|
| ACS |
cd05966 |
Acetyl-CoA synthetase (also known as acetate-CoA ligase and acetyl-activating enzyme); ... |
27-340 |
4.95e-53 |
|
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: 184.30 E-value: 4.95e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755522749 27 LTESDIFWNTTDTGWVKA-AWTLFSAWSNGACIFVHE----LPrvDAKTILNTLCRFPITTLCCVPTLFRLLVQ---EDL 98
Cdd:cd05966 270 YHPDDIYWCTADIGWITGhSYIVYGPLANGATTVMFEgtptYP--DPGRYWDIVEKHKVTIFYTAPTAIRALMKfgdEWV 347
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755522749 99 TRYKFQCLRHCLTGGEALNPDVrdkWK---SQTGLE---LHEGYGQSET--VVICGNSRNSTIKSGSMGKASPPYDVQIV 170
Cdd:cd05966 348 KKHDLSSLRVLGSVGEPINPEA---WMwyyEVIGKErcpIVDTWWQTETggIMITPLPGATPLKPGSATRPFFGIEPAIL 424
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755522749 171 DEEGNVLPPGKEGNIAvrIKPTRPFCFFNCYLDNP--EKTAASEQGDFYITGDRAHMDEDGYFWFLGRNDDVINSSSYRI 248
Cdd:cd05966 425 DEEGNEVEGEVEGYLV--IKRPWPGMARTIYGDHEryEDTYFSKFPGYYFTGDGARRDEDGYYWITGRVDDVINVSGHRL 502
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755522749 249 GPVEVESALAEHPAVLESAVVSSPDPIRGEVVKAFIVLSPAYASHDpeALTRELQEHVKTVTAPYKYPRKVAFISELPKT 328
Cdd:cd05966 503 GTAEVESALVAHPAVAEAAVVGRPHDIKGEAIYAFVTLKDGEEPSD--ELRKELRKHVRKEIGPIATPDKIQFVPGLPKT 580
|
330
....*....|..
gi 755522749 329 VSGKILRSKLRN 340
Cdd:cd05966 581 RSGKIMRRILRK 592
|
|
| Firefly_Luc_like |
cd05911 |
Firefly luciferase of light emitting insects and 4-Coumarate-CoA Ligase (4CL); This family ... |
46-334 |
9.37e-53 |
|
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: 180.87 E-value: 9.37e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755522749 46 WTLFSAWsNGACIFVHelPRVDAKTILNTLCRFPITTLCCVPTLFRLLVQ-EDLTRYKFQCLRHCLTGGEALNPDVRDKW 124
Cdd:cd05911 206 TTLASLL-NGATVIIM--PKFDSELFLDLIEKYKITFLYLVPPIAAALAKsPLLDKYDLSSLRVILSGGAPLSKELQELL 282
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755522749 125 KSQTGL-ELHEGYGQSETVVICGNSRNSTIKSGSMGKASPPYDVQIVDEEGN-VLPPGKEGNIAVRIkptrPFCFfNCYL 202
Cdd:cd05911 283 AKRFPNaTIKQGYGMTETGGILTVNPDGDDKPGSVGRLLPNVEAKIVDDDGKdSLGPNEPGEICVRG----PQVM-KGYY 357
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755522749 203 DNPEKTAAS--EQGdFYITGDRAHMDEDGYFWFLGRNDDVINSSSYRIGPVEVESALAEHPAVLESAVVSSPDPIRGEVV 280
Cdd:cd05911 358 NNPEATKETfdEDG-WLHTGDIGYFDEDGYLYIVDRKKELIKYKGFQVAPAELEAVLLEHPGVADAAVIGIPDEVSGELP 436
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*
gi 755522749 281 KAFIVLSPayashDPEALTRELQEHVKTVTAPYKYPRK-VAFISELPKTVSGKIL 334
Cdd:cd05911 437 RAYVVRKP-----GEKLTEKEVKDYVAKKVASYKQLRGgVVFVDEIPKSASGKIL 486
|
|
| LC_FACS_like |
cd05935 |
Putative long-chain fatty acid CoA ligase; The members of this family are putative long-chain ... |
19-338 |
6.14e-52 |
|
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: 177.67 E-value: 6.14e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755522749 19 LKTRRWMALTESDIFWNTTD----TGWVKaawTLFSAWSNGACIFVheLPRVDAKTILNTLCRFPITTLCCVPT-LFRLL 93
Cdd:cd05935 114 LQSAVWTGLTPSDVILACLPlfhvTGFVG---SLNTAVYVGGTYVL--MARWDRETALELIEKYKVTFWTNIPTmLVDLL 188
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755522749 94 VQEDLTRYKFQCLRHCLTGGEALNPDVRDKWKSQTGLELHEGYGQSETVVICGNSRNSTIKSGSMGKASPPYDVQIVD-E 172
Cdd:cd05935 189 ATPEFKTRDLSSLKVLTGGGAPMPPAVAEKLLKLTGLRFVEGYGLTETMSQTHTNPPLRPKLQCLGIP*FGVDARVIDiE 268
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755522749 173 EGNVLPPGKEGNIAVRiKPTrpfcFFNCYLDNPEKTAASEQGD----FYITGDRAHMDEDGYFWFLGRNDDVINSSSYRI 248
Cdd:cd05935 269 TGRELPPNEVGEIVVR-GPQ----IFKGYWNRPEETEESFIEIkgrrFFRTGDLGYMDEEGYFFFVDRVKRMINVSGFKV 343
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755522749 249 GPVEVESALAEHPAVLESAVVSSPDPIRGEVVKAFIVLSPAY-ASHDPEaltrELQEHVKTVTAPYKYPRKVAFISELPK 327
Cdd:cd05935 344 WPAEVEAKLYKHPAI*EVCVISVPDERVGEEVKAFIVLRPEYrGKVTEE----DIIEWAREQMAAYKYPREVEFVDELPR 419
|
330
....*....|.
gi 755522749 328 TVSGKILRSKL 338
Cdd:cd05935 420 SASGKILWRLL 430
|
|
| PRK07656 |
PRK07656 |
long-chain-fatty-acid--CoA ligase; Validated |
43-341 |
6.42e-52 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236072 [Multi-domain] Cd Length: 513 Bit Score: 179.33 E-value: 6.42e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755522749 43 KAAWTlfSAWSNGACIFVHelPRVDAKTILNTLCRFPITTLCCVPTLFR-LLVQEDLTRYKFQCLRHCLTGGEALNP--- 118
Cdd:PRK07656 223 KAGVN--APLMRGATILPL--PVFDPDEVFRLIETERITVLPGPPTMYNsLLQHPDRSAEDLSSLRLAVTGAASMPVall 298
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755522749 119 -DVRDKWKSQTGLElheGYGQSE---TVVICGNSRNSTIKSGSMGKASPPYDVQIVDEEGNVLPPGKEGNIAVRikptrp 194
Cdd:PRK07656 299 eRFESELGVDIVLT---GYGLSEasgVTTFNRLDDDRKTVAGTIGTAIAGVENKIVNELGEEVPVGEVGELLVR------ 369
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755522749 195 fcFFNC---YLDNPEKTAASEQGDFYI-TGDRAHMDEDGYFWFLGRNDDVINSSSYRIGPVEVESALAEHPAVLESAVVS 270
Cdd:PRK07656 370 --GPNVmkgYYDDPEATAAAIDADGWLhTGDLGRLDEEGYLYIVDRKKDMFIVGGFNVYPAEVEEVLYEHPAVAEAAVIG 447
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 755522749 271 SPDPIRGEVVKAFIVLSPAyASHDPEaltrELQEHVKTVTAPYKYPRKVAFISELPKTVSGKILRSKLRNQ 341
Cdd:PRK07656 448 VPDERLGEVGKAYVVLKPG-AELTEE----ELIAYCREHLAKYKVPRSIEFLDELPKNATGKVLKRALREK 513
|
|
| PRK07059 |
PRK07059 |
Long-chain-fatty-acid--CoA ligase; Validated |
64-340 |
9.01e-52 |
|
Long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 235923 [Multi-domain] Cd Length: 557 Bit Score: 179.83 E-value: 9.01e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755522749 64 PRvDAKTILNTLCRFPITTLCCVPTLFR-LLVQEDLTRYKFQCLRHCLTGGEALNPDVRDKWKSQTGLELHEGYGQSETV 142
Cdd:PRK07059 287 PR-DIPGFIKELKKYQVHIFPAVNTLYNaLLNNPDFDKLDFSKLIVANGGGMAVQRPVAERWLEMTGCPITEGYGLSETS 365
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755522749 143 -VICGNSRNSTIKSGSMGKASPPYDVQIVDEEGNVLPPGKEGNIAVRIKPTRPfcffnCYLDNPEKTAASEQGD-FYITG 220
Cdd:PRK07059 366 pVATCNPVDATEFSGTIGLPLPSTEVSIRDDDGNDLPLGEPGEICIRGPQVMA-----GYWNRPDETAKVMTADgFFRTG 440
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755522749 221 DRAHMDEDGYFWFLGRNDDVINSSSYRIGPVEVESALAEHPAVLESAVVSSPDPIRGEVVKAFIVlspayaSHDPeALTR 300
Cdd:PRK07059 441 DVGVMDERGYTKIVDRKKDMILVSGFNVYPNEIEEVVASHPGVLEVAAVGVPDEHSGEAVKLFVV------KKDP-ALTE 513
|
250 260 270 280
....*....|....*....|....*....|....*....|.
gi 755522749 301 E-LQEHVKTVTAPYKYPRKVAFISELPKTVSGKILRSKLRN 340
Cdd:PRK07059 514 EdVKAFCKERLTNYKRPKFVEFRTELPKTNVGKILRRELRD 554
|
|
| PRK08974 |
PRK08974 |
long-chain-fatty-acid--CoA ligase FadD; |
64-342 |
1.15e-51 |
|
long-chain-fatty-acid--CoA ligase FadD;
Pssm-ID: 236359 [Multi-domain] Cd Length: 560 Bit Score: 179.48 E-value: 1.15e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755522749 64 PRvDAKTILNTLCRFPITTLCCVPTLFRLLVQ-EDLTRYKFQCLRHCLTGGEALNPDVRDKWKSQTGLELHEGYGQSE-T 141
Cdd:PRK08974 285 PR-DIPGFVKELKKYPFTAITGVNTLFNALLNnEEFQELDFSSLKLSVGGGMAVQQAVAERWVKLTGQYLLEGYGLTEcS 363
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755522749 142 VVICGNSRNSTIKSGSMGKASPPYDVQIVDEEGNVLPPGKEGNIAVRiKPTrpfcFFNCYLDNPEKTAASEQGDFYITGD 221
Cdd:PRK08974 364 PLVSVNPYDLDYYSGSIGLPVPSTEIKLVDDDGNEVPPGEPGELWVK-GPQ----VMLGYWQRPEATDEVIKDGWLATGD 438
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755522749 222 RAHMDEDGYFWFLGRNDDVINSSSYRIGPVEVESALAEHPAVLESAVVSSPDPIRGEVVKAFIVlspayaSHDPeALTR- 300
Cdd:PRK08974 439 IAVMDEEGFLRIVDRKKDMILVSGFNVYPNEIEDVVMLHPKVLEVAAVGVPSEVSGEAVKIFVV------KKDP-SLTEe 511
|
250 260 270 280
....*....|....*....|....*....|....*....|..
gi 755522749 301 ELQEHVKTVTAPYKYPRKVAFISELPKTVSGKILRSKLRNQE 342
Cdd:PRK08974 512 ELITHCRRHLTGYKVPKLVEFRDELPKSNVGKILRRELRDEA 553
|
|
| ACS-like |
cd17634 |
acetate-CoA ligase; This family includes acyl- and aryl-CoA ligases, as well as the ... |
31-334 |
1.24e-51 |
|
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: 180.08 E-value: 1.24e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755522749 31 DIFWNTTDTGWVKA-AWTLFSAWSNGACIFVHELPRV--DAKTILNTLCRFPITTLCCVPTLFRLLVQED---LTRYKFQ 104
Cdd:cd17634 275 DIYWCTADVGWVTGhSYLLYGPLACGATTLLYEGVPNwpTPARMWQVVDKHGVNILYTAPTAIRALMAAGddaIEGTDRS 354
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755522749 105 CLRHCLTGGEALNPDV-RDKWK--SQTGLELHEGYGQSETV-VICGNSRNST-IKSGSMGKASPPYDVQIVDEEGNVLPP 179
Cdd:cd17634 355 SLRILGSVGEPINPEAyEWYWKkiGKEKCPVVDTWWQTETGgFMITPLPGAIeLKAGSATRPVFGVQPAVVDNEGHPQPG 434
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755522749 180 GKEGNIAVRIK-PTRPFCFFNcylDNPE--KTAASEQGDFYITGDRAHMDEDGYFWFLGRNDDVINSSSYRIGPVEVESA 256
Cdd:cd17634 435 GTEGNLVITDPwPGQTRTLFG---DHERfeQTYFSTFKGMYFSGDGARRDEDGYYWITGRSDDVINVAGHRLGTAEIESV 511
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 755522749 257 LAEHPAVLESAVVSSPDPIRGEVVKAFIVLSPAYAshDPEALTRELQEHVKTVTAPYKYPRKVAFISELPKTVSGKIL 334
Cdd:cd17634 512 LVAHPKVAEAAVVGIPHAIKGQAPYAYVVLNHGVE--PSPELYAELRNWVRKEIGPLATPDVVHWVDSLPKTRSGKIM 587
|
|
| A_NRPS |
cd05930 |
The adenylation domain of nonribosomal peptide synthetases (NRPS); The adenylation (A) domain ... |
23-338 |
3.69e-50 |
|
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: 173.10 E-value: 3.69e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755522749 23 RWMA----LTESDIFWNTTDTGWVKAAWTLFSAWSNGACI-FVHELPRVDAKTILNTLCRFPITTLCCVPTLFRLLVQEd 97
Cdd:cd05930 123 LWMQeaypLTPGDRVLQFTSFSFDVSVWEIFGALLAGATLvVLPEEVRKDPEALADLLAEEGITVLHLTPSLLRLLLQE- 201
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755522749 98 LTRYKFQCLRHCLTGGEALNPDVRDKW-KSQTGLELHEGYGQSETVVIC---------GNSRNSTIksgsmGKASPPYDV 167
Cdd:cd05930 202 LELAALPSLRLVLVGGEALPPDLVRRWrELLPGARLVNLYGPTEATVDAtyyrvppddEEDGRVPI-----GRPIPNTRV 276
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755522749 168 QIVDEEGNVLPPGKEGNIAV------RikptrpfcffnCYLDNPEKTAAS------EQGD-FYITGDRAHMDEDGYFWFL 234
Cdd:cd05930 277 YVLDENLRPVPPGVPGELYIggaglaR-----------GYLNRPELTAERfvpnpfGPGErMYRTGDLVRWLPDGNLEFL 345
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755522749 235 GRNDDVINSSSYRIGPVEVESALAEHPAVLESAVVSSPDPIRGEVVKAFIVlspayASHDPEALTRELQEHVKTVTAPYK 314
Cdd:cd05930 346 GRIDDQVKIRGYRIELGEIEAALLAHPGVREAAVVAREDGDGEKRLVAYVV-----PDEGGELDEEELRAHLAERLPDYM 420
|
330 340
....*....|....*....|....
gi 755522749 315 YPRKVAFISELPKTVSGKILRSKL 338
Cdd:cd05930 421 VPSAFVVLDALPLTPNGKVDRKAL 444
|
|
| FACL_fum10p_like |
cd05926 |
Subfamily of fatty acid CoA ligase (FACL) similar to Fum10p of Gibberella moniliformis; FACL ... |
47-340 |
8.10e-50 |
|
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: 173.27 E-value: 8.10e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755522749 47 TLFSawsnGACIFVHelPRVDAKTILNTLCRFPITTLCCVPTLFRLLVQ--EDLTRYKFQCLRHCLTGGEALNPDVRDKW 124
Cdd:cd05926 212 TLAA----GGSVVLP--PRFSASTFWPDVRDYNATWYTAVPTIHQILLNrpEPNPESPPPKLRFIRSCSASLPPAVLEAL 285
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755522749 125 KSQTGLELHEGYGQSETV--VICGNSRNSTIKSGSMGKASPPyDVQIVDEEGNVLPPGKEGNIAVRIKptrpfcffNC-- 200
Cdd:cd05926 286 EATFGAPVLEAYGMTEAAhqMTSNPLPPGPRKPGSVGKPVGV-EVRILDEDGEILPPGVVGEICLRGP--------NVtr 356
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755522749 201 -YLDNPEKTAAS-EQGDFYITGDRAHMDEDGYFWFLGRNDDVINSSSYRIGPVEVESALAEHPAVLESAVVSSPDPIRGE 278
Cdd:cd05926 357 gYLNNPEANAEAaFKDGWFRTGDLGYLDADGYLFLTGRIKELINRGGEKISPLEVDGVLLSHPAVLEAVAFGVPDEKYGE 436
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 755522749 279 VVKAFIVLSPAYashdpEALTRELQEHVKTVTAPYKYPRKVAFISELPKTVSGKILRSKLRN 340
Cdd:cd05926 437 EVAAAVVLREGA-----SVTEEELRAFCRKHLAAFKVPKKVYFVDELPKTATGKIQRRKVAE 493
|
|
| PRK05605 |
PRK05605 |
long-chain-fatty-acid--CoA ligase; Validated |
63-339 |
4.12e-49 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 235531 [Multi-domain] Cd Length: 573 Bit Score: 172.88 E-value: 4.12e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755522749 63 LPRVDAKTILNTLCRFPITTLCCVPTLFRLLVQE------DLTRykfqcLRHCLTGGEALNPDVRDKWKSQTGLELHEGY 136
Cdd:PRK05605 294 LPAPDIDLILDAMKKHPPTWLPGVPPLYEKIAEAaeergvDLSG-----VRNAFSGAMALPVSTVELWEKLTGGLLVEGY 368
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755522749 137 GQSETV-VICGNSRNSTIKSGSMGKASPPYDVQIVDEE--GNVLPPGKEGNIAVRiKPTRpfcfFNCYLDNPEKTAASEQ 213
Cdd:PRK05605 369 GLTETSpIIVGNPMSDDRRPGYVGVPFPDTEVRIVDPEdpDETMPDGEEGELLVR-GPQV----FKGYWNRPEETAKSFL 443
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755522749 214 GDFYITGDRAHMDEDGYFWFLGRNDDVINSSSYRIGPVEVESALAEHPAVLESAVVSSPDPIRGEVVKAFIVLSPAyASH 293
Cdd:PRK05605 444 DGWFRTGDVVVMEEDGFIRIVDRIKELIITGGFNVYPAEVEEVLREHPGVEDAAVVGLPREDGSEEVVAAVVLEPG-AAL 522
|
250 260 270 280
....*....|....*....|....*....|....*....|....*.
gi 755522749 294 DPEAltreLQEHVKTVTAPYKYPRKVAFISELPKTVSGKILRSKLR 339
Cdd:PRK05605 523 DPEG----LRAYCREHLTRYKVPRRFYHVDELPRDQLGKVRRREVR 564
|
|
| PRK00174 |
PRK00174 |
acetyl-CoA synthetase; Provisional |
29-339 |
5.00e-49 |
|
acetyl-CoA synthetase; Provisional
Pssm-ID: 234677 [Multi-domain] Cd Length: 637 Bit Score: 173.79 E-value: 5.00e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755522749 29 ESDIFWNTTDTGWVKA-AWTLFSAWSNGACIFVHE-LPRV-DAKTILNTLCRFPITTLCCVPTLFRLLVQ---EDLTRYK 102
Cdd:PRK00174 286 DGDVYWCTADVGWVTGhSYIVYGPLANGATTLMFEgVPNYpDPGRFWEVIDKHKVTIFYTAPTAIRALMKegdEHPKKYD 365
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755522749 103 FQCLRhcLTG--GEALNPDVRdKWksqtgleLHEGYGQSETVVIcgnsrnST-------------------IKSGSMGKA 161
Cdd:PRK00174 366 LSSLR--LLGsvGEPINPEAW-EW-------YYKVVGGERCPIV------DTwwqtetggimitplpgatpLKPGSATRP 429
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755522749 162 SPPYDVQIVDEEGNVLPPGKEGNIAVrikpTRPFcffncyldnP-------------EKTAASEQGDFYITGDRAHMDED 228
Cdd:PRK00174 430 LPGIQPAVVDEEGNPLEGGEGGNLVI----KDPW---------PgmmrtiygdherfVKTYFSTFKGMYFTGDGARRDED 496
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755522749 229 GYFWFLGRNDDVINSSSYRIGPVEVESALAEHPAVLESAVVSSPDPIRGEVVKAFIVLSPAYASHDpeALTRELQEHVKT 308
Cdd:PRK00174 497 GYYWITGRVDDVLNVSGHRLGTAEIESALVAHPKVAEAAVVGRPDDIKGQGIYAFVTLKGGEEPSD--ELRKELRNWVRK 574
|
330 340 350
....*....|....*....|....*....|.
gi 755522749 309 VTAPYKYPRKVAFISELPKTVSGKILRSKLR 339
Cdd:PRK00174 575 EIGPIAKPDVIQFAPGLPKTRSGKIMRRILR 605
|
|
| FACL_like_2 |
cd05917 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
56-339 |
1.69e-48 |
|
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: 166.30 E-value: 1.69e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755522749 56 ACIFVHelPRVDAKTILNTLCRFPITTLCCVPTLF-RLLVQEDLTRYKFQCLRHCLTGGEALNPDVRDKWKSQTGL-ELH 133
Cdd:cd05917 71 TMVFPS--PSFDPLAVLEAIEKEKCTALHGVPTMFiAELEHPDFDKFDLSSLRTGIMAGAPCPPELMKRVIEVMNMkDVT 148
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755522749 134 EGYGQSETVVICGNSR-NSTI--KSGSMGKASPPYDVQIVDEEGNVLPP-GKEGNIAVRikptrPFCFFNCYLDNPEKTA 209
Cdd:cd05917 149 IAYGMTETSPVSTQTRtDDSIekRVNTVGRIMPHTEAKIVDPEGGIVPPvGVPGELCIR-----GYSVMKGYWNDPEKTA 223
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755522749 210 ASEQGD-FYITGDRAHMDEDGYFWFLGRNDDVINSSSYRIGPVEVESALAEHPAVLESAVVSSPDPIRGEVVKAFIVLSP 288
Cdd:cd05917 224 EAIDGDgWLHTGDLAVMDEDGYCRIVGRIKDMIIRGGENIYPREIEEFLHTHPKVSDVQVVGVPDERYGEEVCAWIRLKE 303
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|.
gi 755522749 289 ayashDPEALTRELQEHVKTVTAPYKYPRKVAFISELPKTVSGKILRSKLR 339
Cdd:cd05917 304 -----GAELTEEDIKAYCKGKIAHYKVPRYVFFVDEFPLTVSGKIQKFKLR 349
|
|
| PRK07514 |
PRK07514 |
malonyl-CoA synthase; Validated |
48-341 |
3.44e-48 |
|
malonyl-CoA synthase; Validated
Pssm-ID: 181011 [Multi-domain] Cd Length: 504 Bit Score: 169.29 E-value: 3.44e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755522749 48 LFSAwSNGAC------IFvheLPRVDAKTILNTLCRfpITTLCCVPTLF-RLLVQEDLTRYKFQCLRHCLTGGEALNPDV 120
Cdd:PRK07514 212 LFVA-TNVALlagasmIF---LPKFDPDAVLALMPR--ATVMMGVPTFYtRLLQEPRLTREAAAHMRLFISGSAPLLAET 285
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755522749 121 RDKWKSQTGLELHEGYGQSETVVICGNSRNSTIKSGSMGKASPPYDVQIVD-EEGNVLPPGKEGNIAVRiKPTrpfcFFN 199
Cdd:PRK07514 286 HREFQERTGHAILERYGMTETNMNTSNPYDGERRAGTVGFPLPGVSLRVTDpETGAELPPGEIGMIEVK-GPN----VFK 360
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755522749 200 CYLDNPEKTAASEQGD-FYITGDRAHMDEDGYFWFLGRNDDVINSSSYRIGPVEVESALAEHPAVLESAVVSSPDPIRGE 278
Cdd:PRK07514 361 GYWRMPEKTAEEFRADgFFITGDLGKIDERGYVHIVGRGKDLIISGGYNVYPKEVEGEIDELPGVVESAVIGVPHPDFGE 440
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 755522749 279 VVKAFIVLSPAyASHDPEALTRELQEHVktvtAPYKYPRKVAFISELPKTVSGKILRSKLRNQ 341
Cdd:PRK07514 441 GVTAVVVPKPG-AALDEAAILAALKGRL----ARFKQPKRVFFVDELPRNTMGKVQKNLLREQ 498
|
|
| PRK06710 |
PRK06710 |
long-chain-fatty-acid--CoA ligase; Validated |
63-342 |
7.06e-48 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 180666 [Multi-domain] Cd Length: 563 Bit Score: 169.44 E-value: 7.06e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755522749 63 LPRVDAKTILNTLCRFPITTLCCVPTLFRLLVQEDLTR-YKFQCLRHCLTGGEALNPDVRDKWKSQTGLELHEGYGQSET 141
Cdd:PRK06710 281 IPKFDMKMVFEAIKKHKVTLFPGAPTIYIALLNSPLLKeYDISSIRACISGSAPLPVEVQEKFETVTGGKLVEGYGLTES 360
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755522749 142 V-VICGNSRNSTIKSGSMGKASPPYDVQIVD-EEGNVLPPGKEGNIAVRiKPTrpfcFFNCYLDNPEKTAASEQGDFYIT 219
Cdd:PRK06710 361 SpVTHSNFLWEKRVPGSIGVPWPDTEAMIMSlETGEALPPGEIGEIVVK-GPQ----IMKGYWNKPEETAAVLQDGWLHT 435
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755522749 220 GDRAHMDEDGYFWFLGRNDDVINSSSYRIGPVEVESALAEHPAVLESAVVSSPDPIRGEVVKAFIVLspayaSHDPEALT 299
Cdd:PRK06710 436 GDVGYMDEDGFFYVKDRKKDMIVASGFNVYPREVEEVLYEHEKVQEVVTIGVPDPYRGETVKAFVVL-----KEGTECSE 510
|
250 260 270 280
....*....|....*....|....*....|....*....|...
gi 755522749 300 RELQEHVKTVTAPYKYPRKVAFISELPKTVSGKILRSKLRNQE 342
Cdd:PRK06710 511 EELNQFARKYLAAYKVPKVYEFRDELPKTTVGKILRRVLIEEE 553
|
|
| PRK12406 |
PRK12406 |
long-chain-fatty-acid--CoA ligase; Provisional |
64-343 |
2.20e-47 |
|
long-chain-fatty-acid--CoA ligase; Provisional
Pssm-ID: 183506 [Multi-domain] Cd Length: 509 Bit Score: 167.18 E-value: 2.20e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755522749 64 PRVDAKTILNTLCRFPITTLCCVPTLF-RLLVQEDLTRYKF--QCLRHCLTGGEALNPDVR----DKWksqtGLELHEGY 136
Cdd:PRK12406 228 PRFDPEELLQLIERHRITHMHMVPTMFiRLLKLPEEVRAKYdvSSLRHVIHAAAPCPADVKramiEWW----GPVIYEYY 303
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755522749 137 GQSET-VVICGNSRNSTIKSGSMGKASPPYDVQIVDEEGNVLPPGKEGNIAVRIKPTRPFCffncYLDNPEKTAASEQGD 215
Cdd:PRK12406 304 GSTESgAVTFATSEDALSHPGTVGKAAPGAELRFVDEDGRPLPQGEIGEIYSRIAGNPDFT----YHNKPEKRAEIDRGG 379
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755522749 216 FYITGDRAHMDEDGYFWFLGRNDDVINSSSYRIGPVEVESALAEHPAVLESAVVSSPDPIRGEVVKAFIVLSPAyASHDP 295
Cdd:PRK12406 380 FITSGDVGYLDADGYLFLCDRKRDMVISGGVNIYPAEIEAVLHAVPGVHDCAVFGIPDAEFGEALMAVVEPQPG-ATLDE 458
|
250 260 270 280
....*....|....*....|....*....|....*....|....*...
gi 755522749 296 EALTRELQEHVktvtAPYKYPRKVAFISELPKTVSGKILRSKLRNQEW 343
Cdd:PRK12406 459 ADIRAQLKARL----AGYKVPKHIEIMAELPREDSGKIFKRRLRDPYW 502
|
|
| ACLS-CaiC |
cd17637 |
acyl-CoA synthetase (AMP-forming)/AMP-acid ligase II; This family contains fatty acid CoA ... |
87-335 |
3.15e-46 |
|
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: 160.13 E-value: 3.15e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755522749 87 PTLFRLLVQEDLTRYKFQCLRHcLTGGEAlnPDVRDKWKSQTGLELHEGYGQSET--VVICGNSRNstiKSGSMGKASPP 164
Cdd:cd17637 97 PILSNLLDAAEKSGVDLSSLRH-VLGLDA--PETIQRFEETTGATFWSLYGQTETsgLVTLSPYRE---RPGSAGRPGPL 170
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755522749 165 YDVQIVDEEGNVLPPGKEGNIAVRiKPTrpfcFFNCYLDNPEKTAASEQGDFYITGDRAHMDEDGYFWFLGRN--DDVIN 242
Cdd:cd17637 171 VRVRIVDDNDRPVPAGETGEIVVR-GPL----VFQGYWNLPELTAYTFRNGWHHTGDLGRFDEDGYLWYAGRKpeKELIK 245
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755522749 243 SSSYRIGPVEVESALAEHPAVLESAVVSSPDPIRGEVVKAFIVLSPAyashdpEALT-RELQEHVKTVTAPYKYPRKVAF 321
Cdd:cd17637 246 PGGENVYPAEVEKVILEHPAIAEVCVIGVPDPKWGEGIKAVCVLKPG------ATLTaDELIEFVGSRIARYKKPRYVVF 319
|
250
....*....|....
gi 755522749 322 ISELPKTVSGKILR 335
Cdd:cd17637 320 VEALPKTADGSIDR 333
|
|
| PRK08751 |
PRK08751 |
long-chain fatty acid--CoA ligase; |
55-340 |
8.58e-46 |
|
long-chain fatty acid--CoA ligase;
Pssm-ID: 181546 [Multi-domain] Cd Length: 560 Bit Score: 163.89 E-value: 8.58e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755522749 55 GACIFVHELPRvDAKTILNTLCRFPITTLCCVPTLFR-LLVQEDLTRYKFQCLRHCLTGGEALNPDVRDKWKSQTGLELH 133
Cdd:PRK08751 280 GGCNHLISNPR-DMPGFVKELKKTRFTAFTGVNTLFNgLLNTPGFDQIDFSSLKMTLGGGMAVQRSVAERWKQVTGLTLV 358
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755522749 134 EGYGQSETV-VICGNSRNSTIKSGSMGKASPPYDVQIVDEEGNVLPPGKEGNIAVRiKPTrpfcFFNCYLDNPEKTAASE 212
Cdd:PRK08751 359 EAYGLTETSpAACINPLTLKEYNGSIGLPIPSTDACIKDDAGTVLAIGEIGELCIK-GPQ----VMKGYWKRPEETAKVM 433
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755522749 213 QGDFYI-TGDRAHMDEDGYFWFLGRNDDVINSSSYRIGPVEVESALAEHPAVLESAVVSSPDPIRGEVVKAFIVlspaya 291
Cdd:PRK08751 434 DADGWLhTGDIARMDEQGFVYIVDRKKDMILVSGFNVYPNEIEDVIAMMPGVLEVAAVGVPDEKSGEIVKVVIV------ 507
|
250 260 270 280
....*....|....*....|....*....|....*....|....*....
gi 755522749 292 SHDPEALTRELQEHVKTVTAPYKYPRKVAFISELPKTVSGKILRSKLRN 340
Cdd:PRK08751 508 KKDPALTAEDVKAHARANLTGYKQPRIIEFRKELPKTNVGKILRRELRD 556
|
|
| PRK06155 |
PRK06155 |
crotonobetaine/carnitine-CoA ligase; Provisional |
106-341 |
3.39e-45 |
|
crotonobetaine/carnitine-CoA ligase; Provisional
Pssm-ID: 235719 [Multi-domain] Cd Length: 542 Bit Score: 161.85 E-value: 3.39e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755522749 106 LRHCLTGGEAlnPDVRDKWKSQTGLELHEGYGQSETVVICGNSRNSTiKSGSMGKASPPYDVQIVDEEGNVLPPGKEGNI 185
Cdd:PRK06155 296 VRVALGPGVP--AALHAAFRERFGVDLLDGYGSTETNFVIAVTHGSQ-RPGSMGRLAPGFEARVVDEHDQELPDGEPGEL 372
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755522749 186 AVRIKPtrPFCFFNCYLDNPEKTAASEQGDFYITGDRAHMDEDGYFWFLGRNDDVINSSSYRIGPVEVESALAEHPAVLE 265
Cdd:PRK06155 373 LLRADE--PFAFATGYFGMPEKTVEAWRNLWFHTGDRVVRDADGWFRFVDRIKDAIRRRGENISSFEVEQVLLSHPAVAA 450
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 755522749 266 SAVVSSPDPIRGEVVKAFIVLSPAYAShDPEALTRelqeHVKTVTAPYKYPRKVAFISELPKTVSGKILRSKLRNQ 341
Cdd:PRK06155 451 AAVFPVPSELGEDEVMAAVVLRDGTAL-EPVALVR----HCEPRLAYFAVPRYVEFVAALPKTENGKVQKFVLREQ 521
|
|
| PRK05677 |
PRK05677 |
long-chain-fatty-acid--CoA ligase; Validated |
64-342 |
1.50e-44 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 168170 [Multi-domain] Cd Length: 562 Bit Score: 160.70 E-value: 1.50e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755522749 64 PRvDAKTILNTLCRFPITTLCCVPTLFRLLVQ-EDLTRYKFQCLRHCLTGGEALNPDVRDKWKSQTGLELHEGYGQSETV 142
Cdd:PRK05677 286 PR-DLPAMVKELGKWKFSGFVGLNTLFVALCNnEAFRKLDFSALKLTLSGGMALQLATAERWKEVTGCAICEGYGMTETS 364
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755522749 143 -VICGNSRNStIKSGSMGKASPPYDVQIVDEEGNVLPPGKEGNIAVRiKPTrpfcFFNCYLDNPEKTAASEQGDFYI-TG 220
Cdd:PRK05677 365 pVVSVNPSQA-IQVGTIGIPVPSTLCKVIDDDGNELPLGEVGELCVK-GPQ----VMKGYWQRPEATDEILDSDGWLkTG 438
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755522749 221 DRAHMDEDGYFWFLGRNDDVINSSSYRIGPVEVESALAEHPAVLESAVVSSPDPIRGEVVKAFIVLSPAyashdpEALTR 300
Cdd:PRK05677 439 DIALIQEDGYMRIVDRKKDMILVSGFNVYPNELEDVLAALPGVLQCAAIGVPDEKSGEAIKVFVVVKPG------ETLTK 512
|
250 260 270 280
....*....|....*....|....*....|....*....|...
gi 755522749 301 E-LQEHVKTVTAPYKYPRKVAFISELPKTVSGKILRSKLRNQE 342
Cdd:PRK05677 513 EqVMEHMRANLTGYKVPKAVEFRDELPTTNVGKILRRELRDEE 555
|
|
| OSB_CoA_lg |
cd05912 |
O-succinylbenzoate-CoA ligase (also known as O-succinylbenzoate-CoA synthase, OSB-CoA ... |
54-339 |
2.25e-44 |
|
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: 157.12 E-value: 2.25e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755522749 54 NGACIFVHElpRVDAKTILNTLCRFPITTLCCVPTLFRLLVQEDLTRY--KFQCLrhcLTGGEALNPDVRDKWKsQTGLE 131
Cdd:cd05912 142 YGMTVYLVD--KFDAEQVLHLINSGKVTIISVVPTMLQRLLEILGEGYpnNLRCI---LLGGGPAPKPLLEQCK-EKGIP 215
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755522749 132 LHEGYGQSETV--VICGNSRNSTIKSGSMGKASPPYDVQIVDEEGnvlPPGKEGNIAVRiKPTrpfcFFNCYLDNPEKTA 209
Cdd:cd05912 216 VYQSYGMTETCsqIVTLSPEDALNKIGSAGKPLFPVELKIEDDGQ---PPYEVGEILLK-GPN----VTKGYLNRPDATE 287
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755522749 210 ASEQGDFYITGDRAHMDEDGYFWFLGRNDDVINSSSYRIGPVEVESALAEHPAVLESAVVSSPDPIRGEVVKAFIVLSpa 289
Cdd:cd05912 288 ESFENGWFKTGDIGYLDEEGFLYVLDRRSDLIISGGENIYPAEIEEVLLSHPAIKEAGVVGIPDDKWGQVPVAFVVSE-- 365
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|.
gi 755522749 290 yashdpEALTR-ELQEHVKTVTAPYKYPRKVAFISELPKTVSGKILRSKLR 339
Cdd:cd05912 366 ------RPISEeELIAYCSEKLAKYKVPKKIYFVDELPRTASGKLLRHELK 410
|
|
| AMP-binding |
pfam00501 |
AMP-binding enzyme; |
21-244 |
2.37e-44 |
|
AMP-binding enzyme;
Pssm-ID: 459834 [Multi-domain] Cd Length: 417 Bit Score: 157.09 E-value: 2.37e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755522749 21 TRRWMALTESDIFWNTT----DTGWVkaaWTLFSAWSNGACI-FVHELPRVDAKTILNTLCRFPITTLCCVPTLFRLLVQ 95
Cdd:pfam00501 191 RPRGFGLGPDDRVLSTLplfhDFGLS---LGLLGPLLAGATVvLPPGFPALDPAALLELIERYKVTVLYGVPTLLNMLLE 267
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755522749 96 -EDLTRYKFQCLRHCLTGGEALNPDVRDKWKSQTGLELHEGYGQSETVVICGNSRN---STIKSGSMGKASPPYDVQIVD 171
Cdd:pfam00501 268 aGAPKRALLSSLRLVLSGGAPLPPELARRFRELFGGALVNGYGLTETTGVVTTPLPldeDLRSLGSVGRPLPGTEVKIVD 347
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 755522749 172 EE-GNVLPPGKEGNIAVRikptRPfCFFNCYLDNPEKTAAS-EQGDFYITGDRAHMDEDGYFWFLGRNDDVINSS 244
Cdd:pfam00501 348 DEtGEPVPPGEPGELCVR----GP-GVMKGYLNDPELTAEAfDEDGWYRTGDLGRRDEDGYLEIVGRKKDQIKLG 417
|
|
| PRK08276 |
PRK08276 |
long-chain-fatty-acid--CoA ligase; Validated |
64-344 |
2.52e-44 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236215 [Multi-domain] Cd Length: 502 Bit Score: 158.91 E-value: 2.52e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755522749 64 PRVDAKTILNTLCRFPITTLCCVPTLF-RLLV--QEDLTRYKFQCLRHCLTGGEALNPDVR----DKWksqtGLELHEGY 136
Cdd:PRK08276 219 EKFDAEEALALIERYRVTHSQLVPTMFvRMLKlpEEVRARYDVSSLRVAIHAAAPCPVEVKramiDWW----GPIIHEYY 294
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755522749 137 GQSE----TVVicgNSRNSTIKSGSMGKASPPyDVQIVDEEGNVLPPGKEGNIAVRiKPTRPFCffncYLDNPEKTAASE 212
Cdd:PRK08276 295 ASSEgggvTVI---TSEDWLAHPGSVGKAVLG-EVRILDEDGNELPPGEIGTVYFE-MDGYPFE----YHNDPEKTAAAR 365
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755522749 213 QG-DFYITGDRAHMDEDGYFWFLGRNDDVINSSSYRIGPVEVESALAEHPAVLESAVVSSPDPIRGEVVKAfiVLSPAYA 291
Cdd:PRK08276 366 NPhGWVTVGDVGYLDEDGYLYLTDRKSDMIISGGVNIYPQEIENLLVTHPKVADVAVFGVPDEEMGERVKA--VVQPADG 443
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|...
gi 755522749 292 SHDPEALTRELQEHVKTVTAPYKYPRKVAFISELPKTVSGKILRSKLRNQEWG 344
Cdd:PRK08276 444 ADAGDALAAELIAWLRGRLAHYKCPRSIDFEDELPRTPTGKLYKRRLRDRYWE 496
|
|
| 4CL |
cd05904 |
4-Coumarate-CoA Ligase (4CL); 4-Coumarate:coenzyme A ligase is a key enzyme in the ... |
53-338 |
4.13e-44 |
|
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: 158.17 E-value: 4.13e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755522749 53 SNGACIFVheLPRVDAKTILNTLCRFPITTLCCVPTLFRLLVQEDLT-RYKFQCLRHCLTGGEALNPDVRDKWKSQ-TGL 130
Cdd:cd05904 225 RLGATVVV--MPRFDLEELLAAIERYKVTHLPVVPPIVLALVKSPIVdKYDLSSLRQIMSGAAPLGKELIEAFRAKfPNV 302
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755522749 131 ELHEGYGQSET---VVICGNSRNSTIKSGSMGKASPPYDVQIVD-EEGNVLPPGKEGNIAVRiKPtrpfCFFNCYLDNPE 206
Cdd:cd05904 303 DLGQGYGMTEStgvVAMCFAPEKDRAKYGSVGRLVPNVEAKIVDpETGESLPPNQTGELWIR-GP----SIMKGYLNNPE 377
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755522749 207 KTAAS--EQGdFYITGDRAHMDEDGYFWFLGRNDDVINSSSYRIGPVEVESALAEHPAVLESAVVSSPDPIRGEVVKAFI 284
Cdd:cd05904 378 ATAATidKEG-WLHTGDLCYIDEDGYLFIVDRLKELIKYKGFQVAPAELEALLLSHPEILDAAVIPYPDEEAGEVPMAFV 456
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....
gi 755522749 285 VLSPayASHDPEAltrELQEHVKTVTAPYKYPRKVAFISELPKTVSGKILRSKL 338
Cdd:cd05904 457 VRKP--GSSLTED---EIMDFVAKQVAPYKKVRKVAFVDAIPKSPSGKILRKEL 505
|
|
| BACL_like |
cd05929 |
Bacterial Bile acid CoA ligases and similar proteins; Bile acid-Coenzyme A ligase catalyzes ... |
63-339 |
2.34e-43 |
|
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: 155.61 E-value: 2.34e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755522749 63 LPRVDAKTILNTLCRFPITTLCCVPTLF-RLLVQEDLTRYKFQ--CLRHCLTGGEALNPDVRDKWKSQTGLELHEGYGQS 139
Cdd:cd05929 200 MEKFDPEEFLRLIERYRVTFAQFVPTMFvRLLKLPEAVRNAYDlsSLKRVIHAAAPCPPWVKEQWIDWGGPIIWEYYGGT 279
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755522749 140 ETV-VICGNSRNSTIKSGSMGKASPPyDVQIVDEEGNVLPPGKEGNIAVRIKPTrpfcfFNcYLDNPEKTAASEQGDFYI 218
Cdd:cd05929 280 EGQgLTIINGEEWLTHPGSVGRAVLG-KVHILDEDGNEVPPGEIGEVYFANGPG-----FE-YTNDPEKTAAARNEGGWS 352
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755522749 219 T-GDRAHMDEDGYFWFLGRNDDVINSSSYRIGPVEVESALAEHPAVLESAVVSSPDPIRGEVVKAfiVLSPAYASHDPEA 297
Cdd:cd05929 353 TlGDVGYLDEDGYLYLTDRRSDMIISGGVNIYPQEIENALIAHPKVLDAAVVGVPDEELGQRVHA--VVQPAPGADAGTA 430
|
250 260 270 280
....*....|....*....|....*....|....*....|..
gi 755522749 298 LTRELQEHVKTVTAPYKYPRKVAFISELPKTVSGKILRSKLR 339
Cdd:cd05929 431 LAEELIAFLRDRLSRYKCPRSIEFVAELPRDDTGKLYRRLLR 472
|
|
| PRK13390 |
PRK13390 |
acyl-CoA synthetase; Provisional |
22-339 |
2.46e-43 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 139538 [Multi-domain] Cd Length: 501 Bit Score: 156.32 E-value: 2.46e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755522749 22 RRWMALTESDIFWNTTdtgwvkaawTLFSAWSNGACIFVHEL-------PRVDAKTILNTLCRFPITTLCCVPTLF-RLL 93
Cdd:PRK13390 187 RAFYDISESDIYYSSA---------PIYHAAPLRWCSMVHALggtvvlaKRFDAQATLGHVERYRITVTQMVPTMFvRLL 257
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755522749 94 VQED--LTRYKFQCLRHCLTGGEALNPDVRDKWKSQTGLELHEGYGQSE----TVVicgNSRNSTIKSGSMGKaSPPYDV 167
Cdd:PRK13390 258 KLDAdvRTRYDVSSLRAVIHAAAPCPVDVKHAMIDWLGPIVYEYYSSTEahgmTFI---DSPDWLAHPGSVGR-SVLGDL 333
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755522749 168 QIVDEEGNVLPPGKEGNIAVRiKPTRPFCffncYLDNPEKTAASEQ--GDFYIT-GDRAHMDEDGYFWFLGRNDDVINSS 244
Cdd:PRK13390 334 HICDDDGNELPAGRIGTVYFE-RDRLPFR----YLNDPEKTAAAQHpaHPFWTTvGDLGSVDEDGYLYLADRKSFMIISG 408
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755522749 245 SYRIGPVEVESALAEHPAVLESAVVSSPDPIRGEVVKAFIVLSpayASHDP-EALTRELQEHVKTVTAPYKYPRKVAFIS 323
Cdd:PRK13390 409 GVNIYPQETENALTMHPAVHDVAVIGVPDPEMGEQVKAVIQLV---EGIRGsDELARELIDYTRSRIAHYKAPRSVEFVD 485
|
330
....*....|....*.
gi 755522749 324 ELPKTVSGKILRSKLR 339
Cdd:PRK13390 486 ELPRTPTGKLVKGLLR 501
|
|
| prpE |
PRK10524 |
propionyl-CoA synthetase; Provisional |
31-335 |
9.27e-43 |
|
propionyl-CoA synthetase; Provisional
Pssm-ID: 182517 [Multi-domain] Cd Length: 629 Bit Score: 156.65 E-value: 9.27e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755522749 31 DIFWNTTDTGWVKA-AWTLFSAWSNGACIFVHE-LP-RVDAkTILNTLC-RFPITTLCCVPTLFRLLVQED---LTRYKF 103
Cdd:PRK10524 276 ETFFCASDIGWVVGhSYIVYAPLLAGMATIMYEgLPtRPDA-GIWWRIVeKYKVNRMFSAPTAIRVLKKQDpalLRKHDL 354
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755522749 104 QCLRHCLTGGEALN-PDVRdkWKSQT-GLELHEGYGQSET----VVICGNSRNSTIKSGSMGKASPPYDVQIVDEE-GNV 176
Cdd:PRK10524 355 SSLRALFLAGEPLDePTAS--WISEAlGVPVIDNYWQTETgwpiLAIARGVEDRPTRLGSPGVPMYGYNVKLLNEVtGEP 432
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755522749 177 LPPGKEGNIAVRiKPTRPFC----------FFNCYLdnpekTAASEQgdFYITGDRAHMDEDGYFWFLGRNDDVINSSSY 246
Cdd:PRK10524 433 CGPNEKGVLVIE-GPLPPGCmqtvwgdddrFVKTYW-----SLFGRQ--VYSTFDWGIRDADGYYFILGRTDDVINVAGH 504
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755522749 247 RIGPVEVESALAEHPAVLESAVVSSPDPIRGEVVKAFIVLSPAYASHDPE---ALTRELQEHVKTVTAPYKYPRKVAFIS 323
Cdd:PRK10524 505 RLGTREIEESISSHPAVAEVAVVGVKDALKGQVAVAFVVPKDSDSLADREarlALEKEIMALVDSQLGAVARPARVWFVS 584
|
330
....*....|..
gi 755522749 324 ELPKTVSGKILR 335
Cdd:PRK10524 585 ALPKTRSGKLLR 596
|
|
| PRK08316 |
PRK08316 |
acyl-CoA synthetase; Validated |
63-341 |
1.74e-42 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 181381 [Multi-domain] Cd Length: 523 Bit Score: 154.32 E-value: 1.74e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755522749 63 LPRVDAKTILNTLCRFPITTLCCVPTLF-RLLVQEDLTRYKFQCLRHCLTG-----GEALNpDVRDKWksqTGLELHEGY 136
Cdd:PRK08316 244 LDAPDPELILRTIEAERITSFFAPPTVWiSLLRHPDFDTRDLSSLRKGYYGasimpVEVLK-ELRERL---PGLRFYNCY 319
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755522749 137 GQSE-----TVVicgNSRNSTIKSGSMGKASPPYDVQIVDEEGNVLPPGKEGNIAVRikpTRPFCffNCYLDNPEKTAAS 211
Cdd:PRK08316 320 GQTEiaplaTVL---GPEEHLRRPGSAGRPVLNVETRVVDDDGNDVAPGEVGEIVHR---SPQLM--LGYWDDPEKTAEA 391
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755522749 212 EQGDFYITGDRAHMDEDGYFWFLGRNDDVINSSSYRIGPVEVESALAEHPAVLESAVVSSPDPIRGEVVKAFIVLSPAyA 291
Cdd:PRK08316 392 FRGGWFHSGDLGVMDEEGYITVVDRKKDMIKTGGENVASREVEEALYTHPAVAEVAVIGLPDPKWIEAVTAVVVPKAG-A 470
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|
gi 755522749 292 SHDPEaltrELQEHVKTVTAPYKYPRKVAFISELPKTVSGKILRSKLRNQ 341
Cdd:PRK08316 471 TVTED----ELIAHCRARLAGFKVPKRVIFVDELPRNPSGKILKRELRER 516
|
|
| FACL_like_6 |
cd05922 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
48-339 |
1.03e-41 |
|
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: 151.05 E-value: 1.03e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755522749 48 LFSAWSNGACIFVHELPRVDAKTIlnTLCR-FPITTLCCVPTLFRLLVQEDLTRYKFQCLRHCLTGGEALNPDVRDKWKS 126
Cdd:cd05922 176 LNTHLLRGATLVLTNDGVLDDAFW--EDLReHGATGLAGVPSTYAMLTRLGFDPAKLPSLRYLTQAGGRLPQETIARLRE 253
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755522749 127 Q-TGLELHEGYGQSETvvicgnSRNSTI--------KSGSMGKASPPYDVQIVDEEGNVLPPGKEGNIAVRikptRPFCF 197
Cdd:cd05922 254 LlPGAQVYVMYGQTEA------TRRMTYlpperileKPGSIGLAIPGGEFEILDDDGTPTPPGEPGEIVHR----GPNVM 323
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755522749 198 FNCYLDNPEKTAASEQGDFYITGDRAHMDEDGYFWFLGRNDDVINSSSYRIGPVEVESALAEHPAVLESAVVSSPDPIrG 277
Cdd:cd05922 324 KGYWNDPPYRRKEGRGGGVLHTGDLARRDEDGFLFIVGRRDRMIKLFGNRISPTEIEAAARSIGLIIEAAAVGLPDPL-G 402
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 755522749 278 EVVKAFIVLSPAYashDPEALTRELQEhvktVTAPYKYPRKVAFISELPKTVSGKILRSKLR 339
Cdd:cd05922 403 EKLALFVTAPDKI---DPKDVLRSLAE----RLPPYKVPATVRVVDELPLTASGKVDYAALR 457
|
|
| PRK06188 |
PRK06188 |
acyl-CoA synthetase; Validated |
59-344 |
2.05e-41 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 235731 [Multi-domain] Cd Length: 524 Bit Score: 151.29 E-value: 2.05e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755522749 59 FVHELPRVDAKTILNTLCRFPITTLCCVPT-LFRLLVQEDLTRYKFQCLRHCLTGGEALNPdVRdkwksqtgleLHEG-- 135
Cdd:PRK06188 235 TVIVLAKFDPAEVLRAIEEQRITATFLVPTmIYALLDHPDLRTRDLSSLETVYYGASPMSP-VR----------LAEAie 303
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755522749 136 ---------YGQSETV-VIC-----GNSRNSTIKSGSMGKASPPYDVQIVDEEGNVLPPGKEGNIAVRikptRPFcFFNC 200
Cdd:PRK06188 304 rfgpifaqyYGQTEAPmVITylrkrDHDPDDPKRLTSCGRPTPGLRVALLDEDGREVAQGEVGEICVR----GPL-VMDG 378
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755522749 201 YLDNPEKTAASEQGDFYITGDRAHMDEDGYFWFLGRNDDVINSSSYRIGPVEVESALAEHPAVLESAVVSSPDPIRGEVV 280
Cdd:PRK06188 379 YWNRPEETAEAFRDGWLHTGDVAREDEDGFYYIVDRKKDMIVTGGFNVFPREVEDVLAEHPAVAQVAVIGVPDEKWGEAV 458
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 755522749 281 KAFIVLSPAyASHDPEaltrELQEHVKTVTAPYKYPRKVAFISELPKTVSGKILRSKLRNQEWG 344
Cdd:PRK06188 459 TAVVVLRPG-AAVDAA----ELQAHVKERKGSVHAPKQVDFVDSLPLTALGKPDKKALRARYWE 517
|
|
| AACS_like |
cd05968 |
Uncharacterized acyl-CoA synthetase subfamily similar to Acetoacetyl-CoA synthetase; This ... |
32-339 |
3.99e-41 |
|
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: 151.87 E-value: 3.99e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755522749 32 IFWnTTDTGWVKAAWTLFSAWSNGACIFVHE----LPrvDAKTILNTLCRFPITTLCCVPTLFRLLV---QEDLTRYKFQ 104
Cdd:cd05968 281 LTW-FTDLGWMMGPWLIFGGLILGATMVLYDgapdHP--KADRLWRMVEDHEITHLGLSPTLIRALKprgDAPVNAHDLS 357
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755522749 105 CLRHCLTGGEALNPD-----VRDKWKSQT-------GLELHEGygqsetvvICGNSRNSTIKSGSMGKASPPYDVQIVDE 172
Cdd:cd05968 358 SLRVLGSTGEPWNPEpwnwlFETVGKGRNpiinysgGTEISGG--------ILGNVLIKPIKPSSFNGPVPGMKADVLDE 429
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755522749 173 EGNVLPPgKEGNIAVRiKP----TRPFC-----FFNCYLDNPEktaaseqgDFYITGDRAHMDEDGYFWFLGRNDDVINS 243
Cdd:cd05968 430 SGKPARP-EVGELVLL-APwpgmTRGFWrdedrYLETYWSRFD--------NVWVHGDFAYYDEEGYFYILGRSDDTINV 499
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755522749 244 SSYRIGPVEVESALAEHPAVLESAVVSSPDPIRGEVVKAFIVLSPAYAshDPEALTRELQEHVKTVTAPYKYPRKVAFIS 323
Cdd:cd05968 500 AGKRVGPAEIESVLNAHPAVLESAAIGVPHPVKGEAIVCFVVLKPGVT--PTEALAEELMERVADELGKPLSPERILFVK 577
|
330
....*....|....*.
gi 755522749 324 ELPKTVSGKILRSKLR 339
Cdd:cd05968 578 DLPKTRNAKVMRRVIR 593
|
|
| PRK07529 |
PRK07529 |
AMP-binding domain protein; Validated |
77-339 |
6.36e-41 |
|
AMP-binding domain protein; Validated
Pssm-ID: 236043 [Multi-domain] Cd Length: 632 Bit Score: 151.26 E-value: 6.36e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755522749 77 RFPITTLCCVPTLFRLLVQEDLTRYKFQCLRHCLTGGEALNPDVRDKWKSQTGLELHEGYGQSE-TVVICGNSRNSTIKS 155
Cdd:PRK07529 306 RYRINFLSGVPTVYAALLQVPVDGHDISSLRYALCGAAPLPVEVFRRFEAATGVRIVEGYGLTEaTCVSSVNPPDGERRI 385
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755522749 156 GSMGKASPPYDVQIV--DEEGNVL---PPGKEGNIAVRiKPTrpfcFFNCYLdNPEKTAASE-QGDFYITGDRAHMDEDG 229
Cdd:PRK07529 386 GSVGLRLPYQRVRVVilDDAGRYLrdcAVDEVGVLCIA-GPN----VFSGYL-EAAHNKGLWlEDGWLNTGDLGRIDADG 459
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755522749 230 YFWFLGRNDDVINSSSYRIGPVEVESALAEHPAVLESAVVSSPDPIRGEVVKAFIVLSPAyASHDPEaltrELQEHVKTV 309
Cdd:PRK07529 460 YFWLTGRAKDLIIRGGHNIDPAAIEEALLRHPAVALAAAVGRPDAHAGELPVAYVQLKPG-ASATEA----ELLAFARDH 534
|
250 260 270
....*....|....*....|....*....|.
gi 755522749 310 TA-PYKYPRKVAFISELPKTVSGKILRSKLR 339
Cdd:PRK07529 535 IAeRAAVPKHVRILDALPKTAVGKIFKPALR 565
|
|
| caiC |
PRK08008 |
putative crotonobetaine/carnitine-CoA ligase; Validated |
44-339 |
7.40e-41 |
|
putative crotonobetaine/carnitine-CoA ligase; Validated
Pssm-ID: 181195 [Multi-domain] Cd Length: 517 Bit Score: 149.83 E-value: 7.40e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755522749 44 AAWTLFSAwsnGACIFVHElpRVDAKTILNTLCRFPITTLCCVPTLFR-LLVQEDLTRYKFQCLRHCLTggeALNPDVRD 122
Cdd:PRK08008 232 AAMAAFSA---GATFVLLE--KYSARAFWGQVCKYRATITECIPMMIRtLMVQPPSANDRQHCLREVMF---YLNLSDQE 303
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755522749 123 K--WKSQTGLELHEGYGQSETVV-ICGNSRNSTIKSGSMGKASPPYDVQIVDEEGNVLPPGKEGNIAVRIKPTRpfCFFN 199
Cdd:PRK08008 304 KdaFEERFGVRLLTSYGMTETIVgIIGDRPGDKRRWPSIGRPGFCYEAEIRDDHNRPLPAGEIGEICIKGVPGK--TIFK 381
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755522749 200 CYLDNPEKTAASEQGDFYI-TGDRAHMDEDGYFWFLGRNDDVINSSSYRIGPVEVESALAEHPAVLESAVVSSPDPIRGE 278
Cdd:PRK08008 382 EYYLDPKATAKVLEADGWLhTGDTGYVDEEGFFYFVDRRCNMIKRGGENVSCVELENIIATHPKIQDIVVVGIKDSIRDE 461
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 755522749 279 VVKAFIVLSPAyASHDPEALTRELQEHVktvtAPYKYPRKVAFISELPKTVSGKILRSKLR 339
Cdd:PRK08008 462 AIKAFVVLNEG-ETLSEEEFFAFCEQNM----AKFKVPSYLEIRKDLPRNCSGKIIKKNLK 517
|
|
| PRK06178 |
PRK06178 |
acyl-CoA synthetase; Validated |
63-338 |
1.82e-40 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 235724 [Multi-domain] Cd Length: 567 Bit Score: 149.42 E-value: 1.82e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755522749 63 LPRVDAKTILNTLCRFPIT-TLCCVPTLFRLLVQEDLTRYKFQCLRH--CLTGGEALNPDVRDKWKSQTGLELHEG-YGQ 138
Cdd:PRK06178 283 LARWDAVAFMAAVERYRVTrTVMLVDNAVELMDHPRFAEYDLSSLRQvrVVSFVKKLNPDYRQRWRALTGSVLAEAaWGM 362
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755522749 139 SETvvicgNSRNsTIKSGS-------------MGKASPPYDVQIVDEE-GNVLPPGKEGNIAVRiKPTrpfcFFNCYLDN 204
Cdd:PRK06178 363 TET-----HTCD-TFTAGFqdddfdllsqpvfVGLPVPGTEFKICDFEtGELLPLGAEGEIVVR-TPS----LLKGYWNK 431
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755522749 205 PEKTAASEQGDFYITGDRAHMDEDGYFWFLGRNDDVINSSSYRIGPVEVESALAEHPAVLESAVVSSPDPIRGEVVKAFI 284
Cdd:PRK06178 432 PEATAEALRDGWLHTGDIGKIDEQGFLHYLGRRKEMLKVNGMSVFPSEVEALLGQHPAVLGSAVVGRPDPDKGQVPVAFV 511
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....
gi 755522749 285 VLSPAyASHDPEALTRELQEHVktvtAPYKYPrKVAFISELPKTVSGKILRSKL 338
Cdd:PRK06178 512 QLKPG-ADLTAAALQAWCRENM----AVYKVP-EIRIVDALPMTATGKVRKQDL 559
|
|
| PRK06839 |
PRK06839 |
o-succinylbenzoate--CoA ligase; |
49-341 |
2.39e-40 |
|
o-succinylbenzoate--CoA ligase;
Pssm-ID: 168698 [Multi-domain] Cd Length: 496 Bit Score: 148.08 E-value: 2.39e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755522749 49 FSAWSNGACIFVHElpRVDAKTILNTLCRFPITTLCCVPTLFRLLVQE-DLTRYKFQCLRHCLTGGeALNPDVRDKWKSQ 127
Cdd:PRK06839 210 FPTLFAGGVIIVPR--KFEPTKALSMIEKHKVTVVMGVPTIHQALINCsKFETTNLQSVRWFYNGG-APCPEELMREFID 286
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755522749 128 TGLELHEGYGQSET--VVICGNSRNSTIKSGSMGKASPPYDVQIVDEEGNVLPPGKEGNIAVRiKPTrpfcFFNCYLDNP 205
Cdd:PRK06839 287 RGFLFGQGFGMTETspTVFMLSEEDARRKVGSIGKPVLFCDYELIDENKNKVEVGEVGELLIR-GPN----VMKEYWNRP 361
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755522749 206 EKTAASEQGDFYITGDRAHMDEDGYFWFLGRNDDVINSSSYRIGPVEVESALAEHPAVLESAVVSSPDPIRGEVVKAFIV 285
Cdd:PRK06839 362 DATEETIQDGWLCTGDLARVDEDGFVYIVGRKKEMIISGGENIYPLEVEQVINKLSDVYEVAVVGRQHVKWGEIPIAFIV 441
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*.
gi 755522749 286 LSPAYAshdpeALTRELQEHVKTVTAPYKYPRKVAFISELPKTVSGKILRSKLRNQ 341
Cdd:PRK06839 442 KKSSSV-----LIEKDVIEHCRLFLAKYKIPKEIVFLKELPKNATGKIQKAQLVNQ 492
|
|
| PRK03640 |
PRK03640 |
o-succinylbenzoate--CoA ligase; |
64-340 |
5.29e-40 |
|
o-succinylbenzoate--CoA ligase;
Pssm-ID: 235146 [Multi-domain] Cd Length: 483 Bit Score: 147.03 E-value: 5.29e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755522749 64 PRVDAKTILNTLCRFPITTLCCVPT-LFRLLVQEDLTRY--KFQCLrhcLTGGEALNPDVRDKWKsQTGLELHEGYGQSE 140
Cdd:PRK03640 214 EKFDAEKINKLLQTGGVTIISVVSTmLQRLLERLGEGTYpsSFRCM---LLGGGPAPKPLLEQCK-EKGIPVYQSYGMTE 289
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755522749 141 TV--VICGNSRNSTIKSGSMGKASPPYDVQIVDEeGNVLPPGKEGNIAVR---IKPTrpfcffncYLDNPEKTAASEQGD 215
Cdd:PRK03640 290 TAsqIVTLSPEDALTKLGSAGKPLFPCELKIEKD-GVVVPPFEEGEIVVKgpnVTKG--------YLNREDATRETFQDG 360
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755522749 216 FYITGDRAHMDEDGYFWFLGRNDDVINSSSYRIGPVEVESALAEHPAVLESAVVSSPDPIRGEVVKAFIVLSpayaSHDP 295
Cdd:PRK03640 361 WFKTGDIGYLDEEGFLYVLDRRSDLIISGGENIYPAEIEEVLLSHPGVAEAGVVGVPDDKWGQVPVAFVVKS----GEVT 436
|
250 260 270 280
....*....|....*....|....*....|....*....|....*
gi 755522749 296 EAltrELQEHVKTVTAPYKYPRKVAFISELPKTVSGKILRSKLRN 340
Cdd:PRK03640 437 EE---ELRHFCEEKLAKYKVPKRFYFVEELPRNASGKLLRHELKQ 478
|
|
| PRK13382 |
PRK13382 |
bile acid CoA ligase; |
65-339 |
8.05e-40 |
|
bile acid CoA ligase;
Pssm-ID: 172019 [Multi-domain] Cd Length: 537 Bit Score: 147.21 E-value: 8.05e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755522749 65 RVDAKTILNTLCRFPITTLCCVPTLFRL---LVQEDLTRYKFQCLRHCLTGGEALNPDVRDKWKSQTGLELHEGYGQSET 141
Cdd:PRK13382 270 RFDPEATLDLIDRHRATGLAVVPVMFDRimdLPAEVRNRYSGRSLRFAAASGSRMRPDVVIAFMDQFGDVIYNNYNATEA 349
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755522749 142 VVIC-GNSRNSTIKSGSMGKASPPYDVQIVDEEGNVLPPGKEGNIAVRIKptrpfCFFNCYldNPEKTAASEQGdFYITG 220
Cdd:PRK13382 350 GMIAtATPADLRAAPDTAGRPAEGTEIRILDQDFREVPTGEVGTIFVRND-----TQFDGY--TSGSTKDFHDG-FMASG 421
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755522749 221 DRAHMDEDGYFWFLGRNDDVINSSSYRIGPVEVESALAEHPAVLESAVVSSPDPIRGEVVKAFIVLSPayashDPEALTR 300
Cdd:PRK13382 422 DVGYLDENGRLFVVGRDDEMIVSGGENVYPIEVEKTLATHPDVAEAAVIGVDDEQYGQRLAAFVVLKP-----GASATPE 496
|
250 260 270
....*....|....*....|....*....|....*....
gi 755522749 301 ELQEHVKTVTAPYKYPRKVAFISELPKTVSGKILRSKLR 339
Cdd:PRK13382 497 TLKQHVRDNLANYKVPRDIVVLDELPRGATGKILRRELQ 535
|
|
| PRK07787 |
PRK07787 |
acyl-CoA synthetase; Validated |
86-342 |
9.93e-40 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236096 [Multi-domain] Cd Length: 471 Bit Score: 145.90 E-value: 9.93e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755522749 86 VPTLF-RLLVQEDLTRyKFQCLRHCLTGGEALNPDVRDKWKSQTGLELHEGYGQSETVVICGNSRNSTIKSGSMGKASPP 164
Cdd:PRK07787 223 VPTVWsRIAADPEAAR-ALRGARLLVSGSAALPVPVFDRLAALTGHRPVERYGMTETLITLSTRADGERRPGWVGLPLAG 301
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755522749 165 YDVQIVDEEGNVLPPGKE--GNIAVRiKPTrpfcFFNCYLDNPEKTAASEQGD-FYITGDRAHMDEDGYFWFLGRND-DV 240
Cdd:PRK07787 302 VETRLVDEDGGPVPHDGEtvGELQVR-GPT----LFDGYLNRPDATAAAFTADgWFRTGDVAVVDPDGMHRIVGREStDL 376
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755522749 241 INSSSYRIGPVEVESALAEHPAVLESAVVSSPDPIRGEVVKAFIVlspayaSHDPEALTrELQEHVKTVTAPYKYPRKVA 320
Cdd:PRK07787 377 IKSGGYRIGAGEIETALLGHPGVREAAVVGVPDDDLGQRIVAYVV------GADDVAAD-ELIDFVAQQLSVHKRPREVR 449
|
250 260
....*....|....*....|..
gi 755522749 321 FISELPKTVSGKILRSKLRNQE 342
Cdd:PRK07787 450 FVDALPRNAMGKVLKKQLLSEG 471
|
|
| A_NRPS_AB3403-like |
cd17646 |
Peptide Synthetase; The adenylation (A) domain of NRPS recognizes a specific amino acid or ... |
44-338 |
1.16e-39 |
|
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: 145.88 E-value: 1.16e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755522749 44 AAWTLFSAWSNGACIFVHElP--RVDAKTILNTLCRFPITTLCCVPTLFRLLVQEdLTRYKFQCLRHCLTGGEALNPDVR 121
Cdd:cd17646 193 SVWELFWPLVAGARLVVAR-PggHRDPAYLAALIREHGVTTCHFVPSMLRVFLAE-PAAGSCASLRRVFCSGEALPPELA 270
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755522749 122 DKWKSQTGLELHEGYGQSETVV------ICGNSRNSTIksgSMGKASPPYDVQIVDEEGNVLPPGKEGNIAVR-IKPTRP 194
Cdd:cd17646 271 ARFLALPGAELHNLYGPTEAAIdvthwpVRGPAETPSV---PIGRPVPNTRLYVLDDALRPVPVGVPGELYLGgVQLARG 347
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755522749 195 fcffncYLDNPEKTAAS------EQGD-FYITGDRAHMDEDGYFWFLGRNDDVINSSSYRIGPVEVESALAEHPAVLESA 267
Cdd:cd17646 348 ------YLGRPALTAERfvpdpfGPGSrMYRTGDLARWRPDGALEFLGRSDDQVKIRGFRVEPGEIEAALAAHPAVTHAV 421
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 755522749 268 VVSSPDPIRGEVVKAFIVLSPAYASHDPEALTRELQEHVktvtAPYKYPRKVAFISELPKTVSGKILRSKL 338
Cdd:cd17646 422 VVARAAPAGAARLVGYVVPAAGAAGPDTAALRAHLAERL----PEYMVPAAFVVLDALPLTANGKLDRAAL 488
|
|
| PRK07788 |
PRK07788 |
acyl-CoA synthetase; Validated |
39-342 |
7.92e-39 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236097 [Multi-domain] Cd Length: 549 Bit Score: 144.68 E-value: 7.92e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755522749 39 TGWvkAAWTLfsAWSNGACIFVHElpRVDAKTILNTLCRFPITTLCCVPTLFRLLV---QEDLTRYKFQCLRHCLTGGEA 115
Cdd:PRK07788 261 TGW--AHLTL--AMALGSTVVLRR--RFDPEATLEDIAKHKATALVVVPVMLSRILdlgPEVLAKYDTSSLKIIFVSGSA 334
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755522749 116 LNPDVRDKWKSQTGLELHEGYGQSE-TVVICGNSRNSTIKSGSMGKASPPYDVQIVDEEGNVLPPGKEGNIAVRIKPTrp 194
Cdd:PRK07788 335 LSPELATRALEAFGPVLYNLYGSTEvAFATIATPEDLAEAPGTVGRPPKGVTVKILDENGNEVPRGVVGRIFVGNGFP-- 412
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755522749 195 fcfFNCYLDNPEKTAAseqGDFYITGDRAHMDEDGYFWFLGRNDDVINSSSYRIGPVEVESALAEHPAVLESAVVSSPDP 274
Cdd:PRK07788 413 ---FEGYTDGRDKQII---DGLLSSGDVGYFDEDGLLFVDGRDDDMIVSGGENVFPAEVEDLLAGHPDVVEAAVIGVDDE 486
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 755522749 275 IRGEVVKAFIVLSPAyASHDPEaltrELQEHVKTVTAPYKYPRKVAFISELPKTVSGKILRSKLRNQE 342
Cdd:PRK07788 487 EFGQRLRAFVVKAPG-AALDED----AIKDYVRDNLARYKVPRDVVFLDELPRNPTGKVLKRELREMD 549
|
|
| PRK13391 |
PRK13391 |
acyl-CoA synthetase; Provisional |
53-345 |
1.50e-38 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 184022 [Multi-domain] Cd Length: 511 Bit Score: 143.29 E-value: 1.50e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755522749 53 SNGACIFVHElpRVDAKTILNTLCRFPITTLCCVPTLF-RLLV--QEDLTRYKFQCLRHCLTGGEALNPDVRDKWKSQTG 129
Cdd:PRK13391 223 RLGGTVIVME--HFDAEQYLALIEEYGVTHTQLVPTMFsRMLKlpEEVRDKYDLSSLEVAIHAAAPCPPQVKEQMIDWWG 300
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755522749 130 LELHEGYGQSETVVICG-NSRNSTIKSGSMGKASPPyDVQIVDEEGNVLPPGKEGNIAvrIKPTRPFCFFNcyldNPEKT 208
Cdd:PRK13391 301 PIIHEYYAATEGLGFTAcDSEEWLAHPGTVGRAMFG-DLHILDDDGAELPPGEPGTIW--FEGGRPFEYLN----DPAKT 373
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755522749 209 AAS--EQGDFYITGDRAHMDEDGYFWFLGRNDDVINSSSYRIGPVEVESALAEHPAVLESAVVSSPDPIRGEVVKAfiVL 286
Cdd:PRK13391 374 AEArhPDGTWSTVGDIGYVDEDGYLYLTDRAAFMIISGGVNIYPQEAENLLITHPKVADAAVFGVPNEDLGEEVKA--VV 451
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*....
gi 755522749 287 SPAYASHDPEALTRELQEHVKTVTAPYKYPRKVAFISELPKTVSGKILRSKLRNQEWGR 345
Cdd:PRK13391 452 QPVDGVDPGPALAAELIAFCRQRLSRQKCPRSIDFEDELPRLPTGKLYKRLLRDRYWGN 510
|
|
| FACL_like_4 |
cd05944 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
77-339 |
2.23e-38 |
|
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: 139.92 E-value: 2.23e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755522749 77 RFPITTLCCVPTLFRLLVQEDLTRyKFQCLRHCLTGGEALNPDVRDKWKSQTGLELHEGYGQSE-TVVICGNSRNSTIKS 155
Cdd:cd05944 95 RYRITSLSTVPTVYAALLQVPVNA-DISSLRFAMSGAAPLPVELRARFEDATGLPVVEGYGLTEaTCLVAVNPPDGPKRP 173
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755522749 156 GSMGKASPPYDVQIV--DEEGNVL---PPGKEGNIAVRiKPTrpfcFFNCYLDNPEKTAASEQGDFYITGDRAHMDEDGY 230
Cdd:cd05944 174 GSVGLRLPYARVRIKvlDGVGRLLrdcAPDEVGEICVA-GPG----VFGGYLYTEGNKNAFVADGWLNTGDLGRLDADGY 248
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755522749 231 FWFLGRNDDVINSSSYRIGPVEVESALAEHPAVLESAVVSSPDPIRGEVVKAFIVLSPAyASHDPEALTRELQEHVKTVT 310
Cdd:cd05944 249 LFITGRAKDLIIRGGHNIDPALIEEALLRHPAVAFAGAVGQPDAHAGELPVAYVQLKPG-AVVEEEELLAWARDHVPERA 327
|
250 260
....*....|....*....|....*....
gi 755522749 311 ApykYPRKVAFISELPKTVSGKILRSKLR 339
Cdd:cd05944 328 A---VPKHIEVLEELPVTAVGKVFKPALR 353
|
|
| PRK09088 |
PRK09088 |
acyl-CoA synthetase; Validated |
80-341 |
6.73e-38 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 181644 [Multi-domain] Cd Length: 488 Bit Score: 141.10 E-value: 6.73e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755522749 80 ITTLCCVPTLFRLL-VQEDLTRYKFQCLRHCLTGGEA-LNPDVRdKWKSQtGLELHEGYGQSETVVICGNSRNSTI---K 154
Cdd:PRK09088 227 ITHYFCVPQMAQAFrAQPGFDAAALRHLTALFTGGAPhAAEDIL-GWLDD-GIPMVDGFGMSEAGTVFGMSVDCDViraK 304
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755522749 155 SGSMGKASPPYDVQIVDEEGNVLPPGKEGNIAVRiKPTrpfcFFNCYLDNPEKTAASEQGD-FYITGDRAHMDEDGYFWF 233
Cdd:PRK09088 305 AGAAGIPTPTVQTRVVDDQGNDCPAGVPGELLLR-GPN----LSPGYWRRPQATARAFTGDgWFRTGDIARRDADGFFWV 379
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755522749 234 LGRNDDVINSSSYRIGPVEVESALAEHPAVLESAVVSSPDPIRGEVVKAFIVLSPAyASHDPEaltrELQEHVKTVTAPY 313
Cdd:PRK09088 380 VDRKKDMFISGGENVYPAEIEAVLADHPGIRECAVVGMADAQWGEVGYLAIVPADG-APLDLE----RIRSHLSTRLAKY 454
|
250 260
....*....|....*....|....*...
gi 755522749 314 KYPRKVAFISELPKTVSGKILRSKLRNQ 341
Cdd:PRK09088 455 KVPKHLRLVDALPRTASGKLQKARLRDA 482
|
|
| ttLC_FACS_AEE21_like |
cd12118 |
Fatty acyl-CoA synthetases similar to LC-FACS from Thermus thermophiles and Arabidopsis; This ... |
63-340 |
8.50e-38 |
|
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: 140.90 E-value: 8.50e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755522749 63 LPRVDAKTILNTLCRFPITTLCCVPTLFRLLVQ-EDLTRYKFQCLRHCLTGGEALNPDVRDKwKSQTGLELHEGYGQSET 141
Cdd:cd12118 205 LRKVDAKAIYDLIEKHKVTHFCGAPTVLNMLANaPPSDARPLPHRVHVMTAGAPPPAAVLAK-MEELGFDVTHVYGLTET 283
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755522749 142 ---VVICG-----NSRNSTIKSGSMGKASPPY----DVQIVDEEGNVLPP--GKE-GNIAVRIKPTrpfcfFNCYLDNPE 206
Cdd:cd12118 284 ygpATVCAwkpewDELPTEERARLKARQGVRYvgleEVDVLDPETMKPVPrdGKTiGEIVFRGNIV-----MKGYLKNPE 358
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755522749 207 KTAASEQGDFYITGDRAHMDEDGYFWFLGRNDDVINSSSYRIGPVEVESALAEHPAVLESAVVSSPDPIRGEVVKAFIVL 286
Cdd:cd12118 359 ATAEAFRGGWFHSGDLAVIHPDGYIEIKDRSKDIIISGGENISSVEVEGVLYKHPAVLEAAVVARPDEKWGEVPCAFVEL 438
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....
gi 755522749 287 SPAYashdpEALTRELQEHVKTVTAPYKYPRKVAFiSELPKTVSGKILRSKLRN 340
Cdd:cd12118 439 KEGA-----KVTEEEIIAFCREHLAGFMVPKTVVF-GELPKTSTGKIQKFVLRD 486
|
|
| PRK06145 |
PRK06145 |
acyl-CoA synthetase; Validated |
67-341 |
1.24e-37 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 102207 [Multi-domain] Cd Length: 497 Bit Score: 140.79 E-value: 1.24e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755522749 67 DAKTILNTLCRFPITTLCCVPTLF-RLLVQEDLTRYKFQCLRHCLTGGEAlNPD--VRDKWKSQTGLELHEGYGQSETvv 143
Cdd:PRK06145 226 DPEAVLAAIERHRLTCAWMAPVMLsRVLTVPDRDRFDLDSLAWCIGGGEK-TPEsrIRDFTRVFTRARYIDAYGLTET-- 302
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755522749 144 iCGNSR-----NSTIKSGSMGKASPPYDVQIVDEEGNVLPPGKEGNIAVR-IKPTRPfcffncYLDNPEKTAASEQGDFY 217
Cdd:PRK06145 303 -CSGDTlmeagREIEKIGSTGRALAHVEIRIADGAGRWLPPNMKGEICMRgPKVTKG------YWKDPEKTAEAFYGDWF 375
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755522749 218 ITGDRAHMDEDGYFWFLGRNDDVINSSSYRIGPVEVESALAEHPAVLESAVVSSPDPIRGEVVKAFIVLSPAyASHDPEA 297
Cdd:PRK06145 376 RSGDVGYLDEEGFLYLTDRKKDMIISGGENIASSEVERVIYELPEVAEAAVIGVHDDRWGERITAVVVLNPG-ATLTLEA 454
|
250 260 270 280
....*....|....*....|....*....|....*....|....
gi 755522749 298 LTRelqeHVKTVTAPYKYPRKVAFISELPKTVSGKILRSKLRNQ 341
Cdd:PRK06145 455 LDR----HCRQRLASFKVPRQLKVRDELPRNPSGKVLKRVLRDE 494
|
|
| OSB_MenE-like |
cd17630 |
O-succinylbenzoic acid-CoA ligase; This family contains O-succinylbenzoyl-CoA (OSB-CoA) ... |
72-340 |
3.43e-37 |
|
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: 135.92 E-value: 3.43e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755522749 72 LNTLCRFPITTLCCVPTLFRLLVQEDLTRYKFQCLRHCLTGGEALNPDVRDKwKSQTGLELHEGYGQSETVVICGNSRNS 151
Cdd:cd17630 79 AEDLAPPGVTHVSLVPTQLQRLLDSGQGPAALKSLRAVLLGGAPIPPELLER-AADRGIPLYTTYGMTETASQVATKRPD 157
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755522749 152 TIKSGSMGKASPPYDVQIVDEegnvlppgkeGNIAVRikptrPFCFFNCYLDNPEKTAASEQGDFYiTGDRAHMDEDGYF 231
Cdd:cd17630 158 GFGRGGVGVLLPGRELRIVED----------GEIWVG-----GASLAMGYLRGQLVPEFNEDGWFT-TKDLGELHADGRL 221
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755522749 232 WFLGRNDDVINSSSYRIGPVEVESALAEHPAVLESAVVSSPDPIRGEVVKAFIVLspayashDPEALTRELQEHVKTVTA 311
Cdd:cd17630 222 TVLGRADNMIISGGENIQPEEIEAALAAHPAVRDAFVVGVPDEELGQRPVAVIVG-------RGPADPAELRAWLKDKLA 294
|
250 260
....*....|....*....|....*....
gi 755522749 312 PYKYPRKVAFISELPKTVSGKILRSKLRN 340
Cdd:cd17630 295 RFKLPKRIYPVPELPRTGGGKVDRRALRA 323
|
|
| EntE |
COG1021 |
EntE, 2,3-dihydroxybenzoate-AMP synthase component of non-ribosomal peptide synthetase ... |
48-341 |
3.84e-37 |
|
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: 139.90 E-value: 3.84e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755522749 48 LFSAWSNGACIFVHELPRVDAktilntlCrFP------ITTLCCVPTLFRLLVQ-EDLTRYKFQCLRHCLTGGEALNPDV 120
Cdd:COG1021 245 VLGVLYAGGTVVLAPDPSPDT-------A-FPliererVTVTALVPPLALLWLDaAERSRYDLSSLRVLQVGGAKLSPEL 316
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755522749 121 RDKWKSQTGLELHEGYGQSETVVIC---GNSRNSTIksGSMGKASPPYD-VQIVDEEGNVLPPGKEGNIAVRIKPTrpfc 196
Cdd:COG1021 317 ARRVRPALGCTLQQVFGMAEGLVNYtrlDDPEEVIL--TTQGRPISPDDeVRIVDEDGNPVPPGEVGELLTRGPYT---- 390
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755522749 197 fFNCYLDNPEKTAAS--EQGdFYITGDRAHMDEDGYFWFLGRNDDVINSSSYRIGPVEVESALAEHPAVLESAVVSSPDP 274
Cdd:COG1021 391 -IRGYYRAPEHNARAftPDG-FYRTGDLVRRTPDGYLVVEGRAKDQINRGGEKIAAEEVENLLLAHPAVHDAAVVAMPDE 468
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 755522749 275 IRGEVVKAFIVLspayashDPEALT-RELQEHVKTV-TAPYKYPRKVAFISELPKTVSGKILRSKLRNQ 341
Cdd:COG1021 469 YLGERSCAFVVP-------RGEPLTlAELRRFLRERgLAAFKLPDRLEFVDALPLTAVGKIDKKALRAA 530
|
|
| ttLC_FACS_AlkK_like |
cd12119 |
Fatty acyl-CoA synthetases similar to LC-FACS from Thermus thermophiles; This family includes ... |
45-340 |
9.01e-37 |
|
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: 138.53 E-value: 9.01e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755522749 45 AWTL-FSAWSNGACiFVHELPRVDAKTILNTLCRFPITTLCCVPTLFRLLVQE-DLTRYKFQCLRHCLTGGEALNPDVRD 122
Cdd:cd12119 220 AWGLpYAAAMVGAK-LVLPGPYLDPASLAELIEREGVTFAAGVPTVWQGLLDHlEANGRDLSSLRRVVIGGSAVPRSLIE 298
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755522749 123 KWKsQTGLELHEGYGQSET--VVICGNSRNSTIKSGSMGKAS-------PPYDVQ--IVDEEGNVLP-PGKE-GNIAVR- 188
Cdd:cd12119 299 AFE-ERGVRVIHAWGMTETspLGTVARPPSEHSNLSEDEQLAlrakqgrPVPGVElrIVDDDGRELPwDGKAvGELQVRg 377
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755522749 189 --IKPTrpfcffncYLDNPEKTAASEQGDFYITGDRAHMDEDGYFWFLGRNDDVINSSSYRIGPVEVESALAEHPAVLES 266
Cdd:cd12119 378 pwVTKS--------YYKNDEESEALTEDGWLRTGDVATIDEDGYLTITDRSKDVIKSGGEWISSVELENAIMAHPAVAEA 449
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 755522749 267 AVVSSPDPIRGEVVKAFIVLSPAyASHDPEaltrELQEHVKTVTAPYKYPRKVAFISELPKTVSGKILRSKLRN 340
Cdd:cd12119 450 AVIGVPHPKWGERPLAVVVLKEG-ATVTAE----ELLEFLADKVAKWWLPDDVVFVDEIPKTSTGKIDKKALRE 518
|
|
| FADD10 |
cd17635 |
adenylate forming domain, fatty acid CoA ligase (FadD10); This family contains long chain ... |
45-335 |
9.78e-37 |
|
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: 135.08 E-value: 9.78e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755522749 45 AWTLFSAWSNGACIFVHElpRVDAKTILNTLCRFPITTLCCVPTLFRLLVQE--DLTRYKFQcLRHCLTGGE-ALNPDVR 121
Cdd:cd17635 59 WWILTCLIHGGLCVTGGE--NTTYKSLFKILTTNAVTTTCLVPTLLSKLVSElkSANATVPS-LRLIGYGGSrAIAADVR 135
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755522749 122 D-KWKSQTGLELHegYGQSET-VVICGNSRNSTIKSGSMGKASPPYDVQIVDEEGNVLPPGKEGNIAvrIKPTRpfcFFN 199
Cdd:cd17635 136 FiEATGLTNTAQV--YGLSETgTALCLPTDDDSIEINAVGRPYPGVDVYLAATDGIAGPSASFGTIW--IKSPA---NML 208
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755522749 200 CYLDNPEKTAASEQGDFYITGDRAHMDEDGYFWFLGRNDDVINSSSYRIGPVEVESALAEHPAVLESAVVSSPDPIRGEV 279
Cdd:cd17635 209 GYWNNPERTAEVLIDGWVNTGDLGERREDGFLFITGRSSESINCGGVKIAPDEVERIAEGVSGVQECACYEISDEEFGEL 288
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*.
gi 755522749 280 VKAFIVLSpayaSHDPEALTRELQEHVKTVTAPYKYPRKVAFISELPKTVSGKILR 335
Cdd:cd17635 289 VGLAVVAS----AELDENAIRALKHTIRRELEPYARPSTIVIVTDIPRTQSGKVKR 340
|
|
| A_NRPS_VisG_like |
cd17651 |
similar to adenylation domain of virginiamycin S synthetase; This family of the adenylation (A) ... |
44-339 |
1.47e-36 |
|
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: 137.48 E-value: 1.47e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755522749 44 AAWTLFSAWSNGACI-FVHELPRVDAKTILNTLCRFPITtLCCVPTLFRLLVQEDLTRYKFQ--CLRHCLTGGEAL--NP 118
Cdd:cd17651 191 SVQEIFSTLCAGATLvLPPEEVRTDPPALAAWLDEQRIS-RVFLPTVALRALAEHGRPLGVRlaALRYLLTGGEQLvlTE 269
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755522749 119 DVRDKWKSQTGLELHEGYGQSET-VVICGNSRNSTIKSG---SMGKASPPYDVQIVDEEGNVLPPGKEGNIAVRIKptrp 194
Cdd:cd17651 270 DLREFCAGLPGLRLHNHYGPTEThVVTALSLPGDPAAWPappPIGRPIDNTRVYVLDAALRPVPPGVPGELYIGGA---- 345
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755522749 195 fCFFNCYLDNPEKTAA-------SEQGDFYITGDRAHMDEDGYFWFLGRNDDVINSSSYRIGPVEVESALAEHPAVLESA 267
Cdd:cd17651 346 -GLARGYLNRPELTAErfvpdpfVPGARMYRTGDLARWLPDGELEFLGRADDQVKIRGFRIELGEIEAALARHPGVREAV 424
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 755522749 268 VVSSPDPIRGEVVKAFIVLSPAyASHDPEALTRELQEHVktvtAPYKYPRKVAFISELPKTVSGKILRSKLR 339
Cdd:cd17651 425 VLAREDRPGEKRLVAYVVGDPE-APVDAAELRAALATHL----PEYMVPSAFVLLDALPLTPNGKLDRRALP 491
|
|
| FadD3 |
cd17638 |
acyl-CoA synthetase FadD3 and similar proteins; This family contains long chain fatty acid CoA ... |
43-335 |
1.91e-36 |
|
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: 134.17 E-value: 1.91e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755522749 43 KAAWtlFSAWSNGACIFVHELprVDAKTILNTLCRFPITTLCCVPTLFR-LLVQEDLTRYKFQCLRHCLTGGEALNPDVR 121
Cdd:cd17638 57 KAGI--VACLLTGATVVPVAV--FDVDAILEAIERERITVLPGPPTLFQsLLDHPGRKKFDLSSLRAAVTGAATVPVELV 132
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755522749 122 DKWKSQTGLE-LHEGYGQSETVV--ICGNSRNSTIKSGSMGKASPPYDVQIVDEeGNVLPPGKegNIAVRikptrpfcff 198
Cdd:cd17638 133 RRMRSELGFEtVLTAYGLTEAGVatMCRPGDDAETVATTCGRACPGFEVRIADD-GEVLVRGY--NVMQG---------- 199
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755522749 199 ncYLDNPEKTAASEQGDFYI-TGDRAHMDEDGYFWFLGRNDDVINSSSYRIGPVEVESALAEHPAVLESAVVSSPDPIRG 277
Cdd:cd17638 200 --YLDDPEATAEAIDADGWLhTGDVGELDERGYLRITDRLKDMYIVGGFNVYPAEVEGALAEHPGVAQVAVIGVPDERMG 277
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*...
gi 755522749 278 EVVKAFIVLSPAyASHDPEALTRELQEHVktvtAPYKYPRKVAFISELPKTVSGKILR 335
Cdd:cd17638 278 EVGKAFVVARPG-VTLTEEDVIAWCRERL----ANYKVPRFVRFLDELPRNASGKVMK 330
|
|
| PRK07786 |
PRK07786 |
long-chain-fatty-acid--CoA ligase; Validated |
55-341 |
2.16e-36 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 169098 [Multi-domain] Cd Length: 542 Bit Score: 137.99 E-value: 2.16e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755522749 55 GACIFVHELPRVDAKTILNTLCRFPITTLCCVPTLFRLLVQEDLTRYKFQCLRhCLTGGEALNPD--VRDKWKSQTGLEL 132
Cdd:PRK07786 241 GAPTVIYPLGAFDPGQLLDVLEAEKVTGIFLVPAQWQAVCAEQQARPRDLALR-VLSWGAAPASDtlLRQMAATFPEAQI 319
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755522749 133 HEGYGQSE----TVVICGNsrNSTIKSGSMGKASPPYDVQIVDEEGNVLPPGKEGNIAVRiKPTrpfcFFNCYLDNPEKT 208
Cdd:PRK07786 320 LAAFGQTEmspvTCMLLGE--DAIRKLGSVGKVIPTVAARVVDENMNDVPVGEVGEIVYR-APT----LMSGYWNNPEAT 392
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755522749 209 AASEQGDFYITGDRAHMDEDGYFWFLGRNDDVINSSSYRIGPVEVESALAEHPAVLESAVVSSPDPIRGEVVKAFIVLSP 288
Cdd:PRK07786 393 AEAFAGGWFHSGDLVRQDEEGYVWVVDRKKDMIISGGENIYCAEVENVLASHPDIVEVAVIGRADEKWGEVPVAVAAVRN 472
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|...
gi 755522749 289 AYASHDPEALTRELQEHVktvtAPYKYPRKVAFISELPKTVSGKILRSKLRNQ 341
Cdd:PRK07786 473 DDAALTLEDLAEFLTDRL----ARYKHPKALEIVDALPRNPAGKVLKTELRER 521
|
|
| CHC_CoA_lg |
cd05903 |
Cyclohexanecarboxylate-CoA ligase (also called cyclohex-1-ene-1-carboxylate:CoA ligase); ... |
136-339 |
2.82e-36 |
|
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: 135.97 E-value: 2.82e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755522749 136 YGQSETVVICGNSRN--STIKSGSMGKASPPYDVQIVDEEGNVLPPGKEGNIAVRiKPTrpfcFFNCYLDNPEKTAASEQ 213
Cdd:cd05903 240 YGSTECPGAVTSITPapEDRRLYTDGRPLPGVEIKVVDDTGATLAPGVEGELLSR-GPS----VFLGYLDRPDLTADAAP 314
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755522749 214 GDFYITGDRAHMDEDGYFWFLGRNDDVINSSSYRIGPVEVESALAEHPAVLESAVVSSPDPIRGEVVKAFIVLSPAyASH 293
Cdd:cd05903 315 EGWFRTGDLARLDEDGYLRITGRSKDIIIRGGENIPVLEVEDLLLGHPGVIEAAVVALPDERLGERACAVVVTKSG-ALL 393
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 755522749 294 DPEALTRELQEHvktVTAPYKYPRKVAFISELPKTVSGKILRSKLR 339
Cdd:cd05903 394 TFDELVAYLDRQ---GVAKQYWPERLVHVDDLPRTPSGKVQKFRLR 436
|
|
| PRK07470 |
PRK07470 |
acyl-CoA synthetase; Validated |
53-339 |
5.82e-36 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 180988 [Multi-domain] Cd Length: 528 Bit Score: 136.32 E-value: 5.82e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755522749 53 SNGACIfvHELPRV--DAKTILNTLCRFPI------------TTLCCVPTLFRLLVQ-EDLTRYKFQCLRHCLTGGEaln 117
Cdd:PRK07470 216 SHGAGI--HQLCQVarGAATVLLPSERFDPaevwalverhrvTNLFTVPTILKMLVEhPAVDRYDHSSLRYVIYAGA--- 290
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755522749 118 PDVRDKWK---SQTGLELHEGYGQSE-----TVV-ICGNSRNS--TIKSGSMGKASPPYDVQIVDEEGNVLPPGKEGNIA 186
Cdd:PRK07470 291 PMYRADQKralAKLGKVLVQYFGLGEvtgniTVLpPALHDAEDgpDARIGTCGFERTGMEVQIQDDEGRELPPGETGEIC 370
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755522749 187 VRIKPTrpfcfFNCYLDNPEKTAASEQGDFYITGDRAHMDEDGYFWFLGRNDDVINSSSYRIGPVEVESALAEHPAVLES 266
Cdd:PRK07470 371 VIGPAV-----FAGYYNNPEANAKAFRDGWFRTGDLGHLDARGFLYITGRASDMYISGGSNVYPREIEEKLLTHPAVSEV 445
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 755522749 267 AVVSSPDPIRGEVVKAFIVLSPAyASHDPEaltrELQEHVKTVTAPYKYPRKVAFISELPKTVSGKILRSKLR 339
Cdd:PRK07470 446 AVLGVPDPVWGEVGVAVCVARDG-APVDEA----ELLAWLDGKVARYKLPKRFFFWDALPKSGYGKITKKMVR 513
|
|
| EntF |
COG1020 |
EntF, seryl-AMP synthase component of non-ribosomal peptide synthetase [Secondary metabolites ... |
44-345 |
9.00e-36 |
|
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: 138.07 E-value: 9.00e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755522749 44 AAWTLFSAWSNGACI-FVHELPRVDAKTILNTLCRFPITTLCCVPTLFRLLVQEDLTRykFQCLRHCLTGGEALNPDVRD 122
Cdd:COG1020 672 SVWEIFGALLSGATLvLAPPEARRDPAALAELLARHRVTVLNLTPSLLRALLDAAPEA--LPSLRLVLVGGEALPPELVR 749
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755522749 123 KWKSQT-GLELHEGYGQSETVVicgnsrNST---IKSGSMGKASPPY-------DVQIVDEEGNVLPPGKEGNIAV---- 187
Cdd:COG1020 750 RWRARLpGARLVNLYGPTETTV------DSTyyeVTPPDADGGSVPIgrpiantRVYVLDAHLQPVPVGVPGELYIggag 823
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755522749 188 --RikptrpfcffnCYLDNPEKTAA-------SEQGD-FYITGDRAHMDEDGYFWFLGRNDD-V-INssSYRIGPVEVES 255
Cdd:COG1020 824 laR-----------GYLNRPELTAErfvadpfGFPGArLYRTGDLARWLPDGNLEFLGRADDqVkIR--GFRIELGEIEA 890
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755522749 256 ALAEHPAVLESAVVSSPDPIRGEVVKAFIVLSPayashDPEALTRELQEHVKTVTAPYKYPRKVAFISELPKTVSGKILR 335
Cdd:COG1020 891 ALLQHPGVREAVVVAREDAPGDKRLVAYVVPEA-----GAAAAAALLRLALALLLPPYMVPAAVVLLLPLPLTGNGKLDR 965
|
330
....*....|
gi 755522749 336 SKLRNQEWGR 345
Cdd:COG1020 966 LALPAPAAAA 975
|
|
| CBAL |
cd05923 |
4-Chlorobenzoate-CoA ligase (CBAL); CBAL catalyzes the conversion of 4-chlorobenzoate (4-CB) ... |
54-338 |
9.08e-36 |
|
4-Chlorobenzoate-CoA ligase (CBAL); CBAL catalyzes the conversion of 4-chlorobenzoate (4-CB) to 4-chlorobenzoyl-coenzyme A (4-CB-CoA) by the two-step adenylation and thioester-forming reactions. 4-Chlorobenzoate (4-CBA) is an environmental pollutant derived from microbial breakdown of aromatic pollutants, such as polychlorinated biphenyls (PCBs), DDT, and certain herbicides. The 4-CBA degrading pathway converts 4-CBA to the metabolite 4-hydroxybezoate (4-HBA), allowing some soil-dwelling microbes to utilize 4-CBA as an alternate carbon source. This pathway consists of three chemical steps catalyzed by 4-CBA-CoA ligase, 4-CBA-CoA dehalogenase, and 4HBA-CoA thioesterase in sequential reactions.
Pssm-ID: 341247 [Multi-domain] Cd Length: 493 Bit Score: 135.33 E-value: 9.08e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755522749 54 NGACIFVHELPRVDAktiLNTLCRFPITTLCCVPTLFRLLV-QEDLTRYKFQCLRHCLTGGEALNPDVRDKWKSQTGLEL 132
Cdd:cd05923 219 DGTYVVVEEFDPADA---LKLIEQERVTSLFATPTHLDALAaAAEFAGLKLSSLRHVTFAGATMPDAVLERVNQHLPGEK 295
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755522749 133 HEGYGQSETVvicgnsrNSTI----KSGSMGKASPPYDVQIVDEEGNV---LPPGKEGNIAVRIKPTRPFcffNCYLDNP 205
Cdd:cd05923 296 VNIYGTTEAM-------NSLYmrdaRTGTEMRPGFFSEVRIVRIGGSPdeaLANGEEGELIVAAAADAAF---TGYLNQP 365
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755522749 206 EKTAASEQGDFYITGDRAHMDEDGYFWFLGRNDDVINSSSYRIGPVEVESALAEHPAVLESAVVSSPDPIRGEVVKAFIV 285
Cdd:cd05923 366 EATAKKLQDGWYRTGDVGYVDPSGDVRILGRVDDMIISGGENIHPSEIERVLSRHPGVTEVVVIGVADERWGQSVTACVV 445
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....
gi 755522749 286 LSPAYASHDpealtrELQEHVKTVT-APYKYPRKVAFISELPKTVSGKILRSKL 338
Cdd:cd05923 446 PREGTLSAD------ELDQFCRASElADFKRPRRYFFLDELPKNAMNKVLRRQL 493
|
|
| FACL_like_5 |
cd05924 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
4-332 |
1.29e-35 |
|
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ATP-dependent activation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions.
Pssm-ID: 341248 [Multi-domain] Cd Length: 364 Bit Score: 132.51 E-value: 1.29e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755522749 4 VLWPVEGIGRVCLGGLKTRRWMALTESDIFW---NTTDTGWVKAA--------WTLFSAWSNGACIFVHElPRVDAKTIL 72
Cdd:cd05924 21 VMWRQEDIFRMLMGGADFGTGEFTPSEDAHKaaaAAAGTVMFPAPplmhgtgsWTAFGGLLGGQTVVLPD-DRFDPEEVW 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755522749 73 NTLCRFPITTLCCVPTLF-RLLVQE--DLTRYKFQCLRHCLTGGEALNPDVRDKW-KSQTGLELHEGYGQSET-VVICGN 147
Cdd:cd05924 100 RTIEKHKVTSMTIVGDAMaRPLIDAlrDAGPYDLSSLFAISSGGALLSPEVKQGLlELVPNITLVDAFGSSETgFTGSGH 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755522749 148 SRNSTIKSGSMGKASPpyDVQIVDEEGNVLPPGKE--GNIAVR-IKPtrpfcffNCYLDNPEKTAAS--EQGD--FYITG 220
Cdd:cd05924 180 SAGSGPETGPFTRANP--DTVVLDDDGRVVPPGSGgvGWIARRgHIP-------LGYYGDEAKTAETfpEVDGvrYAVPG 250
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755522749 221 DRAHMDEDGYFWFLGRNDDVINSSSYRIGPVEVESALAEHPAVLESAVVSSPDPIRGEVVKAFIVLSPAyasHDPEAltR 300
Cdd:cd05924 251 DRATVEADGTVTLLGRGSVCINTGGEKVFPEEVEEALKSHPAVYDVLVVGRPDERWGQEVVAVVQLREG---AGVDL--E 325
|
330 340 350
....*....|....*....|....*....|..
gi 755522749 301 ELQEHVKTVTAPYKYPRKVAFISELPKTVSGK 332
Cdd:cd05924 326 ELREHCRTRIARYKLPKQVVFVDEIERSPAGK 357
|
|
| PtmA |
cd17636 |
long-chain fatty acid CoA ligase (FadD); This family contains fatty acid CoA ligases, ... |
55-331 |
1.36e-35 |
|
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: 132.04 E-value: 1.36e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755522749 55 GACIFVhelPRVDAKTILNTLCRFPIT-TLCCVPTLFRLLVQEDLTRYKFQCLRHCLT--GGEALNPDVRDKWKSQTGle 131
Cdd:cd17636 67 GTNVFV---RRVDAEEVLELIEAERCThAFLLPPTIDQIVELNADGLYDLSSLRSSPAapEWNDMATVDTSPWGRKPG-- 141
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755522749 132 lheGYGQSET---VVICGNSRNSTiksGSMGKASPPYDVQIVDEEGNVLPPGKEGNIAVRiKPTrpfcFFNCYLDNPEKT 208
Cdd:cd17636 142 ---GYGQTEVmglATFAALGGGAI---GGAGRPSPLVQVRILDEDGREVPDGEVGEIVAR-GPT----VMAGYWNRPEVN 210
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755522749 209 AASEQGDFYITGDRAHMDEDGYFWFLGRNDDVINSSSYRIGPVEVESALAEHPAVLESAVVSSPDPIRGEVVKAFIVLSP 288
Cdd:cd17636 211 ARRTRGGWHHTNDLGRREPDGSLSFVGPKTRMIKSGAENIYPAEVERCLRQHPAVADAAVIGVPDPRWAQSVKAIVVLKP 290
|
250 260 270 280
....*....|....*....|....*....|....*....|...
gi 755522749 289 AyASHDPEaltrELQEHVKTVTAPYKYPRKVAFISELPKTVSG 331
Cdd:cd17636 291 G-ASVTEA----ELIEHCRARIASYKKPKSVEFADALPRTAGG 328
|
|
| PRK12583 |
PRK12583 |
acyl-CoA synthetase; Provisional |
53-339 |
1.97e-35 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 237145 [Multi-domain] Cd Length: 558 Bit Score: 135.29 E-value: 1.97e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755522749 53 SNGACIfVHELPRVDAKTILNTLCRFPITTLCCVPTLF-RLLVQEDLTRYKFQCLRHCLTGGEALNPDVRDKWKSQTGL- 130
Cdd:PRK12583 266 TVGACL-VYPNEAFDPLATLQAVEEERCTALYGVPTMFiAELDHPQRGNFDLSSLRTGIMAGAPCPIEVMRRVMDEMHMa 344
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755522749 131 ELHEGYGQSETV-VICGNSRNSTI--KSGSMGKASPPYDVQIVDEEGNVLPPGKEGNIAvrikpTRPFCFFNCYLDNPEK 207
Cdd:PRK12583 345 EVQIAYGMTETSpVSLQTTAADDLerRVETVGRTQPHLEVKVVDPDGATVPRGEIGELC-----TRGYSVMKGYWNNPEA 419
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755522749 208 TAASEQGDFYI-TGDRAHMDEDGYFWFLGRNDDVINSSSYRIGPVEVESALAEHPAVLESAVVSSPDPIRGEVVKAFIVL 286
Cdd:PRK12583 420 TAESIDEDGWMhTGDLATMDEQGYVRIVGRSKDMIIRGGENIYPREIEEFLFTHPAVADVQVFGVPDEKYGEEIVAWVRL 499
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|...
gi 755522749 287 SPAYAshdpeALTRELQEHVKTVTAPYKYPRKVAFISELPKTVSGKILRSKLR 339
Cdd:PRK12583 500 HPGHA-----ASEEELREFCKARIAHFKVPRYFRFVDEFPMTVTGKVQKFRMR 547
|
|
| AA-adenyl-dom |
TIGR01733 |
amino acid adenylation domain; This model represents a domain responsible for the specific ... |
44-269 |
5.96e-35 |
|
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: 131.62 E-value: 5.96e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755522749 44 AAWTLFSAWSNGACIFVheLPRVDAKTILNTLCRF----PITTLCCVPTLFRLLVQEDLTRykFQCLRHCLTGGEALNPD 119
Cdd:TIGR01733 175 SVEEIFGALLAGATLVV--PPEDEERDDAALLAALiaehPVTVLNLTPSLLALLAAALPPA--LASLRLVILGGEALTPA 250
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755522749 120 VRDKWKSQTG-LELHEGYGQSETVVICGNSR-----NSTIKSGSMGKASPPYDVQIVDEEGNVLPPGKEGNIAVRIKptr 193
Cdd:TIGR01733 251 LVDRWRARGPgARLINLYGPTETTVWSTATLvdpddAPRESPVPIGRPLANTRLYVLDDDLRPVPVGVVGELYIGGP--- 327
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755522749 194 pfCFFNCYLDNPEKTAA---------SEQGDFYITGDRAHMDEDGYFWFLGRNDDVINSSSYRIGPVEVESALAEHPAVl 264
Cdd:TIGR01733 328 --GVARGYLNRPELTAErfvpdpfagGDGARLYRTGDLVRYLPDGNLEFLGRIDDQVKIRGYRIELGEIEAALLRHPGV- 404
|
....*
gi 755522749 265 ESAVV 269
Cdd:TIGR01733 405 REAVV 409
|
|
| Firefly_Luc |
cd17642 |
insect luciferase, similar to plant 4-coumarate: CoA ligases; This family contains insect ... |
63-339 |
6.91e-35 |
|
insect luciferase, similar to plant 4-coumarate: CoA ligases; This family contains insect firefly luciferases that share significant sequence similarity to plant 4-coumarate:coenzyme A ligases, despite their functional diversity. Luciferase catalyzes the production of light in the presence of MgATP, molecular oxygen, and luciferin. In the first step, luciferin is activated by acylation of its carboxylate group with ATP, resulting in an enzyme-bound luciferyl adenylate. In the second step, luciferyl adenylate reacts with molecular oxygen, producing an enzyme-bound excited state product (Luc=O*) and releasing AMP. This excited-state product then decays to the ground state (Luc=O), emitting a quantum of visible light.
Pssm-ID: 341297 [Multi-domain] Cd Length: 532 Bit Score: 133.42 E-value: 6.91e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755522749 63 LPRVDAKTILNTLCRFPITTLCCVPTLFRLLVQEDLT-RYKFQCLRHCLTGGEALNPDVRDKWKSQTGLE-LHEGYGQSE 140
Cdd:cd17642 259 MYKFEEELFLRSLQDYKVQSALLVPTLFAFFAKSTLVdKYDLSNLHEIASGGAPLSKEVGEAVAKRFKLPgIRQGYGLTE 338
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755522749 141 TVVICGNSRNSTIKSGSMGKASPPYDVQIVD-EEGNVLPPGKEGNIAVRiKPTrpfcFFNCYLDNPEKTAASEQGDFYI- 218
Cdd:cd17642 339 TTSAILITPEGDDKPGAVGKVVPFFYAKVVDlDTGKTLGPNERGELCVK-GPM----IMKGYVNNPEATKALIDKDGWLh 413
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755522749 219 TGDRAHMDEDGYFWFLGRNDDVINSSSYRIGPVEVESALAEHPAVLESAVVSSPDPIRGEVVKAFIVLspayaSHDPEAL 298
Cdd:cd17642 414 SGDIAYYDEDGHFFIVDRLKSLIKYKGYQVPPAELESILLQHPKIFDAGVAGIPDEDAGELPAAVVVL-----EAGKTMT 488
|
250 260 270 280
....*....|....*....|....*....|....*....|..
gi 755522749 299 TRELQEHVKTVTAPYKYPR-KVAFISELPKTVSGKILRSKLR 339
Cdd:cd17642 489 EKEVMDYVASQVSTAKRLRgGVKFVDEVPKGLTGKIDRRKIR 530
|
|
| A_NRPS_Cytc1-like |
cd17643 |
similar to adenylation domain of cytotrienin synthetase CytC1; This family of the adenylation ... |
21-338 |
1.95e-34 |
|
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: 131.28 E-value: 1.95e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755522749 21 TRRWMALTESDIFWNTTDTGWVKAAWTLFSAWSNGACIFV--HELPRvDAKTILNTLCRFPITTLCCVPTLFRLLVQEDL 98
Cdd:cd17643 125 TQRWFGFNEDDVWTLFHSYAFDFSVWEIWGALLHGGRLVVvpYEVAR-SPEDFARLLRDEGVTVLNQTPSAFYQLVEAAD 203
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755522749 99 TRYKFQ-CLRHCLTGGEALNPDVRDKWKSQTGL---ELHEGYGQSETVVicgnsrNSTIK-----------SGSMGKASP 163
Cdd:cd17643 204 RDGRDPlALRYVIFGGEALEAAMLRPWAGRFGLdrpQLVNMYGITETTV------HVTFRpldaadlpaaaASPIGRPLP 277
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755522749 164 PYDVQIVDEEGNVLPPGKEGNIAV-RIKPTRPfcffncYLDNPEKTA-------ASEQGD-FYITGDRAHMDEDGYFWFL 234
Cdd:cd17643 278 GLRVYVLDADGRPVPPGVVGELYVsGAGVARG------YLGRPELTAerfvanpFGGPGSrMYRTGDLARRLPDGELEYL 351
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755522749 235 GRNDDVINSSSYRIGPVEVESALAEHPAVLESAVVSSPDPIRGEVVKAFIVlspayASHDPEALTRELQEHVKTVTAPYK 314
Cdd:cd17643 352 GRADEQVKIRGFRIELGEIEAALATHPSVRDAAVIVREDEPGDTRLVAYVV-----ADDGAAADIAELRALLKELLPDYM 426
|
330 340
....*....|....*....|....
gi 755522749 315 YPRKVAFISELPKTVSGKILRSKL 338
Cdd:cd17643 427 VPARYVPLDALPLTVNGKLDRAAL 450
|
|
| 23DHB-AMP_lg |
cd05920 |
2,3-dihydroxybenzoate-AMP ligase; 2,3-dihydroxybenzoate-AMP ligase activates 2, ... |
80-338 |
2.55e-34 |
|
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: 131.30 E-value: 2.55e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755522749 80 ITTLccVPTLFRLLVQE-DLTRYKFQCLRHCLTGGEALNPDVRDKWKSQTGLELHEGYGQSETVVicgnsrNST------ 152
Cdd:cd05920 232 VTAL--VPALVSLWLDAaASRRADLSSLRLLQVGGARLSPALARRVPPVLGCTLQQVFGMAEGLL------NYTrlddpd 303
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755522749 153 -IKSGSMGKASPPYD-VQIVDEEGNVLPPGKEGNIAVRIKPTrpfcfFNCYLDNPEKTAAS--EQGdFYITGDRAHMDED 228
Cdd:cd05920 304 eVIIHTQGRPMSPDDeIRVVDEEGNPVPPGEEGELLTRGPYT-----IRGYYRAPEHNARAftPDG-FYRTGDLVRRTPD 377
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755522749 229 GYFWFLGRNDDVINSSSYRIGPVEVESALAEHPAVLESAVVSSPDPIRGEVVKAFIVLSpayashDPEALTRELQEHVKT 308
Cdd:cd05920 378 GYLVVEGRIKDQINRGGEKIAAEEVENLLLRHPAVHDAAVVAMPDELLGERSCAFVVLR------DPPPSAAQLRRFLRE 451
|
250 260 270
....*....|....*....|....*....|.
gi 755522749 309 V-TAPYKYPRKVAFISELPKTVSGKILRSKL 338
Cdd:cd05920 452 RgLAAYKLPDRIEFVDSLPLTAVGKIDKKAL 482
|
|
| AAS_C |
cd05909 |
C-terminal domain of the acyl-acyl carrier protein synthetase (also called ... |
47-333 |
7.77e-34 |
|
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: 130.14 E-value: 7.77e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755522749 47 TLFSAWSNGACIFVHELPrVDAKTILNTLCRFPITTLCCVPTLFRLLVQEdLTRYKFQCLRHCLTGGEALNPDVRDKWKS 126
Cdd:cd05909 206 CLWLPLLSGIKVVFHPNP-LDYKKIPELIYDKKATILLGTPTFLRGYARA-AHPEDFSSLRLVVAGAEKLKDTLRQEFQE 283
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755522749 127 QTGLELHEGYGQSETV-VICGNSRNSTIKSGSMGKASPPYDVQIVDEEGNV-LPPGKEGNIAVRiKPTrpfcFFNCYLDN 204
Cdd:cd05909 284 KFGIRILEGYGTTECSpVISVNTPQSPNKEGTVGRPLPGMEVKIVSVETHEeVPIGEGGLLLVR-GPN----VMLGYLNE 358
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755522749 205 PEKTAASEQGDFYITGDRAHMDEDGYFWFLGRnddviNSSSYRIG----PVE-VESALAEH-PAVLESAVVSSPDPIRGE 278
Cdd:cd05909 359 PELTSFAFGDGWYDTGDIGKIDGEGFLTITGR-----LSRFAKIAgemvSLEaIEDILSEIlPEDNEVAVVSVPDGRKGE 433
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*..
gi 755522749 279 VVKAFivlspayasHDPEALTR-ELQEHVKTVTAPYKY-PRKVAFISELPKTVSGKI 333
Cdd:cd05909 434 KIVLL---------TTTTDTDPsSLNDILKNAGISNLAkPSYIHQVEEIPLLGTGKP 481
|
|
| A_NRPS_Srf_like |
cd12117 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including Bacillus subtilis ... |
4-338 |
8.09e-34 |
|
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: 130.01 E-value: 8.09e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755522749 4 VLWPVEGIGRVCLGglktRRWMALTESDIFWNTTDTGWVKAAWTLFSAWSNGACIFVHELPRV-DAKTILNTLCRFPITT 82
Cdd:cd12117 154 VAVTHRGVVRLVKN----TNYVTLGPDDRVLQTSPLAFDASTFEIWGALLNGARLVLAPKGTLlDPDALGALIAEEGVTV 229
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755522749 83 LCCVPTLFRLLVQEDLTRykFQCLRHCLTGGEALNPD-VRDKWKSQTGLELHEGYGQSET-------VVICGNSRNSTIk 154
Cdd:cd12117 230 LWLTAALFNQLADEDPEC--FAGLRELLTGGEVVSPPhVRRVLAACPGLRLVNGYGPTENttfttshVVTELDEVAGSI- 306
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755522749 155 sgSMGKASPPYDVQIVDEEGNVLPPGKEGNIavrikptrpfcffnC---------YLDNPEKTAAS-------EQGDFYI 218
Cdd:cd12117 307 --PIGRPIANTRVYVLDEDGRPVPPGVPGEL--------------YvggdglalgYLNRPALTAERfvadpfgPGERLYR 370
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755522749 219 TGDRAHMDEDGYFWFLGRNDDVINSSSYRIGPVEVESALAEHPAVLESAVVsspdPIRGEVVKAFIVlspAYASHDPEAL 298
Cdd:cd12117 371 TGDLARWLPDGRLEFLGRIDDQVKIRGFRIELGEIEAALRAHPGVREAVVV----VREDAGGDKRLV---AYVVAEGALD 443
|
330 340 350 360
....*....|....*....|....*....|....*....|
gi 755522749 299 TRELQEHVKTVTAPYKYPRKVAFISELPKTVSGKILRSKL 338
Cdd:cd12117 444 AAELRAFLRERLPAYMVPAAFVVLDELPLTANGKVDRRAL 483
|
|
| PRK12492 |
PRK12492 |
long-chain-fatty-acid--CoA ligase; Provisional |
64-340 |
1.09e-33 |
|
long-chain-fatty-acid--CoA ligase; Provisional
Pssm-ID: 171539 [Multi-domain] Cd Length: 562 Bit Score: 130.71 E-value: 1.09e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755522749 64 PRvDAKTILNTLCRFPITTLCCVPTLF-RLLVQEDLTRYKFQCLRHCLTGGEALNPDVRDKWKSQTGLELHEGYGQSETV 142
Cdd:PRK12492 293 PR-DIPGFIKELGKWRFSALLGLNTLFvALMDHPGFKDLDFSALKLTNSGGTALVKATAERWEQLTGCTIVEGYGLTETS 371
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755522749 143 -VICGNSRNSTIKSGSMGKASPPYDVQIVDEEGNVLPPGKEGNIAVRiKPTrpfcFFNCYLDNPEKTAASEQGD-FYITG 220
Cdd:PRK12492 372 pVASTNPYGELARLGTVGIPVPGTALKVIDDDGNELPLGERGELCIK-GPQ----VMKGYWQQPEATAEALDAEgWFKTG 446
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755522749 221 DRAHMDEDGYFWFLGRNDDVINSSSYRIGPVEVESALAEHPAVLESAVVSSPDPIRGEVVKAFIVlspayaSHDPEALTR 300
Cdd:PRK12492 447 DIAVIDPDGFVRIVDRKKDLIIVSGFNVYPNEIEDVVMAHPKVANCAAIGVPDERSGEAVKLFVV------ARDPGLSVE 520
|
250 260 270 280
....*....|....*....|....*....|....*....|
gi 755522749 301 ELQEHVKTVTAPYKYPRKVAFISELPKTVSGKILRSKLRN 340
Cdd:PRK12492 521 ELKAYCKENFTGYKVPKHIVLRDSLPMTPVGKILRRELRD 560
|
|
| PRK07798 |
PRK07798 |
acyl-CoA synthetase; Validated |
44-332 |
1.56e-33 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236100 [Multi-domain] Cd Length: 533 Bit Score: 129.62 E-value: 1.56e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755522749 44 AAWTLFSAWSNGACIFVHELPRVDAKTILNTLCRFPITTLCCVPTLF-RLLVQE--DLTRYKFQCLRHCLTGGEALNPDV 120
Cdd:PRK07798 233 GQWAAFAALFSGQTVVLLPDVRFDADEVWRTIEREKVNVITIVGDAMaRPLLDAleARGPYDLSSLFAIASGGALFSPSV 312
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755522749 121 RDKWKSQ-TGLELHEGYGQSETvvicGNSRNSTIKSGSMGKASPPY----DVQIVDEEGNVLPPG--------KEGNIAV 187
Cdd:PRK07798 313 KEALLELlPNVVLTDSIGSSET----GFGGSGTVAKGAVHTGGPRFtigpRTVVLDEDGNPVEPGsgeigwiaRRGHIPL 388
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755522749 188 RikptrpfcffncYLDNPEKTAAS---EQGDFY-ITGDRAHMDEDGYFWFLGRNDDVINSSSYRIGPVEVESALAEHPAV 263
Cdd:PRK07798 389 G------------YYKDPEKTAETfptIDGVRYaIPGDRARVEADGTITLLGRGSVCINTGGEKVFPEEVEEALKAHPDV 456
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 755522749 264 LESAVVSSPDPIRGEVVKAFIVLSPAyASHDPEaltrELQEHVKTVTAPYKYPRKVAFISELPKTVSGK 332
Cdd:PRK07798 457 ADALVVGVPDERWGQEVVAVVQLREG-ARPDLA----ELRAHCRSSLAGYKVPRAIWFVDEVQRSPAGK 520
|
|
| PLN02654 |
PLN02654 |
acetate-CoA ligase |
30-339 |
1.99e-33 |
|
acetate-CoA ligase
Pssm-ID: 215353 [Multi-domain] Cd Length: 666 Bit Score: 130.40 E-value: 1.99e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755522749 30 SDIFWNTTDTGWVKA-AWTLFSAWSNGACIFVHE-LPRV-DAKTILNTLCRFPITTLCCVPTLFRLLVQED---LTRYKF 103
Cdd:PLN02654 317 TDVYWCTADCGWITGhSYVTYGPMLNGATVLVFEgAPNYpDSGRCWDIVDKYKVTIFYTAPTLVRSLMRDGdeyVTRHSR 396
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755522749 104 QCLRHCLTGGEALNPDVrdkWK------SQTGLELHEGYGQSET--VVICGNSRNSTIKSGSmgKASPPYDVQ--IVDEE 173
Cdd:PLN02654 397 KSLRVLGSVGEPINPSA---WRwffnvvGDSRCPISDTWWQTETggFMITPLPGAWPQKPGS--ATFPFFGVQpvIVDEK 471
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755522749 174 GNVLPPGKEGNIAvrIKPTRPFCFFNCYLDNP--EKTAASEQGDFYITGDRAHMDEDGYFWFLGRNDDVINSSSYRIGPV 251
Cdd:PLN02654 472 GKEIEGECSGYLC--VKKSWPGAFRTLYGDHEryETTYFKPFAGYYFSGDGCSRDKDGYYWLTGRVDDVINVSGHRIGTA 549
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755522749 252 EVESALAEHPAVLESAVVSSPDPIRGEVVKAFIVLSPAYAShdPEALTRELQEHVKTVTAPYKYPRKVAFISELPKTVSG 331
Cdd:PLN02654 550 EVESALVSHPQCAEAAVVGIEHEVKGQGIYAFVTLVEGVPY--SEELRKSLILTVRNQIGAFAAPDKIHWAPGLPKTRSG 627
|
....*...
gi 755522749 332 KILRSKLR 339
Cdd:PLN02654 628 KIMRRILR 635
|
|
| DltA |
cd05945 |
D-alanine:D-alanyl carrier protein ligase (DltA) and similar proteins; This family includes ... |
23-338 |
2.78e-33 |
|
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: 128.13 E-value: 2.78e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755522749 23 RWM----ALTESDIFWNTTDTGWVKAAWTLFSAWSNGACIFVheLPR---VDAKTILNTLCRFPITTLCCVPTLFRLLVQ 95
Cdd:cd05945 127 NWMlsdfPLGPGDVFLNQAPFSFDLSVMDLYPALASGATLVP--VPRdatADPKQLFRFLAEHGITVWVSTPSFAAMCLL 204
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755522749 96 -EDLTRYKFQCLRHCLTGGEALNPDVRDKWKSQT-GLELHEGYGQSETVVICgnsrnSTI----------KSGSMGKASP 163
Cdd:cd05945 205 sPTFTPESLPSLRHFLFCGEVLPHKTARALQQRFpDARIYNTYGPTEATVAV-----TYIevtpevldgyDRLPIGYAKP 279
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755522749 164 PYDVQIVDEEGNVLPPGKEGNIAVRIKptrpfCFFNCYLDNPEKTAAS----EQGDFYITGDRAHMDEDGYFWFLGRNDD 239
Cdd:cd05945 280 GAKLVILDEDGRPVPPGEKGELVISGP-----SVSKGYLNNPEKTAAAffpdEGQRAYRTGDLVRLEADGLLFYRGRLDF 354
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755522749 240 VINSSSYRIGPVEVESALAEHPAVLESAVVSSPDPIRGEVVKAFIVLSPayasHDPEALTRELQEHVKTVTAPYKYPRKV 319
Cdd:cd05945 355 QVKLNGYRIELEEIEAALRQVPGVKEAVVVPKYKGEKVTELIAFVVPKP----GAEAGLTKAIKAELAERLPPYMIPRRF 430
|
330
....*....|....*....
gi 755522749 320 AFISELPKTVSGKILRSKL 338
Cdd:cd05945 431 VYLDELPLNANGKIDRKAL 449
|
|
| PRK13295 |
PRK13295 |
cyclohexanecarboxylate-CoA ligase; Reviewed |
82-341 |
3.92e-33 |
|
cyclohexanecarboxylate-CoA ligase; Reviewed
Pssm-ID: 171961 [Multi-domain] Cd Length: 547 Bit Score: 128.63 E-value: 3.92e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755522749 82 TLCCVPTLFRLLVQEDLTRYKFQCLRHCLTGGEALNPDVRDKWKSQTGLELHEGYGQSET--VVICGNSRNSTIKSGSMG 159
Cdd:PRK13295 290 TMASTPFLTDLTRAVKESGRPVSSLRTFLCAGAPIPGALVERARAALGAKIVSAWGMTENgaVTLTKLDDPDERASTTDG 369
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755522749 160 KASPPYDVQIVDEEGNVLPPGKEGNIAVRIkptrpfCF-FNCYLDNPEKTAASEQGdFYITGDRAHMDEDGYFWFLGRND 238
Cdd:PRK13295 370 CPLPGVEVRVVDADGAPLPAGQIGRLQVRG------CSnFGGYLKRPQLNGTDADG-WFDTGDLARIDADGYIRISGRSK 442
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755522749 239 DVINSSSYRIGPVEVESALAEHPAVLESAVVSSPDPIRGEVVKAFIVLSPAyASHDPEALTRELQEHvkTVTAPYkYPRK 318
Cdd:PRK13295 443 DVIIRGGENIPVVEIEALLYRHPAIAQVAIVAYPDERLGERACAFVVPRPG-QSLDFEEMVEFLKAQ--KVAKQY-IPER 518
|
250 260
....*....|....*....|...
gi 755522749 319 VAFISELPKTVSGKILRSKLRNQ 341
Cdd:PRK13295 519 LVVRDALPRTPSGKIQKFRLREM 541
|
|
| PRK06060 |
PRK06060 |
p-hydroxybenzoic acid--AMP ligase FadD22; |
50-341 |
4.70e-33 |
|
p-hydroxybenzoic acid--AMP ligase FadD22;
Pssm-ID: 180374 [Multi-domain] Cd Length: 705 Bit Score: 129.77 E-value: 4.70e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755522749 50 SAW---SNGACIFVHELPrVDAKTILNTLCRFPITTLCCVPTLFRLLVqEDLTRYKFQCLRHCLTGGEALNPDVRDKWKS 126
Cdd:PRK06060 205 SVWfplATGGSAVINSAP-VTPEAAAILSARFGPSVLYGVPNFFARVI-DSCSPDSFRSLRCVVSAGEALELGLAERLME 282
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755522749 127 Q-TGLELHEGYGQSETVVICGNSRNSTIKSGSMGKASPPYDVQIVDEEGNVLPPGKEGNIAVRiKPTrpfcFFNCYLDNP 205
Cdd:PRK06060 283 FfGGIPILDGIGSTEVGQTFVSNRVDEWRLGTLGRVLPPYEIRVVAPDGTTAGPGVEGDLWVR-GPA----IAKGYWNRP 357
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755522749 206 EKTAasEQGDFYITGDRAHMDEDGYFWFLGRNDDVINSSSYRIGPVEVESALAEHPAVLESAVVSSPDPIRGEVVKAFIV 285
Cdd:PRK06060 358 DSPV--ANEGWLDTRDRVCIDSDGWVTYRCRADDTEVIGGVNVDPREVERLIIEDEAVAEAAVVAVRESTGASTLQAFLV 435
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*.
gi 755522749 286 lsPAYASHDPEALTRELQEHVKTVTAPYKYPRKVAFISELPKTVSGKILRSKLRNQ 341
Cdd:PRK06060 436 --ATSGATIDGSVMRDLHRGLLNRLSAFKVPHRFAVVDRLPRTPNGKLVRGALRKQ 489
|
|
| PLN02574 |
PLN02574 |
4-coumarate--CoA ligase-like |
53-339 |
6.94e-33 |
|
4-coumarate--CoA ligase-like
Pssm-ID: 215312 [Multi-domain] Cd Length: 560 Bit Score: 128.42 E-value: 6.94e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755522749 53 SNGACIFVheLPRVDAKTILNTLCRFPITTLCCVPTLFRLLVQ--EDLTRYKFQCLRHCLTGGEALNPD-VRDKWKSQTG 129
Cdd:PLN02574 268 SLGSTIVV--MRRFDASDMVKVIDRFKVTHFPVVPPILMALTKkaKGVCGEVLKSLKQVSCGAAPLSGKfIQDFVQTLPH 345
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755522749 130 LELHEGYGQSETVVICGNSRNS--TIKSGSMGKASPPYDVQIVD-EEGNVLPPGKEGNIAVRiKPTrpfcFFNCYLDNPE 206
Cdd:PLN02574 346 VDFIQGYGMTESTAVGTRGFNTekLSKYSSVGLLAPNMQAKVVDwSTGCLLPPGNCGELWIQ-GPG----VMKGYLNNPK 420
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755522749 207 KTAASEQGDFYI-TGDRAHMDEDGYFWFLGRNDDVINSSSYRIGPVEVESALAEHPAVLESAVVSSPDPIRGEVVKAFIV 285
Cdd:PLN02574 421 ATQSTIDKDGWLrTGDIAYFDEDGYLYIVDRLKEIIKYKGFQIAPADLEAVLISHPEIIDAAVTAVPDKECGEIPVAFVV 500
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*
gi 755522749 286 LSPAyashdpEALTRE-LQEHVKTVTAPYKYPRKVAFISELPKTVSGKILRSKLR 339
Cdd:PLN02574 501 RRQG------STLSQEaVINYVAKQVAPYKKVRKVVFVQSIPKSPAGKILRRELK 549
|
|
| A_NRPS_PvdJ-like |
cd17649 |
non-ribosomal peptide synthetase; This family of the adenylation (A) domain of nonribosomal ... |
48-339 |
9.91e-33 |
|
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: 126.33 E-value: 9.91e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755522749 48 LFSAWSNGACIFVHELPR-VDAKTILNTLCRFPITTLCCVPTLFRLLVQE--DLTRYKFQCLRHCLTGGEALNPDVRDKW 124
Cdd:cd17649 153 LLPPLICGACVVLRPDELwASADELAEMVRELGVTVLDLPPAYLQQLAEEadRTGDGRPPSLRLYIFGGEALSPELLRRW 232
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755522749 125 KsQTGLELHEGYGQSETVV---ICGNSRNSTIKSGSM--GKASPPYDVQIVDEEGNVLPPGKEGN--IAVRikptrpfCF 197
Cdd:cd17649 233 L-KAPVRLFNAYGPTEATVtplVWKCEAGAARAGASMpiGRPLGGRSAYILDADLNPVPVGVTGElyIGGE-------GL 304
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755522749 198 FNCYLDNPEKTA--------ASEQGDFYITGDRAHMDEDGYFWFLGRNDDVINSSSYRIGPVEVESALAEHPAVLESAVV 269
Cdd:cd17649 305 ARGYLGRPELTAerfvpdpfGAPGSRLYRTGDLARWRDDGVIEYLGRVDHQVKIRGFRIELGEIEAALLEHPGVREAAVV 384
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755522749 270 SSPDPIRGEVVkAFIVLSPAYAShdpEALTRELQEHVKTVTAPYKYPRKVAFISELPKTVSGKILRSKLR 339
Cdd:cd17649 385 ALDGAGGKQLV-AYVVLRAAAAQ---PELRAQLRTALRASLPDYMVPAHLVFLARLPLTPNGKLDRKALP 450
|
|
| PRK08315 |
PRK08315 |
AMP-binding domain protein; Validated |
53-341 |
1.09e-32 |
|
AMP-binding domain protein; Validated
Pssm-ID: 236236 [Multi-domain] Cd Length: 559 Bit Score: 127.62 E-value: 1.09e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755522749 53 SNGACIfVHELPRVDAKTILNTLCRFPITTLCCVPTLF-RLLVQEDLTRYKFQCLRhclTGGEALNP-------DVRDKw 124
Cdd:PRK08315 264 THGATM-VYPGEGFDPLATLAAVEEERCTALYGVPTMFiAELDHPDFARFDLSSLR---TGIMAGSPcpievmkRVIDK- 338
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755522749 125 ksqtgLELHE---GYGQSETV-VICGNSRNSTI--KSGSMGKASPPYDVQIVDEE-GNVLPPGKEGNIAvrikpTRPFCF 197
Cdd:PRK08315 339 -----MHMSEvtiAYGMTETSpVSTQTRTDDPLekRVTTVGRALPHLEVKIVDPEtGETVPRGEQGELC-----TRGYSV 408
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755522749 198 FNCYLDNPEKTAASEQGDFYI-TGDRAHMDEDGYFWFLGRNDDVI-----NsssyrIGPVEVESALAEHPAVLESAVVSS 271
Cdd:PRK08315 409 MKGYWNDPEKTAEAIDADGWMhTGDLAVMDEEGYVNIVGRIKDMIirggeN-----IYPREIEEFLYTHPKIQDVQVVGV 483
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755522749 272 PDPIRGEVVKAFIVLSPAyASHDPEaltrELQEHVKTVTAPYKYPRKVAFISELPKTVSGKILRSKLRNQ 341
Cdd:PRK08315 484 PDEKYGEEVCAWIILRPG-ATLTEE----DVRDFCRGKIAHYKIPRYIRFVDEFPMTVTGKIQKFKMREM 548
|
|
| A_NRPS_SidN3_like |
cd05918 |
The adenylation (A) domain of siderophore-synthesizing nonribosomal peptide synthetases (NRPS); ... |
49-340 |
2.91e-32 |
|
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: 125.73 E-value: 2.91e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755522749 49 FSAWSNGACIFV-HELPRVD--AKTIlntlCRFPITTLCCVPTLFRLLVQEDLTrykfqCLRHCLTGGEALNPDVRDKWK 125
Cdd:cd05918 166 FTTLAAGGCLCIpSEEDRLNdlAGFI----NRLRVTWAFLTPSVARLLDPEDVP-----SLRTLVLGGEALTQSDVDTWA 236
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755522749 126 SqtGLELHEGYGQSETVVIC-GNSRNSTIKSGSMGkasPPYDVQ--IVDEEGN--VLPPGK------EGNIAVRikptrp 194
Cdd:cd05918 237 D--RVRLINAYGPAECTIAAtVSPVVPSTDPRNIG---RPLGATcwVVDPDNHdrLVPIGAvgelliEGPILAR------ 305
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755522749 195 fcffnCYLDNPEKTAAS--------------EQGDFYITGDRAHMDEDGYFWFLGRNDDVINSSSYRIGPVEVESALAEH 260
Cdd:cd05918 306 -----GYLNDPEKTAAAfiedpawlkqegsgRGRRLYRTGDLVRYNPDGSLEYVGRKDTQVKIRGQRVELGEIEHHLRQS 380
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755522749 261 PAVLESAVVSSPDPIRGEVVK---AFIVLSPAYA------------SHDPEALTRELQEHVKTVTAPYKYPRKVAFISEL 325
Cdd:cd05918 381 LPGAKEVVVEVVKPKDGSSSPqlvAFVVLDGSSSgsgdgdslflepSDEFRALVAELRSKLRQRLPSYMVPSVFLPLSHL 460
|
330
....*....|....*
gi 755522749 326 PKTVSGKILRSKLRN 340
Cdd:cd05918 461 PLTASGKIDRRALRE 475
|
|
| AFD_YhfT-like |
cd17633 |
fatty acid-CoA ligase VraA; This family of acyl-CoA ligases includes Bacillus subtilis YhfT, ... |
48-335 |
4.71e-32 |
|
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: 122.13 E-value: 4.71e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755522749 48 LFSAWSNGAcifVHELPRVDAKTILNTLCRFPITTLCCVPTLFRLLVQEDLTRYKFQCLrhcLTGGEALNPDVRDKWKSQ 127
Cdd:cd17633 60 ISALYLGGT---FIGQRKFNPKSWIRKINQYNATVIYLVPTMLQALARTLEPESKIKSI---FSSGQKLFESTKKKLKNI 133
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755522749 128 T-GLELHEGYGQSETVVICGNSRNSTIKSGSMGKASPPYDVQIVDEEGnvlppGKEGNIAVRIKptrpfCFFNCYLDNPE 206
Cdd:cd17633 134 FpKANLIEFYGTSELSFITYNFNQESRPPNSVGRPFPNVEIEIRNADG-----GEIGKIFVKSE-----MVFSGYVRGGF 203
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755522749 207 ktaaSEQGDFYITGDRAHMDEDGYFWFLGRNDDVINSSSYRIGPVEVESALAEHPAVLESAVVSSPDPIRGEVVKAFIVL 286
Cdd:cd17633 204 ----SNPDGWMSVGDIGYVDEEGYLYLVGRESDMIIIGGINIFPTEIESVLKAIPGIEEAIVVGIPDARFGEIAVALYSG 279
|
250 260 270 280
....*....|....*....|....*....|....*....|....*....
gi 755522749 287 SpayashdpEALTRELQEHVKTVTAPYKYPRKVAFISELPKTVSGKILR 335
Cdd:cd17633 280 D--------KLTYKQLKRFLKQKLSRYEIPKKIIFVDSLPYTSSGKIAR 320
|
|
| PRK06087 |
PRK06087 |
medium-chain fatty-acid--CoA ligase; |
87-345 |
3.83e-31 |
|
medium-chain fatty-acid--CoA ligase;
Pssm-ID: 180393 [Multi-domain] Cd Length: 547 Bit Score: 123.32 E-value: 3.83e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755522749 87 PTLFRLLVQEDLTRYKFQCLRHCLTGGEALNPD-VRDKWksQTGLELHEGYGQSETV--VICGNSRNSTIKSGSMGKASP 163
Cdd:PRK06087 285 PFIYDLLNLLEKQPADLSALRFFLCGGTTIPKKvARECQ--QRGIKLLSVYGSTESSphAVVNLDDPLSRFMHTDGYAAA 362
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755522749 164 PYDVQIVDEEGNVLPPGKEGNIAVRikptRPFCFFNcYLDNPEKTAAS--EQGDFYiTGDRAHMDEDGYFWFLGRNDDVI 241
Cdd:PRK06087 363 GVEIKVVDEARKTLPPGCEGEEASR----GPNVFMG-YLDEPELTARAldEEGWYY-SGDLCRMDEAGYIKITGRKKDII 436
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755522749 242 NSSSYRIGPVEVESALAEHPAVLESAVVSSPDPIRGEVVKAFIVLSPAYASHDPEALTRELQEhvKTVtAPYKYPRKVAF 321
Cdd:PRK06087 437 VRGGENISSREVEDILLQHPKIHDACVVAMPDERLGERSCAYVVLKAPHHSLTLEEVVAFFSR--KRV-AKYKYPEHIVV 513
|
250 260
....*....|....*....|....
gi 755522749 322 ISELPKTVSGKILRSKLRnQEWGR 345
Cdd:PRK06087 514 IDKLPRTASGKIQKFLLR-KDIMR 536
|
|
| PLN02330 |
PLN02330 |
4-coumarate--CoA ligase-like 1 |
65-341 |
2.33e-30 |
|
4-coumarate--CoA ligase-like 1
Pssm-ID: 215189 [Multi-domain] Cd Length: 546 Bit Score: 120.85 E-value: 2.33e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755522749 65 RVDAKTILNTLCRFPITTLCCVPTLFRLLVQE------DLTRYKfqcLRHCLTGGEALNPDVRDKWKSQ-TGLELHEGYG 137
Cdd:PLN02330 261 RFELRTFLNALITQEVSFAPIVPPIILNLVKNpiveefDLSKLK---LQAIMTAAAPLAPELLTAFEAKfPGVQVQEAYG 337
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755522749 138 QSETVVIC---GN-SRNSTI-KSGSMGKASPPYDVQIVD-EEGNVLPPGKEGNIAVRIKptrpfCFFNCYLDNPEKTAAS 211
Cdd:PLN02330 338 LTEHSCITlthGDpEKGHGIaKKNSVGFILPNLEVKFIDpDTGRSLPKNTPGELCVRSQ-----CVMQGYYNNKEETDRT 412
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755522749 212 EQGDFYI-TGDRAHMDEDGYFWFLGRNDDVINSSSYRIGPVEVESALAEHPAVLESAVVSSPDPIRGEVVKAFIVLSPAY 290
Cdd:PLN02330 413 IDEDGWLhTGDIGYIDDDGDIFIVDRIKELIKYKGFQVAPAELEAILLTHPSVEDAAVVPLPDEEAGEIPAACVVINPKA 492
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|.
gi 755522749 291 ASHDPEALtrelqEHVKTVTAPYKYPRKVAFISELPKTVSGKILRSKLRNQ 341
Cdd:PLN02330 493 KESEEDIL-----NFVAANVAHYKKVRVVQFVDSIPKSLSGKIMRRLLKEK 538
|
|
| PRK08162 |
PRK08162 |
acyl-CoA synthetase; Validated |
40-341 |
2.81e-30 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236169 [Multi-domain] Cd Length: 545 Bit Score: 120.82 E-value: 2.81e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755522749 40 GWVkAAWTLFSAWSNGACifvheLPRVDAKTILNTLCRFPITTLCCVPTLFRLLVQ-EDLTRYKFQCLRHCLTGGEALNP 118
Cdd:PRK08162 237 GWC-FPWTVAARAGTNVC-----LRKVDPKLIFDLIREHGVTHYCGAPIVLSALINaPAEWRAGIDHPVHAMVAGAAPPA 310
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755522749 119 DVRDKWKsQTGLELHEGYGQSET---VVICG-----NSRNSTIKSGSMGKASPPYDVQivdEEGNVLPP---------GK 181
Cdd:PRK08162 311 AVIAKME-EIGFDLTHVYGLTETygpATVCAwqpewDALPLDERAQLKARQGVRYPLQ---EGVTVLDPdtmqpvpadGE 386
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755522749 182 E-GNIAVR----IKPtrpfcffncYLDNPEKTAASEQGDFYITGDRAHMDEDGYFWFLGRNDDVINSSSYRIGPVEVESA 256
Cdd:PRK08162 387 TiGEIMFRgnivMKG---------YLKNPKATEEAFAGGWFHTGDLAVLHPDGYIKIKDRSKDIIISGGENISSIEVEDV 457
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755522749 257 LAEHPAVLESAVVSSPDPIRGEVVKAFIVLSPAyASHDPEaltrELQEHVKTVTAPYKYPRKVAFiSELPKTVSGKILRS 336
Cdd:PRK08162 458 LYRHPAVLVAAVVAKPDPKWGEVPCAFVELKDG-ASATEE----EIIAHCREHLAGFKVPKAVVF-GELPKTSTGKIQKF 531
|
....*
gi 755522749 337 KLRNQ 341
Cdd:PRK08162 532 VLREQ 536
|
|
| A_NRPS_Sfm_like |
cd12115 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including Saframycin A gene ... |
48-338 |
1.30e-29 |
|
The adenylation domain of nonribosomal peptide synthetases (NRPS), including Saframycin A gene cluster from Streptomyces lavendulae; The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions. This family includes the saframycin A gene cluster from Streptomyces lavendulae which implicates the NRPS system for assembling the unusual tetrapeptidyl skeleton in an iterative manner. It also includes saframycin Mx1 produced by Myxococcus xanthus NRPS.
Pssm-ID: 341280 [Multi-domain] Cd Length: 447 Bit Score: 117.80 E-value: 1.30e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755522749 48 LFSAWSNGACIFVHE-------LPRVDAKTILNTlcrfpittlccVPTLFRLLVQEDLTRYKFQCLrhCLtGGEALNPD- 119
Cdd:cd12115 164 LFGPLATGGKVVLADnvlalpdLPAAAEVTLINT-----------VPSAAAELLRHDALPASVRVV--NL-AGEPLPRDl 229
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755522749 120 VRDKWKSQTGLELHEGYGQSET-------VVICGNSRNSTIksgsmGKASPPYDVQIVDEEGNVLPPGKEGNIAVR-IKP 191
Cdd:cd12115 230 VQRLYARLQVERVVNLYGPSEDttystvaPVPPGASGEVSI-----GRPLANTQAYVLDRALQPVPLGVPGELYIGgAGV 304
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755522749 192 TRpfcffnCYLDNPEKTAAS------EQGD-FYITGDRAHMDEDGYFWFLGRNDDVINSSSYRIGPVEVESALAEHPAVL 264
Cdd:cd12115 305 AR------GYLGRPGLTAERflpdpfGPGArLYRTGDLVRWRPDGLLEFLGRADNQVKVRGFRIELGEIEAALRSIPGVR 378
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 755522749 265 ESAVVSSPDPIRGEVVKAFIVLSPAYAShdpeaLTRELQEHVKTVTAPYKYPRKVAFISELPKTVSGKILRSKL 338
Cdd:cd12115 379 EAVVVAIGDAAGERRLVAYIVAEPGAAG-----LVEDLRRHLGTRLPAYMVPSRFVRLDALPLTPNGKIDRSAL 447
|
|
| PLN03102 |
PLN03102 |
acyl-activating enzyme; Provisional |
46-340 |
3.40e-28 |
|
acyl-activating enzyme; Provisional
Pssm-ID: 215576 [Multi-domain] Cd Length: 579 Bit Score: 115.12 E-value: 3.40e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755522749 46 WTLfsAWSNGA------CIfvhelPRVDAKTILNTLCRFPITTLCCVPTLFRLLVQEDLTRYKFQCLR-HCLTGGEAlNP 118
Cdd:PLN03102 242 WTF--TWGTAArggtsvCM-----RHVTAPEIYKNIEMHNVTHMCCVPTVFNILLKGNSLDLSPRSGPvHVLTGGSP-PP 313
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755522749 119 DVRDKWKSQTGLELHEGYGQSET---VVIC-----------GNSRNSTIKSGSMGKASPPYDVQIVDEEGNVLPPGKE-G 183
Cdd:PLN03102 314 AALVKKVQRLGFQVMHAYGLTEAtgpVLFCewqdewnrlpeNQQMELKARQGVSILGLADVDVKNKETQESVPRDGKTmG 393
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755522749 184 NIAVRIKptrpfCFFNCYLDNPEKTAASEQGDFYITGDRAHMDEDGYFWFLGRNDDVINSSSYRIGPVEVESALAEHPAV 263
Cdd:PLN03102 394 EIVIKGS-----SIMKGYLKNPKATSEAFKHGWLNTGDVGVIHPDGHVEIKDRSKDIIISGGENISSVEVENVLYKYPKV 468
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755522749 264 LESAVVSSPDPIRGEVVKAFIVLSPAYASHDPEA---LTRE--LQEHVKTVTAPYKYPRKVAFISELPKTVSGKILRSKL 338
Cdd:PLN03102 469 LETAVVAMPHPTWGETPCAFVVLEKGETTKEDRVdklVTRErdLIEYCRENLPHFMCPRKVVFLQELPKNGNGKILKPKL 548
|
..
gi 755522749 339 RN 340
Cdd:PLN03102 549 RD 550
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
44-338 |
7.77e-28 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 115.05 E-value: 7.77e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755522749 44 AAWTLFSAWSNGACIFVHELPRVDAKTILNTLCRFPITTLCCVPTLFRLLVQEDLTRYKFQCLRHCLTGGEALNPDVRDK 123
Cdd:PRK12316 4749 SHEGLYHPLINGASVVIRDDSLWDPERLYAEIHEHRVTVLVFPPVYLQQLAEHAERDGEPPSLRVYCFGGEAVAQASYDL 4828
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755522749 124 -WKSQTGLELHEGYGQSETVV--ICGNSRNSTIKSGS---MGKASPPYDVQIVDEEGNVLPPGKEGNIAVRIKptrpfCF 197
Cdd:PRK12316 4829 aWRALKPVYLFNGYGPTETTVtvLLWKARDGDACGAAympIGTPLGNRSGYVLDGQLNPLPVGVAGELYLGGE-----GV 4903
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755522749 198 FNCYLDNPEKTAA-------SEQGD-FYITGDRAHMDEDGYFWFLGRNDDVINSSSYRIGPVEVESALAEHPAVLESAVV 269
Cdd:PRK12316 4904 ARGYLERPALTAErfvpdpfGAPGGrLYRTGDLARYRADGVIDYLGRVDHQVKIRGFRIELGEIEARLREHPAVREAVVI 4983
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 755522749 270 SSPDPIRGEVVKAFIVLSPAYASHDPE--ALTRELQEHVKTVTAPYKYPRKVAFISELPKTVSGKILRSKL 338
Cdd:PRK12316 4984 AQEGAVGKQLVGYVVPQDPALADADEAqaELRDELKAALRERLPEYMVPAHLVFLARMPLTPNGKLDRKAL 5054
|
|
| PRK07867 |
PRK07867 |
acyl-CoA synthetase; Validated |
112-343 |
1.10e-27 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236120 [Multi-domain] Cd Length: 529 Bit Score: 113.24 E-value: 1.10e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755522749 112 GGEALNPDVrDKWKSQTGLELHEGYGQSETVVICgnSRNSTIKSGSMGKASPpyDVQIVD-EEGNVLPPGK-------EG 183
Cdd:PRK07867 274 GNEGAPGDI-ARFARRFGCVVVDGFGSTEGGVAI--TRTPDTPPGALGPLPP--GVAIVDpDTGTECPPAEdadgrllNA 348
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755522749 184 NIAV--RIKPTRPfCFFNCYLDNPEKTAASEQGDFYITGDRAHMDEDGYFWFLGRNDDVINSSSYRIGPVEVESALAEHP 261
Cdd:PRK07867 349 DEAIgeLVNTAGP-GGFEGYYNDPEADAERMRGGVYWSGDLAYRDADGYAYFAGRLGDWMRVDGENLGTAPIERILLRYP 427
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755522749 262 AVLESAVVSSPDPIRGEVVKAFIVLSPAyASHDPEALTRELqeHVKTVTAPYKYPRKVAFISELPKTVSGKILRSKLRNQ 341
Cdd:PRK07867 428 DATEVAVYAVPDPVVGDQVMAALVLAPG-AKFDPDAFAEFL--AAQPDLGPKQWPSYVRVCAELPRTATFKVLKRQLSAE 504
|
..
gi 755522749 342 EW 343
Cdd:PRK07867 505 GV 506
|
|
| AMP-binding_C |
pfam13193 |
AMP-binding enzyme C-terminal domain; This is a small domain that is found C terminal to ... |
252-332 |
1.31e-27 |
|
AMP-binding enzyme C-terminal domain; This is a small domain that is found C terminal to pfam00501. It has a central beta sheet core that is flanked by alpha helices.
Pssm-ID: 463804 [Multi-domain] Cd Length: 76 Bit Score: 103.01 E-value: 1.31e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755522749 252 EVESALAEHPAVLESAVVSSPDPIRGEVVKAFIVLSPayashDPEALTRELQEHVKTVTAPYKYPRKVAFISELPKTVSG 331
Cdd:pfam13193 1 EVESALVSHPAVAEAAVVGVPDELKGEAPVAFVVLKP-----GVELLEEELVAHVREELGPYAVPKEVVFVDELPKTRSG 75
|
.
gi 755522749 332 K 332
Cdd:pfam13193 76 K 76
|
|
| entE |
PRK10946 |
(2,3-dihydroxybenzoyl)adenylate synthase; |
162-339 |
7.81e-27 |
|
(2,3-dihydroxybenzoyl)adenylate synthase;
Pssm-ID: 236803 [Multi-domain] Cd Length: 536 Bit Score: 110.85 E-value: 7.81e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755522749 162 SPPYDVQIVDEEGNVLPPGKEGNIAVRIKPTrpfcfFNCYLDNPEKTAAS--EQGdFYITGDRAHMDEDGYFWFLGRNDD 239
Cdd:PRK10946 360 SPDDEVWVADADGNPLPQGEVGRLMTRGPYT-----FRGYYKSPQHNASAfdANG-FYCSGDLVSIDPDGYITVVGREKD 433
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755522749 240 VINSSSYRIGPVEVESALAEHPAVLESAVVSSPDPIRGEVVKAFIVLSPAYashDPEALTRELQEHvktVTAPYKYPRKV 319
Cdd:PRK10946 434 QINRGGEKIAAEEIENLLLRHPAVIHAALVSMEDELMGEKSCAFLVVKEPL---KAVQLRRFLREQ---GIAEFKLPDRV 507
|
170 180
....*....|....*....|
gi 755522749 320 AFISELPKTVSGKILRSKLR 339
Cdd:PRK10946 508 ECVDSLPLTAVGKVDKKQLR 527
|
|
| PRK07638 |
PRK07638 |
acyl-CoA synthetase; Validated |
60-341 |
1.07e-26 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236071 [Multi-domain] Cd Length: 487 Bit Score: 109.87 E-value: 1.07e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755522749 60 VHELPRVDAKTILNTLCRFPITTLCCVPTLFRLLVQEDltRYKFQCLRhCLTGGEALNPDVRDKWKSQ-TGLELHEGYGQ 138
Cdd:PRK07638 212 VHLMRKFIPNQVLDKLETENISVMYTVPTMLESLYKEN--RVIENKMK-IISSGAKWEAEAKEKIKNIfPYAKLYEFYGA 288
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755522749 139 SE-TVVICGNSRNSTIKSGSMGKASPPYDVQIVDEEGNVLPPGKEGNIAVRikptRPFcFFNCYLDNPEKTAASEQGDFY 217
Cdd:PRK07638 289 SElSFVTALVDEESERRPNSVGRPFHNVQVRICNEAGEEVQKGEIGTVYVK----SPQ-FFMGYIIGGVLARELNADGWM 363
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755522749 218 ITGDRAHMDEDGYFWFLGRNDDVINSSSYRIGPVEVESALAEHPAVLESAVVSSPDPIRGEVVKAFIvlspayashDPEA 297
Cdd:PRK07638 364 TVRDVGYEDEEGFIYIVGREKNMILFGGINIFPEEIESVLHEHPAVDEIVVIGVPDSYWGEKPVAII---------KGSA 434
|
250 260 270 280
....*....|....*....|....*....|....*....|....
gi 755522749 298 LTRELQEHVKTVTAPYKYPRKVAFISELPKTVSGKILRSKLRNQ 341
Cdd:PRK07638 435 TKQQLKSFCLQRLSSFKIPKEWHFVDEIPYTNSGKIARMEAKSW 478
|
|
| PRK06164 |
PRK06164 |
acyl-CoA synthetase; Validated |
47-341 |
4.75e-26 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 235722 [Multi-domain] Cd Length: 540 Bit Score: 108.68 E-value: 4.75e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755522749 47 TLFSAWSNGACifVHELPRVDAKTILNTLCRFPITTLCCVPTLFRLLVQEDLTRYKFQCLRHCltGGEALNPDVRD--KW 124
Cdd:PRK06164 239 TLLGALAGGAP--LVCEPVFDAARTARALRRHRVTHTFGNDEMLRRILDTAGERADFPSARLF--GFASFAPALGElaAL 314
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755522749 125 KSQTGLELHEGYGQSETVVICGNSRNSTIKS----GSMGKASPPYDVQIVD-EEGNVLPPGKEGNIAVRiKPTRpfcfFN 199
Cdd:PRK06164 315 ARARGVPLTGLYGSSEVQALVALQPATDPVSvrieGGGRPASPEARVRARDpQDGALLPDGESGEIEIR-APSL----MR 389
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755522749 200 CYLDNPEKTAASEQGD-FYITGDRAHMDEDGYFWFLGRNDDVINSSSYRIGPVEVESALAEHPAVLESAVVSSpdPIRGE 278
Cdd:PRK06164 390 GYLDNPDATARALTDDgYFRTGDLGYTRGDGQFVYQTRMGDSLRLGGFLVNPAEIEHALEALPGVAAAQVVGA--TRDGK 467
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 755522749 279 -VVKAFIVLSPAyASHDPEALTRELQEHVktvtAPYKYPRKVAFISELPKTVSG---KILRSKLRNQ 341
Cdd:PRK06164 468 tVPVAFVIPTDG-ASPDEAGLMAACREAL----AGFKVPARVQVVEAFPVTESAngaKIQKHRLREM 529
|
|
| A_NRPS_Bac |
cd17655 |
bacitracin synthetase and related proteins; This family of the adenylation (A) domain of ... |
45-338 |
7.83e-26 |
|
bacitracin synthetase and related proteins; This family of the adenylation (A) domain of nonribosomal peptide synthases (NRPS) includes bacitracin synthetases 1, 2, and 3 (BA1, also known as ATP-dependent cysteine adenylase or cysteine activase, BA2, also known as ATP-dependent lysine adenylase or lysine activase, and BA3, also known as ATP-dependent isoleucine adenylase or isoleucine activase) in Bacilli. Bacitracin is a mixture of related cyclic peptides used as a polypeptide antibiotic. This family also includes gramicidin synthetase 1 involved in synthesis of the cyclic peptide antibiotic gramicidin S via activation of phenylalanine. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.
Pssm-ID: 341310 [Multi-domain] Cd Length: 490 Bit Score: 107.41 E-value: 7.83e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755522749 45 AWTLFSAWSNGACIFV--HElPRVDAKTILNTLCRFPITTLCCVPTLFRLLVQEDLTryKFQCLRHCLTGGEALNPDVRD 122
Cdd:cd17655 193 VTEIFASLLSGNTLYIvrKE-TVLDGQALTQYIRQNRITIIDLTPAHLKLLDAADDS--EGLSLKHLIVGGEALSTELAK 269
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755522749 123 KWKSQTGL--ELHEGYGQSETVVIC--GNSRNSTIKSGS--MGKASPPYDVQIVDEEGNVLPPGKEGNIAV------Rik 190
Cdd:cd17655 270 KIIELFGTnpTITNAYGPTETTVDAsiYQYEPETDQQVSvpIGKPLGNTRIYILDQYGRPQPVGVAGELYIggegvaR-- 347
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755522749 191 ptrpfcffnCYLDNPEKTAAS------EQGD-FYITGDRAHMDEDGYFWFLGRNDDVINSSSYRIGPVEVESALAEHPAV 263
Cdd:cd17655 348 ---------GYLNRPELTAEKfvddpfVPGErMYRTGDLARWLPDGNIEFLGRIDHQVKIRGYRIELGEIEARLLQHPDI 418
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 755522749 264 LESAVVSSPDPIRGEVVKAFIVlspayasHDPEALTRELQEHVKTVTAPYKYPRKVAFISELPKTVSGKILRSKL 338
Cdd:cd17655 419 KEAVVIARKDEQGQNYLCAYIV-------SEKELPVAQLREFLARELPDYMIPSYFIKLDEIPLTPNGKVDRKAL 486
|
|
| A_NRPS_Ta1_like |
cd12116 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including salinosporamide A ... |
65-338 |
2.25e-25 |
|
The adenylation domain of nonribosomal peptide synthetases (NRPS), including salinosporamide A polyketide synthase; The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions. This family includes the myxovirescin (TA) antibiotic biosynthetic gene in Myxococcus xanthus; TA production plays a role in predation. It also includes the salinosporamide A polyketide synthase which is involved in the biosynthesis of salinosporamide A, a marine microbial metabolite whose chlorine atom is crucial for potent proteasome inhibition and anticancer activity.
Pssm-ID: 341281 [Multi-domain] Cd Length: 470 Bit Score: 106.22 E-value: 2.25e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755522749 65 RVDAKTILNTLCRFPITTLCCVPTLFRLLVQEDltrykFQCLR--HCLTGGEALNPDVRDKWKSQTGlELHEGYGQSETV 142
Cdd:cd12116 203 QRDPEALARLIEAHSITVMQATPATWRMLLDAG-----WQGRAglTALCGGEALPPDLAARLLSRVG-SLWNLYGPTETT 276
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755522749 143 V------ICGNSRNSTIksgsmGKASPPYDVQIVDEEGNVLPPGKEGNIAVrikptrpfcffnC-------YLDNPEKTA 209
Cdd:cd12116 277 IwstaarVTAAAGPIPI-----GRPLANTQVYVLDAALRPVPPGVPGELYI------------GgdgvaqgYLGRPALTA 339
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755522749 210 AS--------EQGDFYITGDRAHMDEDGYFWFLGRNDDVINSSSYRIGPVEVESALAEHPAVLESAVVSSPDPIRGEVVk 281
Cdd:cd12116 340 ERfvpdpfagPGSRLYRTGDLVRRRADGRLEYLGRADGQVKIRGHRIELGEIEAALAAHPGVAQAAVVVREDGGDRRLV- 418
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*...
gi 755522749 282 AFIVLspayasHDPEAL-TRELQEHVKTVTAPYKYPRKVAFISELPKTVSGKILRSKL 338
Cdd:cd12116 419 AYVVL------KAGAAPdAAALRAHLRATLPAYMVPSAFVRLDALPLTANGKLDRKAL 470
|
|
| PRK13388 |
PRK13388 |
acyl-CoA synthetase; Provisional |
106-343 |
2.79e-25 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 237374 [Multi-domain] Cd Length: 540 Bit Score: 106.26 E-value: 2.79e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755522749 106 LRHCLtGGEAlNPDVRDKWKSQTGLELHEGYGQSETVVICgnSRNSTIKSGSMGKASPpyDVQIV-------------DE 172
Cdd:PRK13388 267 LRVAF-GNEA-SPRDIAEFSRRFGCQVEDGYGSSEGAVIV--VREPGTPPGSIGRGAP--GVAIYnpetltecavarfDA 340
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755522749 173 EGNVLPPGKegniAV-RIKPTRPFCFFNCYLDNPEKTAASEQGDFYITGDRAHMDEDGYFWFLGRNDDVINSSSYRIGPV 251
Cdd:PRK13388 341 HGALLNADE----AIgELVNTAGAGFFEGYYNNPEATAERMRHGMYWSGDLAYRDADGWIYFAGRTADWMRVDGENLSAA 416
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755522749 252 EVESALAEHPAVLESAVVSSPDPIRGEVVKAFIVLSPAyASHDPEALTREL--QEHVKTVTApykyPRKVAFISELPKTV 329
Cdd:PRK13388 417 PIERILLRHPAINRVAVYAVPDERVGDQVMAALVLRDG-ATFDPDAFAAFLaaQPDLGTKAW----PRYVRIAADLPSTA 491
|
250
....*....|....
gi 755522749 330 SGKILRSKLRNQEW 343
Cdd:PRK13388 492 TNKVLKRELIAQGW 505
|
|
| PLN02479 |
PLN02479 |
acetate-CoA ligase |
40-339 |
4.65e-25 |
|
acetate-CoA ligase
Pssm-ID: 178097 [Multi-domain] Cd Length: 567 Bit Score: 105.70 E-value: 4.65e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755522749 40 GWVkAAWTLFSAWSNGACifvheLPRVDAKTILNTLCRFPITTLCCVPTLFRLLVQ--EDLTRYKFQCLRHCLTGGEALN 117
Cdd:PLN02479 250 GWC-FTWTLAALCGTNIC-----LRQVTAKAIYSAIANYGVTHFCAAPVVLNTIVNapKSETILPLPRVVHVMTAGAAPP 323
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755522749 118 PDVRDKWkSQTGLELHEGYGQSETV---VICG----------------NSRNSTIKSGSMGkasppydVQIVDEEGNVLP 178
Cdd:PLN02479 324 PSVLFAM-SEKGFRVTHTYGLSETYgpsTVCAwkpewdslppeeqarlNARQGVRYIGLEG-------LDVVDTKTMKPV 395
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755522749 179 P--GKE-GNIAVRIKPTrpfcfFNCYLDNPEKTAASEQGDFYITGDRAHMDEDGYFWFLGRNDDVINSSSYRIGPVEVES 255
Cdd:PLN02479 396 PadGKTmGEIVMRGNMV-----MKGYLKNPKANEEAFANGWFHSGDLGVKHPDGYIEIKDRSKDIIISGGENISSLEVEN 470
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755522749 256 ALAEHPAVLESAVVSSPDPIRGEVVKAFIVLSPAYASHDPEALTRELQEHVKTVTAPYKYPRKVAFiSELPKTVSGKILR 335
Cdd:PLN02479 471 VVYTHPAVLEASVVARPDERWGESPCAFVTLKPGVDKSDEAALAEDIMKFCRERLPAYWVPKSVVF-GPLPKTATGKIQK 549
|
....
gi 755522749 336 SKLR 339
Cdd:PLN02479 550 HVLR 553
|
|
| PLN02246 |
PLN02246 |
4-coumarate--CoA ligase |
55-341 |
5.61e-25 |
|
4-coumarate--CoA ligase
Pssm-ID: 215137 [Multi-domain] Cd Length: 537 Bit Score: 105.45 E-value: 5.61e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755522749 55 GACIFVheLPRVDAKTILNTLCRFPITTLCCVPTLFRLLVQED-LTRYKFQCLRHCLTGGEALNPDVRDKWKSQ-TGLEL 132
Cdd:PLN02246 250 GAAILI--MPKFEIGALLELIQRHKVTIAPFVPPIVLAIAKSPvVEKYDLSSIRMVLSGAAPLGKELEDAFRAKlPNAVL 327
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755522749 133 HEGYGQSET---VVIC-GNSRNST-IKSGSMGKASPPYDVQIVD-EEGNVLPPGKEGNIAVR----IKPtrpfcffncYL 202
Cdd:PLN02246 328 GQGYGMTEAgpvLAMClAFAKEPFpVKSGSCGTVVRNAELKIVDpETGASLPRNQPGEICIRgpqiMKG---------YL 398
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755522749 203 DNPEKTAASEQGDFYI-TGDRAHMDEDGYFWFLGRNDDVINSSSYRIGPVEVESALAEHPAVLESAVVSSPDPIRGEVVK 281
Cdd:PLN02246 399 NDPEATANTIDKDGWLhTGDIGYIDDDDELFIVDRLKELIKYKGFQVAPAELEALLISHPSIADAAVVPMKDEVAGEVPV 478
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|
gi 755522749 282 AFIVLSPayashDPEALTRELQEHVKTVTAPYKYPRKVAFISELPKTVSGKILRSKLRNQ 341
Cdd:PLN02246 479 AFVVRSN-----GSEITEDEIKQFVAKQVVFYKRIHKVFFVDSIPKAPSGKILRKDLRAK 533
|
|
| PRK05852 |
PRK05852 |
fatty acid--CoA ligase family protein; |
48-341 |
6.14e-25 |
|
fatty acid--CoA ligase family protein;
Pssm-ID: 235625 [Multi-domain] Cd Length: 534 Bit Score: 105.35 E-value: 6.14e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755522749 48 LFSAWSNGACIFVHELPRVDAKTILNTLCRFPITTLCCVPTLFRLLVQ---EDLTRYKFQCLRHCLTGGEALNPDVRDKW 124
Cdd:PRK05852 236 LLATLASGGAVLLPARGRFSAHTFWDDIKAVGATWYTAVPTIHQILLEraaTEPSGRKPAALRFIRSCSAPLTAETAQAL 315
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755522749 125 KSQTGLELHEGYGQSET--------VVICGNSRNSTIKSGSMGKASPPyDVQIVDEEGNVLPPGKEGNIAVRiKPTrpfc 196
Cdd:PRK05852 316 QTEFAAPVVCAFGMTEAthqvtttqIEGIGQTENPVVSTGLVGRSTGA-QIRIVGSDGLPLPAGAVGEVWLR-GTT---- 389
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755522749 197 FFNCYLDNPEKTAASEQGDFYITGDRAHMDEDGYFWFLGRNDDVINSSSYRIGPVEVESALAEHPAVLESAVVSSPDPIR 276
Cdd:PRK05852 390 VVRGYLGDPTITAANFTDGWLRTGDLGSLSAAGDLSIRGRIKELINRGGEKISPERVEGVLASHPNVMEAAVFGVPDQLY 469
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 755522749 277 GEVVKAFIVlsPAYASHdPEAltRELQEHVKTVTAPYKYPRKVAFISELPKTVSGKILRSKLRNQ 341
Cdd:PRK05852 470 GEAVAAVIV--PRESAP-PTA--EELVQFCRERLAAFEIPASFQEASGLPHTAKGSLDRRAVAEQ 529
|
|
| PRK08633 |
PRK08633 |
2-acyl-glycerophospho-ethanolamine acyltransferase; Validated |
67-333 |
1.16e-24 |
|
2-acyl-glycerophospho-ethanolamine acyltransferase; Validated
Pssm-ID: 236315 [Multi-domain] Cd Length: 1146 Bit Score: 105.39 E-value: 1.16e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755522749 67 DAKTILNTLCRFPITTLCCVPTLFRLLvqedlTRYK------FQCLRHCLTGGEALNPDVRDKWKSQTGLELHEGYGQSE 140
Cdd:PRK08633 860 DALGIAKLVAKHRATILLGTPTFLRLY-----LRNKklhplmFASLRLVVAGAEKLKPEVADAFEEKFGIRILEGYGATE 934
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755522749 141 TV-VICGNSRNSTI---------KSGSMGKASPPYDVQIVD-EEGNVLPPGKEGNIAVRiKPTRpfcfFNCYLDNPEKTA 209
Cdd:PRK08633 935 TSpVASVNLPDVLAadfkrqtgsKEGSVGMPLPGVAVRIVDpETFEELPPGEDGLILIG-GPQV----MKGYLGDPEKTA 1009
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755522749 210 A----SEQGDFYITGDRAHMDEDGYFWFLGRnddviNSSSYRIG----PV-EVESALAE--HPAVLESAVVSSPDPIRGE 278
Cdd:PRK08633 1010 EvikdIDGIGWYVTGDKGHLDEDGFLTITDR-----YSRFAKIGgemvPLgAVEEELAKalGGEEVVFAVTAVPDEKKGE 1084
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*
gi 755522749 279 VvkafIVLSPAYASHDPEALTRELQEhvKTVTAPYKyPRKVAFISELPKTVSGKI 333
Cdd:PRK08633 1085 K----LVVLHTCGAEDVEELKRAIKE--SGLPNLWK-PSRYFKVEALPLLGSGKL 1132
|
|
| A_NRPS_CmdD_like |
cd17652 |
similar to adenylation domain of chondramide synthase cmdD; This family of the adenylation (A) ... |
44-338 |
1.32e-24 |
|
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: 103.49 E-value: 1.32e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755522749 44 AAWTLFSAWSNGACIFVhelprVDAKTIL------NTLCRFPITTLCCVPTLFRLLVQEDLTRykfqcLRHCLTGGEALN 117
Cdd:cd17652 148 SVWELLMALLAGATLVL-----APAEELLpgeplaDLLREHRITHVTLPPAALAALPPDDLPD-----LRTLVVAGEACP 217
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755522749 118 PDVRDKWKsqTGLELHEGYGQSETVVicgnsrNSTIKSGSMGKASPP-------YDVQIVDEEGNVLPPGKEGNIAVR-I 189
Cdd:cd17652 218 AELVDRWA--PGRRMINAYGPTETTV------CATMAGPLPGGGVPPigrpvpgTRVYVLDARLRPVPPGVPGELYIAgA 289
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755522749 190 KPTRPfcffncYLDNPEKTAASEQGD--------FYITGDRAHMDEDGYFWFLGRNDDVINSSSYRIGPVEVESALAEHP 261
Cdd:cd17652 290 GLARG------YLNRPGLTAERFVADpfgapgsrMYRTGDLARWRADGQLEFLGRADDQVKIRGFRIELGEVEAALTEHP 363
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 755522749 262 AVLESAVVSSPDPIRGEVVKAFIVLSPayashDPEALTRELQEHVKTVTAPYKYPRKVAFISELPKTVSGKILRSKL 338
Cdd:cd17652 364 GVAEAVVVVRDDRPGDKRLVAYVVPAP-----GAAPTAAELRAHLAERLPGYMVPAAFVVLDALPLTPNGKLDRRAL 435
|
|
| PLN02860 |
PLN02860 |
o-succinylbenzoate-CoA ligase |
55-341 |
6.84e-24 |
|
o-succinylbenzoate-CoA ligase
Pssm-ID: 215464 [Multi-domain] Cd Length: 563 Bit Score: 102.57 E-value: 6.84e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755522749 55 GAC-IFvheLPRVDAKTILNTLCRFPITTLCCVPTLFRLLV---QEDLTRYKFQCLRHCLTGGEALNPDVRDKWK----- 125
Cdd:PLN02860 238 GAChVL---LPKFDAKAALQAIKQHNVTSMITVPAMMADLIsltRKSMTWKVFPSVRKILNGGGSLSSRLLPDAKklfpn 314
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755522749 126 --------------SQTGLELHEGYGQSETVVICGNSRnstIKSGS--------MGKASPPYDVQIVDEEgnvlpPGKEG 183
Cdd:PLN02860 315 aklfsaygmteacsSLTFMTLHDPTLESPKQTLQTVNQ---TKSSSvhqpqgvcVGKPAPHVELKIGLDE-----SSRVG 386
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755522749 184 NIAvrikpTRPFCFFNCYLDNPEKTAASEQGDFYI-TGDRAHMDEDGYFWFLGRNDDVINSSSYRIGPVEVESALAEHPA 262
Cdd:PLN02860 387 RIL-----TRGPHVMLGYWGQNSETASVLSNDGWLdTGDIGWIDKAGNLWLIGRSNDRIKTGGENVYPEEVEAVLSQHPG 461
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755522749 263 VLESAVVSSPDPIRGEVVKAFIVLSPAYASHDPEALTR---------ELQEHVKTVT-APYKYPRK-VAFISELPKTVSG 331
Cdd:PLN02860 462 VASVVVVGVPDSRLTEMVVACVRLRDGWIWSDNEKENAkknltlsseTLRHHCREKNlSRFKIPKLfVQWRKPFPLTTTG 541
|
330
....*....|
gi 755522749 332 KILRSKLRNQ 341
Cdd:PLN02860 542 KIRRDEVRRE 551
|
|
| PRK13383 |
PRK13383 |
acyl-CoA synthetase; Provisional |
83-338 |
7.44e-24 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 139531 [Multi-domain] Cd Length: 516 Bit Score: 102.00 E-value: 7.44e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755522749 83 LCCVP-TLFRLLVQEDLTRYK--FQCLRHCLTGGEALNPDVRDKWKSQTGLELHEGYGQSEtVVICGNSRNSTIKSG--S 157
Cdd:PRK13383 268 FTAVPvVLARILELPPRVRARnpLPQLRVVMSSGDRLDPTLGQRFMDTYGDILYNGYGSTE-VGIGALATPADLRDApeT 346
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755522749 158 MGKASPPYDVQIVDEEGNVLPPGKEGNIAV--RIKPTRpfcffncYLDNPEKTAASEQGDfyiTGDRAHMDEDGYFWFLG 235
Cdd:PRK13383 347 VGKPVAGCPVRILDRNNRPVGPRVTGRIFVggELAGTR-------YTDGGGKAVVDGMTS---TGDMGYLDNAGRLFIVG 416
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755522749 236 RNDDVINSSSYRIGPVEVESALAEHPAVLESAVVSSPDPIRGEVVKAFIVLSPAyASHDPEAltreLQEHVKTVTAPYKY 315
Cdd:PRK13383 417 REDDMIISGGENVYPRAVENALAAHPAVADNAVIGVPDERFGHRLAAFVVLHPG-SGVDAAQ----LRDYLKDRVSRFEQ 491
|
250 260
....*....|....*....|...
gi 755522749 316 PRKVAFISELPKTVSGKILRSKL 338
Cdd:PRK13383 492 PRDINIVSSIPRNPTGKVLRKEL 514
|
|
| VL_LC_FACS_like |
cd05907 |
Long-chain fatty acid CoA synthetases and Bubblegum-like very long-chain fatty acid CoA ... |
55-305 |
1.90e-23 |
|
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: 100.36 E-value: 1.90e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755522749 55 GACIFVHElprvDAKTILNTLCRFPITTLCCVPTLFR----LLVQEDLTRYK--------FQCLRHCLTGGEALNPDVrD 122
Cdd:cd05907 154 GARIYFAS----SAETLLDDLSEVRPTVFLAVPRVWEkvyaAIKVKAVPGLKrklfdlavGGRLRFAASGGAPLPAEL-L 228
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755522749 123 KWKSQTGLELHEGYGQSETVVICGNSRNSTIKSGSMGKASPPYDVQIVDEegnvlppgkeGNIAVRIKPTrpfcfFNCYL 202
Cdd:cd05907 229 HFFRALGIPVYEGYGLTETSAVVTLNPPGDNRIGTVGKPLPGVEVRIADD----------GEILVRGPNV-----MLGYY 293
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755522749 203 DNPEKTAASEQGD-FYITGDRAHMDEDGYFWFLGRNDDVI-NSSSYRIGPVEVESALAEHPAVLESAVVSSPDPirgeVV 280
Cdd:cd05907 294 KNPEATAEALDADgWLHTGDLGEIDEDGFLHITGRKKDLIiTSGGKNISPEPIENALKASPLISQAVVIGDGRP----FL 369
|
250 260
....*....|....*....|....*
gi 755522749 281 KAFIVLspayashDPEALTRELQEH 305
Cdd:cd05907 370 VALIVP-------DPEALEAWAEEH 387
|
|
| PTZ00237 |
PTZ00237 |
acetyl-CoA synthetase; Provisional |
24-340 |
1.99e-23 |
|
acetyl-CoA synthetase; Provisional
Pssm-ID: 240325 [Multi-domain] Cd Length: 647 Bit Score: 101.36 E-value: 1.99e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755522749 24 WMALTESD---IFWNTTDTGWVKAAWTLFSAWSNGACIFVHE----LPRVDAKTILNTLCRFPITTLCCVPTLFRLLVQE 96
Cdd:PTZ00237 287 WRSIIEKDiptVVFSHSSIGWVSFHGFLYGSLSLGNTFVMFEggiiKNKHIEDDLWNTIEKHKVTHTLTLPKTIRYLIKT 366
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755522749 97 D------LTRYKFQCLRHCLTGGEALNPDVRDKWKSQTGLELHEGYGQSE---TVVICGNSRNSTIKSgsMGKASPPYDV 167
Cdd:PTZ00237 367 DpeatiiRSKYDLSNLKEIWCGGEVIEESIPEYIENKLKIKSSRGYGQTEigiTYLYCYGHINIPYNA--TGVPSIFIKP 444
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755522749 168 QIVDEEGNVLPPGKEGNIAvrIKPTRPFCFFNCYLDNPE--KTAASEQGDFYITGDRAHMDEDGYFWFLGRNDDVINSSS 245
Cdd:PTZ00237 445 SILSEDGKELNVNEIGEVA--FKLPMPPSFATTFYKNDEkfKQLFSKFPGYYNSGDLGFKDENGYYTIVSRSDDQIKISG 522
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755522749 246 YRIGPVEVESALAEHPAVLESAVVSSPDPIRGEVVKAFIVLSPAYASH--DPEALTRELQEHVKTVTAPYKYPRKVAFIS 323
Cdd:PTZ00237 523 NKVQLNTIETSILKHPLVLECCSIGIYDPDCYNVPIGLLVLKQDQSNQsiDLNKLKNEINNIITQDIESLAVLRKIIIVN 602
|
330
....*....|....*..
gi 755522749 324 ELPKTVSGKILRSKLRN 340
Cdd:PTZ00237 603 QLPKTKTGKIPRQIISK 619
|
|
| PRK12467 |
PRK12467 |
peptide synthase; Provisional |
21-338 |
8.38e-23 |
|
peptide synthase; Provisional
Pssm-ID: 237108 [Multi-domain] Cd Length: 3956 Bit Score: 99.85 E-value: 8.38e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755522749 21 TRRWMALTESDIFWNTTDTGWVKAAWTLFSAWSNGACIFV--HELPRvDAKTILNTLCRFPITTLCCVPTLFRLLVQEDL 98
Cdd:PRK12467 1750 TQEAYQLSAADVVLQFTSFAFDVSVWELFWPLINGARLVIapPGAHR-DPEQLIQLIERQQVTTLHFVPSMLQQLLQMDE 1828
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755522749 99 TRYKFQCLRHCLTGGEALNPDVRDKWKSQTG-LELHEGYGQSETVV-----ICGNSRNSTIKSGSMGKASPPYDVQIVDE 172
Cdd:PRK12467 1829 QVEHPLSLRRVVCGGEALEVEALRPWLERLPdTGLFNLYGPTETAVdvthwTCRRKDLEGRDSVPIGQPIANLSTYILDA 1908
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755522749 173 EGNVLPPGKEGNIAV------RikptrpfcffnCYLDNPEKTA--------ASEQGDFYITGDRAHMDEDGYFWFLGRND 238
Cdd:PRK12467 1909 SLNPVPIGVAGELYLggvglaR-----------GYLNRPALTAerfvadpfGTVGSRLYRTGDLARYRADGVIEYLGRID 1977
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755522749 239 DVINSSSYRIGPVEVESALAEHPAVLESAVVSSpDPIRGEVVKAFIVLSPA---YASHDPEALTRELQEHVKTVTAPYKY 315
Cdd:PRK12467 1978 HQVKIRGFRIELGEIEARLREQGGVREAVVIAQ-DGANGKQLVAYVVPTDPglvDDDEAQVALRAILKNHLKASLPEYMV 2056
|
330 340
....*....|....*....|...
gi 755522749 316 PRKVAFISELPKTVSGKILRSKL 338
Cdd:PRK12467 2057 PAHLVFLARMPLTPNGKLDRKAL 2079
|
|
| PRK12467 |
PRK12467 |
peptide synthase; Provisional |
46-338 |
1.55e-22 |
|
peptide synthase; Provisional
Pssm-ID: 237108 [Multi-domain] Cd Length: 3956 Bit Score: 99.08 E-value: 1.55e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755522749 46 WTLFSAWSNGACifVHELPR---VDAKTILNTLCRFPITTLCCVPTLFRLLVQEDLTRykfQCLR-HCLT-GGEALNPDV 120
Cdd:PRK12467 713 TELFGALASGAT--LHLLPPdcaRDAEAFAALMADQGVTVLKIVPSHLQALLQASRVA---LPRPqRALVcGGEALQVDL 787
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755522749 121 RDKWKS-QTGLELHEGYGQSETVVI-----CGNSrNSTIKSGSMGKASPPYDVQIVDEEGNVLPPGKEGNIAV------R 188
Cdd:PRK12467 788 LARVRAlGPGARLINHYGPTETTVGvstyeLSDE-ERDFGNVPIGQPLANLGLYILDHYLNPVPVGVVGELYIggaglaR 866
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755522749 189 IKPTRPFCFFNCYLDNPEKTAAseqGDFYITGDRAHMDEDGYFWFLGRNDDVINSSSYRIGPVEVESALAEHPAVLESAV 268
Cdd:PRK12467 867 GYHRRPALTAERFVPDPFGADG---GRLYRTGDLARYRADGVIEYLGRMDHQVKIRGFRIELGEIEARLLAQPGVREAVV 943
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755522749 269 VSSPDPIRGEVVkAFIVLSPAYASHDPEALTRELQEHVKTVTAPYKYPRKVAFISELPKTVSGKILRSKL 338
Cdd:PRK12467 944 LAQPGDAGLQLV-AYLVPAAVADGAEHQATRDELKAQLRQVLPDYMVPAHLLLLDSLPLTPNGKLDRKAL 1012
|
|
| A_NRPS_LgrA-like |
cd17645 |
adenylation (A) domain of linear gramicidin synthetase (LgrA) and similar proteins; This ... |
45-338 |
3.18e-22 |
|
adenylation (A) domain of linear gramicidin synthetase (LgrA) and similar proteins; This family of the adenylation (A) domain of nonribosomal peptide synthases (NRPS) includes linear gramicidin synthetase (LgrA) in Brevibacillus brevis. LgrA has a formylation domain fused to the N-terminal end that formylates its substrate for linear gramicidin synthesis to proceed. This formyl group is essential for the clinically important antibacterial activity of gramicidin by enabling head-to-head gramicidin dimers to make a beta-helical pore in gram-positive bacterial membranes, allowing free passage of monovalent cations, destroying the ion gradient and killing bacteria. This family also includes bacitracin synthetase 1 (known as ATP-dependent cysteine adenylase or BA1); it activates cysteine, incorporates two D-amino acids, releases and cyclizes the mature bacitracin, an antibiotic that is a mixture of related cyclic peptides that disrupt gram positive bacteria by interfering with cell wall and peptidoglycan synthesis. Also included is surfactin synthetase which activates and polymerizes the amino acids Leu, Glu, Asp, and Val to form the antibiotic surfactin.
Pssm-ID: 341300 [Multi-domain] Cd Length: 440 Bit Score: 96.85 E-value: 3.18e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755522749 45 AWTLFSAWSNGACifVHELP---RVDAKTiLNTLCRFPITTLCCVPTLfrllVQEDLTRYKFQCLRHCLTGGEALNPDVR 121
Cdd:cd17645 160 AWEIFPHLTAGAA--LHVVPserRLDLDA-LNDYFNQEGITISFLPTG----AAEQFMQLDNQSLRVLLTGGDKLKKIER 232
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755522749 122 DKWKsqtgleLHEGYGQSE-TVVICGNSRNSTIKSGSMGKASPPYDVQIVDEEGNVLPPGKEGNIAVRIKPtrpfcFFNC 200
Cdd:cd17645 233 KGYK------LVNNYGPTEnTVVATSFEIDKPYANIPIGKPIDNTRVYILDEALQLQPIGVAGELCIAGEG-----LARG 301
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755522749 201 YLDNPEKTAASEQGD-------FYITGDRAHMDEDGYFWFLGRNDDVINSSSYRIGPVEVESALAEHPAVLESAVVSSPD 273
Cdd:cd17645 302 YLNRPELTAEKFIVHpfvpgerMYRTGDLAKFLPDGNIEFLGRLDQQVKIRGYRIEPGEIEPFLMNHPLIELAAVLAKED 381
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 755522749 274 pirGEVVKAFIvlspAYASHDPEALTRELQEHVKTVTAPYKYPRKVAFISELPKTVSGKILRSKL 338
Cdd:cd17645 382 ---ADGRKYLV----AYVTAPEEIPHEELREWLKNDLPDYMIPTYFVHLKALPLTANGKVDRKAL 439
|
|
| PRK05857 |
PRK05857 |
fatty acid--CoA ligase; |
46-338 |
5.14e-22 |
|
fatty acid--CoA ligase;
Pssm-ID: 180293 [Multi-domain] Cd Length: 540 Bit Score: 97.00 E-value: 5.14e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755522749 46 WTLFSAWSNGACIFVHElprvDAKTILNTLCRFPITTLCCVPTLFRLLVQE-DLTRYKFQCLRHCLTGG-EALNPDVRdk 123
Cdd:PRK05857 231 WILTCLMHGGLCVTGGE----NTTSLLEILTTNAVATTCLVPTLLSKLVSElKSANATVPSLRLVGYGGsRAIAADVR-- 304
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755522749 124 WKSQTGLELHEGYGQSET--VVIC---GNSRNSTIKSGSMGKASPPYDVQIVDEEG------NVLPPGKEGNIAVRiKPT 192
Cdd:PRK05857 305 FIEATGVRTAQVYGLSETgcTALClptDDGSIVKIEAGAVGRPYPGVDVYLAATDGigptapGAGPSASFGTLWIK-SPA 383
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755522749 193 RPFCFFNcyldNPEKTAASEQGDFYITGDRAHMDEDGYFWFLGRNDDVINSSSYRIGPVEVESALAEHPAVLESAVVSSP 272
Cdd:PRK05857 384 NMLGYWN----NPERTAEVLIDGWVNTGDLLERREDGFFYIKGRSSEMIICGGVNIAPDEVDRIAEGVSGVREAACYEIP 459
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 755522749 273 DPIRGEVVKAFIVLSPAYASHDPEALTRELQEHVKTVTAPYKYPRKVAFISELPKTVSGKILRSKL 338
Cdd:PRK05857 460 DEEFGALVGLAVVASAELDESAARALKHTIAARFRRESEPMARPSTIVIVTDIPRTQSGKVMRASL 525
|
|
| LC_FACL_like |
cd05914 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); The members of this family are ... |
106-335 |
1.12e-21 |
|
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: 95.59 E-value: 1.12e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755522749 106 LRHCLTGGEALNPDVRDKWKSqTGLELHEGYGQSETVVICGNSRNSTIKSGSMGKASPPYDVQIVDEEgnvlPPGKEGNI 185
Cdd:cd05914 236 IKEFVIGGAKINPDVEEFLRT-IGFPYTIGYGMTETAPIISYSPPNRIRLGSAGKVIDGVEVRIDSPD----PATGEGEI 310
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755522749 186 AVRIKptrpfcffNC---YLDNPEKTAA--SEQGDFYiTGDRAHMDEDGYFWFLGRNDDVINSSSYR-IGPVEVESALAE 259
Cdd:cd05914 311 IVRGP--------NVmkgYYKNPEATAEafDKDGWFH-TGDLGKIDAEGYLYIRGRKKEMIVLSSGKnIYPEEIEAKINN 381
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755522749 260 HPAVLESAVVsspdpIRGEVVKAFIVLSPAYA-------SHDPEALTRELQEHVKTVTAPYKYPRKVAFI-SELPKTVSG 331
Cdd:cd05914 382 MPFVLESLVV-----VQEKKLVALAYIDPDFLdvkalkqRNIIDAIKWEVRDKVNQKVPNYKKISKVKIVkEEFEKTPKG 456
|
....
gi 755522749 332 KILR 335
Cdd:cd05914 457 KIKR 460
|
|
| A_NRPS_GliP_like |
cd17653 |
nonribosomal peptide synthase GliP-like; This family includes the adenylation (A) domain of ... |
45-340 |
2.27e-21 |
|
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: 94.30 E-value: 2.27e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755522749 45 AWTLFSAWSNGAcIFVHELPRVDAKTILNTLCRFPITtlccvPTLFRLLVQEDltrykFQCLRHCLTGGEALNPDVRDKW 124
Cdd:cd17653 161 IGEIFSTLCNGG-TLVLADPSDPFAHVARTVDALMST-----PSILSTLSPQD-----FPNLKTIFLGGEAVPPSLLDRW 229
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755522749 125 KSqtGLELHEGYGQSETVVICGNSRNSTIKSGSMGKASPPYDVQIVDEEGNVLPPGKEGNIAVR-IKPTRPfcffncYLD 203
Cdd:cd17653 230 SP--GRRLYNAYGPTECTISSTMTELLPGQPVTIGKPIPNSTCYILDADLQPVPEGVVGEICISgVQVARG------YLG 301
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755522749 204 NPEKTAASEQGD-------FYITGDRAHMDEDGYFWFLGRNDDVINSSSYRIGPVEVESALAEHPAVLESAVVSspdpir 276
Cdd:cd17653 302 NPALTASKFVPDpfwpgsrMYRTGDYGRWTEDGGLEFLGREDNQVKVRGFRINLEEIEEVVLQSQPEVTQAAAI------ 375
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 755522749 277 geVVKAFIVLSPAYASHDPEALTRELQEHVktvtAPYKYPRKVAFISELPKTVSGKILRSKLRN 340
Cdd:cd17653 376 --VVNGRLVAFVTPETVDVDGLRSELAKHL----PSYAVPDRIIALDSFPLTANGKVDRKALRE 433
|
|
| FAA1 |
COG1022 |
Long-chain acyl-CoA synthetase (AMP-forming) [Lipid transport and metabolism]; |
106-305 |
3.94e-21 |
|
Long-chain acyl-CoA synthetase (AMP-forming) [Lipid transport and metabolism];
Pssm-ID: 440645 [Multi-domain] Cd Length: 603 Bit Score: 94.40 E-value: 3.94e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755522749 106 LRHCLTGGEALNPDVrDKWKSQTGLELHEGYGQSET-VVICGNsRNSTIKSGSMGKASPPYDVQIvDEEGNVLPPGkeGN 184
Cdd:COG1022 349 LRFAVSGGAALGPEL-ARFFRALGIPVLEGYGLTETsPVITVN-RPGDNRIGTVGPPLPGVEVKI-AEDGEILVRG--PN 423
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755522749 185 IavrikptrpfcfFNCYLDNPEKTAAS--EQGDFYiTGDRAHMDEDGYFWFLGRNDDVI-NSSSYRIGPVEVESALAEHP 261
Cdd:COG1022 424 V------------MKGYYKNPEATAEAfdADGWLH-TGDIGELDEDGFLRITGRKKDLIvTSGGKNVAPQPIENALKASP 490
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 755522749 262 AVLESAVVsspdpirGE---VVKAFIVLspayashDPEALTRELQEH 305
Cdd:COG1022 491 LIEQAVVV-------GDgrpFLAALIVP-------DFEALGEWAEEN 523
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
25-338 |
6.40e-21 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 94.25 E-value: 6.40e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755522749 25 MALTESDIFWNTTDTGWVKAAWTLFSAWSNGACIFVHELPRVDAKTILNTLCRFP-ITTLCCVPTLFRLLVQEDLTRyKF 103
Cdd:PRK12316 3232 YGLGVGDRVLQFTTFSFDVFVEELFWPLMSGARVVLAGPEDWRDPALLVELINSEgVDVLHAYPSMLQAFLEEEDAH-RC 3310
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755522749 104 QCLRHCLTGGEALNPDVRDKWKSqtGLELHEGYGQSETVVICGNSRNSTIKSGS--MGKASPPYDVQIVDEEGNVLPPGK 181
Cdd:PRK12316 3311 TSLKRIVCGGEALPADLQQQVFA--GLPLYNLYGPTEATITVTHWQCVEEGKDAvpIGRPIANRACYILDGSLEPVPVGA 3388
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755522749 182 EGNIAV------RIKPTRPFCFFNCYLDNPektaASEQGDFYITGDRAHMDEDGYFWFLGRNDDVINSSSYRIGPVEVES 255
Cdd:PRK12316 3389 LGELYLggeglaRGYHNRPGLTAERFVPDP----FVPGERLYRTGDLARYRADGVIEYIGRVDHQVKIRGFRIELGEIEA 3464
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755522749 256 ALAEHPAVLESAVVSspdpIRGEVVKAFIVLSPAYAshdpeALTRELQEHVKTVTAPYKYPRKVAFISELPKTVSGKILR 335
Cdd:PRK12316 3465 RLLEHPWVREAVVLA----VDGRQLVAYVVPEDEAG-----DLREALKAHLKASLPEYMVPAHLLFLERMPLTPNGKLDR 3535
|
...
gi 755522749 336 SKL 338
Cdd:PRK12316 3536 KAL 3538
|
|
| A_NRPS_TlmIV_like |
cd12114 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including ... |
44-338 |
7.90e-21 |
|
The adenylation domain of nonribosomal peptide synthetases (NRPS), including Streptoalloteichus tallysomycin biosynthesis genes; The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions. This family includes the TLM biosynthetic gene cluster from Streptoalloteichus that consists of nine NRPS genes; the N-terminal module of TlmVI (NRPS-5) and the starter module of BlmVI (NRPS-5) are comprised of the acyl CoA ligase (AL) and acyl carrier protein (ACP)-like domains, which are thought to be involved in the biosynthesis of the beta-aminoalaninamide moiety.
Pssm-ID: 341279 [Multi-domain] Cd Length: 477 Bit Score: 93.10 E-value: 7.90e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755522749 44 AAWTLFSAWSNGACI-FVHELPRVDAKTILNTLCRFPITTLCCVPTLFRLLVQEDLTRYKFQC-LRHCLTGGEALNPDVR 121
Cdd:cd12114 181 SVYDIFGALSAGATLvLPDEARRRDPAHWAELIERHGVTLWNSVPALLEMLLDVLEAAQALLPsLRLVLLSGDWIPLDLP 260
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755522749 122 DKWKSQT-GLELHEGYGQSETVVIcgnSRNSTIKSGSMGKASPPYDV-------QIVDEEGNVLPPGKEGNI-------A 186
Cdd:cd12114 261 ARLRALApDARLISLGGATEASIW---SIYHPIDEVPPDWRSIPYGRplanqryRVLDPRGRDCPDWVPGELwiggrgvA 337
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755522749 187 vrikptrpfcffNCYLDNPEKTAAS-----EQGDFYITGDRAHMDEDGYFWFLGRNDDVINSSSYRIGPVEVESALAEHP 261
Cdd:cd12114 338 ------------LGYLGDPELTAARfvthpDGERLYRTGDLGRYRPDGTLEFLGRRDGQVKVRGYRIELGEIEAALQAHP 405
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 755522749 262 AVLESAVVSSPDPiRGEVVKAFIVLSPAYASHDPEALTRELQEHVktvtAPYKYPRKVAFISELPKTVSGKILRSKL 338
Cdd:cd12114 406 GVARAVVVVLGDP-GGKRLAAFVVPDNDGTPIAPDALRAFLAQTL----PAYMIPSRVIALEALPLTANGKVDRAAL 477
|
|
| A_NRPS_ApnA-like |
cd17644 |
similar to adenylation domain of anabaenopeptin synthetase (ApnA); This family of the ... |
44-338 |
8.54e-21 |
|
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: 92.88 E-value: 8.54e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755522749 44 AAWTLFSAWSNGAC-IFVHELPRVDAKTILNTLCRFPITTLCCVPTLFRLLVQEDL--TRYKFQCLRHCLTGGEALNPDV 120
Cdd:cd17644 161 AAEEIYVTLLSGATlVLRPEEMRSSLEDFVQYIQQWQLTVLSLPPAYWHLLVLELLlsTIDLPSSLRLVIVGGEAVQPEL 240
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755522749 121 RDKWKSQTG--LELHEGYGQSE---TVVICGNSRNST--IKSGSMGKASPPYDVQIVDEEGNVLPPGKEGNIavRIKPTR 193
Cdd:cd17644 241 VRQWQKNVGnfIQLINVYGPTEatiAATVCRLTQLTErnITSVPIGRPIANTQVYILDENLQPVPVGVPGEL--HIGGVG 318
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755522749 194 pfcFFNCYLDNPEKTA---------ASEQGDFYITGDRAHMDEDGYFWFLGRNDDVINSSSYRIGPVEVESALAEHPAVL 264
Cdd:cd17644 319 ---LARGYLNRPELTAekfishpfnSSESERLYKTGDLARYLPDGNIEYLGRIDNQVKIRGFRIELGEIEAVLSQHNDVK 395
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 755522749 265 ESAVVSSPDPIRGEVVKAFIVlsPAYashDPEALTRELQEHVKTVTAPYKYPRKVAFISELPKTVSGKILRSKL 338
Cdd:cd17644 396 TAVVIVREDQPGNKRLVAYIV--PHY---EESPSTVELRQFLKAKLPDYMIPSAFVVLEELPLTPNGKIDRRAL 464
|
|
| A_NRPS_ProA |
cd17656 |
gramicidin S synthase 2, also known as ATP-dependent proline adenylase; This family of the ... |
48-338 |
2.47e-20 |
|
gramicidin S synthase 2, also known as ATP-dependent proline adenylase; This family of the adenylation (A) domain of nonribosomal peptide synthases (NRPS) contains gramicidin S synthase 2 (also known as ATP-dependent proline adenylase or proline activase or ProA). ProA is a multifunctional enzyme involved in synthesis of the cyclic peptide antibiotic gramicidin S and able to activate and polymerize the amino acids proline, valine, ornithine and leucine. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.
Pssm-ID: 341311 [Multi-domain] Cd Length: 479 Bit Score: 91.38 E-value: 2.47e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755522749 48 LFSAWSNGACIF-VHELPRVDAKTILNTLCRFPITTLCCVPTLFRLLVQE-DLTRYKFQCLRHCLTGGEAL--NPDVRDK 123
Cdd:cd17656 187 IFSTLLSGGTLYiIREETKRDVEQLFDLVKRHNIEVVFLPVAFLKFIFSErEFINRFPTCVKHIITAGEQLviTNEFKEM 266
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755522749 124 WKSQtGLELHEGYGQSETVVICGNSRNSTIKSGSM---GKASPPYDVQIVDEEGNVLPPGKEGNIAVR-IKPTRPfcffn 199
Cdd:cd17656 267 LHEH-NVHLHNHYGPSETHVVTTYTINPEAEIPELppiGKPISNTWIYILDQEQQLQPQGIVGELYISgASVARG----- 340
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755522749 200 cYLDNPEKTAASEQGD-------FYITGDRAHMDEDGYFWFLGRNDDVINSSSYRIGPVEVESALAEHPAVLESAVVSSP 272
Cdd:cd17656 341 -YLNRQELTAEKFFPDpfdpnerMYRTGDLARYLPDGNIEFLGRADHQVKIRGYRIELGEIEAQLLNHPGVSEAVVLDKA 419
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 755522749 273 DPIRGEVVKAFIVLSPAYAshdpealTRELQEHVKTVTAPYKYPRKVAFISELPKTVSGKILRSKL 338
Cdd:cd17656 420 DDKGEKYLCAYFVMEQELN-------ISQLREYLAKQLPEYMIPSFFVPLDQLPLTPNGKVDRKAL 478
|
|
| PRK07008 |
PRK07008 |
long-chain-fatty-acid--CoA ligase; Validated |
45-341 |
4.38e-20 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 235908 [Multi-domain] Cd Length: 539 Bit Score: 90.92 E-value: 4.38e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755522749 45 AWTL-FSAWSNGaCIFVHELPRVDAKTILNTLCRFPITTLCCVPTLFRLLVQE-DLTRYKFQCLRHCLTGGEALNPDVRD 122
Cdd:PRK07008 233 AWGLpYSAPLTG-AKLVLPGPDLDGKSLYELIEAERVTFSAGVPTVWLGLLNHmREAGLRFSTLRRTVIGGSACPPAMIR 311
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755522749 123 KWKSQTGLELHEGYGQSE-----TVVICGNSRNSTIKSGSM------GKASPPYDVQIVDEEGNVLP-PGKE-GNIAVRi 189
Cdd:PRK07008 312 TFEDEYGVEVIHAWGMTEmsplgTLCKLKWKHSQLPLDEQRkllekqGRVIYGVDMKIVGDDGRELPwDGKAfGDLQVR- 390
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755522749 190 kptRPFCffncyLDNPEKTAASEQGD-FYITGDRAHMDEDGYFWFLGRNDDVINSSSYRIGPVEVESALAEHPAVLESAV 268
Cdd:PRK07008 391 ---GPWV-----IDRYFRGDASPLVDgWFPTGDVATIDADGFMQITDRSKDVIKSGGEWISSIDIENVAVAHPAVAEAAC 462
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 755522749 269 VSSPDPIRGEVVKAFIVLSPAYashdpeALTR-ELQEHVKTVTAPYKYPRKVAFISELPKTVSGKILRSKLRNQ 341
Cdd:PRK07008 463 IACAHPKWDERPLLVVVKRPGA------EVTReELLAFYEGKVAKWWIPDDVVFVDAIPHTATGKLQKLKLREQ 530
|
|
| PRK05691 |
PRK05691 |
peptide synthase; Validated |
24-343 |
6.29e-20 |
|
peptide synthase; Validated
Pssm-ID: 235564 [Multi-domain] Cd Length: 4334 Bit Score: 91.38 E-value: 6.29e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755522749 24 WM----ALTESDIFWNTTDTGWVKAAWTLFSAWSNGaCIFVHELP--RVDAKTILNTLCRFPITTLCCVPTLFRLLVQED 97
Cdd:PRK05691 1304 WMqatyALDDSDVLMQKAPISFDVSVWECFWPLITG-CRLVLAGPgeHRDPQRIAELVQQYGVTTLHFVPPLLQLFIDEP 1382
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755522749 98 LTRykfQC--LRHCLTGGEALNPDVRDKWKSQ-TGLELHEGYGQSETVVicgnsrNSTIK--SGSMGKASP---PYD--- 166
Cdd:PRK05691 1383 LAA---ACtsLRRLFSGGEALPAELRNRVLQRlPQVQLHNRYGPTETAI------NVTHWqcQAEDGERSPigrPLGnvl 1453
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755522749 167 VQIVDEEGNVLPPGKEGNIAVR-IKPTRPfcffncYLDNPEKTAA-------SEQGD-FYITGDRAHMDEDGYFWFLGRN 237
Cdd:PRK05691 1454 CRVLDAELNLLPPGVAGELCIGgAGLARG------YLGRPALTAErfvpdplGEDGArLYRTGDRARWNADGALEYLGRL 1527
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755522749 238 DDVINSSSYRIGPVEVESALAEHPAVLESAVVsspdpIRGEVVKAFIV---LSPAYASHDPEALTRELQEHVKTvtapYK 314
Cdd:PRK05691 1528 DQQVKLRGFRVEPEEIQARLLAQPGVAQAAVL-----VREGAAGAQLVgyyTGEAGQEAEAERLKAALAAELPE----YM 1598
|
330 340
....*....|....*....|....*....
gi 755522749 315 YPRKVAFISELPKTVSGKILRSKLRNQEW 343
Cdd:PRK05691 1599 VPAQLIRLDQMPLGPSGKLDRRALPEPVW 1627
|
|
| A_NRPS_TubE_like |
cd05906 |
The adenylation domain (A domain) of a family of nonribosomal peptide synthetases (NRPSs) ... |
100-341 |
3.42e-19 |
|
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: 88.49 E-value: 3.42e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755522749 100 RYKFQCLRHCLTGGEALNpdvrdkwkSQTG---LELHE-----------GYGQSETV-VICGNSRNSTIKSG------SM 158
Cdd:cd05906 285 TWDLSSLRYLVNAGEAVV--------AKTIrrlLRLLEpyglppdairpAFGMTETCsGVIYSRSFPTYDHSqalefvSL 356
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755522749 159 GKASPPYDVQIVDEEGNVLPPGKEGNIAVRiKPTRpfcfFNCYLDNPEKTAASEQGD-FYITGDRAHMDeDGYFWFLGRN 237
Cdd:cd05906 357 GRPIPGVSMRIVDDEGQLLPEGEVGRLQVR-GPVV----TKGYYNNPEANAEAFTEDgWFRTGDLGFLD-NGNLTITGRT 430
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755522749 238 DDVINSSSYRIGPVEVESALAEHPAVLES--AVVSSPDPIRGEVVKAfIVLSPAYASHDP-EALTRELQEHVK---TVTA 311
Cdd:cd05906 431 KDTIIVNGVNYYSHEIEAAVEEVPGVEPSftAAFAVRDPGAETEELA-IFFVPEYDLQDAlSETLRAIRSVVSrevGVSP 509
|
250 260 270
....*....|....*....|....*....|.
gi 755522749 312 PYKYP-RKvafiSELPKTVSGKILRSKLRNQ 341
Cdd:cd05906 510 AYLIPlPK----EEIPKTSLGKIQRSKLKAA 536
|
|
| PRK12467 |
PRK12467 |
peptide synthase; Provisional |
44-338 |
4.57e-19 |
|
peptide synthase; Provisional
Pssm-ID: 237108 [Multi-domain] Cd Length: 3956 Bit Score: 88.68 E-value: 4.57e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755522749 44 AAWTLFSAWSNGACIFVHELPRVDAKTILNTLCRFPITTLCCVPTLFRLLVQeDLTRYKFQCLRHCLTGGEALNPDVRDK 123
Cdd:PRK12467 3292 AQERFLWTLICGGCLVVRDNDLWDPEELWQAIHAHRISIACFPPAYLQQFAE-DAGGADCASLDIYVFGGEAVPPAAFEQ 3370
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755522749 124 WKS---QTGLelHEGYGQSETVVI-----CGNSRNSTIKSGSMGKASPPYDVQIVDEEGNVLPPGKEGNIAV------RI 189
Cdd:PRK12467 3371 VKRklkPRGL--TNGYGPTEAVVTvtlwkCGGDAVCEAPYAPIGRPVAGRSIYVLDGQLNPVPVGVAGELYIggvglaRG 3448
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755522749 190 KPTRPFCFFNCYLDNPEKTAAseqGDFYITGDRAHMDEDGYFWFLGRNDDVINSSSYRIGPVEVESALAEHPAVLESAVV 269
Cdd:PRK12467 3449 YHQRPSLTAERFVADPFSGSG---GRLYRTGDLARYRADGVIEYLGRIDHQVKIRGFRIELGEIEARLLQHPSVREAVVL 3525
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755522749 270 SSpDPIRGEVVKAFIVLspayasHDP-EALTRELQEHVKTVTAPYKYPRKVAFISELPKTVSGKILRSKL 338
Cdd:PRK12467 3526 AR-DGAGGKQLVAYVVP------ADPqGDWRETLRDHLAASLPDYMVPAQLLVLAAMPLGPNGKVDRKAL 3588
|
|
| PRK07445 |
PRK07445 |
O-succinylbenzoic acid--CoA ligase; Reviewed |
86-339 |
1.14e-18 |
|
O-succinylbenzoic acid--CoA ligase; Reviewed
Pssm-ID: 236019 [Multi-domain] Cd Length: 452 Bit Score: 86.59 E-value: 1.14e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755522749 86 VPTLFRLLVQEDLTRykFQCLRHCLTGGEALNPDVRDKWKsQTGLELHEGYGQSETVvicgnSRNSTIK-------SGSM 158
Cdd:PRK07445 214 VPTQLQRLLQLRPQW--LAQFRTILLGGAPAWPSLLEQAR-QLQLRLAPTYGMTETA-----SQIATLKpddflagNNSS 285
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755522749 159 GKASPPYDVQIVdeegnvlpPGKEGNIAVRIKPTrpfcFFNCYldnPEKTAASEqgdFYITGDRAHMDEDGYFWFLGRND 238
Cdd:PRK07445 286 GQVLPHAQITIP--------ANQTGNITIQAQSL----ALGYY---PQILDSQG---IFETDDLGYLDAQGYLHILGRNS 347
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755522749 239 DVINSSSYRIGPVEVESALAEHPAVLESAVVSSPDPIRGEVVKAFIVlsPAYASHDPEaltrELQEHVKTVTAPYKYPRK 318
Cdd:PRK07445 348 QKIITGGENVYPAEVEAAILATGLVQDVCVLGLPDPHWGEVVTAIYV--PKDPSISLE----ELKTAIKDQLSPFKQPKH 421
|
250 260
....*....|....*....|.
gi 755522749 319 VAFISELPKTVSGKILRSKLR 339
Cdd:PRK07445 422 WIPVPQLPRNPQGKINRQQLQ 442
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
44-338 |
1.40e-18 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 87.32 E-value: 1.40e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755522749 44 AAWTLFSAWSNGACIFVHELPRVDAKTILNTLCRFPITTLCCVPTLFRLLVQEDLTRYKFQCLRHCLTGGEALNPDVRDK 123
Cdd:PRK12316 2201 AHEQWFHPLLNGARVLIRDDELWDPEQLYDEMERHGVTILDFPPVYLQQLAEHAERDGRPPAVRVYCFGGEAVPAASLRL 2280
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755522749 124 WKSQTGLE-LHEGYGQSETVVI-----CGNSRNSTIKSGSMGKASPPYDVQIVDEEGNVLPPGKEGNIAVRIKptrpfCF 197
Cdd:PRK12316 2281 AWEALRPVyLFNGYGPTEAVVTpllwkCRPQDPCGAAYVPIGRALGNRRAYILDADLNLLAPGMAGELYLGGE-----GL 2355
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755522749 198 FNCYLDNPEKTA--------ASEQGDFYITGDRAHMDEDGYFWFLGRNDDVINSSSYRIGPVEVESALAEHPAVLESAVV 269
Cdd:PRK12316 2356 ARGYLNRPGLTAerfvpdpfSASGERLYRTGDLARYRADGVVEYLGRIDHQVKIRGFRIELGEIEARLQAHPAVREAVVV 2435
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 755522749 270 SSpDPIRGEVVKAFIVlsPAYASHDpeaLTRELQEHVKTVTAPYKYPRKVAFISELPKTVSGKILRSKL 338
Cdd:PRK12316 2436 AQ-DGASGKQLVAYVV--PDDAAED---LLAELRAWLAARLPAYMVPAHWVVLERLPLNPNGKLDRKAL 2498
|
|
| A_NRPS_acs4 |
cd17654 |
acyl-CoA synthetase family member 4; This family of the adenylation (A) domain of nonribosomal ... |
48-338 |
1.15e-17 |
|
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: 83.68 E-value: 1.15e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755522749 48 LFSAWSNGACIFV--HELPRVDAKTILNTLCRFPITTLCCVPTLFRLLVQEDLTRY---KFQCLRHCLTGGEALNPDVRD 122
Cdd:cd17654 177 IFLSLSSGATLLIvpTSVKVLPSKLADILFKRHRITVLQATPTLFRRFGSQSIKSTvlsATSSLRVLALGGEPFPSLVIL 256
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755522749 123 KWKSQTGLELH--EGYGQSETvviCGNSRNSTIKSGSMGK--ASPPYD--VQIVDEEGNvlppgkEGNIAVRIKPTRPFC 196
Cdd:cd17654 257 SSWRGKGNRTRifNIYGITEV---SCWALAYKVPEEDSPVqlGSPLLGtvIEVRDQNGS------EGTGQVFLGGLNRVC 327
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755522749 197 FFNCYLDNPEktaaseqGDFYITGDRAHMdEDGYFWFLGRNDDVINSSSYRIGPVEVESALAEHPAVLESAVVSSPDpir 276
Cdd:cd17654 328 ILDDEVTVPK-------GTMRATGDFVTV-KDGELFFLGRKDSQIKRRGKRINLDLIQQVIESCLGVESCAVTLSDQ--- 396
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 755522749 277 gEVVKAFIVlspayashDPEALTRELQEHVKTVTAPYKYPRKVAFISELPKTVSGKILRSKL 338
Cdd:cd17654 397 -QRLIAFIV--------GESSSSRIHKELQLTLLSSHAIPDTFVQIDKLPLTSHGKVDKSEL 449
|
|
| PRK04813 |
PRK04813 |
D-alanine--poly(phosphoribitol) ligase subunit DltA; |
159-338 |
1.41e-17 |
|
D-alanine--poly(phosphoribitol) ligase subunit DltA;
Pssm-ID: 235313 [Multi-domain] Cd Length: 503 Bit Score: 83.41 E-value: 1.41e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755522749 159 GKASPPYDVQIVDEEGNVLPPGKEGNIAVrIKPtrpfCFFNCYLDNPEKTAA---SEQGD-FYITGDRAHMDeDGYFWFL 234
Cdd:PRK04813 321 GYAKPDSPLLIIDEEGTKLPDGEQGEIVI-SGP----SVSKGYLNNPEKTAEaffTFDGQpAYHTGDAGYLE-DGLLFYQ 394
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755522749 235 GRNDDVINSSSYRIGPVEVESALAEHPAVlESAVVSspdPI-RGEVVK---AFIVLSPayasHDPE---ALTRELQEHVK 307
Cdd:PRK04813 395 GRIDFQIKLNGYRIELEEIEQNLRQSSYV-ESAVVV---PYnKDHKVQyliAYVVPKE----EDFErefELTKAIKKELK 466
|
170 180 190
....*....|....*....|....*....|.
gi 755522749 308 TVTAPYKYPRKVAFISELPKTVSGKILRSKL 338
Cdd:PRK04813 467 ERLMEYMIPRKFIYRDSLPLTPNGKIDRKAL 497
|
|
| LC_FACS_bac |
cd05932 |
Bacterial long-chain fatty acid CoA synthetase (LC-FACS), including Marinobacter ... |
104-322 |
1.43e-17 |
|
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: 83.29 E-value: 1.43e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755522749 104 QClRHCLTGGEALNPDVRDkWKSQTGLELHEGYGQSETVVICGNSRNSTIKSGSMGKASPPYDVQIVDEegnvlppgkeG 183
Cdd:cd05932 276 QC-RLAGCGSAPVPPALLE-WYRSLGLNILEAYGMTENFAYSHLNYPGRDKIGTVGNAGPGVEVRISED----------G 343
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755522749 184 NIAVRIKPTrpfcfFNCYLDNPEKTAASEQGD-FYITGDRAHMDEDGYFWFLGRNDDVINSSSYR-IGPVEVESALAEHP 261
Cdd:cd05932 344 EILVRSPAL-----MMGYYKDPEATAEAFTADgFLRTGDKGELDADGNLTITGRVKDIFKTSKGKyVAPAPIENKLAEHD 418
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 755522749 262 AVLESAVVSS--PDPIRGEVVKAFIVLSPAYAshDPEALTRELQEHVKTVTAPYKYPRKVAFI 322
Cdd:cd05932 419 RVEMVCVIGSglPAPLALVVLSEEARLRADAF--ARAELEASLRAHLARVNSTLDSHEQLAGI 479
|
|
| PRK06018 |
PRK06018 |
putative acyl-CoA synthetase; Provisional |
45-341 |
2.44e-17 |
|
putative acyl-CoA synthetase; Provisional
Pssm-ID: 235673 [Multi-domain] Cd Length: 542 Bit Score: 82.88 E-value: 2.44e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755522749 45 AWTL-FSAWSNGACIfVHELPRVDAKTILNTLCRFPITTLCCVPTLFRLLVQE-DLTRYKFQCLRHCLTGGEALnPDVRD 122
Cdd:PRK06018 234 SWGIaFSAPSMGTKL-VMPGAKLDGASVYELLDTEKVTFTAGVPTVWLMLLQYmEKEGLKLPHLKMVVCGGSAM-PRSMI 311
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755522749 123 KWKSQTGLELHEGYGQSETVVIcgnsrnstiksGSMGKASPPYD----------------------VQIVDEEGNVLP-P 179
Cdd:PRK06018 312 KAFEDMGVEVRHAWGMTEMSPL-----------GTLAALKPPFSklpgdarldvlqkqgyppfgveMKITDDAGKELPwD 380
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755522749 180 GKE-GNIAVRiKPTRPFCFFNCyldnpEKTAASEQGdFYITGDRAHMDEDGYFWFLGRNDDVINSSSYRIGPVEVESALA 258
Cdd:PRK06018 381 GKTfGRLKVR-GPAVAAAYYRV-----DGEILDDDG-FFDTGDVATIDAYGYMRITDRSKDVIKSGGEWISSIDLENLAV 453
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755522749 259 EHPAVLESAVVSSPDPIRGEVVKAFIVLSPayashDPEALTRELQEHVKTVTAPYKYPRKVAFISELPKTVSGKILRSKL 338
Cdd:PRK06018 454 GHPKVAEAAVIGVYHPKWDERPLLIVQLKP-----GETATREEILKYMDGKIAKWWMPDDVAFVDAIPHTATGKILKTAL 528
|
...
gi 755522749 339 RNQ 341
Cdd:PRK06018 529 REQ 531
|
|
| entF |
PRK10252 |
enterobactin non-ribosomal peptide synthetase EntF; |
24-338 |
2.76e-17 |
|
enterobactin non-ribosomal peptide synthetase EntF;
Pssm-ID: 236668 [Multi-domain] Cd Length: 1296 Bit Score: 83.17 E-value: 2.76e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755522749 24 WM----ALTESDIFWNTTDTGWVKAAWTLFSAWSNGACIFV-----HELPRVDAKTIlntlCRFPITTLCCVPTLFRLLV 94
Cdd:PRK10252 629 WMqnhyPLTADDVVLQKTPCSFDVSVWEFFWPFIAGAKLVMaepeaHRDPLAMQQFF----AEYGVTTTHFVPSMLAAFV 704
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755522749 95 QE---DLTRYKFQCLRHCLTGGEALNPDVRDKWKSQTGLELHEGYGQSETVV------ICGNSRNSTiKSGSMGKASPPY 165
Cdd:PRK10252 705 ASltpEGARQSCASLRQVFCSGEALPADLCREWQQLTGAPLHNLYGPTEAAVdvswypAFGEELAAV-RGSSVPIGYPVW 783
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755522749 166 DVQ--IVDEEGNVLPPGKEGNIAVR-IKPTRPfcffncYLDNPEKTA-------ASEQGDFYITGDRAHMDEDGYFWFLG 235
Cdd:PRK10252 784 NTGlrILDARMRPVPPGVAGDLYLTgIQLAQG------YLGRPDLTAsrfiadpFAPGERMYRTGDVARWLDDGAVEYLG 857
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755522749 236 RNDDVINSSSYRIGPVEVESALAEHP----AVLESAVVSSPDPIRGEVVK--AFIVlspayaSHDPEALTRE-LQEHVKT 308
Cdd:PRK10252 858 RSDDQLKIRGQRIELGEIDRAMQALPdveqAVTHACVINQAAATGGDARQlvGYLV------SQSGLPLDTSaLQAQLRE 931
|
330 340 350
....*....|....*....|....*....|
gi 755522749 309 VTAPYKYPRKVAFISELPKTVSGKILRSKL 338
Cdd:PRK10252 932 RLPPHMVPVVLLQLDQLPLSANGKLDRKAL 961
|
|
| PRK08308 |
PRK08308 |
acyl-CoA synthetase; Validated |
69-335 |
3.57e-17 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236231 [Multi-domain] Cd Length: 414 Bit Score: 82.01 E-value: 3.57e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755522749 69 KTILNTLCRFPITTLCCVPTLFRLLVQedLTRYKFQcLRHCLTGGEALNPDVRDKWKSQTgLELHEGYGQSET--VVICG 146
Cdd:PRK08308 180 KFALNILRNTPQHILYAVPLMLHILGR--LLPGTFQ-FHAVMTSGTPLPEAWFYKLRERT-TYMMQQYGCSEAgcVSICP 255
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755522749 147 NSRNStiksGSMGKASPPYDVQIVDEEGNvlpPGKegnIAVRIKptrpfcffncyldnpEKTAAseqgdfyiTGDRAHMD 226
Cdd:PRK08308 256 DMKSH----LDLGNPLPHVSVSAGSDENA---PEE---IVVKMG---------------DKEIF--------TKDLGYKS 302
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755522749 227 EDGYFWFLGRNDDVINSSSYRIGPVEVESALAEHPAVLESAVVSSPDPIRGEVVKAfivlspAYASH---DPEALTRELQ 303
Cdd:PRK08308 303 ERGTLHFMGRMDDVINVSGLNVYPIEVEDVMLRLPGVQEAVVYRGKDPVAGERVKA------KVISHeeiDPVQLREWCI 376
|
250 260 270
....*....|....*....|....*....|..
gi 755522749 304 EHVktvtAPYKYPRKVAFISELPKTVSGKILR 335
Cdd:PRK08308 377 QHL----APYQVPHEIESVTEIPKNANGKVSR 404
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
46-338 |
9.82e-17 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 81.93 E-value: 9.82e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755522749 46 WTLFSAWSNGACIFV--HELPRvDAKTILNTLCRFPITTLCCVPTLFRLLVQEDLTRykfQC--LRHCLTGGEALNPDVR 121
Cdd:PRK12316 712 WEFFWPLMSGARLVVaaPGDHR-DPAKLVELINREGVDTLHFVPSMLQAFLQDEDVA---SCtsLRRIVCSGEALPADAQ 787
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755522749 122 DKW---KSQTGLELHegYGQSETV--VICGNSRNSTIKSGSMGKASPPYDVQIVDEEGNVLPPGKEGNIAVRIKP-TRPf 195
Cdd:PRK12316 788 EQVfakLPQAGLYNL--YGPTEAAidVTHWTCVEEGGDSVPIGRPIANLACYILDANLEPVPVGVLGELYLAGRGlARG- 864
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755522749 196 cffncYLDNPEKTA----ASEQGD---FYITGDRAHMDEDGYFWFLGRNDDVINSSSYRIGPVEVESALAEHPAVLESAV 268
Cdd:PRK12316 865 -----YHGRPGLTAerfvPSPFVAgerMYRTGDLARYRADGVIEYAGRIDHQVKLRGLRIELGEIEARLLEHPWVREAAV 939
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 755522749 269 VSspdpIRGEVVKAFIVLSpayashDPEALTRE-LQEHVKTVTAPYKYPRKVAFISELPKTVSGKILRSKL 338
Cdd:PRK12316 940 LA----VDGKQLVGYVVLE------SEGGDWREaLKAHLAASLPEYMVPAQWLALERLPLTPNGKLDRKAL 1000
|
|
| PLN03051 |
PLN03051 |
acyl-activating enzyme; Provisional |
25-341 |
1.63e-16 |
|
acyl-activating enzyme; Provisional
Pssm-ID: 215552 [Multi-domain] Cd Length: 499 Bit Score: 80.25 E-value: 1.63e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755522749 25 MALTESDIFWNTTDTGWVKAAWTLFSAWSNGACIFVHElprvdAKTILNTLCRF----PITTLCCVPTLFR--------L 92
Cdd:PLN03051 155 MDIQPGDVVCWPTNLGWMMGPWLLYSAFLNGATLALYG-----GAPLGRGFGKFvqdaGVTVLGLVPSIVKawrhtgafA 229
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755522749 93 LVQEDLTRYKFQClrhclTGGEALNPDvRDKWKSQT------------GLELHEGYGQSETVVICGNSrnsTIKSGSMGK 160
Cdd:PLN03051 230 MEGLDWSKLRVFA-----STGEASAVD-DVLWLSSVrgyykpvieycgGTELASGYISSTLLQPQAPG---AFSTASLGT 300
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755522749 161 AsppydVQIVDEEGNVLPPGKE--GNIAVRIkptrPFCFFNCYLDNPEKTAASEQG--DFYITGD--RAHMDE-----DG 229
Cdd:PLN03051 301 R-----FVLLNDNGVPYPDDQPcvGEVALAP----PMLGASDRLLNADHDKVYYKGmpMYGSKGMplRRHGDImkrtpGG 371
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755522749 230 YFWFLGRNDDVINSSSYRIGPVEVESALAE-HPAVLESAVVSSPDPIRGE----VVKAFIVLSPAYASHDPEALTRELQE 304
Cdd:PLN03051 372 YFCVQGRADDTMNLGGIKTSSVEIERACDRaVAGIAETAAVGVAPPDGGPellvIFLVLGEEKKGFDQARPEALQKKFQE 451
|
330 340 350
....*....|....*....|....*....|....*..
gi 755522749 305 HVKTVTAPYKYPRKVAFISELPKTVSGKILRSKLRNQ 341
Cdd:PLN03051 452 AIQTNLNPLFKVSRVKIVPELPRNASNKLLRRVLRDQ 488
|
|
| A_NRPS_ACVS-like |
cd17648 |
N-(5-amino-5-carboxypentanoyl)-L-cysteinyl-D-valine synthase; This family contains ACV ... |
106-333 |
1.66e-16 |
|
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: 80.14 E-value: 1.66e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755522749 106 LRHCLTGGEALNPDVRDKWKSQTGLELHEGYGQSETVVICGNSRNSTI--KSGSMGKASPPYDVQIVDEEGNVLPPGKEG 183
Cdd:cd17648 209 LKRVDAAGEEFTAPVFEKLRSRFAGLIINAYGPTETTVTNHKRFFPGDqrFDKSLGRPVRNTKCYVLNDAMKRVPVGAVG 288
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755522749 184 NIAVRikptrPFCFFNCYLDNPEKTA--------ASEQ-------GDFYITGDRAHMDEDGYFWFLGRNDDVINSSSYRI 248
Cdd:cd17648 289 ELYLG-----GDGVARGYLNRPELTAerflpnpfQTEQerargrnARLYKTGDLVRWLPSGELEYLGRNDFQVKIRGQRI 363
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755522749 249 GPVEVESALAEHPAVLESAVVSSPDP-IRGEVVKAFIVlspAYASHDPEALTR-ELQEHVKTVTAPYKYPRKVAFISELP 326
Cdd:cd17648 364 EPGEVEAALASYPGVRECAVVAKEDAsQAQSRIQKYLV---GYYLPEPGHVPEsDLLSFLRAKLPRYMVPARLVRLEGIP 440
|
....*..
gi 755522749 327 KTVSGKI 333
Cdd:cd17648 441 VTINGKL 447
|
|
| ttLC_FACS_like |
cd05915 |
Fatty acyl-CoA synthetases similar to LC-FACS from Thermus thermophiles; This family includes ... |
187-339 |
4.20e-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. Fatty acyl-CoA synthetases are responsible for fatty acid degradation as well as physiological regulation of cellular functions via the production of fatty acyl-CoA esters. The fatty acyl-CoA synthetase from Thermus thermophiles in this family has been shown to catalyze the long-chain fatty acid, myristoyl acid, while another member in this family, the AlkK protein identified in Pseudomonas oleovorans, targets medium chain fatty acids. This family also includes an uncharacterized subgroup of FACS.
Pssm-ID: 213283 [Multi-domain] Cd Length: 509 Bit Score: 79.01 E-value: 4.20e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755522749 187 VRIKPTRPFCFFNCYLDNPEKTAASE-QGDFYITGDRAHMDEDGYFWFLGRNDDVINSSSYRIGPVEVESALAEHPAVLE 265
Cdd:cd05915 360 LGEVQLKGPWITGGYYGNEEATRSALtPDGFFRTGDIAVWDEEGYVEIKDRLKDLIKSGGEWISSVDLENALMGHPKVKE 439
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 755522749 266 SAVVSSPDPIRGEVVKAFIVLSPAyashdpEALTRELQEHVKTVTAPYKY-PRKVAFISELPKTVSGKILRSKLR 339
Cdd:cd05915 440 AAVVAIPHPKWQERPLAVVVPRGE------KPTPEELNEHLLKAGFAKWQlPDAYVFAEEIPRTSAGKFLKRALR 508
|
|
| PRK05691 |
PRK05691 |
peptide synthase; Validated |
67-338 |
4.36e-16 |
|
peptide synthase; Validated
Pssm-ID: 235564 [Multi-domain] Cd Length: 4334 Bit Score: 79.83 E-value: 4.36e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755522749 67 DAKTILNTLCRFPITTLCCVPTLFRLLVQEDLTRYKFQCLRHCLTGGEALNPD----VRDKWKSQtglELHEGYGQSETV 142
Cdd:PRK05691 2411 GAEEICQLIREQQVSILGFTPSYGSQLAQWLAGQGEQLPVRMCITGGEALTGEhlqrIRQAFAPQ---LFFNAYGPTETV 2487
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755522749 143 VI-----CGNSRNSTIKSGSMGKASPPYDVQIVDEEGNVLPPGKEGNIAVRIKPtrpfcFFNCYLDNPEKTA-------- 209
Cdd:PRK05691 2488 VMplaclAPEQLEEGAASVPIGRVVGARVAYILDADLALVPQGATGELYVGGAG-----LAQGYHDRPGLTAerfvadpf 2562
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755522749 210 ASEQGDFYITGDRAHMDEDGYFWFLGRNDDVINSSSYRIGPVEVESALAEHPAVLEsAVVSSPDPIRGEVVKAFIVLSPA 289
Cdd:PRK05691 2563 AADGGRLYRTGDLVRLRADGLVEYVGRIDHQVKIRGFRIELGEIESRLLEHPAVRE-AVVLALDTPSGKQLAGYLVSAVA 2641
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|
gi 755522749 290 YASHDPEALTRE-LQEHVKTVTAPYKYPRKVAFISELPKTVSGKILRSKL 338
Cdd:PRK05691 2642 GQDDEAQAALREaLKAHLKQQLPDYMVPAHLILLDSLPLTANGKLDRRAL 2691
|
|
| PRK07824 |
PRK07824 |
o-succinylbenzoate--CoA ligase; |
110-339 |
4.06e-15 |
|
o-succinylbenzoate--CoA ligase;
Pssm-ID: 236108 [Multi-domain] Cd Length: 358 Bit Score: 75.47 E-value: 4.06e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755522749 110 LTGGEALNPDVRDKwKSQTGLELHEGYGQSETvviCGnsrnstiksGSM--GKASPPYDVQIVDEE----GNVLPPGkeg 183
Cdd:PRK07824 157 LVGGGPAPAPVLDA-AAAAGINVVRTYGMSET---SG---------GCVydGVPLDGVRVRVEDGRialgGPTLAKG--- 220
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755522749 184 niavrikptrpfcffncYLDNPEKTAASEQGDFyITGDRAHMDeDGYFWFLGRNDDVINSSSYRIGPVEVESALAEHPAV 263
Cdd:PRK07824 221 -----------------YRNPVDPDPFAEPGWF-RTDDLGALD-DGVLTVLGRADDAISTGGLTVLPQVVEAALATHPAV 281
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 755522749 264 LESAVVSSPDPIRGEVVKAFIVlspayASHDPEALTRELQEHVKTVTAPYKYPRKVAFISELPKTVSGKILRSKLR 339
Cdd:PRK07824 282 ADCAVFGLPDDRLGQRVVAAVV-----GDGGPAPTLEALRAHVARTLDRTAAPRELHVVDELPRRGIGKVDRRALV 352
|
|
| PRK09274 |
PRK09274 |
peptide synthase; Provisional |
66-305 |
4.37e-15 |
|
peptide synthase; Provisional
Pssm-ID: 236443 [Multi-domain] Cd Length: 552 Bit Score: 76.09 E-value: 4.37e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755522749 66 VDAKTILNTLCRFPITTLCCVPTLFRLLVQEDLTR-YKFQCLRHCLTGG------------EALNPDVrdkwksqtglEL 132
Cdd:PRK09274 249 VDPAKLFAAIERYGVTNLFGSPALLERLGRYGEANgIKLPSLRRVISAGapvpiavierfrAMLPPDA----------EI 318
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755522749 133 HEGYGQSETVVIC--------GNSRNSTIKSGS--MGKASPPYDVQIVD---------EEGNVLPPGKEGNIAVRiKP-- 191
Cdd:PRK09274 319 LTPYGATEALPISsiesreilFATRAATDNGAGicVGRPVDGVEVRIIAisdapipewDDALRLATGEIGEIVVA-GPmv 397
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755522749 192 TRpfcffnCYLDNPEKTAAS----EQGDFY-ITGDRAHMDEDGYFWFLGRNDDVINSSSYRIGPVEVESALAEHPAVLES 266
Cdd:PRK09274 398 TR------SYYNRPEATRLAkipdGQGDVWhRMGDLGYLDAQGRLWFCGRKAHRVETAGGTLYTIPCERIFNTHPGVKRS 471
|
250 260 270
....*....|....*....|....*....|....*....
gi 755522749 267 AVVSSPDPirGEVVKAFIVLSPAYASHDPEALTRELQEH 305
Cdd:PRK09274 472 ALVGVGVP--GAQRPVLCVELEPGVACSKSALYQELRAL 508
|
|
| A_NRPS_PpsD_like |
cd17650 |
similar to adenylation domain of plipastatin synthase (PpsD); This family of the adenylation ... |
65-338 |
1.75e-14 |
|
similar to adenylation domain of plipastatin synthase (PpsD); This family of the adenylation (A) domain of nonribosomal peptide synthases (NRPS) includes bacitracin synthetase 1 (BacA) in Bacillus licheniformis, tyrocidine synthetase in Brevibacillus brevis, plipastatin synthase (PpsD, an important antifungal protein) in Bacillus subtilis and mannopeptimycin peptide synthetase (MppB) in Streptomyces hygroscopicus. Plipastatin has strong fungitoxic activity and is involved in inhibition of phospholipase A2 and biofilm formation. Bacitracin, a mixture of related cyclic peptides, is used as a polypeptide antibiotic while function of tyrocidine is thought to be regulation of sporulation. MppB is involved in biosynthetic pathway of mannopeptimycin, a novel class of mannosylated lipoglycopeptides. The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester bond to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.
Pssm-ID: 341305 [Multi-domain] Cd Length: 447 Bit Score: 74.04 E-value: 1.75e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755522749 65 RVDAKTILNTLCRFPITTLCCVPTLFRLLVQE-DLTRYKFQCLRHCLTGGEAlnpdVRDKWKSQTGLELHEG------YG 137
Cdd:cd17650 171 KLDPAALYDLILKSRITLMESTPALIRPVMAYvYRNGLDLSAMRLLIVGSDG----CKAQDFKTLAARFGQGmriinsYG 246
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755522749 138 QSETVVICG---NSRNSTIKSGS--MGKASPPYDVQIVDEEGNVLPPGKEGNIAV------RikptrpfcffnCYLDNPE 206
Cdd:cd17650 247 VTEATIDSTyyeEGRDPLGDSANvpIGRPLPNTAMYVLDERLQPQPVGVAGELYIggagvaR-----------GYLNRPE 315
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755522749 207 KTAA-------SEQGDFYITGDRAHMDEDGYFWFLGRNDDVINSSSYRIGPVEVESALAEHPAVLESAVVSSPDPiRGEV 279
Cdd:cd17650 316 LTAErfvenpfAPGERMYRTGDLARWRADGNVELLGRVDHQVKIRGFRIELGEIESQLARHPAIDEAVVAVREDK-GGEA 394
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|
gi 755522749 280 -VKAFIVlspayASHDPEalTRELQEHVKTVTAPYKYPRKVAFISELPKTVSGKILRSKL 338
Cdd:cd17650 395 rLCAYVV-----AAATLN--TAELRAFLAKELPSYMIPSYYVQLDALPLTPNGKVDRRAL 447
|
|
| LC_FACS_like |
cd17640 |
Long-chain fatty acid CoA synthetase; This family includes long-chain fatty acid (C12-C20) CoA ... |
69-340 |
2.10e-14 |
|
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: 73.93 E-value: 2.10e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755522749 69 KTILNTLCRFPITTLCCVPTLFRLL---VQEDLTRYKF------------QCLRHCLTGGEALNPDVrDKWKSQTGLELH 133
Cdd:cd17640 163 RTLKDDLKRVKPHYIVSVPRLWESLysgIQKQVSKSSPikqflflfflsgGIFKFGISGGGALPPHV-DTFFEAIGIEVL 241
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755522749 134 EGYGQSETVVICGNSRNSTIKSGSMGKASPPYDVQIVDEEGN-VLPPGKEGNIAVRIKPTrpfcfFNCYLDNPEKTAASE 212
Cdd:cd17640 242 NGYGLTETSPVVSARRLKCNVRGSVGRPLPGTEIKIVDPEGNvVLPPGEKGIVWVRGPQV-----MKGYYKNPEATSKVL 316
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755522749 213 QGD-FYITGDRAHMDEDGYFWFLGRNDDVIN-SSSYRIGPVEVESALAEHPaVLESAVVSSPDPIRgevVKAFIVlsPay 290
Cdd:cd17640 317 DSDgWFNTGDLGWLTCGGELVLTGRAKDTIVlSNGENVEPQPIEEALMRSP-FIEQIMVVGQDQKR---LGALIV--P-- 388
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|
gi 755522749 291 ashDPEALTRELQEhvktvtapykypRKVAFISELPKTVSGKILRSKLRN 340
Cdd:cd17640 389 ---NFEELEKWAKE------------SGVKLANDRSQLLASKKVLKLYKN 423
|
|
| PRK07768 |
PRK07768 |
long-chain-fatty-acid--CoA ligase; Validated |
91-341 |
2.38e-14 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236091 [Multi-domain] Cd Length: 545 Bit Score: 73.88 E-value: 2.38e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755522749 91 RLLVQEDLTRYKFQCLRHCLTGGEALNP-DVRDKWKSQTGLELHEG-----YGQSETVVI-----CGN------------ 147
Cdd:PRK07768 263 RLRRQAKPGAFDLSSLRFALNGAEPIDPaDVEDLLDAGARFGLRPEailpaYGMAEATLAvsfspCGAglvvdevdadll 342
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755522749 148 ---------SRNSTIKSGSMGKASPPYDVQIVDEEGNVLPPGKEGNIAVRIKPTRPFcffncYLDNPEKTAASEQGDFYI 218
Cdd:PRK07768 343 aalrravpaTKGNTRRLATLGPPLPGLEVRVVDEDGQVLPPRGVGVIELRGESVTPG-----YLTMDGFIPAQDADGWLD 417
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755522749 219 TGDRAHMDEDGYFWFLGRNDDVINSSSYRIGPVEVESALAEHPAVLESAVVSSPDPiRGEVVKAFIVLSPAYASHDPEAL 298
Cdd:PRK07768 418 TGDLGYLTEEGEVVVCGRVKDVIIMAGRNIYPTDIERAAARVEGVRPGNAVAVRLD-AGHSREGFAVAVESNAFEDPAEV 496
|
250 260 270 280
....*....|....*....|....*....|....*....|....*.
gi 755522749 299 TRELQEHVKTVTAPYKY-PRKVAFIS--ELPKTVSGKILRSKLRNQ 341
Cdd:PRK07768 497 RRIRHQVAHEVVAEVGVrPRNVVVLGpgSIPKTPSGKLRRANAAEL 542
|
|
| PRK05691 |
PRK05691 |
peptide synthase; Validated |
24-338 |
3.49e-14 |
|
peptide synthase; Validated
Pssm-ID: 235564 [Multi-domain] Cd Length: 4334 Bit Score: 74.05 E-value: 3.49e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755522749 24 WMALTESDIFWNTTDTGWVKAAWTLFSAWSNGAcifvhelpRVDakTILNTLCRFP-----------ITTLCCVPTLFRL 92
Cdd:PRK05691 3904 YLALSEADVIAQTASQSFDISVWQFLAAPLFGA--------RVE--IVPNAIAHDPqgllahvqaqgITVLESVPSLIQG 3973
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755522749 93 LVQEDltRYKFQCLRHCLTGGEALNPDVRDKW-KSQTGLELHEGYGQSETV-------VICGNSRNSTIKSGSmgkaspP 164
Cdd:PRK05691 3974 MLAED--RQALDGLRWMLPTGEAMPPELARQWlQRYPQIGLVNAYGPAECSddvaffrVDLASTRGSYLPIGS------P 4045
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755522749 165 YD---VQIVDEEGNVLPPGKEGNIAV------RikptrpfcffnCYLDNPEKTAAS-------EQGD-FYITGDRAHMDE 227
Cdd:PRK05691 4046 TDnnrLYLLDEALELVPLGAVGELCVagtgvgR-----------GYVGDPLRTALAfvphpfgAPGErLYRTGDLARRRS 4114
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755522749 228 DGYFWFLGRNDDVINSSSYRIGPVEVESALAEHPAVLESAVVSSPDPiRGEVVKAFIVlsPAYASHDPEALTRELQEHVK 307
Cdd:PRK05691 4115 DGVLEYVGRIDHQVKIRGYRIELGEIEARLHEQAEVREAAVAVQEGV-NGKHLVGYLV--PHQTVLAQGALLERIKQRLR 4191
|
330 340 350
....*....|....*....|....*....|.
gi 755522749 308 TVTAPYKYPRKVAFISELPKTVSGKILRSKL 338
Cdd:PRK05691 4192 AELPDYMVPLHWLWLDRLPLNANGKLDRKAL 4222
|
|
| LC_FACS_bac1 |
cd17641 |
bacterial long-chain fatty acid CoA synthetase; The members of this family are bacterial ... |
89-289 |
4.93e-14 |
|
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: 72.84 E-value: 4.93e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755522749 89 LFRLLVQEDL-TRYKFQCLRHCLTGGEALNPDVRDKWKSqTGLELHEGYGQSETVVICGNSRNSTIKSGSMGKASPPYDV 167
Cdd:cd17641 308 LADALLFRPLrDRLGFSRLRSAATGGAALGPDTFRFFHA-IGVPLKQLYGQTELAGAYTVHRDGDVDPDTVGVPFPGTEV 386
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755522749 168 QIvDEEGNVLppgkegniavrikpTRPFCFFNCYLDNPEKTAASEQGD-FYITGDRAHMDEDGYFWFLGRNDDVINSS-S 245
Cdd:cd17641 387 RI-DEVGEIL--------------VRSPGVFVGYYKNPEATAEDFDEDgWLHTGDAGYFKENGHLVVIDRAKDVGTTSdG 451
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 755522749 246 YRIGPVEVESALAEHPAVLESAVVSSPDPIrgevVKAFIVLSPA 289
Cdd:cd17641 452 TRFSPQFIENKLKFSPYIAEAVVLGAGRPY----LTAFICIDYA 491
|
|
| PRK05620 |
PRK05620 |
long-chain fatty-acid--CoA ligase; |
86-340 |
3.22e-12 |
|
long-chain fatty-acid--CoA ligase;
Pssm-ID: 180167 [Multi-domain] Cd Length: 576 Bit Score: 67.50 E-value: 3.22e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755522749 86 VPTLF-RLLVQEDLTRYKFQCLRHCLTGGEALNPDVRDKWKSQTGLELHEGYGQSETVVICGNSRNSTIKSG-------- 156
Cdd:PRK05620 279 VPTLWiQLMVHYLKNPPERMSLQEIYVGGSAVPPILIKAWEERYGVDVVHVWGMTETSPVGTVARPPSGVSGearwayrv 358
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755522749 157 SMGKASPPYDVQIVDeEGNVLPPG--KEGNIAVRiKPTRPFCFFNCylDNPEKTAAS--------EQGD-------FYIT 219
Cdd:PRK05620 359 SQGRFPASLEYRIVN-DGQVMESTdrNEGEIQVR-GNWVTASYYHS--PTEEGGGAAstfrgedvEDANdrftadgWLRT 434
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755522749 220 GDRAHMDEDGYFWFLGRNDDVINSSSYRIGPVEVESALAEHPAVLESAVVSSPDPIRGEVVKAFIVLSPAYashDPEALT 299
Cdd:PRK05620 435 GDVGSVTRDGFLTIHDRARDVIRSGGEWIYSAQLENYIMAAPEVVECAVIGYPDDKWGERPLAVTVLAPGI---EPTRET 511
|
250 260 270 280
....*....|....*....|....*....|....*....|..
gi 755522749 300 RE-LQEHVKTVTAPYKYPRKVAFISELPKTVSGKILRSKLRN 340
Cdd:PRK05620 512 AErLRDQLRDRLPNWMLPEYWTFVDEIDKTSVGKFDKKDLRQ 553
|
|
| FATP_FACS |
cd05940 |
Fatty acid transport proteins (FATP) play dual roles as fatty acid transporters and its ... |
113-341 |
1.07e-11 |
|
Fatty acid transport proteins (FATP) play dual roles as fatty acid transporters and its activation enzymes; Fatty acid transport protein (FATP) transports long-chain or very-long-chain fatty acids across the plasma membrane. FATPs also have fatty acid CoA synthetase activity, thus playing dual roles as fatty acid transporters and its activation enzymes. At least five copies of FATPs are identified in mammalian cells. This family also includes prokaryotic FATPs. FATPs are the key players in the trafficking of exogenous fatty acids into the cell and in intracellular fatty acid homeostasis.
Pssm-ID: 341263 [Multi-domain] Cd Length: 449 Bit Score: 65.45 E-value: 1.07e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755522749 113 GEALNPDVRDKWKSQTGL-ELHEGYGQSETVVICGN--------SRNSTIKSGSMGKASPPYDVQ----IVDEEGNV--L 177
Cdd:cd05940 203 GNGLRPDIWEEFKERFGVpRIAEFYAATEGNSGFINffgkpgaiGRNPSLLRKVAPLALVKYDLEsgepIRDAEGRCikV 282
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755522749 178 PPGKEGNIAVRIKPTRPFcffNCYLDNPEKTA-----ASEQGDFYI-TGDRAHMDEDGYFWFLGRNDDVINSSSYRIGPV 251
Cdd:cd05940 283 PRGEPGLLISRINPLEPF---DGYTDPAATEKkilrdVFKKGDAWFnTGDLMRLDGEGFWYFVDRLGDTFRWKGENVSTT 359
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755522749 252 EVESALAEHPAVLESAV--VSSPDpIRGEVVKAFIVLSPAYaSHDPEALTRELQEHVktvtAPYKYPRKVAFISELPKTV 329
Cdd:cd05940 360 EVAAVLGAFPGVEEANVygVQVPG-TDGRAGMAAIVLQPNE-EFDLSALAAHLEKNL----PGYARPLFLRLQPEMEITG 433
|
250
....*....|..
gi 755522749 330 SGKILRSKLRNQ 341
Cdd:cd05940 434 TFKQQKVDLRNE 445
|
|
| PRK06814 |
PRK06814 |
acyl-[ACP]--phospholipid O-acyltransferase; |
101-333 |
1.28e-11 |
|
acyl-[ACP]--phospholipid O-acyltransferase;
Pssm-ID: 235865 [Multi-domain] Cd Length: 1140 Bit Score: 65.76 E-value: 1.28e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755522749 101 YKFQCLRHCLTGGEALNPDVRDKWKSQTGLELHEGYGQSETV-VICGNS--RNstiKSGSMGKASPPYD-----VQIVDE 172
Cdd:PRK06814 904 YDFRSLRYVFAGAEKVKEETRQTWMEKFGIRILEGYGVTETApVIALNTpmHN---KAGTVGRLLPGIEyrlepVPGIDE 980
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755522749 173 EGNVLPPGKegNIAVRikptrpfcffncYL--DNPEKTAASEQGdFYITGDRAHMDEDGYFWFLGRNDDVINSSSYRIGP 250
Cdd:PRK06814 981 GGRLFVRGP--NVMLG------------YLraENPGVLEPPADG-WYDTGDIVTIDEEGFITIKGRAKRFAKIAGEMISL 1045
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755522749 251 VEVESALAEHPAVLESAVVSSPDPIRGEVvkafIVLSPayashDPEALTRE-LQEHVKTVTAPYKY-PRKVAFISELPKT 328
Cdd:PRK06814 1046 AAVEELAAELWPDALHAAVSIPDARKGER----IILLT-----TASDATRAaFLAHAKAAGASELMvPAEIITIDEIPLL 1116
|
....*
gi 755522749 329 VSGKI 333
Cdd:PRK06814 1117 GTGKI 1121
|
|
| FAAL |
cd05931 |
Fatty acyl-AMP ligase (FAAL); FAAL belongs to the class I adenylate forming enzyme family and ... |
157-339 |
1.75e-11 |
|
Fatty acyl-AMP ligase (FAAL); FAAL belongs to the class I adenylate forming enzyme family and is homologous to fatty acyl-coenzyme A (CoA) ligases (FACLs). However, FAALs produce only the acyl adenylate and are unable to perform the thioester-forming reaction, while FACLs perform a two-step catalytic reaction; AMP ligation followed by CoA ligation using ATP and CoA as cofactors. FAALs have insertion motifs between the N-terminal and C-terminal subdomains that distinguish them from the FACLs. This insertion motif precludes the binding of CoA, thus preventing CoA ligation. It has been suggested that the acyl adenylates serve as substrates for multifunctional polyketide synthases to permit synthesis of complex lipids such as phthiocerol dimycocerosate, sulfolipids, mycolic acids, and mycobactin.
Pssm-ID: 341254 [Multi-domain] Cd Length: 547 Bit Score: 64.95 E-value: 1.75e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755522749 157 SMGKASPPYDVQIVDEEGN-VLPPGKEGNIAVRIKPTRPfcffnCYLDNPEKTAASEQ-------GDFYITGDRAHMDeD 228
Cdd:cd05931 356 SCGRPLPDQEVRIVDPETGrELPDGEVGEIWVRGPSVAS-----GYWGRPEATAETFGalaatdeGGWLRTGDLGFLH-D 429
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755522749 229 GYFWFLGRNDDVINSSSYRIGPVEVESALAEHPAVLES---AVVSSPDPIRGEVVkAFIVLSPAYASHDPEALTRELQEH 305
Cdd:cd05931 430 GELYITGRLKDLIIVRGRNHYPQDIEATAEEAHPALRPgcvAAFSVPDDGEERLV-VVAEVERGADPADLAAIAAAIRAA 508
|
170 180 190
....*....|....*....|....*....|....*....
gi 755522749 306 VKT---VTapykyPRKVAFIS--ELPKTVSGKILRSKLR 339
Cdd:cd05931 509 VARehgVA-----PADVVLVRpgSIPRTSSGKIQRRACR 542
|
|
| FATP_chFAT1_like |
cd05937 |
Uncharacterized subfamily of bifunctional fatty acid transporter/very-long-chain acyl-CoA ... |
113-343 |
1.64e-10 |
|
Uncharacterized subfamily of bifunctional fatty acid transporter/very-long-chain acyl-CoA synthetase in fungi; Fatty acid transport protein (FATP) transports long-chain or very-long-chain fatty acids across the plasma membrane. FATPs also have fatty acid CoA synthetase activity, thus playing dual roles as fatty acid transporters and its activation enzymes. FATPs are the key players in the trafficking of exogenous fatty acids into the cell and in intracellular fatty acid homeostasis. Members of this family are fungal FATPs, including FAT1 from Cochliobolus heterostrophus.
Pssm-ID: 341260 [Multi-domain] Cd Length: 468 Bit Score: 62.06 E-value: 1.64e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755522749 113 GEALNPDVRDKWKSQTGL-ELHEGYGQSETVVICGNSRNSTIKSGSMGKASPPYD---------VQIVDEEGNVL----- 177
Cdd:cd05937 209 GNGLRPDIWERFRERFNVpEIGEFYAATEGVFALTNHNVGDFGAGAIGHHGLIRRwkfenqvvlVKMDPETDDPIrdpkt 288
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755522749 178 ------PPGKEGNIAVRIkPTRPFCFFNCYLDNPEKTAAS------EQGD-FYITGDRAHMDEDGYFWFLGRNDDVINSS 244
Cdd:cd05937 289 gfcvraPVGEPGEMLGRV-PFKNREAFQGYLHNEDATESKlvrdvfRKGDiYFRTGDLLRQDADGRWYFLDRLGDTFRWK 367
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755522749 245 SYRIGPVEVESALAEHPAVLESAVVSSPDP-IRGEVVKAFIVLSPAYASHDPEALTReLQEHVKTVTAPYKYPRKVAFIS 323
Cdd:cd05937 368 SENVSTTEVADVLGAHPDIAEANVYGVKVPgHDGRAGCAAITLEESSAVPTEFTKSL-LASLARKNLPSYAVPLFLRLTE 446
|
250 260
....*....|....*....|
gi 755522749 324 ELPKTVSGKILRSKLRNQEW 343
Cdd:cd05937 447 EVATTDNHKQQKGVLRDEGV 466
|
|
| A_NRPS_MycA_like |
cd05908 |
The adenylation domain of nonribosomal peptide synthetases (NRPS) similar to mycosubtilin ... |
118-341 |
3.45e-10 |
|
The adenylation domain of nonribosomal peptide synthetases (NRPS) similar to mycosubtilin synthase subunit A (MycA); The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as (amino)-acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms thioester to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. This family includes NRPS similar to mycosubtilin synthase subunit A (MycA). Mycosubtilin, which is characterized by a beta-amino fatty acid moiety linked to the circular heptapeptide Asn-Tyr-Asn-Gln-Pro-Ser-Asn, belongs to the iturin family of lipopeptide antibiotics. The mycosubtilin synthase subunit A (MycA) combines functional domains derived from peptide synthetases, amino transferases, and fatty acid synthases. Nonribosomal peptide synthetases are large multifunction enzymes that synthesize many therapeutically useful peptides. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and, in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.
Pssm-ID: 341234 [Multi-domain] Cd Length: 499 Bit Score: 60.97 E-value: 3.45e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755522749 118 PDVRDKWKSQTGLELHEGYGQSETVVICGNSRNSTIKSgsMGKASPPYDVQIVDEEGNVLPPGKEGNIAVRIKPTRPfcf 197
Cdd:cd05908 278 PKAQSPFKTITLGRRHVTHGEPEPEVDKKDSECLTFVE--VGKPIDETDIRICDEDNKILPDGYIGHIQIRGKNVTP--- 352
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755522749 198 fnCYLDNPEKTAA--SEQGdFYITGDRAHMdEDGYFWFLGRNDDVINSSSYRIGPVEVESALAEHPAVLESAVVS---SP 272
Cdd:cd05908 353 --GYYNNPEATAKvfTDDG-WLKTGDLGFI-RNGRLVITGREKDIIFVNGQNVYPHDIERIAEELEGVELGRVVAcgvNN 428
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 755522749 273 DPIRGEVVKAFIVlsPAYASHDPEALTRELQEHVKTVTApyKYPRKVAFISELPKTVSGKILRSKLRNQ 341
Cdd:cd05908 429 SNTRNEEIFCFIE--HRKSEDDFYPLGKKIKKHLNKRGG--WQINEVLPIRRIPKTTSGKVKRYELAQR 493
|
|
| PLN03052 |
PLN03052 |
acetate--CoA ligase; Provisional |
25-341 |
1.35e-09 |
|
acetate--CoA ligase; Provisional
Pssm-ID: 215553 [Multi-domain] Cd Length: 728 Bit Score: 59.32 E-value: 1.35e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755522749 25 MALTESDIFWNTTDTGWVKAAWTLFSAWSNGACI--------------FVHelprvDAKtilntlcrfpITTLCCVPTLF 90
Cdd:PLN03052 392 LDIRKGDIVCWPTNLGWMMGPWLVYASLLNGATLalyngsplgrgfakFVQ-----DAK----------VTMLGTVPSIV 456
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755522749 91 RLL----VQEDLTRYKFQCLRhclTGGEALNPDvRDKWKSQT-----------GLELHEGYgqsetvvICGnsrnSTIKS 155
Cdd:PLN03052 457 KTWkntnCMAGLDWSSIRCFG---STGEASSVD-DYLWLMSRagykpiieycgGTELGGGF-------VTG----SLLQP 521
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755522749 156 GSMGKASPP---YDVQIVDEEGNVLPPGKEGNIAVRIKPTrpfcFFNC--YLDNPEKTAASEQGDFYITGD--RAHMDE- 227
Cdd:PLN03052 522 QAFAAFSTPamgCKLFILDDSGNPYPDDAPCTGELALFPL----MFGAssTLLNADHYKVYFKGMPVFNGKilRRHGDIf 597
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755522749 228 ----DGYFWFLGRNDDVINSSSYRIGPVEVESAL-AEHPAVLESAVVSSPDPIRG--EVVKAFIVLSPAYASHDPEALTR 300
Cdd:PLN03052 598 ertsGGYYRAHGRADDTMNLGGIKVSSVEIERVCnAADESVLETAAIGVPPPGGGpeQLVIAAVLKDPPGSNPDLNELKK 677
|
330 340 350 360
....*....|....*....|....*....|....*....|.
gi 755522749 301 ELQEHVKTVTAPYKYPRKVAFISELPKTVSGKILRSKLRNQ 341
Cdd:PLN03052 678 IFNSAIQKKLNPLFKVSAVVIVPSFPRTASNKVMRRVLRQQ 718
|
|
| PRK03584 |
PRK03584 |
acetoacetate--CoA ligase; |
220-334 |
1.95e-09 |
|
acetoacetate--CoA ligase;
Pssm-ID: 235134 [Multi-domain] Cd Length: 655 Bit Score: 58.65 E-value: 1.95e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755522749 220 GDRAHMDEDGYFWFLGRNDDVINSSSYRIGPVEVESALAEHPAVLESAVVSSPDPIRGEVVKAFIVLSPAYASHDpeALT 299
Cdd:PRK03584 503 GDWIEITEHGGVVIYGRSDATLNRGGVRIGTAEIYRQVEALPEVLDSLVIGQEWPDGDVRMPLFVVLAEGVTLDD--ALR 580
|
90 100 110
....*....|....*....|....*....|....*
gi 755522749 300 RELQEHVKTVTAPYKYPRKVAFISELPKTVSGKIL 334
Cdd:PRK03584 581 ARIRTTIRTNLSPRHVPDKIIAVPDIPRTLSGKKV 615
|
|
| PRK09192 |
PRK09192 |
fatty acyl-AMP ligase; |
159-340 |
2.36e-09 |
|
fatty acyl-AMP ligase;
Pssm-ID: 236403 [Multi-domain] Cd Length: 579 Bit Score: 58.48 E-value: 2.36e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755522749 159 GKASPPYDVQIVDEEGNVLPPGKEGNIAVRiKPTrpfcFFNCYLDNPEKTAASEQGDFYITGDRAHMdEDGYFWFLGRND 238
Cdd:PRK09192 388 GKALPGHEIEIRNEAGMPLPERVVGHICVR-GPS----LMSGYFRDEESQDVLAADGWLDTGDLGYL-LDGYLYITGRAK 461
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755522749 239 DVINSSSYRIGPVEVESALAEHPAVL--ESAVVSSPDPIRGEVVkafiVLSPAYAShDPE---ALTRELQEHVKTVTApy 313
Cdd:PRK09192 462 DLIIINGRNIWPQDIEWIAEQEPELRsgDAAAFSIAQENGEKIV----LLVQCRIS-DEErrgQLIHALAALVRSEFG-- 534
|
170 180
....*....|....*....|....*....
gi 755522749 314 kYPRKVAFIS--ELPKTVSGKILRSKLRN 340
Cdd:PRK09192 535 -VEAAVELVPphSLPRTSSGKLSRAKAKK 562
|
|
| AACS |
cd05943 |
Acetoacetyl-CoA synthetase (acetoacetate-CoA ligase, AACS); AACS is a cytosolic ligase that ... |
32-334 |
3.94e-09 |
|
Acetoacetyl-CoA synthetase (acetoacetate-CoA ligase, AACS); AACS is a cytosolic ligase that specifically activates acetoacetate to its coenzyme A ester by a two-step reaction. Acetoacetate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This is the first step of the mevalonate pathway of isoprenoid biosynthesis via isopentenyl diphosphate. Isoprenoids are a large class of compounds found in all living organisms. AACS is widely distributed in bacteria, archaea and eukaryotes. In bacteria, AACS is known to exhibit an important role in the metabolism of poly-b-hydroxybutyrate, an intracellular reserve of organic carbon and chemical energy by some microorganisms. In mammals, AACS influences the rate of ketone body utilization for the formation of physiologically important fatty acids and cholesterol.
Pssm-ID: 341265 [Multi-domain] Cd Length: 629 Bit Score: 58.05 E-value: 3.94e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755522749 32 IFWNTTdTGWVKAAWtLFSAWSNGACI----------FVHELPRVDAKTilntlcrfPITTLCCVPTLFRLLVQEDL--- 98
Cdd:cd05943 294 LFYYTT-CGWMMWNW-LVSGLAVGATIvlydgspfypDTNALWDLADEE--------GITVFGTSAKYLDALEKAGLkpa 363
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755522749 99 TRYKFQCLRHCLTGGEALNPD----VRDKWKSqtGLELHEGYGQSETV-VICGNSRNSTIKSGSMGKASPPYDVQIVDEE 173
Cdd:cd05943 364 ETHDLSSLRTILSTGSPLKPEsfdyVYDHIKP--DVLLASISGGTDIIsCFVGGNPLLPVYRGEIQCRGLGMAVEAFDEE 441
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755522749 174 GNVLPPGKEGNIAVRIKPTRPFCFFNcyldnpeKTAASEQGDFYIT--------GDRAHMDEDGYFWFLGRNDDVINSSS 245
Cdd:cd05943 442 GKPVWGEKGELVCTKPFPSMPVGFWN-------DPDGSRYRAAYFAkypgvwahGDWIEITPRGGVVILGRSDGTLNPGG 514
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755522749 246 YRIGPVEVESALAEHPAVLESAVVSSPDPIRGEVVKAFIVLSPAyashdpEALTRELQEHVKTVTA----PYKYPRKVAF 321
Cdd:cd05943 515 VRIGTAEIYRVVEKIPEVEDSLVVGQEWKDGDERVILFVKLREG------VELDDELRKRIRSTIRsalsPRHVPAKIIA 588
|
330
....*....|...
gi 755522749 322 ISELPKTVSGKIL 334
Cdd:cd05943 589 VPDIPRTLSGKKV 601
|
|
| PRK06334 |
PRK06334 |
long chain fatty acid--[acyl-carrier-protein] ligase; Validated |
106-260 |
2.54e-08 |
|
long chain fatty acid--[acyl-carrier-protein] ligase; Validated
Pssm-ID: 180533 [Multi-domain] Cd Length: 539 Bit Score: 55.21 E-value: 2.54e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755522749 106 LRHCLTGGEALNPDVRDK-WKSQTGLELHEGYGQSE-TVVICGNSRNSTIKSGSMGKASPPYDVQIVDEEGNV-LPPGKE 182
Cdd:PRK06334 301 LRFVVIGGDAFKDSLYQEaLKTFPHIQLRQGYGTTEcSPVITINTVNSPKHESCVGMPIRGMDVLIVSEETKVpVSSGET 380
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755522749 183 GNIAvrikpTRPFCFFNCYLDNPEKTAASEQG--DFYITGDRAHMDEDGYFWFLGRNDDVINSSSYRIGPVEVESALAEH 260
Cdd:PRK06334 381 GLVL-----TRGTSLFSGYLGEDFGQGFVELGgeTWYVTGDLGYVDRHGELFLKGRLSRFVKIGAEMVSLEALESILMEG 455
|
|
| PRK08043 |
PRK08043 |
bifunctional acyl-ACP--phospholipid O-acyltransferase/long-chain-fatty-acid--ACP ligase; |
101-332 |
4.04e-08 |
|
bifunctional acyl-ACP--phospholipid O-acyltransferase/long-chain-fatty-acid--ACP ligase;
Pssm-ID: 181207 [Multi-domain] Cd Length: 718 Bit Score: 54.72 E-value: 4.04e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755522749 101 YKFQCLRHCLTGGEALNPDVRDKWKSQTGLELHEGYGQSETV-VICGNSRNSTiKSGSMGKASPPYDVQIVD----EEGN 175
Cdd:PRK08043 476 YDFARLRYVVAGAEKLQESTKQLWQDKFGLRILEGYGVTECApVVSINVPMAA-KPGTVGRILPGMDARLLSvpgiEQGG 554
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755522749 176 VLPPgKEGNIavrikptrpfcfFNCYL--DNPEK----TAASEQGD----FYITGDRAHMDEDGYFWFLGRNDDVINSSS 245
Cdd:PRK08043 555 RLQL-KGPNI------------MNGYLrvEKPGVlevpTAENARGEmergWYDTGDIVRFDEQGFVQIQGRAKRFAKIAG 621
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755522749 246 YRIGPVEVES-ALAEHPAVLESAVVSSpDPIRGEVVKAFivlspayaSHDPEaLTRE-LQEHVKTVTAP-YKYPRKVAFI 322
Cdd:PRK08043 622 EMVSLEMVEQlALGVSPDKQHATAIKS-DASKGEALVLF--------TTDSE-LTREkLQQYAREHGVPeLAVPRDIRYL 691
|
250
....*....|
gi 755522749 323 SELPKTVSGK 332
Cdd:PRK08043 692 KQLPLLGSGK 701
|
|
| FACL_like_1 |
cd05910 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
65-269 |
2.06e-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: 341236 [Multi-domain] Cd Length: 457 Bit Score: 52.46 E-value: 2.06e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755522749 65 RVDAKTILNTLCRFPITTLCCVPTLFRLLvqedlTRY------KFQCLRHCLTGGEALNPDVRDKWKS--QTGLELHEGY 136
Cdd:cd05910 159 RADPQKLVGAIRQYGVSIVFGSPALLERV-----ARYcaqhgiTLPSLRRVLSAGAPVPIALAARLRKmlSDEAEILTPY 233
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755522749 137 GQSETVVICGNSRNSTIKSGS----------MGKASPPYDVQIV--DEEG-------NVLPPGKEGNIAVRIKPTRPfcf 197
Cdd:cd05910 234 GATEALPVSSIGSRELLATTTaatsggagtcVGRPIPGVRVRIIeiDDEPiaewddtLELPRGEIGEITVTGPTVTP--- 310
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 755522749 198 fnCYLDNPEKTAASE-----QGDFYITGDRAHMDEDGYFWFLGRNDDVINSSSYRIGPVEVESALAEHPAVLESAVV 269
Cdd:cd05910 311 --TYVNRPVATALAKiddnsEGFWHRMGDLGYLDDEGRLWFCGRKAHRVITTGGTLYTEPVERVFNTHPGVRRSALV 385
|
|
| hsFATP4_like |
cd05939 |
Fatty acid transport proteins (FATP), including FATP4 and FATP1, and similar proteins; Fatty ... |
134-341 |
2.53e-07 |
|
Fatty acid transport proteins (FATP), including FATP4 and FATP1, and similar proteins; Fatty acid transport protein (FATP) transports long-chain or very-long-chain fatty acids across the plasma membrane. At least five copies of FATPs are identified in mammalian cells. This family includes FATP4, FATP1, and homologous proteins. Each FATP has unique patterns of tissue distribution. FATP4 is mainly expressed in the brain, testis, colon and kidney. FATPs also have fatty acid CoA synthetase activity, thus playing dual roles as fatty acid transporters and its activation enzymes. FATPs are the key players in the trafficking of exogenous fatty acids into the cell and in intracellular fatty acid homeostasis.
Pssm-ID: 341262 [Multi-domain] Cd Length: 474 Bit Score: 52.04 E-value: 2.53e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755522749 134 EGYGQSEtvvicGNSR--NSTIKSGSMGKAS--PP--YDVQIV-----------DEEGNVLP--PGKEGNIAVRIKPTRP 194
Cdd:cd05939 248 EFYGATE-----GNSSlvNIDNHVGACGFNSriLPsvYPIRLIkvdedtgelirDSDGLCIPcqPGEPGLLVGKIIQNDP 322
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755522749 195 FCFFNCYLD---NPEKTAAS--EQGD-FYITGDRAHMDEDGYFWFLGRNDDVINSSSYRIGPVEVESALAEHPAVLESAV 268
Cdd:cd05939 323 LRRFDGYVNegaTNKKIARDvfKKGDsAFLSGDVLVMDELGYLYFKDRTGDTFRWKGENVSTTEVEGILSNVLGLEDVVV 402
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 755522749 269 --VSSPDpIRGEVVKAFIVlSPAyASHDPEALTRELQEhvktVTAPYKYPRKVAFISELPKTVSGKILRSKLRNQ 341
Cdd:cd05939 403 ygVEVPG-VEGRAGMAAIV-DPE-RKVDLDRFSAVLAK----SLPPYARPQFIRLLPEVDKTGTFKLQKTDLQKE 470
|
|
| ACSBG_like |
cd05933 |
Bubblegum-like very long-chain fatty acid CoA synthetase (VL-FACS); This family of very ... |
105-259 |
8.48e-07 |
|
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: 50.43 E-value: 8.48e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755522749 105 CLRhCLTGGEALNPDVRDKWKSqTGLELHEGYGQSETVVICGNSRNSTIKSGSMGKASPPYDVQIVDEEGNvlppgKEGN 184
Cdd:cd05933 322 CQK-FFTGAAPISRETLEFFLS-LNIPIMELYGMSETSGPHTISNPQAYRLLSCGKALPGCKTKIHNPDAD-----GIGE 394
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755522749 185 IavrikptrpfCF-----FNCYLDNPEKTAASEQGDFYI-TGDRAHMDEDGYFWFLGRNDD-VINSSSYRIGPVEVESAL 257
Cdd:cd05933 395 I----------CFwgrhvFMGYLNMEDKTEEAIDEDGWLhSGDLGKLDEDGFLYITGRIKElIITAGGENVPPVPIEDAV 464
|
..
gi 755522749 258 AE 259
Cdd:cd05933 465 KK 466
|
|
| PRK08279 |
PRK08279 |
long-chain-acyl-CoA synthetase; Validated |
113-305 |
3.85e-06 |
|
long-chain-acyl-CoA synthetase; Validated
Pssm-ID: 236217 [Multi-domain] Cd Length: 600 Bit Score: 48.33 E-value: 3.85e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755522749 113 GEALNPDVRDKWKSQTGLE-LHEGYGQSETVVICGNSRNstiKSGSMGKaSPP----------YDVQ----IVDEEGNVL 177
Cdd:PRK08279 321 GNGLRPDIWDEFQQRFGIPrILEFYAASEGNVGFINVFN---FDGTVGR-VPLwlahpyaivkYDVDtgepVRDADGRCI 396
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755522749 178 P--PGKEGNIAVRIKPTRPFcffNCYLDnPEKTAAS------EQGDFYI-TGDRAHMDEDGYFWFLGRNDDvinssSYR- 247
Cdd:PRK08279 397 KvkPGEVGLLIGRITDRGPF---DGYTD-PEASEKKilrdvfKKGDAWFnTGDLMRDDGFGHAQFVDRLGD-----TFRw 467
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 755522749 248 ----IGPVEVESALAEHPAVLESAV--VSSPDpIRGEVVKAFIVLSPAyASHDPEALTRELQEH 305
Cdd:PRK08279 468 kgenVATTEVENALSGFPGVEEAVVygVEVPG-TDGRAGMAAIVLADG-AEFDLAALAAHLYER 529
|
|
| FCS |
cd05921 |
Feruloyl-CoA synthetase (FCS); Feruloyl-CoA synthetase is an essential enzyme in the feruloyl ... |
86-301 |
1.00e-05 |
|
Feruloyl-CoA synthetase (FCS); Feruloyl-CoA synthetase is an essential enzyme in the feruloyl acid degradation pathway and enables some proteobacteria to grow on media containing feruloyl acid as the sole carbon source. It catalyzes the transfer of CoA to the carboxyl group of ferulic acid, which then forms feruloyl-CoA in the presence of ATP and Mg2. The resulting feruloyl-CoA is further degraded to vanillin and acetyl-CoA. Feruloyl-CoA synthetase (FCS) is a subfamily of the adenylate-forming enzymes superfamily.
Pssm-ID: 341245 [Multi-domain] Cd Length: 561 Bit Score: 47.04 E-value: 1.00e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755522749 86 VPTLFRLLVQ-----EDLTRYKFQCLRHCLTGGEALNPDVRDKWKS----QTG--LELHEGYGQSETVVICGNSRNSTIK 154
Cdd:cd05921 267 VPAGWEMLVAalekdEALRRRFFKRLKLMFYAGAGLSQDVWDRLQAlavaTVGerIPMMAGLGATETAPTATFTHWPTER 346
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755522749 155 SGSMGKASPPYDVQIVdeegnvlPPGkeGNIAVRIK-PTrpfcFFNCYLDNPEKTAAS--EQGdFYITGDRAHM----DE 227
Cdd:cd05921 347 SGLIGLPAPGTELKLV-------PSG--GKYEVRVKgPN----VTPGYWRQPELTAQAfdEEG-FYCLGDAAKLadpdDP 412
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755522749 228 DGYFWFLGR--NDDVINSSSY-RIGPVEVESALAEHPAVLEsAVVSSPDpirGEVVKAFIV--------LSPAYASHDPE 296
Cdd:cd05921 413 AKGLVFDGRvaEDFKLASGTWvSVGPLRARAVAACAPLVHD-AVVAGED---RAEVGALVFpdllacrrLVGLQEASDAE 488
|
....*
gi 755522749 297 ALTRE 301
Cdd:cd05921 489 VLRHA 493
|
|
| PRK05851 |
PRK05851 |
long-chain-fatty acid--ACP ligase MbtM; |
158-341 |
1.14e-05 |
|
long-chain-fatty acid--ACP ligase MbtM;
Pssm-ID: 180289 [Multi-domain] Cd Length: 525 Bit Score: 47.07 E-value: 1.14e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755522749 158 MGKASPPYDVQIVDEEGNVLPPGKE-GNIAVRIKptrpfCFFNCYLDNpektAASEQGDFYITGDRAHMDEDGYFwFLGR 236
Cdd:PRK05851 347 LGNPIPGMEVRISPGDGAAGVAGREiGEIEIRGA-----SMMSGYLGQ----APIDPDDWFPTGDLGYLVDGGLV-VCGR 416
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755522749 237 NDDVINSSSYRIGPVEVESALAEHPAVLESAVVSSPDPIRGevVKAFIVLSPAYASHDPEALTRELQEHVKTVTApyKYP 316
Cdd:PRK05851 417 AKELITVAGRNIFPTEIERVAAQVRGVREGAVVAVGTGEGS--ARPGLVIAAEFRGPDEAGARSEVVQRVASECG--VVP 492
|
170 180
....*....|....*....|....*..
gi 755522749 317 RKVAFIS--ELPKTVSGKILRSKLRNQ 341
Cdd:PRK05851 493 SDVVFVApgSLPRTSSGKLRRLAVKRS 519
|
|
| LC-FACS_euk |
cd05927 |
Eukaryotic long-chain fatty acid CoA synthetase (LC-FACS); The members of this family are ... |
110-229 |
1.54e-05 |
|
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: 46.44 E-value: 1.54e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755522749 110 LTGGEALNPDVRDKWKSQTGLELHEGYGQSETVVICGNSRNSTIKSGSMGKASPPYDVQIVD-EEGN--VLPPGKEGNIA 186
Cdd:cd05927 280 LTGSAPLSPEVLEFLRVALGCPVLEGYGQTECTAGATLTLPGDTSVGHVGGPLPCAEVKLVDvPEMNydAKDPNPRGEVC 359
|
90 100 110 120
....*....|....*....|....*....|....*....|....
gi 755522749 187 VRikptrPFCFFNCYLDNPEKTA-ASEQGDFYITGDRAHMDEDG 229
Cdd:cd05927 360 IR-----GPNVFSGYYKDPEKTAeALDEDGWLHTGDIGEWLPNG 398
|
|
| A_NRPS_alphaAR |
cd17647 |
Alpha-aminoadipate reductase; This family contains L-2-aminoadipate reductase, also known as ... |
217-338 |
5.57e-05 |
|
Alpha-aminoadipate reductase; This family contains L-2-aminoadipate reductase, also known as alpha-aminoadipate reductase (EC 1.2.1.95) or alpha-AR or L-aminoadipate-semialdehyde dehydrogenase (EC 1.2.1.31), which catalyzes the activation of alpha-aminoadipate by ATP-dependent adenylation and the reduction of activated alpha-aminoadipate by NADPH. The activated alpha-aminoadipate is bound to the phosphopantheinyl group of the enzyme itself before it is reduced to (S)-2-amino-6-oxohexanoate.
Pssm-ID: 341302 [Multi-domain] Cd Length: 520 Bit Score: 44.82 E-value: 5.57e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755522749 217 YITGDRAHMDEDGYFWFLGRNDDVINSSSYRIGPVEVESALAEHPAVLES------------AVVS--SPDPIRGEVVKA 282
Cdd:cd17647 374 YRTGDLGRYLPNGDCECCGRADDQVKIRGFRIELGEIDTHISQHPLVRENitlvrrdkdeepTLVSyiVPRFDKPDDESF 453
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 755522749 283 FIVLSPAYASHDPEA--------LTRELQEHVKTVTAPYKYPRKVAFISELPKTVSGKILRSKL 338
Cdd:cd17647 454 AQEDVPKEVSTDPIVkgligyrkLIKDIREFLKKRLASYAIPSLIVVLDKLPLNPNGKVDKPKL 517
|
|
| alpha_am_amid |
TIGR03443 |
L-aminoadipate-semialdehyde dehydrogenase; Members of this protein family are ... |
217-338 |
2.85e-03 |
|
L-aminoadipate-semialdehyde dehydrogenase; Members of this protein family are L-aminoadipate-semialdehyde dehydrogenase (EC 1.2.1.31), product of the LYS2 gene. It is also called alpha-aminoadipate reductase. In fungi, lysine is synthesized via aminoadipate. Currently, all members of this family are fungal.
Pssm-ID: 274582 [Multi-domain] Cd Length: 1389 Bit Score: 39.66 E-value: 2.85e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755522749 217 YITGDRAHMDEDGYFWFLGRNDDVINSSSYRIGPVEVESALAEHPAVLE----------------SAVVSSPDPirgEVV 280
Cdd:TIGR03443 680 YRTGDLGRYLPDGNVECCGRADDQVKIRGFRIELGEIDTHLSQHPLVREnvtlvrrdkdeeptlvSYIVPQDKS---DEL 756
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 755522749 281 KAFIVLSPAYASHDP--------EALTRELQEHVKTVTAPYKYPRKVAFISELPKTVSGKILRSKL 338
Cdd:TIGR03443 757 EEFKSEVDDEESSDPvvkglikyRKLIKDIREYLKKKLPSYAIPTVIVPLKKLPLNPNGKVDKPAL 822
|
|
| PRK09188 |
PRK09188 |
serine/threonine protein kinase; Provisional |
235-341 |
3.09e-03 |
|
serine/threonine protein kinase; Provisional
Pssm-ID: 236400 [Multi-domain] Cd Length: 365 Bit Score: 38.98 E-value: 3.09e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755522749 235 GRNDDVINSssyriGPVeVESALAEHPAVLESAVVSSPDPIRGEVVKAFIvlspayaSHDPEALTRELQEHVKTVTAPyK 314
Cdd:PRK09188 233 GTGDRIDNE-----APA-IQAALKSDPAVSDVAIALFSLPAKGVGLYAFV-------EAELPADEKSLRARLAGAKPP-K 298
|
90 100 110
....*....|....*....|....*....|.
gi 755522749 315 YPRKVAFISELPKTVSGK----ILRSKLRNQ 341
Cdd:PRK09188 299 PPEHIQPVAALPRDADGTvrddILRLIAMNQ 329
|
|
| PLN02430 |
PLN02430 |
long-chain-fatty-acid-CoA ligase |
106-343 |
3.51e-03 |
|
long-chain-fatty-acid-CoA ligase
Pssm-ID: 178049 [Multi-domain] Cd Length: 660 Bit Score: 39.03 E-value: 3.51e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755522749 106 LRHCLTGGEALNPDVRDKWKSQTGLELHEGYGQSETvviCGNSR----NSTIKSGSMGKASPPYDVQI--VDEEG-NVLP 178
Cdd:PLN02430 385 LRLLISGGAPLSTEIEEFLRVTSCAFVVQGYGLTET---LGPTTlgfpDEMCMLGTVGAPAVYNELRLeeVPEMGyDPLG 461
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755522749 179 PGKEGNIAVRIKptrpfCFFNCYLDNPEKTAASEQGDFYITGDRAHMDEDGYFWFLGRNDDVINSSSYRIGPVE-VESAL 257
Cdd:PLN02430 462 EPPRGEICVRGK-----CLFSGYYKNPELTEEVMKDGWFHTGDIGEILPNGVLKIIDRKKNLIKLSQGEYVALEyLENVY 536
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755522749 258 AEHPAVLESAVVsspdpirGEVVKAFIVlspAYASHDPEALTR--ELQEHVKTVTAPYKYPR-KVAFISELPKTVSgkil 334
Cdd:PLN02430 537 GQNPIVEDIWVY-------GDSFKSMLV---AVVVPNEENTNKwaKDNGFTGSFEELCSLPElKEHILSELKSTAE---- 602
|
....*....
gi 755522749 335 RSKLRNQEW 343
Cdd:PLN02430 603 KNKLRGFEY 611
|
|
| hsFATP2a_ACSVL_like |
cd05938 |
Fatty acid transport proteins (FATP) including hsFATP2, hsFATP5, and hsFATP6, and similar ... |
113-341 |
3.56e-03 |
|
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: 39.20 E-value: 3.56e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755522749 113 GEALNPDVRDKWKSQTG-LELHEGYGQSEtvvicGN--SRNSTIKSGSMGKAS-------P----PYDVQ----IVDEEG 174
Cdd:cd05938 265 GNGLRADVWREFLRRFGpIRIREFYGSTE-----GNigFFNYTGKIGAVGRVSylykllfPfeliKFDVEkeepVRDAQG 339
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755522749 175 NVLP--PGKEGNIAVRIKPTRPFcffNCYLDNPEKTAAS------EQGDFYI-TGDRAHMDEDGYFWFLGRNDDVINSSS 245
Cdd:cd05938 340 FCIPvaKGEPGLLVAKITQQSPF---LGYAGDKEQTEKKllrdvfKKGDVYFnTGDLLVQDQQNFLYFHDRVGDTFRWKG 416
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755522749 246 YRIGPVEVESALAEHPAVLESAV--VSSPDpIRGEVVKAFIVLSPayashdPEALT-RELQEHVKTVTAPYKYPRKVAFI 322
Cdd:cd05938 417 ENVATTEVADVLGLLDFLQEVNVygVTVPG-HEGRIGMAAVKLKP------GHEFDgKKLYQHVREYLPAYARPRFLRIQ 489
|
250
....*....|....*....
gi 755522749 323 SELPKTVSGKILRSKLRNQ 341
Cdd:cd05938 490 DSLEITGTFKQQKVRLVEE 508
|
|
| |
