|
Name |
Accession |
Description |
Interval |
E-value |
| PRK07445 |
PRK07445 |
O-succinylbenzoic acid--CoA ligase; Reviewed |
42-436 |
0e+00 |
|
O-succinylbenzoic acid--CoA ligase; Reviewed
Pssm-ID: 236019 [Multi-domain] Cd Length: 452 Bit Score: 523.40 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 428688192 42 IFLSTNNPQQFISVFFASIITKSSIFLLNPHWQQEELQQVYKLVKPDFLF-SDHLEK-TYYNPPHNHSYQG-----IMIP 114
Cdd:PRK07445 48 ILLAESDPLQFLAAFLAAVAAGCPVFLANPHWGQQEWQQVLNLVQPDQIWgLDQLKLsHPPPLPSQGILPNletgwIMIP 127
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 428688192 115 TGGTSGNIKFAIHTWETLNASAKGFSQFWQRRKINFFCCLPLYHVSGLMQIVRTFVTGGSLAIYDYSLLKKE-IQNHNYD 193
Cdd:PRK07445 128 TGGSSGQIRFAIHTWETLTASVQGFQRYFQLQQVNSFCVLPLYHVSGLMQFMRSFLTGGKLVILPYKRLKSGqELPPNPS 207
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 428688192 194 NFFISLVPTQLNFLLENFPDWLKKFETVLVGGSATPKTLLQNCYRQKINLALTYGMTETASGVTILKPENFFKGINNSGH 273
Cdd:PRK07445 208 DFFLSLVPTQLQRLLQLRPQWLAQFRTILLGGAPAWPSLLEQARQLQLRLAPTYGMTETASQIATLKPDDFLAGNNSSGQ 287
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 428688192 274 LLPHSQIVIKKNQAkfGQIIIKSDSLFKGYYPHYKNS-NYFLTDDLGYFDQDNFLHIVGRNSQKIISGGENVYPCEIENV 352
Cdd:PRK07445 288 VLPHAQITIPANQT--GNITIQAQSLALGYYPQILDSqGIFETDDLGYLDAQGYLHILGRNSQKIITGGENVYPAEVEAA 365
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 428688192 353 VIKTGLVKDIVVVGKNDHYWGQIICAVYVaisGYDTEYLVNNIKAKLRSHLSHYKIPKLWLKVDQIPRNPQGKIDYGYLE 432
Cdd:PRK07445 366 ILATGLVQDVCVLGLPDPHWGEVVTAIYV---PKDPSISLEELKTAIKDQLSPFKQPKHWIPVPQLPRNPQGKINRQQLQ 442
|
....
gi 428688192 433 KMLT 436
Cdd:PRK07445 443 QIAV 446
|
|
| OSB_MenE-like |
cd17630 |
O-succinylbenzoic acid-CoA ligase; This family contains O-succinylbenzoyl-CoA (OSB-CoA) ... |
111-428 |
2.49e-84 |
|
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: 261.50 E-value: 2.49e-84
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 428688192 111 IMIPTGGTSGNIKFAIHTWETLNASAKGFSQFW-QRRKINFFCCLPLYHVSGLMQIVRTFVTGGSLAIYDYSLLKKEiQN 189
Cdd:cd17630 4 TVILTSGSTGTPKAVVHTAANLLASAAGLHSRLgFGGGDSWLLSLPLYHVGGLAILVRSLLAGAELVLLERNQALAE-DL 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 428688192 190 HNYDNFFISLVPTQLNFLLEN--FPDWLKKFETVLVGGSATPKTLLQNCYRQKINLALTYGMTETASGVTILKPENFFKG 267
Cdd:cd17630 83 APPGVTHVSLVPTQLQRLLDSgqGPAALKSLRAVLLGGAPIPPELLERAADRGIPLYTTYGMTETASQVATKRPDGFGRG 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 428688192 268 inNSGHLLPHSQIVIKKNqakfGQIIIKSDSLFKGYY-----PHYKNSNYFLTDDLGYFDQDNFLHIVGRNSQKIISGGE 342
Cdd:cd17630 163 --GVGVLLPGRELRIVED----GEIWVGGASLAMGYLrgqlvPEFNEDGWFTTKDLGELHADGRLTVLGRADNMIISGGE 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 428688192 343 NVYPCEIENVVIKTGLVKDIVVVGKNDHYWGQIICAVYVaisgYDTEYLVNNIKAKLRSHLSHYKIPKLWLKVDQIPRNP 422
Cdd:cd17630 237 NIQPEEIEAALAAHPAVRDAFVVGVPDEELGQRPVAVIV----GRGPADPAELRAWLKDKLARFKLPKRIYPVPELPRTG 312
|
....*.
gi 428688192 423 QGKIDY 428
Cdd:cd17630 313 GGKVDR 318
|
|
| menE |
TIGR01923 |
O-succinylbenzoate-CoA ligase; This model represents an enzyme, O-succinylbenzoate-CoA ligase, ... |
37-427 |
1.22e-76 |
|
O-succinylbenzoate-CoA ligase; This model represents an enzyme, O-succinylbenzoate-CoA ligase, which is involved in the fourth step of the menaquinone biosynthesis pathway. O-succinylbenzoate-CoA ligase, together with menB - naphtoate synthase, take 2-succinylbenzoate and convert it into 1,4-di-hydroxy-2- naphtoate. [Biosynthesis of cofactors, prosthetic groups, and carriers, Menaquinone and ubiquinone]
Pssm-ID: 162605 [Multi-domain] Cd Length: 436 Bit Score: 245.44 E-value: 1.22e-76
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 428688192 37 QQNRIIFLSTNNPQQFIsVFFASIITKSSIFLLNPHWQQEELQQVYKLVKPDFLFSDHL------------EKTYYNP-P 103
Cdd:TIGR01923 23 SGSRVALVGQNSIEMVL-LLHACLLLGAEIAMLNTRLTENERTNQLEDLDVQLLLTDSLleekdfqadsldRIEAAGRyE 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 428688192 104 HNHSYQGIM------IPTGGTSGNIKFAIHTWETLNASAKGFSQ-FWQRRKINFFCCLPLYHVSGLMQIVRTFVTGGSLA 176
Cdd:TIGR01923 102 TSLSASFNMdqiatlMFTSGTTGKPKAVPHTFRNHYASAVGSKEnLGFTEDDNWLLSLPLYHISGLSILFRWLIEGATLR 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 428688192 177 IYD-YSLLKKEIQNHNYDNffISLVPTQLNFLLE--NFPDWLKKFetvLVGGSATPKTLLQNCYRQKINLALTYGMTETA 253
Cdd:TIGR01923 182 IVDkFNQLLEMIANERVTH--ISLVPTQLNRLLDegGHNENLRKI---LLGGSAIPAPLIEEAQQYGLPIYLSYGMTETC 256
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 428688192 254 SGVTILKPEnFFKGINNSGHLLPHSQIVIKK-NQAKFGQIIIKSDSLFKGYY------PHYKNSNYFLTDDLGYFDQDNF 326
Cdd:TIGR01923 257 SQVTTATPE-MLHARPDVGRPLAGREIKIKVdNKEGHGEIMVKGANLMKGYLyqgeltPAFEQQGWFNTGDIGELDGEGF 335
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 428688192 327 LHIVGRNSQKIISGGENVYPCEIENVVIKTGLVKDIVVVGKNDHYWGQIICAVYVAISGYDTEYLVnnikAKLRSHLSHY 406
Cdd:TIGR01923 336 LYVLGRRDDLIISGGENIYPEEIETVLYQHPGIQEAVVVPKPDAEWGQVPVAYIVSESDISQAKLI----AYLTEKLAKY 411
|
410 420
....*....|....*....|.
gi 428688192 407 KIPKLWLKVDQIPRNPQGKID 427
Cdd:TIGR01923 412 KVPIAFEKLDELPYNASGKIL 432
|
|
| OSB_CoA_lg |
cd05912 |
O-succinylbenzoate-CoA ligase (also known as O-succinylbenzoate-CoA synthase, OSB-CoA ... |
36-426 |
3.06e-73 |
|
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: 235.70 E-value: 3.06e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 428688192 36 NQQNRIIFLSTNNPQQFISVFFASIITKSsIFLLNPHWQQEELQQVYKLVKPDflfsdhLEKTYynpphnhsyqgIMIPT 115
Cdd:cd05912 24 RKGDRVALLSKNSIEMILLIHALWLLGAE-AVLLNTRLTPNELAFQLKDSDVK------LDDIA-----------TIMYT 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 428688192 116 GGTSGNIKFAIHTWETLNASAKGFSQ-FWQRRKINFFCCLPLYHVSGLMQIVRTFVTGGSLAI---YDYSLLKKEIQNHN 191
Cdd:cd05912 86 SGTTGKPKGVQQTFGNHWWSAIGSALnLGLTEDDNWLCALPLFHISGLSILMRSVIYGMTVYLvdkFDAEQVLHLINSGK 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 428688192 192 YDnfFISLVPTQLNFLLENFPDWL-KKFETVLVGGSATPKTLLQNCYRQKINLALTYGMTETASGVTILKPENFFKGINN 270
Cdd:cd05912 166 VT--IISVVPTMLQRLLEILGEGYpNNLRCILLGGGPAPKPLLEQCKEKGIPVYQSYGMTETCSQIVTLSPEDALNKIGS 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 428688192 271 SGHLLPHSQIVIKK-NQAKF--GQIIIKSDSLFKGYY------PHYKNSNYFLTDDLGYFDQDNFLHIVGRNSQKIISGG 341
Cdd:cd05912 244 AGKPLFPVELKIEDdGQPPYevGEILLKGPNVTKGYLnrpdatEESFENGWFKTGDIGYLDEEGFLYVLDRRSDLIISGG 323
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 428688192 342 ENVYPCEIENVVIKTGLVKDIVVVGKNDHYWGQIICAVYVAisgyDTEYLVNNIKAKLRSHLSHYKIPKLWLKVDQIPRN 421
Cdd:cd05912 324 ENIYPAEIEEVLLSHPAIKEAGVVGIPDDKWGQVPVAFVVS----ERPISEEELIAYCSEKLAKYKVPKKIYFVDELPRT 399
|
....*
gi 428688192 422 PQGKI 426
Cdd:cd05912 400 ASGKL 404
|
|
| MenE/FadK |
COG0318 |
O-succinylbenzoic acid-CoA ligase MenE or related acyl-CoA synthetase (AMP-forming) [Lipid ... |
40-435 |
2.78e-68 |
|
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: 223.92 E-value: 2.78e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 428688192 40 RIIFLSTNNPQqFISVFFASIITKSSIFLLNPHWQQEELQQVYKLVKPDFLFSdhlektyynpphnhsyqGIMIPTGGTS 119
Cdd:COG0318 51 RVALLLPNSPE-FVVAFLAALRAGAVVVPLNPRLTAEELAYILEDSGARALVT-----------------ALILYTSGTT 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 428688192 120 GNIKFAIHTWETLNASAKGFSQFWQ-RRKINFFCCLPLYHVSGLMQ-IVRTFVTGGSLAIY---DYSLLKKEIQNHNYDN 194
Cdd:COG0318 113 GRPKGVMLTHRNLLANAAAIAAALGlTPGDVVLVALPLFHVFGLTVgLLAPLLAGATLVLLprfDPERVLELIERERVTV 192
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 428688192 195 FFisLVPTQLNFLLE--NFPDW-LKKFETVLVGGSATPKTLLQNCyRQKINLALT--YGMTETASGVTILKPENFFKGIN 269
Cdd:COG0318 193 LF--GVPTMLARLLRhpEFARYdLSSLRLVVSGGAPLPPELLERF-EERFGVRIVegYGLTETSPVVTVNPEDPGERRPG 269
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 428688192 270 NSGHLLPHSQIVIKKNQAKF------GQIIIKSDSLFKGYYphyKNS---------NYFLTDDLGYFDQDNFLHIVGRNS 334
Cdd:COG0318 270 SVGRPLPGVEVRIVDEDGRElppgevGEIVVRGPNVMKGYW---NDPeataeafrdGWLRTGDLGRLDEDGYLYIVGRKK 346
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 428688192 335 QKIISGGENVYPCEIENVVIKTGLVKDIVVVGKNDHYWGQIICAVYVAISGYDTEylVNNIKAKLRSHLSHYKIPKLWLK 414
Cdd:COG0318 347 DMIISGGENVYPAEVEEVLAAHPGVAEAAVVGVPDEKWGERVVAFVVLRPGAELD--AEELRAFLRERLARYKVPRRVEF 424
|
410 420
....*....|....*....|.
gi 428688192 415 VDQIPRNPQGKIDYGYLEKML 435
Cdd:COG0318 425 VDELPRTASGKIDRRALRERY 445
|
|
| PRK03640 |
PRK03640 |
o-succinylbenzoate--CoA ligase; |
34-426 |
4.27e-64 |
|
o-succinylbenzoate--CoA ligase;
Pssm-ID: 235146 [Multi-domain] Cd Length: 483 Bit Score: 214.06 E-value: 4.27e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 428688192 34 RENQqnRIIFLSTNNPQQFISVFFASIITKSSIFL---LNPH---WQQEELQQVYKLVKPDF----------LFSDhLEK 97
Cdd:PRK03640 50 KKGD--RVALLMKNGMEMILVIHALQQLGAVAVLLntrLSREellWQLDDAEVKCLITDDDFeaklipgisvKFAE-LMN 126
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 428688192 98 TYYNPP------HNHSYQGIMIpTGGTSGNIKFAIHTWETLNASAKGFS-QFWQRRKINFFCCLPLYHVSGLMQIVRTFV 170
Cdd:PRK03640 127 GPKEEAeiqeefDLDEVATIMY-TSGTTGKPKGVIQTYGNHWWSAVGSAlNLGLTEDDCWLAAVPIFHISGLSILMRSVI 205
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 428688192 171 TGGSLAI---YDYSLLKKEIQNHNYDnfFISLVPTQLNFLLENFPD--WLKKFETVLVGGSATPKTLLQNCYRQKINLAL 245
Cdd:PRK03640 206 YGMRVVLvekFDAEKINKLLQTGGVT--IISVVSTMLQRLLERLGEgtYPSSFRCMLLGGGPAPKPLLEQCKEKGIPVYQ 283
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 428688192 246 TYGMTETASGVTILKPENFFKGINNSGHLLPHSQIVIKKNQ-----AKFGQIIIKSDSLFKGYYpHYKNSN-------YF 313
Cdd:PRK03640 284 SYGMTETASQIVTLSPEDALTKLGSAGKPLFPCELKIEKDGvvvppFEEGEIVVKGPNVTKGYL-NREDATretfqdgWF 362
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 428688192 314 LTDDLGYFDQDNFLHIVGRNSQKIISGGENVYPCEIENVVIKTGLVKDIVVVGKNDHYWGQIICAVYVAisgyDTEYLVN 393
Cdd:PRK03640 363 KTGDIGYLDEEGFLYVLDRRSDLIISGGENIYPAEIEEVLLSHPGVAEAGVVGVPDDKWGQVPVAFVVK----SGEVTEE 438
|
410 420 430
....*....|....*....|....*....|...
gi 428688192 394 NIKAKLRSHLSHYKIPKLWLKVDQIPRNPQGKI 426
Cdd:PRK03640 439 ELRHFCEEKLAKYKVPKRFYFVEELPRNASGKL 471
|
|
| AFD_class_I |
cd04433 |
Adenylate forming domain, Class I, also known as the ANL superfamily; This family is known as ... |
112-427 |
1.12e-61 |
|
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: 203.29 E-value: 1.12e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 428688192 112 MIPTGGTSGNIKFAIHTWETLNASAKGFSQ-FWQRRKINFFCCLPLYHVSGLMQIVRTFVTGGSLAIYDYS---LLKKEI 187
Cdd:cd04433 5 ILYTSGTTGKPKGVVLSHRNLLAAAAALAAsGGLTEGDVFLSTLPLFHIGGLFGLLGALLAGGTVVLLPKFdpeAALELI 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 428688192 188 QNHNYDNFFisLVPTQLNFLLE--NFPDW-LKKFETVLVGGSATPKTLLQNcYRQKINLALT--YGMTETASGVTILKPE 262
Cdd:cd04433 85 EREKVTILL--GVPTLLARLLKapESAGYdLSSLRALVSGGAPLPPELLER-FEEAPGIKLVngYGLTETGGTVATGPPD 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 428688192 263 NFFKGINNSGHLLPHSQIVIKKNQAKF------GQIIIKSDSLFKGYYPHYKNSN------YFLTDDLGYFDQDNFLHIV 330
Cdd:cd04433 162 DDARKPGSVGRPVPGVEVRIVDPDGGElppgeiGELVVRGPSVMKGYWNNPEATAavdedgWYRTGDLGRLDEDGYLYIV 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 428688192 331 GRNSQKIISGGENVYPCEIENVVIKTGLVKDIVVVGKNDHYWGQIICAVYVAISGYDTeyLVNNIKAKLRSHLSHYKIPK 410
Cdd:cd04433 242 GRLKDMIKSGGENVYPAEVEAVLLGHPGVAEAAVVGVPDPEWGERVVAVVVLRPGADL--DAEELRAHVRERLAPYKVPR 319
|
330
....*....|....*..
gi 428688192 411 LWLKVDQIPRNPQGKID 427
Cdd:cd04433 320 RVVFVDALPRTASGKID 336
|
|
| FACL_FadD13-like |
cd17631 |
fatty acyl-CoA synthetase, including FadD13; This family contains fatty acyl-CoA synthetases, ... |
39-427 |
2.04e-56 |
|
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: 192.44 E-value: 2.04e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 428688192 39 NRIIFLSTNNPQQFISVFFASIItkSSIFL-LNPHWQQEELQQVYKLVKPDFLFSDhlektyynpphnhsYQGIMIpTGG 117
Cdd:cd17631 46 DRVAVLSKNSPEFLELLFAAARL--GAVFVpLNFRLTPPEVAYILADSGAKVLFDD--------------LALLMY-TSG 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 428688192 118 TSGNIKFAIHTWETL--NASAKGFSQFWQRRKInFFCCLPLYHVSGL-MQIVRTFVTGGSLAI---YDYSLLKKEIQNHN 191
Cdd:cd17631 109 TTGRPKGAMLTHRNLlwNAVNALAALDLGPDDV-LLVVAPLFHIGGLgVFTLPTLLRGGTVVIlrkFDPETVLDLIERHR 187
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 428688192 192 YDNFFisLVPTQLNFLLeNFPDW----LKKFETVLVGGSATPKTLLQNCYRQKINLALTYGMTETASGVTILKPENFFKG 267
Cdd:cd17631 188 VTSFF--LVPTMIQALL-QHPRFattdLSSLRAVIYGGAPMPERLLRALQARGVKFVQGYGMTETSPGVTFLSPEDHRRK 264
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 428688192 268 INNSGHLLPHSQI-VIKKNQAKF-----GQIIIKSDSLFKGYYphyKNS---------NYFLTDDLGYFDQDNFLHIVGR 332
Cdd:cd17631 265 LGSAGRPVFFVEVrIVDPDGREVppgevGEIVVRGPHVMAGYW---NRPeataaafrdGWFHTGDLGRLDEDGYLYIVDR 341
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 428688192 333 NSQKIISGGENVYPCEIENVVIKTGLVKDIVVVGKNDHYWGQIICAVYVAISGydTEYLVNNIKAKLRSHLSHYKIPKLW 412
Cdd:cd17631 342 KKDMIISGGENVYPAEVEDVLYEHPAVAEVAVIGVPDEKWGEAVVAVVVPRPG--AELDEDELIAHCRERLARYKIPKSV 419
|
410
....*....|....*
gi 428688192 413 LKVDQIPRNPQGKID 427
Cdd:cd17631 420 EFVDALPRNATGKIL 434
|
|
| PRK06187 |
PRK06187 |
long-chain-fatty-acid--CoA ligase; Validated |
111-427 |
7.54e-45 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 235730 [Multi-domain] Cd Length: 521 Bit Score: 163.43 E-value: 7.54e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 428688192 111 IMIPTGGTSGNIKFAIHT----WETLNASAKGFSqfWqRRKINFFCCLPLYHVSGLMQIVRTFVTGGSLAI---YDYSLL 183
Cdd:PRK06187 171 AMLYTSGTTGHPKGVVLShrnlFLHSLAVCAWLK--L-SRDDVYLVIVPMFHVHAWGLPYLALMAGAKQVIprrFDPENL 247
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 428688192 184 KKEIQNHNYDNFFisLVPTQLNFLLEN---FPDWLKKFETVLVGGSATPKTLLQNCY-RQKINLALTYGMTETASGVTIL 259
Cdd:PRK06187 248 LDLIETERVTFFF--AVPTIWQMLLKApraYFVDFSSLRLVIYGGAALPPALLREFKeKFGIDLVQGYGMTETSPVVSVL 325
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 428688192 260 KPENFFKGINN----SGHLLPHSQIVIKKNQAKF--------GQIIIKSDSLFKGYYPHYKNS------NYFLTDDLGYF 321
Cdd:PRK06187 326 PPEDQLPGQWTkrrsAGRPLPGVEARIVDDDGDElppdggevGEIIVRGPWLMQGYWNRPEATaetidgGWLHTGDVGYI 405
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 428688192 322 DQDNFLHIVGRNSQKIISGGENVYPCEIENVVIKTGLVKDIVVVGKNDHYWGQIICAVYVAISGYDTEylVNNIKAKLRS 401
Cdd:PRK06187 406 DEDGYLYITDRIKDVIISGGENIYPRELEDALYGHPAVAEVAVIGVPDEKWGERPVAVVVLKPGATLD--AKELRAFLRG 483
|
330 340
....*....|....*....|....*.
gi 428688192 402 HLSHYKIPKLWLKVDQIPRNPQGKID 427
Cdd:PRK06187 484 RLAKFKLPKRIAFVDELPRTSVGKIL 509
|
|
| FC-FACS_FadD_like |
cd05936 |
Prokaryotic long-chain fatty acid CoA synthetases similar to Escherichia coli FadD; This ... |
115-427 |
5.09e-41 |
|
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: 151.95 E-value: 5.09e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 428688192 115 TGGTSGNIKFAIHTWETL--NASA-KGFSQFWQRRKINFFCCLPLYHVSGLMQIVRTFVTGGSLAIY-----DYSLLKkE 186
Cdd:cd05936 133 TSGTTGVPKGAMLTHRNLvaNALQiKAWLEDLLEGDDVVLAALPLFHVFGLTVALLLPLALGATIVLiprfrPIGVLK-E 211
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 428688192 187 IQNHNYdNFFISlVPTQLNFLLeNFPD----WLKKFETVLVGGSATPKTLLQNCyRQKINLALT--YGMTETASGVTIlk 260
Cdd:cd05936 212 IRKHRV-TIFPG-VPTMYIALL-NAPEfkkrDFSSLRLCISGGAPLPVEVAERF-EELTGVPIVegYGLTETSPVVAV-- 285
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 428688192 261 peNFFKGINNS---GHLLPHSQIVIKKNQAKF------GQIIIKSDSLFKGYYPHYKNS------NYFLTDDLGYFDQDN 325
Cdd:cd05936 286 --NPLDGPRKPgsiGIPLPGTEVKIVDDDGEElppgevGELWVRGPQVMKGYWNRPEETaeafvdGWLRTGDIGYMDEDG 363
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 428688192 326 FLHIVGRNSQKIISGGENVYPCEIENVVIKTGLVKDIVVVGKNDHYWGQIICAVYVAISGYD-TEylvNNIKAKLRSHLS 404
Cdd:cd05936 364 YFFIVDRKKDMIIVGGFNVYPREVEEVLYEHPAVAEAAVVGVPDPYSGEAVKAFVVLKEGASlTE---EEIIAFCREQLA 440
|
330 340
....*....|....*....|...
gi 428688192 405 HYKIPKLWLKVDQIPRNPQGKID 427
Cdd:cd05936 441 GYKVPRQVEFRDELPKSAVGKIL 463
|
|
| AFD_YhfT-like |
cd17633 |
fatty acid-CoA ligase VraA; This family of acyl-CoA ligases includes Bacillus subtilis YhfT, ... |
155-427 |
9.80e-39 |
|
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: 142.16 E-value: 9.80e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 428688192 155 PLYHVSGLMQIVRTFVTGGSLAI---YDYSLLKKEIQNHNYDNFFisLVPTQLNFLL-ENFPDwlKKFETVLVGGSATPK 230
Cdd:cd17633 49 PLSHSLFLYGAISALYLGGTFIGqrkFNPKSWIRKINQYNATVIY--LVPTMLQALArTLEPE--SKIKSIFSSGQKLFE 124
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 428688192 231 TLLQNCYRQ--KINLALTYGMTEtASGVTILKPENFFKgINNSGHLLPHSQIVIKkNQA--KFGQIIIKSDSLFKGYYP- 305
Cdd:cd17633 125 STKKKLKNIfpKANLIEFYGTSE-LSFITYNFNQESRP-PNSVGRPFPNVEIEIR-NADggEIGKIFVKSEMVFSGYVRg 201
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 428688192 306 -HYKNSNYFLTDDLGYFDQDNFLHIVGRNSQKIISGGENVYPCEIENVVIKTGLVKDIVVVGKNDHYWGQIICAVYVAIS 384
Cdd:cd17633 202 gFSNPDGWMSVGDIGYVDEEGYLYLVGRESDMIIIGGINIFPTEIESVLKAIPGIEEAIVVGIPDARFGEIAVALYSGDK 281
|
250 260 270 280
....*....|....*....|....*....|....*....|...
gi 428688192 385 GYDTeylvnNIKAKLRSHLSHYKIPKLWLKVDQIPRNPQGKID 427
Cdd:cd17633 282 LTYK-----QLKRFLKQKLSRYEIPKKIIFVDSLPYTSSGKIA 319
|
|
| PRK09029 |
PRK09029 |
O-succinylbenzoic acid--CoA ligase; Provisional |
66-413 |
1.80e-36 |
|
O-succinylbenzoic acid--CoA ligase; Provisional
Pssm-ID: 236363 [Multi-domain] Cd Length: 458 Bit Score: 139.24 E-value: 1.80e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 428688192 66 IFLLNPHWQQEELQQVYKLVKPDFLFSDHLEKTY----------YNPPHNHSYQGI----MIPTGGTSGNIKFAIHTWET 131
Cdd:PRK09029 80 VLPLNPQLPQPLLEELLPSLTLDFALVLEGENTFsaltslhlqlVEGAHAVAWQPQrlatMTLTSGSTGLPKAAVHTAQA 159
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 428688192 132 LNASAKGFSQFwqrrkINFFCC------LPLYHVSGLMQIVRTFVTGGSLAIYDYSLLKKEIQN--HnydnffISLVPTQ 203
Cdd:PRK09029 160 HLASAEGVLSL-----MPFTAQdswllsLPLFHVSGQGIVWRWLYAGATLVVRDKQPLEQALAGctH------ASLVPTQ 228
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 428688192 204 LNFLLEN--FPDWLKKfetVLVGGSATPKTLLQNCYRQKINLALTYGMTETASGVTILKPEnffkGINNSGHLLPHSQIV 281
Cdd:PRK09029 229 LWRLLDNrsEPLSLKA---VLLGGAAIPVELTEQAEQQGIRCWCGYGLTEMASTVCAKRAD----GLAGVGSPLPGREVK 301
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 428688192 282 IKKnqakfGQIIIKSDSLFKGYY------PHYKNSNYFLTDDLGYFDQDNfLHIVGRNSQKIISGGENVYPCEIENVVIK 355
Cdd:PRK09029 302 LVD-----GEIWLRGASLALGYWrqgqlvPLVNDEGWFATRDRGEWQNGE-LTILGRLDNLFFSGGEGIQPEEIERVINQ 375
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*...
gi 428688192 356 TGLVKDIVVVGKNDHYWGQiicaVYVAISGYDTEYLVNNIKAKLRSHLSHYKIPKLWL 413
Cdd:PRK09029 376 HPLVQQVFVVPVADAEFGQ----RPVAVVESDSEAAVVNLAEWLQDKLARFQQPVAYY 429
|
|
| PRK07638 |
PRK07638 |
acyl-CoA synthetase; Validated |
34-435 |
3.50e-35 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236071 [Multi-domain] Cd Length: 487 Bit Score: 136.06 E-value: 3.50e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 428688192 34 RENQQNRIIFLSTNNpQQFISVFFASIITKSSIFLLNPHWQQEELQQVYKLVKPDFLFSDHLEK---------------- 97
Cdd:PRK07638 46 KESKNKTIAILLENR-IEFLQLFAGAAMAGWTCVPLDIKWKQDELKERLAISNADMIVTERYKLndlpdeegrvieidew 124
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 428688192 98 ---------TYY---NPPHNHSYQGImipTGGTSGNIK-F--AIHTW-ETLNASAKGFSQFWQRRKI---NFFCCLPLY- 157
Cdd:PRK07638 125 krmiekylpTYApieNVQNAPFYMGF---TSGSTGKPKaFlrAQQSWlHSFDCNVHDFHMKREDSVLiagTLVHSLFLYg 201
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 428688192 158 -----HVSGLMQIVRTFVTGGSLaiydySLLKKEiqnhnyDNFFISLVPTQLNFLL--ENFPDWLKKfetVLVGGSATPK 230
Cdd:PRK07638 202 aistlYVGQTVHLMRKFIPNQVL-----DKLETE------NISVMYTVPTMLESLYkeNRVIENKMK---IISSGAKWEA 267
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 428688192 231 TLLQNCYRQKINLALT--YGMTETaSGVTILKPENFFKGINNSGHLLPHSQIVIKKNQAK------FGQIIIKSDSLFKG 302
Cdd:PRK07638 268 EAKEKIKNIFPYAKLYefYGASEL-SFVTALVDEESERRPNSVGRPFHNVQVRICNEAGEevqkgeIGTVYVKSPQFFMG 346
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 428688192 303 Y-----YPHYKNSNYFLT-DDLGYFDQDNFLHIVGRNSQKIISGGENVYPCEIENVVIKTGLVKDIVVVGKNDHYWGQII 376
Cdd:PRK07638 347 YiiggvLARELNADGWMTvRDVGYEDEEGFIYIVGREKNMILFGGINIFPEEIESVLHEHPAVDEIVVIGVPDSYWGEKP 426
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*....
gi 428688192 377 CAVyvaISGYDTeylVNNIKAKLRSHLSHYKIPKLWLKVDQIPRNPQGKIDYGYLEKML 435
Cdd:PRK07638 427 VAI---IKGSAT---KQQLKSFCLQRLSSFKIPKEWHFVDEIPYTNSGKIARMEAKSWI 479
|
|
| LC_FACS_like |
cd05935 |
Putative long-chain fatty acid CoA ligase; The members of this family are putative long-chain ... |
48-426 |
6.26e-34 |
|
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: 131.83 E-value: 6.26e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 428688192 48 NPQQFISVFFASIITKSSIFLLNPHWQQEELQqvyklvkpdFLFSDHLEKTYYNpphnHSYQG--IMIP-TGGTSGNIKF 124
Cdd:cd05935 35 NSPQYVIAYFAIWRANAVVVPINPMLKERELE---------YILNDSGAKVAVV----GSELDdlALIPyTSGTTGLPKG 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 428688192 125 AIHTWETLNASAKGfSQFWQRRKIN--FFCCLPLYHVSGLMQIVRTFVTGGS----LAIYDYSLLKKEIQNhnYDNFFIS 198
Cdd:cd05935 102 CMHTHFSAAANALQ-SAVWTGLTPSdvILACLPLFHVTGFVGSLNTAVYVGGtyvlMARWDRETALELIEK--YKVTFWT 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 428688192 199 LVPTQLNFLLE--NFPDW-LKKFETVLVGGSATPKTLLQNCY-RQKINLALTYGMTETASGVTI---LKPENFFKGINNS 271
Cdd:cd05935 179 NIPTMLVDLLAtpEFKTRdLSSLKVLTGGGAPMPPAVAEKLLkLTGLRFVEGYGLTETMSQTHTnppLRPKLQCLGIP*F 258
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 428688192 272 GHLL----PHSQIVIKKNQAkfGQIIIKSDSLFKGYYP----------HYKNSNYFLTDDLGYFDQDNFLHIVGRNSQKI 337
Cdd:cd05935 259 GVDArvidIETGRELPPNEV--GEIVVRGPQIFKGYWNrpeeteesfiEIKGRRFFRTGDLGYMDEEGYFFFVDRVKRMI 336
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 428688192 338 ISGGENVYPCEIENVVIKTGLVKDIVVVGKNDHYWGQIICAVYVAISGYDTEYLVNNIKAKLRSHLSHYKIPKLWLKVDQ 417
Cdd:cd05935 337 NVSGFKVWPAEVEAKLYKHPAI*EVCVISVPDERVGEEVKAFIVLRPEYRGKVTEEDIIEWAREQMAAYKYPREVEFVDE 416
|
....*....
gi 428688192 418 IPRNPQGKI 426
Cdd:cd05935 417 LPRSASGKI 425
|
|
| MCS |
cd05941 |
Malonyl-CoA synthetase (MCS); MCS catalyzes the formation of malonyl-CoA in a two-step ... |
112-427 |
2.75e-33 |
|
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: 130.10 E-value: 2.75e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 428688192 112 MIPTGGTSGNIKFAIHTWETLNASAKGFSQFWQRRKIN-FFCCLPLYHVSGLMQIVR-TFVTGGSL--------AIYDYS 181
Cdd:cd05941 94 ILYTSGTTGRPKGVVLTHANLAANVRALVDAWRWTEDDvLLHVLPLHHVHGLVNALLcPLFAGASVeflpkfdpKEVAIS 173
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 428688192 182 LLKKEIqnhnydNFFISlVPTQLNFLLE----NFPDWLKK----FETV--LVGGSATPKTLLQNCYRQKINLALT--YGM 249
Cdd:cd05941 174 RLMPSI------TVFMG-VPTIYTRLLQyyeaHFTDPQFAraaaAERLrlMVSGSAALPVPTLEEWEAITGHTLLerYGM 246
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 428688192 250 TETasgvtilkpenffkGINNSGHL------------LPHSQIVIKK-------NQAKFGQIIIKSDSLFKGYY--PH-- 306
Cdd:cd05941 247 TEI--------------GMALSNPLdgerrpgtvgmpLPGVQARIVDeetgeplPRGEVGEIQVRGPSVFKEYWnkPEat 312
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 428688192 307 ---YKNSNYFLTDDLGYFDQDNFLHIVGRNSQKII-SGGENVYPCEIENVVIKTGLVKDIVVVGKNDHYWGQIICAVYVA 382
Cdd:cd05941 313 keeFTDDGWFKTGDLGVVDEDGYYWILGRSSVDIIkSGGYKVSALEIERVLLAHPGVSECAVIGVPDPDWGERVVAVVVL 392
|
330 340 350 360
....*....|....*....|....*....|....*....|....*...
gi 428688192 383 ISGY---DTEYLVNNIKAKlrshLSHYKIPKLWLKVDQIPRNPQGKID 427
Cdd:cd05941 393 RAGAaalSLEELKEWAKQR----LAPYKRPRRLILVDELPRNAMGKVN 436
|
|
| Firefly_Luc_like |
cd05911 |
Firefly luciferase of light emitting insects and 4-Coumarate-CoA Ligase (4CL); This family ... |
36-426 |
1.20e-31 |
|
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: 126.17 E-value: 1.20e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 428688192 36 NQQNRIIFLSTNNPQQFISVFFASIITKSSIFLLNPHWQQEELQQVYKLVKPDFLFSDH--LEK---------------T 98
Cdd:cd05911 32 LKKGDVVGIISPNSTYYPPVFLGCLFAGGIFSAANPIYTADELAHQLKISKPKVIFTDPdgLEKvkeaakelgpkdkiiV 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 428688192 99 YYNPPHNHSYQGIM-------------------------IP-TGGTSGNIKFAIHTWETLNA---SAKGFSQFWQRRKIN 149
Cdd:cd05911 112 LDDKPDGVLSIEDLlsptlgeededlppplkdgkddtaaILySSGTTGLPKGVCLSHRNLIAnlsQVQTFLYGNDGSNDV 191
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 428688192 150 FFCCLPLYHVSGLMQIVRTFVTGGSLAI---YDYSLLKKEIQNHNYDnfFISLVPTQLNFLLENfPDwLKKF-----ETV 221
Cdd:cd05911 192 ILGFLPLYHIYGLFTTLASLLNGATVIImpkFDSELFLDLIEKYKIT--FLYLVPPIAAALAKS-PL-LDKYdlsslRVI 267
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 428688192 222 LVGGSATPKTLLQNCYRQKINLALT--YGMTETASGVTILKPENFFKGinNSGHLLPHSQIVI-----KKNQA--KFGQI 292
Cdd:cd05911 268 LSGGAPLSKELQELLAKRFPNATIKqgYGMTETGGILTVNPDGDDKPG--SVGRLLPNVEAKIvdddgKDSLGpnEPGEI 345
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 428688192 293 IIKSDSLFKGYYphyKN----------SNYFLTDDLGYFDQDNFLHIVGRNSQKIISGGENVYPCEIENVVIKTGLVKDI 362
Cdd:cd05911 346 CVRGPQVMKGYY---NNpeatketfdeDGWLHTGDIGYFDEDGYLYIVDRKKELIKYKGFQVAPAELEAVLLEHPGVADA 422
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 428688192 363 VVVGKNDHYWGQIICAVYVAISGYD-TEylvNNIKAKLRSHLSHYKipklWLK-----VDQIPRNPQGKI 426
Cdd:cd05911 423 AVIGIPDEVSGELPRAYVVRKPGEKlTE---KEVKDYVAKKVASYK----QLRggvvfVDEIPKSASGKI 485
|
|
| PRK06839 |
PRK06839 |
o-succinylbenzoate--CoA ligase; |
103-436 |
2.51e-31 |
|
o-succinylbenzoate--CoA ligase;
Pssm-ID: 168698 [Multi-domain] Cd Length: 496 Bit Score: 125.36 E-value: 2.51e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 428688192 103 PHNHSYQGIMIPTGGTSGNIKFAIHTWETLnasakgfsqFWQRRKiNFF--------CC---LPLYHVSGL-MQIVRTFV 170
Cdd:PRK06839 145 EKNESASFIICYTSGTTGKPKGAVLTQENM---------FWNALN-NTFaidltmhdRSivlLPLFHIGGIgLFAFPTLF 214
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 428688192 171 TGGSLAI---YDYSLLKKEIQNHNYDNFFisLVPTQLNFLLENfPDWLK-KFETVLV---GGSATPKTLLQNCYRQKINL 243
Cdd:PRK06839 215 AGGVIIVprkFEPTKALSMIEKHKVTVVM--GVPTIHQALINC-SKFETtNLQSVRWfynGGAPCPEELMREFIDRGFLF 291
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 428688192 244 ALTYGMTETASGVTILKPENFFKGINNSGHLLPHSQI-VIKKN-----QAKFGQIIIKSDSLFKGYYPHYKNS------N 311
Cdd:PRK06839 292 GQGFGMTETSPTVFMLSEEDARRKVGSIGKPVLFCDYeLIDENknkveVGEVGELLIRGPNVMKEYWNRPDATeetiqdG 371
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 428688192 312 YFLTDDLGYFDQDNFLHIVGRNSQKIISGGENVYPCEIENVVIKTGLVKDIVVVGKNDHYWGQIICAVYVAISGYD-TEy 390
Cdd:PRK06839 372 WLCTGDLARVDEDGFVYIVGRKKEMIISGGENIYPLEVEQVINKLSDVYEVAVVGRQHVKWGEIPIAFIVKKSSSVlIE- 450
|
330 340 350 360
....*....|....*....|....*....|....*....|....*.
gi 428688192 391 lvNNIKAKLRSHLSHYKIPKLWLKVDQIPRNPQGKIDYGYLEKMLT 436
Cdd:PRK06839 451 --KDVIEHCRLFLAKYKIPKEIVFLKELPKNATGKIQKAQLVNQLK 494
|
|
| FACL_like_2 |
cd05917 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
152-426 |
6.93e-31 |
|
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: 121.62 E-value: 6.93e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 428688192 152 CCLPLYHVSGLMQIVRTFVTGGSLAI-----YDYSLLKKEIQN------HNYDNFFISLV--PTQLNFllenfpDwLKKF 218
Cdd:cd05917 48 IPVPLFHCFGSVLGVLACLTHGATMVfpspsFDPLAVLEAIEKekctalHGVPTMFIAELehPDFDKF------D-LSSL 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 428688192 219 ETVLVGGSATPKTLLQNCyRQKINLA---LTYGMTETASGVTILKPEN-FFKGINNSGHLLPHSQ---------IVIKKN 285
Cdd:cd05917 121 RTGIMAGAPCPPELMKRV-IEVMNMKdvtIAYGMTETSPVSTQTRTDDsIEKRVNTVGRIMPHTEakivdpeggIVPPVG 199
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 428688192 286 QAkfGQIIIKSDSLFKGYYPH-------YKNSNYFLTDDLGYFDQDNFLHIVGRNSQKIISGGENVYPCEIENVVIKTGL 358
Cdd:cd05917 200 VP--GELCIRGYSVMKGYWNDpektaeaIDGDGWLHTGDLAVMDEDGYCRIVGRIKDMIIRGGENIYPREIEEFLHTHPK 277
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 428688192 359 VKDIVVVGKNDHYWGQIICAVYVAISGydTEYLVNNIKAKLRSHLSHYKIPKLWLKVDQIPRNPQGKI 426
Cdd:cd05917 278 VSDVQVVGVPDERYGEEVCAWIRLKEG--AELTEEDIKAYCKGKIAHYKVPRYVFFVDEFPLTVSGKI 343
|
|
| FACL_fum10p_like |
cd05926 |
Subfamily of fatty acid CoA ligase (FACL) similar to Fum10p of Gibberella moniliformis; FACL ... |
151-427 |
5.35e-30 |
|
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: 121.65 E-value: 5.35e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 428688192 151 FCCLPLYHVSGLMQIV-RTFVTGGSLAI---YDYSLLKKEIQNHNYdNFFiSLVPTQLNFLLEN-------------F-- 211
Cdd:cd05926 194 LVVMPLFHVHGLVASLlSTLAAGGSVVLpprFSASTFWPDVRDYNA-TWY-TAVPTIHQILLNRpepnpespppklrFir 271
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 428688192 212 -------PDWLKKFETVLvggsATPktLLQncyrqkinlalTYGMTETASGVTilkpENFFkginNSGHLLPHS------ 278
Cdd:cd05926 272 scsaslpPAVLEALEATF----GAP--VLE-----------AYGMTEAAHQMT----SNPL----PPGPRKPGSvgkpvg 326
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 428688192 279 -QIVI------KKNQAKFGQIIIKSDSLFKGYYPHYKNSN-------YFLTDDLGYFDQDNFLHIVGRNSQKIISGGENV 344
Cdd:cd05926 327 vEVRIldedgeILPPGVVGEICLRGPNVTRGYLNNPEANAeaafkdgWFRTGDLGYLDADGYLFLTGRIKELINRGGEKI 406
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 428688192 345 YPCEIENVVIKTGLVKDIVVVGKNDHYWGQIICAVYVAISGYdtEYLVNNIKAKLRSHLSHYKIPKLWLKVDQIPRNPQG 424
Cdd:cd05926 407 SPLEVDGVLLSHPAVLEAVAFGVPDEKYGEEVAAAVVLREGA--SVTEEELRAFCRKHLAAFKVPKKVYFVDELPKTATG 484
|
...
gi 428688192 425 KID 427
Cdd:cd05926 485 KIQ 487
|
|
| ttLC_FACS_AEE21_like |
cd12118 |
Fatty acyl-CoA synthetases similar to LC-FACS from Thermus thermophiles and Arabidopsis; This ... |
115-426 |
2.99e-29 |
|
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: 119.33 E-value: 2.99e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 428688192 115 TGGTSGNIKFAIHTWET--LNASAKGfsQFWQRRKIN-FFCCLPLYHVSGLMQIVRTFVTGGS---LAIYDYSLLKKEIQ 188
Cdd:cd12118 141 TSGTTGRPKGVVYHHRGayLNALANI--LEWEMKQHPvYLWTLPMFHCNGWCFPWTVAAVGGTnvcLRKVDAKAIYDLIE 218
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 428688192 189 NHNYDNFfiSLVPTQLNFLLENFPDWLKKFE---TVLVGGSATPKTLLQNCYRQKINLALTYGMTETASGVTI--LKPE- 262
Cdd:cd12118 219 KHKVTHF--CGAPTVLNMLANAPPSDARPLPhrvHVMTAGAPPPAAVLAKMEELGFDVTHVYGLTETYGPATVcaWKPEw 296
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 428688192 263 -----------NFFKGINNSGH-----LLPHSQIVIKKNQAKFGQIIIKSDSLFKGYYphyKNSN---------YFLTDD 317
Cdd:cd12118 297 delpteerarlKARQGVRYVGLeevdvLDPETMKPVPRDGKTIGEIVFRGNIVMKGYL---KNPEataeafrggWFHSGD 373
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 428688192 318 LGYFDQDNFLHIVGRNSQKIISGGENVYPCEIENVVIKTGLVKDIVVVGKNDHYWGQIICAVYVAISGYDTeyLVNNIKA 397
Cdd:cd12118 374 LAVIHPDGYIEIKDRSKDIIISGGENISSVEVEGVLYKHPAVLEAAVVARPDEKWGEVPCAFVELKEGAKV--TEEEIIA 451
|
330 340
....*....|....*....|....*....
gi 428688192 398 KLRSHLSHYKIPKLwLKVDQIPRNPQGKI 426
Cdd:cd12118 452 FCREHLAGFMVPKT-VVFGELPKTSTGKI 479
|
|
| FADD10 |
cd17635 |
adenylate forming domain, fatty acid CoA ligase (FadD10); This family contains long chain ... |
154-426 |
1.46e-28 |
|
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: 115.05 E-value: 1.46e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 428688192 154 LPLYHVSGLMQIVRTFVTGGSLAIY----DYSLLKKEIQNhnYDNFFISLVPTQLNFLLENFPDWLK---KFETVLVGGS 226
Cdd:cd17635 50 LPATHIGGLWWILTCLIHGGLCVTGgentTYKSLFKILTT--NAVTTTCLVPTLLSKLVSELKSANAtvpSLRLIGYGGS 127
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 428688192 227 ATPKTLLQNCYRQK-INLALTYGMTETaSGVTILKPENFFKGINNSGHLLPHSQIVIKKN------QAKFGQIIIKSDSL 299
Cdd:cd17635 128 RAIAADVRFIEATGlTNTAQVYGLSET-GTALCLPTDDDSIEINAVGRPYPGVDVYLAATdgiagpSASFGTIWIKSPAN 206
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 428688192 300 FKGYYPHYKNS------NYFLTDDLGYFDQDNFLHIVGRNSQKIISGGENVYPCEIENVVIKTGLVKDIVVVGKNDHYWG 373
Cdd:cd17635 207 MLGYWNNPERTaevlidGWVNTGDLGERREDGFLFITGRSSESINCGGVKIAPDEVERIAEGVSGVQECACYEISDEEFG 286
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|...
gi 428688192 374 QIICAvYVAISGYDTEYLVNNIKAKLRSHLSHYKIPKLWLKVDQIPRNPQGKI 426
Cdd:cd17635 287 ELVGL-AVVASAELDENAIRALKHTIRRELEPYARPSTIVIVTDIPRTQSGKV 338
|
|
| PRK07824 |
PRK07824 |
o-succinylbenzoate--CoA ligase; |
110-436 |
2.13e-28 |
|
o-succinylbenzoate--CoA ligase;
Pssm-ID: 236108 [Multi-domain] Cd Length: 358 Bit Score: 114.76 E-value: 2.13e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 428688192 110 GIMIPTGGTSGNIKFAIHTWETLNASAKGFSQF------WqrrkinfFCCLPLYHVSGLMQIVRTFVTGGSLAIYDYSL- 182
Cdd:PRK07824 38 ALVVATSGTTGTPKGAMLTAAALTASADATHDRlggpgqW-------LLALPAHHIAGLQVLVRSVIAGSEPVELDVSAg 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 428688192 183 -----LKKEIQNHNYDNFFISLVPTQLNFLLENFP--DWLKKFETVLVGGSATPKTLLQNCYRQKINLALTYGMTETASG 255
Cdd:PRK07824 111 fdptaLPRAVAELGGGRRYTSLVPMQLAKALDDPAatAALAELDAVLVGGGPAPAPVLDAAAAAGINVVRTYGMSETSGG 190
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 428688192 256 VTIlkpenffkginnSGHLLPHSQIVIKKnqakfGQIIIKSDSLFKGY-----YPHYKNSNYFLTDDLGYFDqDNFLHIV 330
Cdd:PRK07824 191 CVY------------DGVPLDGVRVRVED-----GRIALGGPTLAKGYrnpvdPDPFAEPGWFRTDDLGALD-DGVLTVL 252
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 428688192 331 GRNSQKIISGGENVYPCEIENVVIKTGLVKDIVVVGKNDHYWGQIICAVYVAiSGYDTEYLvnnikAKLRSH----LSHY 406
Cdd:PRK07824 253 GRADDAISTGGLTVLPQVVEAALATHPAVADCAVFGLPDDRLGQRVVAAVVG-DGGPAPTL-----EALRAHvartLDRT 326
|
330 340 350
....*....|....*....|....*....|
gi 428688192 407 KIPKLWLKVDQIPRNPQGKIDYGYLEKMLT 436
Cdd:PRK07824 327 AAPRELHVVDELPRRGIGKVDRRALVRRFA 356
|
|
| CHC_CoA_lg |
cd05903 |
Cyclohexanecarboxylate-CoA ligase (also called cyclohex-1-ene-1-carboxylate:CoA ligase); ... |
48-426 |
3.68e-28 |
|
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: 115.56 E-value: 3.68e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 428688192 48 NPQQFISVFFASIITKSSIFLLNPHWQQEELQQVYKLVKPDFLFSDHLEKTyynppHNHSYQG----IMIPTGGTSGNIK 123
Cdd:cd05903 35 NWWEFAVLYLACLRIGAVTNPILPFFREHELAFILRRAKAKVFVVPERFRQ-----FDPAAMPdavaLLLFTSGTTGEPK 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 428688192 124 FAIHTWETLNASAKGFSQFWQ-RRKINFFCCLPLYHVSGLMQIVRTFVTGGSLAIY------DYSLlkkEIQNHNYDNFF 196
Cdd:cd05903 110 GVMHSHNTLSASIRQYAERLGlGPGDVFLVASPMAHQTGFVYGFTLPLLLGAPVVLqdiwdpDKAL---ALMREHGVTFM 186
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 428688192 197 ISLVP--TQLNFLLENFPDWLKKFETVLVGGSATPKTLLQNCYRQKINLAL-TYGMTETASGVTILKPENFFKGINNSGH 273
Cdd:cd05903 187 MGATPflTDLLNAVEEAGEPLSRLRTFVCGGATVPRSLARRAAELLGAKVCsAYGSTECPGAVTSITPAPEDRRLYTDGR 266
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 428688192 274 LLPHSQI-VIKKNQAKF-----GQIIIKSDSLFKGYY--PHYKNSNY----FLTDDLGYFDQDNFLHIVGRNSQKIISGG 341
Cdd:cd05903 267 PLPGVEIkVVDDTGATLapgveGELLSRGPSVFLGYLdrPDLTADAApegwFRTGDLARLDEDGYLRITGRSKDIIIRGG 346
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 428688192 342 ENVYPCEIENVVIKTGLVKDIVVVGKNDHYWGQIICAVYVAISGYD------TEYLvnnikakLRSHLSHYKIPKLWLKV 415
Cdd:cd05903 347 ENIPVLEVEDLLLGHPGVIEAAVVALPDERLGERACAVVVTKSGALltfdelVAYL-------DRQGVAKQYWPERLVHV 419
|
410
....*....|.
gi 428688192 416 DQIPRNPQGKI 426
Cdd:cd05903 420 DDLPRTPSGKV 430
|
|
| PRK07788 |
PRK07788 |
acyl-CoA synthetase; Validated |
110-426 |
3.82e-28 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236097 [Multi-domain] Cd Length: 549 Bit Score: 116.57 E-value: 3.82e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 428688192 110 GIMIPTGGTSGNIKFAIHTWETLNASAKGF-SQFWQRRKINFFCCLPLYHVSGLMQIVRTFVTGGSLA---IYDYSLLKK 185
Cdd:PRK07788 210 GIVILTSGTTGTPKGAPRPEPSPLAPLAGLlSRVPFRAGETTLLPAPMFHATGWAHLTLAMALGSTVVlrrRFDPEATLE 289
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 428688192 186 EIQNHNYDNffISLVPTQLNFLLENFPDWLKKFET-----VLVGGSATPKTLLQNCYRQ--KI--NLaltYGMTETASgV 256
Cdd:PRK07788 290 DIAKHKATA--LVVVPVMLSRILDLGPEVLAKYDTsslkiIFVSGSALSPELATRALEAfgPVlyNL---YGSTEVAF-A 363
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 428688192 257 TILKPENFFKGINNSGHLLPHSQIVIKKNQAK------FGQIIIKSDSLFKGYY--PHYKNSNYFL-TDDLGYFDQDNFL 327
Cdd:PRK07788 364 TIATPEDLAEAPGTVGRPPKGVTVKILDENGNevprgvVGRIFVGNGFPFEGYTdgRDKQIIDGLLsSGDVGYFDEDGLL 443
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 428688192 328 HIVGRNSQKIISGGENVYPCEIENVVIKTGLVKDIVVVGKNDHYWGQIICAVYVAISGYDTEylVNNIKAKLRSHLSHYK 407
Cdd:PRK07788 444 FVDGRDDDMIVSGGENVFPAEVEDLLAGHPDVVEAAVIGVDDEEFGQRLRAFVVKAPGAALD--EDAIKDYVRDNLARYK 521
|
330
....*....|....*....
gi 428688192 408 IPKLWLKVDQIPRNPQGKI 426
Cdd:PRK07788 522 VPRDVVFLDELPRNPTGKV 540
|
|
| PRK06145 |
PRK06145 |
acyl-CoA synthetase; Validated |
155-426 |
1.60e-27 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 102207 [Multi-domain] Cd Length: 497 Bit Score: 114.60 E-value: 1.60e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 428688192 155 PLYHVSGL-MQIVRTFVTGGSLAI---YDYSLLKKEIQNHNYDNFFisLVPTQLNFLLeNFPDW----LKKFETVLVGGS 226
Cdd:PRK06145 198 PLYHVGAFdLPGIAVLWVGGTLRIhreFDPEAVLAAIERHRLTCAW--MAPVMLSRVL-TVPDRdrfdLDSLAWCIGGGE 274
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 428688192 227 ATPKTLLQNCYRQKINLALT--YGMTETASGVTILKPENFFKGINNSGHLLPHSQIVIKKNQAKF------GQIIIKSDS 298
Cdd:PRK06145 275 KTPESRIRDFTRVFTRARYIdaYGLTETCSGDTLMEAGREIEKIGSTGRALAHVEIRIADGAGRWlppnmkGEICMRGPK 354
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 428688192 299 LFKGYYPHYKNS------NYFLTDDLGYFDQDNFLHIVGRNSQKIISGGENVYPCEIENVVIKTGLVKDIVVVGKNDHYW 372
Cdd:PRK06145 355 VTKGYWKDPEKTaeafygDWFRSGDVGYLDEEGFLYLTDRKKDMIISGGENIASSEVERVIYELPEVAEAAVIGVHDDRW 434
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....
gi 428688192 373 GQIICAVYVAISGYDTEylVNNIKAKLRSHLSHYKIPKLWLKVDQIPRNPQGKI 426
Cdd:PRK06145 435 GERITAVVVLNPGATLT--LEALDRHCRQRLASFKVPRQLKVRDELPRNPSGKV 486
|
|
| PRK13382 |
PRK13382 |
bile acid CoA ligase; |
90-426 |
6.86e-26 |
|
bile acid CoA ligase;
Pssm-ID: 172019 [Multi-domain] Cd Length: 537 Bit Score: 109.85 E-value: 6.86e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 428688192 90 LFSDHLEKTyynPPHNHSYQGIMIPTGGTSGNIKFAIHTWETLNASAKG-FSQFWQRRKINFFCCLPLYHVSGLMQIV-- 166
Cdd:PRK13382 182 LIAAHAGQR---PEPTGRKGRVILLTSGTTGTPKGARRSGPGGIGTLKAiLDRTPWRAEEPTVIVAPMFHAWGFSQLVla 258
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 428688192 167 ----------RTFVTGGSLAIYDysllkkeiQNHNYDnffISLVPTQLNFLLENFPDWLKKFET-----VLVGGSATPKT 231
Cdd:PRK13382 259 aslactivtrRRFDPEATLDLID--------RHRATG---LAVVPVMFDRIMDLPAEVRNRYSGrslrfAAASGSRMRPD 327
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 428688192 232 LLQNcYRQKINLAL--TYGMTEtASGVTILKPENFFKGINNSGHllPHSQIVIKKNQAKF--------GQIIIKSDSLFK 301
Cdd:PRK13382 328 VVIA-FMDQFGDVIynNYNATE-AGMIATATPADLRAAPDTAGR--PAEGTEIRILDQDFrevptgevGTIFVRNDTQFD 403
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 428688192 302 GYYP------HyknSNYFLTDDLGYFDQDNFLHIVGRNSQKIISGGENVYPCEIENVVIKTGLVKDIVVVGKNDHYWGQI 375
Cdd:PRK13382 404 GYTSgstkdfH---DGFMASGDVGYLDENGRLFVVGRDDEMIVSGGENVYPIEVEKTLATHPDVAEAAVIGVDDEQYGQR 480
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|.
gi 428688192 376 ICAvYVAISGyDTEYLVNNIKAKLRSHLSHYKIPKLWLKVDQIPRNPQGKI 426
Cdd:PRK13382 481 LAA-FVVLKP-GASATPETLKQHVRDNLANYKVPRDIVVLDELPRGATGKI 529
|
|
| PRK09088 |
PRK09088 |
acyl-CoA synthetase; Validated |
111-435 |
2.73e-24 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 181644 [Multi-domain] Cd Length: 488 Bit Score: 104.89 E-value: 2.73e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 428688192 111 IMIPTGGTSGNIKFAIHTWETLNASAKGFSQFWQ-RRKINFFCCLPLYHVSGLMQIVR-TFVTGGSLAIYD-----YSLL 183
Cdd:PRK09088 139 LILFTSGTSGQPKGVMLSERNLQQTAHNFGVLGRvDAHSSFLCDAPMFHIIGLITSVRpVLAVGGSILVSNgfepkRTLG 218
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 428688192 184 KKEIQNHNYDNFFIslVPtQLNFLLENFPDW----LKKFETVLVGGSATPKTLLQNCYRQKINLALTYGMTE--TASGVT 257
Cdd:PRK09088 219 RLGDPALGITHYFC--VP-QMAQAFRAQPGFdaaaLRHLTALFTGGAPHAAEDILGWLDDGIPMVDGFGMSEagTVFGMS 295
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 428688192 258 iLKPENFFKGINNSGHLLPHSQIVIKKNQAKF------GQIIIKSDSLFKGYY--PH-----YKNSNYFLTDDLGYFDQD 324
Cdd:PRK09088 296 -VDCDVIRAKAGAAGIPTPTVQTRVVDDQGNDcpagvpGELLLRGPNLSPGYWrrPQataraFTGDGWFRTGDIARRDAD 374
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 428688192 325 NFLHIVGRNSQKIISGGENVYPCEIENVVIKTGLVKDIVVVGKNDHYWGQIICAVYVAISGYDTEYlvnnikAKLRSHLS 404
Cdd:PRK09088 375 GFFWVVDRKKDMFISGGENVYPAEIEAVLADHPGIRECAVVGMADAQWGEVGYLAIVPADGAPLDL------ERIRSHLS 448
|
330 340 350
....*....|....*....|....*....|....*
gi 428688192 405 ----HYKIPKLWLKVDQIPRNPQGKIDYGYLEKML 435
Cdd:PRK09088 449 trlaKYKVPKHLRLVDALPRTASGKLQKARLRDAL 483
|
|
| PRK08308 |
PRK08308 |
acyl-CoA synthetase; Validated |
11-426 |
2.86e-24 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236231 [Multi-domain] Cd Length: 414 Bit Score: 103.96 E-value: 2.86e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 428688192 11 NNCTYNNQHISLEIKYYINKIIKRENQQNRIIfLSTNNPQQFISVFFASIITKSSIFLLNPHWQQEELQQVYKLVKPDFL 90
Cdd:PRK08308 5 NDEEYSKSDFDLRLQRYEEMEQFQEAAGNRFA-VCLKDPFDIITLVFFLKEKGASVLPIHPDTPKEAAIRMAKRAGCHGL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 428688192 91 FSDHLEKTYYNPPHNHSYQGIMIP-TGGTSGNIKFAIHTWETLNASAKGF-SQFWQRRKINFFCCLPLYHVSGLMQIVRT 168
Cdd:PRK08308 84 LYGESDFTKLEAVNYLAEEPSLLQySSGTTGEPKLIRRSWTEIDREIEAYnEALNCEQDETPIVACPVTHSYGLICGVLA 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 428688192 169 FVTGGSLAIYDYSLLKKEIQN--HNYDNFFISLVPTQLnFLLENFPDWLKKFETVLVGGSATPKTLLQNCYRQKINLALT 246
Cdd:PRK08308 164 ALTRGSKPVIITNKNPKFALNilRNTPQHILYAVPLML-HILGRLLPGTFQFHAVMTSGTPLPEAWFYKLRERTTYMMQQ 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 428688192 247 YGMTEtASGVTILKPENFFKGInnsGHLLPHSQIVIKKNQAKFGQIIIKSdslfkgyyphykNSNYFLTDDLGYFDQDNF 326
Cdd:PRK08308 243 YGCSE-AGCVSICPDMKSHLDL---GNPLPHVSVSAGSDENAPEEIVVKM------------GDKEIFTKDLGYKSERGT 306
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 428688192 327 LHIVGRNSQKIISGGENVYPCEIENVVIKTGLVKDIVVVGKNDHYWGQIICAVYVAISGYDTEylvnNIKAKLRSHLSHY 406
Cdd:PRK08308 307 LHFMGRMDDVINVSGLNVYPIEVEDVMLRLPGVQEAVVYRGKDPVAGERVKAKVISHEEIDPV----QLREWCIQHLAPY 382
|
410 420
....*....|....*....|
gi 428688192 407 KIPKLWLKVDQIPRNPQGKI 426
Cdd:PRK08308 383 QVPHEIESVTEIPKNANGKV 402
|
|
| AMP-binding |
pfam00501 |
AMP-binding enzyme; |
112-332 |
7.60e-24 |
|
AMP-binding enzyme;
Pssm-ID: 459834 [Multi-domain] Cd Length: 417 Bit Score: 102.78 E-value: 7.60e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 428688192 112 MIPTGGTSGNIKFAIHTWETLNASAKGFSQ-----FWQRRKINFFCCLPLYHVSGLMQIV-RTFVTGGSLAIYDYS---- 181
Cdd:pfam00501 160 IIYTSGTTGKPKGVMLTHRNLVANVLSIKRvrprgFGLGPDDRVLSTLPLFHDFGLSLGLlGPLLAGATVVLPPGFpald 239
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 428688192 182 --LLKKEIQNHNYDnfFISLVPTQLNFLLENFPDWLKKF---ETVLVGGSATPKTLLQNcYRQKINLAL--TYGMTETAS 254
Cdd:pfam00501 240 paALLELIERYKVT--VLYGVPTLLNMLLEAGAPKRALLsslRLVLSGGAPLPPELARR-FRELFGGALvnGYGLTETTG 316
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 428688192 255 GVTI-LKPENFFKGINNSGHLLPHSQIVIKKNQAKF-------GQIIIKSDSLFKGYY--P-----HYKNSNYFLTDDLG 319
Cdd:pfam00501 317 VVTTpLPLDEDLRSLGSVGRPLPGTEVKIVDDETGEpvppgepGELCVRGPGVMKGYLndPeltaeAFDEDGWYRTGDLG 396
|
250
....*....|...
gi 428688192 320 YFDQDNFLHIVGR 332
Cdd:pfam00501 397 RRDEDGYLEIVGR 409
|
|
| PRK07786 |
PRK07786 |
long-chain-fatty-acid--CoA ligase; Validated |
111-433 |
1.39e-23 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 169098 [Multi-domain] Cd Length: 542 Bit Score: 103.32 E-value: 1.39e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 428688192 111 IMIpTGGTSGNIKFAIHTWETLNASAKGFSQFWqRRKINF---FCCLPLYHVSGLMQIVRTFVTGGSLAIY-----DYSL 182
Cdd:PRK07786 179 IMY-TSGTTGRPKGAVLTHANLTGQAMTCLRTN-GADINSdvgFVGVPLFHIAGIGSMLPGLLLGAPTVIYplgafDPGQ 256
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 428688192 183 LKKEIQNHNYDNFFisLVPTQLNFLL---ENFPDWLKKfeTVLVGGSA-TPKTLLQN---CYRQKINLALtYGMTETASG 255
Cdd:PRK07786 257 LLDVLEAEKVTGIF--LVPAQWQAVCaeqQARPRDLAL--RVLSWGAApASDTLLRQmaaTFPEAQILAA-FGQTEMSPV 331
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 428688192 256 VTILKPENFFKGINNSGHLLPHSQI-VIKKN-----QAKFGQIIIKSDSLFKGYYPHYKNS------NYFLTDDLGYFDQ 323
Cdd:PRK07786 332 TCMLLGEDAIRKLGSVGKVIPTVAArVVDENmndvpVGEVGEIVYRAPTLMSGYWNNPEATaeafagGWFHSGDLVRQDE 411
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 428688192 324 DNFLHIVGRNSQKIISGGENVYPCEIENVVIKTGLVKDIVVVGKNDHYWGQIICAVyVAISGYDTEYLVNNIKAKLRSHL 403
Cdd:PRK07786 412 EGYVWVVDRKKDMIISGGENIYCAEVENVLASHPDIVEVAVIGRADEKWGEVPVAV-AAVRNDDAALTLEDLAEFLTDRL 490
|
330 340 350
....*....|....*....|....*....|
gi 428688192 404 SHYKIPKLWLKVDQIPRNPQGKIDYGYLEK 433
Cdd:PRK07786 491 ARYKHPKALEIVDALPRNPAGKVLKTELRE 520
|
|
| ACLS-CaiC |
cd17637 |
acyl-CoA synthetase (AMP-forming)/AMP-acid ligase II; This family contains fatty acid CoA ... |
154-427 |
1.50e-23 |
|
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: 100.81 E-value: 1.50e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 428688192 154 LPLYHVSGLMQIVRTFVTGGS---LAIYDYSLLKKEIQNHNYdNFFISLVPtqlnfLLENFPDWLKKFETVL-----VGG 225
Cdd:cd17637 48 LPLFHIAGLNLALATFHAGGAnvvMEKFDPAEALELIEEEKV-TLMGSFPP-----ILSNLLDAAEKSGVDLsslrhVLG 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 428688192 226 SATPKTL--LQNCYRQKinLALTYGMTETaSGVTILKPENFFKGinNSGHLLPHSQIVIKKNQAKF------GQIIIKSD 297
Cdd:cd17637 122 LDAPETIqrFEETTGAT--FWSLYGQTET-SGLVTLSPYRERPG--SAGRPGPLVRVRIVDDNDRPvpagetGEIVVRGP 196
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 428688192 298 SLFKGYYPHYKNSNYFL------TDDLGYFDQDNFLHIVGRNSQK--IISGGENVYPCEIENVVIKTGLVKDIVVVGKND 369
Cdd:cd17637 197 LVFQGYWNLPELTAYTFrngwhhTGDLGRFDEDGYLWYAGRKPEKelIKPGGENVYPAEVEKVILEHPAIAEVCVIGVPD 276
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|
gi 428688192 370 HYWGQIICAVYVAISGY--DTEYLVNNIKAKLRShlshYKIPKLWLKVDQIPRNPQGKID 427
Cdd:cd17637 277 PKWGEGIKAVCVLKPGAtlTADELIEFVGSRIAR----YKKPRYVVFVEALPKTADGSID 332
|
|
| CBAL |
cd05923 |
4-Chlorobenzoate-CoA ligase (CBAL); CBAL catalyzes the conversion of 4-chlorobenzoate (4-CB) ... |
154-426 |
2.52e-23 |
|
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: 102.20 E-value: 2.52e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 428688192 154 LPLYHVSGLMQI-VRTFVTGGSLAI---YDYSLLKKEIQNHNYDNFFisLVPTQLNFLL---ENFPDWLKKFETVLVGGS 226
Cdd:cd05923 200 MPLYHVIGFFAVlVAALALDGTYVVveeFDPADALKLIEQERVTSLF--ATPTHLDALAaaaEFAGLKLSSLRHVTFAGA 277
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 428688192 227 ATPKTLLQNCYRQKINLALT-YGMTET--------ASGVTILKPeNFFKGIN------NSGHLLPhsqivikknQAKFGQ 291
Cdd:cd05923 278 TMPDAVLERVNQHLPGEKVNiYGTTEAmnslymrdARTGTEMRP-GFFSEVRivriggSPDEALA---------NGEEGE 347
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 428688192 292 IIIK--SDSLFKGYYPHY------KNSNYFLTDDLGYFDQDNFLHIVGRNSQKIISGGENVYPCEIENVVIKTGLVKDIV 363
Cdd:cd05923 348 LIVAaaADAAFTGYLNQPeatakkLQDGWYRTGDVGYVDPSGDVRILGRVDDMIISGGENIHPSEIERVLSRHPGVTEVV 427
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 428688192 364 VVGKNDHYWGQIICAVYVAISGYDTEYLVNNIkaKLRSHLSHYKIPKLWLKVDQIPRNPQGKI 426
Cdd:cd05923 428 VIGVADERWGQSVTACVVPREGTLSADELDQF--CRASELADFKRPRRYFFLDELPKNAMNKV 488
|
|
| FACL_like_4 |
cd05944 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
115-427 |
4.01e-23 |
|
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: 99.86 E-value: 4.01e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 428688192 115 TGGTSGNIKFAIHTW--ETLNASAKGFSQFWQRRKiNFFCCLPLYHVSGLMQIVRT-FVTGGSLAIYDYSLLKKEiqnHN 191
Cdd:cd05944 10 TGGTTGTPKLAQHTHsnEVYNAWMLALNSLFDPDD-VLLCGLPLFHVNGSVVTLLTpLASGAHVVLAGPAGYRNP---GL 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 428688192 192 YDNF----------FISLVPTQLNFLLEnFPDW--LKKFETVLVGGSATPKTLLqNCYRQKINLALT--YGMTETASGVT 257
Cdd:cd05944 86 FDNFwklveryritSLSTVPTVYAALLQ-VPVNadISSLRFAMSGAAPLPVELR-ARFEDATGLPVVegYGLTEATCLVA 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 428688192 258 iLKPENFFKGINNSGHLLPHSQIVIKKNQA-----------KFGQIIIKSDSLFKGYYPHYKNSNYFL------TDDLGY 320
Cdd:cd05944 164 -VNPPDGPKRPGSVGLRLPYARVRIKVLDGvgrllrdcapdEVGEICVAGPGVFGGYLYTEGNKNAFVadgwlnTGDLGR 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 428688192 321 FDQDNFLHIVGRNSQKIISGGENVYPCEIENVVIKTGLVKDIVVVGKNDHYWGQIICAvYVAISGyDTEYLVNNIKAKLR 400
Cdd:cd05944 243 LDADGYLFITGRAKDLIIRGGHNIDPALIEEALLRHPAVAFAGAVGQPDAHAGELPVA-YVQLKP-GAVVEEEELLAWAR 320
|
330 340
....*....|....*....|....*...
gi 428688192 401 SHL-SHYKIPKLWLKVDQIPRNPQGKID 427
Cdd:cd05944 321 DHVpERAAVPKHIEVLEELPVTAVGKVF 348
|
|
| PRK07529 |
PRK07529 |
AMP-binding domain protein; Validated |
114-381 |
4.85e-23 |
|
AMP-binding domain protein; Validated
Pssm-ID: 236043 [Multi-domain] Cd Length: 632 Bit Score: 101.96 E-value: 4.85e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 428688192 114 PTGGTSGNIKFAIHTW--ETLNASAKGFSQFWQRRKiNFFCCLPLYHVSGLM-QIVRTFVTGGSLAI-----Y-DYSLLK 184
Cdd:PRK07529 220 HTGGTTGMPKLAQHTHgnEVANAWLGALLLGLGPGD-TVFCGLPLFHVNALLvTGLAPLARGAHVVLatpqgYrGPGVIA 298
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 428688192 185 K--EIQNHnYDNFFISLVPTQLNFLLE---NFPDwLKKFETVLVGGSATPKTLLQNCYRQ-KINLALTYGMTETASGVTI 258
Cdd:PRK07529 299 NfwKIVER-YRINFLSGVPTVYAALLQvpvDGHD-ISSLRYALCGAAPLPVEVFRRFEAAtGVRIVEGYGLTEATCVSSV 376
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 428688192 259 lKPENFFKGINNSGHLLPHSQI-VIKKNQA----------KFGQIIIKSDSLFKGYYPHYKNSNYFL------TDDLGYF 321
Cdd:PRK07529 377 -NPPDGERRIGSVGLRLPYQRVrVVILDDAgrylrdcavdEVGVLCIAGPNVFSGYLEAAHNKGLWLedgwlnTGDLGRI 455
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|
gi 428688192 322 DQDNFLHIVGRNSQKIISGGENVYPCEIENVVIKTGLVKDIVVVGKNDHYWGQIICAvYV 381
Cdd:PRK07529 456 DADGYFWLTGRAKDLIIRGGHNIDPAAIEEALLRHPAVALAAAVGRPDAHAGELPVA-YV 514
|
|
| FadD3 |
cd17638 |
acyl-CoA synthetase FadD3 and similar proteins; This family contains long chain fatty acid CoA ... |
149-426 |
6.07e-23 |
|
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: 99.11 E-value: 6.07e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 428688192 149 NFFCCLPLYHVSGLMQ-IVRTFVTGGSL---AIYDYSLLKKEIQNHNydnffISLVP---TQLNFLLENfPDwLKKFE-- 219
Cdd:cd17638 43 RYLIINPFFHTFGYKAgIVACLLTGATVvpvAVFDVDAILEAIERER-----ITVLPgppTLFQSLLDH-PG-RKKFDls 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 428688192 220 --TVLVGGSATPKTLLQNCYRQKI---NLALTYGMTEtASGVTILKPENFFKGI-NNSGHLLPHSQIVIkknqAKFGQII 293
Cdd:cd17638 116 slRAAVTGAATVPVELVRRMRSELgfeTVLTAYGLTE-AGVATMCRPGDDAETVaTTCGRACPGFEVRI----ADDGEVL 190
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 428688192 294 IKSDSLFKGYYPHYKNS-------NYFLTDDLGYFDQDNFLHIVGRNSQKIISGGENVYPCEIENVVIKTGLVKDIVVVG 366
Cdd:cd17638 191 VRGYNVMQGYLDDPEATaeaidadGWLHTGDVGELDERGYLRITDRLKDMYIVGGFNVYPAEVEGALAEHPGVAQVAVIG 270
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 428688192 367 KNDHYWGQIICAVYVAISGY--DTEYLVnnikAKLRSHLSHYKIPKLWLKVDQIPRNPQGKI 426
Cdd:cd17638 271 VPDERMGEVGKAFVVARPGVtlTEEDVI----AWCRERLANYKVPRFVRFLDELPRNASGKV 328
|
|
| A_NRPS |
cd05930 |
The adenylation domain of nonribosomal peptide synthetases (NRPS); The adenylation (A) domain ... |
162-428 |
3.02e-22 |
|
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: 98.37 E-value: 3.02e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 428688192 162 LMQIVRTFVTGGSLAI------YDYSLLKKEIQNHNYDnfFISLVPTQLNFLLEN-FPDWLKKFETVLVGGSATPKTLLQ 234
Cdd:cd05930 149 VWEIFGALLAGATLVVlpeevrKDPEALADLLAEEGIT--VLHLTPSLLRLLLQElELAALPSLRLVLVGGEALPPDLVR 226
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 428688192 235 NCYRQKINLAL--TYGMTETASGVTI--LKPENFFKGINNSGHLLPHSQI-VIKKNQA-----KFGQIIIKSDSLFKGYY 304
Cdd:cd05930 227 RWRELLPGARLvnLYGPTEATVDATYyrVPPDDEEDGRVPIGRPIPNTRVyVLDENLRpvppgVPGELYIGGAGLARGYL 306
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 428688192 305 -------------PHYKNSNYFLTDDLGYFDQDNFLHIVGRN-SQ-KIisGGENVYPCEIENVVIKTGLVKDIVVVGKND 369
Cdd:cd05930 307 nrpeltaerfvpnPFGPGERMYRTGDLVRWLPDGNLEFLGRIdDQvKI--RGYRIELGEIEAALLAHPGVREAAVVARED 384
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*....
gi 428688192 370 HYWGQIICAVYVAISGYDTEylVNNIKAKLRSHLSHYKIPKLWLKVDQIPRNPQGKIDY 428
Cdd:cd05930 385 GDGEKRLVAYVVPDEGGELD--EEELRAHLAERLPDYMVPSAFVVLDALPLTPNGKVDR 441
|
|
| PRK07656 |
PRK07656 |
long-chain-fatty-acid--CoA ligase; Validated |
200-426 |
7.71e-22 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236072 [Multi-domain] Cd Length: 513 Bit Score: 97.67 E-value: 7.71e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 428688192 200 VPTQLNFLLeNFPDWLK-KFETVLV---GGSATPKTLLQNcYRQKINLA--LT-YGMTEtASGVTIL-KPENFFKGI-NN 270
Cdd:PRK07656 262 PPTMYNSLL-QHPDRSAeDLSSLRLavtGAASMPVALLER-FESELGVDivLTgYGLSE-ASGVTTFnRLDDDRKTVaGT 338
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 428688192 271 SGHLLPHSQIVIKKNQAKF------GQIIIKSDSLFKGYY--PH-----YKNSNYFLTDDLGYFDQDNFLHIVGRNSQKI 337
Cdd:PRK07656 339 IGTAIAGVENKIVNELGEEvpvgevGELLVRGPNVMKGYYddPEataaaIDADGWLHTGDLGRLDEEGYLYIVDRKKDMF 418
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 428688192 338 ISGGENVYPCEIENVVIKTGLVKDIVVVGKNDHYWGQIICAVYVAISG--YDTEYLVnnikAKLRSHLSHYKIPKLWLKV 415
Cdd:PRK07656 419 IVGGFNVYPAEVEEVLYEHPAVAEAAVIGVPDERLGEVGKAYVVLKPGaeLTEEELI----AYCREHLAKYKVPRSIEFL 494
|
250
....*....|.
gi 428688192 416 DQIPRNPQGKI 426
Cdd:PRK07656 495 DELPKNATGKV 505
|
|
| PRK06188 |
PRK06188 |
acyl-CoA synthetase; Validated |
115-427 |
1.02e-21 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 235731 [Multi-domain] Cd Length: 524 Bit Score: 97.36 E-value: 1.02e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 428688192 115 TGGTSGNIKFAIHTWETLNASAKGFSQFWQ-RRKINFFCCLPLYHVSGLMqIVRTFVTGGSLAI---YDYSLLKKEIQNH 190
Cdd:PRK06188 176 TGGTTGKPKGVMGTHRSIATMAQIQLAEWEwPADPRFLMCTPLSHAGGAF-FLPTLLRGGTVIVlakFDPAEVLRAIEEQ 254
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 428688192 191 NYDNFFisLVPTQLNFLLENfPDW----LKKFETVLVGGSATPKTLLqncyRQKIN-----LALTYGMTETASGVTILKP 261
Cdd:PRK06188 255 RITATF--LVPTMIYALLDH-PDLrtrdLSSLETVYYGASPMSPVRL----AEAIErfgpiFAQYYGQTEAPMVITYLRK 327
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 428688192 262 ENFFKG----INNSGHLLPHSQIVI------KKNQAKFGQIIIKSDSLFKGYY--PH-----YKNsNYFLTDDLGYFDQD 324
Cdd:PRK06188 328 RDHDPDdpkrLTSCGRPTPGLRVALldedgrEVAQGEVGEICVRGPLVMDGYWnrPEetaeaFRD-GWLHTGDVAREDED 406
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 428688192 325 NFLHIVGRNSQKIISGGENVYPCEIENVVIKTGLVKDIVVVGKNDHYWGQIICAVYVAISGY--DTEYLVNNIKAKLRSH 402
Cdd:PRK06188 407 GFYYIVDRKKDMIVTGGFNVFPREVEDVLAEHPAVAQVAVIGVPDEKWGEAVTAVVVLRPGAavDAAELQAHVKERKGSV 486
|
330 340
....*....|....*....|....*
gi 428688192 403 LShykiPKLWLKVDQIPRNPQGKID 427
Cdd:PRK06188 487 HA----PKQVDFVDSLPLTALGKPD 507
|
|
| MACS_like |
cd05972 |
Medium-chain acyl-CoA synthetase (MACS or ACSM); MACS catalyzes the two-step activation of ... |
185-426 |
1.09e-21 |
|
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: 96.64 E-value: 1.09e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 428688192 185 KEIQNHNYDNFFISlvPTQLNFLLENFPD--WLKKFETVLVGG-SATPKTLlqNCYRQKINLAL--TYGMTETasGVTIl 259
Cdd:cd05972 166 ELLERYGVTSFCGP--PTAYRMLIKQDLSsyKFSHLRLVVSAGePLNPEVI--EWWRAATGLPIrdGYGQTET--GLTV- 238
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 428688192 260 kpeNFFKGIN----NSGHLLPHSQIVIKKNQAKF------GQIIIKSD--SLFKGYYPHYKNS------NYFLTDDLGYF 321
Cdd:cd05972 239 ---GNFPDMPvkpgSMGRPTPGYDVAIIDDDGRElppgeeGDIAIKLPppGLFLGYVGDPEKTeasirgDYYLTGDRAYR 315
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 428688192 322 DQDNFLHIVGRNSQKIISGGENVYPCEIENVVIKTGLVKDIVVVGKNDHYWGQIICAVYVAISGY-DTEYLVNNIKAKLR 400
Cdd:cd05972 316 DEDGYFWFVGRADDIIKSSGYRIGPFEVESALLEHPAVAEAAVVGSPDPVRGEVVKAFVVLTSGYePSEELAEELQGHVK 395
|
250 260
....*....|....*....|....*.
gi 428688192 401 SHLSHYKIPKLWLKVDQIPRNPQGKI 426
Cdd:cd05972 396 KVLAPYKYPREIEFVEELPKTISGKI 421
|
|
| VL_LC_FACS_like |
cd05907 |
Long-chain fatty acid CoA synthetases and Bubblegum-like very long-chain fatty acid CoA ... |
112-405 |
1.44e-21 |
|
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: 96.51 E-value: 1.44e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 428688192 112 MIPTGGTSGNIKFAIHTWETLNASAKGFSQFWQRRKIN-FFCCLPLYHVSGLMQIVRTFVTGGSlAIYDYSLLK------ 184
Cdd:cd05907 92 IIYTSGTTGRPKGVMLSHRNILSNALALAERLPATEGDrHLSFLPLAHVFERRAGLYVPLLAGA-RIYFASSAEtllddl 170
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 428688192 185 KEIQNH-----------NYDNFFISLVPTQLNFLLenfpDW--LKKFETVLVGGSATPKTLLQncYRQKINLALT--YGM 249
Cdd:cd05907 171 SEVRPTvflavprvwekVYAAIKVKAVPGLKRKLF----DLavGGRLRFAASGGAPLPAELLH--FFRALGIPVYegYGL 244
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 428688192 250 TETASGVTILKPENFfkGINNSGHLLPHSQIVIKKNqakfGQIIIKSDSLFKGYYphyKN----------SNYFLTDDLG 319
Cdd:cd05907 245 TETSAVVTLNPPGDN--RIGTVGKPLPGVEVRIADD----GEILVRGPNVMLGYY---KNpeataealdaDGWLHTGDLG 315
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 428688192 320 YFDQDNFLHIVGRNSQKII-SGGENVYPCEIENVVIKTGLVKDIVVVGKNDHYWGQIICAVYVAISGYDTEylvNNIKAK 398
Cdd:cd05907 316 EIDEDGFLHITGRKKDLIItSGGKNISPEPIENALKASPLISQAVVIGDGRPFLVALIVPDPEALEAWAEE---HGIAYT 392
|
....*..
gi 428688192 399 LRSHLSH 405
Cdd:cd05907 393 DVAELAA 399
|
|
| BACL_like |
cd05929 |
Bacterial Bile acid CoA ligases and similar proteins; Bile acid-Coenzyme A ligase catalyzes ... |
317-427 |
1.89e-21 |
|
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: 96.29 E-value: 1.89e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 428688192 317 DLGYFDQDNFLHIVGRNSQKIISGGENVYPCEIENVVIKTGLVKDIVVVGKNDHYWGQIICAVY-VAISGYDTEYLVNNI 395
Cdd:cd05929 356 DVGYLDEDGYLYLTDRRSDMIISGGVNIYPQEIENALIAHPKVLDAAVVGVPDEELGQRVHAVVqPAPGADAGTALAEEL 435
|
90 100 110
....*....|....*....|....*....|..
gi 428688192 396 KAKLRSHLSHYKIPKLWLKVDQIPRNPQGKID 427
Cdd:cd05929 436 IAFLRDRLSRYKCPRSIEFVAELPRDDTGKLY 467
|
|
| PRK07514 |
PRK07514 |
malonyl-CoA synthase; Validated |
247-426 |
2.01e-21 |
|
malonyl-CoA synthase; Validated
Pssm-ID: 181011 [Multi-domain] Cd Length: 504 Bit Score: 96.48 E-value: 2.01e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 428688192 247 YGMTETA--------------------SGVT--ILKPEnffkginnSGHLLPHSQIvikknqakfGQIIIKSDSLFKGYY 304
Cdd:PRK07514 301 YGMTETNmntsnpydgerragtvgfplPGVSlrVTDPE--------TGAELPPGEI---------GMIEVKGPNVFKGYW 363
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 428688192 305 --P-----HYKNSNYFLTDDLGYFDQDNFLHIVGRNSQKIISGGENVYPCEIENVVIKTGLVKDIVVVGKNDHYWGQIIC 377
Cdd:PRK07514 364 rmPektaeEFRADGFFITGDLGKIDERGYVHIVGRGKDLIISGGYNVYPKEVEGEIDELPGVVESAVIGVPHPDFGEGVT 443
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 428688192 378 AVYVAISGYDTEylVNNIKAKLRSHLSHYKIPKLWLKVDQIPRNPQGKI 426
Cdd:PRK07514 444 AVVVPKPGAALD--EAAILAALKGRLARFKQPKRVFFVDELPRNTMGKV 490
|
|
| PLN03102 |
PLN03102 |
acyl-activating enzyme; Provisional |
154-426 |
2.01e-21 |
|
acyl-activating enzyme; Provisional
Pssm-ID: 215576 [Multi-domain] Cd Length: 579 Bit Score: 97.01 E-value: 2.01e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 428688192 154 LPLYHVSGLMQIVRTFVTGG-SLAIYDYSL--LKKEIQNHNYDNffISLVPTQLNFLLE-NFPDWLKKFETV--LVGGSA 227
Cdd:PLN03102 234 LPMFHCNGWTFTWGTAARGGtSVCMRHVTApeIYKNIEMHNVTH--MCCVPTVFNILLKgNSLDLSPRSGPVhvLTGGSP 311
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 428688192 228 TPKTLLQNCYRQKINLALTYGMTEtASGvtilkPENFFKGINNSGHLLPHSQIVIKKNQA-------------------- 287
Cdd:PLN03102 312 PPAALVKKVQRLGFQVMHAYGLTE-ATG-----PVLFCEWQDEWNRLPENQQMELKARQGvsilgladvdvknketqesv 385
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 428688192 288 -----KFGQIIIKSDSLFKGYYPHYKNS------NYFLTDDLGYFDQDNFLHIVGRNSQKIISGGENVYPCEIENVVIKT 356
Cdd:PLN03102 386 prdgkTMGEIVIKGSSIMKGYLKNPKATseafkhGWLNTGDVGVIHPDGHVEIKDRSKDIIISGGENISSVEVENVLYKY 465
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 428688192 357 GLVKDIVVVGKNDHYWGQIICAVYVAISG-----YDTEYLVN---NIKAKLRSHLSHYKIPKLWLKVDQIPRNPQGKI 426
Cdd:PLN03102 466 PKVLETAVVAMPHPTWGETPCAFVVLEKGettkeDRVDKLVTrerDLIEYCRENLPHFMCPRKVVFLQELPKNGNGKI 543
|
|
| PRK08974 |
PRK08974 |
long-chain-fatty-acid--CoA ligase FadD; |
115-426 |
3.85e-21 |
|
long-chain-fatty-acid--CoA ligase FadD;
Pssm-ID: 236359 [Multi-domain] Cd Length: 560 Bit Score: 95.89 E-value: 3.85e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 428688192 115 TGGTSGNIKFAIHTWETLNAS---AKG-FSQFWQRRKINFFCCLPLYHVSGLMQIVRTFVTGGSLAIY-----DYSLLKK 185
Cdd:PRK08974 214 TGGTTGVAKGAMLTHRNMLANleqAKAaYGPLLHPGKELVVTALPLYHIFALTVNCLLFIELGGQNLLitnprDIPGFVK 293
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 428688192 186 EIQNHNYDNffISLVPTQLNFLLENfPDWLK-KFETVLV---GGSATPKTLLQNCYR-QKINLALTYGMTETASGVTIlK 260
Cdd:PRK08974 294 ELKKYPFTA--ITGVNTLFNALLNN-EEFQElDFSSLKLsvgGGMAVQQAVAERWVKlTGQYLLEGYGLTECSPLVSV-N 369
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 428688192 261 PENFfKGINNS-GHLLPHSQIVIKKN------QAKFGQIIIKSDSLFKGYYPHYKNSNYFLTD------DLGYFDQDNFL 327
Cdd:PRK08974 370 PYDL-DYYSGSiGLPVPSTEIKLVDDdgnevpPGEPGELWVKGPQVMLGYWQRPEATDEVIKDgwlatgDIAVMDEEGFL 448
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 428688192 328 HIVGRNSQKIISGGENVYPCEIENVVIKTGLVKDIVVVGKNDHYWGQIICAVYVAISGYDTEylvNNIKAKLRSHLSHYK 407
Cdd:PRK08974 449 RIVDRKKDMILVSGFNVYPNEIEDVVMLHPKVLEVAAVGVPSEVSGEAVKIFVVKKDPSLTE---EELITHCRRHLTGYK 525
|
330
....*....|....*....
gi 428688192 408 IPKLWLKVDQIPRNPQGKI 426
Cdd:PRK08974 526 VPKLVEFRDELPKSNVGKI 544
|
|
| PRK08276 |
PRK08276 |
long-chain-fatty-acid--CoA ligase; Validated |
317-426 |
6.40e-21 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236215 [Multi-domain] Cd Length: 502 Bit Score: 94.97 E-value: 6.40e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 428688192 317 DLGYFDQDNFLHIVGRNSQKIISGGENVYPCEIENVVIKTGLVKDIVVVGKNDHYWGQIICAVYVAISGYD-TEYLVNNI 395
Cdd:PRK08276 375 DVGYLDEDGYLYLTDRKSDMIISGGVNIYPQEIENLLVTHPKVADVAVFGVPDEEMGERVKAVVQPADGADaGDALAAEL 454
|
90 100 110
....*....|....*....|....*....|.
gi 428688192 396 KAKLRSHLSHYKIPKLWLKVDQIPRNPQGKI 426
Cdd:PRK08276 455 IAWLRGRLAHYKCPRSIDFEDELPRTPTGKL 485
|
|
| FACL_DitJ_like |
cd05934 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
47-426 |
6.50e-21 |
|
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: 94.28 E-value: 6.50e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 428688192 47 NNPQqFISVFFASIITKSSIFLLNPHWQQEELQQVYKLVKPDFLFSDhlektyynpPHNhsyqgiMIPTGGTSGNIKFAI 126
Cdd:cd05934 37 NCPE-FLFAWFALAKLGAVLVPINTALRGDELAYIIDHSGAQLVVVD---------PAS------ILYTSGTTGPPKGVV 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 428688192 127 HTWETLNASAKGFS-QFWQRRKINFFCCLPLYHVSGL-MQIVRTFVTGGSLAI---YDYSLLKKEIQNHNYDNFfiSLVP 201
Cdd:cd05934 101 ITHANLTFAGYYSArRFGLGEDDVYLTVLPLFHINAQaVSVLAALSVGATLVLlprFSASRFWSDVRRYGATVT--NYLG 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 428688192 202 TQLNFLLENFPDWLKKFETV-LVGGSATPKTLLQN-CYRQKINLALTYGMTETasGVTILKPENFFKGINNSGHLLPHSQ 279
Cdd:cd05934 179 AMLSYLLAQPPSPDDRAHRLrAAYGAPNPPELHEEfEERFGVRLLEGYGMTET--IVGVIGPRDEPRRPGSIGRPAPGYE 256
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 428688192 280 IVIKKNQAK------FGQIIIKSD---SLFKGYYPHYKNS------NYFLTDDLGYFDQDNFLHIVGRNSQKIISGGENV 344
Cdd:cd05934 257 VRIVDDDGQelpagePGELVIRGLrgwGFFKGYYNMPEATaeamrnGWFHTGDLGYRDADGFFYFVDRKKDMIRRRGENI 336
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 428688192 345 YPCEIENVVIKTGLVKDIVVVGKNDHYWGQIICAVYVAISG--YDTEYLVnnikAKLRSHLSHYKIPKLWLKVDQIPRNP 422
Cdd:cd05934 337 SSAEVERAILRHPAVREAAVVAVPDEVGEDEVKAVVVLRPGetLDPEELF----AFCEGQLAYFKVPRYIRFVDDLPKTP 412
|
....
gi 428688192 423 QGKI 426
Cdd:cd05934 413 TEKV 416
|
|
| Acs |
COG0365 |
Acyl-coenzyme A synthetase/AMP-(fatty) acid ligase [Lipid transport and metabolism]; |
187-426 |
8.24e-21 |
|
Acyl-coenzyme A synthetase/AMP-(fatty) acid ligase [Lipid transport and metabolism];
Pssm-ID: 440134 [Multi-domain] Cd Length: 565 Bit Score: 94.79 E-value: 8.24e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 428688192 187 IQNHNYDNFFISlvPTQLNFLLENFPDWLKKF-----ETVLVGGSA-TPKTLLQncYRQKINLAL--TYGMTETASGV-- 256
Cdd:COG0365 274 IEKYGVTVFFTA--PTAIRALMKAGDEPLKKYdlsslRLLGSAGEPlNPEVWEW--WYEAVGVPIvdGWGQTETGGIFis 349
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 428688192 257 ----TILKPenffkG-------------INNSGHLLPHSQIvikknqakfGQIIIKSD--SLFKGYY--PH-YKNS---- 310
Cdd:COG0365 350 nlpgLPVKP-----GsmgkpvpgydvavVDEDGNPVPPGEE---------GELVIKGPwpGMFRGYWndPErYRETyfgr 415
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 428688192 311 --NYFLTDDLGYFDQDNFLHIVGRNSQKIISGGENVYPCEIENVVIKTGLVKDIVVVGKNDHYWGQIICAVYVAISGY-D 387
Cdd:COG0365 416 fpGWYRTGDGARRDEDGYFWILGRSDDVINVSGHRIGTAEIESALVSHPAVAEAAVVGVPDEIRGQVVKAFVVLKPGVeP 495
|
250 260 270
....*....|....*....|....*....|....*....
gi 428688192 388 TEYLVNNIKAKLRSHLSHYKIPKLWLKVDQIPRNPQGKI 426
Cdd:COG0365 496 SDELAKELQAHVREELGPYAYPREIEFVDELPKTRSGKI 534
|
|
| PRK07470 |
PRK07470 |
acyl-CoA synthetase; Validated |
155-426 |
2.07e-20 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 180988 [Multi-domain] Cd Length: 528 Bit Score: 93.57 E-value: 2.07e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 428688192 155 PLYHVSGLMQIVRtfVTGGSLAI------YDYSLLKKEIQNHNYDNFFIslVPTQLNFLLENfPDwLKKFET-----VLV 223
Cdd:PRK07470 214 PLSHGAGIHQLCQ--VARGAATVllpserFDPAEVWALVERHRVTNLFT--VPTILKMLVEH-PA-VDRYDHsslryVIY 287
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 428688192 224 GGSATpktllqncYRQKINLALT---------YGMTETASGVTILKPENFFK------GINNSGHLLPHSQIVIKKNQAK 288
Cdd:PRK07470 288 AGAPM--------YRADQKRALAklgkvlvqyFGLGEVTGNITVLPPALHDAedgpdaRIGTCGFERTGMEVQIQDDEGR 359
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 428688192 289 ------FGQIIIKSDSLFKGYYPH-------YKNSnYFLTDDLGYFDQDNFLHIVGRNSQKIISGGENVYPCEIENVVIK 355
Cdd:PRK07470 360 elppgeTGEICVIGPAVFAGYYNNpeanakaFRDG-WFRTGDLGHLDARGFLYITGRASDMYISGGSNVYPREIEEKLLT 438
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 428688192 356 TGLVKDIVVVGKNDHYWGQIICAVYVAISGYDTEylvnniKAKLRSHLSH----YKIPKLWLKVDQIPRNPQGKI 426
Cdd:PRK07470 439 HPAVSEVAVLGVPDPVWGEVGVAVCVARDGAPVD------EAELLAWLDGkvarYKLPKRFFFWDALPKSGYGKI 507
|
|
| FACL_like_5 |
cd05924 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
304-428 |
4.45e-20 |
|
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: 91.29 E-value: 4.45e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 428688192 304 YPHYKNSNYFLTDDLGYFDQDNFLHIVGRNSQKIISGGENVYPCEIENVVIKTGLVKDIVVVGKNDHYWGQIICAVYVAI 383
Cdd:cd05924 238 FPEVDGVRYAVPGDRATVEADGTVTLLGRGSVCINTGGEKVFPEEVEEALKSHPAVYDVLVVGRPDERWGQEVVAVVQLR 317
|
90 100 110 120
....*....|....*....|....*....|....*....|....*
gi 428688192 384 SGYDTEylVNNIKAKLRSHLSHYKIPKLWLKVDQIPRNPQGKIDY 428
Cdd:cd05924 318 EGAGVD--LEELREHCRTRIARYKLPKQVVFVDEIERSPAGKADY 360
|
|
| FACL_like_6 |
cd05922 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
111-432 |
6.67e-20 |
|
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: 91.73 E-value: 6.67e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 428688192 111 IMIPTGGTSGNIKFAIHTWETLNASAKGFSQFWQRRKIN-FFCCLPLYHVSGLMQIVRTFVTGGSLAIYDYSLLK----K 185
Cdd:cd05922 121 LLLYTSGSTGSPKLVRLSHQNLLANARSIAEYLGITADDrALTVLPLSYDYGLSVLNTHLLRGATLVLTNDGVLDdafwE 200
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 428688192 186 EIQNHNYDNFfiSLVPTQLNFLLE-NFPDW-LKKFETVLVGGSATPKTLLQNcYRQKINLA---LTYGMTETASGVTILK 260
Cdd:cd05922 201 DLREHGATGL--AGVPSTYAMLTRlGFDPAkLPSLRYLTQAGGRLPQETIAR-LRELLPGAqvyVMYGQTEATRRMTYLP 277
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 428688192 261 PENFFKGINNSGHLLPHSQIVIKKNQA------KFGQIIIKSDSLFKGYY---PHYKNSNYFL----TDDLGYFDQDNFL 327
Cdd:cd05922 278 PERILEKPGSIGLAIPGGEFEILDDDGtptppgEPGEIVHRGPNVMKGYWndpPYRRKEGRGGgvlhTGDLARRDEDGFL 357
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 428688192 328 HIVGRNSQKIISGGENVYPCEIENVVIKTGLVKDIVVVGKNDHYwGQIICAVYVAISGYDTEYLVNnikaKLRSHLSHYK 407
Cdd:cd05922 358 FIVGRRDRMIKLFGNRISPTEIEAAARSIGLIIEAAAVGLPDPL-GEKLALFVTAPDKIDPKDVLR----SLAERLPPYK 432
|
330 340
....*....|....*....|....*
gi 428688192 408 IPKLWLKVDQIPRNPQGKIDYGYLE 432
Cdd:cd05922 433 VPATVRVVDELPLTASGKVDYAALR 457
|
|
| PRK06087 |
PRK06087 |
medium-chain fatty-acid--CoA ligase; |
115-426 |
9.76e-20 |
|
medium-chain fatty-acid--CoA ligase;
Pssm-ID: 180393 [Multi-domain] Cd Length: 547 Bit Score: 91.73 E-value: 9.76e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 428688192 115 TGGTSGNIKFAIHTWETLNASAKGFSQFWQRRKIN-FFCCLPLYHVSGLMQ-IVRTFVTGGSLAIYDYSLLKKEIQNHNY 192
Cdd:PRK06087 195 TSGTEGLPKGVMLTHNNILASERAYCARLNLTWQDvFMMPAPLGHATGFLHgVTAPFLIGARSVLLDIFTPDACLALLEQ 274
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 428688192 193 DNFFISLVPTQLNF----LLENFPDWLKKFETVLVGGSATPKTLLQNCYRQKINLALTYGMTETASGVTILKPENFFKGI 268
Cdd:PRK06087 275 QRCTCMLGATPFIYdllnLLEKQPADLSALRFFLCGGTTIPKKVARECQQRGIKLLSVYGSTESSPHAVVNLDDPLSRFM 354
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 428688192 269 NNSGHLLPHSQI-VIKKNQAKF-----GQIIIKSDSLFKGYYPHYKNSN-------YFLTDDLGYFDQDNFLHIVGRNSQ 335
Cdd:PRK06087 355 HTDGYAAAGVEIkVVDEARKTLppgceGEEASRGPNVFMGYLDEPELTAraldeegWYYSGDLCRMDEAGYIKITGRKKD 434
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 428688192 336 KIISGGENVYPCEIENVVIKTGLVKDIVVVGKNDHYWGQIICAVYVAISGYDTEYLVNNIKAKLRSHLSHYKIPKLWLKV 415
Cdd:PRK06087 435 IIVRGGENISSREVEDILLQHPKIHDACVVAMPDERLGERSCAYVVLKAPHHSLTLEEVVAFFSRKRVAKYKYPEHIVVI 514
|
330
....*....|.
gi 428688192 416 DQIPRNPQGKI 426
Cdd:PRK06087 515 DKLPRTASGKI 525
|
|
| PRK08314 |
PRK08314 |
long-chain-fatty-acid--CoA ligase; Validated |
102-426 |
1.28e-19 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236235 [Multi-domain] Cd Length: 546 Bit Score: 91.17 E-value: 1.28e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 428688192 102 PPHNHSYQGI-MIP-TGGTSGNIKFAIHTWETLNASAKGfSQFWQRRKIN--FFCCLPLYHVSGLMQIVRTFVTGGS--- 174
Cdd:PRK08314 183 PPHTAGPDDLaVLPyTSGTTGVPKGCMHTHRTVMANAVG-SVLWSNSTPEsvVLAVLPLFHVTGMVHSMNAPIYAGAtvv 261
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 428688192 175 -LAIYDYSLLKKEIQNH---NYDNffislVPTQLNFLLENfPDW----LKKFETVLVGGSATPKTLLQNCYRQ-KINLAL 245
Cdd:PRK08314 262 lMPRWDREAAARLIERYrvtHWTN-----IPTMVVDFLAS-PGLaerdLSSLRYIGGGGAAMPEAVAERLKELtGLDYVE 335
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 428688192 246 TYGMTETASGvTILKPENFFK----GIN-----------NSGHLLPHSQIvikknqakfGQIIIKSDSLFKGYYPHYKNS 310
Cdd:PRK08314 336 GYGLTETMAQ-THSNPPDRPKlqclGIPtfgvdarvidpETLEELPPGEV---------GEIVVHGPQVFKGYWNRPEAT 405
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 428688192 311 ----------NYFLTDDLGYFDQDNFLHIVGRNSQKIISGGENVYPCEIENVVIKTGLVKDIVVVGKNDHYWGQIICAVY 380
Cdd:PRK08314 406 aeafieidgkRFFRTGDLGRMDEEGYFFITDRLKRMINASGFKVWPAEVENLLYKHPAIQEACVIATPDPRRGETVKAVV 485
|
330 340 350 360
....*....|....*....|....*....|....*....|....*.
gi 428688192 381 VAISGYDTEYLVNNIKAKLRSHLSHYKIPKLWLKVDQIPRNPQGKI 426
Cdd:PRK08314 486 VLRPEARGKTTEEEIIAWAREHMAAYKYPRIVEFVDSLPKSGSGKI 531
|
|
| PRK13295 |
PRK13295 |
cyclohexanecarboxylate-CoA ligase; Reviewed |
112-435 |
2.25e-19 |
|
cyclohexanecarboxylate-CoA ligase; Reviewed
Pssm-ID: 171961 [Multi-domain] Cd Length: 547 Bit Score: 90.50 E-value: 2.25e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 428688192 112 MIPTGGTSGNIKFAIHTWETLNAsakGFSQFWQRRKIN----FFCCLPLYHVSGLMQIVRTFVTGGSLAIY----DYSLL 183
Cdd:PRK13295 202 LIYTSGTTGEPKGVMHTANTLMA---NIVPYAERLGLGaddvILMASPMAHQTGFMYGLMMPVMLGATAVLqdiwDPARA 278
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 428688192 184 KKEIQNHNYdNFFISLVP--TQLNFLLENFPDWLKKFETVLVGGSATPKTLLQNCyRQKINLALT--YGMTETASgVTIL 259
Cdd:PRK13295 279 AELIRTEGV-TFTMASTPflTDLTRAVKESGRPVSSLRTFLCAGAPIPGALVERA-RAALGAKIVsaWGMTENGA-VTLT 355
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 428688192 260 KPENFF-KGINNSGHLLPHSQI-VIKKNQAKF-----GQIIIKSDSLFKGYY--PHYKNSN---YFLTDDLGYFDQDNFL 327
Cdd:PRK13295 356 KLDDPDeRASTTDGCPLPGVEVrVVDADGAPLpagqiGRLQVRGCSNFGGYLkrPQLNGTDadgWFDTGDLARIDADGYI 435
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 428688192 328 HIVGRNSQKIISGGENVYPCEIENVVIKTGLVKDIVVVGKNDHYWGQIICAVYV--AISGYDTEYLVNNIKAKlrsHLSH 405
Cdd:PRK13295 436 RISGRSKDVIIRGGENIPVVEIEALLYRHPAIAQVAIVAYPDERLGERACAFVVprPGQSLDFEEMVEFLKAQ---KVAK 512
|
330 340 350
....*....|....*....|....*....|
gi 428688192 406 YKIPKLWLKVDQIPRNPQGKIDYGYLEKML 435
Cdd:PRK13295 513 QYIPERLVVRDALPRTPSGKIQKFRLREML 542
|
|
| LC_FACL_like |
cd05914 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); The members of this family are ... |
14-426 |
5.68e-19 |
|
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: 88.65 E-value: 5.68e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 428688192 14 TYNNQHISL-EIKYYINKI-----IKRENQQNRIIFLSTNNPQQFISvFFASIITKSSIFLLNPHWQQEELQQVYKLVKP 87
Cdd:cd05914 2 YYGGEPLTYkDLADNIAKFalllkINGVGTGDRVALMGENRPEWGIA-FFAIWTYGAIAVPILAEFTADEVHHILNHSEA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 428688192 88 DFLFSDHLEKTyynpphnhsyqGIMIPTGGTSGNIKFAIHTWETLNASAKGFSQFWQRRKIN-FFCCLPLYHVSGLMQiv 166
Cdd:cd05914 81 KAIFVSDEDDV-----------ALINYTSGTTGNSKGVMLTYRNIVSNVDGVKEVVLLGKGDkILSILPLHHIYPLTF-- 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 428688192 167 rTFVTGGSLAIYDYSL-------------------------------LKKEIQNHNYDNFFISLVPTQLNF--------- 206
Cdd:cd05914 148 -TLLLPLLNGAHVVFLdkipsakiialafaqvtptlgvpvplviekiFKMDIIPKLTLKKFKFKLAKKINNrkirklafk 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 428688192 207 -LLENFPDWLKKFetvLVGGSATPKTLLQNCYRQKINLALTYGMTETASGVTILKPENFFKGinNSGHLLPHSQIVIKKN 285
Cdd:cd05914 227 kVHEAFGGNIKEF---VIGGAKINPDVEEFLRTIGFPYTIGYGMTETAPIISYSPPNRIRLG--SAGKVIDGVEVRIDSP 301
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 428688192 286 QAKF--GQIIIKSDSLFKGYyphYKN----------SNYFLTDDLGYFDQDNFLHIVGRNSQKIISG-GENVYPCEIENV 352
Cdd:cd05914 302 DPATgeGEIIVRGPNVMKGY---YKNpeataeafdkDGWFHTGDLGKIDAEGYLYIRGRKKEMIVLSsGKNIYPEEIEAK 378
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 428688192 353 VIKTG--LVKDIVVvgknDHYWGQIICAVYVAISGYDTEYLVNNIKA-------KLRSHLSHY-KIPKLWLKVDQIPRNP 422
Cdd:cd05914 379 INNMPfvLESLVVV----QEKKLVALAYIDPDFLDVKALKQRNIIDAikwevrdKVNQKVPNYkKISKVKIVKEEFEKTP 454
|
....
gi 428688192 423 QGKI 426
Cdd:cd05914 455 KGKI 458
|
|
| PRK13390 |
PRK13390 |
acyl-CoA synthetase; Provisional |
247-431 |
8.37e-19 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 139538 [Multi-domain] Cd Length: 501 Bit Score: 88.53 E-value: 8.37e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 428688192 247 YGMTETASGVTILKPENFFKGI-------NNSGHLLPHSQIvikknqakfGQIIIKSDSLFKGYY---------PHYKNS 310
Cdd:PRK13390 308 HGMTFIDSPDWLAHPGSVGRSVlgdlhicDDDGNELPAGRI---------GTVYFERDRLPFRYLndpektaaaQHPAHP 378
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 428688192 311 NYFLTDDLGYFDQDNFLHIVGRNSQKIISGGENVYPCEIENVVIKTGLVKDIVVVGKNDHYWGQIICAVYVAISGYD-TE 389
Cdd:PRK13390 379 FWTTVGDLGSVDEDGYLYLADRKSFMIISGGVNIYPQETENALTMHPAVHDVAVIGVPDPEMGEQVKAVIQLVEGIRgSD 458
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 428688192 390 YLVNNIKAKLRSHLSHYKIPKLWLKVDQIPRNPQGKIDYGYL 431
Cdd:PRK13390 459 ELARELIDYTRSRIAHYKAPRSVEFVDELPRTPTGKLVKGLL 500
|
|
| 4CL |
cd05904 |
4-Coumarate-CoA Ligase (4CL); 4-Coumarate:coenzyme A ligase is a key enzyme in the ... |
117-426 |
8.37e-19 |
|
4-Coumarate-CoA Ligase (4CL); 4-Coumarate:coenzyme A ligase is a key enzyme in the phenylpropanoid metabolic pathway for monolignol and flavonoid biosynthesis. It catalyzes the synthesis of hydroxycinnamate-CoA thioesters in a two-step reaction, involving the formation of hydroxycinnamate-AMP anhydride and the nucleophilic substitution of AMP by CoA. The phenylpropanoid pathway is one of the most important secondary metabolism pathways in plants and hydroxycinnamate-CoA thioesters are the precursors of lignin and other important phenylpropanoids.
Pssm-ID: 341230 [Multi-domain] Cd Length: 505 Bit Score: 88.45 E-value: 8.37e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 428688192 117 GTSGNIKFAIHTWETLNASAKGFSQFWQRRKIN---FFCCLPLYHVSGLMQIVRTFVTGGSLAI----YDYSLLKKEIQN 189
Cdd:cd05904 168 GTTGRSKGVMLTHRNLIAMVAQFVAGEGSNSDSedvFLCVLPMFHIYGLSSFALGLLRLGATVVvmprFDLEELLAAIER 247
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 428688192 190 HNYDNFFIslVPTQL-----NFLLENFPdwLKKFETVLVGGSATPKTLLQNCyRQKI---NLALTYGMTE-TASGVTILK 260
Cdd:cd05904 248 YKVTHLPV--VPPIVlalvkSPIVDKYD--LSSLRQIMSGAAPLGKELIEAF-RAKFpnvDLGQGYGMTEsTGVVAMCFA 322
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 428688192 261 PENFFKGINNSGHLLP--HSQIV-IKKNQA----KFGQIIIKSDSLFKGYYphyKN---------SNYFL-TDDLGYFDQ 323
Cdd:cd05904 323 PEKDRAKYGSVGRLVPnvEAKIVdPETGESlppnQTGELWIRGPSIMKGYL---NNpeataatidKEGWLhTGDLCYIDE 399
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 428688192 324 DNFLHIVGRNSQKIISGGENVYPCEIENVVIKTGLVKDIVVVGKNDHYWGQIICAVYVAISGYD-TEYLVNNIKAKlrsH 402
Cdd:cd05904 400 DGYLFIVDRLKELIKYKGFQVAPAELEALLLSHPEILDAAVIPYPDEEAGEVPMAFVVRKPGSSlTEDEIMDFVAK---Q 476
|
330 340
....*....|....*....|....*
gi 428688192 403 LSHYK-IPKLWLkVDQIPRNPQGKI 426
Cdd:cd05904 477 VAPYKkVRKVAF-VDAIPKSPSGKI 500
|
|
| PLN02860 |
PLN02860 |
o-succinylbenzoate-CoA ligase |
155-426 |
1.31e-18 |
|
o-succinylbenzoate-CoA ligase
Pssm-ID: 215464 [Multi-domain] Cd Length: 563 Bit Score: 88.32 E-value: 1.31e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 428688192 155 PLYHVSGLMQIVRTFVTGGS---LAIYDYSLLKKEIQNHNYDNFFIslVPTQLNFLLEnfPDWLKK----FETV---LVG 224
Cdd:PLN02860 221 PLCHIGGLSSALAMLMVGAChvlLPKFDAKAALQAIKQHNVTSMIT--VPAMMADLIS--LTRKSMtwkvFPSVrkiLNG 296
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 428688192 225 GSATPKTLLQNCYRQKINLAL--TYGMTETASGVTIL------------KPENFFKGINNSGHLL---------PHSQIV 281
Cdd:PLN02860 297 GGSLSSRLLPDAKKLFPNAKLfsAYGMTEACSSLTFMtlhdptlespkqTLQTVNQTKSSSVHQPqgvcvgkpaPHVELK 376
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 428688192 282 IKKNQA-KFGQIIIKSDSLFKGYYPHYK-------NSNYFLTDDLGYFDQDNFLHIVGRNSQKIISGGENVYPCEIENVV 353
Cdd:PLN02860 377 IGLDESsRVGRILTRGPHVMLGYWGQNSetasvlsNDGWLDTGDIGWIDKAGNLWLIGRSNDRIKTGGENVYPEEVEAVL 456
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 428688192 354 IKTGLVKDIVVVGKNDHYWGQIICAVyVAI------SGYDTEYLVNNI---KAKLRSH-----LSHYKIPKLWLK-VDQI 418
Cdd:PLN02860 457 SQHPGVASVVVVGVPDSRLTEMVVAC-VRLrdgwiwSDNEKENAKKNLtlsSETLRHHcreknLSRFKIPKLFVQwRKPF 535
|
....*...
gi 428688192 419 PRNPQGKI 426
Cdd:PLN02860 536 PLTTTGKI 543
|
|
| PRK12406 |
PRK12406 |
long-chain-fatty-acid--CoA ligase; Provisional |
112-426 |
1.34e-18 |
|
long-chain-fatty-acid--CoA ligase; Provisional
Pssm-ID: 183506 [Multi-domain] Cd Length: 509 Bit Score: 87.83 E-value: 1.34e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 428688192 112 MIPTGGTSGNIK----FAIHTWETLNASAKGFSQFWQRRKINFFCCLPLYHVSGLMQIVRTFVTGGSLAI---YDYSLLK 184
Cdd:PRK12406 157 MIYTSGTTGHPKgvrrAAPTPEQAAAAEQMRALIYGLKPGIRALLTGPLYHSAPNAYGLRAGRLGGVLVLqprFDPEELL 236
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 428688192 185 KEIQNHNYDNFFIslVPTQLNFLLENFPDWLKKFET-----VLVGGSATPKTLlqncYRQKIN-----LALTYGMTETaS 254
Cdd:PRK12406 237 QLIERHRITHMHM--VPTMFIRLLKLPEEVRAKYDVsslrhVIHAAAPCPADV----KRAMIEwwgpvIYEYYGSTES-G 309
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 428688192 255 GVTILKPENFFKGINNSGHLLPHSQI-VIKKN-----QAKFGQIIIKSDSlfkgyYPHYKNSNY-----------FLT-D 316
Cdd:PRK12406 310 AVTFATSEDALSHPGTVGKAAPGAELrFVDEDgrplpQGEIGEIYSRIAG-----NPDFTYHNKpekraeidrggFITsG 384
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 428688192 317 DLGYFDQDNFLHIVGRNSQKIISGGENVYPCEIENVVIKTGLVKDIVVVGKNDHYWGQIICAVYVAISGYDTEylVNNIK 396
Cdd:PRK12406 385 DVGYLDADGYLFLCDRKRDMVISGGVNIYPAEIEAVLHAVPGVHDCAVFGIPDAEFGEALMAVVEPQPGATLD--EADIR 462
|
330 340 350
....*....|....*....|....*....|
gi 428688192 397 AKLRSHLSHYKIPKLWLKVDQIPRNPQGKI 426
Cdd:PRK12406 463 AQLKARLAGYKVPKHIEIMAELPREDSGKI 492
|
|
| Firefly_Luc |
cd17642 |
insect luciferase, similar to plant 4-coumarate: CoA ligases; This family contains insect ... |
38-434 |
1.80e-18 |
|
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: 87.58 E-value: 1.80e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 428688192 38 QNRIIFLSTNNPQQFISVFFASIITKSsIFLLNPHWQQEELQQVYKLVKPDfLFSDHLEKTYYNPPHNHSYQ-GIMIPTG 116
Cdd:cd17642 116 KPTIVFCSKKGLQKVLNVQKKLKIIKT-IIILDSKEDYKGYQCLYTFITQN-LPPGFNEYDFKPPSFDRDEQvALIMNSS 193
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 428688192 117 GTSGNIKFAIHTWETLNASakgFSQFWQRRKIN-------FFCCLPLYHVSGLMQIVRTFVTGGSLAI---YDYSLLKKE 186
Cdd:cd17642 194 GSTGLPKGVQLTHKNIVAR---FSHARDPIFGNqiipdtaILTVIPFHHGFGMFTTLGYLICGFRVVLmykFEEELFLRS 270
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 428688192 187 IQNHNYDNFFisLVPTQLNF-----LLENFPdwLKKFETVLVGGSATPKTLlQNCYRQKINLALT---YGMTETASGVtI 258
Cdd:cd17642 271 LQDYKVQSAL--LVPTLFAFfakstLVDKYD--LSNLHEIASGGAPLSKEV-GEAVAKRFKLPGIrqgYGLTETTSAI-L 344
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 428688192 259 LKPENFFKGiNNSGHLLP-HSQIVIKKNQAKF------GQIIIKSDSLFKGYYPHYKNSN-------YFLTDDLGYFDQD 324
Cdd:cd17642 345 ITPEGDDKP-GAVGKVVPfFYAKVVDLDTGKTlgpnerGELCVKGPMIMKGYVNNPEATKalidkdgWLHSGDIAYYDED 423
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 428688192 325 NFLHIVGRNSQKIISGGENVYPCEIENVVIKTGLVKDIVVVGKNDHYWGQIICAVYVAISG-YDTEYLVNNIKAklrSHL 403
Cdd:cd17642 424 GHFFIVDRLKSLIKYKGYQVPPAELESILLQHPKIFDAGVAGIPDEDAGELPAAVVVLEAGkTMTEKEVMDYVA---SQV 500
|
410 420 430
....*....|....*....|....*....|....*.
gi 428688192 404 SHYKipklWLK-----VDQIPRNPQGKIDYGYLEKM 434
Cdd:cd17642 501 STAK----RLRggvkfVDEVPKGLTGKIDRRKIREI 532
|
|
| PRK07798 |
PRK07798 |
acyl-CoA synthetase; Validated |
312-428 |
3.65e-18 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236100 [Multi-domain] Cd Length: 533 Bit Score: 86.86 E-value: 3.65e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 428688192 312 YFLTDDLGYFDQDNFLHIVGRNSQKIISGGENVYPCEIENVVIKTGLVKDIVVVGKNDHYWGQIICAVyVAISGyDTEYL 391
Cdd:PRK07798 409 YAIPGDRARVEADGTITLLGRGSVCINTGGEKVFPEEVEEALKAHPDVADALVVGVPDERWGQEVVAV-VQLRE-GARPD 486
|
90 100 110
....*....|....*....|....*....|....*..
gi 428688192 392 VNNIKAKLRSHLSHYKIPKLWLKVDQIPRNPQGKIDY 428
Cdd:PRK07798 487 LAELRAHCRSSLAGYKVPRAIWFVDEVQRSPAGKADY 523
|
|
| PRK08751 |
PRK08751 |
long-chain fatty acid--CoA ligase; |
115-426 |
4.49e-18 |
|
long-chain fatty acid--CoA ligase;
Pssm-ID: 181546 [Multi-domain] Cd Length: 560 Bit Score: 86.47 E-value: 4.49e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 428688192 115 TGGTSGNIKFAIHTWETLNASAKGFSQFWQ------RRKINFFCCLPLYHVSGLMQIVRTFVTGGSLAIY-----DYSLL 183
Cdd:PRK08751 216 TGGTTGVAKGAMLTHRNLVANMQQAHQWLAgtgkleEGCEVVITALPLYHIFALTANGLVFMKIGGCNHLisnprDMPGF 295
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 428688192 184 KKEIQNHNYDNFfiSLVPTQLNFLLeNFPDW----LKKFETVLVGGSATPKTLLQNcYRQKINLAL--TYGMTETASGVT 257
Cdd:PRK08751 296 VKELKKTRFTAF--TGVNTLFNGLL-NTPGFdqidFSSLKMTLGGGMAVQRSVAER-WKQVTGLTLveAYGLTETSPAAC 371
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 428688192 258 IlKPENFFKGINNSGHLLPHSQIVIKKNQAK------FGQIIIKSDSLFKGYYPHYKNS-------NYFLTDDLGYFDQD 324
Cdd:PRK08751 372 I-NPLTLKEYNGSIGLPIPSTDACIKDDAGTvlaigeIGELCIKGPQVMKGYWKRPEETakvmdadGWLHTGDIARMDEQ 450
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 428688192 325 NFLHIVGRNSQKIISGGENVYPCEIENVVIKTGLVKDIVVVGKNDHYWGQIicaVYVAISGYDTEYLVNNIKAKLRSHLS 404
Cdd:PRK08751 451 GFVYIVDRKKDMILVSGFNVYPNEIEDVIAMMPGVLEVAAVGVPDEKSGEI---VKVVIVKKDPALTAEDVKAHARANLT 527
|
330 340
....*....|....*....|..
gi 428688192 405 HYKIPKLWLKVDQIPRNPQGKI 426
Cdd:PRK08751 528 GYKQPRIIEFRKELPKTNVGKI 549
|
|
| PRK06710 |
PRK06710 |
long-chain-fatty-acid--CoA ligase; Validated |
154-426 |
7.62e-18 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 180666 [Multi-domain] Cd Length: 563 Bit Score: 85.86 E-value: 7.62e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 428688192 154 LPLYHVSGLMQIVRTFVTGGSLAI----YDYSLLKKEIQNHNydnffISLVP--TQLNFLLENFPdWLKKFET----VLV 223
Cdd:PRK06710 256 LPFFHVYGMTAVMNLSIMQGYKMVlipkFDMKMVFEAIKKHK-----VTLFPgaPTIYIALLNSP-LLKEYDIssirACI 329
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 428688192 224 GGSATPKTLLQNCYRQKI--NLALTYGMTETaSGVTilkPENFF--KGINNS-GHLLPHSQIVIKKNQ-------AKFGQ 291
Cdd:PRK06710 330 SGSAPLPVEVQEKFETVTggKLVEGYGLTES-SPVT---HSNFLweKRVPGSiGVPWPDTEAMIMSLEtgealppGEIGE 405
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 428688192 292 IIIKSDSLFKGYYPHYKNSNYFLTD------DLGYFDQDNFLHIVGRNSQKIISGGENVYPCEIENVVIKTGLVKDIVVV 365
Cdd:PRK06710 406 IVVKGPQIMKGYWNKPEETAAVLQDgwlhtgDVGYMDEDGFFYVKDRKKDMIVASGFNVYPREVEEVLYEHEKVQEVVTI 485
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 428688192 366 GKNDHYWGQIICAvYVAISgYDTEYLVNNIKAKLRSHLSHYKIPKLWLKVDQIPRNPQGKI 426
Cdd:PRK06710 486 GVPDPYRGETVKA-FVVLK-EGTECSEEELNQFARKYLAAYKVPKVYEFRDELPKTTVGKI 544
|
|
| PRK13391 |
PRK13391 |
acyl-CoA synthetase; Provisional |
317-426 |
1.06e-17 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 184022 [Multi-domain] Cd Length: 511 Bit Score: 85.13 E-value: 1.06e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 428688192 317 DLGYFDQDNFLHIVGRNSQKIISGGENVYPCEIENVVIKTGLVKDIVVVGKNDHYWGQIICAVYVAISGYD-TEYLVNNI 395
Cdd:PRK13391 388 DIGYVDEDGYLYLTDRAAFMIISGGVNIYPQEAENLLITHPKVADAAVFGVPNEDLGEEVKAVVQPVDGVDpGPALAAEL 467
|
90 100 110
....*....|....*....|....*....|.
gi 428688192 396 KAKLRSHLSHYKIPKLWLKVDQIPRNPQGKI 426
Cdd:PRK13391 468 IAFCRQRLSRQKCPRSIDFEDELPRLPTGKL 498
|
|
| PRK08316 |
PRK08316 |
acyl-CoA synthetase; Validated |
153-426 |
1.32e-17 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 181381 [Multi-domain] Cd Length: 523 Bit Score: 84.98 E-value: 1.32e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 428688192 153 CLPLYHVSG----LMQIVRTFVTGGSLAIYDYSLLKKEIQNHNYDNFFisLVPTQLNFLLeNFPDwlkkFETVLV----- 223
Cdd:PRK08316 218 ALPLYHCAQldvfLGPYLYVGATNVILDAPDPELILRTIEAERITSFF--APPTVWISLL-RHPD----FDTRDLsslrk 290
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 428688192 224 ---GGSATPKTLLQNCYRQKINLAL--TYGMTETASGVTILKPENFFKGINNSGH--LLPHSQIVIKKNQA----KFGQI 292
Cdd:PRK08316 291 gyyGASIMPVEVLKELRERLPGLRFynCYGQTEIAPLATVLGPEEHLRRPGSAGRpvLNVETRVVDDDGNDvapgEVGEI 370
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 428688192 293 IIKSDSLFKGYYphyKNSN---------YFLTDDLGYFDQDNFLHIVGRNSQKIISGGENVYPCEIENVVIKTGLVKDIV 363
Cdd:PRK08316 371 VHRSPQLMLGYW---DDPEktaeafrggWFHSGDLGVMDEEGYITVVDRKKDMIKTGGENVASREVEEALYTHPAVAEVA 447
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 428688192 364 VVGKNDHYWGQIICAVYVAISGYD-TEylvNNIKAKLRSHLSHYKIPKLWLKVDQIPRNPQGKI 426
Cdd:PRK08316 448 VIGLPDPKWIEAVTAVVVPKAGATvTE---DELIAHCRARLAGFKVPKRVIFVDELPRNPSGKI 508
|
|
| FAA1 |
COG1022 |
Long-chain acyl-CoA synthetase (AMP-forming) [Lipid transport and metabolism]; |
241-371 |
2.15e-17 |
|
Long-chain acyl-CoA synthetase (AMP-forming) [Lipid transport and metabolism];
Pssm-ID: 440645 [Multi-domain] Cd Length: 603 Bit Score: 84.38 E-value: 2.15e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 428688192 241 INLALTYGMTETASGVTILKPENFFkgINNSGHLLPHSQIVIkknqAKFGQIIIKSDSLFKGYYphyKNS---------- 310
Cdd:COG1022 372 IPVLEGYGLTETSPVITVNRPGDNR--IGTVGPPLPGVEVKI----AEDGEILVRGPNVMKGYY---KNPeataeafdad 442
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 428688192 311 NYFLTDDLGYFDQDNFLHIVGRNSQKII-SGGENVYPCEIENVVIKTGLVKDIVVVGKNDHY 371
Cdd:COG1022 443 GWLHTGDIGELDEDGFLRITGRKKDLIVtSGGKNVAPQPIENALKASPLIEQAVVVGDGRPF 504
|
|
| PRK12583 |
PRK12583 |
acyl-CoA synthetase; Provisional |
200-426 |
2.20e-17 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 237145 [Multi-domain] Cd Length: 558 Bit Score: 84.44 E-value: 2.20e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 428688192 200 VPTQlnFLLE-NFPDW----LKKFETVLVGGSATPKTLLQNCYRQ----KINLAltYGMTETaSGVTIL--KPENFFKGI 268
Cdd:PRK12583 298 VPTM--FIAElDHPQRgnfdLSSLRTGIMAGAPCPIEVMRRVMDEmhmaEVQIA--YGMTET-SPVSLQttAADDLERRV 372
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 428688192 269 NNSGHLLPHSQIVIKKNQA------KFGQIIIKSDSLFKGYYPHYKNS-------NYFLTDDLGYFDQDNFLHIVGRNSQ 335
Cdd:PRK12583 373 ETVGRTQPHLEVKVVDPDGatvprgEIGELCTRGYSVMKGYWNNPEATaesidedGWMHTGDLATMDEQGYVRIVGRSKD 452
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 428688192 336 KIISGGENVYPCEIENVVIKTGLVKDIVVVGKNDHYWGQIICAVYVAISGY--DTEYLVNNIKAKlrshLSHYKIPKLWL 413
Cdd:PRK12583 453 MIIRGGENIYPREIEEFLFTHPAVADVQVFGVPDEKYGEEIVAWVRLHPGHaaSEEELREFCKAR----IAHFKVPRYFR 528
|
250
....*....|...
gi 428688192 414 KVDQIPRNPQGKI 426
Cdd:PRK12583 529 FVDEFPMTVTGKV 541
|
|
| DltA |
cd05945 |
D-alanine:D-alanyl carrier protein ligase (DltA) and similar proteins; This family includes ... |
69-431 |
2.67e-17 |
|
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: 83.84 E-value: 2.67e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 428688192 69 LNPHWQQEELQQVYKLVKPDFLFSDhlektyynpPHNHSYqgiMIPTGGTSGNIKFAIHTWETLNASAKGFSQFWQRRKI 148
Cdd:cd05945 71 LDASSPAERIREILDAAKPALLIAD---------GDDNAY---IIFTSGSTGRPKGVQISHDNLVSFTNWMLSDFPLGPG 138
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 428688192 149 NFFCCLPLYH--VSgLMQIVRTFVTGGSL------AIYDYSLLKKEIQNHNYdNFFISlVPT--QLNFLLENF-PDWLKK 217
Cdd:cd05945 139 DVFLNQAPFSfdLS-VMDLYPALASGATLvpvprdATADPKQLFRFLAEHGI-TVWVS-TPSfaAMCLLSPTFtPESLPS 215
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 428688192 218 FETVLVGGSATPKTL---LQNCYRQK--INlalTYGMTETASGVTILKPENFFKGINNS---GHLLPHSQIVIKKNQAKF 289
Cdd:cd05945 216 LRHFLFCGEVLPHKTaraLQQRFPDAriYN---TYGPTEATVAVTYIEVTPEVLDGYDRlpiGYAKPGAKLVILDEDGRP 292
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 428688192 290 ------GQIIIKSDSLFKGY----------------YPHYKnsnyflTDDLGYFDQDNFLHIVGRNSQKIISGGENVYPC 347
Cdd:cd05945 293 vppgekGELVISGPSVSKGYlnnpektaaaffpdegQRAYR------TGDLVRLEADGLLFYRGRLDFQVKLNGYRIELE 366
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 428688192 348 EIENVVIKTGLVKDIVVVGKNDHYWGQIICAVYVAISGyDTEYLVNNIKAKLRSHLSHYKIPKLWLKVDQIPRNPQGKID 427
Cdd:cd05945 367 EIEAALRQVPGVKEAVVVPKYKGEKVTELIAFVVPKPG-AEAGLTKAIKAELAERLPPYMIPRRFVYLDELPLNANGKID 445
|
....
gi 428688192 428 YGYL 431
Cdd:cd05945 446 RKAL 449
|
|
| PLN02479 |
PLN02479 |
acetate-CoA ligase |
221-426 |
3.75e-17 |
|
acetate-CoA ligase
Pssm-ID: 178097 [Multi-domain] Cd Length: 567 Bit Score: 83.74 E-value: 3.75e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 428688192 221 VLVGGSATPKTLLQNCYRQKINLALTYGMTET--ASGVTILKPE------------NFFKGINNSGH-----LLPHSQIV 281
Cdd:PLN02479 315 VMTAGAAPPPSVLFAMSEKGFRVTHTYGLSETygPSTVCAWKPEwdslppeeqarlNARQGVRYIGLegldvVDTKTMKP 394
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 428688192 282 IKKNQAKFGQIIIKSDSLFKGYYPHYK------NSNYFLTDDLGYFDQDNFLHIVGRNSQKIISGGENVYPCEIENVVIK 355
Cdd:PLN02479 395 VPADGKTMGEIVMRGNMVMKGYLKNPKaneeafANGWFHSGDLGVKHPDGYIEIKDRSKDIIISGGENISSLEVENVVYT 474
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 428688192 356 TGLVKDIVVVGKNDHYWGQIICAVYVAISGY---DTEYLVNNIKAKLRSHLSHYKIPKLwLKVDQIPRNPQGKI 426
Cdd:PLN02479 475 HPAVLEASVVARPDERWGESPCAFVTLKPGVdksDEAALAEDIMKFCRERLPAYWVPKS-VVFGPLPKTATGKI 547
|
|
| PRK13383 |
PRK13383 |
acyl-CoA synthetase; Provisional |
315-426 |
4.02e-17 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 139531 [Multi-domain] Cd Length: 516 Bit Score: 83.51 E-value: 4.02e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 428688192 315 TDDLGYFDQDNFLHIVGRNSQKIISGGENVYPCEIENVVIKTGLVKDIVVVGKNDHYWGQIICAVYVAISGYDTEylVNN 394
Cdd:PRK13383 400 TGDMGYLDNAGRLFIVGREDDMIISGGENVYPRAVENALAAHPAVADNAVIGVPDERFGHRLAAFVVLHPGSGVD--AAQ 477
|
90 100 110
....*....|....*....|....*....|..
gi 428688192 395 IKAKLRSHLSHYKIPKLWLKVDQIPRNPQGKI 426
Cdd:PRK13383 478 LRDYLKDRVSRFEQPRDINIVSSIPRNPTGKV 509
|
|
| PRK08315 |
PRK08315 |
AMP-binding domain protein; Validated |
247-426 |
6.07e-17 |
|
AMP-binding domain protein; Validated
Pssm-ID: 236236 [Multi-domain] Cd Length: 559 Bit Score: 82.94 E-value: 6.07e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 428688192 247 YGMTETASGVTILKPEN-FFKGINNSGHLLPHSQI---------VIKKNQAkfGQIIIKSDSLFKGYYphyKN------- 309
Cdd:PRK08315 348 YGMTETSPVSTQTRTDDpLEKRVTTVGRALPHLEVkivdpetgeTVPRGEQ--GELCTRGYSVMKGYW---NDpektaea 422
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 428688192 310 --SNYFL-TDDLGYFDQDNFLHIVGRNSQKIISGGENVYPCEIENVVIKTGLVKDIVVVGKNDHYWGQIICAVYVAISGY 386
Cdd:PRK08315 423 idADGWMhTGDLAVMDEEGYVNIVGRIKDMIIRGGENIYPREIEEFLYTHPKIQDVQVVGVPDEKYGEEVCAWIILRPGA 502
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 428688192 387 D-TEylvNNIKAKLRSHLSHYKIPKLWLKVDQIPRNPQGKI 426
Cdd:PRK08315 503 TlTE---EDVRDFCRGKIAHYKIPRYIRFVDEFPMTVTGKI 540
|
|
| PRK05620 |
PRK05620 |
long-chain fatty-acid--CoA ligase; |
150-427 |
8.02e-17 |
|
long-chain fatty-acid--CoA ligase;
Pssm-ID: 180167 [Multi-domain] Cd Length: 576 Bit Score: 82.52 E-value: 8.02e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 428688192 150 FFCCLPLYHVSGLMQIVRTFVTGGSLAIYDYSL----LKKEI------QNHNYDNFFISLvptqLNFLLENFPDWLKkFE 219
Cdd:PRK05620 227 FLCCVPIYHVLSWGVPLAAFMSGTPLVFPGPDLsaptLAKIIatamprVAHGVPTLWIQL----MVHYLKNPPERMS-LQ 301
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 428688192 220 TVLVGGSATPKTLLQNC-YRQKINLALTYGMTETASGVTILKPENFFKG--------------------INNSGHLLPHS 278
Cdd:PRK05620 302 EIYVGGSAVPPILIKAWeERYGVDVVHVWGMTETSPVGTVARPPSGVSGearwayrvsqgrfpasleyrIVNDGQVMEST 381
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 428688192 279 QivikKNQakfGQIIIKSD------------------SLFKGYYPHYKNSNY-----FLTDDLGYFDQDNFLHIVGRNSQ 335
Cdd:PRK05620 382 D----RNE---GEIQVRGNwvtasyyhspteegggaaSTFRGEDVEDANDRFtadgwLRTGDVGSVTRDGFLTIHDRARD 454
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 428688192 336 KIISGGENVYPCEIENVVIKTGLVKDIVVVGKNDHYWGQIICAVYVAISGYD-TEYLVNNIKAKLRSHLSHYKIPKLWLK 414
Cdd:PRK05620 455 VIRSGGEWIYSAQLENYIMAAPEVVECAVIGYPDDKWGERPLAVTVLAPGIEpTRETAERLRDQLRDRLPNWMLPEYWTF 534
|
330
....*....|...
gi 428688192 415 VDQIPRNPQGKID 427
Cdd:PRK05620 535 VDEIDKTSVGKFD 547
|
|
| AAS_C |
cd05909 |
C-terminal domain of the acyl-acyl carrier protein synthetase (also called ... |
149-434 |
1.33e-16 |
|
C-terminal domain of the acyl-acyl carrier protein synthetase (also called 2-acylglycerophosphoethanolamine acyltransferase, Aas); Acyl-acyl carrier protein synthase (Aas) is a membrane protein responsible for a minor pathway of incorporating exogenous fatty acids into membrane phospholipids. Its in vitro activity is characterized by the ligation of free fatty acids between 8 and 18 carbons in length to the acyl carrier protein sulfydryl group (ACP-SH) in the presence of ATP and Mg2+. However, its in vivo function is as a 2-acylglycerophosphoethanolamine (2-acyl-GPE) acyltransferase. The reaction occurs in two steps: the acyl chain is first esterified to acyl carrier protein (ACP) via a thioester bond, followed by a second step where the acyl chain is transferred to a 2-acyllysophospholipid, thus completing the transacylation reaction. This model represents the C-terminal domain of the enzyme, which belongs to the class I adenylate-forming enzyme family, including acyl-CoA synthetases.
Pssm-ID: 341235 [Multi-domain] Cd Length: 490 Bit Score: 81.61 E-value: 1.33e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 428688192 149 NFFCCLPLYHVSGL-MQIVRTFVTGGSLAIYDYSLLKKEIQNHNYDN---FFISlVPTQLNFLLENF-PDWLKKFETVLV 223
Cdd:cd05909 190 VVFGALPFFHSFGLtGCLWLPLLSGIKVVFHPNPLDYKKIPELIYDKkatILLG-TPTFLRGYARAAhPEDFSSLRLVVA 268
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 428688192 224 GGSATPKTLLQNCY-RQKINLALTYGMTETASGVTILKPENFFKgINNSGHLLPHSQIVIKKNQAKF-------GQIIIK 295
Cdd:cd05909 269 GAEKLKDTLRQEFQeKFGIRILEGYGTTECSPVISVNTPQSPNK-EGTVGRPLPGMEVKIVSVETHEevpigegGLLLVR 347
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 428688192 296 SDSLFKGYYPHYKNSN------YFLTDDLGYFDQDNFLHIVGRNSQ--KIisGGENVYPCEIENVVIKT-GLVKDIVVVG 366
Cdd:cd05909 348 GPNVMLGYLNEPELTSfafgdgWYDTGDIGKIDGEGFLTITGRLSRfaKI--AGEMVSLEAIEDILSEIlPEDNEVAVVS 425
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 428688192 367 KNDHYWGQIICAVYVAIsgyDTEylvnniKAKLRSHLSHYKIPKLW-----LKVDQIPRNPQGKIDYGYLEKM 434
Cdd:cd05909 426 VPDGRKGEKIVLLTTTT---DTD------PSSLNDILKNAGISNLAkpsyiHQVEEIPLLGTGKPDYVTLKAL 489
|
|
| PRK07059 |
PRK07059 |
Long-chain-fatty-acid--CoA ligase; Validated |
115-426 |
1.71e-16 |
|
Long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 235923 [Multi-domain] Cd Length: 557 Bit Score: 81.61 E-value: 1.71e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 428688192 115 TGGTSGNIKFAIHTWETLNASaKGFSQFW-----QRRK----INFFCCLPLYH-----VSGLMqivrTFVTGG-SLAI-- 177
Cdd:PRK07059 212 TGGTTGVSKGATLLHRNIVAN-VLQMEAWlqpafEKKPrpdqLNFVCALPLYHifaltVCGLL----GMRTGGrNILIpn 286
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 428688192 178 -YDYSLLKKEIQNHNYDNFfiSLVPTQLNFLLENfPDW----LKKFETVLVGGSATPKTLLQNCYrQKINLALT--YGMT 250
Cdd:PRK07059 287 pRDIPGFIKELKKYQVHIF--PAVNTLYNALLNN-PDFdkldFSKLIVANGGGMAVQRPVAERWL-EMTGCPITegYGLS 362
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 428688192 251 ETASGVTIlkpeNFFKGINNSGHL---LPHSQIVIKKNQAK------FGQIIIKSDSLFKGYYPHYKNS-------NYFL 314
Cdd:PRK07059 363 ETSPVATC----NPVDATEFSGTIglpLPSTEVSIRDDDGNdlplgePGEICIRGPQVMAGYWNRPDETakvmtadGFFR 438
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 428688192 315 TDDLGYFDQDNFLHIVGRNSQKIISGGENVYPCEIENVVIKTGLVKDIVVVGKNDHYWGQiicAVYVAISGYDTEYLVNN 394
Cdd:PRK07059 439 TGDVGVMDERGYTKIVDRKKDMILVSGFNVYPNEIEEVVASHPGVLEVAAVGVPDEHSGE---AVKLFVVKKDPALTEED 515
|
330 340 350
....*....|....*....|....*....|..
gi 428688192 395 IKAKLRSHLSHYKIPKLWLKVDQIPRNPQGKI 426
Cdd:PRK07059 516 VKAFCKERLTNYKRPKFVEFRTELPKTNVGKI 547
|
|
| A_NRPS_Bac |
cd17655 |
bacitracin synthetase and related proteins; This family of the adenylation (A) domain of ... |
94-427 |
2.24e-16 |
|
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: 81.22 E-value: 2.24e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 428688192 94 HLEKTYYNPPHNHSYQGIMIPTGGTSGNIKFAIHTWETLNASAKGFSQ-FWQRRKINFFCCLPLYHVSGLMQIVRTFVTG 172
Cdd:cd17655 124 HEESENLEPVSKSDDLAYVIYTSGSTGKPKGVMIEHRGVVNLVEWANKvIYQGEHLRVALFASISFDASVTEIFASLLSG 203
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 428688192 173 GSLAIY------DYSLLKKEIQNHNYDnfFISLVPTQLNFLLENFPDWLKKFETVLVGGSATPKTLLQN---CYRQKINL 243
Cdd:cd17655 204 NTLYIVrketvlDGQALTQYIRQNRIT--IIDLTPAHLKLLDAADDSEGLSLKHLIVGGEALSTELAKKiieLFGTNPTI 281
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 428688192 244 ALTYGMTETASGVTI--LKPENFFKGINNSGHLLPHSQIVIKKNQAKF------GQIIIKSDSLFKGYY----------- 304
Cdd:cd17655 282 TNAYGPTETTVDASIyqYEPETDQQVSVPIGKPLGNTRIYILDQYGRPqpvgvaGELYIGGEGVARGYLnrpeltaekfv 361
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 428688192 305 --PHYKNSNYFLTDDLGYFDQDNFLHIVGRNSQKIISGGENVYPCEIENVVIKTGLVKDIVVVGKNDHYWGQIICAVYVA 382
Cdd:cd17655 362 ddPFVPGERMYRTGDLARWLPDGNIEFLGRIDHQVKIRGYRIELGEIEARLLQHPDIKEAVVIARKDEQGQNYLCAYIVS 441
|
330 340 350 360
....*....|....*....|....*....|....*....|....*
gi 428688192 383 isgyDTEYLVNNIKAKLRSHLSHYKIPKLWLKVDQIPRNPQGKID 427
Cdd:cd17655 442 ----EKELPVAQLREFLARELPDYMIPSYFIKLDEIPLTPNGKVD 482
|
|
| ttLC_FACS_AlkK_like |
cd12119 |
Fatty acyl-CoA synthetases similar to LC-FACS from Thermus thermophiles; This family includes ... |
115-427 |
2.42e-16 |
|
Fatty acyl-CoA synthetases similar to LC-FACS from Thermus thermophiles; This family includes fatty acyl-CoA synthetases that can activate medium-chain to long-chain fatty acids. They catalyze the ATP-dependent acylation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. The fatty acyl-CoA synthetases are responsible for fatty acid degradation as well as physiological regulation of cellular functions via the production of fatty acyl-CoA esters. The fatty acyl-CoA synthetase from Thermus thermophiles in this family catalyzes the long-chain fatty acid, myristoyl acid, while another member in this family, the AlkK protein identified from Pseudomonas oleovorans, targets medium chain fatty acids. This family also includes uncharacterized FACS proteins.
Pssm-ID: 341284 [Multi-domain] Cd Length: 518 Bit Score: 81.14 E-value: 2.42e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 428688192 115 TGGTSGNIK--------FAIHTWETLNASAKGFSQfwqRRKInfFCCLPLYHV-------SGLMQIVR-----TFVTGGS 174
Cdd:cd12119 171 TSGTTGNPKgvvyshrsLVLHAMAALLTDGLGLSE---SDVV--LPVVPMFHVnawglpyAAAMVGAKlvlpgPYLDPAS 245
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 428688192 175 LaiydYSLLKKEIQNhnydnfFISLVPTQLNFLL---ENFPDWLKKFETVLVGGSATPKTLLQNCYRQKINLALTYGMTE 251
Cdd:cd12119 246 L----AELIEREGVT------FAAGVPTVWQGLLdhlEANGRDLSSLRRVVIGGSAVPRSLIEAFEERGVRVIHAWGMTE 315
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 428688192 252 TASGVTILKPENFFKGIN---------NSGHLLPHSQIVIKKNQAK--------FGQIIIKSDSLFKGYY------PHYK 308
Cdd:cd12119 316 TSPLGTVARPPSEHSNLSedeqlalraKQGRPVPGVELRIVDDDGRelpwdgkaVGELQVRGPWVTKSYYkndeesEALT 395
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 428688192 309 NSNYFLTDDLGYFDQDNFLHIVGRNSQKIISGGENVYPCEIENVVIKTGLVKDIVVVGKNDHYWGQIICAVYVAISGYDT 388
Cdd:cd12119 396 EDGWLRTGDVATIDEDGYLTITDRSKDVIKSGGEWISSVELENAIMAHPAVAEAAVIGVPHPKWGERPLAVVVLKEGATV 475
|
330 340 350 360
....*....|....*....|....*....|....*....|....
gi 428688192 389 EylvnniKAKLRSHLSHyKIPKLWLK-----VDQIPRNPQGKID 427
Cdd:cd12119 476 T------AEELLEFLAD-KVAKWWLPddvvfVDEIPKTSTGKID 512
|
|
| PRK12492 |
PRK12492 |
long-chain-fatty-acid--CoA ligase; Provisional |
247-426 |
3.68e-16 |
|
long-chain-fatty-acid--CoA ligase; Provisional
Pssm-ID: 171539 [Multi-domain] Cd Length: 562 Bit Score: 80.64 E-value: 3.68e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 428688192 247 YGMTETA--------------SGVTILKPENFFKGINNSGHLLPHSQivikknqakFGQIIIKSDSLFKGYYPHYKNS-- 310
Cdd:PRK12492 365 YGLTETSpvastnpygelarlGTVGIPVPGTALKVIDDDGNELPLGE---------RGELCIKGPQVMKGYWQQPEATae 435
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 428688192 311 -----NYFLTDDLGYFDQDNFLHIVGRNSQKIISGGENVYPCEIENVVIKTGLVKDIVVVGKNDHYWGQiicAVYVAISG 385
Cdd:PRK12492 436 aldaeGWFKTGDIAVIDPDGFVRIVDRKKDLIIVSGFNVYPNEIEDVVMAHPKVANCAAIGVPDERSGE---AVKLFVVA 512
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 428688192 386 YDTEYLVNNIKAKLRSHLSHYKIPKLWLKVDQIPRNPQGKI 426
Cdd:PRK12492 513 RDPGLSVEELKAYCKENFTGYKVPKHIVLRDSLPMTPVGKI 553
|
|
| MACS_like_4 |
cd05969 |
Uncharacterized subfamily of Acetyl-CoA synthetase like family (ACS); This family is most ... |
246-426 |
1.48e-15 |
|
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: 78.31 E-value: 1.48e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 428688192 246 TYGMTETASGVTILKPENFFKgINNSGHLLPHSQIVIKKNQA------KFGQIIIKSD--SLFKGYY---PHYKNS---N 311
Cdd:cd05969 238 TWWQTETGSIMIANYPCMPIK-PGSMGKPLPGVKAAVVDENGnelppgTKGILALKPGwpSMFRGIWndeERYKNSfidG 316
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 428688192 312 YFLTDDLGYFDQDNFLHIVGRNSQKIISGGENVYPCEIENVVIKTGLVKDIVVVGKNDHYWGQIICAVYVAISGYD-TEY 390
Cdd:cd05969 317 WYLTGDLAYRDEDGYFWFVGRADDIIKTSGHRVGPFEVESALMEHPAVAEAGVIGKPDPLRGEIIKAFISLKEGFEpSDE 396
|
170 180 190
....*....|....*....|....*....|....*.
gi 428688192 391 LVNNIKAKLRSHLSHYKIPKLWLKVDQIPRNPQGKI 426
Cdd:cd05969 397 LKEEIINFVRQKLGAHVAPREIEFVDNLPKTRSGKI 432
|
|
| LC_FACS_like |
cd17640 |
Long-chain fatty acid CoA synthetase; This family includes long-chain fatty acid (C12-C20) CoA ... |
76-416 |
2.10e-15 |
|
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: 77.78 E-value: 2.10e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 428688192 76 EELQQVYKLVKPDFLFSDHlektyynppHNHSYQGIMIpTGGTSGNIKFAIHTWETLNASAKGFSQFWQ----RRkinFF 151
Cdd:cd17640 67 EELLYILNHSESVALVVEN---------DSDDLATIIY-TSGTTGNPKGVMLTHANLLHQIRSLSDIVPpqpgDR---FL 133
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 428688192 152 CCLPLYHVSGLMQIVRTFVTGGSLAIYDYSLLKKEIQNHNyDNFFISlVPTQLNFLLENFPDWLKK-------------- 217
Cdd:cd17640 134 SILPIWHSYERSAEYFIFACGCSQAYTSIRTLKDDLKRVK-PHYIVS-VPRLWESLYSGIQKQVSKsspikqflflffls 211
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 428688192 218 ---FETVLVGGSATPKTLlQNCYRQ-KINLALTYGMTETASGVTILKPENFFKGinNSGHLLPHSQIVI----KKNQAKF 289
Cdd:cd17640 212 ggiFKFGISGGGALPPHV-DTFFEAiGIEVLNGYGLTETSPVVSARRLKCNVRG--SVGRPLPGTEIKIvdpeGNVVLPP 288
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 428688192 290 GQ---IIIKSDSLFKGYYphyKN----------SNYFLTDDLGYFDQDNFLHIVGRNSQKII-SGGENVYPCEIENVVIK 355
Cdd:cd17640 289 GEkgiVWVRGPQVMKGYY---KNpeatskvldsDGWFNTGDLGWLTCGGELVLTGRAKDTIVlSNGENVEPQPIEEALMR 365
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 428688192 356 TGLVKDIVVVGKNDHYWGQIICAVYVAISGYDTEYLV------------NNIKAKLRSHLSHYKIPKLWLKVD 416
Cdd:cd17640 366 SPFIEQIMVVGQDQKRLGALIVPNFEELEKWAKESGVklandrsqllasKKVLKLYKNEIKDEISNRPGFKSF 438
|
|
| MACS_like_3 |
cd05971 |
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the ... |
190-426 |
5.02e-15 |
|
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: 76.70 E-value: 5.02e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 428688192 190 HNYDNFFisLVPTQLNFLLENFP---DWLKKFETVLVGGSATPKTLLQNCYRQ-KINLALTYGMTET------ASGVTIL 259
Cdd:cd05971 180 YGVTTAF--LPPTALKMMRQQGEqlkHAQVKLRAIATGGESLGEELLGWAREQfGVEVNEFYGQTECnlvignCSALFPI 257
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 428688192 260 KPENFFKG--------INNSGHLLPHSQIvikknqakfGQIIIKSDS--LFKGYYPHYK------NSNYFLTDDLGYFDQ 323
Cdd:cd05971 258 KPGSMGKPipghrvaiVDDNGTPLPPGEV---------GEIAVELPDpvAFLGYWNNPSatekkmAGDWLLTGDLGRKDS 328
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 428688192 324 DNFLHIVGRNSQKIISGGENVYPCEIENVVIKTGLVKDIVVVGKNDHYWGQIICAVYVAISGY-DTEYLVNNIKAKLRSH 402
Cdd:cd05971 329 DGYFWYVGRDDDVITSSGYRIGPAEIEECLLKHPAVLMAAVVGIPDPIRGEIVKAFVVLNPGEtPSDALAREIQELVKTR 408
|
250 260
....*....|....*....|....
gi 428688192 403 LSHYKIPKLWLKVDQIPRNPQGKI 426
Cdd:cd05971 409 LAAHEYPREIEFVNELPRTATGKI 432
|
|
| caiC |
PRK08008 |
putative crotonobetaine/carnitine-CoA ligase; Validated |
236-427 |
5.61e-15 |
|
putative crotonobetaine/carnitine-CoA ligase; Validated
Pssm-ID: 181195 [Multi-domain] Cd Length: 517 Bit Score: 76.64 E-value: 5.61e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 428688192 236 CYRQKINLALTYGMTETASGVTILKP--ENFFKGINNSGhLLPHSQIVIKKNQA----KFGQIIIKS---DSLFKGYYPH 306
Cdd:PRK08008 308 EERFGVRLLTSYGMTETIVGIIGDRPgdKRRWPSIGRPG-FCYEAEIRDDHNRPlpagEIGEICIKGvpgKTIFKEYYLD 386
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 428688192 307 YKNSNYFL-------TDDLGYFDQDNFLHIVGRNSQKIISGGENVYPCEIENVVIKTGLVKDIVVVGKNDHYWGQIICAV 379
Cdd:PRK08008 387 PKATAKVLeadgwlhTGDTGYVDEEGFFYFVDRRCNMIKRGGENVSCVELENIIATHPKIQDIVVVGIKDSIRDEAIKAF 466
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 428688192 380 YVAISGydTEYLVNNIKAKLRSHLSHYKIPKLWLKVDQIPRNPQGKID 427
Cdd:PRK08008 467 VVLNEG--ETLSEEEFFAFCEQNMAKFKVPSYLEIRKDLPRNCSGKII 512
|
|
| PRK05605 |
PRK05605 |
long-chain-fatty-acid--CoA ligase; Validated |
290-426 |
6.09e-15 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 235531 [Multi-domain] Cd Length: 573 Bit Score: 76.96 E-value: 6.09e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 428688192 290 GQIIIKSDSLFKGYY--PHyKNSNYFL-----TDDLGYFDQDNFLHIVGRNSQKIISGGENVYPCEIENVVIKTGLVKDI 362
Cdd:PRK05605 418 GELLVRGPQVFKGYWnrPE-ETAKSFLdgwfrTGDVVVMEEDGFIRIVDRIKELIITGGFNVYPAEVEEVLREHPGVEDA 496
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 428688192 363 VVVGKNDHYWGQIICAVYVAISGYDTEylVNNIKAKLRSHLSHYKIPKLWLKVDQIPRNPQGKI 426
Cdd:PRK05605 497 AVVGLPREDGSEEVVAAVVLEPGAALD--PEGLRAYCREHLTRYKVPRRFYHVDELPRDQLGKV 558
|
|
| ttLC_FACS_like |
cd05915 |
Fatty acyl-CoA synthetases similar to LC-FACS from Thermus thermophiles; This family includes ... |
115-433 |
1.44e-14 |
|
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: 75.55 E-value: 1.44e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 428688192 115 TGGTSGNIKFAI--HTWETLNASAKG-FSQFWQRRKINFFCCLPLYHVSGLMQIVRTFVTGGSLA----IYDYSLLKKEI 187
Cdd:cd05915 161 TTGTTGLPKGVVysHRALVLHSLAASlVDGTALSEKDVVLPVVPMFHVNAWCLPYAATLVGAKQVlpgpRLDPASLVELF 240
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 428688192 188 QNHNYDNFFISlvPTQLNfLLENFPDWLKK----FETVLVGGSATPKTLLQNCYRQKINLALTYGMTETASGVTI----- 258
Cdd:cd05915 241 DGEGVTFTAGV--PTVWL-ALADYLESTGHrlktLRRLVVGGSAAPRSLIARFERMGVEVRQGYGLTETSPVVVQnfvks 317
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 428688192 259 ------------LKPENFFKGINNSGHLLPHSQIVIKKNQAKFGQIIIKSDSLFKGYYPHYKNSN-------YFLTDDLG 319
Cdd:cd05915 318 hleslseeekltLKAKTGLPIPLVRLRVADEEGRPVPKDGKALGEVQLKGPWITGGYYGNEEATRsaltpdgFFRTGDIA 397
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 428688192 320 YFDQDNFLHIVGRNSQKIISGGENVYPCEIENVVIKTGLVKDIVVVGKNDHYWGQIICAvYVAISgyDTEYLVNNIKAKL 399
Cdd:cd05915 398 VWDEEGYVEIKDRLKDLIKSGGEWISSVDLENALMGHPKVKEAAVVAIPHPKWQERPLA-VVVPR--GEKPTPEELNEHL 474
|
330 340 350
....*....|....*....|....*....|....*
gi 428688192 400 RSHLSHYK-IPKLWLKVDQIPRNPQGKIDYGYLEK 433
Cdd:cd05915 475 LKAGFAKWqLPDAYVFAEEIPRTSAGKFLKRALRE 509
|
|
| PRK06178 |
PRK06178 |
acyl-CoA synthetase; Validated |
247-435 |
3.27e-14 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 235724 [Multi-domain] Cd Length: 567 Bit Score: 74.69 E-value: 3.27e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 428688192 247 YGMTETASGVTI----------LKPENFFKGI-----------NNSGHLLPHSQIvikknqakfGQIIIKSDSLFKGYY- 304
Cdd:PRK06178 360 WGMTETHTCDTFtagfqdddfdLLSQPVFVGLpvpgtefkicdFETGELLPLGAE---------GEIVVRTPSLLKGYWn 430
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 428688192 305 -----PHYKNSNYFLTDDLGYFDQDNFLHIVGRNSQKIISGGENVYPCEIENVVIKTGLVKDIVVVGKNDHYWGQIICAV 379
Cdd:PRK06178 431 kpeatAEALRDGWLHTGDIGKIDEQGFLHYLGRRKEMLKVNGMSVFPSEVEALLGQHPAVLGSAVVGRPDPDKGQVPVAF 510
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 428688192 380 YVAISGYDTEylVNNIKAKLRSHLSHYKIPKLWLkVDQIPRNPQGKIDYGYLEKML 435
Cdd:PRK06178 511 VQLKPGADLT--AAALQAWCRENMAVYKVPEIRI-VDALPMTATGKVRKQDLQALA 563
|
|
| 23DHB-AMP_lg |
cd05920 |
2,3-dihydroxybenzoate-AMP ligase; 2,3-dihydroxybenzoate-AMP ligase activates 2, ... |
290-427 |
1.23e-13 |
|
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: 72.36 E-value: 1.23e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 428688192 290 GQIIIKSDSLFKGYY---PHYKNS----NYFLTDDLGYFDQDNFLHIVGRNSQKIISGGENVYPCEIENVVIKTGLVKDI 362
Cdd:cd05920 336 GELLTRGPYTIRGYYrapEHNARAftpdGFYRTGDLVRRTPDGYLVVEGRIKDQINRGGEKIAAEEVENLLLRHPAVHDA 415
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 428688192 363 VVVGKNDHYWGQIICAVYVAiSGYDTEYlvnnikAKLRSHL-----SHYKIPKLWLKVDQIPRNPQGKID 427
Cdd:cd05920 416 AVVAMPDELLGERSCAFVVL-RDPPPSA------AQLRRFLrerglAAYKLPDRIEFVDSLPLTAVGKID 478
|
|
| PRK07787 |
PRK07787 |
acyl-CoA synthetase; Validated |
289-438 |
1.44e-13 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236096 [Multi-domain] Cd Length: 471 Bit Score: 72.33 E-value: 1.44e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 428688192 289 FGQIIIKSDSLFKGYY--PH-----YKNSNYFLTDDLGYFDQDNFLHIVGRNSQKII-SGGENVYPCEIENVVIKTGLVK 360
Cdd:PRK07787 321 VGELQVRGPTLFDGYLnrPDataaaFTADGWFRTGDVAVVDPDGMHRIVGRESTDLIkSGGYRIGAGEIETALLGHPGVR 400
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 428688192 361 DIVVVGKNDHYWGQIICAVYVAISGYDTEYLVNNIKAklrsHLSHYKIPKLWLKVDQIPRNPQGKIdygyLEKMLTMD 438
Cdd:PRK07787 401 EAAVVGVPDDDLGQRIVAYVVGADDVAADELIDFVAQ----QLSVHKRPREVRFVDALPRNAMGKV----LKKQLLSE 470
|
|
| MACS_like_2 |
cd05973 |
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the ... |
300-426 |
1.96e-13 |
|
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: 71.78 E-value: 1.96e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 428688192 300 FKGYYPHYKNS---NYFLTDDLGYFDQDNFLHIVGRNSQKIISGGENVYPCEIENVVIKTGLVKDIVVVGKNDHYWGQII 376
Cdd:cd05973 300 FRGYQLPDTPAidgGYYLTGDTVEFDPDGSFSFIGRADDVITMSGYRIGPFDVESALIEHPAVAEAAVIGVPDPERTEVV 379
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|.
gi 428688192 377 CAVYVAISGYD-TEYLVNNIKAKLRSHLSHYKIPKLWLKVDQIPRNPQGKI 426
Cdd:cd05973 380 KAFVVLRGGHEgTPALADELQLHVKKRLSAHAYPRTIHFVDELPKTPSGKI 430
|
|
| PLN02330 |
PLN02330 |
4-coumarate--CoA ligase-like 1 |
154-441 |
2.06e-13 |
|
4-coumarate--CoA ligase-like 1
Pssm-ID: 215189 [Multi-domain] Cd Length: 546 Bit Score: 71.93 E-value: 2.06e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 428688192 154 LPLYHVSGLMQIV-RTFVTGGS--------LAIYDYSLLKKEIQnhnydnfFISLVPTQL-----NFLLENFPDWLKKFE 219
Cdd:PLN02330 234 IPFFHIYGITGICcATLRNKGKvvvmsrfeLRTFLNALITQEVS-------FAPIVPPIIlnlvkNPIVEEFDLSKLKLQ 306
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 428688192 220 TVLVGGSATPKTLLqNCYRQK---INLALTYGMTEtASGVTIL--KPENFfKGI---NNSGHLLPHSQI---------VI 282
Cdd:PLN02330 307 AIMTAAAPLAPELL-TAFEAKfpgVQVQEAYGLTE-HSCITLThgDPEKG-HGIakkNSVGFILPNLEVkfidpdtgrSL 383
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 428688192 283 KKNQAkfGQIIIKSDSLFKGYYPHYKNSN-------YFLTDDLGYFDQDNFLHIVGRNSQKIISGGENVYPCEIENVVIK 355
Cdd:PLN02330 384 PKNTP--GELCVRSQCVMQGYYNNKEETDrtidedgWLHTGDIGYIDDDGDIFIVDRIKELIKYKGFQVAPAELEAILLT 461
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 428688192 356 TGLVKDIVVVGKNDHYWGQIICA-VYVAISGYDTEYLVNNIKAklrSHLSHYKIPKLWLKVDQIPRNPQGKIDYGYL-EK 433
Cdd:PLN02330 462 HPSVEDAAVVPLPDEEAGEIPAAcVVINPKAKESEEDILNFVA---ANVAHYKKVRVVQFVDSIPKSLSGKIMRRLLkEK 538
|
....*...
gi 428688192 434 MLTMDNSS 441
Cdd:PLN02330 539 MLSINKAN 546
|
|
| PRK04813 |
PRK04813 |
D-alanine--poly(phosphoribitol) ligase subunit DltA; |
246-427 |
1.59e-12 |
|
D-alanine--poly(phosphoribitol) ligase subunit DltA;
Pssm-ID: 235313 [Multi-domain] Cd Length: 503 Bit Score: 69.15 E-value: 1.59e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 428688192 246 TYGMTETASGVT-------IL-----------KPENFFKGINNSGHLLPHSQIvikknqakfGQIIIKSDSLFKGY---- 303
Cdd:PRK04813 292 TYGPTEATVAVTsieitdeMLdqykrlpigyaKPDSPLLIIDEEGTKLPDGEQ---------GEIVISGPSVSKGYlnnp 362
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 428688192 304 ------------YPHYKnsnyflTDDLGYFDqDNFLHIVGRNSQKIISGGENVYPCEIENVVIKTGLVKDIVVVGKN-DH 370
Cdd:PRK04813 363 ektaeafftfdgQPAYH------TGDAGYLE-DGLLFYQGRIDFQIKLNGYRIELEEIEQNLRQSSYVESAVVVPYNkDH 435
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 428688192 371 YWGQIICAVYVAISGYDTEY-LVNNIKAKLRSHLSHYKIPKLWLKVDQIPRNPQGKID 427
Cdd:PRK04813 436 KVQYLIAYVVPKEEDFEREFeLTKAIKKELKERLMEYMIPRKFIYRDSLPLTPNGKID 493
|
|
| PLN02574 |
PLN02574 |
4-coumarate--CoA ligase-like |
102-441 |
2.19e-12 |
|
4-coumarate--CoA ligase-like
Pssm-ID: 215312 [Multi-domain] Cd Length: 560 Bit Score: 68.72 E-value: 2.19e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 428688192 102 PPHNHSYQGIMIPTGGTSGNIKFAIHTWETLNASAKGFSQFWQRRKIN------FFCCLPLYHVSGLMQIVRTFVTGGSL 175
Cdd:PLN02574 193 PVIKQDDVAAIMYSSGTTGASKGVVLTHRNLIAMVELFVRFEASQYEYpgsdnvYLAALPMFHIYGLSLFVVGLLSLGST 272
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 428688192 176 AI----YDYSLLKKEIQNHNYDNFfiSLVPTQLNFLLENFP----DWLKKFETVLVGGSATPKTLLQNCYR--QKINLAL 245
Cdd:PLN02574 273 IVvmrrFDASDMVKVIDRFKVTHF--PVVPPILMALTKKAKgvcgEVLKSLKQVSCGAAPLSGKFIQDFVQtlPHVDFIQ 350
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 428688192 246 TYGMTE-TASGVTILKPENFfKGINNSGHLLPHSQI-VIKKNQAKF------GQIIIKSDSLFKGYYPHYK-------NS 310
Cdd:PLN02574 351 GYGMTEsTAVGTRGFNTEKL-SKYSSVGLLAPNMQAkVVDWSTGCLlppgncGELWIQGPGVMKGYLNNPKatqstidKD 429
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 428688192 311 NYFLTDDLGYFDQDNFLHIVGRNSQKIISGGENVYPCEIENVVIKTGLVKDIVVVGKNDHYWGQIICAVYVAISGYD-TE 389
Cdd:PLN02574 430 GWLRTGDIAYFDEDGYLYIVDRLKEIIKYKGFQIAPADLEAVLISHPEIIDAAVTAVPDKECGEIPVAFVVRRQGSTlSQ 509
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|..
gi 428688192 390 YLVNNIKAKlrsHLSHYKIPKLWLKVDQIPRNPQGKIDYGYLEKMLTMDNSS 441
Cdd:PLN02574 510 EAVINYVAK---QVAPYKKVRKVVFVQSIPKSPAGKILRRELKRSLTNSVSS 558
|
|
| PrpE |
cd05967 |
Propionyl-CoA synthetase (PrpE); EC 6.2.1.17: propanoate:CoA ligase (AMP-forming) or ... |
295-434 |
2.49e-12 |
|
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: 68.88 E-value: 2.49e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 428688192 295 KSDSLFK-GYYPHYKNsnYFLTDDLGYFDQDNFLHIVGRNSQKIISGGENVYPCEIENVVIKTGLVKDIVVVGKNDHYWG 373
Cdd:cd05967 456 KNDERFKkLYLSKFPG--YYDTGDAGYKDEDGYLFIMGRTDDVINVAGHRLSTGEMEESVLSHPAVAECAVVGVRDELKG 533
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 428688192 374 QIICAVYVAISGY--DTEYLVNNIKAKLRSHLSHYKIPKLWLKVDQIPRNPQGKIDYGYLEKM 434
Cdd:cd05967 534 QVPLGLVVLKEGVkiTAEELEKELVALVREQIGPVAAFRLVIFVKRLPKTRSGKILRRTLRKI 596
|
|
| ACSBG_like |
cd05933 |
Bubblegum-like very long-chain fatty acid CoA synthetase (VL-FACS); This family of very ... |
224-353 |
2.97e-12 |
|
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: 68.54 E-value: 2.97e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 428688192 224 GGSATPKTLLQncYRQKINLAL--TYGMTETASGVTILKPENFfkGINNSGHLLPHSQI-VIKKNQAKFGQIIIKSDSLF 300
Cdd:cd05933 328 GAAPISRETLE--FFLSLNIPImeLYGMSETSGPHTISNPQAY--RLLSCGKALPGCKTkIHNPDADGIGEICFWGRHVF 403
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 428688192 301 KGYY-------PHYKNSNYFLTDDLGYFDQDNFLHIVGRNSQKII-SGGENVYPCEIENVV 353
Cdd:cd05933 404 MGYLnmedkteEAIDEDGWLHSGDLGKLDEDGFLYITGRIKELIItAGGENVPPVPIEDAV 464
|
|
| MACS_euk |
cd05928 |
Eukaryotic Medium-chain acyl-CoA synthetase (MACS or ACSM); MACS catalyzes the two-step ... |
221-433 |
3.05e-12 |
|
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: 68.26 E-value: 3.05e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 428688192 221 VLVGGSATPKTLLQncYRQKINLAL--TYGMTETA------SGVTIlKPENFFKG--------INNSGHLLPhsqivikk 284
Cdd:cd05928 297 VTGGEPLNPEVLEK--WKAQTGLDIyeGYGQTETGlicanfKGMKI-KPGSMGKAsppydvqiIDDNGNVLP-------- 365
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 428688192 285 nQAKFGQIIIKSD-----SLFKGYY--PHYKNS----NYFLTDDLGYFDQDNFLHIVGRNSQKIISGGENVYPCEIENVV 353
Cdd:cd05928 366 -PGTEGDIGIRVKpirpfGLFSGYVdnPEKTAAtirgDFYLTGDRGIMDEDGYFWFMGRADDVINSSGYRIGPFEVESAL 444
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 428688192 354 IKTGLVKDIVVVGKNDHYWGQIICAVYV---AISGYDTEYLVNNIKAKLRSHLSHYKIPKLWLKVDQIPRNPQGKIDYGY 430
Cdd:cd05928 445 IEHPAVVESAVVSSPDPIRGEVVKAFVVlapQFLSHDPEQLTKELQQHVKSVTAPYKYPRKVEFVQELPKTVTGKIQRNE 524
|
...
gi 428688192 431 LEK 433
Cdd:cd05928 525 LRD 527
|
|
| MACS_AAE_MA_like |
cd05970 |
Medium-chain acyl-CoA synthetase (MACS) of AAE_MA like; MACS catalyzes the two-step activation ... |
164-426 |
3.24e-12 |
|
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: 68.29 E-value: 3.24e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 428688192 164 QIVRTFVTGGSLAIYDY------SLLKKeIQNHNYDNFFISlvPTQLNFLL-ENFPDW-LKKFETVLVGGSATPKTLLqN 235
Cdd:cd05970 244 KIYGQWIAGAAVFVYDYdkfdpkALLEK-LSKYGVTTFCAP--PTIYRFLIrEDLSRYdLSSLRYCTTAGEALNPEVF-N 319
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 428688192 236 CYRQKINLALTYGMTETASGVTI-----LKPENFFKGINNSGH---LLPHSQIVIKKNQAkfGQIIIKSDS-----LFKG 302
Cdd:cd05970 320 TFKEKTGIKLMEGFGQTETTLTIatfpwMEPKPGSMGKPAPGYeidLIDREGRSCEAGEE--GEIVIRTSKgkpvgLFGG 397
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 428688192 303 YYPHYKNSN------YFLTDDLGYFDQDNFLHIVGRNSQKIISGGENVYPCEIENVVIKTGLVKDIVVVGKNDHYWGQII 376
Cdd:cd05970 398 YYKDAEKTAevwhdgYYHTGDAAWMDEDGYLWFVGRTDDLIKSSGYRIGPFEVESALIQHPAVLECAVTGVPDPIRGQVV 477
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|.
gi 428688192 377 CAVYVAISGYD-TEYLVNNIKAKLRSHLSHYKIPKLWLKVDQIPRNPQGKI 426
Cdd:cd05970 478 KATIVLAKGYEpSEELKKELQDHVKKVTAPYKYPRIVEFVDELPKTISGKI 528
|
|
| PtmA |
cd17636 |
long-chain fatty acid CoA ligase (FadD); This family contains fatty acid CoA ligases, ... |
290-427 |
3.90e-12 |
|
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: 66.94 E-value: 3.90e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 428688192 290 GQIIIKSDSLFKGYY------PHYKNSNYFLTDDLGYFDQDNFLHIVGRNSQKIISGGENVYPCEIENVVIKTGLVKDIV 363
Cdd:cd17636 190 GEIVARGPTVMAGYWnrpevnARRTRGGWHHTNDLGRREPDGSLSFVGPKTRMIKSGAENIYPAEVERCLRQHPAVADAA 269
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 428688192 364 VVGKNDHYWGQIICAVYV--AISGYDTEYLVNNIKAKLRShlshYKIPKLWLKVDQIPRNPQGKID 427
Cdd:cd17636 270 VIGVPDPRWAQSVKAIVVlkPGASVTEAELIEHCRARIAS----YKKPKSVEFADALPRTAGGADD 331
|
|
| PRK05677 |
PRK05677 |
long-chain-fatty-acid--CoA ligase; Validated |
247-426 |
4.80e-12 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 168170 [Multi-domain] Cd Length: 562 Bit Score: 67.87 E-value: 4.80e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 428688192 247 YGMTETASGVTILKPEN-------------FFKGINNSGHLLPHSQIvikknqakfGQIIIKSDSLFKGYYPHYKNSNYF 313
Cdd:PRK05677 358 YGMTETSPVVSVNPSQAiqvgtigipvpstLCKVIDDDGNELPLGEV---------GELCVKGPQVMKGYWQRPEATDEI 428
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 428688192 314 LTD-------DLGYFDQDNFLHIVGRNSQKIISGGENVYPCEIENVVIKTGLVKDIVVVGKNDHYWGQIICAVYVAISGY 386
Cdd:PRK05677 429 LDSdgwlktgDIALIQEDGYMRIVDRKKDMILVSGFNVYPNELEDVLAALPGVLQCAAIGVPDEKSGEAIKVFVVVKPGE 508
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 428688192 387 D-TEylvNNIKAKLRSHLSHYKIPKLWLKVDQIPRNPQGKI 426
Cdd:PRK05677 509 TlTK---EQVMEHMRANLTGYKVPKAVEFRDELPTTNVGKI 546
|
|
| PRK08162 |
PRK08162 |
acyl-CoA synthetase; Validated |
201-426 |
5.43e-12 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236169 [Multi-domain] Cd Length: 545 Bit Score: 67.66 E-value: 5.43e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 428688192 201 PTQLNFLLENFPDWLKKFE---TVLVGGSATPKTLLQNCYRQKINLALTYGMTET------------------------- 252
Cdd:PRK08162 278 PIVLSALINAPAEWRAGIDhpvHAMVAGAAPPAAVIAKMEEIGFDLTHVYGLTETygpatvcawqpewdalplderaqlk 357
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 428688192 253 ---------ASGVTILKPEnffkginnSGHLLPHSQIVIkknqakfGQIIIKSDSLFKGYYphyKN---------SNYFL 314
Cdd:PRK08162 358 arqgvryplQEGVTVLDPD--------TMQPVPADGETI-------GEIMFRGNIVMKGYL---KNpkateeafaGGWFH 419
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 428688192 315 TDDLGYFDQDNFLHIVGRNSQKIISGGENVYPCEIENVVIKTGLVKDIVVVGKNDHYWGQIICA-VYVAISGYDTEylvN 393
Cdd:PRK08162 420 TGDLAVLHPDGYIKIKDRSKDIIISGGENISSIEVEDVLYRHPAVLVAAVVAKPDPKWGEVPCAfVELKDGASATE---E 496
|
250 260 270
....*....|....*....|....*....|...
gi 428688192 394 NIKAKLRSHLSHYKIPKLwLKVDQIPRNPQGKI 426
Cdd:PRK08162 497 EIIAHCREHLAGFKVPKA-VVFGELPKTSTGKI 528
|
|
| A_NRPS_GliP_like |
cd17653 |
nonribosomal peptide synthase GliP-like; This family includes the adenylation (A) domain of ... |
212-433 |
5.90e-12 |
|
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: 66.95 E-value: 5.90e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 428688192 212 PDWLKKFETVLVGGSATPKTLLQncyRQKINLAL--TYGMTETASGVTI--LKPENFfkgiNNSGHLLPHSQIVI-KKN- 285
Cdd:cd17653 205 PQDFPNLKTIFLGGEAVPPSLLD---RWSPGRRLynAYGPTECTISSTMteLLPGQP----VTIGKPIPNSTCYIlDADl 277
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 428688192 286 ----QAKFGQIIIKSDSLFKGYY-------------PHYKNSNYFLTDDLGYFDQDNFLHIVGRNSQKIISGGENVYPCE 348
Cdd:cd17653 278 qpvpEGVVGEICISGVQVARGYLgnpaltaskfvpdPFWPGSRMYRTGDYGRWTEDGGLEFLGREDNQVKVRGFRINLEE 357
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 428688192 349 IENVVIKT-GLVKDIVVVGKNDhywgqIICAvYVAISGYDTEylvnNIKAKLRSHLSHYKIPKLWLKVDQIPRNPQGKID 427
Cdd:cd17653 358 IEEVVLQSqPEVTQAAAIVVNG-----RLVA-FVTPETVDVD----GLRSELAKHLPSYAVPDRIIALDSFPLTANGKVD 427
|
....*.
gi 428688192 428 YGYLEK 433
Cdd:cd17653 428 RKALRE 433
|
|
| EntE |
COG1021 |
EntE, 2,3-dihydroxybenzoate-AMP synthase component of non-ribosomal peptide synthetase ... |
300-436 |
1.59e-11 |
|
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: 65.94 E-value: 1.59e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 428688192 300 FKGYY--PHYkNSNYFlTDDlGYF--------DQDNFLHIVGRNSQKIISGGENVYPCEIENVVIKTGLVKDIVVVGKND 369
Cdd:COG1021 391 IRGYYraPEH-NARAF-TPD-GFYrtgdlvrrTPDGYLVVEGRAKDQINRGGEKIAAEEVENLLLAHPAVHDAAVVAMPD 467
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 428688192 370 HYWGQIICAVYVAISGydteylvnNIKAK-LRSHL-----SHYKIPKLWLKVDQIPRNPQGKIDYGYLEKMLT 436
Cdd:COG1021 468 EYLGERSCAFVVPRGE--------PLTLAeLRRFLrerglAAFKLPDRLEFVDALPLTAVGKIDKKALRAALA 532
|
|
| AMP-binding_C |
pfam13193 |
AMP-binding enzyme C-terminal domain; This is a small domain that is found C terminal to ... |
348-425 |
2.12e-11 |
|
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: 59.48 E-value: 2.12e-11
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 428688192 348 EIENVVIKTGLVKDIVVVGKNDHYWGQIICAVYVAISGYDTeyLVNNIKAKLRSHLSHYKIPKLWLKVDQIPRNPQGK 425
Cdd:pfam13193 1 EVESALVSHPAVAEAAVVGVPDELKGEAPVAFVVLKPGVEL--LEEELVAHVREELGPYAVPKEVVFVDELPKTRSGK 76
|
|
| ABCL |
cd05958 |
2-aminobenzoate-CoA ligase (ABCL); ABCL catalyzes the initial step in the 2-aminobenzoate ... |
315-427 |
3.06e-11 |
|
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: 64.81 E-value: 3.06e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 428688192 315 TDDLGYFDQDNFLHIVGRNSQKIISGGENVYPCEIENVVIKTGLVKDIVVVGKNDHYWGQIICAVYVAISGY-DTEYLVN 393
Cdd:cd05958 321 TGDTYSRDPDGYFRHQGRSDDMIVSGGYNIAPPEVEDVLLQHPAVAECAVVGHPDESRGVVVKAFVVLRPGViPGPVLAR 400
|
90 100 110
....*....|....*....|....*....|....
gi 428688192 394 NIKAKLRSHLSHYKIPKLWLKVDQIPRNPQGKID 427
Cdd:cd05958 401 ELQDHAKAHIAPYKYPRAIEFVTELPRTATGKLQ 434
|
|
| BCL_like |
cd05919 |
Benzoate CoA ligase (BCL) and similar adenylate forming enzymes; This family contains benzoate ... |
290-431 |
1.74e-10 |
|
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: 62.48 E-value: 1.74e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 428688192 290 GQIIIKSDSLFKGYYPHYKNS------NYFLTDDLGYFDQDNFLHIVGRNSQKIISGGENVYPCEIENVVIKTGLVKDIV 363
Cdd:cd05919 287 GDLLVRGPSAAVGYWNNPEKSratfngGWYRTGDKFCRDADGWYTHAGRADDMLKVGGQWVSPVEVESLIIQHPAVAEAA 366
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 428688192 364 VVGKNDHYWGQIICAVYVAISGYD-TEYLVNNIKAKLRSHLSHYKIPKLWLKVDQIPRNPQGKIDYGYL 431
Cdd:cd05919 367 VVAVPESTGLSRLTAFVVLKSPAApQESLARDIHRHLLERLSAHKVPRRIAFVDELPRTATGKLQRFKL 435
|
|
| LC_FACS_bac |
cd05932 |
Bacterial long-chain fatty acid CoA synthetase (LC-FACS), including Marinobacter ... |
112-368 |
2.17e-10 |
|
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: 62.49 E-value: 2.17e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 428688192 112 MIPTGGTSGNIKFAIHTWETLN-ASAKGFSQFWQRRKINFFCCLPLYHVSGLMQIVRTFVTGGSLAIYDYSL--LKKEIQ 188
Cdd:cd05932 142 LIYTSGTTGQPKGVMLTFGSFAwAAQAGIEHIGTEENDRMLSYLPLAHVTERVFVEGGSLYGGVLVAFAESLdtFVEDVQ 221
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 428688192 189 NHNYDNFF-------------ISLVPTQ-LNFLLE-NFPDWLKKFET----------VLVGGSA-TPKTLLQNCYRQKIN 242
Cdd:cd05932 222 RARPTLFFsvprlwtkfqqgvQDKIPQQkLNLLLKiPVVNSLVKRKVlkglgldqcrLAGCGSApVPPALLEWYRSLGLN 301
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 428688192 243 LALTYGMTETASGVTILKPenFFKGINNSGHLLPHSQIVIKKNqakfGQIIIKSDSLFKGYYPH-------YKNSNYFLT 315
Cdd:cd05932 302 ILEAYGMTENFAYSHLNYP--GRDKIGTVGNAGPGVEVRISED----GEILVRSPALMMGYYKDpeataeaFTADGFLRT 375
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....
gi 428688192 316 DDLGYFDQDNFLHIVGRNSQKI-ISGGENVYPCEIENVVIKTGLVKDIVVVGKN 368
Cdd:cd05932 376 GDKGELDADGNLTITGRVKDIFkTSKGKYVAPAPIENKLAEHDRVEMVCVIGSG 429
|
|
| PRK06018 |
PRK06018 |
putative acyl-CoA synthetase; Provisional |
112-427 |
3.91e-10 |
|
putative acyl-CoA synthetase; Provisional
Pssm-ID: 235673 [Multi-domain] Cd Length: 542 Bit Score: 61.69 E-value: 3.91e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 428688192 112 MIPTGGTSGNIKFA--------IHTWETLNASAKGFSQfwqrrKINFFCCLPLYHV-------SGLMQIVRTFVTGGSL- 175
Cdd:PRK06018 182 MCYTSGTTGDPKGVlyshrsnvLHALMANNGDALGTSA-----ADTMLPVVPLFHAnswgiafSAPSMGTKLVMPGAKLd 256
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 428688192 176 --AIYDysLLKKEIQNHNydnffiSLVPTQLNFLLE-------NFPDwLKKfetVLVGGSATPKTLLQNCYRQKINLALT 246
Cdd:PRK06018 257 gaSVYE--LLDTEKVTFT------AGVPTVWLMLLQymekeglKLPH-LKM---VVCGGSAMPRSMIKAFEDMGVEVRHA 324
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 428688192 247 YGMTETA--SGVTILKPEnffkginnSGHLLPHSQIVIKKNQAK-----------------------FGQIIIKSDSLFK 301
Cdd:PRK06018 325 WGMTEMSplGTLAALKPP--------FSKLPGDARLDVLQKQGYppfgvemkitddagkelpwdgktFGRLKVRGPAVAA 396
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 428688192 302 GYYPHYKN----SNYFLTDDLGYFDQDNFLHIVGRNSQKIISGGENVYPCEIENVVIKTGLVKDIVVVGKNDHYWGQIIC 377
Cdd:PRK06018 397 AYYRVDGEilddDGFFDTGDVATIDAYGYMRITDRSKDVIKSGGEWISSIDLENLAVGHPKVAEAAVIGVYHPKWDERPL 476
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*
gi 428688192 378 AVYVAISGydteylVNNIKAKLRSHLSHyKIPKLWLK-----VDQIPRNPQGKID 427
Cdd:PRK06018 477 LIVQLKPG------ETATREEILKYMDG-KIAKWWMPddvafVDAIPHTATGKIL 524
|
|
| PRK12467 |
PRK12467 |
peptide synthase; Provisional |
199-427 |
4.12e-10 |
|
peptide synthase; Provisional
Pssm-ID: 237108 [Multi-domain] Cd Length: 3956 Bit Score: 62.49 E-value: 4.12e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 428688192 199 LVPTQLNFLLEN-FPDWLKKFETVLVGGSATPKTLLQNCYRQKINLAL--TYGMTETASGVTI--LKPENFFKGINNSGH 273
Cdd:PRK12467 753 IVPSHLQALLQAsRVALPRPQRALVCGGEALQVDLLARVRALGPGARLinHYGPTETTVGVSTyeLSDEERDFGNVPIGQ 832
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 428688192 274 LLPHSQIVIKKNQAK------FGQIIIKSDSLFKGYypHYK---NSNYFLTD-------------DLGYFDQDNFLHIVG 331
Cdd:PRK12467 833 PLANLGLYILDHYLNpvpvgvVGELYIGGAGLARGY--HRRpalTAERFVPDpfgadggrlyrtgDLARYRADGVIEYLG 910
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 428688192 332 RNSQKIISGGENVYPCEIENVVIKTGLVKDIVVVGKNDHYWGQIICAVYVAISGYDTEYLVNN--IKAKLRSHLSHYKIP 409
Cdd:PRK12467 911 RMDHQVKIRGFRIELGEIEARLLAQPGVREAVVLAQPGDAGLQLVAYLVPAAVADGAEHQATRdeLKAQLRQVLPDYMVP 990
|
250
....*....|....*...
gi 428688192 410 KLWLKVDQIPRNPQGKID 427
Cdd:PRK12467 991 AHLLLLDSLPLTPNGKLD 1008
|
|
| A_NRPS_LgrA-like |
cd17645 |
adenylation (A) domain of linear gramicidin synthetase (LgrA) and similar proteins; This ... |
197-427 |
4.22e-10 |
|
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: 61.42 E-value: 4.22e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 428688192 197 ISLVPTQL--NFL-LENfpdwlKKFETVLVGGSAtpktlLQNCYRQKINLALTYGMTETASGVT---ILKPENFF---KG 267
Cdd:cd17645 198 ISFLPTGAaeQFMqLDN-----QSLRVLLTGGDK-----LKKIERKGYKLVNNYGPTENTVVATsfeIDKPYANIpigKP 267
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 428688192 268 INNSGHLlphsqIVIKKNQAK----FGQIIIKSDSLFKGY-------------YPHYKNSNYFLTDDLGYFDQDNFLHIV 330
Cdd:cd17645 268 IDNTRVY-----ILDEALQLQpigvAGELCIAGEGLARGYlnrpeltaekfivHPFVPGERMYRTGDLAKFLPDGNIEFL 342
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 428688192 331 GRNSQKIISGGENVYPCEIENVVIKTGLVKDIVVVGKNDHYWGQIICAVYVAisgyDTEYLVNNIKAKLRSHLSHYKIPK 410
Cdd:cd17645 343 GRLDQQVKIRGYRIEPGEIEPFLMNHPLIELAAVLAKEDADGRKYLVAYVTA----PEEIPHEELREWLKNDLPDYMIPT 418
|
250
....*....|....*..
gi 428688192 411 LWLKVDQIPRNPQGKID 427
Cdd:cd17645 419 YFVHLKALPLTANGKVD 435
|
|
| entE |
PRK10946 |
(2,3-dihydroxybenzoyl)adenylate synthase; |
198-435 |
1.16e-09 |
|
(2,3-dihydroxybenzoyl)adenylate synthase;
Pssm-ID: 236803 [Multi-domain] Cd Length: 536 Bit Score: 60.39 E-value: 1.16e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 428688192 198 SLVPTQLNFLLENFPDW-----LKKFETVLVGGSATPKTL------LQNCYRQKInlaltYGMTETASGVTIL--KPENF 264
Cdd:PRK10946 277 ALVPPAVSLWLQAIAEGgsraqLASLKLLQVGGARLSETLarripaELGCQLQQV-----FGMAEGLVNYTRLddSDERI 351
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 428688192 265 F-------------KGINNSGHLLPHSQIvikknqakfGQIIIKSDSLFKGYY--PHYKNS-----NYFLTDDLGYFDQD 324
Cdd:PRK10946 352 FttqgrpmspddevWVADADGNPLPQGEV---------GRLMTRGPYTFRGYYksPQHNASafdanGFYCSGDLVSIDPD 422
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 428688192 325 NFLHIVGRNSQKIISGGENVYPCEIENVVIKTGLVKDIVVVGKNDHYWGQIICAvyvaisgydteYLV--NNIKA-KLRS 401
Cdd:PRK10946 423 GYITVVGREKDQINRGGEKIAAEEIENLLLRHPAVIHAALVSMEDELMGEKSCA-----------FLVvkEPLKAvQLRR 491
|
250 260 270
....*....|....*....|....*....|....*....
gi 428688192 402 HL-----SHYKIPKLWLKVDQIPRNPQGKIDYGYLEKML 435
Cdd:PRK10946 492 FLreqgiAEFKLPDRVECVDSLPLTAVGKVDKKQLRQWL 530
|
|
| A_NRPS_ProA |
cd17656 |
gramicidin S synthase 2, also known as ATP-dependent proline adenylase; This family of the ... |
164-427 |
1.31e-09 |
|
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: 59.80 E-value: 1.31e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 428688192 164 QIVRTFVTGGSLAIY------DYSLLKKEIQNHNYDNFFISLVPTQLNF----LLENFPDWLKkfETVLVGGSATPKTLL 233
Cdd:cd17656 186 EIFSTLLSGGTLYIIreetkrDVEQLFDLVKRHNIEVVFLPVAFLKFIFsereFINRFPTCVK--HIITAGEQLVITNEF 263
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 428688192 234 QNCYRQK-INLALTYGMTET--ASGVTIlKPENFF-------KGINNSGHLLPHSQIVIKKnQAKFGQIIIKSDSLFKGY 303
Cdd:cd17656 264 KEMLHEHnVHLHNHYGPSEThvVTTYTI-NPEAEIpelppigKPISNTWIYILDQEQQLQP-QGIVGELYISGASVARGY 341
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 428688192 304 Y-------------PHYKNSNYFLTDDLGYFDQDNFLHIVGRNSQKIISGGENVYPCEIENVVIKTGLVKDIVVVGKNDH 370
Cdd:cd17656 342 LnrqeltaekffpdPFDPNERMYRTGDLARYLPDGNIEFLGRADHQVKIRGYRIELGEIEAQLLNHPGVSEAVVLDKADD 421
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*..
gi 428688192 371 YWGQIICAVYVAISGYDTEYLvnniKAKLRSHLSHYKIPKLWLKVDQIPRNPQGKID 427
Cdd:cd17656 422 KGEKYLCAYFVMEQELNISQL----REYLAKQLPEYMIPSFFVPLDQLPLTPNGKVD 474
|
|
| PLN02246 |
PLN02246 |
4-coumarate--CoA ligase |
152-426 |
1.65e-09 |
|
4-coumarate--CoA ligase
Pssm-ID: 215137 [Multi-domain] Cd Length: 537 Bit Score: 59.61 E-value: 1.65e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 428688192 152 CCLPLYHVSGLMQI----VRTfvtGGSLAI---YDYSLLKKEIQNHNYDnfFISLVPTQL-----NFLLENFPdwLKKFE 219
Cdd:PLN02246 229 CVLPMFHIYSLNSVllcgLRV---GAAILImpkFEIGALLELIQRHKVT--IAPFVPPIVlaiakSPVVEKYD--LSSIR 301
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 428688192 220 TVLVGGSATPKTLlQNCYRQKINLALT---YGMTE-----------------TASG----------VTILKPEnffkgin 269
Cdd:PLN02246 302 MVLSGAAPLGKEL-EDAFRAKLPNAVLgqgYGMTEagpvlamclafakepfpVKSGscgtvvrnaeLKIVDPE------- 373
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 428688192 270 nSGHLLPHsqivikkNQAkfGQIIIKSDSLFKGYY--PH-----YKNSNYFLTDDLGYFDQDNFLHIVGRNSQKIISGGE 342
Cdd:PLN02246 374 -TGASLPR-------NQP--GEICIRGPQIMKGYLndPEatantIDKDGWLHTGDIGYIDDDDELFIVDRLKELIKYKGF 443
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 428688192 343 NVYPCEIENVVIKTGLVKDIVVVGKNDHYWGQIICAVYVAISGYD-TEylvNNIKAKLRSHLSHYK-IPKLWLkVDQIPR 420
Cdd:PLN02246 444 QVAPAELEALLISHPSIADAAVVPMKDEVAGEVPVAFVVRSNGSEiTE---DEIKQFVAKQVVFYKrIHKVFF-VDSIPK 519
|
....*.
gi 428688192 421 NPQGKI 426
Cdd:PLN02246 520 APSGKI 525
|
|
| PRK05857 |
PRK05857 |
fatty acid--CoA ligase; |
112-426 |
1.96e-09 |
|
fatty acid--CoA ligase;
Pssm-ID: 180293 [Multi-domain] Cd Length: 540 Bit Score: 59.64 E-value: 1.96e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 428688192 112 MIPTGGTSGNIKFAIHTWETLNA-----SAKGFSQF-WQRRKINFfCCLPLYHVSGLMQIVRTFVTGGS-LAIYDYSLLK 184
Cdd:PRK05857 174 MIFTSGTTGEPKAVLLANRTFFAvpdilQKEGLNWVtWVVGETTY-SPLPATHIGGLWWILTCLMHGGLcVTGGENTTSL 252
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 428688192 185 KEIQNHNYDNFfISLVPTQLNFLLENFpdwlkKFETVLV--------GGSATPKTLLQNCYRQKINLALTYGMTETasGV 256
Cdd:PRK05857 253 LEILTTNAVAT-TCLVPTLLSKLVSEL-----KSANATVpslrlvgyGGSRAIAADVRFIEATGVRTAQVYGLSET--GC 324
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 428688192 257 TIL------------------KP----ENFFKGINNSGHLLPHSqivikKNQAKFGQIIIKSDSLFKGYYPHYKNSNYFL 314
Cdd:PRK05857 325 TALclptddgsivkieagavgRPypgvDVYLAATDGIGPTAPGA-----GPSASFGTLWIKSPANMLGYWNNPERTAEVL 399
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 428688192 315 TD------DLGYFDQDNFLHIVGRNSQKIISGGENVYPCEIENVVIKTGLVKDIVVVGKNDHYWGQIICAVYVAISGYD- 387
Cdd:PRK05857 400 IDgwvntgDLLERREDGFFYIKGRSSEMIICGGVNIAPDEVDRIAEGVSGVREAACYEIPDEEFGALVGLAVVASAELDe 479
|
330 340 350 360
....*....|....*....|....*....|....*....|.
gi 428688192 388 --TEYLVNNIKAKLRSHLSHYKIPKLWLKVDQIPRNPQGKI 426
Cdd:PRK05857 480 saARALKHTIAARFRRESEPMARPSTIVIVTDIPRTQSGKV 520
|
|
| A_NRPS_Sfm_like |
cd12115 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including Saframycin A gene ... |
197-431 |
2.99e-09 |
|
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: 58.87 E-value: 2.99e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 428688192 197 ISLVPTQLNFLLEN--FPDWLKkfeTVLVGGSATPKTLLQNCYRQK-----INLaltYGMTE--TASGVTILKPENffKG 267
Cdd:cd12115 195 INTVPSAAAELLRHdaLPASVR---VVNLAGEPLPRDLVQRLYARLqvervVNL---YGPSEdtTYSTVAPVPPGA--SG 266
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 428688192 268 INNSGHLLPHSQI-VIKKNQAKF-----GQIIIKSDSLFKGYY-------------PHYKNSNYFLTDDLGYFDQDNFLH 328
Cdd:cd12115 267 EVSIGRPLANTQAyVLDRALQPVplgvpGELYIGGAGVARGYLgrpgltaerflpdPFGPGARLYRTGDLVRWRPDGLLE 346
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 428688192 329 IVGRNSQKIISGGENVYPCEIENVVIKTGLVKDIVVVGKNDHYWGQIICAvYVAISGyDTEYLVNNIKAKLRSHLSHYKI 408
Cdd:cd12115 347 FLGRADNQVKVRGFRIELGEIEAALRSIPGVREAVVVAIGDAAGERRLVA-YIVAEP-GAAGLVEDLRRHLGTRLPAYMV 424
|
250 260
....*....|....*....|...
gi 428688192 409 PKLWLKVDQIPRNPQGKIDYGYL 431
Cdd:cd12115 425 PSRFVRLDALPLTPNGKIDRSAL 447
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
206-427 |
5.75e-09 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 58.82 E-value: 5.75e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 428688192 206 FLLENFPDWLKKFETVLVGGSATPKTLLQNCYRQkINLALTYGMTETASGVTILKPENFFKGINNSGHLLPHSQIVIKKN 285
Cdd:PRK12316 3301 FLEEEDAHRCTSLKRIVCGGEALPADLQQQVFAG-LPLYNLYGPTEATITVTHWQCVEEGKDAVPIGRPIANRACYILDG 3379
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 428688192 286 ------QAKFGQIIIKSDSLFKGYY-------------PHYKNSNYFLTDDLGYFDQDNFLHIVGRNSQKIISGGENVYP 346
Cdd:PRK12316 3380 slepvpVGALGELYLGGEGLARGYHnrpgltaerfvpdPFVPGERLYRTGDLARYRADGVIEYIGRVDHQVKIRGFRIEL 3459
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 428688192 347 CEIENVVIKTGLVKDIVVVGKNdhywGQIICAvYVAISGYDTEyLVNNIKAKLRSHLSHYKIPKLWLKVDQIPRNPQGKI 426
Cdd:PRK12316 3460 GEIEARLLEHPWVREAVVLAVD----GRQLVA-YVVPEDEAGD-LREALKAHLKASLPEYMVPAHLLFLERMPLTPNGKL 3533
|
.
gi 428688192 427 D 427
Cdd:PRK12316 3534 D 3534
|
|
| BCL_4HBCL |
cd05959 |
Benzoate CoA ligase (BCL) and 4-Hydroxybenzoate-Coenzyme A Ligase (4-HBA-CoA ligase); Benzoate ... |
290-427 |
9.57e-09 |
|
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: 57.38 E-value: 9.57e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 428688192 290 GQIIIKSDSLFKGYYPHYKNS------NYFLTDDLGYFDQDNFLHIVGRNSQKIISGGENVYPCEIENVVIKTGLVKDIV 363
Cdd:cd05959 359 GELYVRGPSSATMYWNNRDKTrdtfqgEWTRTGDKYVRDDDGFYTYAGRADDMLKVSGIWVSPFEVESALVQHPAVLEAA 438
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 428688192 364 VVGKNDHYWGQIICAVYVAISGY-DTEYLVNNIKAKLRSHLSHYKIPKLWLKVDQIPRNPQGKID 427
Cdd:cd05959 439 VVGVEDEDGLTKPKAFVVLRPGYeDSEALEEELKEFVKDRLAPYKYPRWIVFVDELPKTATGKIQ 503
|
|
| A_NRPS_VisG_like |
cd17651 |
similar to adenylation domain of virginiamycin S synthetase; This family of the adenylation (A) ... |
290-428 |
1.37e-08 |
|
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: 56.58 E-value: 1.37e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 428688192 290 GQIIIKSDSLFKGYY-------------PHYKNSNYFLTDDLGYFDQDNFLHIVGRNSQKIISGGENVYPCEIENVVIKT 356
Cdd:cd17651 338 GELYIGGAGLARGYLnrpeltaerfvpdPFVPGARMYRTGDLARWLPDGELEFLGRADDQVKIRGFRIELGEIEAALARH 417
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 428688192 357 GLVKDIVVVGKNDHYWGQIICAVYVAisGYDTEYLVNNIKAKLRSHLSHYKIPKLWLKVDQIPRNPQGKIDY 428
Cdd:cd17651 418 PGVREAVVLAREDRPGEKRLVAYVVG--DPEAPVDAAELRAALATHLPEYMVPSAFVLLDALPLTPNGKLDR 487
|
|
| PRK04319 |
PRK04319 |
acetyl-CoA synthetase; Provisional |
298-426 |
1.69e-08 |
|
acetyl-CoA synthetase; Provisional
Pssm-ID: 235279 [Multi-domain] Cd Length: 570 Bit Score: 56.44 E-value: 1.69e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 428688192 298 SLFKGY------YPHYKNSNYFLTDDLGYFDQDNFLHIVGRNSQKIISGGENVYPCEIENVVIKTGLVKDIVVVGKNDHY 371
Cdd:PRK04319 413 SMMRGIwnnpekYESYFAGDWYVSGDSAYMDEDGYFWFQGRVDDVIKTSGERVGPFEVESKLMEHPAVAEAGVIGKPDPV 492
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*..
gi 428688192 372 WGQIICAvYVAI-SGYD-TEYLVNNIKAKLRSHLSHYKIPKLWLKVDQIPRNPQGKI 426
Cdd:PRK04319 493 RGEIIKA-FVALrPGYEpSEELKEEIRGFVKKGLGAHAAPREIEFKDKLPKTRSGKI 548
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
170-427 |
2.14e-08 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 56.89 E-value: 2.14e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 428688192 170 VTGGSLAIYDYSL-----LKKEIQNHNYDnfFISLVPTQLNFLLENFPDW--LKKFETVLVGGSATPKTLLQNCYRQKIN 242
Cdd:PRK12316 4758 INGASVVIRDDSLwdperLYAEIHEHRVT--VLVFPPVYLQQLAEHAERDgePPSLRVYCFGGEAVAQASYDLAWRALKP 4835
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 428688192 243 LAL--TYGMTETASGVTILKPENFFKGINNS---GHLLPHSQIVIKKNQAKF------GQIIIKSDSLFKGYY------- 304
Cdd:PRK12316 4836 VYLfnGYGPTETTVTVLLWKARDGDACGAAYmpiGTPLGNRSGYVLDGQLNPlpvgvaGELYLGGEGVARGYLerpalta 4915
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 428688192 305 ------PHYKN-SNYFLTDDLGYFDQDNFLHIVGRNSQKIISGGENVYPCEIENVVIKTGLVKDIVVVGKNDHYWGQIIC 377
Cdd:PRK12316 4916 erfvpdPFGAPgGRLYRTGDLARYRADGVIDYLGRVDHQVKIRGFRIELGEIEARLREHPAVREAVVIAQEGAVGKQLVG 4995
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*
gi 428688192 378 AV-----YVAISGYDTEYLVNNIKAKLRSHLSHYKIPKLWLKVDQIPRNPQGKID 427
Cdd:PRK12316 4996 YVvpqdpALADADEAQAELRDELKAALRERLPEYMVPAHLVFLARMPLTPNGKLD 5050
|
|
| PRK06060 |
PRK06060 |
p-hydroxybenzoic acid--AMP ligase FadD22; |
84-426 |
2.18e-08 |
|
p-hydroxybenzoic acid--AMP ligase FadD22;
Pssm-ID: 180374 [Multi-domain] Cd Length: 705 Bit Score: 56.58 E-value: 2.18e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 428688192 84 LVKPDFLFSD--HLEKTYYNPPHNHSYqGIMIPTGGTSGNIKFAIHTwetlNASAKGFSQFWQRRKINF------FCCLP 155
Cdd:PRK06060 121 VAEAAELMSEaaRVAPGGYEPMGGDAL-AYATYTSGTTGPPKAAIHR----HADPLTFVDAMCRKALRLtpedtgLCSAR 195
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 428688192 156 LYHVSGLMQIVRTFVTGGSLAIYDYSLLKKEIQNHNYDNFFISLVPTQLNFLLENF----PDWLKKFETVLVGGSAtpkt 231
Cdd:PRK06060 196 MYFAYGLGNSVWFPLATGGSAVINSAPVTPEAAAILSARFGPSVLYGVPNFFARVIdscsPDSFRSLRCVVSAGEA---- 271
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 428688192 232 llqncyrqkINLALTYGMTETASGVTIL----KPENFFKGINNS---------GHLLPHSQI-VIKKNQAKFG-----QI 292
Cdd:PRK06060 272 ---------LELGLAERLMEFFGGIPILdgigSTEVGQTFVSNRvdewrlgtlGRVLPPYEIrVVAPDGTTAGpgvegDL 342
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 428688192 293 IIKSDSLFKGYY----PHYKNSNYFLTDDLGYFDQDNFLHIVGRNSQKIISGGENVYPCEIENVVIKTGLVKDIVVVGKN 368
Cdd:PRK06060 343 WVRGPAIAKGYWnrpdSPVANEGWLDTRDRVCIDSDGWVTYRCRADDTEVIGGVNVDPREVERLIIEDEAVAEAAVVAVR 422
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*....
gi 428688192 369 DHYWGQIICAVYV-AISGYDTEYLVNNIKAKLRSHLSHYKIPKLWLKVDQIPRNPQGKI 426
Cdd:PRK06060 423 ESTGASTLQAFLVaTSGATIDGSVMRDLHRGLLNRLSAFKVPHRFAVVDRLPRTPNGKL 481
|
|
| LC_FACS_bac1 |
cd17641 |
bacterial long-chain fatty acid CoA synthetase; The members of this family are bacterial ... |
241-384 |
3.72e-08 |
|
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: 55.51 E-value: 3.72e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 428688192 241 INLALTYGMTETASGVTI-----LKPENFfkginnsGHLLPHSQIVIKKNqakfGQIIIKSDSLFKGYYPHYKNS----- 310
Cdd:cd17641 349 VPLKQLYGQTELAGAYTVhrdgdVDPDTV-------GVPFPGTEVRIDEV----GEILVRSPGVFVGYYKNPEATaedfd 417
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 428688192 311 --NYFLTDDLGYFDQDNFLHIVGRNSQ-KIISGGENVYPCEIENVVIKTGLVKDIVVVGKNDHYWGQIICAVYVAIS 384
Cdd:cd17641 418 edGWLHTGDAGYFKENGHLVVIDRAKDvGTTSDGTRFSPQFIENKLKFSPYIAEAVVLGAGRPYLTAFICIDYAIVG 494
|
|
| ACS-like |
cd17634 |
acetate-CoA ligase; This family includes acyl- and aryl-CoA ligases, as well as the ... |
311-426 |
5.90e-08 |
|
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: 54.89 E-value: 5.90e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 428688192 311 NYFLTDDLGYFDQDNFLHIVGRNSQKIISGGENVYPCEIENVVIKTGLVKDIVVVGKNDHYWGQIICAVYVAISGY-DTE 389
Cdd:cd17634 470 GMYFSGDGARRDEDGYYWITGRSDDVINVAGHRLGTAEIESVLVAHPKVAEAAVVGIPHAIKGQAPYAYVVLNHGVePSP 549
|
90 100 110
....*....|....*....|....*....|....*..
gi 428688192 390 YLVNNIKAKLRSHLSHYKIPKLWLKVDQIPRNPQGKI 426
Cdd:cd17634 550 ELYAELRNWVRKEIGPLATPDVVHWVDSLPKTRSGKI 586
|
|
| PRK08633 |
PRK08633 |
2-acyl-glycerophospho-ethanolamine acyltransferase; Validated |
228-427 |
1.10e-07 |
|
2-acyl-glycerophospho-ethanolamine acyltransferase; Validated
Pssm-ID: 236315 [Multi-domain] Cd Length: 1146 Bit Score: 54.54 E-value: 1.10e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 428688192 228 TPKTLLQNCYRQKINLALTYGMTETASGVTILKPENFfkginnsgHLLPHSQIvikknqakfGQIIIKSDSLFKGYY--- 304
Cdd:PRK08633 943 LPDVLAADFKRQTGSKEGSVGMPLPGVAVRIVDPETF--------EELPPGED---------GLILIGGPQVMKGYLgdp 1005
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 428688192 305 -------PHYKNSNYFLTDDLGYFDQDNFLHIVGRNSQ--KIisGGENVYPCEIEN---VVIKTGLVKdIVVVGKNDHYW 372
Cdd:PRK08633 1006 ektaeviKDIDGIGWYVTGDKGHLDEDGFLTITDRYSRfaKI--GGEMVPLGAVEEelaKALGGEEVV-FAVTAVPDEKK 1082
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 428688192 373 GQIICAVYVAISGydteylvnnIKAKLRSHLSHYKIPKLW-----LKVDQIPRNPQGKID 427
Cdd:PRK08633 1083 GEKLVVLHTCGAE---------DVEELKRAIKESGLPNLWkpsryFKVEALPLLGSGKLD 1133
|
|
| PRK05852 |
PRK05852 |
fatty acid--CoA ligase family protein; |
111-427 |
3.00e-07 |
|
fatty acid--CoA ligase family protein;
Pssm-ID: 235625 [Multi-domain] Cd Length: 534 Bit Score: 52.58 E-value: 3.00e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 428688192 111 IMIpTGGTSGNIKFAIHTWETLNASAKGFSQFWQRRKIN-FFCCLPLYHVSGLMQ-IVRTFVTGGSLAI-----YDYSLL 183
Cdd:PRK05852 181 IMF-TGGTTGLPKMVPWTHANIASSVRAIITGYRLSPRDaTVAVMPLYHGHGLIAaLLATLASGGAVLLpargrFSAHTF 259
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 428688192 184 KKEIqnHNYDNFFISLVPTQLNFLLEnfpdwlkKFETVLVGGSATPKTLLQNC---YRQKINLAL----------TYGMT 250
Cdd:PRK05852 260 WDDI--KAVGATWYTAVPTIHQILLE-------RAATEPSGRKPAALRFIRSCsapLTAETAQALqtefaapvvcAFGMT 330
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 428688192 251 ETASGVTILKPENFFKGIN--NSGHLLPHS-----QIVIKKNQ----AKFGQIIIKSDSLFKGYY--PHYKNSNY----F 313
Cdd:PRK05852 331 EATHQVTTTQIEGIGQTENpvVSTGLVGRStgaqiRIVGSDGLplpaGAVGEVWLRGTTVVRGYLgdPTITAANFtdgwL 410
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 428688192 314 LTDDLGYFDQDNFLHIVGRNSQKIISGGENVYPCEIENVVIKTGLVKDIVVVGKNDHYWGQIICAVYVAISGYDTEylVN 393
Cdd:PRK05852 411 RTGDLGSLSAAGDLSIRGRIKELINRGGEKISPERVEGVLASHPNVMEAAVFGVPDQLYGEAVAAVIVPRESAPPT--AE 488
|
330 340 350
....*....|....*....|....*....|....
gi 428688192 394 NIKAKLRSHLSHYKIPKLWLKVDQIPRNPQGKID 427
Cdd:PRK05852 489 ELVQFCRERLAAFEIPASFQEASGLPHTAKGSLD 522
|
|
| A_NRPS_SidN3_like |
cd05918 |
The adenylation (A) domain of siderophore-synthesizing nonribosomal peptide synthetases (NRPS); ... |
313-427 |
3.08e-07 |
|
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: 52.54 E-value: 3.08e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 428688192 313 FLTDDLGYFDQDNFLHIVGRN-SQ-KIisGGENVYPCEIENVVIKTGLVKDIVVVG---KNDHYWGQIICAVYVA----- 382
Cdd:cd05918 337 YRTGDLVRYNPDGSLEYVGRKdTQvKI--RGQRVELGEIEHHLRQSLPGAKEVVVEvvkPKDGSSSPQLVAFVVLdgsss 414
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*
gi 428688192 383 --------ISGYDTEY--LVNNIKAKLRSHLSHYKIPKLWLKVDQIPRNPQGKID 427
Cdd:cd05918 415 gsgdgdslFLEPSDEFraLVAELRSKLRQRLPSYMVPSVFLPLSHLPLTASGKID 469
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
197-427 |
4.42e-07 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 52.65 E-value: 4.42e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 428688192 197 ISLVPTQLN-FLLENFPDWLKKFETVLVGGSATPKTLLQNCYRQKINLALT--YGMTETASGVT-------------ILK 260
Cdd:PRK12316 750 LHFVPSMLQaFLQDEDVASCTSLRRIVCSGEALPADAQEQVFAKLPQAGLYnlYGPTEAAIDVThwtcveeggdsvpIGR 829
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 428688192 261 PenffkgINNSGHLLPHSQIVIKKNQAKfGQIIIKSDSLFKGYY-------------PHYKNSNYFLTDDLGYFDQDNFL 327
Cdd:PRK12316 830 P------IANLACYILDANLEPVPVGVL-GELYLAGRGLARGYHgrpgltaerfvpsPFVAGERMYRTGDLARYRADGVI 902
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 428688192 328 HIVGRNSQKIISGGENVYPCEIENVVIKTGLVKDIVVVGKNdhywGQIICAVYVAISgyDTEYLVNNIKAKLRSHLSHYK 407
Cdd:PRK12316 903 EYAGRIDHQVKLRGLRIELGEIEARLLEHPWVREAAVLAVD----GKQLVGYVVLES--EGGDWREALKAHLAASLPEYM 976
|
250 260
....*....|....*....|
gi 428688192 408 IPKLWLKVDQIPRNPQGKID 427
Cdd:PRK12316 977 VPAQWLALERLPLTPNGKLD 996
|
|
| A_NRPS_Cytc1-like |
cd17643 |
similar to adenylation domain of cytotrienin synthetase CytC1; This family of the adenylation ... |
312-427 |
7.52e-07 |
|
similar to adenylation domain of cytotrienin synthetase CytC1; This family of the adenylation (A) domain of nonribosomal peptide synthases (NRPS) includes Streptomyces sp. cytotrienin synthetase (CytC1), a relatively promiscuous adenylation enzyme that installs the aminoacyl moieties on the phosphopantetheinyl arm of the holo carrier protein CytC2. Also included are Streptomyces sp Thr1, involved in the biosynthesis of 4-chlorothreonine, Pseudomonas aeruginosa pyoverdine synthetase D (PvdD), involved in the biosynthesis of the siderophore pyoverdine and Pseudomonas syringae syringopeptin synthetase, where syringpeptin is a necrosis-inducing phytotoxin that functions as a virulence determinant in the plant-pathogen interaction. The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester bond to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.
Pssm-ID: 341298 [Multi-domain] Cd Length: 450 Bit Score: 51.15 E-value: 7.52e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 428688192 312 YFLTDDLGYFDQDNFLHIVGRNSQKIISGGENVYPCEIENVVIKTGLVKDIVVVGKNDHYWGQIICAVYVAISGydTEYL 391
Cdd:cd17643 333 MYRTGDLARRLPDGELEYLGRADEQVKIRGFRIELGEIEAALATHPSVRDAAVIVREDEPGDTRLVAYVVADDG--AAAD 410
|
90 100 110
....*....|....*....|....*....|....*.
gi 428688192 392 VNNIKAKLRSHLSHYKIPKLWLKVDQIPRNPQGKID 427
Cdd:cd17643 411 IAELRALLKELLPDYMVPARYVPLDALPLTVNGKLD 446
|
|
| A_NRPS_ACVS-like |
cd17648 |
N-(5-amino-5-carboxypentanoyl)-L-cysteinyl-D-valine synthase; This family contains ACV ... |
247-427 |
7.81e-07 |
|
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: 51.25 E-value: 7.81e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 428688192 247 YGMTETAsgVTILKpeNFFKG---INNS-GHLLPHSQIVIKKNQAK------FGQIIIKSDSLFKGYY------------ 304
Cdd:cd17648 239 YGPTETT--VTNHK--RFFPGdqrFDKSlGRPVRNTKCYVLNDAMKrvpvgaVGELYLGGDGVARGYLnrpeltaerflp 314
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 428688192 305 -PHY--------KNSNYFLTDDLGYFDQDNFLHIVGRNSQKIISGGENVYPCEIENVVIKTGLVKDIVVVGKNDHYWGQI 375
Cdd:cd17648 315 nPFQteqerargRNARLYKTGDLVRWLPSGELEYLGRNDFQVKIRGQRIEPGEVEAALASYPGVRECAVVAKEDASQAQS 394
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 428688192 376 -----ICAVYVAISGYDTEylvNNIKAKLRSHLSHYKIPKLWLKVDQIPRNPQGKID 427
Cdd:cd17648 395 riqkyLVGYYLPEPGHVPE---SDLLSFLRAKLPRYMVPARLVRLEGIPVTINGKLD 448
|
|
| A_NRPS_PpsD_like |
cd17650 |
similar to adenylation domain of plipastatin synthase (PpsD); This family of the adenylation ... |
69-427 |
1.66e-06 |
|
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: 50.16 E-value: 1.66e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 428688192 69 LNPHWQQEELQqvyklvkpdFLFSDHLEKTYYNPPHNHSYqgiMIPTGGTSGNIKFAIHTWETLNASAKGfsqfWQRRki 148
Cdd:cd17650 67 IDPDYPAERLQ---------YMLEDSGAKLLLTQPEDLAY---VIYTSGTTGKPKGVMVEHRNVAHAAHA----WRRE-- 128
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 428688192 149 nffcclplYHVSG----LMQI------------VRTFVTGGSLAI------YDYSLLKKEIQNHNYDNFfiSLVPTQLNF 206
Cdd:cd17650 129 --------YELDSfpvrLLQMasfsfdvfagdfARSLLNGGTLVIcpdevkLDPAALYDLILKSRITLM--ESTPALIRP 198
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 428688192 207 LLEnFPDWLK---KFETVLVGGSAT-----PKTLLQNcYRQKINLALTYGMTETASGVTILK------PENFFKGInnsG 272
Cdd:cd17650 199 VMA-YVYRNGldlSAMRLLIVGSDGckaqdFKTLAAR-FGQGMRIINSYGVTEATIDSTYYEegrdplGDSANVPI---G 273
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 428688192 273 HLLPHSQIVIKKNQAK------FGQIIIKSDSLFKGYY-------------PHYKNSNYFLTDDLGYFDQDNFLHIVGRN 333
Cdd:cd17650 274 RPLPNTAMYVLDERLQpqpvgvAGELYIGGAGVARGYLnrpeltaerfvenPFAPGERMYRTGDLARWRADGNVELLGRV 353
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 428688192 334 SQKIISGGENVYPCEIENVVIKTGLVKDIVVVGKNDHYWGQIICAVYVAISGYDTeylvNNIKAKLRSHLSHYKIPKLWL 413
Cdd:cd17650 354 DHQVKIRGFRIELGEIESQLARHPAIDEAVVAVREDKGGEARLCAYVVAAATLNT----AELRAFLAKELPSYMIPSYYV 429
|
410
....*....|....
gi 428688192 414 KVDQIPRNPQGKID 427
Cdd:cd17650 430 QLDALPLTPNGKVD 443
|
|
| A_NRPS_PvdJ-like |
cd17649 |
non-ribosomal peptide synthetase; This family of the adenylation (A) domain of nonribosomal ... |
221-427 |
1.69e-06 |
|
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: 50.06 E-value: 1.69e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 428688192 221 VLVGGSATPKTLLQNCYRQKINLALTYGMTETASGVTILKPENFFKGINNS---GHLLPHSQIVIKKNQAKF------GQ 291
Cdd:cd17649 217 YIFGGEALSPELLRRWLKAPVRLFNAYGPTEATVTPLVWKCEAGAARAGASmpiGRPLGGRSAYILDADLNPvpvgvtGE 296
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 428688192 292 IIIKSDSLFKGYypHYK----------------NSNYFLTDDLGYFDQDNFLHIVGRNSQKIISGGENVYPCEIENVVIK 355
Cdd:cd17649 297 LYIGGEGLARGY--LGRpeltaerfvpdpfgapGSRLYRTGDLARWRDDGVIEYLGRVDHQVKIRGFRIELGEIEAALLE 374
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 428688192 356 TGLVKDIVVVGKnDHYWGQIICAVYVAISGYDTEYLVNNIKAKLRSHLSHYKIPKLWLKVDQIPRNPQGKID 427
Cdd:cd17649 375 HPGVREAAVVAL-DGAGGKQLVAYVVLRAAAAQPELRAQLRTALRASLPDYMVPAHLVFLARLPLTPNGKLD 445
|
|
| A_NRPS_AB3403-like |
cd17646 |
Peptide Synthetase; The adenylation (A) domain of NRPS recognizes a specific amino acid or ... |
315-428 |
2.07e-06 |
|
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: 49.97 E-value: 2.07e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 428688192 315 TDDLGYFDQDNFLHIVGRNSQKIISGGENVYPCEIENVVIKTGLVKDIVVVGKNDHYWGQIICAvYVAISGYDTEYLVNN 394
Cdd:cd17646 373 TGDLARWRPDGALEFLGRSDDQVKIRGFRVEPGEIEAALAAHPAVTHAVVVARAAPAGAARLVG-YVVPAAGAAGPDTAA 451
|
90 100 110
....*....|....*....|....*....|....
gi 428688192 395 IKAKLRSHLSHYKIPKLWLKVDQIPRNPQGKIDY 428
Cdd:cd17646 452 LRAHLAERLPEYMVPAAFVVLDALPLTANGKLDR 485
|
|
| LC-FACS_euk |
cd05927 |
Eukaryotic long-chain fatty acid CoA synthetase (LC-FACS); The members of this family are ... |
115-393 |
3.29e-06 |
|
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: 49.14 E-value: 3.29e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 428688192 115 TGGTSGNIKFAIHTWETLNASAKGFSQFWQRR-KIN----FFCCLPLYHVSGLMQIVRTFVTGGSLAIY--DYSLLKKEI 187
Cdd:cd05927 122 TSGTTGNPKGVMLTHGNIVSNVAGVFKILEILnKINptdvYISYLPLAHIFERVVEALFLYHGAKIGFYsgDIRLLLDDI 201
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 428688192 188 Q--------------NHNYDNFFISLV--PTQLNFLLeNF-----------------PDW----LKKFETVLVG------ 224
Cdd:cd05927 202 KalkptvfpgvprvlNRIYDKIFNKVQakGPLKRKLF-NFalnyklaelrsgvvrasPFWdklvFNKIKQALGGnvrlml 280
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 428688192 225 -GSA--TPKTL--LQNCYrqKINLALTYGMTETASGVTILKPenffkGINNSGHL---LPHSQIVIK----------KNQ 286
Cdd:cd05927 281 tGSAplSPEVLefLRVAL--GCPVLEGYGQTECTAGATLTLP-----GDTSVGHVggpLPCAEVKLVdvpemnydakDPN 353
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 428688192 287 AKfGQIIIKSDSLFKGYyphYKNSNyfLTDDLgyFDQDNFLHI--VGR----NSQKII---------SGGENVYPCEIEN 351
Cdd:cd05927 354 PR-GEVCIRGPNVFSGY---YKDPE--KTAEA--LDEDGWLHTgdIGEwlpnGTLKIIdrkknifklSQGEYVAPEKIEN 425
|
330 340 350 360
....*....|....*....|....*....|....*....|..
gi 428688192 352 VVIKTGLVKDIVVVGKNDHYWgqiicavYVAISGYDTEYLVN 393
Cdd:cd05927 426 IYARSPFVAQIFVYGDSLKSF-------LVAIVVPDPDVLKE 460
|
|
| LC_FACS_euk1 |
cd17639 |
Eukaryotic long-chain fatty acid CoA synthetase (LC-FACS), including fungal proteins; The ... |
247-332 |
3.77e-06 |
|
Eukaryotic long-chain fatty acid CoA synthetase (LC-FACS), including fungal proteins; The members of this family are eukaryotic fatty acid CoA synthetases (EC 6.2.1.3) that activate fatty acids with chain lengths of 12 to 20 and includes fungal proteins. They act on a wide range of long-chain saturated and unsaturated fatty acids, but the enzymes from different tissues show some variation in specificity. LC-FACS catalyzes the formation of fatty acyl-CoA in a two-step reaction: the formation of a fatty acyl-AMP molecule as an intermediate, and the formation of a fatty acyl-CoA. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions. Organisms tend to have multiple isoforms of LC-FACS genes with multiple splice variants. For example, nine genes are found in Arabidopsis and six genes are expressed in mammalian cells. In Schizosaccharomyces pombe, lcf1 gene encodes a new fatty acyl-CoA synthetase that preferentially recognizes myristic acid as a substrate.
Pssm-ID: 341294 [Multi-domain] Cd Length: 507 Bit Score: 49.14 E-value: 3.77e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 428688192 247 YGMTETASGVTILKPENFFKGInnSGHLLPHSQIVIK---------KNQAKFGQIIIKSDSLFKGYY--PH-----YKNS 310
Cdd:cd17639 281 YGLTETCAGGTVQDPGDLETGR--VGPPLPCCEIKLVdweeggystDKPPPRGEILIRGPNVFKGYYknPEktkeaFDGD 358
|
90 100
....*....|....*....|..
gi 428688192 311 NYFLTDDLGYFDQDNFLHIVGR 332
Cdd:cd17639 359 GWFHTGDIGEFHPDGTLKIIDR 380
|
|
| PRK05851 |
PRK05851 |
long-chain-fatty acid--ACP ligase MbtM; |
272-369 |
5.24e-06 |
|
long-chain-fatty acid--ACP ligase MbtM;
Pssm-ID: 180289 [Multi-domain] Cd Length: 525 Bit Score: 48.61 E-value: 5.24e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 428688192 272 GHLLPHSQIVI-------KKNQAKFGQIIIKSDSLFKGYYPH--YKNSNYFLTDDLGYFdQDNFLHIVGRNSQKIISGGE 342
Cdd:PRK05851 348 GNPIPGMEVRIspgdgaaGVAGREIGEIEIRGASMMSGYLGQapIDPDDWFPTGDLGYL-VDGGLVVCGRAKELITVAGR 426
|
90 100
....*....|....*....|....*....
gi 428688192 343 NVYPCEIENVVIKTGLVKD--IVVVGKND 369
Cdd:PRK05851 427 NIFPTEIERVAAQVRGVREgaVVAVGTGE 455
|
|
| A_NRPS_MycA_like |
cd05908 |
The adenylation domain of nonribosomal peptide synthetases (NRPS) similar to mycosubtilin ... |
272-426 |
6.33e-06 |
|
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: 48.25 E-value: 6.33e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 428688192 272 GHLLPHSQIVIKKNQAK------FGQIIIKSDSLFKGYYPHYKNSNYFLTDD-------LGyFDQDNFLHIVGRNSQKII 338
Cdd:cd05908 317 GKPIDETDIRICDEDNKilpdgyIGHIQIRGKNVTPGYYNNPEATAKVFTDDgwlktgdLG-FIRNGRLVITGREKDIIF 395
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 428688192 339 SGGENVYPCEIENVVIKTG--LVKDIVVVGKNDHYWGQ--IICAVYVAISGYDTEYLVNNIKaklrSHLSHYK---IPKL 411
Cdd:cd05908 396 VNGQNVYPHDIERIAEELEgvELGRVVACGVNNSNTRNeeIFCFIEHRKSEDDFYPLGKKIK----KHLNKRGgwqINEV 471
|
170
....*....|....*
gi 428688192 412 wLKVDQIPRNPQGKI 426
Cdd:cd05908 472 -LPIRRIPKTTSGKV 485
|
|
| AACS_like |
cd05968 |
Uncharacterized acyl-CoA synthetase subfamily similar to Acetoacetyl-CoA synthetase; This ... |
317-426 |
2.04e-05 |
|
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: 46.71 E-value: 2.04e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 428688192 317 DLGYFDQDNFLHIVGRNSQKIISGGENVYPCEIENVVIKTGLVKDIVVVGKNDHYWGQIICAVYVAISGYD-TEYLVNNI 395
Cdd:cd05968 477 DFAYYDEEGYFYILGRSDDTINVAGKRVGPAEIESVLNAHPAVLESAAIGVPHPVKGEAIVCFVVLKPGVTpTEALAEEL 556
|
90 100 110
....*....|....*....|....*....|.
gi 428688192 396 KAKLRSHLSHYKIPKLWLKVDQIPRNPQGKI 426
Cdd:cd05968 557 MERVADELGKPLSPERILFVKDLPKTRNAKV 587
|
|
| ACS |
cd05966 |
Acetyl-CoA synthetase (also known as acetate-CoA ligase and acetyl-activating enzyme); ... |
246-426 |
2.45e-05 |
|
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: 46.79 E-value: 2.45e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 428688192 246 TYGMTETAS-------GVTILKPEN----FFkGI------NNSGHLLPHSQ--IVIKKNQAKFGQIIIKSDSLF-KGYYP 305
Cdd:cd05966 387 TWWQTETGGimitplpGATPLKPGSatrpFF-GIepaildEEGNEVEGEVEgyLVIKRPWPGMARTIYGDHERYeDTYFS 465
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 428688192 306 HYKNsnYFLTDDLGYFDQDNFLHIVGRNSQKIISGGENVYPCEIENVVIKTGLVKDIVVVGKNDHYWGQIICAVYVAISG 385
Cdd:cd05966 466 KFPG--YYFTGDGARRDEDGYYWITGRVDDVINVSGHRLGTAEVESALVAHPAVAEAAVVGRPHDIKGEAIYAFVTLKDG 543
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 428688192 386 YD-TEYLVNNIKAKLRSHLSHYKIPKLWLKVDQIPRNPQGKI 426
Cdd:cd05966 544 EEpSDELRKELRKHVRKEIGPIATPDKIQFVPGLPKTRSGKI 585
|
|
| PRK06164 |
PRK06164 |
acyl-CoA synthetase; Validated |
271-419 |
2.73e-05 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 235722 [Multi-domain] Cd Length: 540 Bit Score: 46.27 E-value: 2.73e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 428688192 271 SGHLLPHSQIvikknqakfGQIIIKSDSLFKGYYPH-------YKNSNYFLTDDLGYFDQDNFLHIVGRNSQKIISGGEN 343
Cdd:PRK06164 368 DGALLPDGES---------GEIEIRAPSLMRGYLDNpdataraLTDDGYFRTGDLGYTRGDGQFVYQTRMGDSLRLGGFL 438
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 428688192 344 VYPCEIENVVIKTGLVKDIVVVGKNDHywGQIICAVYV-AISGYDTEylVNNIKAKLRSHLSHYKIPKLWLKVDQIP 419
Cdd:PRK06164 439 VNPAEIEHALEALPGVAAAQVVGATRD--GKTVPVAFViPTDGASPD--EAGLMAACREALAGFKVPARVQVVEAFP 511
|
|
| PRK05691 |
PRK05691 |
peptide synthase; Validated |
315-427 |
3.23e-05 |
|
peptide synthase; Validated
Pssm-ID: 235564 [Multi-domain] Cd Length: 4334 Bit Score: 46.70 E-value: 3.23e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 428688192 315 TDDLGYFDQDNFLHIVGRNSQKIISGGENVYPCEIENVVIKTGLVKDiVVVGKNDHYWGQIICAVYVAISGY-DTEYLVN 393
Cdd:PRK05691 4106 TGDLARRRSDGVLEYVGRIDHQVKIRGYRIELGEIEARLHEQAEVRE-AAVAVQEGVNGKHLVGYLVPHQTVlAQGALLE 4184
|
90 100 110
....*....|....*....|....*....|....
gi 428688192 394 NIKAKLRSHLSHYKIPKLWLKVDQIPRNPQGKID 427
Cdd:PRK05691 4185 RIKQRLRAELPDYMVPLHWLWLDRLPLNANGKLD 4218
|
|
| PRK06334 |
PRK06334 |
long chain fatty acid--[acyl-carrier-protein] ligase; Validated |
215-355 |
5.39e-05 |
|
long chain fatty acid--[acyl-carrier-protein] ligase; Validated
Pssm-ID: 180533 [Multi-domain] Cd Length: 539 Bit Score: 45.58 E-value: 5.39e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 428688192 215 LKKFETVLVGGSATPKTLLQNCYRQKINLALT--YGMTETASGVTIlKPENFFKGINNSGHLLPHSQIVIKKNQAKF--- 289
Cdd:PRK06334 298 LPSLRFVVIGGDAFKDSLYQEALKTFPHIQLRqgYGTTECSPVITI-NTVNSPKHESCVGMPIRGMDVLIVSEETKVpvs 376
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 428688192 290 ----GQIIIKSDSLFKGY--------YPHYKNSNYFLTDDLGYFDQDNFLHIVGRNSQKIISGGENVYPCEIENVVIK 355
Cdd:PRK06334 377 sgetGLVLTRGTSLFSGYlgedfgqgFVELGGETWYVTGDLGYVDRHGELFLKGRLSRFVKIGAEMVSLEALESILME 454
|
|
| FATP_FACS |
cd05940 |
Fatty acid transport proteins (FATP) play dual roles as fatty acid transporters and its ... |
113-366 |
8.05e-05 |
|
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: 44.65 E-value: 8.05e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 428688192 113 IPTGGTSGNIKFAIHTWETLnASAKGFSQFWQRRKIN--FFCCLPLYHVSGLM-QIVRTFVTGGSLAI---YDYSLLKKE 186
Cdd:cd05940 87 IYTSGTTGLPKAAIISHRRA-WRGGAFFAGSGGALPSdvLYTCLPLYHSTALIvGWSACLASGATLVIrkkFSASNFWDD 165
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 428688192 187 IQNHNYDNFfiSLVPTQLNFLLENFPDWLKKFETVlvggsatpKTLLQNCYRQKI-----------NLALTYGMTETASG 255
Cdd:cd05940 166 IRKYQATIF--QYIGELCRYLLNQPPKPTERKHKV--------RMIFGNGLRPDIweefkerfgvpRIAEFYAATEGNSG 235
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 428688192 256 VTILkpENFFKGINNSGHLLPH--------------------SQIVIKKNQAKFGQII--IKSDSLFKGYYPHYKNSN-- 311
Cdd:cd05940 236 FINF--FGKPGAIGRNPSLLRKvaplalvkydlesgepirdaEGRCIKVPRGEPGLLIsrINPLEPFDGYTDPAATEKki 313
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 428688192 312 ----------YFLTDDLGYFDQDNFLHIVGRNSQKIISGGENVYPCEIENVVIKTGLVKDIVVVG 366
Cdd:cd05940 314 lrdvfkkgdaWFNTGDLMRLDGEGFWYFVDRLGDTFRWKGENVSTTEVAAVLGAFPGVEEANVYG 378
|
|
| PRK05691 |
PRK05691 |
peptide synthase; Validated |
315-428 |
8.82e-05 |
|
peptide synthase; Validated
Pssm-ID: 235564 [Multi-domain] Cd Length: 4334 Bit Score: 45.16 E-value: 8.82e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 428688192 315 TDDLGYFDQDNFLHIVGRNSQKIISGGENVYPCEIENVVIKTGLVKDIVVVGKNDHYWGQIIcAVYVAISGYDTEYLvnN 394
Cdd:PRK05691 1509 TGDRARWNADGALEYLGRLDQQVKLRGFRVEPEEIQARLLAQPGVAQAAVLVREGAAGAQLV-GYYTGEAGQEAEAE--R 1585
|
90 100 110
....*....|....*....|....*....|....
gi 428688192 395 IKAKLRSHLSHYKIPKLWLKVDQIPRNPQGKIDY 428
Cdd:PRK05691 1586 LKAALAAELPEYMVPAQLIRLDQMPLGPSGKLDR 1619
|
|
| PTZ00237 |
PTZ00237 |
acetyl-CoA synthetase; Provisional |
112-439 |
1.09e-04 |
|
acetyl-CoA synthetase; Provisional
Pssm-ID: 240325 [Multi-domain] Cd Length: 647 Bit Score: 44.73 E-value: 1.09e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 428688192 112 MIPTGGTSGNIKFAIHTwetlNASA-KGFSQFWQRRKINFFCCLPLYHVS-----------GLMQIVRTFVT--GGSLAI 177
Cdd:PTZ00237 259 ILYTSGTTGNSKAVVRS----NGPHlVGLKYYWRSIIEKDIPTVVFSHSSigwvsfhgflyGSLSLGNTFVMfeGGIIKN 334
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 428688192 178 YDYSL-LKKEIQNHNYDNFFISlvPTQLNFLLENFPDW--------LKKFETVLVGGSATPKTLlQNCYRQKINLALTYG 248
Cdd:PTZ00237 335 KHIEDdLWNTIEKHKVTHTLTL--PKTIRYLIKTDPEAtiirskydLSNLKEIWCGGEVIEESI-PEYIENKLKIKSSRG 411
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 428688192 249 MTETASGVTIL--------------KPENFFKG--INNSGHLLPHSQI---VIK------------KNQAKFGQIIIKsd 297
Cdd:PTZ00237 412 YGQTEIGITYLycyghinipynatgVPSIFIKPsiLSEDGKELNVNEIgevAFKlpmppsfattfyKNDEKFKQLFSK-- 489
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 428688192 298 slFKGYYphykNSNyfltdDLGYFDQDNFLHIVGRNSQKIISGGENVYPCEIENVVIKTGLVKDIVVVGKNDHYWGQIIC 377
Cdd:PTZ00237 490 --FPGYY----NSG-----DLGFKDENGYYTIVSRSDDQIKISGNKVQLNTIETSILKHPLVLECCSIGIYDPDCYNVPI 558
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 428688192 378 AVYV-----AISGYDTEYLVNNIKAKLRSHLSHYKIPKLWLKVDQIPRNPQGKIDYGYLEKMLTMDN 439
Cdd:PTZ00237 559 GLLVlkqdqSNQSIDLNKLKNEINNIITQDIESLAVLRKIIIVNQLPKTKTGKIPRQIISKFLNDSN 625
|
|
| AA-adenyl-dom |
TIGR01733 |
amino acid adenylation domain; This model represents a domain responsible for the specific ... |
162-364 |
1.18e-04 |
|
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: 44.18 E-value: 1.18e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 428688192 162 LMQIVRTFVTGGSLAIYDYSLLKKEIQNHNY--DNFFIS---LVPTQLNFLLENFPDWLKKFETVLVGGSATPKTLLQNC 236
Cdd:TIGR01733 176 VEEIFGALLAGATLVVPPEDEERDDAALLAAliAEHPVTvlnLTPSLLALLAAALPPALASLRLVILGGEALTPALVDRW 255
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 428688192 237 YRQKINLAL--TYGMTETASGVTIL---KPENFFKGINNSGHLLPHSQIVIKKNQAKF------GQIIIKSDSLFKGYY- 304
Cdd:TIGR01733 256 RARGPGARLinLYGPTETTVWSTATlvdPDDAPRESPVPIGRPLANTRLYVLDDDLRPvpvgvvGELYIGGPGVARGYLn 335
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 428688192 305 ------------PHYKNSNYFL--TDDLGYFDQDNFLHIVGRN-SQ-KIisGGENVYPCEIENVVIKTGLVKDIVV 364
Cdd:TIGR01733 336 rpeltaerfvpdPFAGGDGARLyrTGDLVRYLPDGNLEFLGRIdDQvKI--RGYRIELGEIEAALLRHPGVREAVV 409
|
|
| PRK07768 |
PRK07768 |
long-chain-fatty-acid--CoA ligase; Validated |
268-350 |
1.40e-04 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236091 [Multi-domain] Cd Length: 545 Bit Score: 44.22 E-value: 1.40e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 428688192 268 INNSGHLLPHSQIvikknqakfGQIIIKSDSLFKGYY------PHYKNSNYFLTDDLGYFDQDNFLHIVGRNSQKIISGG 341
Cdd:PRK07768 374 VDEDGQVLPPRGV---------GVIELRGESVTPGYLtmdgfiPAQDADGWLDTGDLGYLTEEGEVVVCGRVKDVIIMAG 444
|
....*....
gi 428688192 342 ENVYPCEIE 350
Cdd:PRK07768 445 RNIYPTDIE 453
|
|
| EntF |
COG1020 |
EntF, seryl-AMP synthase component of non-ribosomal peptide synthetase [Secondary metabolites ... |
164-258 |
2.95e-04 |
|
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: 43.31 E-value: 2.95e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 428688192 164 QIVRTFVTGGSLAIYDYS------LLKKEIQNHNYDnfFISLVPTQLNFLLENFPDWLKKFETVLVGGSATPKTLLQNCY 237
Cdd:COG1020 675 EIFGALLSGATLVLAPPEarrdpaALAELLARHRVT--VLNLTPSLLRALLDAAPEALPSLRLVLVGGEALPPELVRRWR 752
|
90 100
....*....|....*....|...
gi 428688192 238 RQKINLAL--TYGMTETASGVTI 258
Cdd:COG1020 753 ARLPGARLvnLYGPTETTVDSTY 775
|
|
| PRK13388 |
PRK13388 |
acyl-CoA synthetase; Provisional |
300-382 |
5.22e-04 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 237374 [Multi-domain] Cd Length: 540 Bit Score: 42.32 E-value: 5.22e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 428688192 300 FKGYYphyKNSN---------YFLTDDLGYFDQDNFLHIVGRNSQKIISGGENVYPCEIENVVIKTGLVKDIVVVGKNDH 370
Cdd:PRK13388 363 FEGYY---NNPEataermrhgMYWSGDLAYRDADGWIYFAGRTADWMRVDGENLSAAPIERILLRHPAINRVAVYAVPDE 439
|
90
....*....|...
gi 428688192 371 YWG-QIICAVYVA 382
Cdd:PRK13388 440 RVGdQVMAALVLR 452
|
|
| FAAL |
cd05931 |
Fatty acyl-AMP ligase (FAAL); FAAL belongs to the class I adenylate forming enzyme family and ... |
290-353 |
6.06e-04 |
|
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: 42.23 E-value: 6.06e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 428688192 290 GQIIIKSDSLFKGYY-------------PHYKNSNYFLTDDLGYFDQDNfLHIVGRNSQKIISGGENVYPCEIENVV 353
Cdd:cd05931 383 GEIWVRGPSVASGYWgrpeataetfgalAATDEGGWLRTGDLGFLHDGE-LYITGRLKDLIIVRGRNHYPQDIEATA 458
|
|
| PLN02430 |
PLN02430 |
long-chain-fatty-acid-CoA ligase |
247-366 |
6.83e-04 |
|
long-chain-fatty-acid-CoA ligase
Pssm-ID: 178049 [Multi-domain] Cd Length: 660 Bit Score: 42.11 E-value: 6.83e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 428688192 247 YGMTETASGVTILKPENFFKgINNSGHLLPHSQIVIKK---------NQAKFGQIIIKSDSLFKGYY--PHYKNS----N 311
Cdd:PLN02430 415 YGLTETLGPTTLGFPDEMCM-LGTVGAPAVYNELRLEEvpemgydplGEPPRGEICVRGKCLFSGYYknPELTEEvmkdG 493
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*.
gi 428688192 312 YFLTDDLGYFDQDNFLHIVGRNSQKI-ISGGENVYPCEIENVVIKTGLVKDIVVVG 366
Cdd:PLN02430 494 WFHTGDIGEILPNGVLKIIDRKKNLIkLSQGEYVALEYLENVYGQNPIVEDIWVYG 549
|
|
| MACS_like_1 |
cd05974 |
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the ... |
247-426 |
1.44e-03 |
|
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: 40.63 E-value: 1.44e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 428688192 247 YGMTETASGVTILKPENFFKGinNSGHLLPHSQIVI---KKNQAKFGQIIIK-SDS----LFKGYY------PHYKNSNY 312
Cdd:cd05974 232 YGQTETTALVGNSPGQPVKAG--SMGRPLPGYRVALldpDGAPATEGEVALDlGDTrpvgLMKGYAgdpdktAHAMRGGY 309
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 428688192 313 FLTDDLGYFDQDNFLHIVGRNSQKIISGGENVYPCEIENVVIKTGLVKDIVVVGKNDHYWGQIICAVYVAISGYD-TEYL 391
Cdd:cd05974 310 YRTGDIAMRDEDGYLTYVGRADDVFKSSDYRISPFELESVLIEHPAVAEAAVVPSPDPVRLSVPKAFIVLRAGYEpSPET 389
|
170 180 190
....*....|....*....|....*....|....*
gi 428688192 392 VNNIKAKLRSHLSHYKIPKLwLKVDQIPRNPQGKI 426
Cdd:cd05974 390 ALEIFRFSRERLAPYKRIRR-LEFAELPKTISGKI 423
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|
| A_NRPS_alphaAR |
cd17647 |
Alpha-aminoadipate reductase; This family contains L-2-aminoadipate reductase, also known as ... |
391-427 |
2.17e-03 |
|
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: 40.19 E-value: 2.17e-03
10 20 30
....*....|....*....|....*....|....*..
gi 428688192 391 LVNNIKAKLRSHLSHYKIPKLWLKVDQIPRNPQGKID 427
Cdd:cd17647 477 LIKDIREFLKKRLASYAIPSLIVVLDKLPLNPNGKVD 513
|
|
| alpha_am_amid |
TIGR03443 |
L-aminoadipate-semialdehyde dehydrogenase; Members of this protein family are ... |
391-427 |
5.08e-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: 39.28 E-value: 5.08e-03
10 20 30
....*....|....*....|....*....|....*..
gi 428688192 391 LVNNIKAKLRSHLSHYKIPKLWLKVDQIPRNPQGKID 427
Cdd:TIGR03443 782 LIKDIREYLKKKLPSYAIPTVIVPLKKLPLNPNGKVD 818
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