|
Name |
Accession |
Description |
Interval |
E-value |
| EntF |
COG1020 |
EntF, seryl-AMP synthase component of non-ribosomal peptide synthetase [Secondary metabolites ... |
1-303 |
7.95e-111 |
|
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: 349.16 E-value: 7.95e-111
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 758185221 1 AAFLPIDPDTPEERIRYSLEDSGAKFAVVNERNMTAIGQYEGTIVSLDDGKWRNESKERPSSISGSRNLAYVIYTSGTAG 80
Cdd:COG1020 551 AAYVPLDPAYPAERLAYMLEDAGARLVLTQSALAARLPELGVPVLALDALALAAEPATNPPVPVTPDDLAYVIYTSGSTG 630
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 758185221 81 KPKGVQIEHRNLTNYVSWFSEEASLTENDKTVLLSSYASDLGYTSMFPVLLGGGELHIVQKETYTAPDEIAHYIKEYGIT 160
Cdd:COG1020 631 RPKGVMVEHRALVNLLAWMQRRYGLGPGDRVLQFASLSFDASVWEIFGALLSGATLVLAPPEARRDPAALAELLARHRVT 710
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 758185221 161 YIKLTPSLFHTIVNTASfakdANFESLRLIVLGGEKIIPTDVLAFRKIYGHTEFINHYGPTEATIGAIAGRVDlsEPDAF 240
Cdd:COG1020 711 VLNLTPSLLRALLDAAP----EALPSLRLVLVGGEALPPELVRRWRARLPGARLVNLYGPTETTVDSTYYEVT--PPDAD 784
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 758185221 241 AKRPTIGRPIANAGALVLNEALKLVPPGASGQLYITGQGLARGYLNRPQLTAERFVENPYS-PG 303
Cdd:COG1020 785 GGSVPIGRPIANTRVYVLDAHLQPVPVGVPGELYIGGAGLARGYLNRPELTAERFVADPFGfPG 848
|
|
| A_NRPS |
cd05930 |
The adenylation domain of nonribosomal peptide synthetases (NRPS); The adenylation (A) domain ... |
1-303 |
2.62e-108 |
|
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: 321.78 E-value: 2.62e-108
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 758185221 1 AAFLPIDPDTPEERIRYSLEDSGAKFAVVNernmtaigqyegtivslddgkwrneskerpssisgSRNLAYVIYTSGTAG 80
Cdd:cd05930 62 AAYVPLDPSYPAERLAYILEDSGAKLVLTD-----------------------------------PDDLAYVIYTSGSTG 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 758185221 81 KPKGVQIEHRNLTNYVSWFSEEASLTENDKTVLLSSYASDLGYTSMFPVLLGGGELHIVQKETYTAPDEIAHYIKEYGIT 160
Cdd:cd05930 107 KPKGVMVEHRGLVNLLLWMQEAYPLTPGDRVLQFTSFSFDVSVWEIFGALLAGATLVVLPEEVRKDPEALADLLAEEGIT 186
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 758185221 161 YIKLTPSLFHTIVNTASfakDANFESLRLIVLGGEKIIPTDVLAFRKIYGHTEFINHYGPTEATIGAIAGRVDlsEPDAF 240
Cdd:cd05930 187 VLHLTPSLLRLLLQELE---LAALPSLRLVLVGGEALPPDLVRRWRELLPGARLVNLYGPTEATVDATYYRVP--PDDEE 261
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 758185221 241 AKRPTIGRPIANAGALVLNEALKLVPPGASGQLYITGQGLARGYLNRPQLTAERFVENPYSPG 303
Cdd:cd05930 262 DGRVPIGRPIPNTRVYVLDENLRPVPPGVPGELYIGGAGLARGYLNRPELTAERFVPNPFGPG 324
|
|
| AA-adenyl-dom |
TIGR01733 |
amino acid adenylation domain; This model represents a domain responsible for the specific ... |
1-303 |
4.33e-102 |
|
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: 304.57 E-value: 4.33e-102
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 758185221 1 AAFLPIDPDTPEERIRYSLEDSGAKFAVVNERNMTAIGQYEGTIVSLD----DGKWRNESKERPSSISGSRNLAYVIYTS 76
Cdd:TIGR01733 50 AAYVPLDPAYPAERLAFILEDAGARLLLTDSALASRLAGLVLPVILLDplelAALDDAPAPPPPDAPSGPDDLAYVIYTS 129
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 758185221 77 GTAGKPKGVQIEHRNLTNYVSWFSEEASLTENDKTVLLSSYASDLGYTSMFPVLLGGGEL-HIVQKETYTAPDEIAHYIK 155
Cdd:TIGR01733 130 GSTGRPKGVVVTHRSLVNLLAWLARRYGLDPDDRVLQFASLSFDASVEEIFGALLAGATLvVPPEDEERDDAALLAALIA 209
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 758185221 156 EYGITYIKLTPSLFHTIVNtasfAKDANFESLRLIVLGGEKIIPTDVLAFRKIYGHTEFINHYGPTEATIGAIAGRVDLS 235
Cdd:TIGR01733 210 EHPVTVLNLTPSLLALLAA----ALPPALASLRLVILGGEALTPALVDRWRARGPGARLINLYGPTETTVWSTATLVDPD 285
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 758185221 236 EPDAFAKRPtIGRPIANAGALVLNEALKLVPPGASGQLYITGQGLARGYLNRPQLTAERFVENPYSPG 303
Cdd:TIGR01733 286 DAPRESPVP-IGRPLANTRLYVLDDDLRPVPVGVVGELYIGGPGVARGYLNRPELTAERFVPDPFAGG 352
|
|
| A_NRPS_Bac |
cd17655 |
bacitracin synthetase and related proteins; This family of the adenylation (A) domain of ... |
1-303 |
5.45e-91 |
|
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: 278.83 E-value: 5.45e-91
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 758185221 1 AAFLPIDPDTPEERIRYSLEDSGAKFaVVNERNMTAIGQYEGTIVSLDDGKWRNESKERPSSISGSRNLAYVIYTSGTAG 80
Cdd:cd17655 72 GAYLPIDPDYPEERIQYILEDSGADI-LLTQSHLQPPIAFIGLIDLLDEDTIYHEESENLEPVSKSDDLAYVIYTSGSTG 150
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 758185221 81 KPKGVQIEHRNLTNYVSWFSEEASLTENDKTVLLSSYASDLGYTSMFPVLLGGGELHIVQKETYTAPDEIAHYIKEYGIT 160
Cdd:cd17655 151 KPKGVMIEHRGVVNLVEWANKVIYQGEHLRVALFASISFDASVTEIFASLLSGNTLYIVRKETVLDGQALTQYIRQNRIT 230
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 758185221 161 YIKLTPSLFHTIVntasFAKDANFESLRLIVLGGEKIIPTDVLAFRKIYGHT-EFINHYGPTEATIGAIAGRVDLSepDA 239
Cdd:cd17655 231 IIDLTPAHLKLLD----AADDSEGLSLKHLIVGGEALSTELAKKIIELFGTNpTITNAYGPTETTVDASIYQYEPE--TD 304
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 758185221 240 FAKRPTIGRPIANAGALVLNEALKLVPPGASGQLYITGQGLARGYLNRPQLTAERFVENPYSPG 303
Cdd:cd17655 305 QQVSVPIGKPLGNTRIYILDQYGRPQPVGVAGELYIGGEGVARGYLNRPELTAEKFVDDPFVPG 368
|
|
| A_NRPS_Srf_like |
cd12117 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including Bacillus subtilis ... |
1-303 |
7.78e-83 |
|
The adenylation domain of nonribosomal peptide synthetases (NRPS), including Bacillus subtilis termination module Surfactin (SrfA-C); The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and, in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions. This family includes the adenylation domain of the Bacillus subtilis termination module (Surfactin domain, SrfA-C) which recognizes a specific amino acid building block, which is then activated and transferred to the terminal thiol of the 4'-phosphopantetheine (Ppan) arm of the downstream peptidyl carrier protein (PCP) domain.
Pssm-ID: 341282 [Multi-domain] Cd Length: 483 Bit Score: 257.90 E-value: 7.78e-83
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 758185221 1 AAFLPIDPDTPEERIRYSLEDSGAKFAVVNERNMTAIGQYEGTIVSLDDgkWRNESKERPSSISGSRNLAYVIYTSGTAG 80
Cdd:cd12117 72 AAYVPLDPELPAERLAFMLADAGAKVLLTDRSLAGRAGGLEVAVVIDEA--LDAGPAGNPAVPVSPDDLAYVMYTSGSTG 149
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 758185221 81 KPKGVQIEHRNLTNYV--SWFseeASLTENDKTVLLSSYASDLGYTSMFPVLLGGGELHIVQKETYTAPDEIAHYIKEYG 158
Cdd:cd12117 150 RPKGVAVTHRGVVRLVknTNY---VTLGPDDRVLQTSPLAFDASTFEIWGALLNGARLVLAPKGTLLDPDALGALIAEEG 226
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 758185221 159 ITYIKLTPSLFHTIVNTASFAkdanFESLRLIVLGGEKIIPTDVLAFRKIYGHTEFINHYGPTEATIGAIAGRVDlsEPD 238
Cdd:cd12117 227 VTVLWLTAALFNQLADEDPEC----FAGLRELLTGGEVVSPPHVRRVLAACPGLRLVNGYGPTENTTFTTSHVVT--ELD 300
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 758185221 239 AFAKRPTIGRPIANAGALVLNEALKLVPPGASGQLYITGQGLARGYLNRPQLTAERFVENPYSPG 303
Cdd:cd12117 301 EVAGSIPIGRPIANTRVYVLDEDGRPVPPGVPGELYVGGDGLALGYLNRPALTAERFVADPFGPG 365
|
|
| A_NRPS_VisG_like |
cd17651 |
similar to adenylation domain of virginiamycin S synthetase; This family of the adenylation (A) ... |
1-303 |
5.25e-75 |
|
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: 237.63 E-value: 5.25e-75
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 758185221 1 AAFLPIDPDTPEERIRYSLEDSGAKFAVVNERNMTAIGQYEGTIVSLDDGKWRNESKERPSSISGSRNLAYVIYTSGTAG 80
Cdd:cd17651 70 AAYVPLDPAYPAERLAFMLADAGPVLVLTHPALAGELAVELVAVTLLDQPGAAAGADAEPDPALDADDLAYVIYTSGSTG 149
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 758185221 81 KPKGVQIEHRNLTNYVSWFSEEASLTENDKTVLLSSYASDLGYTSMFPVLLGGGELHIVQKETYTAPDEIAHYIKEYGIT 160
Cdd:cd17651 150 RPKGVVMPHRSLANLVAWQARASSLGPGARTLQFAGLGFDVSVQEIFSTLCAGATLVLPPEEVRTDPPALAAWLDEQRIS 229
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 758185221 161 YIKLTPSLFHTIVNtASFAKDANFESLRLIVLGGEKIIPT-DVLAFRKIYGHTEFINHYGPTEATIgAIAGRVDlSEPDA 239
Cdd:cd17651 230 RVFLPTVALRALAE-HGRPLGVRLAALRYLLTGGEQLVLTeDLREFCAGLPGLRLHNHYGPTETHV-VTALSLP-GDPAA 306
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 758185221 240 FAKRPTIGRPIANAGALVLNEALKLVPPGASGQLYITGQGLARGYLNRPQLTAERFVENPYSPG 303
Cdd:cd17651 307 WPAPPPIGRPIDNTRVYVLDAALRPVPPGVPGELYIGGAGLARGYLNRPELTAERFVPDPFVPG 370
|
|
| AMP-binding |
pfam00501 |
AMP-binding enzyme; |
1-300 |
1.06e-74 |
|
AMP-binding enzyme;
Pssm-ID: 459834 [Multi-domain] Cd Length: 417 Bit Score: 234.90 E-value: 1.06e-74
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 758185221 1 AAFLPIDPDTPEERIRYSLEDSGAKFAVVNERNM-------TAIGQYEGTIVSLDDGKWRNE-----------SKERPSS 62
Cdd:pfam00501 71 AVYVPLNPRLPAEELAYILEDSGAKVLITDDALKleelleaLGKLEVVKLVLVLDRDPVLKEeplpeeakpadVPPPPPP 150
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 758185221 63 ISGSRNLAYVIYTSGTAGKPKGVQIEHRNLTNYVSWFSEEA----SLTENDKTVLLSSYASDLGYTS-MFPVLLGGGELH 137
Cdd:pfam00501 151 PPDPDDLAYIIYTSGTTGKPKGVMLTHRNLVANVLSIKRVRprgfGLGPDDRVLSTLPLFHDFGLSLgLLGPLLAGATVV 230
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 758185221 138 IVQKETYTAPDEIAHYIKEYGITYIKLTPSLFHTIVNtASFAKDANFESLRLIVLGGEKIIPTDVLAFRKIYGHtEFINH 217
Cdd:pfam00501 231 LPPGFPALDPAALLELIERYKVTVLYGVPTLLNMLLE-AGAPKRALLSSLRLVLSGGAPLPPELARRFRELFGG-ALVNG 308
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 758185221 218 YGPTEATIGAIagrVDLSEPDAFAKRPTIGRPIANAGALVLNEA-LKLVPPGASGQLYITGQGLARGYLNRPQLTAERFV 296
Cdd:pfam00501 309 YGLTETTGVVT---TPLPLDEDLRSLGSVGRPLPGTEVKIVDDEtGEPVPPGEPGELCVRGPGVMKGYLNDPELTAEAFD 385
|
....
gi 758185221 297 ENPY 300
Cdd:pfam00501 386 EDGW 389
|
|
| A_NRPS_ApnA-like |
cd17644 |
similar to adenylation domain of anabaenopeptin synthetase (ApnA); This family of the ... |
1-300 |
1.54e-73 |
|
similar to adenylation domain of anabaenopeptin synthetase (ApnA); This family of the adenylation (A) domain of nonribosomal peptide synthases (NRPS) includes Planktothrix agardhii anabaenopeptin synthetase (ApnA A1), which is capable of activating two chemically distinct amino acids (Arg and Tyr). Structural studies show that the architecture of the active site forces Arg to adopt a Tyr-like conformation, thus explaining the bispecificity. The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester bond to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.
Pssm-ID: 341299 [Multi-domain] Cd Length: 465 Bit Score: 233.10 E-value: 1.54e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 758185221 1 AAFLPIDPDTPEERIRYSLEDSGAKFAVVNERNmtaigqyegtivslddgkwrneskerpssisgsrnLAYVIYTSGTAG 80
Cdd:cd17644 75 GAYVPLDPNYPQERLTYILEDAQISVLLTQPEN-----------------------------------LAYVIYTSGSTG 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 758185221 81 KPKGVQIEHRNLTNYVSWFSEEASLTENDKTVLLSSYASDLGYTSMFPVLLGGGELHIVQKETYTAPDEIAHYIKEYGIT 160
Cdd:cd17644 120 KPKGVMIEHQSLVNLSHGLIKEYGITSSDRVLQFASIAFDVAAEEIYVTLLSGATLVLRPEEMRSSLEDFVQYIQQWQLT 199
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 758185221 161 YIKLTPSLFHTIVNTASFAKDANFESLRLIVLGGEKIIPTDVLAFRKIYGH-TEFINHYGPTEATIGAIAGRVdLSEPDA 239
Cdd:cd17644 200 VLSLPPAYWHLLVLELLLSTIDLPSSLRLVIVGGEAVQPELVRQWQKNVGNfIQLINVYGPTEATIAATVCRL-TQLTER 278
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 758185221 240 FAKRPTIGRPIANAGALVLNEALKLVPPGASGQLYITGQGLARGYLNRPQLTAERFVENPY 300
Cdd:cd17644 279 NITSVPIGRPIANTQVYILDENLQPVPVGVPGELHIGGVGLARGYLNRPELTAEKFISHPF 339
|
|
| A_NRPS_AB3403-like |
cd17646 |
Peptide Synthetase; The adenylation (A) domain of NRPS recognizes a specific amino acid or ... |
1-303 |
3.19e-73 |
|
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: 232.94 E-value: 3.19e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 758185221 1 AAFLPIDPDTPEERIRYSLEDSGAKFaVVNERNMTAIGQYEGTIVSLDDGKWRNESKERPSSISGSRNLAYVIYTSGTAG 80
Cdd:cd17646 73 AAYLPLDPGYPADRLAYMLADAGPAV-VLTTADLAARLPAGGDVALLGDEALAAPPATPPLVPPRPDNLAYVIYTSGSTG 151
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 758185221 81 KPKGVQIEHRNLTNYVSWFSEEASLTENDKTVLLSSYASDLGYTSMFPVLLGGGELHIVQKETYTAPDEIAHYIKEYGIT 160
Cdd:cd17646 152 RPKGVMVTHAGIVNRLLWMQDEYPLGPGDRVLQKTPLSFDVSVWELFWPLVAGARLVVARPGGHRDPAYLAALIREHGVT 231
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 758185221 161 YIKLTPSLFHTIVNTASFAKDAnfeSLRLIVLGGEKIiPTDVLA-FRKIyGHTEFINHYGPTEATIGAIAGRVDlsePDA 239
Cdd:cd17646 232 TCHFVPSMLRVFLAEPAAGSCA---SLRRVFCSGEAL-PPELAArFLAL-PGAELHNLYGPTEAAIDVTHWPVR---GPA 303
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 758185221 240 FAKRPTIGRPIANAGALVLNEALKLVPPGASGQLYITGQGLARGYLNRPQLTAERFVENPYSPG 303
Cdd:cd17646 304 ETPSVPIGRPVPNTRLYVLDDALRPVPVGVPGELYLGGVQLARGYLGRPALTAERFVPDPFGPG 367
|
|
| PRK12467 |
PRK12467 |
peptide synthase; Provisional |
1-302 |
5.36e-73 |
|
peptide synthase; Provisional
Pssm-ID: 237108 [Multi-domain] Cd Length: 3956 Bit Score: 244.30 E-value: 5.36e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 758185221 1 AAFLPIDPDTPEERIRYSLEDSGAKFAVVNERNMTAIGQYEG-TIVSLDDG--KWRNESKERPSSISGSRNLAYVIYTSG 77
Cdd:PRK12467 587 GAYVPLDPEYPQDRLAYMLDDSGVRLLLTQSHLLAQLPVPAGlRSLCLDEPadLLCGYSGHNPEVALDPDNLAYVIYTSG 666
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 758185221 78 TAGKPKGVQIEHRNLTNYVSWFSEEASLTENDKTVLLSSYASDLGYTSMFPVLLGGGELHIVQKETYTAPDEIAHYIKEY 157
Cdd:PRK12467 667 STGQPKGVAISHGALANYVCVIAERLQLAADDSMLMVSTFAFDLGVTELFGALASGATLHLLPPDCARDAEAFAALMADQ 746
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 758185221 158 GITYIKLTPSLFHTIVNTASFAKDanfESLRLIVLGGEkIIPTDVLA-FRKIYGHTEFINHYGPTEATIGAIAGrvDLSE 236
Cdd:PRK12467 747 GVTVLKIVPSHLQALLQASRVALP---RPQRALVCGGE-ALQVDLLArVRALGPGARLINHYGPTETTVGVSTY--ELSD 820
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 758185221 237 PDAFAKRPTIGRPIANAGALVLNEALKLVPPGASGQLYITGQGLARGYLNRPQLTAERFVENPYSP 302
Cdd:PRK12467 821 EERDFGNVPIGQPLANLGLYILDHYLNPVPVGVVGELYIGGAGLARGYHRRPALTAERFVPDPFGA 886
|
|
| A_NRPS_Ta1_like |
cd12116 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including salinosporamide A ... |
1-303 |
5.82e-71 |
|
The adenylation domain of nonribosomal peptide synthetases (NRPS), including salinosporamide A polyketide synthase; The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions. This family includes the myxovirescin (TA) antibiotic biosynthetic gene in Myxococcus xanthus; TA production plays a role in predation. It also includes the salinosporamide A polyketide synthase which is involved in the biosynthesis of salinosporamide A, a marine microbial metabolite whose chlorine atom is crucial for potent proteasome inhibition and anticancer activity.
Pssm-ID: 341281 [Multi-domain] Cd Length: 470 Bit Score: 226.79 E-value: 5.82e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 758185221 1 AAFLPIDPDTPEERIRYSLEDSGAKFAVVNERNMTAigqYEGTIVSLDDGKWRNE-SKERPSSISGSRNLAYVIYTSGTA 79
Cdd:cd12116 62 AAYVPLDPDYPADRLRYILEDAEPALVLTDDALPDR---LPAGLPVLLLALAAAAaAPAAPRTPVSPDDLAYVIYTSGST 138
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 758185221 80 GKPKGVQIEHRNLTNYVSWFSEEASLTENDKTVLLSSYASDLGYTSMFPVLLGGGELHIVQKETYTAPDEIAHYIKEYGI 159
Cdd:cd12116 139 GRPKGVVVSHRNLVNFLHSMRERLGLGPGDRLLAVTTYAFDISLLELLLPLLAGARVVIAPRETQRDPEALARLIEAHSI 218
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 758185221 160 TYIKLTPSLFHTIVNTASFAKdanfESLRLIVlGGEKIIPTdvLAFRKIYGHTEFINHYGPTEATIGAIAGRVDLSepda 239
Cdd:cd12116 219 TVMQATPATWRMLLDAGWQGR----AGLTALC-GGEALPPD--LAARLLSRVGSLWNLYGPTETTIWSTAARVTAA---- 287
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 758185221 240 fAKRPTIGRPIANAGALVLNEALKLVPPGASGQLYITGQGLARGYLNRPQLTAERFVENPYSPG 303
Cdd:cd12116 288 -AGPIPIGRPLANTQVYVLDAALRPVPPGVPGELYIGGDGVAQGYLGRPALTAERFVPDPFAGP 350
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
2-303 |
7.92e-70 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 235.24 E-value: 7.92e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 758185221 2 AFLPIDPDTPEERIRYSLEDSGAKFAVVNERNMTAIGQYEGT-IVSLDD-GKW-RNESKERPSSISGSRNLAYVIYTSGT 78
Cdd:PRK12316 587 AYVPLDPEYPAERLAYMLEDSGVQLLLSQSHLGRKLPLAAGVqVLDLDRpAAWlEGYSEENPGTELNPENLAYVIYTSGS 666
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 758185221 79 AGKPKGVQIEHRNLTNYVSWFSEEASLTENDKTVLLSSYASDLGYTSMFPVLLGGGELHIVQKETYTAPDEIAHYIKEYG 158
Cdd:PRK12316 667 TGKPKGAGNRHRALSNRLCWMQQAYGLGVGDTVLQKTPFSFDVSVWEFFWPLMSGARLVVAAPGDHRDPAKLVELINREG 746
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 758185221 159 ITYIKLTPSLFHTIVNtasFAKDANFESLRLIVLGGEKIIPTDVLAFRKIYGHTEFINHYGPTEATIGAiagrVDLSEPD 238
Cdd:PRK12316 747 VDTLHFVPSMLQAFLQ---DEDVASCTSLRRIVCSGEALPADAQEQVFAKLPQAGLYNLYGPTEAAIDV----THWTCVE 819
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 758185221 239 AFAKRPTIGRPIANAGALVLNEALKLVPPGASGQLYITGQGLARGYLNRPQLTAERFVENPYSPG 303
Cdd:PRK12316 820 EGGDSVPIGRPIANLACYILDANLEPVPVGVLGELYLAGRGLARGYHGRPGLTAERFVPSPFVAG 884
|
|
| A_NRPS_PvdJ-like |
cd17649 |
non-ribosomal peptide synthetase; This family of the adenylation (A) domain of nonribosomal ... |
1-303 |
4.71e-68 |
|
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: 218.78 E-value: 4.71e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 758185221 1 AAFLPIDPDTPEERIRYSLEDSGAKfavvnernmTAIGQyegtivslddgkwrneskerpssisGSRNLAYVIYTSGTAG 80
Cdd:cd17649 62 GAYVPLDPEYPAERLRYMLEDSGAG---------LLLTH-------------------------HPRQLAYVIYTSGSTG 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 758185221 81 KPKGVQIEHRNLTNYVSWFSEEASLTENDKTVLLSSYASDLGYTSMFPVLLGGGELHIVQKETYTAPDEIAHYIKEYGIT 160
Cdd:cd17649 108 TPKGVAVSHGPLAAHCQATAERYGLTPGDRELQFASFNFDGAHEQLLPPLICGACVVLRPDELWASADELAEMVRELGVT 187
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 758185221 161 YIKLTPSLFHTIVNTASFAKDANFESLRLIVLGGEKIIPTDVLAFRKIygHTEFINHYGPTEATIGAIAGRVDLSEPDAF 240
Cdd:cd17649 188 VLDLPPAYLQQLAEEADRTGDGRPPSLRLYIFGGEALSPELLRRWLKA--PVRLFNAYGPTEATVTPLVWKCEAGAARAG 265
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 758185221 241 AKRPtIGRPIANAGALVLNEALKLVPPGASGQLYITGQGLARGYLNRPQLTAERFVENPYS-PG 303
Cdd:cd17649 266 ASMP-IGRPLGGRSAYILDADLNPVPVGVTGELYIGGEGLARGYLGRPELTAERFVPDPFGaPG 328
|
|
| A_NRPS_CmdD_like |
cd17652 |
similar to adenylation domain of chondramide synthase cmdD; This family of the adenylation (A) ... |
1-302 |
4.17e-67 |
|
similar to adenylation domain of chondramide synthase cmdD; This family of the adenylation (A) domain of nonribosomal peptide synthases (NRPS) includes phosphinothricin tripeptide (PTT, phosphinothricylalanylalanine) synthetase, where PTT is a natural-product antibiotic and potent herbicide that is produced by Streptomyces hygroscopicus. This adenylation domain has been confirmed to directly activate beta-tyrosine, and fluorinated chondramides are produced through precursor-directed biosynthesis. Also included in this family is chondramide synthase D (also known as ATP-dependent phenylalanine adenylase or phenylalanine activase or tyrosine activase). Chondramides A-D are depsipeptide antitumor and antifungal antibiotics produced by C. crocatus, are a class of mixed peptide/polyketide depsipeptides comprised of three amino acids (alanine, N-methyltryptophan, plus the unusual amino acid beta-tyrosine or alpha-methoxy-beta-tyrosine) and a polyketide chain ([E]-7-hydroxy-2,4,6-trimethyloct-4-enoic acid).
Pssm-ID: 341307 [Multi-domain] Cd Length: 436 Bit Score: 215.58 E-value: 4.17e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 758185221 1 AAFLPIDPDTPEERIRYSLEDSGAkfAVVnernmtaigqyegtivslddgkwrneskerpssISGSRNLAYVIYTSGTAG 80
Cdd:cd17652 62 AAYLPLDPAYPAERIAYMLADARP--ALL---------------------------------LTTPDNLAYVIYTSGSTG 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 758185221 81 KPKGVQIEHRNLTNYVSWFSEEASLTENDKTVLLSSYASDLGYTSMFPVLLGGGELHIVQKETYTAPDEIAHYIKEYGIT 160
Cdd:cd17652 107 RPKGVVVTHRGLANLAAAQIAAFDVGPGSRVLQFASPSFDASVWELLMALLAGATLVLAPAEELLPGEPLADLLREHRIT 186
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 758185221 161 YIKLTPSLFHTIvntasfaKDANFESLRLIVLGGEKIIPTdvLAFRKIYGHTeFINHYGPTEATIGAIagrvdLSEPDAF 240
Cdd:cd17652 187 HVTLPPAALAAL-------PPDDLPDLRTLVVAGEACPAE--LVDRWAPGRR-MINAYGPTETTVCAT-----MAGPLPG 251
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 758185221 241 AKRPTIGRPIANAGALVLNEALKLVPPGASGQLYITGQGLARGYLNRPQLTAERFVENPYSP 302
Cdd:cd17652 252 GGVPPIGRPVPGTRVYVLDARLRPVPPGVPGELYIAGAGLARGYLNRPGLTAERFVADPFGA 313
|
|
| PRK12467 |
PRK12467 |
peptide synthase; Provisional |
1-301 |
6.01e-67 |
|
peptide synthase; Provisional
Pssm-ID: 237108 [Multi-domain] Cd Length: 3956 Bit Score: 226.97 E-value: 6.01e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 758185221 1 AAFLPIDPDTPEERIRYSLEDSGAKFAVVNERNMTAIGQYEG-TIVSLDDGKWRNESKERPSSISGSRNLAYVIYTSGTA 79
Cdd:PRK12467 3170 GAYVPLDPEYPRERLAYMIEDSGVKLLLTQAHLLEQLPAPAGdTALTLDRLDLNGYSENNPSTRVMGENLAYVIYTSGST 3249
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 758185221 80 GKPKGVQIEHRNLTNYVSWFSEEASLTENDKTVLLSSYASDLGYTSMFPVLLGGGELHIVQKETYTaPDEIAHYIKEYGI 159
Cdd:PRK12467 3250 GKPKGVGVRHGALANHLCWIAEAYELDANDRVLLFMSFSFDGAQERFLWTLICGGCLVVRDNDLWD-PEELWQAIHAHRI 3328
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 758185221 160 TYIKLTPSLFHTIvntASFAKDANFESLRLIVLGGEKIIPTDVLAFRKIYGHTEFINHYGPTEATIGAIAGRVDLSEPDA 239
Cdd:PRK12467 3329 SIACFPPAYLQQF---AEDAGGADCASLDIYVFGGEAVPPAAFEQVKRKLKPRGLTNGYGPTEAVVTVTLWKCGGDAVCE 3405
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 758185221 240 FAKRPtIGRPIANAGALVLNEALKLVPPGASGQLYITGQGLARGYLNRPQLTAERFVENPYS 301
Cdd:PRK12467 3406 APYAP-IGRPVAGRSIYVLDGQLNPVPVGVAGELYIGGVGLARGYHQRPSLTAERFVADPFS 3466
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
1-300 |
1.09e-66 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 225.99 E-value: 1.09e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 758185221 1 AAFLPIDPDTPEERIRYSLEDSGAKFAVVNERNMTAIGQYEGtIVSLD---DGKWRNESKERPSSISGSRNLAYVIYTSG 77
Cdd:PRK12316 4626 GAYVPLDPEYPRERLAYMMEDSGAALLLTQSHLLQRLPIPDG-LASLAldrDEDWEGFPAHDPAVRLHPDNLAYVIYTSG 4704
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 758185221 78 TAGKPKGVQIEHRNLTNYVSWFSEEASLTENDKTVLLSSYASDLGYTSMFPVLLGGGELHIvQKETYTAPDEIAHYIKEY 157
Cdd:PRK12316 4705 STGRPKGVAVSHGSLVNHLHATGERYELTPDDRVLQFMSFSFDGSHEGLYHPLINGASVVI-RDDSLWDPERLYAEIHEH 4783
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 758185221 158 GITYIKLTPSLFHTIVNTAsfAKDANFESLRLIVLGGEKIIPTDV-LAFRKIYgHTEFINHYGPTEATIGAIAGRVDLSE 236
Cdd:PRK12316 4784 RVTVLVFPPVYLQQLAEHA--ERDGEPPSLRVYCFGGEAVAQASYdLAWRALK-PVYLFNGYGPTETTVTVLLWKARDGD 4860
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 758185221 237 PDAFAKRPtIGRPIANAGALVLNEALKLVPPGASGQLYITGQGLARGYLNRPQLTAERFVENPY 300
Cdd:PRK12316 4861 ACGAAYMP-IGTPLGNRSGYVLDGQLNPLPVGVAGELYLGGEGVARGYLERPALTAERFVPDPF 4923
|
|
| A_NRPS_Cytc1-like |
cd17643 |
similar to adenylation domain of cytotrienin synthetase CytC1; This family of the adenylation ... |
1-303 |
2.62e-66 |
|
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: 214.09 E-value: 2.62e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 758185221 1 AAFLPIDPDTPEERIRYSLEDSGAKFAVVnernmtaigqyegtivslddgkwrneskeRPSsisgsrNLAYVIYTSGTAG 80
Cdd:cd17643 62 GAYVPIDPAYPVERIAFILADSGPSLLLT-----------------------------DPD------DLAYVIYTSGSTG 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 758185221 81 KPKGVQIEHRNLTNYVS----WFSeeasLTENDKTVLLSSYASDLGYTSMFPVLLGGGELHIVQKETYTAPDEIAHYIKE 156
Cdd:cd17643 107 RPKGVVVSHANVLALFAatqrWFG----FNEDDVWTLFHSYAFDFSVWEIWGALLHGGRLVVVPYEVARSPEDFARLLRD 182
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 758185221 157 YGITYIKLTPSLFHTIVNTASFAKDANfESLRLIVLGGEKIIPTDVLAFRKIYGH--TEFINHYGPTEATIGAIAGRVDL 234
Cdd:cd17643 183 EGVTVLNQTPSAFYQLVEAADRDGRDP-LALRYVIFGGEALEAAMLRPWAGRFGLdrPQLVNMYGITETTVHVTFRPLDA 261
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 758185221 235 SEPDAFAKRPtIGRPIANAGALVLNEALKLVPPGASGQLYITGQGLARGYLNRPQLTAERFVENPYSPG 303
Cdd:cd17643 262 ADLPAAAASP-IGRPLPGLRVYVLDADGRPVPPGVVGELYVSGAGVARGYLGRPELTAERFVANPFGGP 329
|
|
| PRK12467 |
PRK12467 |
peptide synthase; Provisional |
1-303 |
3.56e-65 |
|
peptide synthase; Provisional
Pssm-ID: 237108 [Multi-domain] Cd Length: 3956 Bit Score: 221.57 E-value: 3.56e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 758185221 1 AAFLPIDPDTPEERIRYSLEDSGAKFAVVNERNMTAIGQYEGT-IVSLD-DGKWR-NESKERPSSISGSRNLAYVIYTSG 77
Cdd:PRK12467 1649 GAYVPLDPEYPRERLAYMIEDSGIELLLTQSHLQARLPLPDGLrSLVLDqEDDWLeGYSDSNPAVNLAPQNLAYVIYTSG 1728
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 758185221 78 TAGKPKGVQIEHRNLTNYVSWFSEEASLTENDKTVLLSSYASDLGYTSMFPVLLGGGELHIVQKETYTAPDEIAHYIKEY 157
Cdd:PRK12467 1729 STGRPKGAGNRHGALVNRLCATQEAYQLSAADVVLQFTSFAFDVSVWELFWPLINGARLVIAPPGAHRDPEQLIQLIERQ 1808
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 758185221 158 GITYIKLTPSLFHTIVNTAsfAKDANFESLRLIVLGGEKiIPTDVL--AFRKIyGHTEFINHYGPTEATIGAIAGRVDLS 235
Cdd:PRK12467 1809 QVTTLHFVPSMLQQLLQMD--EQVEHPLSLRRVVCGGEA-LEVEALrpWLERL-PDTGLFNLYGPTETAVDVTHWTCRRK 1884
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 758185221 236 EPDAFAKRPtIGRPIANAGALVLNEALKLVPPGASGQLYITGQGLARGYLNRPQLTAERFVENPYSPG 303
Cdd:PRK12467 1885 DLEGRDSVP-IGQPIANLSTYILDASLNPVPIGVAGELYLGGVGLARGYLNRPALTAERFVADPFGTV 1951
|
|
| A_NRPS_LgrA-like |
cd17645 |
adenylation (A) domain of linear gramicidin synthetase (LgrA) and similar proteins; This ... |
1-303 |
1.46e-64 |
|
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: 209.33 E-value: 1.46e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 758185221 1 AAFLPIDPDTPEERIRYSLEDSGAKFAvvnernmtaigqyegtivslddgkwrneskerpssISGSRNLAYVIYTSGTAG 80
Cdd:cd17645 73 GAYVPIDPDYPGERIAYMLADSSAKIL-----------------------------------LTNPDDLAYVIYTSGSTG 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 758185221 81 KPKGVQIEHRNLTNYVSWFSEEASLTENDKTVLLSSYASDLGYTSMFPVLLGGGELHIVQKETYTAPDEIAHYIKEYGIT 160
Cdd:cd17645 118 LPKGVMIEHHNLVNLCEWHRPYFGVTPADKSLVYASFSFDASAWEIFPHLTAGAALHVVPSERRLDLDALNDYFNQEGIT 197
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 758185221 161 yIKLTPS----LFHTIVNTasfakdanfeSLRLIVLGGEKIiptdVLAFRKIYghtEFINHYGPTEATIGAIAGRVDLSE 236
Cdd:cd17645 198 -ISFLPTgaaeQFMQLDNQ----------SLRVLLTGGDKL----KKIERKGY---KLVNNYGPTENTVVATSFEIDKPY 259
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 758185221 237 PDAfakrpTIGRPIANAGALVLNEALKLVPPGASGQLYITGQGLARGYLNRPQLTAERFVENPYSPG 303
Cdd:cd17645 260 ANI-----PIGKPIDNTRVYILDEALQLQPIGVAGELCIAGEGLARGYLNRPELTAEKFIVHPFVPG 321
|
|
| A_NRPS_ProA |
cd17656 |
gramicidin S synthase 2, also known as ATP-dependent proline adenylase; This family of the ... |
2-302 |
7.15e-64 |
|
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: 208.48 E-value: 7.15e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 758185221 2 AFLPIDPDTPEERIRYSLEDSGAKFaVVNERNMTAIGQYEGTIVSLDDGKWRNESKERPSSISGSRNLAYVIYTSGTAGK 81
Cdd:cd17656 64 AFVPIDPEYPEERRIYIMLDSGVRV-VLTQRHLKSKLSFNKSTILLEDPSISQEDTSNIDYINNSDDLLYIIYTSGTTGK 142
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 758185221 82 PKGVQIEHRNLTNYVSWFSEEASLTENDKTVLLSSYASDLGYTSMFPVLLGGGELHIVQKETYTAPDEIAHYIKEYGITY 161
Cdd:cd17656 143 PKGVQLEHKNMVNLLHFEREKTNINFSDKVLQFATCSFDVCYQEIFSTLLSGGTLYIIREETKRDVEQLFDLVKRHNIEV 222
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 758185221 162 IKLTPSLFHTIVNTASFAKDAnFESLRLIVLGGEKIIPT----DVLAFRKIYGHtefiNHYGPTEATIgAIAGRVDLSEP 237
Cdd:cd17656 223 VFLPVAFLKFIFSEREFINRF-PTCVKHIITAGEQLVITnefkEMLHEHNVHLH----NHYGPSETHV-VTTYTINPEAE 296
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 758185221 238 daFAKRPTIGRPIANAGALVLNEALKLVPPGASGQLYITGQGLARGYLNRPQLTAERFVENPYSP 302
Cdd:cd17656 297 --IPELPPIGKPISNTWIYILDQEQQLQPQGIVGELYISGASVARGYLNRQELTAEKFFPDPFDP 359
|
|
| A_NRPS_ACVS-like |
cd17648 |
N-(5-amino-5-carboxypentanoyl)-L-cysteinyl-D-valine synthase; This family contains ACV ... |
1-300 |
4.20e-60 |
|
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: 198.01 E-value: 4.20e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 758185221 1 AAFLPIDPDTPEERIRYSLEDSGAKfaVVnernmtaigqyegtivslddgkwrneskerpssISGSRNLAYVIYTSGTAG 80
Cdd:cd17648 63 AAYVPIDPSYPDERIQFILEDTGAR--VV---------------------------------ITNSTDLAYAIYTSGTTG 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 758185221 81 KPKGVQIEHRNLTNYVSWFSEEASLTENDKTVLL--SSYASDLGYTSMFPVLLGGGELHIVQKETYTAPDEIAHYIKEYG 158
Cdd:cd17648 108 KPKGVLVEHGSVVNLRTSLSERYFGRDNGDEAVLffSNYVFDFFVEQMTLALLNGQKLVVPPDEMRFDPDRFYAYINREK 187
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 758185221 159 ITYIKLTPSLFHTIvntasfaKDANFESLRLIVLGGEKIIPTdvlAFRKIYGhtEF----INHYGPTEATIGAIagrVDL 234
Cdd:cd17648 188 VTYLSGTPSVLQQY-------DLARLPHLKRVDAAGEEFTAP---VFEKLRS--RFagliINAYGPTETTVTNH---KRF 252
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 758185221 235 SEPDAfAKRPTIGRPIANAGALVLNEALKLVPPGASGQLYITGQGLARGYLNRPQLTAERFVENPY 300
Cdd:cd17648 253 FPGDQ-RFDKSLGRPVRNTKCYVLNDAMKRVPVGAVGELYLGGDGVARGYLNRPELTAERFLPNPF 317
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
1-301 |
6.89e-59 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 203.65 E-value: 6.89e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 758185221 1 AAFLPIDPDTPEERIRYSLEDSGAKFaVVNERNMTAIGQYEGTIVSLD---DGKWRNESKERPSSISGSRNLAYVIYTSG 77
Cdd:PRK12316 2078 GAYVPLDPNYPAERLAYMLEDSGAAL-LLTQRHLLERLPLPAGVARLPldrDAEWADYPDTAPAVQLAGENLAYVIYTSG 2156
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 758185221 78 TAGKPKGVQIEHRNLTNYVSWFSEEASLTENDKTVLLSSYASDLGYTSMFPVLLGGGELhIVQKETYTAPDEIAHYIKEY 157
Cdd:PRK12316 2157 STGLPKGVAVSHGALVAHCQAAGERYELSPADCELQFMSFSFDGAHEQWFHPLLNGARV-LIRDDELWDPEQLYDEMERH 2235
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 758185221 158 GITYIKLTPSLFHTIVNTAsfAKDANFESLRLIVLGGEKIiptDVLAFRKIY---GHTEFINHYGPTEATIGAIAGRVDL 234
Cdd:PRK12316 2236 GVTILDFPPVYLQQLAEHA--ERDGRPPAVRVYCFGGEAV---PAASLRLAWealRPVYLFNGYGPTEAVVTPLLWKCRP 2310
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 758185221 235 SEPDAFAKRPtIGRPIANAGALVLNEALKLVPPGASGQLYITGQGLARGYLNRPQLTAERFVENPYS 301
Cdd:PRK12316 2311 QDPCGAAYVP-IGRALGNRRAYILDADLNLLAPGMAGELYLGGEGLARGYLNRPGLTAERFVPDPFS 2376
|
|
| A_NRPS_PpsD_like |
cd17650 |
similar to adenylation domain of plipastatin synthase (PpsD); This family of the adenylation ... |
2-303 |
3.17e-58 |
|
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: 193.07 E-value: 3.17e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 758185221 2 AFLPIDPDTPEERIRYSLEDSGAKFAVVNernmtaigqyegtivslddgkwrneskerPSsisgsrNLAYVIYTSGTAGK 81
Cdd:cd17650 63 AYVPIDPDYPAERLQYMLEDSGAKLLLTQ-----------------------------PE------DLAYVIYTSGTTGK 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 758185221 82 PKGVQIEHRNLTN-YVSWFSEEASLTENDKTVLLSSYASDLGYTSMFPVLLGGGELHIVQKETYTAPDEIAHYIKEYGIT 160
Cdd:cd17650 108 PKGVMVEHRNVAHaAHAWRREYELDSFPVRLLQMASFSFDVFAGDFARSLLNGGTLVICPDEVKLDPAALYDLILKSRIT 187
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 758185221 161 YIKLTPSLFHTIVNTASFAKdANFESLRLIVLGGEKIIPTD-VLAFRKIYGHTEFINHYGPTEATIGAIAGRVDLSEPDA 239
Cdd:cd17650 188 LMESTPALIRPVMAYVYRNG-LDLSAMRLLIVGSDGCKAQDfKTLAARFGQGMRIINSYGVTEATIDSTYYEEGRDPLGD 266
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 758185221 240 FAKRPtIGRPIANAGALVLNEALKLVPPGASGQLYITGQGLARGYLNRPQLTAERFVENPYSPG 303
Cdd:cd17650 267 SANVP-IGRPLPNTAMYVLDERLQPQPVGVAGELYIGGAGVARGYLNRPELTAERFVENPFAPG 329
|
|
| A_NRPS_SidN3_like |
cd05918 |
The adenylation (A) domain of siderophore-synthesizing nonribosomal peptide synthetases (NRPS); ... |
1-299 |
1.56e-57 |
|
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: 191.99 E-value: 1.56e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 758185221 1 AAFLPIDPDTPEERIRYSLEDSGAKFAVVnernmtaigqyegtivslddgkwrneskerpSSISgsrNLAYVIYTSGTAG 80
Cdd:cd05918 74 GAFVPLDPSHPLQRLQEILQDTGAKVVLT-------------------------------SSPS---DAAYVIFTSGSTG 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 758185221 81 KPKGVQIEHRNLTNYVSWFSEEASLTENDKTVLLSSYASDLGYTSMFPVLLGGGELHIvqketytAPDE-----IAHYIK 155
Cdd:cd05918 120 KPKGVVIEHRALSTSALAHGRALGLTSESRVLQFASYTFDVSILEIFTTLAAGGCLCI-------PSEEdrlndLAGFIN 192
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 758185221 156 EYGITYIKLTPSLFHTIvntasfaKDANFESLRLIVLGGEKIIPTDVLAFRkiyGHTEFINHYGPTEATIGAIAgrvdlS 235
Cdd:cd05918 193 RLRVTWAFLTPSVARLL-------DPEDVPSLRTLVLGGEALTQSDVDTWA---DRVRLINAYGPAECTIAATV-----S 257
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 758185221 236 EPDAFAKRPTIGRPIAnAGALVLNEA--LKLVPPGASGQLYITGQGLARGYLNRPQLTAERFVENP 299
Cdd:cd05918 258 PVVPSTDPRNIGRPLG-ATCWVVDPDnhDRLVPIGAVGELLIEGPILARGYLNDPEKTAAAFIEDP 322
|
|
| A_NRPS_TlmIV_like |
cd12114 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including ... |
1-299 |
2.01e-54 |
|
The adenylation domain of nonribosomal peptide synthetases (NRPS), including Streptoalloteichus tallysomycin biosynthesis genes; The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions. This family includes the TLM biosynthetic gene cluster from Streptoalloteichus that consists of nine NRPS genes; the N-terminal module of TlmVI (NRPS-5) and the starter module of BlmVI (NRPS-5) are comprised of the acyl CoA ligase (AL) and acyl carrier protein (ACP)-like domains, which are thought to be involved in the biosynthesis of the beta-aminoalaninamide moiety.
Pssm-ID: 341279 [Multi-domain] Cd Length: 477 Bit Score: 183.63 E-value: 2.01e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 758185221 1 AAFLPIDPDTPEERIRYSLEDSGAKFAVVNErnMTAIGQYEGTIVSLDDGKWRNESKERPSSISGSRNLAYVIYTSGTAG 80
Cdd:cd12114 62 AAYVPVDIDQPAARREAILADAGARLVLTDG--PDAQLDVAVFDVLILDLDALAAPAPPPPVDVAPDDLAYVIFTSGSTG 139
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 758185221 81 KPKGVQIEHRNLTNYVSWFSEEASLTENDKTVLLSSYASDLGYTSMFPVLLGGGELHIVQKETYTAPDEIAHYIKEYGIT 160
Cdd:cd12114 140 TPKGVMISHRAALNTILDINRRFAVGPDDRVLALSSLSFDLSVYDIFGALSAGATLVLPDEARRRDPAHWAELIERHGVT 219
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 758185221 161 YIKLTPSLFHTIVNTASFAKDANfESLRLIVLGGEKIIPTDVLAFRKIYGHTEFINHYGPTEATIGAIAGRVDLSEPDaf 240
Cdd:cd12114 220 LWNSVPALLEMLLDVLEAAQALL-PSLRLVLLSGDWIPLDLPARLRALAPDARLISLGGATEASIWSIYHPIDEVPPD-- 296
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 758185221 241 akRPTI--GRPIANAGALVLNEALKLVPPGASGQLYITGQGLARGYLNRPQLTAERFVENP 299
Cdd:cd12114 297 --WRSIpyGRPLANQRYRVLDPRGRDCPDWVPGELWIGGRGVALGYLGDPELTAARFVTHP 355
|
|
| A_NRPS_GliP_like |
cd17653 |
nonribosomal peptide synthase GliP-like; This family includes the adenylation (A) domain of ... |
1-303 |
1.05e-53 |
|
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: 180.97 E-value: 1.05e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 758185221 1 AAFLPIDPDTPEERIRYSLEDSGAKFAVVNernmtaigqyegtivslddgkwrneskerpssiSGSRNLAYVIYTSGTAG 80
Cdd:cd17653 72 AAYVPLDAKLPSARIQAILRTSGATLLLTT---------------------------------DSPDDLAYIIFTSGSTG 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 758185221 81 KPKGVQIEHRNLTNYVSWFSEEASLTENDKTVLLSSYASDLGYTSMFPVLLGGGELHIVqketyTAPDEIAHYIKEYGIT 160
Cdd:cd17653 119 IPKGVMVPHRGVLNYVSQPPARLDVGPGSRVAQVLSIAFDACIGEIFSTLCNGGTLVLA-----DPSDPFAHVARTVDAL 193
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 758185221 161 YIklTPSLFHTIvntasfaKDANFESLRLIVLGGEKiiPTDVLAfRKIYGHTEFINHYGPTEATIGAIAGRVdlsEPDaf 240
Cdd:cd17653 194 MS--TPSILSTL-------SPQDFPNLKTIFLGGEA--VPPSLL-DRWSPGRRLYNAYGPTECTISSTMTEL---LPG-- 256
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 758185221 241 aKRPTIGRPIANAGALVLNEALKLVPPGASGQLYITGQGLARGYLNRPQLTAERFVENPYSPG 303
Cdd:cd17653 257 -QPVTIGKPIPNSTCYILDADLQPVPEGVVGEICISGVQVARGYLGNPALTASKFVPDPFWPG 318
|
|
| entF |
PRK10252 |
enterobactin non-ribosomal peptide synthetase EntF; |
1-303 |
1.82e-53 |
|
enterobactin non-ribosomal peptide synthetase EntF;
Pssm-ID: 236668 [Multi-domain] Cd Length: 1296 Bit Score: 187.94 E-value: 1.82e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 758185221 1 AAFLPIDPDTPEERIRYSLEDSGAKFAVvnernmTAIGQyEGTIVSLDDGK------WRNESKERPSSISGSRNLAYVIY 74
Cdd:PRK10252 533 AAWLPLDTGYPDDRLKMMLEDARPSLLI------TTADQ-LPRFADVPDLTslcynaPLAPQGAAPLQLSQPHHTAYIIF 605
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 758185221 75 TSGTAGKPKGVQIEHRNLTNYVSWFSEEASLTENDKtVLLSSYAS-DLGYTSMFPVLLGGGELHIVQKETYTAPDEIAHY 153
Cdd:PRK10252 606 TSGSTGRPKGVMVGQTAIVNRLLWMQNHYPLTADDV-VLQKTPCSfDVSVWEFFWPFIAGAKLVMAEPEAHRDPLAMQQF 684
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 758185221 154 IKEYGITYIKLTPSLFHTIVNT-ASFAKDANFESLRLIVLGGEKIiPTDVLafRKIYGHT--EFINHYGPTEATigaiag 230
Cdd:PRK10252 685 FAEYGVTTTHFVPSMLAAFVASlTPEGARQSCASLRQVFCSGEAL-PADLC--REWQQLTgaPLHNLYGPTEAA------ 755
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 758185221 231 rVDLS----EPDAFAKRPT----IGRPIANAGALVLNEALKLVPPGASGQLYITGQGLARGYLNRPQLTAERFVENPYSP 302
Cdd:PRK10252 756 -VDVSwypaFGEELAAVRGssvpIGYPVWNTGLRILDARMRPVPPGVAGDLYLTGIQLAQGYLGRPDLTASRFIADPFAP 834
|
.
gi 758185221 303 G 303
Cdd:PRK10252 835 G 835
|
|
| A_NRPS_Sfm_like |
cd12115 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including Saframycin A gene ... |
1-303 |
2.04e-53 |
|
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: 180.59 E-value: 2.04e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 758185221 1 AAFLPIDPDTPEERIRYSLEDSGAKFAVVnernmtaigqyegtivslddgkwrneskerpssisGSRNLAYVIYTSGTAG 80
Cdd:cd12115 74 AAYVPLDPAYPPERLRFILEDAQARLVLT-----------------------------------DPDDLAYVIYTSGSTG 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 758185221 81 KPKGVQIEHRNLTNYVSWFSEEASLTENDKTVLLSSYASDLGYTSMFPVLLGGGELHIVQkETYTAPDEIAHYikeyGIT 160
Cdd:cd12115 119 RPKGVAIEHRNAAAFLQWAAAAFSAEELAGVLASTSICFDLSVFELFGPLATGGKVVLAD-NVLALPDLPAAA----EVT 193
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 758185221 161 YIKLTPSLFHTIVNtasfaKDANFESLRLIVLGGEKIIPTDVlafRKIYGH---TEFINHYGPTEATIGAIAGRVDLSEP 237
Cdd:cd12115 194 LINTVPSAAAELLR-----HDALPASVRVVNLAGEPLPRDLV---QRLYARlqvERVVNLYGPSEDTTYSTVAPVPPGAS 265
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 758185221 238 DAfakrPTIGRPIANAGALVLNEALKLVPPGASGQLYITGQGLARGYLNRPQLTAERFVENPYSPG 303
Cdd:cd12115 266 GE----VSIGRPLANTQAYVLDRALQPVPLGVPGELYIGGAGVARGYLGRPGLTAERFLPDPFGPG 327
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
2-303 |
1.22e-51 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 182.85 E-value: 1.22e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 758185221 2 AFLPIDPDTPEERIRYSLEDSGAKFAVVNERnmTAIGQYEGTIVSLDDGKWRNESKERPSSISGSRNLAYVIYTSGTAGK 81
Cdd:PRK12316 3133 AYVPLDPEYPEERLAYMLEDSGAQLLLSQSH--LRLPLAQGVQVLDLDRGDENYAEANPAIRTMPENLAYVIYTSGSTGK 3210
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 758185221 82 PKGVQIEHRNLTNYVSWFSEEASLTENDKTVLLSSYASDLGYTSMFPVLLGGGELHIVQKETYTAPDEIAHYIKEYGITY 161
Cdd:PRK12316 3211 PKGVGIRHSALSNHLCWMQQAYGLGVGDRVLQFTTFSFDVFVEELFWPLMSGARVVLAGPEDWRDPALLVELINSEGVDV 3290
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 758185221 162 IKLTPSlfhTIVNTASFAKDANFESLRLIVLGGEKIiPTDVLAfrKIYGHTEFINHYGPTEATIGAIAGRVDLSEPDAfa 241
Cdd:PRK12316 3291 LHAYPS---MLQAFLEEEDAHRCTSLKRIVCGGEAL-PADLQQ--QVFAGLPLYNLYGPTEATITVTHWQCVEEGKDA-- 3362
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 758185221 242 krPTIGRPIANAGALVLNEALKLVPPGASGQLYITGQGLARGYLNRPQLTAERFVENPYSPG 303
Cdd:PRK12316 3363 --VPIGRPIANRACYILDGSLEPVPVGALGELYLGGEGLARGYHNRPGLTAERFVPDPFVPG 3422
|
|
| MenE/FadK |
COG0318 |
O-succinylbenzoic acid-CoA ligase MenE or related acyl-CoA synthetase (AMP-forming) [Lipid ... |
1-297 |
9.20e-50 |
|
O-succinylbenzoic acid-CoA ligase MenE or related acyl-CoA synthetase (AMP-forming) [Lipid transport and metabolism]; O-succinylbenzoic acid-CoA ligase MenE or related acyl-CoA synthetase (AMP-forming) is part of the Pathway/BioSystem: Menaquinone biosynthesis
Pssm-ID: 440087 [Multi-domain] Cd Length: 452 Bit Score: 170.76 E-value: 9.20e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 758185221 1 AAFLPIDPDTPEERIRYSLEDSGAKFAVVnernmtaigqyegtivslddgkwrneskerpssisgsrnlAYVIYTSGTAG 80
Cdd:COG0318 74 AVVVPLNPRLTAEELAYILEDSGARALVT----------------------------------------ALILYTSGTTG 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 758185221 81 KPKGVQIEHRNLTNYVSWFSEEASLTENDKTVLLSSYASDLGYT-SMFPVLLGGGELHIVQKetyTAPDEIAHYIKEYGI 159
Cdd:COG0318 114 RPKGVMLTHRNLLANAAAIAAALGLTPGDVVLVALPLFHVFGLTvGLLAPLLAGATLVLLPR---FDPERVLELIERERV 190
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 758185221 160 TYIKLTPSLFHTIVNTASFAKdANFESLRLIVLGGEKIiPTDVL-AFRKIYGHtEFINHYGPTEATIGAIAGRVDLSEpd 238
Cdd:COG0318 191 TVLFGVPTMLARLLRHPEFAR-YDLSSLRLVVSGGAPL-PPELLeRFEERFGV-RIVEGYGLTETSPVVTVNPEDPGE-- 265
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*....
gi 758185221 239 afAKRPTIGRPIANAGALVLNEALKLVPPGASGQLYITGQGLARGYLNRPQLTAERFVE 297
Cdd:COG0318 266 --RRPGSVGRPLPGVEVRIVDEDGRELPPGEVGEIVVRGPNVMKGYWNDPEATAEAFRD 322
|
|
| PRK05691 |
PRK05691 |
peptide synthase; Validated |
2-301 |
1.34e-48 |
|
peptide synthase; Validated
Pssm-ID: 235564 [Multi-domain] Cd Length: 4334 Bit Score: 173.82 E-value: 1.34e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 758185221 2 AFLPIDPDTPEERIRYSLEDSGAKFAVVNERNMTAIGQYEGTIV----SLDDGKWrneskerPSSISG----SRNLAYVI 73
Cdd:PRK05691 1207 AYVPLDPDYPAERLAYMLADSGVELLLTQSHLLERLPQAEGVSAialdSLHLDSW-------PSQAPGlhlhGDNLAYVI 1279
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 758185221 74 YTSGTAGKPKGVQIEHRNLTNYVSWFSEEASLTENDktVLL--SSYASDLGYTSMFPVLLGGGELHIVQKETYTAPDEIA 151
Cdd:PRK05691 1280 YTSGSTGQPKGVGNTHAALAERLQWMQATYALDDSD--VLMqkAPISFDVSVWECFWPLITGCRLVLAGPGEHRDPQRIA 1357
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 758185221 152 HYIKEYGITYIKLTPSLFHTIVNTASFAkdaNFESLRLIVLGGEKIIPTDVLAFRKIYGHTEFINHYGPTEATIGAIAGR 231
Cdd:PRK05691 1358 ELVQQYGVTTLHFVPPLLQLFIDEPLAA---ACTSLRRLFSGGEALPAELRNRVLQRLPQVQLHNRYGPTETAINVTHWQ 1434
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 758185221 232 VDLSEpdafAKRPTIGRPIANAGALVLNEALKLVPPGASGQLYITGQGLARGYLNRPQLTAERFVENPYS 301
Cdd:PRK05691 1435 CQAED----GERSPIGRPLGNVLCRVLDAELNLLPPGVAGELCIGGAGLARGYLGRPALTAERFVPDPLG 1500
|
|
| DltA |
cd05945 |
D-alanine:D-alanyl carrier protein ligase (DltA) and similar proteins; This family includes ... |
1-299 |
3.36e-47 |
|
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: 163.96 E-value: 3.36e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 758185221 1 AAFLPIDPDTPEERIRYSLEDSGAKFAVVNErnmtaigqyegtivslDDgkwrneskerpssisgsrnLAYVIYTSGTAG 80
Cdd:cd05945 66 HAYVPLDASSPAERIREILDAAKPALLIADG----------------DD-------------------NAYIIFTSGSTG 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 758185221 81 KPKGVQIEHRNLTNYVSWFSEEASLTENDktVLLS--SYASDLGYTSMFPVLLGGGELHIVQKETYTAPDEIAHYIKEYG 158
Cdd:cd05945 111 RPKGVQISHDNLVSFTNWMLSDFPLGPGD--VFLNqaPFSFDLSVMDLYPALASGATLVPVPRDATADPKQLFRFLAEHG 188
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 758185221 159 ITYIKLTPSLFHTIVNTASFAKdANFESLRLIVLGGEKIIPTDVLAFRKIYGHTEFINHYGPTEATIGAIAGRVDlSEPD 238
Cdd:cd05945 189 ITVWVSTPSFAAMCLLSPTFTP-ESLPSLRHFLFCGEVLPHKTARALQQRFPDARIYNTYGPTEATVAVTYIEVT-PEVL 266
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 758185221 239 AFAKRPTIGRPIANAGALVLNEALKLVPPGASGQLYITGQGLARGYLNRPQLTAERFVENP 299
Cdd:cd05945 267 DGYDRLPIGYAKPGAKLVILDEDGRPVPPGEKGELVISGPSVSKGYLNNPEKTAAAFFPDE 327
|
|
| PRK05691 |
PRK05691 |
peptide synthase; Validated |
1-302 |
4.47e-45 |
|
peptide synthase; Validated
Pssm-ID: 235564 [Multi-domain] Cd Length: 4334 Bit Score: 163.80 E-value: 4.47e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 758185221 1 AAFLPIDPDTPEERIRYSLEDSGAKFAVVNERNMTAIGQYEGTIV--SLDD--GKWRNESKERPSSISGSRNLAYVIYTS 76
Cdd:PRK05691 2263 GAYVPLDPEYPLERLHYMIEDSGIGLLLSDRALFEALGELPAGVArwCLEDdaAALAAYSDAPLPFLSLPQHQAYLIYTS 2342
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 758185221 77 GTAGKPKGVQIEHRNLTNYVSWFSEEASLTENDKTVLLSSYASDLGYTSMFPVLLGGGELhIVQKETYTAPDEIAHYIKE 156
Cdd:PRK05691 2343 GSTGKPKGVVVSHGEIAMHCQAVIERFGMRADDCELHFYSINFDAASERLLVPLLCGARV-VLRAQGQWGAEEICQLIRE 2421
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 758185221 157 YGITYIKLTPSLFHTIVNTasFAKDANFESLRLIVLGGEKIIPTDVLAFRKIYGHTEFINHYGPTEATIGAIAGRVDLSE 236
Cdd:PRK05691 2422 QQVSILGFTPSYGSQLAQW--LAGQGEQLPVRMCITGGEALTGEHLQRIRQAFAPQLFFNAYGPTETVVMPLACLAPEQL 2499
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 758185221 237 PDAFAKRPtIGRPIANAGALVLNEALKLVPPGASGQLYITGQGLARGYLNRPQLTAERFVENPYSP 302
Cdd:PRK05691 2500 EEGAASVP-IGRVVGARVAYILDADLALVPQGATGELYVGGAGLAQGYHDRPGLTAERFVADPFAA 2564
|
|
| AFD_class_I |
cd04433 |
Adenylate forming domain, Class I, also known as the ANL superfamily; This family is known as ... |
69-297 |
2.24e-39 |
|
Adenylate forming domain, Class I, also known as the ANL superfamily; This family is known as the ANL (acyl-CoA synthetases, the NRPS adenylation domains, and the Luciferase enzymes) superfamily. It includes acyl- and aryl-CoA ligases, as well as the adenylation domain of nonribosomal peptide synthetases and firefly luciferases.The adenylate-forming enzymes catalyze an ATP-dependent two-step reaction to first activate a carboxylate substrate as an adenylate and then transfer the carboxylate to the pantetheine group of either coenzyme A or an acyl-carrier protein. The active site of the domain is located at the interface of a large N-terminal subdomain and a smaller C-terminal subdomain.
Pssm-ID: 341228 [Multi-domain] Cd Length: 336 Bit Score: 140.88 E-value: 2.24e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 758185221 69 LAYVIYTSGTAGKPKGVQIEHRNLTNYVSWFSEEASLTENDKTVLLSSYASDLGYTSMFPVLLGGGELHIVQKETytaPD 148
Cdd:cd04433 2 PALILYTSGTTGKPKGVVLSHRNLLAAAAALAASGGLTEGDVFLSTLPLFHIGGLFGLLGALLAGGTVVLLPKFD---PE 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 758185221 149 EIAHYIKEYGITYIKLTPSLFHTIVNTASFAkDANFESLRLIVLGGEKIIPTDVLAFRKIYGhTEFINHYGPTEATIGAI 228
Cdd:cd04433 79 AALELIEREKVTILLGVPTLLARLLKAPESA-GYDLSSLRALVSGGAPLPPELLERFEEAPG-IKLVNGYGLTETGGTVA 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 758185221 229 AGRVDLSEpdafAKRPTIGRPIANAGALVLNEALKLVPPGASGQLYITGQGLARGYLNRPQLTAERFVE 297
Cdd:cd04433 157 TGPPDDDA----RKPGSVGRPVPGVEVRIVDPDGGELPPGEIGELVVRGPSVMKGYWNNPEATAAVDED 221
|
|
| PRK05691 |
PRK05691 |
peptide synthase; Validated |
1-303 |
3.24e-34 |
|
peptide synthase; Validated
Pssm-ID: 235564 [Multi-domain] Cd Length: 4334 Bit Score: 132.21 E-value: 3.24e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 758185221 1 AAFLPIDPDTPEERIRYSLEDSGAKFAVVN----ERNMTAIGQYEGT----IVSLDDGKWRNESKERPSSISGSRNLAYV 72
Cdd:PRK05691 3795 AGYLPLDPGLPAQRLQRIIELSRTPVLVCSaacrEQARALLDELGCAnrprLLVWEEVQAGEVASHNPGIYSGPDNLAYV 3874
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 758185221 73 IYTSGTAGKPKGVQIEHRNLTNYVSWFSEEASLTENDKTVLLSSYASDLGYTSMFPVLLGGGELHIVqketytaPDEIAH 152
Cdd:PRK05691 3875 IYTSGSTGLPKGVMVEQRGMLNNQLSKVPYLALSEADVIAQTASQSFDISVWQFLAAPLFGARVEIV-------PNAIAH 3947
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 758185221 153 -------YIKEYGITYIKLTPSLFhtivnTASFAKD-ANFESLRLIVLGGEKIIPTDVLAFRKIYGHTEFINHYGPTEAT 224
Cdd:PRK05691 3948 dpqgllaHVQAQGITVLESVPSLI-----QGMLAEDrQALDGLRWMLPTGEAMPPELARQWLQRYPQIGLVNAYGPAECS 4022
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 758185221 225 IGAIAGRVDLSEPDAfAKRPtIGRPIANAGALVLNEALKLVPPGASGQLYITGQGLARGYLNRPQLTAERFVENPY-SPG 303
Cdd:PRK05691 4023 DDVAFFRVDLASTRG-SYLP-IGSPTDNNRLYLLDEALELVPLGAVGELCVAGTGVGRGYVGDPLRTALAFVPHPFgAPG 4100
|
|
| FACL_FadD13-like |
cd17631 |
fatty acyl-CoA synthetase, including FadD13; This family contains fatty acyl-CoA synthetases, ... |
1-295 |
1.02e-33 |
|
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: 127.73 E-value: 1.02e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 758185221 1 AAFLPIDPD-TPEErIRYSLEDSGAKfavvnernmtaigqyegtiVSLDDgkwrneskerpssisgsrnLAYVIYTSGTA 79
Cdd:cd17631 70 AVFVPLNFRlTPPE-VAYILADSGAK-------------------VLFDD-------------------LALLMYTSGTT 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 758185221 80 GKPKGVQIEHRNLT-NYVSWFSEeASLTENDKTVLLS--SYASDLGYTsMFPVLLGGGELHIVQKETytaPDEIAHYIKE 156
Cdd:cd17631 111 GRPKGAMLTHRNLLwNAVNALAA-LDLGPDDVLLVVAplFHIGGLGVF-TLPTLLRGGTVVILRKFD---PETVLDLIER 185
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 758185221 157 YGITYIKLTPSLFHTIVNTASFAkDANFESLRLIVLGGEKIiPTDVLAFRKIYGhTEFINHYGPTEATIGAIAgrvdLSE 236
Cdd:cd17631 186 HRVTSFFLVPTMIQALLQHPRFA-TTDLSSLRAVIYGGAPM-PERLLRALQARG-VKFVQGYGMTETSPGVTF----LSP 258
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*....
gi 758185221 237 PDAFAKRPTIGRPIANAGALVLNEALKLVPPGASGQLYITGQGLARGYLNRPQLTAERF 295
Cdd:cd17631 259 EDHRRKLGSAGRPVFFVEVRIVDPDGREVPPGEVGEIVVRGPHVMAGYWNRPEATAAAF 317
|
|
| PRK04813 |
PRK04813 |
D-alanine--poly(phosphoribitol) ligase subunit DltA; |
2-297 |
7.01e-32 |
|
D-alanine--poly(phosphoribitol) ligase subunit DltA;
Pssm-ID: 235313 [Multi-domain] Cd Length: 503 Bit Score: 123.47 E-value: 7.01e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 758185221 2 AFLPIDPDTPEERIRYSLEDSGAKFAV-VNERNMTAIGQYEGTIVSLDDGKWRNESKERPSSISGSRNlAYVIYTSGTAG 80
Cdd:PRK04813 78 AYIPVDVSSPAERIEMIIEVAKPSLIIaTEELPLEILGIPVITLDELKDIFATGNPYDFDHAVKGDDN-YYIIFTSGTTG 156
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 758185221 81 KPKGVQIEHRNLTNYVSWFSEEASLTENDKTVLLSSYASDLGYTSMFPVLLGGGELHIVQKETYTAPDEIAHYIKEYGIT 160
Cdd:PRK04813 157 KPKGVQISHDNLVSFTNWMLEDFALPEGPQFLNQAPYSFDLSVMDLYPTLASGGTLVALPKDMTANFKQLFETLPQLPIN 236
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 758185221 161 yikltpslfhTIVNTASFAK----DANFE-----SLRLIVLGGEKIIPTDVLAFRKIYGHTEFINHYGPTEATIGAIAGR 231
Cdd:PRK04813 237 ----------VWVSTPSFADmcllDPSFNeehlpNLTHFLFCGEELPHKTAKKLLERFPSATIYNTYGPTEATVAVTSIE 306
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 758185221 232 VDlsePDAFAKRPT--IGRPIANAGALVLNEALKLVPPGASGQLYITGQGLARGYLNRPQLTAERFVE 297
Cdd:PRK04813 307 IT---DEMLDQYKRlpIGYAKPDSPLLIIDEEGTKLPDGEQGEIVISGPSVSKGYLNNPEKTAEAFFT 371
|
|
| FC-FACS_FadD_like |
cd05936 |
Prokaryotic long-chain fatty acid CoA synthetases similar to Escherichia coli FadD; This ... |
1-296 |
1.04e-29 |
|
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: 117.28 E-value: 1.04e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 758185221 1 AAFLPIDPDTPEERIRYSLEDSGAKFAVVNERNMTAIGQYEGT----IVSLDDgkwrneskerpssisgsrnLAYVIYTS 76
Cdd:cd05936 74 AVVVPLNPLYTPRELEHILNDSGAKALIVAVSFTDLLAAGAPLgervALTPED-------------------VAVLQYTS 134
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 758185221 77 GTAGKPKGVQIEHRNLT-N-YVSWFSEEASLTENDKTVLLSSYASDLGYTS--MFPVLLGGgelHIVQKETYTAPDEIAH 152
Cdd:cd05936 135 GTTGVPKGAMLTHRNLVaNaLQIKAWLEDLLEGDDVVLAALPLFHVFGLTValLLPLALGA---TIVLIPRFRPIGVLKE 211
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 758185221 153 yIKEYGITYIKLTPSLFHTIVNTASFAKdANFESLRLIVLGGEKIiPTDVL-AFRKIYGhTEFINHYGPTEATIGAIAGR 231
Cdd:cd05936 212 -IRKHRVTIFPGVPTMYIALLNAPEFKK-RDFSSLRLCISGGAPL-PVEVAeRFEELTG-VPIVEGYGLTETSPVVAVNP 287
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 758185221 232 VDlsepdaFAKRP-TIGRPIANAGALVLNEALKLVPPGASGQLYITGQGLARGYLNRPQLTAERFV 296
Cdd:cd05936 288 LD------GPRKPgSIGIPLPGTEVKIVDDDGEELPPGEVGELWVRGPQVMKGYWNRPEETAEAFV 347
|
|
| A_NRPS_acs4 |
cd17654 |
acyl-CoA synthetase family member 4; This family of the adenylation (A) domain of nonribosomal ... |
1-288 |
6.73e-29 |
|
acyl-CoA synthetase family member 4; This family of the adenylation (A) domain of nonribosomal peptide synthases (NRPS) contains acyl-CoA synthethase family member 4, also known as 2-aminoadipic 6-semialdehyde dehydrogenase or aminoadipate-semialdehyde dehydrogenase, most of which are uncharacterized. Acyl-CoA synthetase catalyzes the initial reaction in fatty acid metabolism, by forming a thioester with CoA. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.
Pssm-ID: 341309 [Multi-domain] Cd Length: 449 Bit Score: 114.88 E-value: 6.73e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 758185221 1 AAFLPIDPDTPEERIRYSLEDSGAKFAVVNERNMTAigqyegtivslddgKWRNESKERPSSISGSRNLAYVIYTSGTAG 80
Cdd:cd17654 66 AAYAPIDPASPEQRSLTVMKKCHVSYLLQNKELDNA--------------PLSFTPEHRHFNIRTDECLAYVIHTSGTTG 131
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 758185221 81 KPKGVQIEHRNLTNYVSWFSEEASLTENDKTVLLSSYASDLGYTSMFPVLLGGGELHIVQKETYTAPDEIAHYI-KEYGI 159
Cdd:cd17654 132 TPKIVAVPHKCILPNIQHFRSLFNITSEDILFLTSPLTFDPSVVEIFLSLSSGATLLIVPTSVKVLPSKLADILfKRHRI 211
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 758185221 160 TYIKLTPSLFHTIvnTASFAKDANF---ESLRLIVLGGEKiIPTDVL--AFRKIYGHTEFINHYGPTEATIGAIAGRVdl 234
Cdd:cd17654 212 TVLQATPTLFRRF--GSQSIKSTVLsatSSLRVLALGGEP-FPSLVIlsSWRGKGNRTRIFNIYGITEVSCWALAYKV-- 286
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*..
gi 758185221 235 sePDAFAKRPtIGRPIANagalVLNEALKLVPPGASGQLYITGQ---GLARGYLNRP 288
Cdd:cd17654 287 --PEEDSPVQ-LGSPLLG----TVIEVRDQNGSEGTGQVFLGGLnrvCILDDEVTVP 336
|
|
| ligase_PEP_1 |
TIGR03098 |
acyl-CoA ligase (AMP-forming), exosortase A-associated; This group of proteins contains an ... |
1-303 |
4.58e-27 |
|
acyl-CoA ligase (AMP-forming), exosortase A-associated; This group of proteins contains an AMP-binding domain (pfam00501) associated with acyl CoA-ligases. These proteins are generally found in genomes containing the exosortase/PEP-CTERM protein expoert system, specifically the type 1 variant of this system described by the Genome Property GenProp0652. When found in this context they are invariably present next to a decarboxylase enzyme. A number of sequences from Burkholderia species also hit this model, but the genomic context is obviously different. The hypothesis of a constant substrate for this family is only strong where the exosortase context is present.
Pssm-ID: 211788 [Multi-domain] Cd Length: 517 Bit Score: 110.26 E-value: 4.58e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 758185221 1 AAFLPIDPDTPEERIRYSLEDSGAKFAVVNE----------------RNMTAIGQYEGTIVSLDDGK---WRnESKERPS 61
Cdd:TIGR03098 75 GVFVPINPLLKAEQVAHILADCNVRLLVTSSerldllhpalpgchdlRTLIIVGDPAHASEGHPGEEpasWP-KLLALGD 153
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 758185221 62 SISGSR----NLAYVIYTSGTAGKPKGVQIEHRNLTNYVSWFSEEASLTENDKTVLLSSYASDLGYTSMFPVLLGGGELH 137
Cdd:TIGR03098 154 ADPPHPvidsDMAAILYTSGSTGRPKGVVLSHRNLVAGAQSVATYLENRPDDRLLAVLPLSFDYGFNQLTTAFYVGATVV 233
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 758185221 138 IVQketYTAPDEIAHYIKEYGITYIKLTPSLFHTIVNTAsfAKDANFESLRLIVLGGEKIIPTDVLAFRKIYGHTEFINH 217
Cdd:TIGR03098 234 LHD---YLLPRDVLKALEKHGITGLAAVPPLWAQLAQLD--WPESAAPSLRYLTNSGGAMPRATLSRLRSFLPNARLFLM 308
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 758185221 218 YGPTEATigaiagRVDLSEPDAFAKRPT-IGRPIANAGALVLNEALKLVPPGASGQLYITGQGLARGYLNRPQLTAERFV 296
Cdd:TIGR03098 309 YGLTEAF------RSTYLPPEEVDRRPDsIGKAIPNAEVLVLREDGSECAPGEEGELVHRGALVAMGYWNDPEKTAERFR 382
|
....*..
gi 758185221 297 ENPYSPG 303
Cdd:TIGR03098 383 PLPPFPG 389
|
|
| FACL_like_6 |
cd05922 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
3-289 |
4.29e-26 |
|
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: 107.14 E-value: 4.29e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 758185221 3 FLPIDPDTPEERIRYSLEDSGAKFAVVNERNMT----AIGQYEGTIVSLDDGKWRNESKERPSSISGSRNLAYVIYTSGT 78
Cdd:cd05922 49 FVPLNPTLKESVLRYLVADAGGRIVLADAGAADrlrdALPASPDPGTVLDADGIRAARASAPAHEVSHEDLALLLYTSGS 128
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 758185221 79 AGKPKGVQIEHRNLTNYVSWFSEEASLTENDK--TVLLSSYasDLGYTSMFPVLLGGGELhiVQKETYTAPDEIAHYIKE 156
Cdd:cd05922 129 TGSPKLVRLSHQNLLANARSIAEYLGITADDRalTVLPLSY--DYGLSVLNTHLLRGATL--VLTNDGVLDDAFWEDLRE 204
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 758185221 157 YGITYIKLTPSLFhTIVNTASFAkDANFESLRLIVLGGEKIIPTDVLAFRKIYGHTEFINHYGPTEATigaiaGRVDLSE 236
Cdd:cd05922 205 HGATGLAGVPSTY-AMLTRLGFD-PAKLPSLRYLTQAGGRLPQETIARLRELLPGAQVYVMYGQTEAT-----RRMTYLP 277
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....
gi 758185221 237 PDAFAKRPT-IGRPIANAGALVLNEALKLVPPGASGQLYITGQGLARGYLNRPQ 289
Cdd:cd05922 278 PERILEKPGsIGLAIPGGEFEILDDDGTPTPPGEPGEIVHRGPNVMKGYWNDPP 331
|
|
| A_NRPS_alphaAR |
cd17647 |
Alpha-aminoadipate reductase; This family contains L-2-aminoadipate reductase, also known as ... |
74-298 |
1.67e-25 |
|
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: 105.68 E-value: 1.67e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 758185221 74 YTSGTAGKPKGVQIEHRNLTNYVSWFSEEASLTENDKTVLLSSYASDLGYTSMFPVLLGGGELHIVQKETYTAPDEIAHY 153
Cdd:cd17647 116 FTSGSEGIPKGVLGRHFSLAYYFPWMAKRFNLSENDKFTMLSGIAHDPIQRDMFTPLFLGAQLLVPTQDDIGTPGRLAEW 195
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 758185221 154 IKEYGITYIKLTPSLFHTIVNTAsfakDANFESLRLIVLGGEKIIPTDVLAFRKIYGHTEFINHYGPTEATIGaiagrVD 233
Cdd:cd17647 196 MAKYGATVTHLTPAMGQLLTAQA----TTPFPKLHHAFFVGDILTKRDCLRLQTLAENVRIVNMYGTTETQRA-----VS 266
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 758185221 234 LSEPDAFAKRPTI----------GRPIANAGALVLN--EALKLVPPGASGQLYITGQGLARGYLNRPQLTAERFVEN 298
Cdd:cd17647 267 YFEVPSRSSDPTFlknlkdvmpaGRGMLNVQLLVVNrnDRTQICGIGEVGEIYVRAGGLAEGYRGLPELNKEKFVNN 343
|
|
| Firefly_Luc_like |
cd05911 |
Firefly luciferase of light emitting insects and 4-Coumarate-CoA Ligase (4CL); This family ... |
1-297 |
7.05e-25 |
|
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: 103.83 E-value: 7.05e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 758185221 1 AAFLPIDPDTPEERIRYSLEDSGAKFAVVNERN-------------------MTAIGQYEGTIVSLDDGKWRNESKERP- 60
Cdd:cd05911 60 GIFSAANPIYTADELAHQLKISKPKVIFTDPDGlekvkeaakelgpkdkiivLDDKPDGVLSIEDLLSPTLGEEDEDLPp 139
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 758185221 61 SSISGSRNLAYVIYTSGTAGKPKGVQIEHRNLTN--YVSWFSEEASLTENDKTVLLSSYASDLGYTSMFPVLLGGGELHI 138
Cdd:cd05911 140 PLKDGKDDTAAILYSSGTTGLPKGVCLSHRNLIAnlSQVQTFLYGNDGSNDVILGFLPLYHIYGLFTTLASLLNGATVII 219
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 758185221 139 VQKetyTAPDEIAHYIKEYGITYIKLTPSLFHTIVNTASFAKdANFESLRLIVLGGEKIIPTDVLAFRKIYGHTEFINHY 218
Cdd:cd05911 220 MPK---FDSELFLDLIEKYKITFLYLVPPIAAALAKSPLLDK-YDLSSLRVILSGGAPLSKELQELLAKRFPNATIKQGY 295
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 758185221 219 GPTEATIGAIagrvdlSEPDAFAKRPTIGRPIANAGALVLNEALK-LVPPGASGQLYITGQGLARGYLNRPQLTAERFVE 297
Cdd:cd05911 296 GMTETGGILT------VNPDGDDKPGSVGRLLPNVEAKIVDDDGKdSLGPNEPGEICVRGPQVMKGYYNNPEATKETFDE 369
|
|
| PRK07656 |
PRK07656 |
long-chain-fatty-acid--CoA ligase; Validated |
1-293 |
9.50e-25 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236072 [Multi-domain] Cd Length: 513 Bit Score: 103.45 E-value: 9.50e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 758185221 1 AAFLPIDPD-TPEErIRYSLEDSGAK-------FAVVNERNMTAIGQYEgTIVSLDDGK----------W-----RNESK 57
Cdd:PRK07656 80 AVVVPLNTRyTADE-AAYILARGDAKalfvlglFLGVDYSATTRLPALE-HVVICETEEddphtekmktFtdflaAGDPA 157
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 758185221 58 ERPSSISGSrNLAYVIYTSGTAGKPKGVQIEHRNLT-NYVSWfSEEASLTENDKTVLLSSYASDLGYT-SMFPVLLGGGE 135
Cdd:PRK07656 158 ERAPEVDPD-DVADILFTSGTTGRPKGAMLTHRQLLsNAADW-AEYLGLTEGDRYLAANPFFHVFGYKaGVNAPLMRGAT 235
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 758185221 136 LHIVQKetyTAPDEIAHYIKEYGITYIKLTPSLFHTIVNTASfAKDANFESLRLIVLGGEKIIPTDVLAFRKIYGHTEFI 215
Cdd:PRK07656 236 ILPLPV---FDPDEVFRLIETERITVLPGPPTMYNSLLQHPD-RSAEDLSSLRLAVTGAASMPVALLERFESELGVDIVL 311
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 758185221 216 NHYGPTEAtigaiAGRVDLSEPDAFAKRP--TIGRPIANAGALVLNEALKLVPPGASGQLYITGQGLARGYLNRPQLTAE 293
Cdd:PRK07656 312 TGYGLSEA-----SGVTTFNRLDDDRKTVagTIGTAIAGVENKIVNELGEEVPVGEVGELLVRGPNVMKGYYDDPEATAA 386
|
|
| PRK06188 |
PRK06188 |
acyl-CoA synthetase; Validated |
59-295 |
2.28e-24 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 235731 [Multi-domain] Cd Length: 524 Bit Score: 102.37 E-value: 2.28e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 758185221 59 RPSSISGSRNLAYVIYTSGTAGKPKGVQIEHRNLTNYVSWFSEEASLTEnDKTVLLSSYASDLGYTSMFPVLLGGGELHI 138
Cdd:PRK06188 160 PLVAAALPPDIAGLAYTGGTTGKPKGVMGTHRSIATMAQIQLAEWEWPA-DPRFLMCTPLSHAGGAFFLPTLLRGGTVIV 238
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 758185221 139 VQKetyTAPDEIAHYIKEYGITYIKLTPSLFHTIVNTASFAkDANFESLRLIVLGGEKIIPTDVLAFRKIYGHTeFINHY 218
Cdd:PRK06188 239 LAK---FDPAEVLRAIEEQRITATFLVPTMIYALLDHPDLR-TRDLSSLETVYYGASPMSPVRLAEAIERFGPI-FAQYY 313
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 758185221 219 GPTEA--TIGAIAGRV-DLSEPDAFAkrpTIGRPIANAGALVLNEALKLVPPGASGQLYITGQGLARGYLNRPQLTAERF 295
Cdd:PRK06188 314 GQTEApmVITYLRKRDhDPDDPKRLT---SCGRPTPGLRVALLDEDGREVAQGEVGEICVRGPLVMDGYWNRPEETAEAF 390
|
|
| alpha_am_amid |
TIGR03443 |
L-aminoadipate-semialdehyde dehydrogenase; Members of this protein family are ... |
74-298 |
2.73e-24 |
|
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: 103.22 E-value: 2.73e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 758185221 74 YTSGTAGKPKGVQIEHRNLTNYVSWFSEEASLTENDKTVLLSSYASDLGYTSMFPVLLGGGELHIVQKETYTAPDEIAHY 153
Cdd:TIGR03443 422 FTSGSEGIPKGVLGRHFSLAYYFPWMAKRFGLSENDKFTMLSGIAHDPIQRDMFTPLFLGAQLLVPTADDIGTPGRLAEW 501
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 758185221 154 IKEYGITYIKLTPSLFHTIVNTASfakdANFESLRLIVLGGEKIIPTDVLAFRKIYGHTEFINHYGPTEA----TIGAIA 229
Cdd:TIGR03443 502 MAKYGATVTHLTPAMGQLLSAQAT----TPIPSLHHAFFVGDILTKRDCLRLQTLAENVCIVNMYGTTETqravSYFEIP 577
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 758185221 230 GRvdlSEPDAFAKR-----PTiGRPIANAGALVLN--EALKLVPPGASGQLYITGQGLARGYLNRPQLTAERFVEN 298
Cdd:TIGR03443 578 SR---SSDSTFLKNlkdvmPA-GKGMKNVQLLVVNrnDRTQTCGVGEVGEIYVRAGGLAEGYLGLPELNAEKFVNN 649
|
|
| PRK06187 |
PRK06187 |
long-chain-fatty-acid--CoA ligase; Validated |
10-296 |
2.67e-22 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 235730 [Multi-domain] Cd Length: 521 Bit Score: 96.41 E-value: 2.67e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 758185221 10 TPEErIRYSLEDSGAKFAVVNERNMTAIGQYEG------TIVSLDDGK-------------WRN-ESKERPSSISGSRNL 69
Cdd:PRK06187 91 KPEE-IAYILNDAEDRVVLVDSEFVPLLAAILPqlptvrTVIVEGDGPaaplapevgeyeeLLAaASDTFDFPDIDENDA 169
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 758185221 70 AYVIYTSGTAGKPKGVQIEHRNLTNYV----SWFSeeasLTENDktVLLS------SYASDLGYtsmFPVLLGGGelHIV 139
Cdd:PRK06187 170 AAMLYTSGTTGHPKGVVLSHRNLFLHSlavcAWLK----LSRDD--VYLVivpmfhVHAWGLPY---LALMAGAK--QVI 238
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 758185221 140 QKEtYtAPDEIAHYIKEYGITYIKLTPSLFHTIVNtASFAKDANFESLRLIVLGGEKIIPTDVLAFRKIYGhTEFINHYG 219
Cdd:PRK06187 239 PRR-F-DPENLLDLIETERVTFFFAVPTIWQMLLK-APRAYFVDFSSLRLVIYGGAALPPALLREFKEKFG-IDLVQGYG 314
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 758185221 220 PTEAT-IGAIAgRVDLSEPDAFAKRPTIGRPIANAGALVLNEALKLVPP--GASGQLYITGQGLARGYLNRPQLTAERFV 296
Cdd:PRK06187 315 MTETSpVVSVL-PPEDQLPGQWTKRRSAGRPLPGVEARIVDDDGDELPPdgGEVGEIIVRGPWLMQGYWNRPEATAETID 393
|
|
| BCL_like |
cd05919 |
Benzoate CoA ligase (BCL) and similar adenylate forming enzymes; This family contains benzoate ... |
69-303 |
4.22e-22 |
|
Benzoate CoA ligase (BCL) and similar adenylate forming enzymes; This family contains benzoate CoA ligase (BCL) and related ligases that catalyze the acylation of benzoate derivatives, 2-aminobenzoate and 4-hydroxybenzoate. Aromatic compounds represent the second most abundant class of organic carbon compounds after carbohydrates. Xenobiotic aromatic compounds are also a major class of man-made pollutants. Some bacteria use benzoate as the sole source of carbon and energy through benzoate degradation. Benzoate degradation starts with its activation to benzoyl-CoA by benzoate CoA ligase. The reaction catalyzed by benzoate CoA ligase proceeds via a two-step process; the first ATP-dependent step forms an acyl-AMP intermediate, and the second step forms the acyl-CoA ester with release of the AMP.
Pssm-ID: 341243 [Multi-domain] Cd Length: 436 Bit Score: 95.61 E-value: 4.22e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 758185221 69 LAYVIYTSGTAGKPKGVQIEHRNLTNYVSWFSEEA-SLTENDKTVLLSS--YASDLGYTSMFPVLLGGGelhIVQKETYT 145
Cdd:cd05919 93 IAYLLYSSGTTGPPKGVMHAHRDPLLFADAMAREAlGLTPGDRVFSSAKmfFGYGLGNSLWFPLAVGAS---AVLNPGWP 169
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 758185221 146 APDEIAHYIKEYGITYIKLTPSLFHTIVNTASFAKDAnFESLRLIVLGGEKIiPTDVLAFRKIYGHTEFINHYGPTEATI 225
Cdd:cd05919 170 TAERVLATLARFRPTVLYGVPTFYANLLDSCAGSPDA-LRSLRLCVSAGEAL-PRGLGERWMEHFGGPILDGIGATEVGH 247
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 758185221 226 GAIAGRVDLSEPDafakrpTIGRPIANAGALVLNEALKLVPPGASGQLYITGQGLARGYLNRPQLTAERFVENPYSPG 303
Cdd:cd05919 248 IFLSNRPGAWRLG------STGRPVPGYEIRLVDEEGHTIPPGEEGDLLVRGPSAAVGYWNNPEKSRATFNGGWYRTG 319
|
|
| Acs |
COG0365 |
Acyl-coenzyme A synthetase/AMP-(fatty) acid ligase [Lipid transport and metabolism]; |
70-297 |
1.92e-21 |
|
Acyl-coenzyme A synthetase/AMP-(fatty) acid ligase [Lipid transport and metabolism];
Pssm-ID: 440134 [Multi-domain] Cd Length: 565 Bit Score: 94.02 E-value: 1.92e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 758185221 70 AYVIYTSGTAGKPKGVQIEHRNLTNYVSWFSEEA-SLTENDktVLLssYASDLG------YTSMFPVLLGGGELHIVQKE 142
Cdd:COG0365 187 LFILYTSGTTGKPKGVVHTHGGYLVHAATTAKYVlDLKPGD--VFW--CTADIGwatghsYIVYGPLLNGATVVLYEGRP 262
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 758185221 143 TYTAPDEIAHYIKEYGITYIKLTPSLFHTIVNTA-SFAKDANFESLRLIVLGGEKIIPTdvlAFRKIYGHT--EFINHYG 219
Cdd:COG0365 263 DFPDPGRLWELIEKYGVTVFFTAPTAIRALMKAGdEPLKKYDLSSLRLLGSAGEPLNPE---VWEWWYEAVgvPIVDGWG 339
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 758185221 220 PTEaTIGAIAGRVDLSEPdafakRP-TIGRPIANAGALVLNEALKLVPPGASGQLYITGQ--GLARGYLNRPQLTAERFV 296
Cdd:COG0365 340 QTE-TGGIFISNLPGLPV-----KPgSMGKPVPGYDVAVVDEDGNPVPPGEEGELVIKGPwpGMFRGYWNDPERYRETYF 413
|
.
gi 758185221 297 E 297
Cdd:COG0365 414 G 414
|
|
| AAS_C |
cd05909 |
C-terminal domain of the acyl-acyl carrier protein synthetase (also called ... |
69-303 |
2.28e-21 |
|
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: 93.55 E-value: 2.28e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 758185221 69 LAYVIYTSGTAGKPKGVQIEHRNLTNYVSWFSEEASLTENDKTVLLSSYASDLGYTS--MFPVLLGggeLHIVQKETYTA 146
Cdd:cd05909 149 PAVILFTSGSEGLPKGVVLSHKNLLANVEQITAIFDPNPEDVVFGALPFFHSFGLTGclWLPLLSG---IKVVFHPNPLD 225
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 758185221 147 PDEIAHYIKEYGITYIKLTPSLFHTIVNtasFAKDANFESLRLIVLGGEKIIPTDVLAFRKIYGhTEFINHYGPTEAtig 226
Cdd:cd05909 226 YKKIPELIYDKKATILLGTPTFLRGYAR---AAHPEDFSSLRLVVAGAEKLKDTLRQEFQEKFG-IRILEGYGTTEC--- 298
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 758185221 227 aiAGRVDLSEPDAFAKRPTIGRPIANAGALVLN-EALKLVPPGASGQLYITGQGLARGYLNRPQLTAERFVENPYSPG 303
Cdd:cd05909 299 --SPVISVNTPQSPNKEGTVGRPLPGMEVKIVSvETHEEVPIGEGGLLLVRGPNVMLGYLNEPELTSFAFGDGWYDTG 374
|
|
| BCL_4HBCL |
cd05959 |
Benzoate CoA ligase (BCL) and 4-Hydroxybenzoate-Coenzyme A Ligase (4-HBA-CoA ligase); Benzoate ... |
4-296 |
2.75e-21 |
|
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: 93.59 E-value: 2.75e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 758185221 4 LPIDPDTPEERIRYSLEDSGAKFAVVN----ERNMTAIGQYEGTIVSLD--DGK------------WRNESKERPSSISG 65
Cdd:cd05959 82 VPVNTLLTPDDYAYYLEDSRARVVVVSgelaPVLAAALTKSEHTLVVLIvsGGAgpeagalllaelVAAEAEQLKPAATH 161
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 758185221 66 SRNLAYVIYTSGTAGKPKGVQIEHRNLTnyvsWFSEEAS-----LTENDktVLLSS----YASDLGYTSMFPVLLGGGEL 136
Cdd:cd05959 162 ADDPAFWLYSSGSTGRPKGVVHLHADIY----WTAELYArnvlgIREDD--VCFSAaklfFAYGLGNSLTFPLSVGATTV 235
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 758185221 137 HIVQKETytaPDEIAHYIKEYGITYIKLTPSLFHTIVNtASFAKDANFESLRLIVLGGEkIIPTDV-LAFRKIYGHtEFI 215
Cdd:cd05959 236 LMPERPT---PAAVFKRIRRYRPTVFFGVPTLYAAMLA-APNLPSRDLSSLRLCVSAGE-ALPAEVgERWKARFGL-DIL 309
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 758185221 216 NHYGPTEatigaiAGRVDLSE-PDafAKRP-TIGRPIANAGALVLNEALKLVPPGASGQLYITGQGLARGYLNRPQLTAE 293
Cdd:cd05959 310 DGIGSTE------MLHIFLSNrPG--RVRYgTTGKPVPGYEVELRDEDGGDVADGEPGELYVRGPSSATMYWNNRDKTRD 381
|
...
gi 758185221 294 RFV 296
Cdd:cd05959 382 TFQ 384
|
|
| FACL_DitJ_like |
cd05934 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
69-295 |
1.89e-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. Members of this family include DitJ from Pseudomonas and similar proteins.
Pssm-ID: 341257 [Multi-domain] Cd Length: 422 Bit Score: 90.81 E-value: 1.89e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 758185221 69 LAYVIYTSGTAGKPKGVQIEHRNLTNYVSWFSEEASLTENDktVLLSS---YASDLGYTSMFPVLLGGGELHIVqkETYT 145
Cdd:cd05934 83 PASILYTSGTTGPPKGVVITHANLTFAGYYSARRFGLGEDD--VYLTVlplFHINAQAVSVLAALSVGATLVLL--PRFS 158
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 758185221 146 APDEIAHyIKEYGITYIKLTPSLFHTIVNTASFAKDANfESLRLIvlGGEKIIPTDVLAFRKIYGhTEFINHYGPTEATI 225
Cdd:cd05934 159 ASRFWSD-VRRYGATVTNYLGAMLSYLLAQPPSPDDRA-HRLRAA--YGAPNPPELHEEFEERFG-VRLLEGYGMTETIV 233
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 758185221 226 GAIagrvdlSEPDAFAKRPTIGRPIANAGALVLNEALKLVPPGASGQLYIT---GQGLARGYLNRPQLTAERF 295
Cdd:cd05934 234 GVI------GPRDEPRRPGSIGRPAPGYEVRIVDDDGQELPAGEPGELVIRglrGWGFFKGYYNMPEATAEAM 300
|
|
| 4CL |
cd05904 |
4-Coumarate-CoA Ligase (4CL); 4-Coumarate:coenzyme A ligase is a key enzyme in the ... |
10-293 |
4.10e-20 |
|
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: 89.99 E-value: 4.10e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 758185221 10 TPEErIRYSLEDSGAKFAVVNERNMTAIGQYEGTIVSLDDGKWRNESKERPSSISGSRNLAYVI----------YTSGTA 79
Cdd:cd05904 92 TPAE-IAKQVKDSGAKLAFTTAELAEKLASLALPVVLLDSAEFDSLSFSDLLFEADEAEPPVVVikqddvaallYSSGTT 170
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 758185221 80 GKPKGVQIEHRNLTNYVSWF-SEEASLTENDKTVLLS-----SYasdlGYTSMFPVLLG-GGELHIVQKetYTAPDEIAH 152
Cdd:cd05904 171 GRSKGVMLTHRNLIAMVAQFvAGEGSNSDSEDVFLCVlpmfhIY----GLSSFALGLLRlGATVVVMPR--FDLEELLAA 244
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 758185221 153 yIKEYGITYIKLTPSLFHTIVNTASfAKDANFESLRLIVLGGEKIIPTDVLAFRKIYGHTEFINHYGPTEATigAIAGRV 232
Cdd:cd05904 245 -IERYKVTHLPVVPPIVLALVKSPI-VDKYDLSSLRQIMSGAAPLGKELIEAFRAKFPNVDLGQGYGMTEST--GVVAMC 320
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 758185221 233 DLSEPDAfAKRPTIGRPIANAGALVLN-EALKLVPPGASGQLYITGQGLARGYLNRPQLTAE 293
Cdd:cd05904 321 FAPEKDR-AKYGSVGRLVPNVEAKIVDpETGESLPPNQTGELWIRGPSIMKGYLNNPEATAA 381
|
|
| PRK08316 |
PRK08316 |
acyl-CoA synthetase; Validated |
10-295 |
5.78e-20 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 181381 [Multi-domain] Cd Length: 523 Bit Score: 89.61 E-value: 5.78e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 758185221 10 TPEErIRYSLEDSGAKFAVV------NERNMTAIGQYEGTIVSL------DDGKWRN-------ESKERPSSISGSRNLA 70
Cdd:PRK08316 96 TGEE-LAYILDHSGARAFLVdpalapTAEAALALLPVDTLILSLvlggreAPGGWLDfadwaeaGSVAEPDVELADDDLA 174
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 758185221 71 YVIYTSGTAGKPKGVQIEHRNLT-NYVSWFSEeASLTENDKTV-LLSSYASDLGYTSMFPVLLGGGELHIVQKETytaPD 148
Cdd:PRK08316 175 QILYTSGTESLPKGAMLTHRALIaEYVSCIVA-GDMSADDIPLhALPLYHCAQLDVFLGPYLYVGATNVILDAPD---PE 250
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 758185221 149 EIAHYIKEYGITYIKLTPSLFHTIVNTASFAKdANFESLRLIVLGGEkIIPTDVLA-FRKIYGHTEFINHYGPTE----A 223
Cdd:PRK08316 251 LILRTIEAERITSFFAPPTVWISLLRHPDFDT-RDLSSLRKGYYGAS-IMPVEVLKeLRERLPGLRFYNCYGQTEiaplA 328
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 758185221 224 TIgaiagrvdLSEPDAFAKRPTIGRPIANAGALVLNEALKLVPPGASGQLYITGQGLARGYLNRPQLTAERF 295
Cdd:PRK08316 329 TV--------LGPEEHLRRPGSAGRPVLNVETRVVDDDGNDVAPGEVGEIVHRSPQLMLGYWDDPEKTAEAF 392
|
|
| LC_FACS_like |
cd05935 |
Putative long-chain fatty acid CoA ligase; The members of this family are putative long-chain ... |
1-297 |
9.21e-20 |
|
Putative long-chain fatty acid CoA ligase; The members of this family are putative long-chain fatty acyl-CoA synthetases, which catalyze the ATP-dependent activation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. Fatty acyl-CoA synthetases are responsible for fatty acid degradation as well as physiological regulation of cellular functions via the production of fatty acyl-CoA esters.
Pssm-ID: 341258 [Multi-domain] Cd Length: 430 Bit Score: 88.69 E-value: 9.21e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 758185221 1 AAFLPIDPDTPEERIRYSLEDSGAKFAVVNErnmtaigqyegtivSLDDgkwrneskerpssisgsrnLAYVIYTSGTAG 80
Cdd:cd05935 51 AVVVPINPMLKERELEYILNDSGAKVAVVGS--------------ELDD-------------------LALIPYTSGTTG 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 758185221 81 KPKGVQIEHRNLTNYVSWFSEEASLTENDKTVLLSSYASDLGYT-SMFPVLLGGGELHIVQK-ETYTAPDEIahyiKEYG 158
Cdd:cd05935 98 LPKGCMHTHFSAAANALQSAVWTGLTPSDVILACLPLFHVTGFVgSLNTAVYVGGTYVLMARwDRETALELI----EKYK 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 758185221 159 ITYIKLTPSLFHTIVNTASFaKDANFESLRLIVLGGEKIIPTDVLAFRKIYGhTEFINHYGPTEaTIGAIAgrvdlSEPD 238
Cdd:cd05935 174 VTFWTNIPTMLVDLLATPEF-KTRDLSSLKVLTGGGAPMPPAVAEKLLKLTG-LRFVEGYGLTE-TMSQTH-----TNPP 245
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|
gi 758185221 239 AFAKRPTIGRPIANAGALVLN-EALKLVPPGASGQLYITGQGLARGYLNRPQLTAERFVE 297
Cdd:cd05935 246 LRPKLQCLGIP*FGVDARVIDiETGRELPPNEVGEIVVRGPQIFKGYWNRPEETEESFIE 305
|
|
| PLN02574 |
PLN02574 |
4-coumarate--CoA ligase-like |
60-298 |
1.24e-19 |
|
4-coumarate--CoA ligase-like
Pssm-ID: 215312 [Multi-domain] Cd Length: 560 Bit Score: 88.75 E-value: 1.24e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 758185221 60 PSSISGSRNLAYVIYTSGTAGKPKGVQIEHRNLTNYVSWFSE-EASLTENDKT--VLLSSYASDLGY-TSMFPV-LLGGG 134
Cdd:PLN02574 191 PKPVIKQDDVAAIMYSSGTTGASKGVVLTHRNLIAMVELFVRfEASQYEYPGSdnVYLAALPMFHIYgLSLFVVgLLSLG 270
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 758185221 135 ELHIVQKEtYTApDEIAHYIKEYGITYIKLTPSLFHTIVNTASFAKDANFESLRLIVLGGEKIIPTDVLAFRKIYGHTEF 214
Cdd:PLN02574 271 STIVVMRR-FDA-SDMVKVIDRFKVTHFPVVPPILMALTKKAKGVCGEVLKSLKQVSCGAAPLSGKFIQDFVQTLPHVDF 348
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 758185221 215 INHYGPTEATigAIAGRVDLSEpdAFAKRPTIGRPIANAGALVLN-EALKLVPPGASGQLYITGQGLARGYLNRPQLTAE 293
Cdd:PLN02574 349 IQGYGMTEST--AVGTRGFNTE--KLSKYSSVGLLAPNMQAKVVDwSTGCLLPPGNCGELWIQGPGVMKGYLNNPKATQS 424
|
....*
gi 758185221 294 RFVEN 298
Cdd:PLN02574 425 TIDKD 429
|
|
| CBAL |
cd05923 |
4-Chlorobenzoate-CoA ligase (CBAL); CBAL catalyzes the conversion of 4-chlorobenzoate (4-CB) ... |
5-303 |
1.90e-18 |
|
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: 85.25 E-value: 1.90e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 758185221 5 PIDPDTPEERIRYSLEDSGAKFAV--VNERNMTAIGQYEGTIVSLDD----GKWRNESKERPSSISGSRNLAYVIYTSGT 78
Cdd:cd05923 82 LINPRLKAAELAELIERGEMTAAViaVDAQVMDAIFQSGVRVLALSDlvglGEPESAGPLIEDPPREPEQPAFVFYTSGT 161
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 758185221 79 AGKPKGVQIEHRNLTNYVSWFSEEASLTENDKTVLLS--SYASDLGYTSMFPVLLGGGELHIVQkeTYTAPDEIAHYIKE 156
Cdd:cd05923 162 TGLPKGAVIPQRAAESRVLFMSTQAGLRHGRHNVVLGlmPLYHVIGFFAVLVAALALDGTYVVV--EEFDPADALKLIEQ 239
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 758185221 157 YGITYIKLTPSLFHTIVNTASFAKdANFESLRLIVLGGEKiIPTDVLafRKIYGH--TEFINHYGPTEATIGAIAgrvdl 234
Cdd:cd05923 240 ERVTSLFATPTHLDALAAAAEFAG-LKLSSLRHVTFAGAT-MPDAVL--ERVNQHlpGEKVNIYGTTEAMNSLYM----- 310
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 758185221 235 sePDafAKRPTIGRPIANAG---ALVLNEALKLVPPGASGQLYITGQGLA--RGYLNRPQLTAERFVENPYSPG 303
Cdd:cd05923 311 --RD--ARTGTEMRPGFFSEvriVRIGGSPDEALANGEEGELIVAAAADAafTGYLNQPEATAKKLQDGWYRTG 380
|
|
| CHC_CoA_lg |
cd05903 |
Cyclohexanecarboxylate-CoA ligase (also called cyclohex-1-ene-1-carboxylate:CoA ligase); ... |
1-303 |
2.16e-18 |
|
Cyclohexanecarboxylate-CoA ligase (also called cyclohex-1-ene-1-carboxylate:CoA ligase); Cyclohexanecarboxylate-CoA ligase activates the aliphatic ring compound, cyclohexanecarboxylate, for degradation. It catalyzes the synthesis of cyclohexanecarboxylate-CoA thioesters in a two-step reaction involving the formation of cyclohexanecarboxylate-AMP anhydride, followed by the nucleophilic substitution of AMP by CoA.
Pssm-ID: 341229 [Multi-domain] Cd Length: 437 Bit Score: 84.74 E-value: 2.16e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 758185221 1 AAFLPIDPDTPEERIRYSLEDSGAKFAVVNERnmtaigqyegtivslddgkWRnesKERPSSISGSrnLAYVIYTSGTAG 80
Cdd:cd05903 51 AVTNPILPFFREHELAFILRRAKAKVFVVPER-------------------FR---QFDPAAMPDA--VALLLFTSGTTG 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 758185221 81 KPKGVQIEHRNLTNYVSWFSEEASLTENDkTVLLSS---YASDLGYTSMFPVLLGGGelhIVQKETYTaPDEIAHYIKEY 157
Cdd:cd05903 107 EPKGVMHSHNTLSASIRQYAERLGLGPGD-VFLVASpmaHQTGFVYGFTLPLLLGAP---VVLQDIWD-PDKALALMREH 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 758185221 158 GITYIKLTPSLFHTIVNTASFAkDANFESLRLIVLGGEKIiPTDVLAFRKIYGHTEFINHYGPTEATigAIAGRVDLSEP 237
Cdd:cd05903 182 GVTFMMGATPFLTDLLNAVEEA-GEPLSRLRTFVCGGATV-PRSLARRAAELLGAKVCSAYGSTECP--GAVTSITPAPE 257
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 758185221 238 DAFAKrpTIGRPIANAGALVLNEALKLVPPGASGQLYITGQGLARGYLNRPQLTAERFVENPYSPG 303
Cdd:cd05903 258 DRRLY--TDGRPLPGVEIKVVDDTGATLAPGVEGELLSRGPSVFLGYLDRPDLTADAAPEGWFRTG 321
|
|
| MCS |
cd05941 |
Malonyl-CoA synthetase (MCS); MCS catalyzes the formation of malonyl-CoA in a two-step ... |
1-297 |
1.07e-17 |
|
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: 82.72 E-value: 1.07e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 758185221 1 AAFLPIDPDTPEERIRYSLEDSGAKFAVvnernmtaigqyegtivslddgkwrneskerpssisgsrNLAYVIYTSGTAG 80
Cdd:cd05941 62 GVAVPLNPSYPLAELEYVITDSEPSLVL---------------------------------------DPALILYTSGTTG 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 758185221 81 KPKGVQIEHRNLTNYVSWFSEEASLTENDktVLLSS----YASDLGYTSMFPvLLGGGELHIVQKETytaPDEIAHYIKE 156
Cdd:cd05941 103 RPKGVVLTHANLAANVRALVDAWRWTEDD--VLLHVlplhHVHGLVNALLCP-LFAGASVEFLPKFD---PKEVAISRLM 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 758185221 157 YGIT--------YIKLTPSLFHTIVNTASFAKDAnFESLRLIVlGGEKIIPTDVLA-FRKIYGHTeFINHYGPTEATIGa 227
Cdd:cd05941 177 PSITvfmgvptiYTRLLQYYEAHFTDPQFARAAA-AERLRLMV-SGSAALPVPTLEeWEAITGHT-LLERYGMTEIGMA- 252
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 758185221 228 iagrvdLSEPDAFAKRP-TIGRPIANAGA-LVLNEALKLVPPGASGQLYITGQGLARGYLNRPQLTAERFVE 297
Cdd:cd05941 253 ------LSNPLDGERRPgTVGMPLPGVQArIVDEETGEPLPRGEVGEIQVRGPSVFKEYWNKPEATKEEFTD 318
|
|
| PRK08633 |
PRK08633 |
2-acyl-glycerophospho-ethanolamine acyltransferase; Validated |
69-293 |
2.25e-17 |
|
2-acyl-glycerophospho-ethanolamine acyltransferase; Validated
Pssm-ID: 236315 [Multi-domain] Cd Length: 1146 Bit Score: 82.66 E-value: 2.25e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 758185221 69 LAYVIYTSGTAGKPKGVQIEHRNLTNYVSWFSEEASLTENDktVLLSS---YASdLGY--TSMFPVLLGGGelhivqkeT 143
Cdd:PRK08633 784 TATIIFSSGSEGEPKGVMLSHHNILSNIEQISDVFNLRNDD--VILSSlpfFHS-FGLtvTLWLPLLEGIK--------V 852
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 758185221 144 YTAPD-----EIAHYIKEYGITYIKLTPSLFHTIVNTASfAKDANFESLRLIVLGGEKiIPTDV-LAFRKIYGHtEFINH 217
Cdd:PRK08633 853 VYHPDptdalGIAKLVAKHRATILLGTPTFLRLYLRNKK-LHPLMFASLRLVVAGAEK-LKPEVaDAFEEKFGI-RILEG 929
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 758185221 218 YGPTEATigaiaGRVDLSEPDAFA---------KRPTIGRPIANAGALVLN-EALKLVPPGASGQLYITGQGLARGYLNR 287
Cdd:PRK08633 930 YGATETS-----PVASVNLPDVLAadfkrqtgsKEGSVGMPLPGVAVRIVDpETFEELPPGEDGLILIGGPQVMKGYLGD 1004
|
....*.
gi 758185221 288 PQLTAE 293
Cdd:PRK08633 1005 PEKTAE 1010
|
|
| FADD10 |
cd17635 |
adenylate forming domain, fatty acid CoA ligase (FadD10); This family contains long chain ... |
67-297 |
4.64e-17 |
|
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: 80.38 E-value: 4.64e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 758185221 67 RNLAYVIYTSGTAGKPKGVQIEHRNL-TNYVSWFSEEASLTENDKTVLLSSYASDLGYTSMFPVLLGGGeLHIVQKE--T 143
Cdd:cd17635 1 EDPLAVIFTSGTTGEPKAVLLANKTFfAVPDILQKEGLNWVVGDVTYLPLPATHIGGLWWILTCLIHGG-LCVTGGEntT 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 758185221 144 YTAPDEIahyIKEYGITYIKLTPSLFHTIVNtasFAKDAN--FESLRLIVLGGEKIIPTDVlAFRKIYGHTEFINHYGPT 221
Cdd:cd17635 80 YKSLFKI---LTTNAVTTTCLVPTLLSKLVS---ELKSANatVPSLRLIGYGGSRAIAADV-RFIEATGLTNTAQVYGLS 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 758185221 222 E-ATIGAIAGRVDLSEPDAfakrptIGRPIANAGALVLNEALKLVPPGASGQLYITGQGLARGYLNRPQLTAERFVE 297
Cdd:cd17635 153 EtGTALCLPTDDDSIEINA------VGRPYPGVDVYLAATDGIAGPSASFGTIWIKSPANMLGYWNNPERTAEVLID 223
|
|
| FACL_like_2 |
cd05917 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
74-293 |
6.72e-17 |
|
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ATP-dependent activation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions.
Pssm-ID: 341241 [Multi-domain] Cd Length: 349 Bit Score: 79.63 E-value: 6.72e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 758185221 74 YTSGTAGKPKGVQIEHRNLTNYVSWFSEEASLTENDKTV----LLSSYASDLGYTSMfpvlLGGGELHIVQKETYTAPDE 149
Cdd:cd05917 9 FTSGTTGSPKGATLTHHNIVNNGYFIGERLGLTEQDRLCipvpLFHCFGSVLGVLAC----LTHGATMVFPSPSFDPLAV 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 758185221 150 IaHYIKEYGITYIKLTPSLFHTIVNTASFAKdANFESLRLIVLGGeKIIPTDVL-AFRKIYGHTEFINHYGPTEATIGAI 228
Cdd:cd05917 85 L-EAIEKEKCTALHGVPTMFIAELEHPDFDK-FDLSSLRTGIMAG-APCPPELMkRVIEVMNMKDVTIAYGMTETSPVST 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 758185221 229 AGRVDlsepDAFAKR-PTIGRPIANAGALVLNEALKLVPP-GASGQLYITGQGLARGYLNRPQLTAE 293
Cdd:cd05917 162 QTRTD----DSIEKRvNTVGRIMPHTEAKIVDPEGGIVPPvGVPGELCIRGYSVMKGYWNDPEKTAE 224
|
|
| PRK06145 |
PRK06145 |
acyl-CoA synthetase; Validated |
1-303 |
1.81e-16 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 102207 [Multi-domain] Cd Length: 497 Bit Score: 79.54 E-value: 1.81e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 758185221 1 AAFLPIDPDTPEERIRYSLEDSGAKFAVVNERnMTAIGQYEGTIVSLDDGKWRNESK-------ERPSSISGSRNLAYVI 73
Cdd:PRK06145 77 AVFLPINYRLAADEVAYILGDAGAKLLLVDEE-FDAIVALETPKIVIDAAAQADSRRlaqggleIPPQAAVAPTDLVRLM 155
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 758185221 74 YTSGTAGKPKGVQIEHRNltnyVSWFSEEA----SLTENDKTVLLSSY----ASDLgytSMFPVLLGGGELHIVQKetyT 145
Cdd:PRK06145 156 YTSGTTDRPKGVMHSYGN----LHWKSIDHvialGLTASERLLVVGPLyhvgAFDL---PGIAVLWVGGTLRIHRE---F 225
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 758185221 146 APDEIAHYIKEYGITYIKLTPSLFHTIVnTASFAKDANFESLRLIVLGGEKIIPTDVLAFRKIYGHTEFINHYGPTEATI 225
Cdd:PRK06145 226 DPEAVLAAIERHRLTCAWMAPVMLSRVL-TVPDRDRFDLDSLAWCIGGGEKTPESRIRDFTRVFTRARYIDAYGLTETCS 304
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 758185221 226 GAI---AGRvdlsepdAFAKRPTIGRPIANAGALVLNEALKLVPPGASGQLYITGQGLARGYLNRPQLTAERFVENPYSP 302
Cdd:PRK06145 305 GDTlmeAGR-------EIEKIGSTGRALAHVEIRIADGAGRWLPPNMKGEICMRGPKVTKGYWKDPEKTAEAFYGDWFRS 377
|
.
gi 758185221 303 G 303
Cdd:PRK06145 378 G 378
|
|
| FACL_fum10p_like |
cd05926 |
Subfamily of fatty acid CoA ligase (FACL) similar to Fum10p of Gibberella moniliformis; FACL ... |
5-300 |
2.00e-16 |
|
Subfamily of fatty acid CoA ligase (FACL) similar to Fum10p of Gibberella moniliformis; FACL catalyzes the formation of fatty acyl-CoA in a two-step reaction: the formation of a fatty acyl-AMP molecule as an intermediate, followed by the formation of a fatty acyl-CoA. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions. Fum10p is a fatty acid CoA ligase involved in the synthesis of fumonisin, a polyketide mycotoxin, in Gibberella moniliformis.
Pssm-ID: 341249 [Multi-domain] Cd Length: 493 Bit Score: 79.28 E-value: 2.00e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 758185221 5 PIDPDTPEERIRYSLEDSGAKFAVV-NERNMTAI---GQYEGTIVSL--DDGKWRN--ESKERPSSISGSRN-------- 68
Cdd:cd05926 68 PLNPAYKKAEFEFYLADLGSKLVLTpKGELGPASraaSKLGLAILELalDVGVLIRapSAESLSNLLADKKNaksegvpl 147
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 758185221 69 ---LAYVIYTSGTAGKPKGVQIEHRNLTNYVSWFSEEASLTENDKTVLLssyasdlgyTSMF----------PVLLGGGE 135
Cdd:cd05926 148 pddLALILHTSGTTGRPKGVPLTHRNLAASATNITNTYKLTPDDRTLVV---------MPLFhvhglvasllSTLAAGGS 218
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 758185221 136 LHIvqketytAPDEIAH----YIKEYGITYIKLTPSLFHTIVNTASFAKDANFESLRLIVLGGEKIIPTDVLAFRKIYGh 211
Cdd:cd05926 219 VVL-------PPRFSAStfwpDVRDYNATWYTAVPTIHQILLNRPEPNPESPPPKLRFIRSCSASLPPAVLEALEATFG- 290
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 758185221 212 TEFINHYGPTEATIGAIAGRVDLSEPdafaKRPTIGRPiANAGALVLNEALKLVPPGASGQLYITGQGLARGYLNRPQLT 291
Cdd:cd05926 291 APVLEAYGMTEAAHQMTSNPLPPGPR----KPGSVGKP-VGVEVRILDEDGEILPPGVVGEICLRGPNVTRGYLNNPEAN 365
|
....*....
gi 758185221 292 AERFVENPY 300
Cdd:cd05926 366 AEAAFKDGW 374
|
|
| OSB_CoA_lg |
cd05912 |
O-succinylbenzoate-CoA ligase (also known as O-succinylbenzoate-CoA synthase, OSB-CoA ... |
70-298 |
2.18e-16 |
|
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: 78.93 E-value: 2.18e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 758185221 70 AYVIYTSGTAGKPKGVQIEHRNltnyvSWFSEEAS-----LTENDK--TVLLSSYASdlGYTSMFPVLLGGGELHIVQKe 142
Cdd:cd05912 80 ATIMYTSGTTGKPKGVQQTFGN-----HWWSAIGSalnlgLTEDDNwlCALPLFHIS--GLSILMRSVIYGMTVYLVDK- 151
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 758185221 143 tyTAPDEIAHYIKEYGITYIKLTPSLFHTIVntasfAKDANF--ESLRLIVLGGEKiIPTDVLAFRKIYGhTEFINHYGP 220
Cdd:cd05912 152 --FDAEQVLHLINSGKVTIISVVPTMLQRLL-----EILGEGypNNLRCILLGGGP-APKPLLEQCKEKG-IPVYQSYGM 222
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 758185221 221 TEATIGAIAgrvdLSEPDAFAKRPTIGRPIANAGALVLNEalkLVPPGASGQLYITGQGLARGYLNRPQLTAERFVEN 298
Cdd:cd05912 223 TETCSQIVT----LSPEDALNKIGSAGKPLFPVELKIEDD---GQPPYEVGEILLKGPNVTKGYLNRPDATEESFENG 293
|
|
| LC_FACS_like |
cd17640 |
Long-chain fatty acid CoA synthetase; This family includes long-chain fatty acid (C12-C20) CoA ... |
9-293 |
4.73e-16 |
|
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: 78.17 E-value: 4.73e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 758185221 9 DTPEERIRYSLEDSGAKFAVVNernmtaigqyegtivslddgkwrneskerpssiSGSRNLAYVIYTSGTAGKPKGVQIE 88
Cdd:cd17640 63 DSSVEELLYILNHSESVALVVE---------------------------------NDSDDLATIIYTSGTTGNPKGVMLT 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 758185221 89 HRNLTNYVSWFSEEASLTENDKTVLL----SSYASDLGYTsmfpVLLGGGElhivqkETYTAPDEIAHYIKEYGITYIKL 164
Cdd:cd17640 110 HANLLHQIRSLSDIVPPQPGDRFLSIlpiwHSYERSAEYF----IFACGCS------QAYTSIRTLKDDLKRVKPHYIVS 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 758185221 165 TPSLFHTI-------VNTASFAKDANFESLRLI-----VLGGEKIIPTDVLAFRKIYGhTEFINHYGPTEATIGAIAGRv 232
Cdd:cd17640 180 VPRLWESLysgiqkqVSKSSPIKQFLFLFFLSGgifkfGISGGGALPPHVDTFFEAIG-IEVLNGYGLTETSPVVSARR- 257
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 758185221 233 dLSEPdafaKRPTIGRPIANAGA-LVLNEALKLVPPGASGQLYITGQGLARGYLNRPQLTAE 293
Cdd:cd17640 258 -LKCN----VRGSVGRPLPGTEIkIVDPEGNVVLPPGEKGIVWVRGPQVMKGYYKNPEATSK 314
|
|
| PRK06839 |
PRK06839 |
o-succinylbenzoate--CoA ligase; |
10-293 |
5.27e-16 |
|
o-succinylbenzoate--CoA ligase;
Pssm-ID: 168698 [Multi-domain] Cd Length: 496 Bit Score: 77.98 E-value: 5.27e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 758185221 10 TPEERIrYSLEDSGAKFAVVNERNMTAIGQYEGTI-----VSLDDGKwRNESKERPSSISGSRNLAYVI-YTSGTAGKPK 83
Cdd:PRK06839 88 TENELI-FQLKDSGTTVLFVEKTFQNMALSMQKVSyvqrvISITSLK-EIEDRKIDNFVEKNESASFIIcYTSGTTGKPK 165
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 758185221 84 GVQIEHRNLTNYVSWFSEEASLTENDKT-VLLSSYasDLGYTSMF--PVLLGGGELHIVQKetyTAPDEIAHYIKEYGIT 160
Cdd:PRK06839 166 GAVLTQENMFWNALNNTFAIDLTMHDRSiVLLPLF--HIGGIGLFafPTLFAGGVIIVPRK---FEPTKALSMIEKHKVT 240
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 758185221 161 YIKLTPSLFHTIVNTASFAKdANFESLRLIVLGGEKIiPTDVLAFRKIYGHtEFINHYGPTEATIGAIAgrvdLSEPDAF 240
Cdd:PRK06839 241 VVMGVPTIHQALINCSKFET-TNLQSVRWFYNGGAPC-PEELMREFIDRGF-LFGQGFGMTETSPTVFM----LSEEDAR 313
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|...
gi 758185221 241 AKRPTIGRPIANAGALVLNEALKLVPPGASGQLYITGQGLARGYLNRPQLTAE 293
Cdd:PRK06839 314 RKVGSIGKPVLFCDYELIDENKNKVEVGEVGELLIRGPNVMKEYWNRPDATEE 366
|
|
| PRK13295 |
PRK13295 |
cyclohexanecarboxylate-CoA ligase; Reviewed |
65-292 |
5.53e-16 |
|
cyclohexanecarboxylate-CoA ligase; Reviewed
Pssm-ID: 171961 [Multi-domain] Cd Length: 547 Bit Score: 78.17 E-value: 5.53e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 758185221 65 GSRNLAYVIYTSGTAGKPKGVQIEHRNL-TNYVSwFSEEASLTENDKTVLLSSYASDLG--YTSMFPVLLGGgelHIVQK 141
Cdd:PRK13295 195 GPDDVTQLIYTSGTTGEPKGVMHTANTLmANIVP-YAERLGLGADDVILMASPMAHQTGfmYGLMMPVMLGA---TAVLQ 270
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 758185221 142 ETYTaPDEIAHYIKEYGITY-IKLTPSLfHTIVNTASfAKDANFESLRLIVLGGEKIIPTDVLAFRKIYGhTEFINHYGP 220
Cdd:PRK13295 271 DIWD-PARAAELIRTEGVTFtMASTPFL-TDLTRAVK-ESGRPVSSLRTFLCAGAPIPGALVERARAALG-AKIVSAWGM 346
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 758185221 221 TEAtigaiaGRVDLSEPDAFAKRP--TIGRPIANAGALVLNEALKLVPPGASGQLYITGQGLARGYLNRPQLTA 292
Cdd:PRK13295 347 TEN------GAVTLTKLDDPDERAstTDGCPLPGVEVRVVDADGAPLPAGQIGRLQVRGCSNFGGYLKRPQLNG 414
|
|
| A_NRPS_TubE_like |
cd05906 |
The adenylation domain (A domain) of a family of nonribosomal peptide synthetases (NRPSs) ... |
63-297 |
1.19e-15 |
|
The adenylation domain (A domain) of a family of nonribosomal peptide synthetases (NRPSs) synthesizing toxins and antitumor agents; The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino)-acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. This family includes NRPSs that synthesize toxins and antitumor agents; for example, TubE for Tubulysine, CrpA for cryptophycin, TdiA for terrequinone A, KtzG for kutzneride, and Vlm1/Vlm2 for Valinomycin. Nonribosomal peptide synthetases are large multifunctional enzymes which synthesize many therapeutically useful peptides. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and, in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.
Pssm-ID: 341232 [Multi-domain] Cd Length: 540 Bit Score: 76.94 E-value: 1.19e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 758185221 63 ISGSRNLAYVIYTSGTAGKPKGVQIEHRNLTNYVSWFSEEASLTENDktVLLSSYASD----LGYTSMFPVLLGGGELHI 138
Cdd:cd05906 163 QSRPDDLALLMLTSGSTGFPKAVPLTHRNILARSAGKIQHNGLTPQD--VFLNWVPLDhvggLVELHLRAVYLGCQQVHV 240
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 758185221 139 VQKETYTAPDEIAHYIKEYGITyIKLTPSLFHTIVNTASFA---KDANFESLRLIVLGGEKIIPTDVLAFRKI---YGHT 212
Cdd:cd05906 241 PTEEILADPLRWLDLIDRYRVT-ITWAPNFAFALLNDLLEEiedGTWDLSSLRYLVNAGEAVVAKTIRRLLRLlepYGLP 319
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 758185221 213 EFINH--YGPTEATIGAIAGRVDLSEP----DAFAKrptIGRPIANAGALVLNEALKLVPPGASGQLYITGQGLARGYLN 286
Cdd:cd05906 320 PDAIRpaFGMTETCSGVIYSRSFPTYDhsqaLEFVS---LGRPIPGVSMRIVDDEGQLLPEGEVGRLQVRGPVVTKGYYN 396
|
250
....*....|.
gi 758185221 287 RPQLTAERFVE 297
Cdd:cd05906 397 NPEANAEAFTE 407
|
|
| PRK08751 |
PRK08751 |
long-chain fatty acid--CoA ligase; |
68-293 |
1.22e-15 |
|
long-chain fatty acid--CoA ligase;
Pssm-ID: 181546 [Multi-domain] Cd Length: 560 Bit Score: 76.84 E-value: 1.22e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 758185221 68 NLAYVIYTSGTAGKPKGVQIEHRNLTNYV----SWFSEEASLTENDKTVL--LSSY------ASDLGYTSMfpvllgGGE 135
Cdd:PRK08751 209 DIAFLQYTGGTTGVAKGAMLTHRNLVANMqqahQWLAGTGKLEEGCEVVItaLPLYhifaltANGLVFMKI------GGC 282
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 758185221 136 LHIVqketyTAPDEIAHYIKE---YGITYIKLTPSLFHTIVNTASFAKdANFESLRlIVLGGEKIIPTDVLAFRKIYGHT 212
Cdd:PRK08751 283 NHLI-----SNPRDMPGFVKElkkTRFTAFTGVNTLFNGLLNTPGFDQ-IDFSSLK-MTLGGGMAVQRSVAERWKQVTGL 355
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 758185221 213 EFINHYGPTEATIGAIAGRVDLSEPDAfakrpTIGRPIANAGALVLNEALKLVPPGASGQLYITGQGLARGYLNRPQLTA 292
Cdd:PRK08751 356 TLVEAYGLTETSPAACINPLTLKEYNG-----SIGLPIPSTDACIKDDAGTVLAIGEIGELCIKGPQVMKGYWKRPEETA 430
|
.
gi 758185221 293 E 293
Cdd:PRK08751 431 K 431
|
|
| PRK06334 |
PRK06334 |
long chain fatty acid--[acyl-carrier-protein] ligase; Validated |
65-285 |
7.26e-15 |
|
long chain fatty acid--[acyl-carrier-protein] ligase; Validated
Pssm-ID: 180533 [Multi-domain] Cd Length: 539 Bit Score: 74.47 E-value: 7.26e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 758185221 65 GSRNLAYVIYTSGTAGKPKGVQIEHRNLTNyvswfSEEASL-----TENDktVLLS----SYASDLGYTSMFPVLLGgge 135
Cdd:PRK06334 181 DPEDVAVILFTSGTEKLPKGVPLTHANLLA-----NQRACLkffspKEDD--VMMSflppFHAYGFNSCTLFPLLSG--- 250
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 758185221 136 LHIVQKETYTAPDEIAHYIKEYGITYIKLTPSLFHTIVNTASfAKDANFESLRLIVLGGEKIIPTDVLAFRKIYGHTEFI 215
Cdd:PRK06334 251 VPVVFAYNPLYPKKIVEMIDEAKVTFLGSTPVFFDYILKTAK-KQESCLPSLRFVVIGGDAFKDSLYQEALKTFPHIQLR 329
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 758185221 216 NHYGPTEATigaiaGRVDLSEPDAFAKRPTIGRPIANAGALVLNEALKL-VPPGASGQLYITGQGLARGYL 285
Cdd:PRK06334 330 QGYGTTECS-----PVITINTVNSPKHESCVGMPIRGMDVLIVSEETKVpVSSGETGLVLTRGTSLFSGYL 395
|
|
| FadD3 |
cd17638 |
acyl-CoA synthetase FadD3 and similar proteins; This family contains long chain fatty acid CoA ... |
68-293 |
7.73e-15 |
|
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: 73.69 E-value: 7.73e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 758185221 68 NLAYVIYTSGTAGKPKGVQIEHR-NLTNYVSWfSEEASLTENDKTVLLSSYASDLGYTSMFPVLLGGGELhIVQKETYTa 146
Cdd:cd17638 1 DVSDIMFTSGTTGRSKGVMCAHRqTLRAAAAW-ADCADLTEDDRYLIINPFFHTFGYKAGIVACLLTGAT-VVPVAVFD- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 758185221 147 PDEIAHYIKEYGITYIKLTPSLFHTIVNTASfAKDANFESLRLIVLGGEKIIPTDVLAFRKIYGHTEFINHYGPTEatig 226
Cdd:cd17638 78 VDAILEAIERERITVLPGPPTLFQSLLDHPG-RKKFDLSSLRAAVTGAATVPVELVRRMRSELGFETVLTAYGLTE---- 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 758185221 227 aiAGRVDLSEP--DAFAKRPTIGRPIANAGalvlnealklVPPGASGQLYITGQGLARGYLNRPQLTAE 293
Cdd:cd17638 153 --AGVATMCRPgdDAETVATTCGRACPGFE----------VRIADDGEVLVRGYNVMQGYLDDPEATAE 209
|
|
| FAA1 |
COG1022 |
Long-chain acyl-CoA synthetase (AMP-forming) [Lipid transport and metabolism]; |
5-297 |
1.03e-14 |
|
Long-chain acyl-CoA synthetase (AMP-forming) [Lipid transport and metabolism];
Pssm-ID: 440645 [Multi-domain] Cd Length: 603 Bit Score: 74.37 E-value: 1.03e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 758185221 5 PIDPDTPEERIRYSLEDSGAKFAVV-NERNMTAIGQYEG------TIVSLDDGKWRNESK-------------------- 57
Cdd:COG1022 94 PIYPTSSAEEVAYILNDSGAKVLFVeDQEQLDKLLEVRDelpslrHIVVLDPRGLRDDPRllsldellalgrevadpael 173
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 758185221 58 -ERPSSISGSrNLAYVIYTSGTAGKPKGVQIEHRNLTNYVSWFSEEASLTENDKTVL---LS-SYASDLGYTSMFpvllG 132
Cdd:COG1022 174 eARRAAVKPD-DLATIIYTSGTTGRPKGVMLTHRNLLSNARALLERLPLGPGDRTLSflpLAhVFERTVSYYALA----A 248
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 758185221 133 GGELHIVQKetytaPDEIAHYIKEYGITYIKLTPSLFHTIVNT-------ASFAKDANFE-SLRLivlgGEKIIPT---- 200
Cdd:COG1022 249 GATVAFAES-----PDTLAEDLREVKPTFMLAVPRVWEKVYAGiqakaeeAGGLKRKLFRwALAV----GRRYARArlag 319
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 758185221 201 --------------DVLAFRKIY----GHTEF-----------INH------------YGPTEATiGAIAGRvdlsEPDA 239
Cdd:COG1022 320 kspslllrlkhalaDKLVFSKLRealgGRLRFavsggaalgpeLARffralgipvlegYGLTETS-PVITVN----RPGD 394
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*...
gi 758185221 240 FaKRPTIGRPIANAgalvlneALKLvppGASGQLYITGQGLARGYLNRPQLTAERFVE 297
Cdd:COG1022 395 N-RIGTVGPPLPGV-------EVKI---AEDGEILVRGPNVMKGYYKNPEATAEAFDA 441
|
|
| PRK08974 |
PRK08974 |
long-chain-fatty-acid--CoA ligase FadD; |
68-293 |
2.25e-14 |
|
long-chain-fatty-acid--CoA ligase FadD;
Pssm-ID: 236359 [Multi-domain] Cd Length: 560 Bit Score: 73.16 E-value: 2.25e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 758185221 68 NLAYVIYTSGTAGKPKGVQIEHRN-LTNY--VSWFSEEASLTENDKTV----LLSSYAsdLGYTSMFPVLLGGGELHIvq 140
Cdd:PRK08974 207 DLAFLQYTGGTTGVAKGAMLTHRNmLANLeqAKAAYGPLLHPGKELVVtalpLYHIFA--LTVNCLLFIELGGQNLLI-- 282
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 758185221 141 ketyTAPDEIAHYIKE---YGITYIKLTPSLFHTIVNTASFaKDANFESLRLIVLGGEKIIPTDVLAFRKIYGhTEFINH 217
Cdd:PRK08974 283 ----TNPRDIPGFVKElkkYPFTAITGVNTLFNALLNNEEF-QELDFSSLKLSVGGGMAVQQAVAERWVKLTG-QYLLEG 356
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 758185221 218 YGPTEATIGAIAGRVDLSEPDAfakrpTIGRPIANAGALVLNEALKLVPPGASGQLYITGQGLARGYLNRPQLTAE 293
Cdd:PRK08974 357 YGLTECSPLVSVNPYDLDYYSG-----SIGLPVPSTEIKLVDDDGNEVPPGEPGELWVKGPQVMLGYWQRPEATDE 427
|
|
| LC_FACL_like |
cd05914 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); The members of this family are ... |
1-298 |
3.55e-14 |
|
Uncharacterized subfamily of fatty acid CoA ligase (FACL); The members of this family are bacterial long-chain fatty acid CoA synthetase, most of which are as yet uncharacterized. LC-FACS catalyzes the formation of fatty acyl-CoA in a two-step reaction: the formation of a fatty acyl-AMP molecule as an intermediate, and the formation of a fatty acyl-CoA. Free fatty acids must be "activated" to their CoA thioesters before participating in most catabolic and anabolic reactions.
Pssm-ID: 341240 [Multi-domain] Cd Length: 463 Bit Score: 72.47 E-value: 3.55e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 758185221 1 AAFLPIDPDTPEERIRYSLEDSGAKFAVVNERnmtaigqyegtivslDDgkwrneskerpssisgsrnLAYVIYTSGTAG 80
Cdd:cd05914 57 AIAVPILAEFTADEVHHILNHSEAKAIFVSDE---------------DD-------------------VALINYTSGTTG 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 758185221 81 KPKGVQIEHRNLTNYVSWFSEEASLTENDKTVLLSSYASDLG--YTSMFPVLLGGgelHIV-------------QKETYT 145
Cdd:cd05914 103 NSKGVMLTYRNIVSNVDGVKEVVLLGKGDKILSILPLHHIYPltFTLLLPLLNGA---HVVfldkipsakiialAFAQVT 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 758185221 146 ------APDEIAHYIKEYGITYIKLTPSLF--HTIVNTASFAK-------DANFESLRLIVLGGEKIIPtDVLAFRKIYG 210
Cdd:cd05914 180 ptlgvpVPLVIEKIFKMDIIPKLTLKKFKFklAKKINNRKIRKlafkkvhEAFGGNIKEFVIGGAKINP-DVEEFLRTIG 258
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 758185221 211 HTeFINHYGPTEAtiGAIagrVDLSEPDAFaKRPTIGRPIANAGALVLNEAlklvPPGASGQLYITGQGLARGYLNRPQL 290
Cdd:cd05914 259 FP-YTIGYGMTET--API---ISYSPPNRI-RLGSAGKVIDGVEVRIDSPD----PATGEGEIIVRGPNVMKGYYKNPEA 327
|
....*...
gi 758185221 291 TAERFVEN 298
Cdd:cd05914 328 TAEAFDKD 335
|
|
| VL_LC_FACS_like |
cd05907 |
Long-chain fatty acid CoA synthetases and Bubblegum-like very long-chain fatty acid CoA ... |
5-300 |
3.75e-14 |
|
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: 72.24 E-value: 3.75e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 758185221 5 PIDPDTPEERIRYSLEDSGAKFAVVnernmtaigqyegtivslddgkwrneskerpssiSGSRNLAYVIYTSGTAGKPKG 84
Cdd:cd05907 59 PIYPTSSAEQIAYILNDSEAKALFV----------------------------------EDPDDLATIIYTSGTTGRPKG 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 758185221 85 VQIEHRNLTNYVSWFSEEASLTENDKTVL---LS-SYASDLGYtsMFPVLLGGgelHIVqketYTAPDE-IAHYIKEYGI 159
Cdd:cd05907 105 VMLSHRNILSNALALAERLPATEGDRHLSflpLAhVFERRAGL--YVPLLAGA---RIY----FASSAEtLLDDLSEVRP 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 758185221 160 TYIKLTPSLFHTIVNTASFAKD----------ANFESLRLIVLGGEKiIPTDVLAFRKIYGHTeFINHYGPTEaTIGAIA 229
Cdd:cd05907 176 TVFLAVPRVWEKVYAAIKVKAVpglkrklfdlAVGGRLRFAASGGAP-LPAELLHFFRALGIP-VYEGYGLTE-TSAVVT 252
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 758185221 230 grvdLSEPDAFaKRPTIGRPIANAGALVlnealklvppGASGQLYITGQGLARGYLNRPQLTAERFVENPY 300
Cdd:cd05907 253 ----LNPPGDN-RIGTVGKPLPGVEVRI----------ADDGEILVRGPNVMLGYYKNPEATAEALDADGW 308
|
|
| ttLC_FACS_AlkK_like |
cd12119 |
Fatty acyl-CoA synthetases similar to LC-FACS from Thermus thermophiles; This family includes ... |
68-296 |
7.79e-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. 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: 71.51 E-value: 7.79e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 758185221 68 NLAYVI-YTSGTAGKPKGVQIEHRNLtnyvswFSEEASLTENDkTVLLSSYASDLGYTSMFPV---------LLGGGELh 137
Cdd:cd12119 163 NTAAAIcYTSGTTGNPKGVVYSHRSL------VLHAMAALLTD-GLGLSESDVVLPVVPMFHVnawglpyaaAMVGAKL- 234
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 758185221 138 iVQKETYTAPDEIAHYIKEYGITYIKLTPSLFHTIVNTASfAKDANFESLRLIVLGGEKIIPTDVLAFRKIYghTEFINH 217
Cdd:cd12119 235 -VLPGPYLDPASLAELIEREGVTFAAGVPTVWQGLLDHLE-ANGRDLSSLRRVVIGGSAVPRSLIEAFEERG--VRVIHA 310
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 758185221 218 YGPTEA-TIGAIAGR----VDLSEPDAFAKRPTIGRPIANAGALVLNEALKLVP--PGASGQLYITGQGLARGYLNRPQL 290
Cdd:cd12119 311 WGMTETsPLGTVARPpsehSNLSEDEQLALRAKQGRPVPGVELRIVDDDGRELPwdGKAVGELQVRGPWVTKSYYKNDEE 390
|
....*.
gi 758185221 291 TAERFV 296
Cdd:cd12119 391 SEALTE 396
|
|
| caiC |
PRK08008 |
putative crotonobetaine/carnitine-CoA ligase; Validated |
70-293 |
1.38e-13 |
|
putative crotonobetaine/carnitine-CoA ligase; Validated
Pssm-ID: 181195 [Multi-domain] Cd Length: 517 Bit Score: 70.87 E-value: 1.38e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 758185221 70 AYVIYTSGTAGKPKGVQIEHRNLT---NYVSWfseEASLTENDktVLLS---SYASDLGYTSMFPVLLGGGELHIVQKet 143
Cdd:PRK08008 176 AEILFTSGTTSRPKGVVITHYNLRfagYYSAW---QCALRDDD--VYLTvmpAFHIDCQCTAAMAAFSAGATFVLLEK-- 248
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 758185221 144 YTApDEIAHYIKEYGITYIKLTPSLFHTIVNTASFAKDANFEsLR-----LIVLGGEKiiptdvLAFRKIYGhTEFINHY 218
Cdd:PRK08008 249 YSA-RAFWGQVCKYRATITECIPMMIRTLMVQPPSANDRQHC-LRevmfyLNLSDQEK------DAFEERFG-VRLLTSY 319
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 758185221 219 GPTEATIGAIAGRvdlsePDAFAKRPTIGRPIANAGALVLNEALKLVPPGASGQLYIT---GQGLARGYLNRPQLTAE 293
Cdd:PRK08008 320 GMTETIVGIIGDR-----PGDKRRWPSIGRPGFCYEAEIRDDHNRPLPAGEIGEICIKgvpGKTIFKEYYLDPKATAK 392
|
|
| MACS_like |
cd05972 |
Medium-chain acyl-CoA synthetase (MACS or ACSM); MACS catalyzes the two-step activation of ... |
10-303 |
3.29e-13 |
|
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: 69.29 E-value: 3.29e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 758185221 10 TPEErIRYSLEDSGAKFAVVNERNMtaigqyegtivslddgkwrneskerpssisgsrnlAYVIYTSGTAGKPKGVQIEH 89
Cdd:cd05972 60 GPKD-IEYRLEAAGAKAIVTDAEDP-----------------------------------ALIYFTSGTTGLPKGVLHTH 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 758185221 90 RNLTNYVSWFSEEASLTENDK--TVLLSSYASDLGYTSMFPVLLGggeLHIVqkeTYTA----PDEIAHYIKEYGITYIK 163
Cdd:cd05972 104 SYPLGHIPTAAYWLGLRPDDIhwNIADPGWAKGAWSSFFGPWLLG---ATVF---VYEGprfdAERILELLERYGVTSFC 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 758185221 164 LTPSLFHTI--VNTASFakdaNFESLRLIVLGGEKIIPTDVLAFRKIYGHTeFINHYGPTE--ATIGAIagrvdlsePDA 239
Cdd:cd05972 178 GPPTAYRMLikQDLSSY----KFSHLRLVVSAGEPLNPEVIEWWRAATGLP-IRDGYGQTEtgLTVGNF--------PDM 244
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 758185221 240 FAKRPTIGRPIANAGALVLNEALKLVPPGASGQLYI--TGQGLARGYLNRPQLTAERFVENPYSPG 303
Cdd:cd05972 245 PVKPGSMGRPTPGYDVAIIDDDGRELPPGEEGDIAIklPPPGLFLGYVGDPEKTEASIRGDYYLTG 310
|
|
| PRK06087 |
PRK06087 |
medium-chain fatty-acid--CoA ligase; |
53-292 |
6.18e-13 |
|
medium-chain fatty-acid--CoA ligase;
Pssm-ID: 180393 [Multi-domain] Cd Length: 547 Bit Score: 69.01 E-value: 6.18e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 758185221 53 RNESKERPSSISGSrNLAYVIYTSGTAGKPKGVQIEHRNLTnyvswFSEEA-----SLTENDkTVLLssyASDLGYTSMF 127
Cdd:PRK06087 174 DYEPLTTAITTHGD-ELAAVLFTSGTEGLPKGVMLTHNNIL-----ASERAycarlNLTWQD-VFMM---PAPLGHATGF 243
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 758185221 128 ------PVLLGGgelHIVQKETYTaPDEIAHYIKEYGITY-IKLTPSLFhTIVNTASfAKDANFESLRLIVLGGeKIIPT 200
Cdd:PRK06087 244 lhgvtaPFLIGA---RSVLLDIFT-PDACLALLEQQRCTCmLGATPFIY-DLLNLLE-KQPADLSALRFFLCGG-TTIPK 316
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 758185221 201 DVLafRKIYGH-TEFINHYGPTEATIGAIagrVDLSEPDAFAKRpTIGRPIANAGALVLNEALKLVPPGASGQLYITGQG 279
Cdd:PRK06087 317 KVA--RECQQRgIKLLSVYGSTESSPHAV---VNLDDPLSRFMH-TDGYAAAGVEIKVVDEARKTLPPGCEGEEASRGPN 390
|
250
....*....|...
gi 758185221 280 LARGYLNRPQLTA 292
Cdd:PRK06087 391 VFMGYLDEPELTA 403
|
|
| PRK07787 |
PRK07787 |
acyl-CoA synthetase; Validated |
1-297 |
7.36e-13 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236096 [Multi-domain] Cd Length: 471 Bit Score: 68.48 E-value: 7.36e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 758185221 1 AAFLPIDPDTPEERIRYSLEDSGAKfAVVNERNMTAIGqYEGTIVSLDDGKWRNESKERPSSIsgsrnlAYVIYTSGTAG 80
Cdd:PRK07787 70 VPVVPVPPDSGVAERRHILADSGAQ-AWLGPAPDDPAG-LPHVPVRLHARSWHRYPEPDPDAP------ALIVYTSGTTG 141
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 758185221 81 KPKGVQIEHRNLTNYVSWFSEEASLTENDKTV----LLSSYASDLGytsmfpvLLG----GGELHIVQKETytaPDEIAH 152
Cdd:PRK07787 142 PPKGVVLSRRAIAADLDALAEAWQWTADDVLVhglpLFHVHGLVLG-------VLGplriGNRFVHTGRPT---PEAYAQ 211
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 758185221 153 YIKEYGITYIKLtPSLFHTIVNTASFAKdaNFESLRLIVLGGEKIIPTDVLAFRKIYGHtEFINHYGPTEaTIGAIAGRV 232
Cdd:PRK07787 212 ALSEGGTLYFGV-PTVWSRIAADPEAAR--ALRGARLLVSGSAALPVPVFDRLAALTGH-RPVERYGMTE-TLITLSTRA 286
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 758185221 233 DlSEPdafakRP-TIGRPIANAGALVLNEALKLVPP-GAS-GQLYITGQGLARGYLNRPQLTAERFVE 297
Cdd:PRK07787 287 D-GER-----RPgWVGLPLAGVETRLVDEDGGPVPHdGETvGELQVRGPTLFDGYLNRPDATAAAFTA 348
|
|
| MACS_like_4 |
cd05969 |
Uncharacterized subfamily of Acetyl-CoA synthetase like family (ACS); This family is most ... |
12-303 |
9.17e-13 |
|
Uncharacterized subfamily of Acetyl-CoA synthetase like family (ACS); This family is most similar to acetyl-CoA synthetase. Acetyl-CoA synthetase (ACS) catalyzes the formation of acetyl-CoA from acetate, CoA, and ATP. Synthesis of acetyl-CoA is carried out in a two-step reaction. In the first step, the enzyme catalyzes the synthesis of acetyl-AMP intermediate from acetate and ATP. In the second step, acetyl-AMP reacts with CoA to produce acetyl-CoA. This enzyme is only present in bacteria.
Pssm-ID: 341273 [Multi-domain] Cd Length: 442 Bit Score: 68.30 E-value: 9.17e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 758185221 12 EERIRYSLEDSGAKFAVVNERnmtaigQYEGTivslddgkwrneSKERPssisgsrnlAYVIYTSGTAGKPKGVQIEHRN 91
Cdd:cd05969 61 PEAIRDRLENSEAKVLITTEE------LYERT------------DPEDP---------TLLHYTSGTTGTPKGVLHVHDA 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 758185221 92 LTNYvsWFSEEASLTENDKTVLLSSyaSDLGYTS-----MFPVLLGGgeLHIVQKETYTAPDEIAHYIKEYGITYIKLTP 166
Cdd:cd05969 114 MIFY--YFTGKYVLDLHPDDIYWCT--ADPGWVTgtvygIWAPWLNG--VTNVVYEGRFDAESWYGIIERVKVTVWYTAP 187
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 758185221 167 SLFHTIVNT-ASFAKDANFESLRLIVLGGEKIIPTDVLAFRKIYGhTEFINHYGPTEATIGAIAgrvdlSEPDAFAKRPT 245
Cdd:cd05969 188 TAIRMLMKEgDELARKYDLSSLRFIHSVGEPLNPEAIRWGMEVFG-VPIHDTWWQTETGSIMIA-----NYPCMPIKPGS 261
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|
gi 758185221 246 IGRPIANAGALVLNEALKLVPPGASGQLYITGQ--GLARGYLNRPQLTAERFVENPYSPG 303
Cdd:cd05969 262 MGKPLPGVKAAVVDENGNELPPGTKGILALKPGwpSMFRGIWNDEERYKNSFIDGWYLTG 321
|
|
| FACL_like_1 |
cd05910 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
70-292 |
9.72e-13 |
|
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ATP-dependent activation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions.
Pssm-ID: 341236 [Multi-domain] Cd Length: 457 Bit Score: 68.26 E-value: 9.72e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 758185221 70 AYVIYTSGTAGKPKGVQIEHRNLTNYVSWFSEEASLTENDKTV----LLSSYASDLGYTSMFPVLlgggelhIVQKETYT 145
Cdd:cd05910 88 AAILFTSGSTGTPKGVVYRHGTFAAQIDALRQLYGIRPGEVDLatfpLFALFGPALGLTSVIPDM-------DPTRPARA 160
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 758185221 146 APDEIAHYIKEYGITYIKLTPSLFHTiVNTASFAKDANFESLRLIVLGGEKIIPTDVLAFRKIYG-HTEFINHYGPTEA- 223
Cdd:cd05910 161 DPQKLVGAIRQYGVSIVFGSPALLER-VARYCAQHGITLPSLRRVLSAGAPVPIALAARLRKMLSdEAEILTPYGATEAl 239
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 758185221 224 TIGAIAGRVDLSEPDAFAKR---PTIGRPIA---------NAGALVLNEALKLVPPGASGQLYITGQGLARGYLNRPQLT 291
Cdd:cd05910 240 PVSSIGSRELLATTTAATSGgagTCVGRPIPgvrvriieiDDEPIAEWDDTLELPRGEIGEITVTGPTVTPTYVNRPVAT 319
|
.
gi 758185221 292 A 292
Cdd:cd05910 320 A 320
|
|
| PRK08314 |
PRK08314 |
long-chain-fatty-acid--CoA ligase; Validated |
1-297 |
1.55e-12 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236235 [Multi-domain] Cd Length: 546 Bit Score: 67.68 E-value: 1.55e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 758185221 1 AAFLPIDPDTPEERIRYSLEDSGAKFAVVN----ERNMTAIG----------QYEGTI-----VSLDDG----------- 50
Cdd:PRK08314 86 AVVVPVNPMNREEELAHYVTDSGARVAIVGselaPKVAPAVGnlrlrhvivaQYSDYLpaepeIAVPAWlraepplqala 165
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 758185221 51 -----KWRNESKER---PSSISGSRNLAYVIYTSGTAGKPKGVQIEHRNL-TNYVS---WFSEEASltendkTVLLSSya 118
Cdd:PRK08314 166 pggvvAWKEALAAGlapPPHTAGPDDLAVLPYTSGTTGVPKGCMHTHRTVmANAVGsvlWSNSTPE------SVVLAV-- 237
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 758185221 119 sdlgyTSMFPV----------LLGGGELHIVQK-ETYTAPDEIAHYikeyGITYIKLTPSLFHTIVNTASFAkDANFESL 187
Cdd:PRK08314 238 -----LPLFHVtgmvhsmnapIYAGATVVLMPRwDREAAARLIERY----RVTHWTNIPTMVVDFLASPGLA-ERDLSSL 307
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 758185221 188 RLIVlGGEKIIPTDVLafRKIYGHT--EFINHYGPTEaTIGAIagrvdLSEPDAFAKRPTIGRPIANAGALVLN-EALKL 264
Cdd:PRK08314 308 RYIG-GGGAAMPEAVA--ERLKELTglDYVEGYGLTE-TMAQT-----HSNPPDRPKLQCLGIPTFGVDARVIDpETLEE 378
|
330 340 350
....*....|....*....|....*....|...
gi 758185221 265 VPPGASGQLYITGQGLARGYLNRPQLTAERFVE 297
Cdd:PRK08314 379 LPPGEVGEIVVHGPQVFKGYWNRPEATAEAFIE 411
|
|
| PRK03640 |
PRK03640 |
o-succinylbenzoate--CoA ligase; |
10-296 |
2.69e-12 |
|
o-succinylbenzoate--CoA ligase;
Pssm-ID: 235146 [Multi-domain] Cd Length: 483 Bit Score: 66.91 E-value: 2.69e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 758185221 10 TPEErIRYSLEDSGAKFAVVNERNMTAI-GQYEGTIVSLDDGKWRNESKERPSSISgsrNLAYVIYTSGTAGKPKGVQIE 88
Cdd:PRK03640 87 SREE-LLWQLDDAEVKCLITDDDFEAKLiPGISVKFAELMNGPKEEAEIQEEFDLD---EVATIMYTSGTTGKPKGVIQT 162
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 758185221 89 HRNltnyvSWFSEEAS-----LTENDK--TVLLSSYASdlGYTSMFPVLLGGGELHIVQKetYTApDEIAHYIKEYGITY 161
Cdd:PRK03640 163 YGN-----HWWSAVGSalnlgLTEDDCwlAAVPIFHIS--GLSILMRSVIYGMRVVLVEK--FDA-EKINKLLQTGGVTI 232
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 758185221 162 IKLTPSLFHTIVntASFAKDANFESLRLIVLGGEKiIPTDVLAFRKIYGhTEFINHYGPTEaTIGAIagrVDLSEPDAFA 241
Cdd:PRK03640 233 ISVVSTMLQRLL--ERLGEGTYPSSFRCMLLGGGP-APKPLLEQCKEKG-IPVYQSYGMTE-TASQI---VTLSPEDALT 304
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*
gi 758185221 242 KRPTIGRPIANAGaLVLNEALKLVPPGASGQLYITGQGLARGYLNRPQLTAERFV 296
Cdd:PRK03640 305 KLGSAGKPLFPCE-LKIEKDGVVVPPFEEGEIVVKGPNVTKGYLNREDATRETFQ 358
|
|
| PRK07786 |
PRK07786 |
long-chain-fatty-acid--CoA ligase; Validated |
10-295 |
4.29e-12 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 169098 [Multi-domain] Cd Length: 542 Bit Score: 66.34 E-value: 4.29e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 758185221 10 TPEErIRYSLEDSGAKfAVVNE----------RN--------MTAIGQYEGTIVSLDDGKWRNESKERPSSISGSrNLAY 71
Cdd:PRK07786 102 TPPE-IAFLVSDCGAH-VVVTEaalapvatavRDivpllstvVVAGGSSDDSVLGYEDLLAEAGPAHAPVDIPND-SPAL 178
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 758185221 72 VIYTSGTAGKPKGVQIEHRNLTNYVSWFSEEASLTENDKTVLLSS---YASDLGytSMFPVLLGGGELHIVQKETYTaPD 148
Cdd:PRK07786 179 IMYTSGTTGRPKGAVLTHANLTGQAMTCLRTNGADINSDVGFVGVplfHIAGIG--SMLPGLLLGAPTVIYPLGAFD-PG 255
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 758185221 149 EIAHYIKEYGITYIKLTPSLFHTIVnTASFAKDANFeSLRLIVLGGEKIIPTDVLAFRKIYGHTEFINHYGPTEAT-IGA 227
Cdd:PRK07786 256 QLLDVLEAEKVTGIFLVPAQWQAVC-AEQQARPRDL-ALRVLSWGAAPASDTLLRQMAATFPEAQILAAFGQTEMSpVTC 333
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 758185221 228 IagrvdLSEPDAFAKRPTIGRPIANAGALVLNEALKLVPPGASGQLYITGQGLARGYLNRPQLTAERF 295
Cdd:PRK07786 334 M-----LLGEDAIRKLGSVGKVIPTVAARVVDENMNDVPVGEVGEIVYRAPTLMSGYWNNPEATAEAF 396
|
|
| PRK06060 |
PRK06060 |
p-hydroxybenzoic acid--AMP ligase FadD22; |
70-289 |
8.35e-12 |
|
p-hydroxybenzoic acid--AMP ligase FadD22;
Pssm-ID: 180374 [Multi-domain] Cd Length: 705 Bit Score: 65.44 E-value: 8.35e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 758185221 70 AYVIYTSGTAGKPKGVQIEHRNLTNYVSWFSEEA-SLTENDktVLLSS----YASDLGYTSMFPVLLGGGElhIVQKETY 144
Cdd:PRK06060 148 AYATYTSGTTGPPKAAIHRHADPLTFVDAMCRKAlRLTPED--TGLCSarmyFAYGLGNSVWFPLATGGSA--VINSAPV 223
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 758185221 145 TApdEIAHYIKE-------YGItyikltPSLFHTIVNTASfakDANFESLRLIVLGGEKIIPTDVLAFRKIYGHTEFINH 217
Cdd:PRK06060 224 TP--EAAAILSArfgpsvlYGV------PNFFARVIDSCS---PDSFRSLRCVVSAGEALELGLAERLMEFFGGIPILDG 292
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 758185221 218 YGPTEATIGAIAGRVDLSEPDAFAK--RPTIGRPIANAGAlvlnealkLVPPGASGQLYITGQGLARGYLNRPQ 289
Cdd:PRK06060 293 IGSTEVGQTFVSNRVDEWRLGTLGRvlPPYEIRVVAPDGT--------TAGPGVEGDLWVRGPAIAKGYWNRPD 358
|
|
| PRK07768 |
PRK07768 |
long-chain-fatty-acid--CoA ligase; Validated |
23-285 |
2.92e-11 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236091 [Multi-domain] Cd Length: 545 Bit Score: 63.86 E-value: 2.92e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 758185221 23 GAKFAVVNERNMTAIGQYEG---TIVSLDDgKWRNESKERPSSisGSRNLAYVIYTSGTAGKPKGVQIEHRNLTNYVSWF 99
Cdd:PRK07768 108 GAKAVVVGEPFLAAAPVLEEkgiRVLTVAD-LLAADPIDPVET--GEDDLALMQLTSGSTGSPKAVQITHGNLYANAEAM 184
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 758185221 100 SEEASLTEnDKTVLLS--SYASDLGYTSMF--PVLLGGGELHIVQKETYTAPDEIAHYIKEYGITyIKLTPSLFHTIVNT 175
Cdd:PRK07768 185 FVAAEFDV-ETDVMVSwlPLFHDMGMVGFLtvPMYFGAELVKVTPMDFLRDPLLWAELISKYRGT-MTAAPNFAYALLAR 262
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 758185221 176 --ASFAKDANFE--SLRLIVLGGEKIIPTDVLAF-----RKIYGHTEFINHYGPTEATIGAIAG------RVDLSEPDAF 240
Cdd:PRK07768 263 rlRRQAKPGAFDlsSLRFALNGAEPIDPADVEDLldagaRFGLRPEAILPAYGMAEATLAVSFSpcgaglVVDEVDADLL 342
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*....
gi 758185221 241 A--------------KRPTIGRPIANAGALVLNEALKLVPPGASGQLYITGQGLARGYL 285
Cdd:PRK07768 343 AalrravpatkgntrRLATLGPPLPGLEVRVVDEDGQVLPPRGVGVIELRGESVTPGYL 401
|
|
| ACS-like |
cd17634 |
acetate-CoA ligase; This family includes acyl- and aryl-CoA ligases, as well as the ... |
28-301 |
3.52e-11 |
|
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: 63.75 E-value: 3.52e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 758185221 28 VVNERNMTAIGQYEGTIVSLDDGKWRNESKERPSSISGSRNLaYVIYTSGTAGKPKGVQIEHRNLTNYVSW-FSEEASLT 106
Cdd:cd17634 194 IVLKRTGSDIDWQEGRDLWWRDLIAKASPEHQPEAMNAEDPL-FILYTSGTTGKPKGVLHTTGGYLVYAATtMKYVFDYG 272
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 758185221 107 ENDktvlLSSYASDLG------YTSMFPVLLGGGELHIVQKETYTAPDEIAHYIKEYGITYIKLTPSLFHTIVNTASFA- 179
Cdd:cd17634 273 PGD----IYWCTADVGwvtghsYLLYGPLACGATTLLYEGVPNWPTPARMWQVVDKHGVNILYTAPTAIRALMAAGDDAi 348
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 758185221 180 KDANFESLRLIVLGGEKIIPTDVLAFRKIYGHTE--FINHYGPTEATIGAIAGRVDLSEPDafAKRPTigRPIANAGALV 257
Cdd:cd17634 349 EGTDRSSLRILGSVGEPINPEAYEWYWKKIGKEKcpVVDTWWQTETGGFMITPLPGAIELK--AGSAT--RPVFGVQPAV 424
|
250 260 270 280
....*....|....*....|....*....|....*....|....*.
gi 758185221 258 LNEALKLVPPGASGQLYITGQ--GLARGYLNRPqltaERFVENPYS 301
Cdd:cd17634 425 VDNEGHPQPGGTEGNLVITDPwpGQTRTLFGDH----ERFEQTYFS 466
|
|
| LC-FACS_euk |
cd05927 |
Eukaryotic long-chain fatty acid CoA synthetase (LC-FACS); The members of this family are ... |
68-298 |
7.74e-11 |
|
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: 62.62 E-value: 7.74e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 758185221 68 NLAYVIYTSGTAGKPKGVQIEHRNLTNYVSWFSEEA----SLTENDktvllsSYASDLGYTSMFP------VLLGGGELH 137
Cdd:cd05927 115 DLATICYTSGTTGNPKGVMLTHGNIVSNVAGVFKILeilnKINPTD------VYISYLPLAHIFErvvealFLYHGAKIG 188
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 758185221 138 IVQKETYTAPDEiahyIKEYGITYIKLTPSLFH------------------TIVNTASFAKDANFES------------- 186
Cdd:cd05927 189 FYSGDIRLLLDD----IKALKPTVFPGVPRVLNriydkifnkvqakgplkrKLFNFALNYKLAELRSgvvraspfwdklv 264
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 758185221 187 -----------LRLIVLGGEKIIPTDVLAFRKIYGhTEFINHYGPTEATIGAIagrvdLSEPDAFAKrPTIGRPIANaga 255
Cdd:cd05927 265 fnkikqalggnVRLMLTGSAPLSPEVLEFLRVALG-CPVLEGYGQTECTAGAT-----LTLPGDTSV-GHVGGPLPC--- 334
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|..
gi 758185221 256 lvlNEA-LKLVP--------PGASGQLYITGQGLARGYLNRPQLTAERFVEN 298
Cdd:cd05927 335 ---AEVkLVDVPemnydakdPNPRGEVCIRGPNVFSGYYKDPEKTAEALDED 383
|
|
| PRK05605 |
PRK05605 |
long-chain-fatty-acid--CoA ligase; Validated |
69-303 |
2.16e-10 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 235531 [Multi-domain] Cd Length: 573 Bit Score: 61.17 E-value: 2.16e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 758185221 69 LAYVIYTSGTAGKPKGVQIEHRNL-TNYV---SWFSEeasLTENDKTVL-----LSSYASDLGYTsmFPVLLGGgELHIV 139
Cdd:PRK05605 221 VALILYTSGTTGKPKGAQLTHRNLfANAAqgkAWVPG---LGDGPERVLaalpmFHAYGLTLCLT--LAVSIGG-ELVLL 294
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 758185221 140 QKetyTAPDEIAHYIKEYGITYIKLTPSLFHTIVNTASfAKDANFESLRLIVLGGEKIIPTDVLAFRKIYGhTEFINHYG 219
Cdd:PRK05605 295 PA---PDIDLILDAMKKHPPTWLPGVPPLYEKIAEAAE-ERGVDLSGVRNAFSGAMALPVSTVELWEKLTG-GLLVEGYG 369
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 758185221 220 PTEaTIGAIAGrvdlsEPDAFAKRP-TIGRPIANAGALVLN-EAL-KLVPPGASGQLYITGQGLARGYLNRPQLTAERFV 296
Cdd:PRK05605 370 LTE-TSPIIVG-----NPMSDDRRPgYVGVPFPDTEVRIVDpEDPdETMPDGEEGELLVRGPQVFKGYWNRPEETAKSFL 443
|
....*..
gi 758185221 297 ENPYSPG 303
Cdd:PRK05605 444 DGWFRTG 450
|
|
| FAAL |
cd05931 |
Fatty acyl-AMP ligase (FAAL); FAAL belongs to the class I adenylate forming enzyme family and ... |
1-295 |
3.43e-10 |
|
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: 60.33 E-value: 3.43e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 758185221 1 AAFL----------PIDPDTPE---ERIRYSLEDSGAKFAVVNERNMTAIGQYEGTIVSLDDGKWR-----NESKERPSS 62
Cdd:cd05931 63 AAFLgclyagaiavPLPPPTPGrhaERLAAILADAGPRVVLTTAAALAAVRAFAASRPAAGTPRLLvvdllPDTSAADWP 142
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 758185221 63 IS--GSRNLAYVIYTSGTAGKPKGVQIEHRNLTNYVSWFSEEASLTENDKTVLLSSYASDLG--YTSMFPVLLGGgelHI 138
Cdd:cd05931 143 PPspDPDDIAYLQYTSGSTGTPKGVVVTHRNLLANVRQIRRAYGLDPGDVVVSWLPLYHDMGliGGLLTPLYSGG---PS 219
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 758185221 139 VqketYTAPdeiAHYIKEygityikltPSLF------HTIVNTA--SFA--------KDANFE-----SLRLIVLGGEKI 197
Cdd:cd05931 220 V----LMSP---AAFLRR---------PLRWlrlisrYRATISAapNFAydlcvrrvRDEDLEgldlsSWRVALNGAEPV 283
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 758185221 198 IPTDVLAFRKI---YG--HTEFINHYGPTEATI---GAIAG---RVDLSEPDAFAKRPTI--------------GRPIAN 252
Cdd:cd05931 284 RPATLRRFAEAfapFGfrPEAFRPSYGLAEATLfvsGGPPGtgpVVLRVDRDALAGRAVAvaaddpaarelvscGRPLPD 363
|
330 340 350 360
....*....|....*....|....*....|....*....|....
gi 758185221 253 AGALVLNEA-LKLVPPGASGQLYITGQGLARGYLNRPQLTAERF 295
Cdd:cd05931 364 QEVRIVDPEtGRELPDGEVGEIWVRGPSVASGYWGRPEATAETF 407
|
|
| PRK06710 |
PRK06710 |
long-chain-fatty-acid--CoA ligase; Validated |
52-292 |
4.44e-10 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 180666 [Multi-domain] Cd Length: 563 Bit Score: 60.05 E-value: 4.44e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 758185221 52 WRNESKERPSSIS----GSRNLAYVIYTSGTAGKPKGVQIEHRNLTNY----VSWFSeeaSLTENDKTVL-LSSYASDLG 122
Cdd:PRK06710 187 WNSVEKEVNTGVEvpcdPENDLALLQYTGGTTGFPKGVMLTHKNLVSNtlmgVQWLY---NCKEGEEVVLgVLPFFHVYG 263
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 758185221 123 YTSMFPV-LLGGGELHIVQKETYTApdeIAHYIKEYGITYIKLTPSLFHTIVNTAsFAKDANFESLRLIVlGGEKIIPTD 201
Cdd:PRK06710 264 MTAVMNLsIMQGYKMVLIPKFDMKM---VFEAIKKHKVTLFPGAPTIYIALLNSP-LLKEYDISSIRACI-SGSAPLPVE 338
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 758185221 202 VL-AFRKIYGhTEFINHYGPTEATIGAIAGRVdlsepdaFAKR--PTIGRPIANAGALVLN-EALKLVPPGASGQLYITG 277
Cdd:PRK06710 339 VQeKFETVTG-GKLVEGYGLTESSPVTHSNFL-------WEKRvpGSIGVPWPDTEAMIMSlETGEALPPGEIGEIVVKG 410
|
250
....*....|....*
gi 758185221 278 QGLARGYLNRPQLTA 292
Cdd:PRK06710 411 PQIMKGYWNKPEETA 425
|
|
| PRK07638 |
PRK07638 |
acyl-CoA synthetase; Validated |
4-293 |
5.36e-10 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236071 [Multi-domain] Cd Length: 487 Bit Score: 59.79 E-value: 5.36e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 758185221 4 LPIDPDTPEERIRYSLEDSGAKFAVVNERNMTAIGQYEGTIVSLDdgKWR---NESKERPSSISGSRNLA-YVIYTSGTA 79
Cdd:PRK07638 78 VPLDIKWKQDELKERLAISNADMIVTERYKLNDLPDEEGRVIEID--EWKrmiEKYLPTYAPIENVQNAPfYMGFTSGST 155
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 758185221 80 GKPKGVQIEHRNLTNYVSWFSEEASLTENDKTVLLSSYASDLGYTSMFPVLLGGGELHIVQKETytaPDEIAHYIKEYGI 159
Cdd:PRK07638 156 GKPKAFLRAQQSWLHSFDCNVHDFHMKREDSVLIAGTLVHSLFLYGAISTLYVGQTVHLMRKFI---PNQVLDKLETENI 232
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 758185221 160 TYIKLTPSLfhtivnTASFAKDANF-ESLRLIVLGGEKIIPTDVLAFRKIYGHTEFINHYGPTEATIgaiagrVDLSEPD 238
Cdd:PRK07638 233 SVMYTVPTM------LESLYKENRViENKMKIISSGAKWEAEAKEKIKNIFPYAKLYEFYGASELSF------VTALVDE 300
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*.
gi 758185221 239 AFAKRPT-IGRPIANAGALVLNEALKLVPPGASGQLYITGQGLARGYLNRPQLTAE 293
Cdd:PRK07638 301 ESERRPNsVGRPFHNVQVRICNEAGEEVQKGEIGTVYVKSPQFFMGYIIGGVLARE 356
|
|
| PRK13383 |
PRK13383 |
acyl-CoA synthetase; Provisional |
55-284 |
5.51e-10 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 139531 [Multi-domain] Cd Length: 516 Bit Score: 60.01 E-value: 5.51e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 758185221 55 ESKERPSSISGSRnlaYVIYTSGTAGKPKGVQIEHRNLTNYVSWFS--EEASLTENDKTVLLSSYASDLGYTS-MFPVLL 131
Cdd:PRK13383 165 ESGGRPAVAAPGR---IVLLTSGTTGKPKGVPRAPQLRSAVGVWVTilDRTRLRTGSRISVAMPMFHGLGLGMlMLTIAL 241
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 758185221 132 GGGelhIVQKETYTAPDEIAHYI--KEYGITYIkltPSLFHTIVNTASFAKDAN-FESLRLIVLGGEKIIPTDVLAFRKI 208
Cdd:PRK13383 242 GGT---VLTHRHFDAEAALAQASlhRADAFTAV---PVVLARILELPPRVRARNpLPQLRVVMSSGDRLDPTLGQRFMDT 315
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 758185221 209 YGHTEFiNHYGPTEATIGAIAGRVDLSE-PDafakrpTIGRPIANAGALVLNEALKLVPPGASGQLYITGQGLARGY 284
Cdd:PRK13383 316 YGDILY-NGYGSTEVGIGALATPADLRDaPE------TVGKPVAGCPVRILDRNNRPVGPRVTGRIFVGGELAGTRY 385
|
|
| ACLS-CaiC |
cd17637 |
acyl-CoA synthetase (AMP-forming)/AMP-acid ligase II; This family contains fatty acid CoA ... |
72-295 |
6.68e-10 |
|
acyl-CoA synthetase (AMP-forming)/AMP-acid ligase II; This family contains fatty acid CoA ligases, including acyl-CoA synthetase (AMP-forming)/AMP-acid ligase II, most of which are yet to be characterized, but may be similar to Carnitine-CoA ligase (CaiC) which catalyzes the transfer of CoA to carnitine. Fatty acyl-CoA ligases catalyze the ATP-dependent activation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions.
Pssm-ID: 341292 [Multi-domain] Cd Length: 333 Bit Score: 59.21 E-value: 6.68e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 758185221 72 VIYTSGTAGKPKGVQIEHRNLTNYVSWFSEEASLTENDKTVLLSSYASDLGYTSMFPVLLGGGELHIVQKetyTAPDEIA 151
Cdd:cd17637 5 IIHTAAVAGRPRGAVLSHGNLIAANLQLIHAMGLTEADVYLNMLPLFHIAGLNLALATFHAGGANVVMEK---FDPAEAL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 758185221 152 HYIKEYGITYIKLTPSLFHTIVNTASfAKDANFESLRlIVLGGEkiIPTDVLAFRKIYGHTeFINHYGPTEAtigaiAGR 231
Cdd:cd17637 82 ELIEEEKVTLMGSFPPILSNLLDAAE-KSGVDLSSLR-HVLGLD--APETIQRFEETTGAT-FWSLYGQTET-----SGL 151
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 758185221 232 VDLSEpdaFAKRP-TIGRPIANAGALVLNEALKLVPPGASGQLYITGQGLARGYLNRPQLTAERF 295
Cdd:cd17637 152 VTLSP---YRERPgSAGRPGPLVRVRIVDDNDRPVPAGETGEIVVRGPLVFQGYWNLPELTAYTF 213
|
|
| PRK06178 |
PRK06178 |
acyl-CoA synthetase; Validated |
1-297 |
9.36e-10 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 235724 [Multi-domain] Cd Length: 567 Bit Score: 59.28 E-value: 9.36e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 758185221 1 AAFLPIDPDTPEERIRYSLEDSGAKFAVVNERNMTAIGQY-------EGTIVSLDDGKWRNESKERPSSISGSR------ 67
Cdd:PRK06178 108 AVHVPVSPLFREHELSYELNDAGAEVLLALDQLAPVVEQVraetslrHVIVTSLADVLPAEPTLPLPDSLRAPRlaaaga 187
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 758185221 68 ----------------------NLAYVIYTSGTAGKPKGVQIEHRNLTnYVSWFSEEASLTENDKTVLLSSYA------S 119
Cdd:PRK06178 188 idllpalractapvplpppaldALAALNYTGGTTGMPKGCEHTQRDMV-YTAAAAYAVAVVGGEDSVFLSFLPefwiagE 266
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 758185221 120 DLGYtsMFPVLLGGGELHIVQKETYTAPDEIAHYikeyGITYIKLTPSLFHTIVNTASFAkDANFESLR--LIVLGGEKI 197
Cdd:PRK06178 267 NFGL--LFPLFSGATLVLLARWDAVAFMAAVERY----RVTRTVMLVDNAVELMDHPRFA-EYDLSSLRqvRVVSFVKKL 339
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 758185221 198 IPTDVLAFRKIYGHTEFINHYGPTEA------TIGAIAGRVDLSEPDAFakrptIGRPIANAGALVLN-EALKLVPPGAS 270
Cdd:PRK06178 340 NPDYRQRWRALTGSVLAEAAWGMTEThtcdtfTAGFQDDDFDLLSQPVF-----VGLPVPGTEFKICDfETGELLPLGAE 414
|
330 340
....*....|....*....|....*..
gi 758185221 271 GQLYITGQGLARGYLNRPQLTAERFVE 297
Cdd:PRK06178 415 GEIVVRTPSLLKGYWNKPEATAEALRD 441
|
|
| A_NRPS_MycA_like |
cd05908 |
The adenylation domain of nonribosomal peptide synthetases (NRPS) similar to mycosubtilin ... |
69-298 |
1.25e-09 |
|
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: 58.65 E-value: 1.25e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 758185221 69 LAYVIYTSGTAGKPKGVQIEHRNLTNYVSWFSEEASLTENDKTVLLSSYASDLGYTS--MFPVLLGGGELHIVQKETYTA 146
Cdd:cd05908 108 LAFIQFSSGSTGDPKGVMLTHENLVHNMFAILNSTEWKTKDRILSWMPLTHDMGLIAfhLAPLIAGMNQYLMPTRLFIRR 187
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 758185221 147 PDEIAHYIKEYGITYIKlTPS----LFHTIVNTASfAKDANFESLRLIVLGGEKIIPTDVLAFRK---IYG--HTEFINH 217
Cdd:cd05908 188 PILWLKKASEHKATIVS-SPNfgykYFLKTLKPEK-ANDWDLSSIRMILNGAEPIDYELCHEFLDhmsKYGlkRNAILPV 265
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 758185221 218 YGPTEATIGA------------IAGR-----------VDLSEPDAfAKRPTIGRPIANAGALVLNEALKLVPPGASGQLY 274
Cdd:cd05908 266 YGLAEASVGAslpkaqspfktiTLGRrhvthgepepeVDKKDSEC-LTFVEVGKPIDETDIRICDEDNKILPDGYIGHIQ 344
|
250 260
....*....|....*....|....
gi 758185221 275 ITGQGLARGYLNRPQLTAERFVEN 298
Cdd:cd05908 345 IRGKNVTPGYYNNPEATAKVFTDD 368
|
|
| PRK09088 |
PRK09088 |
acyl-CoA synthetase; Validated |
58-297 |
2.02e-09 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 181644 [Multi-domain] Cd Length: 488 Bit Score: 58.28 E-value: 2.02e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 758185221 58 ERPSSIsgsrnlayvIYTSGTAGKPKGVQIEHRNLTNYVSWFSEEASLTENDKTVLLSSYASDLGY-TSMFPVLLGGGEL 136
Cdd:PRK09088 135 ERVSLI---------LFTSGTSGQPKGVMLSERNLQQTAHNFGVLGRVDAHSSFLCDAPMFHIIGLiTSVRPVLAVGGSI 205
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 758185221 137 HIVQ----KETYTAPDEIAhyikeYGITYIKLTPSLFHTIVNTASFAKDAnFESLRLIVLGGEKIIPTDVLAFrkIYGHT 212
Cdd:PRK09088 206 LVSNgfepKRTLGRLGDPA-----LGITHYFCVPQMAQAFRAQPGFDAAA-LRHLTALFTGGAPHAAEDILGW--LDDGI 277
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 758185221 213 EFINHYGPTEAtiGAIAGR-VDLSEPDAfaKRPTIGRPIANAGALVLNEALKLVPPGASGQLYITGQGLARGYLNRPQLT 291
Cdd:PRK09088 278 PMVDGFGMSEA--GTVFGMsVDCDVIRA--KAGAAGIPTPTVQTRVVDDQGNDCPAGVPGELLLRGPNLSPGYWRRPQAT 353
|
....*.
gi 758185221 292 AERFVE 297
Cdd:PRK09088 354 ARAFTG 359
|
|
| ABCL |
cd05958 |
2-aminobenzoate-CoA ligase (ABCL); ABCL catalyzes the initial step in the 2-aminobenzoate ... |
63-283 |
2.61e-09 |
|
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: 57.49 E-value: 2.61e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 758185221 63 ISGSRNLAYVIYTSGTAGKPKGVQIEHRNLTNYVSWFSEEA-SLTENDKTVLLSSYASDLGYTSM--FPVLLGGGELHIV 139
Cdd:cd05958 93 LTASDDICILAFTSGTTGAPKATMHFHRDPLASADRYAVNVlRLREDDRFVGSPPLAFTFGLGGVllFPFGVGASGVLLE 172
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 758185221 140 QketyTAPDEIAHYIKEYGITYIKLTPSLFHTIVNTASFAKdANFESLRLIVLGGEKIIPTDVLAFRKIYGhTEFINHYG 219
Cdd:cd05958 173 E----ATPDLLLSAIARYKPTVLFTAPTAYRAMLAHPDAAG-PDLSSLRKCVSAGEALPAALHRAWKEATG-IPIIDGIG 246
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 758185221 220 PTEATIGAIAGRVDlsepdafAKRP-TIGRPIANAGALVLNEALKLVPPGASGQLYITGQGLARG 283
Cdd:cd05958 247 STEMFHIFISARPG-------DARPgATGKPVPGYEAKVVDDEGNPVPDGTIGRLAVRGPTGCRY 304
|
|
| MACS_like_3 |
cd05971 |
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the ... |
65-296 |
5.98e-09 |
|
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: 56.67 E-value: 5.98e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 758185221 65 GSRNLAYVIYTSGTAGKPKGVQIEHRNLTNYVSWFSEEASLTENDKTVLLSSyaSDLGYTS-----MFPVLLGGGELhIV 139
Cdd:cd05971 86 GSDDPALIIYTSGTTGPPKGALHAHRVLLGHLPGVQFPFNLFPRDGDLYWTP--ADWAWIGglldvLLPSLYFGVPV-LA 162
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 758185221 140 QKETYTAPDEIAHYIKEYGITYIKLTPSLFHTIVNTASFAKDANFEsLRLIVLGGEKIIPTDVLAFRKIYGHT--EFinh 217
Cdd:cd05971 163 HRMTKFDPKAALDLMSRYGVTTAFLPPTALKMMRQQGEQLKHAQVK-LRAIATGGESLGEELLGWAREQFGVEvnEF--- 238
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 758185221 218 YGPTEATigAIAGrvdlSEPDAFAKRP-TIGRPIANAGALVLNEALKLVPPGASGQLyitgqGLAR-------GYLNRPQ 289
Cdd:cd05971 239 YGQTECN--LVIG----NCSALFPIKPgSMGKPIPGHRVAIVDDNGTPLPPGEVGEI-----AVELpdpvaflGYWNNPS 307
|
....*..
gi 758185221 290 LTAERFV 296
Cdd:cd05971 308 ATEKKMA 314
|
|
| PRK05677 |
PRK05677 |
long-chain-fatty-acid--CoA ligase; Validated |
65-293 |
7.80e-09 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 168170 [Multi-domain] Cd Length: 562 Bit Score: 56.31 E-value: 7.80e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 758185221 65 GSRNLAYVIYTSGTAGKPKGVQIEHRNL-TNYVSWFSEEASLTENDKTVLLSS------YAsdLGYTSMFPVLLGGGELH 137
Cdd:PRK05677 205 QADDVAVLQYTGGTTGVAKGAMLTHRNLvANMLQCRALMGSNLNEGCEILIAPlplyhiYA--FTFHCMAMMLIGNHNIL 282
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 758185221 138 IvqketyTAPDEIAHYIKEYGIT----YIKLTpSLFHTIVNTASFaKDANFESLRLIVLGGEKIIPTDVLAFRKIYGhTE 213
Cdd:PRK05677 283 I------SNPRDLPAMVKELGKWkfsgFVGLN-TLFVALCNNEAF-RKLDFSALKLTLSGGMALQLATAERWKEVTG-CA 353
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 758185221 214 FINHYGPTEATigaiagRVDLSEPDAFAKRPTIGRPIANAGALVLNEALKLVPPGASGQLYITGQGLARGYLNRPQLTAE 293
Cdd:PRK05677 354 ICEGYGMTETS------PVVSVNPSQAIQVGTIGIPVPSTLCKVIDDDGNELPLGEVGELCVKGPQVMKGYWQRPEATDE 427
|
|
| PRK07788 |
PRK07788 |
acyl-CoA synthetase; Validated |
58-286 |
1.44e-08 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236097 [Multi-domain] Cd Length: 549 Bit Score: 55.70 E-value: 1.44e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 758185221 58 ERPSSIsgsrnlayVIYTSGTAGKPKGVQIEHrnltnyVSWFSEEASLTE------NDKTVLLSSYASDLGYtSMFPVLL 131
Cdd:PRK07788 206 PKPGGI--------VILTSGTTGTPKGAPRPE------PSPLAPLAGLLSrvpfraGETTLLPAPMFHATGW-AHLTLAM 270
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 758185221 132 GGGElHIVQKETYTaPDEIAHYIKEYGITYIKLTPSLFHTIVNTASfAKDANFE--SLRLIVLGGEKIIPTDVLAFRKIY 209
Cdd:PRK07788 271 ALGS-TVVLRRRFD-PEATLEDIAKHKATALVVVPVMLSRILDLGP-EVLAKYDtsSLKIIFVSGSALSPELATRALEAF 347
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 758185221 210 GhtEFI-NHYGPTEATIGAIAGRVDLSEPDAFAKRPTIGRPIAnagalVLNEALKLVPPGASGQLYITGQGLARGYLN 286
Cdd:PRK07788 348 G--PVLyNLYGSTEVAFATIATPEDLAEAPGTVGRPPKGVTVK-----ILDENGNEVPRGVVGRIFVGNGFPFEGYTD 418
|
|
| MACS_like_2 |
cd05973 |
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the ... |
73-275 |
1.81e-08 |
|
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: 55.22 E-value: 1.81e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 758185221 73 IYTSGTAGKPKGVQIEHRNLTNYVSWFSEEASLTENDKTVLLSS--YASDLGYTSMFPVLLGGGELHIvqkETYTAPDEI 150
Cdd:cd05973 94 MFTSGTTGLPKGVPVPLRALAAFGAYLRDAVDLRPEDSFWNAADpgWAYGLYYAITGPLALGHPTILL---EGGFSVEST 170
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 758185221 151 AHYIKEYGITYIKLTPSLFHTIVNTASFAKDANFESLRLIVLGGEKIIPTDVLAFRKIYGhTEFINHYGPTEATIgAIAG 230
Cdd:cd05973 171 WRVIERLGVTNLAGSPTAYRLLMAAGAEVPARPKGRLRRVSSAGEPLTPEVIRWFDAALG-VPIHDHYGQTELGM-VLAN 248
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 758185221 231 RVDLSEPdafAKRPTIGRPIANAGALVLNEALKLVPPGASGQLYI 275
Cdd:cd05973 249 HHALEHP---VHAGSAGRAMPGWRVAVLDDDGDELGPGEPGRLAI 290
|
|
| PRK07867 |
PRK07867 |
acyl-CoA synthetase; Validated |
69-303 |
2.21e-08 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236120 [Multi-domain] Cd Length: 529 Bit Score: 55.07 E-value: 2.21e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 758185221 69 LAYVIYTSGTAGKPKGVQIEHRNLTNYVSWFSEEASLTENDkTVLLS-----SYASDLGYTsmfPVLLGGGELHIVQKet 143
Cdd:PRK07867 154 LFMLIFTSGTSGDPKAVRCTHRKVASAGVMLAQRFGLGPDD-VCYVSmplfhSNAVMAGWA---VALAAGASIALRRK-- 227
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 758185221 144 YTA----PDeiahyIKEYGITYIKLTPSLFHTIVNTASFAKDANfESLRlIVLGGEKiIPTDVLAFRKIYGhTEFINHYG 219
Cdd:PRK07867 228 FSAsgflPD-----VRRYGATYANYVGKPLSYVLATPERPDDAD-NPLR-IVYGNEG-APGDIARFARRFG-CVVVDGFG 298
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 758185221 220 PTEatiGAIA-GRVDLSEPDAfakrptIGRPIANAgALVLNEALKLVPPG------------ASGQLY-ITGQGLARGYL 285
Cdd:PRK07867 299 STE---GGVAiTRTPDTPPGA------LGPLPPGV-AIVDPDTGTECPPAedadgrllnadeAIGELVnTAGPGGFEGYY 368
|
250
....*....|....*...
gi 758185221 286 NRPQLTAERFVENPYSPG 303
Cdd:PRK07867 369 NDPEADAERMRGGVYWSG 386
|
|
| Firefly_Luc |
cd17642 |
insect luciferase, similar to plant 4-coumarate: CoA ligases; This family contains insect ... |
54-293 |
2.52e-08 |
|
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: 54.84 E-value: 2.52e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 758185221 54 NESKERPSSISGSRNLAYVIYTSGTAGKPKGVQIEHRNLtnyVSWFSEEASLT----ENDKTVLLS--------SYASDL 121
Cdd:cd17642 171 NEYDFKPPSFDRDEQVALIMNSSGSTGLPKGVQLTHKNI---VARFSHARDPIfgnqIIPDTAILTvipfhhgfGMFTTL 247
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 758185221 122 GY-TSMFPVLLgggeLHIVQKETYTAPdeiahyIKEYGITYIKLTPSLFhTIVNTASFAKDANFESLRLIVLGGEKIIPT 200
Cdd:cd17642 248 GYlICGFRVVL----MYKFEEELFLRS------LQDYKVQSALLVPTLF-AFFAKSTLVDKYDLSNLHEIASGGAPLSKE 316
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 758185221 201 DVLAFRKIYgHTEFINH-YGPTEATIGAIAgrvdlsEPDAFAKRPTIGRPIANAGALVLN-EALKLVPPGASGQLYITGQ 278
Cdd:cd17642 317 VGEAVAKRF-KLPGIRQgYGLTETTSAILI------TPEGDDKPGAVGKVVPFFYAKVVDlDTGKTLGPNERGELCVKGP 389
|
250
....*....|....*
gi 758185221 279 GLARGYLNRPQLTAE 293
Cdd:cd17642 390 MIMKGYVNNPEATKA 404
|
|
| PRK07769 |
PRK07769 |
long-chain-fatty-acid--CoA ligase; Validated |
69-295 |
5.67e-08 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 181109 [Multi-domain] Cd Length: 631 Bit Score: 53.96 E-value: 5.67e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 758185221 69 LAYVIYTSGTAGKPKGVQIEHRNLTNYVSWFSEEASLTENDKTVLLSSYASDLGY-TSMFPVLLGGgelHIvqkeTYTAP 147
Cdd:PRK07769 182 IAYLQYTSGSTRIPAGVQITHLNLPTNVLQVIDALEGQEGDRGVSWLPFFHDMGLiTVLLPALLGH---YI----TFMSP 254
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 758185221 148 deiAHYIKEYGiTYIKLTPSLFHTIVNTASFAKDANFE-------------SLRL-----IVLGGEKIIPTDVLAFRKIY 209
Cdd:PRK07769 255 ---AAFVRRPG-RWIRELARKPGGTGGTFSAAPNFAFEhaaarglpkdgepPLDLsnvkgLLNGSEPVSPASMRKFNEAF 330
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 758185221 210 G-----HTEFINHYGPTEAT--IGAI-----------------AGR---VDLSEPDAFAKRPTIGRPIANAGALVLNEAL 262
Cdd:PRK07769 331 ApyglpPTAIKPSYGMAEATlfVSTTpmdeeptviyvdrdelnAGRfveVPADAPNAVAQVSAGKVGVSEWAVIVDPETA 410
|
250 260 270
....*....|....*....|....*....|...
gi 758185221 263 KLVPPGASGQLYITGQGLARGYLNRPQLTAERF 295
Cdd:PRK07769 411 SELPDGQIGEIWLHGNNIGTGYWGKPEETAATF 443
|
|
| PRK08043 |
PRK08043 |
bifunctional acyl-ACP--phospholipid O-acyltransferase/long-chain-fatty-acid--ACP ligase; |
70-300 |
1.13e-07 |
|
bifunctional acyl-ACP--phospholipid O-acyltransferase/long-chain-fatty-acid--ACP ligase;
Pssm-ID: 181207 [Multi-domain] Cd Length: 718 Bit Score: 52.79 E-value: 1.13e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 758185221 70 AYVIYTSGTAGKPKGVQIEHRNLTNYVSWFSEEASLTENDKTV----LLSSYASDLGytsMFPVLLGGGELHIvqketYT 145
Cdd:PRK08043 368 ALILFTSGSEGHPKGVVHSHKSLLANVEQIKTIADFTPNDRFMsalpLFHSFGLTVG---LFTPLLTGAEVFL-----YP 439
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 758185221 146 APdeiAHYIKEYGITYIKLTPSLFHT---IVNTASFAKDANFESLRLIVLGGEKIIPTDVLAFRKIYGhTEFINHYGPTE 222
Cdd:PRK08043 440 SP---LHYRIVPELVYDRNCTVLFGTstfLGNYARFANPYDFARLRYVVAGAEKLQESTKQLWQDKFG-LRILEGYGVTE 515
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 758185221 223 AtigaiAGRVDLSEPDAfAKRPTIGRPIANAGAlvlnealKLVP-PGAS--GQLYITGQGLARGYLNrpqltaerfVENP 299
Cdd:PRK08043 516 C-----APVVSINVPMA-AKPGTVGRILPGMDA-------RLLSvPGIEqgGRLQLKGPNIMNGYLR---------VEKP 573
|
.
gi 758185221 300 Y 300
Cdd:PRK08043 574 G 574
|
|
| BACL_like |
cd05929 |
Bacterial Bile acid CoA ligases and similar proteins; Bile acid-Coenzyme A ligase catalyzes ... |
71-293 |
1.22e-07 |
|
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: 52.76 E-value: 1.22e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 758185221 71 YVIYTSGTAGKPKGVQ---------IEHRNLTNYVSWFSEEasltendkTVLLSS---YASDLGYTSMFPVLLGGgelHI 138
Cdd:cd05929 129 KMLYSGGTTGRPKGIKrglpggppdNDTLMAAALGFGPGAD--------SVYLSPaplYHAAPFRWSMTALFMGG---TL 197
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 758185221 139 VQKETYTaPDEIAHYIKEYGITYIKLTPSLFHTIVNTASFAKDA-NFESLR----------------LIVLGGEKIIptd 201
Cdd:cd05929 198 VLMEKFD-PEEFLRLIERYRVTFAQFVPTMFVRLLKLPEAVRNAyDLSSLKrvihaaapcppwvkeqWIDWGGPIIW--- 273
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 758185221 202 vlafrkiyghtEFinhYGPTEATigaiaGRVDLSEPDAFAKRPTIGRPIAnAGALVLNEALKLVPPGASGQLYITGqGLA 281
Cdd:cd05929 274 -----------EY---YGGTEGQ-----GLTIINGEEWLTHPGSVGRAVL-GKVHILDEDGNEVPPGEIGEVYFAN-GPG 332
|
250
....*....|..
gi 758185221 282 RGYLNRPQLTAE 293
Cdd:cd05929 333 FEYTNDPEKTAA 344
|
|
| PRK12583 |
PRK12583 |
acyl-CoA synthetase; Provisional |
74-293 |
1.78e-07 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 237145 [Multi-domain] Cd Length: 558 Bit Score: 52.08 E-value: 1.78e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 758185221 74 YTSGTAGKPKGVQIEHRNLTNYvSWFSEEA-SLTENDKTVLLSSYASDLGYTSMFPVLLGGGELHIVQKETYTaPDEIAH 152
Cdd:PRK12583 208 YTSGTTGFPKGATLSHHNILNN-GYFVAESlGLTEHDRLCVPVPLYHCFGMVLANLGCMTVGACLVYPNEAFD-PLATLQ 285
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 758185221 153 YIKEYGITYIKLTPSLFHTIVNTASFAkDANFESLRLIVLGGEKiIPTDVLafRKIYGH---TEFINHYGPTEAT-IGAI 228
Cdd:PRK12583 286 AVEEERCTALYGVPTMFIAELDHPQRG-NFDLSSLRTGIMAGAP-CPIEVM--RRVMDEmhmAEVQIAYGMTETSpVSLQ 361
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 758185221 229 AGRVDLSEpdafaKR-PTIGRPIANAGALVLNEALKLVPPGASGQLYITGQGLARGYLNRPQLTAE 293
Cdd:PRK12583 362 TTAADDLE-----RRvETVGRTQPHLEVKVVDPDGATVPRGEIGELCTRGYSVMKGYWNNPEATAE 422
|
|
| PRK12492 |
PRK12492 |
long-chain-fatty-acid--CoA ligase; Provisional |
68-293 |
2.06e-07 |
|
long-chain-fatty-acid--CoA ligase; Provisional
Pssm-ID: 171539 [Multi-domain] Cd Length: 562 Bit Score: 52.13 E-value: 2.06e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 758185221 68 NLAYVIYTSGTAGKPKGVQIEHRNL--------TNYVSWFSEEASLTENDKTVLLSS------YAsdlgYTSMFPVLLGG 133
Cdd:PRK12492 208 DIAVLQYTGGTTGLAKGAMLTHGNLvanmlqvrACLSQLGPDGQPLMKEGQEVMIAPlplyhiYA----FTANCMCMMVS 283
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 758185221 134 GELHIVqketYTAPDEIAHYIKEYG---ITYIKLTPSLFHTIVNTASFaKDANFESLRLIVLGGEKIIPTDVLAFRKIYG 210
Cdd:PRK12492 284 GNHNVL----ITNPRDIPGFIKELGkwrFSALLGLNTLFVALMDHPGF-KDLDFSALKLTNSGGTALVKATAERWEQLTG 358
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 758185221 211 HTeFINHYGPTEATigaiagRVDLSEP-DAFAKRPTIGRPIANAGALVLNEALKLVPPGASGQLYITGQGLARGYLNRPQ 289
Cdd:PRK12492 359 CT-IVEGYGLTETS------PVASTNPyGELARLGTVGIPVPGTALKVIDDDGNELPLGERGELCIKGPQVMKGYWQQPE 431
|
....
gi 758185221 290 LTAE 293
Cdd:PRK12492 432 ATAE 435
|
|
| PRK07059 |
PRK07059 |
Long-chain-fatty-acid--CoA ligase; Validated |
59-292 |
2.90e-07 |
|
Long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 235923 [Multi-domain] Cd Length: 557 Bit Score: 51.56 E-value: 2.90e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 758185221 59 RPSSISGSrNLAYVIYTSGTAGKPKGVQIEHRNLTNYV----SWFsEEASLTENDKTVLLSSYASDLGY------TSMFP 128
Cdd:PRK07059 197 KPVKLGPD-DVAFLQYTGGTTGVSKGATLLHRNIVANVlqmeAWL-QPAFEKKPRPDQLNFVCALPLYHifaltvCGLLG 274
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 758185221 129 VLLGGGELHIVQketytaPDEIAHYIKE---YGITYIKLTPSLFHTIVNTASFAKdANFESLRLIVLGGEKIIPTDVLAF 205
Cdd:PRK07059 275 MRTGGRNILIPN------PRDIPGFIKElkkYQVHIFPAVNTLYNALLNNPDFDK-LDFSKLIVANGGGMAVQRPVAERW 347
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 758185221 206 RKIYGhTEFINHYGPTEATIGAIAGRVDLSEpdaFAKrpTIGRPIANAGALVLNEALKLVPPGASGQLYITGQGLARGYL 285
Cdd:PRK07059 348 LEMTG-CPITEGYGLSETSPVATCNPVDATE---FSG--TIGLPLPSTEVSIRDDDGNDLPLGEPGEICIRGPQVMAGYW 421
|
....*..
gi 758185221 286 NRPQLTA 292
Cdd:PRK07059 422 NRPDETA 428
|
|
| PRK13390 |
PRK13390 |
acyl-CoA synthetase; Provisional |
70-302 |
5.72e-07 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 139538 [Multi-domain] Cd Length: 501 Bit Score: 50.78 E-value: 5.72e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 758185221 70 AYVIYTSGTAGKPKGVQ--IEHRNLTN----YVSWFSEEASLTENDktVLLSS----YASDLGYTSMFPVLlgGGElhIV 139
Cdd:PRK13390 151 AVMLYSSGTTGFPKGIQpdLPGRDVDApgdpIVAIARAFYDISESD--IYYSSapiyHAAPLRWCSMVHAL--GGT--VV 224
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 758185221 140 QKETYTAPDEIAHyIKEYGITYIKLTPSLFHTIVN-TASFAKDANFESLRLIVLGGEKiIPTDVLAFRKIYGHTEFINHY 218
Cdd:PRK13390 225 LAKRFDAQATLGH-VERYRITVTQMVPTMFVRLLKlDADVRTRYDVSSLRAVIHAAAP-CPVDVKHAMIDWLGPIVYEYY 302
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 758185221 219 GPTEAtigaiAGRVDLSEPDAFAKRPTIGRPIANAGALVLNEALKLvPPGASGQLYITGQGLARGYLNRPQLTAErfVEN 298
Cdd:PRK13390 303 SSTEA-----HGMTFIDSPDWLAHPGSVGRSVLGDLHICDDDGNEL-PAGRIGTVYFERDRLPFRYLNDPEKTAA--AQH 374
|
....
gi 758185221 299 PYSP 302
Cdd:PRK13390 375 PAHP 378
|
|
| PRK09274 |
PRK09274 |
peptide synthase; Provisional |
69-293 |
5.78e-07 |
|
peptide synthase; Provisional
Pssm-ID: 236443 [Multi-domain] Cd Length: 552 Bit Score: 50.67 E-value: 5.78e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 758185221 69 LAYVIYTSGTAGKPKGVQIEHRNLtnyvswfseEASLTendktVLLSSYASDLGYTSM--FPVL------LGGGElhIV- 139
Cdd:PRK09274 176 MAAILFTSGSTGTPKGVVYTHGMF---------EAQIE-----ALREDYGIEPGEIDLptFPLFalfgpaLGMTS--VIp 239
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 758185221 140 ----QKETYTAPDEIAHYIKEYGITYIKLTPSLFHTIVNtASFAKDANFESLRLIVLGGEKIIPTDVLAFRKIYGH-TEF 214
Cdd:PRK09274 240 dmdpTRPATVDPAKLFAAIERYGVTNLFGSPALLERLGR-YGEANGIKLPSLRRVISAGAPVPIAVIERFRAMLPPdAEI 318
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 758185221 215 INHYGPTEAT-IGAIAGRVDLSEPDAFAKR---PTIGRPIAnaGALV------------LNEALKLvPPGASGQLYITGQ 278
Cdd:PRK09274 319 LTPYGATEALpISSIESREILFATRAATDNgagICVGRPVD--GVEVriiaisdapipeWDDALRL-ATGEIGEIVVAGP 395
|
250
....*....|....*
gi 758185221 279 GLARGYLNRPQLTAE 293
Cdd:PRK09274 396 MVTRSYYNRPEATRL 410
|
|
| AFD_YhfT-like |
cd17633 |
fatty acid-CoA ligase VraA; This family of acyl-CoA ligases includes Bacillus subtilis YhfT, ... |
68-285 |
6.34e-07 |
|
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: 50.10 E-value: 6.34e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 758185221 68 NLAYVIYTSGTAGKPKGVqiehrnLTNYVSWFseeASLTENDKTVLLSSYASDLG----------YTSMFpVLLGGGELH 137
Cdd:cd17633 1 NPFYIGFTSGTTGLPKAY------YRSERSWI---ESFVCNEDLFNISGEDAILApgplshslflYGAIS-ALYLGGTFI 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 758185221 138 IVQKetyTAPDEIAHYIKEYGITYIKLTPSLFHTIVNTasfakDANFESLRLIVLGGEKIIPTDVLAFRKIYGHTEFINH 217
Cdd:cd17633 71 GQRK---FNPKSWIRKINQYNATVIYLVPTMLQALART-----LEPESKIKSIFSSGQKLFESTKKKLKNIFPKANLIEF 142
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 758185221 218 YGPTEATIgaIAGRVDLSEpdafAKRPTIGRPIANAGALVLNEAlklvpPGASGQLYITGQGLARGYL 285
Cdd:cd17633 143 YGTSELSF--ITYNFNQES----RPPNSVGRPFPNVEIEIRNAD-----GGEIGKIFVKSEMVFSGYV 199
|
|
| PrpE |
cd05967 |
Propionyl-CoA synthetase (PrpE); EC 6.2.1.17: propanoate:CoA ligase (AMP-forming) or ... |
71-297 |
8.15e-07 |
|
Propionyl-CoA synthetase (PrpE); EC 6.2.1.17: propanoate:CoA ligase (AMP-forming) or propionate#CoA ligase (PrpE) catalyzes the first step of the 2-methylcitric acid cycle for propionate catabolism. It activates propionate to propionyl-CoA in a two-step reaction, which proceeds through a propionyl-AMP intermediate and requires ATP and Mg2+. In Salmonella enterica, the PrpE protein is required for growth of Salmonella enterica on propionate and can substitute for the acetyl-CoA synthetase (Acs) enzyme during growth on acetate. PrpE can also activate acetate, 3HP, and butyrate to their corresponding CoA-thioesters, although with less efficiency.
Pssm-ID: 341271 [Multi-domain] Cd Length: 617 Bit Score: 50.39 E-value: 8.15e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 758185221 71 YVIYTSGTAGKPKGVQiehRNLTNY---VSWfSEEASLTENDKTVLLSsyASDLG------YTSMFPVLLGGGELHIVQK 141
Cdd:cd05967 234 YILYTSGTTGKPKGVV---RDNGGHavaLNW-SMRNIYGIKPGDVWWA--ASDVGwvvghsYIVYGPLLHGATTVLYEGK 307
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 758185221 142 ETYTaPDEIAHY--IKEYGITYIKLTPSLFHTIVN---TASFAKDANFESLRLIVLGGEKIIPtDVLAFRKIYGHTEFIN 216
Cdd:cd05967 308 PVGT-PDPGAFWrvIEKYQVNALFTAPTAIRAIRKedpDGKYIKKYDLSSLRTLFLAGERLDP-PTLEWAENTLGVPVID 385
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 758185221 217 HYGPTEaTIGAIAGrvdlsEPDAFAKRP----TIGRPIANAGALVLNEALKLVPPGASGQLYITGQgLARGYLNRPQLTA 292
Cdd:cd05967 386 HWWQTE-TGWPITA-----NPVGLEPLPikagSPGKPVPGYQVQVLDEDGEPVGPNELGNIVIKLP-LPPGCLLTLWKND 458
|
....*
gi 758185221 293 ERFVE 297
Cdd:cd05967 459 ERFKK 463
|
|
| PRK08315 |
PRK08315 |
AMP-binding domain protein; Validated |
74-293 |
1.23e-06 |
|
AMP-binding domain protein; Validated
Pssm-ID: 236236 [Multi-domain] Cd Length: 559 Bit Score: 49.42 E-value: 1.23e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 758185221 74 YTSGTAGKPKGVQIEHRNLTNYVSWFSEEASLTENDK------------TVL--LSSYASdlGYTSMFPvllggGE---- 135
Cdd:PRK08315 206 YTSGTTGFPKGATLTHRNILNNGYFIGEAMKLTEEDRlcipvplyhcfgMVLgnLACVTH--GATMVYP-----GEgfdp 278
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 758185221 136 ---LHIVQKETYTApdeiahyikEYGItyikltPSLFHTIVNTASFAKdANFESLRLIVLGGEkIIPTDVLafRKI---Y 209
Cdd:PRK08315 279 latLAAVEEERCTA---------LYGV------PTMFIAELDHPDFAR-FDLSSLRTGIMAGS-PCPIEVM--KRVidkM 339
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 758185221 210 GHTEFINHYGPTEATIGAIAGRVDlsepDAFAKR-PTIGRPIANAGALVLNEAL-KLVPPGASGQLYITGQGLARGYLNR 287
Cdd:PRK08315 340 HMSEVTIAYGMTETSPVSTQTRTD----DPLEKRvTTVGRALPHLEVKIVDPETgETVPRGEQGELCTRGYSVMKGYWND 415
|
....*.
gi 758185221 288 PQLTAE 293
Cdd:PRK08315 416 PEKTAE 421
|
|
| PRK06164 |
PRK06164 |
acyl-CoA synthetase; Validated |
69-300 |
1.46e-06 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 235722 [Multi-domain] Cd Length: 540 Bit Score: 49.36 E-value: 1.46e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 758185221 69 LAYVIYTSGTAGKPKGVQIEHRNLTNYVSWFSEEASLTENDKTVLLSSYASDLGYTSMFPVLLGGGELHIVqkETYTAPd 148
Cdd:PRK06164 183 GALLFTTSGTTSGPKLVLHRQATLLRHARAIARAYGYDPGAVLLAALPFCGVFGFSTLLGALAGGAPLVCE--PVFDAA- 259
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 758185221 149 EIAHYIKEYGITYIKLTPSLFHTIVNTAsfAKDANFESLRLI----VLGGEKIIPTDVLA----FRKIYGHTEFInhygp 220
Cdd:PRK06164 260 RTARALRRHRVTHTFGNDEMLRRILDTA--GERADFPSARLFgfasFAPALGELAALARArgvpLTGLYGSSEVQ----- 332
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 758185221 221 teatigAIAGRVDLSEPDAfAKRPTIGRPIANAGALVLNEAL--KLVPPGASGQLYITGQGLARGYLNRPQLTAERFVEN 298
Cdd:PRK06164 333 ------ALVALQPATDPVS-VRIEGGGRPASPEARVRARDPQdgALLPDGESGEIEIRAPSLMRGYLDNPDATARALTDD 405
|
..
gi 758185221 299 PY 300
Cdd:PRK06164 406 GY 407
|
|
| FACL_like_4 |
cd05944 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
68-286 |
3.28e-06 |
|
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: 47.86 E-value: 3.28e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 758185221 68 NLAYVIYTSGTAGKPKGVQIEHRNLTnYVSWFSEEASLTENDKTVL--LSSYASDLGYTSMFPVLLGGGELHIVQKETYT 145
Cdd:cd05944 3 DVAAYFHTGGTTGTPKLAQHTHSNEV-YNAWMLALNSLFDPDDVLLcgLPLFHVNGSVVTLLTPLASGAHVVLAGPAGYR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 758185221 146 AP---DEIAHYIKEYGITYIKLTPSLfhtIVNTASFAKDANFESLRLiVLGGEKIIPTDVlaFRKIYGHT--EFINHYGP 220
Cdd:cd05944 82 NPglfDNFWKLVERYRITSLSTVPTV---YAALLQVPVNADISSLRF-AMSGAAPLPVEL--RARFEDATglPVVEGYGL 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 758185221 221 TEATIGaiagrVDLSEPDAfAKRP-TIGRPIANAGALVLNE-----ALKLVPPGASGQLYITGQGLARGYLN 286
Cdd:cd05944 156 TEATCL-----VAVNPPDG-PKRPgSVGLRLPYARVRIKVLdgvgrLLRDCAPDEVGEICVAGPGVFGGYLY 221
|
|
| PLN02860 |
PLN02860 |
o-succinylbenzoate-CoA ligase |
68-223 |
3.39e-06 |
|
o-succinylbenzoate-CoA ligase
Pssm-ID: 215464 [Multi-domain] Cd Length: 563 Bit Score: 48.26 E-value: 3.39e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 758185221 68 NLAYVIYTSGTAGKPKGVQIEHRNLTnyVSWFSEEASLTENDKTVLLssYASDL----GYTS-MFPVLLGGGELHIVQKE 142
Cdd:PLN02860 173 DAVLICFTSGTTGRPKGVTISHSALI--VQSLAKIAIVGYGEDDVYL--HTAPLchigGLSSaLAMLMVGACHVLLPKFD 248
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 758185221 143 TYTAPDEiahyIKEYGITYIKLTPSLFHTIVNTASFAK-DANFESLRLIVLGGEKiIPTDVL-AFRKIYGHTEFINHYGP 220
Cdd:PLN02860 249 AKAALQA----IKQHNVTSMITVPAMMADLISLTRKSMtWKVFPSVRKILNGGGS-LSSRLLpDAKKLFPNAKLFSAYGM 323
|
...
gi 758185221 221 TEA 223
Cdd:PLN02860 324 TEA 326
|
|
| MACS_AAE_MA_like |
cd05970 |
Medium-chain acyl-CoA synthetase (MACS) of AAE_MA like; MACS catalyzes the two-step activation ... |
58-303 |
3.83e-06 |
|
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: 48.26 E-value: 3.83e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 758185221 58 ERPS--SISGSRNLAYVIYTSGTAGKPKGVQIEHRNLTNYVSWFSEEASLTENDK--TVLLSSYASDLgYTSMFPVLLGG 133
Cdd:cd05970 174 ERPTanSYPCGEDILLVYFSSGTTGMPKMVEHDFTYPLGHIVTAKYWQNVREGGLhlTVADTGWGKAV-WGKIYGQWIAG 252
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 758185221 134 GELHIVQKETYTaPDEIAHYIKEYGITYIKLTPSLFHTIVNTAsfAKDANFESLRLIVLGGEKIIPTDVLAFRKIYGhTE 213
Cdd:cd05970 253 AAVFVYDYDKFD-PKALLEKLSKYGVTTFCAPPTIYRFLIRED--LSRYDLSSLRYCTTAGEALNPEVFNTFKEKTG-IK 328
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 758185221 214 FINHYGPTEATIgAIAgrvdlSEPDAFAKRPTIGRPIANAGALVLNEALKLVPPGASGQLYITGQ-----GLARGYLNRP 288
Cdd:cd05970 329 LMEGFGQTETTL-TIA-----TFPWMEPKPGSMGKPAPGYEIDLIDREGRSCEAGEEGEIVIRTSkgkpvGLFGGYYKDA 402
|
250
....*....|....*
gi 758185221 289 QLTAERFVENPYSPG 303
Cdd:cd05970 403 EKTAEVWHDGYYHTG 417
|
|
| PRK13382 |
PRK13382 |
bile acid CoA ligase; |
147-284 |
8.97e-06 |
|
bile acid CoA ligase;
Pssm-ID: 172019 [Multi-domain] Cd Length: 537 Bit Score: 47.06 E-value: 8.97e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 758185221 147 PDEIAHYIKEYGITYIKLTPSLFHTIVNTASFAKD-ANFESLRLIVLGGEKIIPTDVLAFRKIYGHTEFiNHYGPTEATI 225
Cdd:PRK13382 273 PEATLDLIDRHRATGLAVVPVMFDRIMDLPAEVRNrYSGRSLRFAAASGSRMRPDVVIAFMDQFGDVIY-NNYNATEAGM 351
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|
gi 758185221 226 GAIAGRVDL-SEPDafakrpTIGRPIANAGALVLNEALKLVPPGASGQLYITGQGLARGY 284
Cdd:PRK13382 352 IATATPADLrAAPD------TAGRPAEGTEIRILDQDFREVPTGEVGTIFVRNDTQFDGY 405
|
|
| PRK05852 |
PRK05852 |
fatty acid--CoA ligase family protein; |
70-297 |
9.20e-06 |
|
fatty acid--CoA ligase family protein;
Pssm-ID: 235625 [Multi-domain] Cd Length: 534 Bit Score: 46.80 E-value: 9.20e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 758185221 70 AYVIYTSGTAGKPKGVQIEHRNLTNYVSWFSEEASLTENDKTVLLSSYASDLGY-TSMFPVLLGGGELHIVQKETYTAPD 148
Cdd:PRK05852 179 AMIMFTGGTTGLPKMVPWTHANIASSVRAIITGYRLSPRDATVAVMPLYHGHGLiAALLATLASGGAVLLPARGRFSAHT 258
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 758185221 149 EIAHyIKEYGITYIKLTPSLFHTIVNTASFAKDANFE-SLRLIVLGGEKIIPTDVLAFRKIYGhTEFINHYGPTEATIGA 227
Cdd:PRK05852 259 FWDD-IKAVGATWYTAVPTIHQILLERAATEPSGRKPaALRFIRSCSAPLTAETAQALQTEFA-APVVCAFGMTEATHQV 336
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 758185221 228 IAGRVDLSEPDAFAKRPT--IGRPIANAGALVLNEALKLvPPGASGQLYITGQGLARGYLNRPQLTAERFVE 297
Cdd:PRK05852 337 TTTQIEGIGQTENPVVSTglVGRSTGAQIRIVGSDGLPL-PAGAVGEVWLRGTTVVRGYLGDPTITAANFTD 407
|
|
| PRK12406 |
PRK12406 |
long-chain-fatty-acid--CoA ligase; Provisional |
72-293 |
9.92e-06 |
|
long-chain-fatty-acid--CoA ligase; Provisional
Pssm-ID: 183506 [Multi-domain] Cd Length: 509 Bit Score: 46.62 E-value: 9.92e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 758185221 72 VIYTSGTAGKPKGVQ-----------IEHRNLTNYvswfseeaSLTENDKTVLLSS-YASDLGYTSMFPVLLGGgelhIV 139
Cdd:PRK12406 157 MIYTSGTTGHPKGVRraaptpeqaaaAEQMRALIY--------GLKPGIRALLTGPlYHSAPNAYGLRAGRLGG----VL 224
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 758185221 140 QKETYTAPDEIAHYIKEYGITYIKLTPSLFHTIVNTASFAKDA-NFESLRLIVLGGEKIiPTDV-LAFRKIYGHTeFINH 217
Cdd:PRK12406 225 VLQPRFDPEELLQLIERHRITHMHMVPTMFIRLLKLPEEVRAKyDVSSLRHVIHAAAPC-PADVkRAMIEWWGPV-IYEY 302
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 758185221 218 YGPTEatIGAIAGRVdlSEpDAFAKRPTIGRPIANAGALVLNEALKLVPPGASGQLYITGQGLAR-GYLNRPQLTAE 293
Cdd:PRK12406 303 YGSTE--SGAVTFAT--SE-DALSHPGTVGKAAPGAELRFVDEDGRPLPQGEIGEIYSRIAGNPDfTYHNKPEKRAE 374
|
|
| PLN02614 |
PLN02614 |
long-chain acyl-CoA synthetase |
55-297 |
1.17e-05 |
|
long-chain acyl-CoA synthetase
Pssm-ID: 166255 [Multi-domain] Cd Length: 666 Bit Score: 46.55 E-value: 1.17e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 758185221 55 ESKERPSSISGSRNLAYVIYTSGTAGKPKGVQIEHRNLTNYVSWF-----SEEASLTENDKTVLLSSYA----------- 118
Cdd:PLN02614 211 EGKQYDLPIKKKSDICTIMYTSGTTGDPKGVMISNESIVTLIAGVirllkSANAALTVKDVYLSYLPLAhifdrvieecf 290
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 758185221 119 ------------------SDLG-----------------YTSMFPVLLGGGelhIVQKETYTAPDEIAHYIKEYGITYIK 163
Cdd:PLN02614 291 iqhgaaigfwrgdvklliEDLGelkptifcavprvldrvYSGLQKKLSDGG---FLKKFVFDSAFSYKFGNMKKGQSHVE 367
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 758185221 164 LTPSLFHTIVNTASFAKDANFEslrlIVLGGEKIIPTDVLAFRKIYGHTEFINHYGPTEATIGAIAgrvdlSEPDAFAKR 243
Cdd:PLN02614 368 ASPLCDKLVFNKVKQGLGGNVR----IILSGAAPLASHVESFLRVVACCHVLQGYGLTESCAGTFV-----SLPDELDML 438
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 758185221 244 PTIGRPIANagalvLNEALKLVP--------PGASGQLYITGQGLARGYLNRPQLTAERFVE 297
Cdd:PLN02614 439 GTVGPPVPN-----VDIRLESVPemeydalaSTPRGEICIRGKTLFSGYYKREDLTKEVLID 495
|
|
| PRK12582 |
PRK12582 |
acyl-CoA synthetase; Provisional |
65-297 |
1.19e-05 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 237144 [Multi-domain] Cd Length: 624 Bit Score: 46.58 E-value: 1.19e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 758185221 65 GSRNLAYVIYTSGTAGKPKGVQIEHR----NLTNYVSWFSEEAsltENDKTVLLS--SYASDLGYTSMF-PVLLGGGELH 137
Cdd:PRK12582 218 TPDTVAKYLFTSGSTGMPKAVINTQRmmcaNIAMQEQLRPREP---DPPPPVSLDwmPWNHTMGGNANFnGLLWGGGTLY 294
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 758185221 138 IvqKETYTAPDEIAHYIK---EYGITYIKLTPSLFHTIVntASFAKDAN-----FESLRLIVLGGEKIiPTDV------L 203
Cdd:PRK12582 295 I--DDGKPLPGMFEETIRnlrEISPTVYGNVPAGYAMLA--EAMEKDDAlrrsfFKNLRLMAYGGATL-SDDLyermqaL 369
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 758185221 204 AFRKIYGHTEFINHYGPTEA---TIGA--IAGRVDLsepdafakrptIGRPIANAgalvlneALKLVPPGASGQLYITGQ 278
Cdd:PRK12582 370 AVRTTGHRIPFYTGYGATETaptTTGThwDTERVGL-----------IGLPLPGV-------ELKLAPVGDKYEVRVKGP 431
|
250
....*....|....*....
gi 758185221 279 GLARGYLNRPQLTAERFVE 297
Cdd:PRK12582 432 NVTPGYHKDPELTAAAFDE 450
|
|
| LC_FACS_bac1 |
cd17641 |
bacterial long-chain fatty acid CoA synthetase; The members of this family are bacterial ... |
69-297 |
1.84e-05 |
|
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: 45.88 E-value: 1.84e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 758185221 69 LAYVIYTSGTAGKPKGVQIEHRNL----TNYVSwfSEEASLTENDKTVLLSSYASDLGYTSMFPvLLGGGELHIVQKETY 144
Cdd:cd17641 160 VAVLCTTSGTTGKPKLAMLSHGNFlghcAAYLA--ADPLGPGDEYVSVLPLPWIGEQMYSVGQA-LVCGFIVNFPEEPET 236
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 758185221 145 TAPDeiahyIKEYGITYIKLTPSLFHTIV------------------------------------------NTASFAKDA 182
Cdd:cd17641 237 MMED-----LREIGPTFVLLPPRVWEGIAadvrarmmdatpfkrfmfelgmklglraldrgkrgrpvslwlRLASWLADA 311
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 758185221 183 ----------NFESLRLIVLGGEKIIPtDVLAF--------RKIYGHTEFINHYgpteaTIGAiAGRVDlsePDafakrp 244
Cdd:cd17641 312 llfrplrdrlGFSRLRSAATGGAALGP-DTFRFfhaigvplKQLYGQTELAGAY-----TVHR-DGDVD---PD------ 375
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|...
gi 758185221 245 TIGRPIANAGALVLNEalklvppgasGQLYITGQGLARGYLNRPQLTAERFVE 297
Cdd:cd17641 376 TVGVPFPGTEVRIDEV----------GEILVRSPGVFVGYYKNPEATAEDFDE 418
|
|
| PRK13388 |
PRK13388 |
acyl-CoA synthetase; Provisional |
73-295 |
2.29e-05 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 237374 [Multi-domain] Cd Length: 540 Bit Score: 45.79 E-value: 2.29e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 758185221 73 IYTSGTAGKPKGVQIEHRNLTNYVSWFSEEASLTendktvllssyASDLGYTSM--F----------PVLLGGGElhIVQ 140
Cdd:PRK13388 156 IFTSGTTGAPKAVRCSHGRLAFAGRALTERFGLT-----------RDDVCYVSMplFhsnavmagwaPAVASGAA--VAL 222
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 758185221 141 KETYTA----PDeiahyIKEYGITYIKLTPSLFHTIVNTASFAKDANFeslRLIVLGGEKIIPTDVLAFRKIYGhTEFIN 216
Cdd:PRK13388 223 PAKFSAsgflDD-----VRRYGATYFNYVGKPLAYILATPERPDDADN---PLRVAFGNEASPRDIAEFSRRFG-CQVED 293
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 758185221 217 HYGPTEAtiGAIAGRVDLSEPDAFAkRPTIGRPIANAGAL------VLNEALKLV-PPGASGQLYIT-GQGLARGYLNRP 288
Cdd:PRK13388 294 GYGSSEG--AVIVVREPGTPPGSIG-RGAPGVAIYNPETLtecavaRFDAHGALLnADEAIGELVNTaGAGFFEGYYNNP 370
|
....*..
gi 758185221 289 QLTAERF 295
Cdd:PRK13388 371 EATAERM 377
|
|
| PRK06155 |
PRK06155 |
crotonobetaine/carnitine-CoA ligase; Provisional |
60-293 |
7.69e-05 |
|
crotonobetaine/carnitine-CoA ligase; Provisional
Pssm-ID: 235719 [Multi-domain] Cd Length: 542 Bit Score: 43.98 E-value: 7.69e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 758185221 60 PSSISGSRNLAyVIYTSGTAGKPKGVQIEHRNLTNYVSWFSEEASLTENDktVLLSSYAsdLGYT----SMFPVLLGGGE 135
Cdd:PRK06155 174 AAAVQPGDTAA-ILYTSGTTGPSKGVCCPHAQFYWWGRNSAEDLEIGADD--VLYTTLP--LFHTnalnAFFQALLAGAT 248
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 758185221 136 LHIVQKetYTA----PDEIAHyikeyGITYIKLTPSLFHTIVNTASFAKDaNFESLRLIVLGGekIIPTDVLAFRKIYGh 211
Cdd:PRK06155 249 YVLEPR--FSAsgfwPAVRRH-----GATVTYLLGAMVSILLSQPARESD-RAHRVRVALGPG--VPAALHAAFRERFG- 317
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 758185221 212 TEFINHYGPTEATIgAIAGRVDlsepdafAKRP-TIGRPIANAGALVLNEALKLVPPGASGQLYITGQ---GLARGYLNR 287
Cdd:PRK06155 318 VDLLDGYGSTETNF-VIAVTHG-------SQRPgSMGRLAPGFEARVVDEHDQELPDGEPGELLLRADepfAFATGYFGM 389
|
....*.
gi 758185221 288 PQLTAE 293
Cdd:PRK06155 390 PEKTVE 395
|
|
| PRK07529 |
PRK07529 |
AMP-binding domain protein; Validated |
58-286 |
8.59e-05 |
|
AMP-binding domain protein; Validated
Pssm-ID: 236043 [Multi-domain] Cd Length: 632 Bit Score: 43.79 E-value: 8.59e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 758185221 58 ERPSSISGSRNLAYViYTSGTAGKPKGVQIEHRNLTnYVSWFSEEASLTENDKTVLLSsyasdlgyTSMFPV-------- 129
Cdd:PRK07529 205 FSGRPIGPDDVAAYF-HTGGTTGMPKLAQHTHGNEV-ANAWLGALLLGLGPGDTVFCG--------LPLFHVnallvtgl 274
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 758185221 130 --LLGGGELHIVQKETYTAPDEIAHY---IKEYGITYIKLTPSLFHTIVNTASFAKDanFESLRlIVLGGEKIIPTDVla 204
Cdd:PRK07529 275 apLARGAHVVLATPQGYRGPGVIANFwkiVERYRINFLSGVPTVYAALLQVPVDGHD--ISSLR-YALCGAAPLPVEV-- 349
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 758185221 205 FRKIYGHT--EFINHYGPTEATIGaiagrVDLSEPDAFAKRPTIGRPI--ANAGALVLNEA---LKLVPPGASGQLYITG 277
Cdd:PRK07529 350 FRRFEAATgvRIVEGYGLTEATCV-----SSVNPPDGERRIGSVGLRLpyQRVRVVILDDAgryLRDCAVDEVGVLCIAG 424
|
....*....
gi 758185221 278 QGLARGYLN 286
Cdd:PRK07529 425 PNVFSGYLE 433
|
|
| PtmA |
cd17636 |
long-chain fatty acid CoA ligase (FadD); This family contains fatty acid CoA ligases, ... |
72-295 |
1.64e-04 |
|
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: 42.67 E-value: 1.64e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 758185221 72 VIYTSGTAGKPKGVQIEHRNLtnyvswfseeasLTENDKTVLLSSYASDLGY----------TSMF--PVLLGGGELHIV 139
Cdd:cd17636 5 AIYTAAFSGRPNGALLSHQAL------------LAQALVLAVLQAIDEGTVFlnsgplfhigTLMFtlATFHAGGTNVFV 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 758185221 140 QKetyTAPDEIAHYIKEYGITYIKLTPSLFHTIV--NTASFAKDANFESLRLIVLGGEKIIPTDVLAFRKIYGhtefinh 217
Cdd:cd17636 73 RR---VDAEEVLELIEAERCTHAFLLPPTIDQIVelNADGLYDLSSLRSSPAAPEWNDMATVDTSPWGRKPGG------- 142
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 758185221 218 YGPTEatIGAIAGRVDLSEPDAfakrPTIGRPIANAGALVLNEALKLVPPGASGQLYITGQGLARGYLNRPQLTAERF 295
Cdd:cd17636 143 YGQTE--VMGLATFAALGGGAI----GGAGRPSPLVQVRILDEDGREVPDGEVGEIVARGPTVMAGYWNRPEVNARRT 214
|
|
| PLN02736 |
PLN02736 |
long-chain acyl-CoA synthetase |
68-109 |
2.98e-04 |
|
long-chain acyl-CoA synthetase
Pssm-ID: 178337 [Multi-domain] Cd Length: 651 Bit Score: 42.39 E-value: 2.98e-04
10 20 30 40
....*....|....*....|....*....|....*....|..
gi 758185221 68 NLAYVIYTSGTAGKPKGVQIEHRNLTNYVSWFSEEASLTEND 109
Cdd:PLN02736 222 DVATICYTSGTTGTPKGVVLTHGNLIANVAGSSLSTKFYPSD 263
|
|
| LC_FACS_bac |
cd05932 |
Bacterial long-chain fatty acid CoA synthetase (LC-FACS), including Marinobacter ... |
4-115 |
3.12e-04 |
|
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: 42.07 E-value: 3.12e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 758185221 4 LPIDPDTPEERIRYSLEDSGAKFAVV---NERNMTAIGQYEGTIVSL--------DDGKWRNESKERPSSIS----GSRN 68
Cdd:cd05932 59 VPLYPTLNPDTIRYVLEHSESKALFVgklDDWKAMAPGVPEGLISISlpppsaanCQYQWDDLIAQHPPLEErptrFPEQ 138
|
90 100 110 120
....*....|....*....|....*....|....*....|....*..
gi 758185221 69 LAYVIYTSGTAGKPKGVQIEHRNLTNYVSWFSEEASLTENDKtvLLS 115
Cdd:cd05932 139 LATLIYTSGTTGQPKGVMLTFGSFAWAAQAGIEHIGTEENDR--MLS 183
|
|
| PLN02430 |
PLN02430 |
long-chain-fatty-acid-CoA ligase |
57-96 |
3.51e-04 |
|
long-chain-fatty-acid-CoA ligase
Pssm-ID: 178049 [Multi-domain] Cd Length: 660 Bit Score: 42.11 E-value: 3.51e-04
10 20 30 40
....*....|....*....|....*....|....*....|..
gi 758185221 57 KERPSSISGSR--NLAYVIYTSGTAGKPKGVQIEHRNLTNYV 96
Cdd:PLN02430 208 KENPSETNPPKplDICTIMYTSGTSGDPKGVVLTHEAVATFV 249
|
|
| prpE |
PRK10524 |
propionyl-CoA synthetase; Provisional |
71-86 |
4.16e-04 |
|
propionyl-CoA synthetase; Provisional
Pssm-ID: 182517 [Multi-domain] Cd Length: 629 Bit Score: 41.86 E-value: 4.16e-04
|
| LC_FACS_euk1 |
cd17639 |
Eukaryotic long-chain fatty acid CoA synthetase (LC-FACS), including fungal proteins; The ... |
64-93 |
4.18e-04 |
|
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: 41.82 E-value: 4.18e-04
10 20 30
....*....|....*....|....*....|
gi 758185221 64 SGSRNLAYVIYTSGTAGKPKGVQIEHRNLT 93
Cdd:cd17639 85 GKPDDLACIMYTSGSTGNPKGVMLTHGNLV 114
|
|
| FATP_chFAT1_like |
cd05937 |
Uncharacterized subfamily of bifunctional fatty acid transporter/very-long-chain acyl-CoA ... |
63-141 |
7.81e-04 |
|
Uncharacterized subfamily of bifunctional fatty acid transporter/very-long-chain acyl-CoA synthetase in fungi; Fatty acid transport protein (FATP) transports long-chain or very-long-chain fatty acids across the plasma membrane. FATPs also have fatty acid CoA synthetase activity, thus playing dual roles as fatty acid transporters and its activation enzymes. FATPs are the key players in the trafficking of exogenous fatty acids into the cell and in intracellular fatty acid homeostasis. Members of this family are fungal FATPs, including FAT1 from Cochliobolus heterostrophus.
Pssm-ID: 341260 [Multi-domain] Cd Length: 468 Bit Score: 40.88 E-value: 7.81e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 758185221 63 ISGSR-------NLAYVIYTSGTAGKPKGVQIEHRNLTNYVSWFSEEASLTENDKT-VLLSSYASDLGYTSMFPVLLGGG 134
Cdd:cd05937 76 LSGSRfvivdpdDPAILIYTSGTTGLPKAAAISWRRTLVTSNLLSHDLNLKNGDRTyTCMPLYHGTAAFLGACNCLMSGG 155
|
....*..
gi 758185221 135 ELHIVQK 141
Cdd:cd05937 156 TLALSRK 162
|
|
| PRK07514 |
PRK07514 |
malonyl-CoA synthase; Validated |
1-92 |
1.64e-03 |
|
malonyl-CoA synthase; Validated
Pssm-ID: 181011 [Multi-domain] Cd Length: 504 Bit Score: 39.86 E-value: 1.64e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 758185221 1 AAFLPIDPD-TPEErIRYSLEDSGAKFAVVNERN---MTAIGQYEGT--IVSLDD---GKWRNESKERPSSIS----GSR 67
Cdd:PRK07514 78 AVFLPLNTAyTLAE-LDYFIGDAEPALVVCDPANfawLSKIAAAAGAphVETLDAdgtGSLLEAAAAAPDDFEtvprGAD 156
|
90 100
....*....|....*....|....*
gi 758185221 68 NLAYVIYTSGTAGKPKGVQIEHRNL 92
Cdd:PRK07514 157 DLAAILYTSGTTGRSKGAMLSHGNL 181
|
|
| ACSBG_like |
cd05933 |
Bubblegum-like very long-chain fatty acid CoA synthetase (VL-FACS); This family of very ... |
73-93 |
1.79e-03 |
|
Bubblegum-like very long-chain fatty acid CoA synthetase (VL-FACS); This family of very long-chain fatty acid CoA synthetase is named bubblegum because Drosophila melanogaster mutant bubblegum (BGM) has elevated levels of very-long-chain fatty acids (VLCFA) caused by a defective gene of this family. The human homolog (hsBG) has been characterized as a very long chain fatty acid CoA synthetase that functions specifically in the brain; hsBG may play a central role in brain VLCFA metabolism and myelinogenesis. VL-FACS is involved in the first reaction step of very long chain fatty acid degradation. It catalyzes the formation of fatty acyl-CoA in a two-step reaction: the formation of a fatty acyl-AMP molecule as an intermediate, and the formation of a fatty acyl-CoA. Free fatty acids must be "activated" to their CoA thioesters before participating in most catabolic and anabolic reactions.
Pssm-ID: 341256 [Multi-domain] Cd Length: 596 Bit Score: 39.65 E-value: 1.79e-03
|
| PLN02387 |
PLN02387 |
long-chain-fatty-acid-CoA ligase family protein |
60-97 |
2.07e-03 |
|
long-chain-fatty-acid-CoA ligase family protein
Pssm-ID: 215217 [Multi-domain] Cd Length: 696 Bit Score: 39.71 E-value: 2.07e-03
10 20 30
....*....|....*....|....*....|....*...
gi 758185221 60 PSSISGSRNLAYVIYTSGTAGKPKGVQIEHRNLTNYVS 97
Cdd:PLN02387 243 DPDLPSPNDIAVIMYTSGSTGLPKGVMMTHGNIVATVA 280
|
|
| PRK08279 |
PRK08279 |
long-chain-acyl-CoA synthetase; Validated |
56-109 |
2.22e-03 |
|
long-chain-acyl-CoA synthetase; Validated
Pssm-ID: 236217 [Multi-domain] Cd Length: 600 Bit Score: 39.47 E-value: 2.22e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*.
gi 758185221 56 SKERPSSISG--SRNLAYVIYTSGTAGKPKGVQIEHRNLTNYVSWFSEEASLTEND 109
Cdd:PRK08279 186 PTTNPASRSGvtAKDTAFYIYTSGTTGLPKAAVMSHMRWLKAMGGFGGLLRLTPDD 241
|
|
| PTZ00216 |
PTZ00216 |
acyl-CoA synthetase; Provisional |
53-93 |
2.26e-03 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 240316 [Multi-domain] Cd Length: 700 Bit Score: 39.57 E-value: 2.26e-03
10 20 30 40
....*....|....*....|....*....|....*....|..
gi 758185221 53 RNESKERPSSISGSRN-LAYVIYTSGTAGKPKGVQIEHRNLT 93
Cdd:PTZ00216 249 HSAGSHHPLNIPENNDdLALIMYTSGTTGDPKGVMHTHGSLT 290
|
|
| PTZ00342 |
PTZ00342 |
acyl-CoA synthetase; Provisional |
72-96 |
2.48e-03 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 240370 [Multi-domain] Cd Length: 746 Bit Score: 39.32 E-value: 2.48e-03
10 20
....*....|....*....|....*
gi 758185221 72 VIYTSGTAGKPKGVQIEHRNLTNYV 96
Cdd:PTZ00342 309 IVYTSGTSGKPKGVMLSNKNLYNTV 333
|
|
| PRK06814 |
PRK06814 |
acyl-[ACP]--phospholipid O-acyltransferase; |
70-285 |
3.03e-03 |
|
acyl-[ACP]--phospholipid O-acyltransferase;
Pssm-ID: 235865 [Multi-domain] Cd Length: 1140 Bit Score: 39.18 E-value: 3.03e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 758185221 70 AYVIYTSGTAGKPKGVQIEHRNLTNYVSWFSEEASLTENDKTV-LLSSYASdLGYTS--MFPVLLGggelhiVQKETYTA 146
Cdd:PRK06814 796 AVILFTSGSEGTPKGVVLSHRNLLANRAQVAARIDFSPEDKVFnALPVFHS-FGLTGglVLPLLSG------VKVFLYPS 868
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 758185221 147 PdeiAHY--IKEygITYIKLTPSLFHTIVNTASFAKDAN---FESLRLIVLGGEKIIPTDVLAFRKIYGHTEFiNHYGPT 221
Cdd:PRK06814 869 P---LHYriIPE--LIYDTNATILFGTDTFLNGYARYAHpydFRSLRYVFAGAEKVKEETRQTWMEKFGIRIL-EGYGVT 942
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 758185221 222 EATIGaIAgrvdLSEPdAFAKRPTIGRpianagALVLNEAlKLVP-PGAS--GQLYITGQGLARGYL 285
Cdd:PRK06814 943 ETAPV-IA----LNTP-MHNKAGTVGR------LLPGIEY-RLEPvPGIDegGRLFVRGPNVMLGYL 996
|
|
| PTZ00237 |
PTZ00237 |
acetyl-CoA synthetase; Provisional |
71-274 |
9.50e-03 |
|
acetyl-CoA synthetase; Provisional
Pssm-ID: 240325 [Multi-domain] Cd Length: 647 Bit Score: 37.41 E-value: 9.50e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 758185221 71 YVIYTSGTAGKPKGVQieHRNLTNYVSWFSEEASLTENDKTVLLSSYASdLGYTSM---FPVLLGGGELHIVQKETYTAP 147
Cdd:PTZ00237 258 YILYTSGTTGNSKAVV--RSNGPHLVGLKYYWRSIIEKDIPTVVFSHSS-IGWVSFhgfLYGSLSLGNTFVMFEGGIIKN 334
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 758185221 148 DEIAHY----IKEYGITYIKLTPSLFHTIVNTASFAKDA----NFESLRLIVLGGEKI---IPTDVLAFRKIyghtEFIN 216
Cdd:PTZ00237 335 KHIEDDlwntIEKHKVTHTLTLPKTIRYLIKTDPEATIIrskyDLSNLKEIWCGGEVIeesIPEYIENKLKI----KSSR 410
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 758185221 217 HYGPTEATIGAIAGRVDLSEPDAFAKRPTIG-RP-IANAGALVLNE------ALKL-VPPGASGQLY 274
Cdd:PTZ00237 411 GYGQTEIGITYLYCYGHINIPYNATGVPSIFiKPsILSEDGKELNVneigevAFKLpMPPSFATTFY 477
|
|
| |
