|
Name |
Accession |
Description |
Interval |
E-value |
| entF |
PRK10252 |
enterobactin non-ribosomal peptide synthetase EntF; |
2-549 |
1.64e-126 |
|
enterobactin non-ribosomal peptide synthetase EntF;
Pssm-ID: 236668 [Multi-domain] Cd Length: 1296 Bit Score: 400.96 E-value: 1.64e-126
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178432446 2 SDVVPIGAPVPGAALVVLDGWLRPVSAGVVGELYVAGRGVGVGYWRRPGLSASRFVACPFGPpGTRMYRTGDRVRWRADG 81
Cdd:PRK10252 773 GSSVPIGYPVWNTGLRILDARMRPVPPGVAGDLYLTGIQLAQGYLGRPDLTASRFIADPFAP-GERMYRTGDVARWLDDG 851
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178432446 82 QLEYLGRTDDQVKIRGYRVELGEIRTALAELEGVEHAAVIAREDRP------GERRLVGYITG----TADPATVRAELAR 151
Cdd:PRK10252 852 AVEYLGRSDDQLKIRGQRIELGEIDRAMQALPDVEQAVTHACVINQaaatggDARQLVGYLVSqsglPLDTSALQAQLRE 931
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178432446 152 RLPAHMVPASVMALQALPLTVNGKLNTRALPAPRYADGDRYRAPANSVEKVLADIYAQVLGVERVGVDDSFFDLGGDSIS 231
Cdd:PRK10252 932 RLPPHMVPVVLLQLDQLPLSANGKLDRKALPLPELKAQVPGRAPKTGTETIIAAAFSSLLGCDVVDADADFFALGGHSLL 1011
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178432446 232 AMRATAAINAALGAGLAVRTLFYAPSVRRLSRQLGTP---ASAEELVPVETLNEGSGVPLWCIHDGFGLSWPYRALGRYL 308
Cdd:PRK10252 1012 AMKLAAQLSRQFARQVTPGQVMVASTVAKLATLLDAEedeSRRLGFGTILPLREGDGPTLFCFHPASGFAWQFSVLSRYL 1091
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178432446 309 D--CPVIGI-NRVPQNGEGEPESIRAMAARYADTLQALYPDGPYKLLGWSFGGVVAQELAIELQRRGCVVQSLVLLDA-P 384
Cdd:PRK10252 1092 DpqWSIYGIqSPRPDGPMQTATSLDEVCEAHLATLLEQQPHGPYHLLGYSLGGTLAQGIAARLRARGEEVAFLGLLDTwP 1171
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178432446 385 ysatkgvtrlgankirasAESQILQRIlRANGIDAQPGPLTYQRAEELIRQKLGSSilpPKELLEFMV-NSANASQsFLA 463
Cdd:PRK10252 1172 ------------------PETQNWREK-EANGLDPEVLAEIDREREAFLAAQQGSL---STELFTTIEgNYADAVR-LLT 1228
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178432446 464 EHVPEVFDGDMVVFSAARNgHRNGGDPTllaqmhkmgthlaarsrlKKWKSHTAGsFTAYSIDCSHYDMLSTASLNMYGE 543
Cdd:PRK10252 1229 TAHSVPFDGKATLFVAERT-LQEGMSPE------------------QAWSPWIAE-LDVYRQDCAHVDIISPEAFEKIGP 1288
|
....*.
gi 1178432446 544 HLKFAL 549
Cdd:PRK10252 1289 ILRATL 1294
|
|
| PRK12467 |
PRK12467 |
peptide synthase; Provisional |
5-383 |
8.16e-103 |
|
peptide synthase; Provisional
Pssm-ID: 237108 [Multi-domain] Cd Length: 3956 Bit Score: 340.60 E-value: 8.16e-103
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178432446 5 VPIGAPVPGAALVVLDGWLRPVSAGVVGELYVAGRGVGVGYWRRPGLSASRFVACPFGPPGTRMYRTGDRVRWRADGQLE 84
Cdd:PRK12467 3409 APIGRPVAGRSIYVLDGQLNPVPVGVAGELYIGGVGLARGYHQRPSLTAERFVADPFSGSGGRLYRTGDLARYRADGVIE 3488
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178432446 85 YLGRTDDQVKIRGYRVELGEIRTALAELEGVEHAAVIAReDRPGERRLVGYITGTADPA----TVRAELARRLPAHMVPA 160
Cdd:PRK12467 3489 YLGRIDHQVKIRGFRIELGEIEARLLQHPSVREAVVLAR-DGAGGKQLVAYVVPADPQGdwreTLRDHLAASLPDYMVPA 3567
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178432446 161 SVMALQALPLTVNGKLNTRALPAPRYADGDRYRAPANSVEKVLADIYAQVLGVERVGVDDSFFDLGGDSISAMRATAAIN 240
Cdd:PRK12467 3568 QLLVLAAMPLGPNGKVDRKALPDPDAKGSREYVAPRSEVEQQLAAIWADVLGVEQVGVTDNFFELGGDSLLALQVLSRIR 3647
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178432446 241 AALGAGLAVRTLFYAPSVRRLSRQLGTP-ASAEELVPVETLNEGSGVpLWCIHDGFGLSWPYRALGRYL--DCPVIGIN- 316
Cdd:PRK12467 3648 QSLGLKLSLRDLMSAPTIAELAGYSPLGdVPVNLLLDLNRLETGFPA-LFCRHEGLGTVFDYEPLAVILegDRHVLGLTc 3726
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1178432446 317 RVPQNGEGEPESIRAMAARYADTLQALYPDGPYKLLGWSFGGVVAQELAIELQRRGCVVQSLVLLDA 383
Cdd:PRK12467 3727 RHLLDDGWQDTSLQAMAVQYADYILWQQAKGPYGLLGWSLGGTLARLVAELLEREGESEAFLGLFDN 3793
|
|
| A_NRPS_CmdD_like |
cd17652 |
similar to adenylation domain of chondramide synthase cmdD; This family of the adenylation (A) ... |
1-182 |
1.33e-89 |
|
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: 282.60 E-value: 1.33e-89
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178432446 1 GSDVVPIGAPVPGAALVVLDGWLRPVSAGVVGELYVAGRGVGVGYWRRPGLSASRFVACPFGPPGTRMYRTGDRVRWRAD 80
Cdd:cd17652 251 GGGVPPIGRPVPGTRVYVLDARLRPVPPGVPGELYIAGAGLARGYLNRPGLTAERFVADPFGAPGSRMYRTGDLARWRAD 330
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178432446 81 GQLEYLGRTDDQVKIRGYRVELGEIRTALAELEGVEHAAVIAREDRPGERRLVGYITG----TADPATVRAELARRLPAH 156
Cdd:cd17652 331 GQLEFLGRADDQVKIRGFRIELGEVEAALTEHPGVAEAVVVVRDDRPGDKRLVAYVVPapgaAPTAAELRAHLAERLPGY 410
|
170 180
....*....|....*....|....*.
gi 1178432446 157 MVPASVMALQALPLTVNGKLNTRALP 182
Cdd:cd17652 411 MVPAAFVVLDALPLTPNGKLDRRALP 436
|
|
| EntF |
COG1020 |
EntF, seryl-AMP synthase component of non-ribosomal peptide synthetase [Secondary metabolites ... |
1-414 |
7.25e-89 |
|
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: 298.69 E-value: 7.25e-89
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178432446 1 GSDVVPIGAPVPGAALVVLDGWLRPVSAGVVGELYVAGRGVGVGYWRRPGLSASRFVACPFGPPGTRMYRTGDRVRWRAD 80
Cdd:COG1020 784 DGGSVPIGRPIANTRVYVLDAHLQPVPVGVPGELYIGGAGLARGYLNRPELTAERFVADPFGFPGARLYRTGDLARWLPD 863
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178432446 81 GQLEYLGRTDDQVKIRGYRVELGEIRTALAELEGVEHAAVIAREDRPGERRLVGYITG----TADPATVRAELARRLPAH 156
Cdd:COG1020 864 GNLEFLGRADDQVKIRGFRIELGEIEAALLQHPGVREAVVVAREDAPGDKRLVAYVVPeagaAAAAALLRLALALLLPPY 943
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178432446 157 MVPASVMALQALPLTVNGKLNTRALPAPRYADGDRYRAPANSVEKVLADIYAQVLGVERVGVDDSFFDLGGDSISAMRAT 236
Cdd:COG1020 944 MVPAAVVLLLPLPLTGNGKLDRLALPAPAAAAAAAAAAPPAEEEEEEAALALLLLLVVVVGDDDFFFFGGGLGLLLLLAL 1023
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178432446 237 AAINAALGAGLAVRTLFYAPSVRRLSRQLGTPASAEELVPVETLNEGSGVPLWCIHDGFGLSWPYRALGRYLDCPVIGIN 316
Cdd:COG1020 1024 ARAARLLLLLLLLLLLFLAAAAAAAAAAAAAAAAAAAAPLAAAAAPLPLPPLLLSLLALLLALLLLLALLALLALLLLLL 1103
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178432446 317 RVPQNGEGEPESIRAMAARYADTLQALYPDGPYKLLGWSFGGVVAQELAIELQRRGCVVQSLVLLDAPYSATKGVTRLGA 396
Cdd:COG1020 1104 LLLLLLALLLLLALLLALLAALRARRAVRQEGPRLRLLVALAAALALAALLALLLAAAAAAAELLAAAALLLLLALLLLA 1183
|
410
....*....|....*...
gi 1178432446 397 NKIRASAESQILQRILRA 414
Cdd:COG1020 1184 LLLLLLLLLLLLLLLLLL 1201
|
|
| A_NRPS |
cd05930 |
The adenylation domain of nonribosomal peptide synthetases (NRPS); The adenylation (A) domain ... |
2-181 |
3.71e-88 |
|
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: 279.03 E-value: 3.71e-88
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178432446 2 SDVVPIGAPVPGAALVVLDGWLRPVSAGVVGELYVAGRGVGVGYWRRPGLSASRFVACPFGPpGTRMYRTGDRVRWRADG 81
Cdd:cd05930 262 DGRVPIGRPIPNTRVYVLDENLRPVPPGVPGELYIGGAGLARGYLNRPELTAERFVPNPFGP-GERMYRTGDLVRWLPDG 340
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178432446 82 QLEYLGRTDDQVKIRGYRVELGEIRTALAELEGVEHAAVIAREDRPGERRLVGYIT----GTADPATVRAELARRLPAHM 157
Cdd:cd05930 341 NLEFLGRIDDQVKIRGYRIELGEIEAALLAHPGVREAAVVAREDGDGEKRLVAYVVpdegGELDEEELRAHLAERLPDYM 420
|
170 180
....*....|....*....|....
gi 1178432446 158 VPASVMALQALPLTVNGKLNTRAL 181
Cdd:cd05930 421 VPSAFVVLDALPLTPNGKVDRKAL 444
|
|
| PRK12467 |
PRK12467 |
peptide synthase; Provisional |
5-277 |
8.73e-84 |
|
peptide synthase; Provisional
Pssm-ID: 237108 [Multi-domain] Cd Length: 3956 Bit Score: 285.52 E-value: 8.73e-84
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178432446 5 VPIGAPVPGAALVVLDGWLRPVSAGVVGELYVAGRGVGVGYWRRPGLSASRFVACPFGPPGTRMYRTGDRVRWRADGQLE 84
Cdd:PRK12467 828 VPIGQPLANLGLYILDHYLNPVPVGVVGELYIGGAGLARGYHRRPALTAERFVPDPFGADGGRLYRTGDLARYRADGVIE 907
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178432446 85 YLGRTDDQVKIRGYRVELGEIRTALAELEGVEHAAVIArEDRPGERRLVGYITGTADPA---------TVRAELARRLPA 155
Cdd:PRK12467 908 YLGRMDHQVKIRGFRIELGEIEARLLAQPGVREAVVLA-QPGDAGLQLVAYLVPAAVADgaehqatrdELKAQLRQVLPD 986
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178432446 156 HMVPASVMALQALPLTVNGKLNTRALPAPR-YADGDRYRAPANSVEKVLADIYAQVLGVERVGVDDSFFDLGGDSISAMR 234
Cdd:PRK12467 987 YMVPAHLLLLDSLPLTPNGKLDRKALPKPDaSAVQATFVAPQTELEKRLAAIWADVLKVERVGLTDNFFELGGHSLLATQ 1066
|
250 260 270 280
....*....|....*....|....*....|....*....|....*
gi 1178432446 235 ATAAINAALGAGLAVRTLFYAPSVRRLSRQLG--TPASAEELVPV 277
Cdd:PRK12467 1067 VISRVRQRLGIQVPLRTLFEHQTLAGFAQAVAaqQQGAQPALPDV 1111
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
1-277 |
7.74e-82 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 279.92 E-value: 7.74e-82
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178432446 1 GSDVVPIGAPVPGAALVVLDGWLRPVSAGVVGELYVAGRGVGVGYWRRPGLSASRFVACPFGPpGTRMYRTGDRVRWRAD 80
Cdd:PRK12316 821 GGDSVPIGRPIANLACYILDANLEPVPVGVLGELYLAGRGLARGYHGRPGLTAERFVPSPFVA-GERMYRTGDLARYRAD 899
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178432446 81 GQLEYLGRTDDQVKIRGYRVELGEIRTALAELEGVEHAAVIAREDrpgeRRLVGYIT----GTADPATVRAELARRLPAH 156
Cdd:PRK12316 900 GVIEYAGRIDHQVKLRGLRIELGEIEARLLEHPWVREAAVLAVDG----KQLVGYVVleseGGDWREALKAHLAASLPEY 975
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178432446 157 MVPASVMALQALPLTVNGKLNTRALPAPRYADGDR-YRAPANSVEKVLADIYAQVLGVERVGVDDSFFDLGGDSISAMRA 235
Cdd:PRK12316 976 MVPAQWLALERLPLTPNGKLDRKALPAPEASVAQQgYVAPRNALERTLAAIWQDVLGVERVGLDDNFFELGGDSIVSIQV 1055
|
250 260 270 280
....*....|....*....|....*....|....*....|...
gi 1178432446 236 TAAINAAlGAGLAVRTLFYAPSVRRLSR-QLGTPASAEELVPV 277
Cdd:PRK12316 1056 VSRARQA-GIQLSPRDLFQHQTIRSLALvAKAGQATAADQGPA 1097
|
|
| A_NRPS_Srf_like |
cd12117 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including Bacillus subtilis ... |
3-181 |
3.74e-80 |
|
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: 259.44 E-value: 3.74e-80
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178432446 3 DVVPIGAPVPGAALVVLDGWLRPVSAGVVGELYVAGRGVGVGYWRRPGLSASRFVACPFGPPGtRMYRTGDRVRWRADGQ 82
Cdd:cd12117 304 GSIPIGRPIANTRVYVLDEDGRPVPPGVPGELYVGGDGLALGYLNRPALTAERFVADPFGPGE-RLYRTGDLARWLPDGR 382
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178432446 83 LEYLGRTDDQVKIRGYRVELGEIRTALAELEGVEHAAVIAREDRPGERRLVGYITGTA--DPATVRAELARRLPAHMVPA 160
Cdd:cd12117 383 LEFLGRIDDQVKIRGFRIELGEIEAALRAHPGVREAVVVVREDAGGDKRLVAYVVAEGalDAAELRAFLRERLPAYMVPA 462
|
170 180
....*....|....*....|.
gi 1178432446 161 SVMALQALPLTVNGKLNTRAL 181
Cdd:cd12117 463 AFVVLDELPLTANGKVDRRAL 483
|
|
| A_NRPS_AB3403-like |
cd17646 |
Peptide Synthetase; The adenylation (A) domain of NRPS recognizes a specific amino acid or ... |
5-181 |
2.22e-78 |
|
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: 254.89 E-value: 2.22e-78
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178432446 5 VPIGAPVPGAALVVLDGWLRPVSAGVVGELYVAGRGVGVGYWRRPGLSASRFVACPFGPpGTRMYRTGDRVRWRADGQLE 84
Cdd:cd17646 308 VPIGRPVPNTRLYVLDDALRPVPVGVPGELYLGGVQLARGYLGRPALTAERFVPDPFGP-GSRMYRTGDLARWRPDGALE 386
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178432446 85 YLGRTDDQVKIRGYRVELGEIRTALAELEGVEHAAVIAREDRPGERRLVGYITGTA-----DPATVRAELARRLPAHMVP 159
Cdd:cd17646 387 FLGRSDDQVKIRGFRVEPGEIEAALAAHPAVTHAVVVARAAPAGAARLVGYVVPAAgaagpDTAALRAHLAERLPEYMVP 466
|
170 180
....*....|....*....|..
gi 1178432446 160 ASVMALQALPLTVNGKLNTRAL 181
Cdd:cd17646 467 AAFVVLDALPLTANGKLDRAAL 488
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
1-272 |
2.28e-78 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 269.90 E-value: 2.28e-78
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178432446 1 GSDVVPIGAPVPGAALVVLDGWLRPVSAGVVGELYVAGRGVGVGYWRRPGLSASRFVACPFGPPGTRMYRTGDRVRWRAD 80
Cdd:PRK12316 4863 GAAYMPIGTPLGNRSGYVLDGQLNPLPVGVAGELYLGGEGVARGYLERPALTAERFVPDPFGAPGGRLYRTGDLARYRAD 4942
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178432446 81 GQLEYLGRTDDQVKIRGYRVELGEIRTALAELEGVEHAAVIAREDrPGERRLVGYI----TGTADPATVRAE-------- 148
Cdd:PRK12316 4943 GVIDYLGRVDHQVKIRGFRIELGEIEARLREHPAVREAVVIAQEG-AVGKQLVGYVvpqdPALADADEAQAElrdelkaa 5021
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178432446 149 LARRLPAHMVPASVMALQALPLTVNGKLNTRALPAPRYADGDR-YRAPANSVEKVLADIYAQVLGVERVGVDDSFFDLGG 227
Cdd:PRK12316 5022 LRERLPEYMVPAHLVFLARMPLTPNGKLDRKALPQPDASLLQQaYVAPRSELEQQVAAIWAEVLQLERVGLDDNFFELGG 5101
|
250 260 270 280
....*....|....*....|....*....|....*....|....*
gi 1178432446 228 DSISAMRATAAINAALGAGLAVRTLFYAPSVRRLSRQLGTPASAE 272
Cdd:PRK12316 5102 HSLLAIQVTSRIQLELGLELPLRELFQTPTLAAFVELAAAAGSGD 5146
|
|
| PRK12467 |
PRK12467 |
peptide synthase; Provisional |
1-262 |
1.88e-77 |
|
peptide synthase; Provisional
Pssm-ID: 237108 [Multi-domain] Cd Length: 3956 Bit Score: 267.03 E-value: 1.88e-77
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178432446 1 GSDVVPIGAPVPGAALVVLDGWLRPVSAGVVGELYVAGRGVGVGYWRRPGLSASRFVACPFGPPGTRMYRTGDRVRWRAD 80
Cdd:PRK12467 1888 GRDSVPIGQPIANLSTYILDASLNPVPIGVAGELYLGGVGLARGYLNRPALTAERFVADPFGTVGSRLYRTGDLARYRAD 1967
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178432446 81 GQLEYLGRTDDQVKIRGYRVELGEIRTALAELEGVEHAAVIAREDRPGeRRLVGYIT--------GTADPATVRAELAR- 151
Cdd:PRK12467 1968 GVIEYLGRIDHQVKIRGFRIELGEIEARLREQGGVREAVVIAQDGANG-KQLVAYVVptdpglvdDDEAQVALRAILKNh 2046
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178432446 152 ---RLPAHMVPASVMALQALPLTVNGKLNTRALPAPRYADGDR-YRAPANSVEKVLADIYAQVLGVERVGVDDSFFDLGG 227
Cdd:PRK12467 2047 lkaSLPEYMVPAHLVFLARMPLTPNGKLDRKALPAPDASELQQaYVAPQSELEQRLAAIWQDVLGLEQVGLHDNFFELGG 2126
|
250 260 270
....*....|....*....|....*....|....*
gi 1178432446 228 DSISAMRATAAINAAlGAGLAVRTLFYAPSVRRLS 262
Cdd:PRK12467 2127 DSIISIQVVSRARQA-GIRFTPKDLFQHQTVQSLA 2160
|
|
| A_NRPS_Cytc1-like |
cd17643 |
similar to adenylation domain of cytotrienin synthetase CytC1; This family of the adenylation ... |
1-181 |
2.35e-77 |
|
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: 251.07 E-value: 2.35e-77
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178432446 1 GSDVVPIGAPVPGAALVVLDGWLRPVSAGVVGELYVAGRGVGVGYWRRPGLSASRFVACPFGPPGTRMYRTGDRVRWRAD 80
Cdd:cd17643 266 AAAASPIGRPLPGLRVYVLDADGRPVPPGVVGELYVSGAGVARGYLGRPELTAERFVANPFGGPGSRMYRTGDLARRLPD 345
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178432446 81 GQLEYLGRTDDQVKIRGYRVELGEIRTALAELEGVEHAAVIAREDRPGERRLVGYITG----TADPATVRAELARRLPAH 156
Cdd:cd17643 346 GELEYLGRADEQVKIRGFRIELGEIEAALATHPSVRDAAVIVREDEPGDTRLVAYVVAddgaAADIAELRALLKELLPDY 425
|
170 180
....*....|....*....|....*
gi 1178432446 157 MVPASVMALQALPLTVNGKLNTRAL 181
Cdd:cd17643 426 MVPARYVPLDALPLTVNGKLDRAAL 450
|
|
| A_NRPS_VisG_like |
cd17651 |
similar to adenylation domain of virginiamycin S synthetase; This family of the adenylation (A) ... |
3-182 |
2.47e-77 |
|
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: 252.26 E-value: 2.47e-77
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178432446 3 DVVPIGAPVPGAALVVLDGWLRPVSAGVVGELYVAGRGVGVGYWRRPGLSASRFVACPFGPpGTRMYRTGDRVRWRADGQ 82
Cdd:cd17651 309 APPPIGRPIDNTRVYVLDAALRPVPPGVPGELYIGGAGLARGYLNRPELTAERFVPDPFVP-GARMYRTGDLARWLPDGE 387
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178432446 83 LEYLGRTDDQVKIRGYRVELGEIRTALAELEGVEHAAVIAREDRPGERRLVGYITGTA----DPATVRAELARRLPAHMV 158
Cdd:cd17651 388 LEFLGRADDQVKIRGFRIELGEIEAALARHPGVREAVVLAREDRPGEKRLVAYVVGDPeapvDAAELRAALATHLPEYMV 467
|
170 180
....*....|....*....|....
gi 1178432446 159 PASVMALQALPLTVNGKLNTRALP 182
Cdd:cd17651 468 PSAFVLLDALPLTPNGKLDRRALP 491
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
1-275 |
4.15e-75 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 260.27 E-value: 4.15e-75
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178432446 1 GSDVVPIGAPVPGAALVVLDGWLRPVSAGVVGELYVAGRGVGVGYWRRPGLSASRFVACPFGPPGTRMYRTGDRVRWRAD 80
Cdd:PRK12316 2315 GAAYVPIGRALGNRRAYILDADLNLLAPGMAGELYLGGEGLARGYLNRPGLTAERFVPDPFSASGERLYRTGDLARYRAD 2394
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178432446 81 GQLEYLGRTDDQVKIRGYRVELGEIRTALAELEGVEHAAVIAReDRPGERRLVGYITG----TADPATVRAELARRLPAH 156
Cdd:PRK12316 2395 GVVEYLGRIDHQVKIRGFRIELGEIEARLQAHPAVREAVVVAQ-DGASGKQLVAYVVPddaaEDLLAELRAWLAARLPAY 2473
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178432446 157 MVPASVMALQALPLTVNGKLNTRALPAPRYADGDR-YRAPANSVEKVLADIYAQVLGVERVGVDDSFFDLGGDSISAMRA 235
Cdd:PRK12316 2474 MVPAHWVVLERLPLNPNGKLDRKALPKPDVSQLRQaYVAPQEGLEQRLAAIWQAVLKVEQVGLDDHFFELGGHSLLATQV 2553
|
250 260 270 280
....*....|....*....|....*....|....*....|
gi 1178432446 236 TAAINAALGAGLAVRTLFYAPSVRRLSRQLGTPASAEELV 275
Cdd:PRK12316 2554 VSRVRQDLGLEVPLRILFERPTLAAFAASLESGQTSRAPV 2593
|
|
| A_NRPS_Ta1_like |
cd12116 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including salinosporamide A ... |
1-181 |
1.45e-73 |
|
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: 241.81 E-value: 1.45e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178432446 1 GSDVVPIGAPVPGAALVVLDGWLRPVSAGVVGELYVAGRGVGVGYWRRPGLSASRFVACPFGPPGTRMYRTGDRVRWRAD 80
Cdd:cd12116 287 AAGPIPIGRPLANTQVYVLDAALRPVPPGVPGELYIGGDGVAQGYLGRPALTAERFVPDPFAGPGSRLYRTGDLVRRRAD 366
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178432446 81 GQLEYLGRTDDQVKIRGYRVELGEIRTALAELEGVEHAAVIAREDRpGERRLVGYITG----TADPATVRAELARRLPAH 156
Cdd:cd12116 367 GRLEYLGRADGQVKIRGHRIELGEIEAALAAHPGVAQAAVVVREDG-GDRRLVAYVVLkagaAPDAAALRAHLRATLPAY 445
|
170 180
....*....|....*....|....*
gi 1178432446 157 MVPASVMALQALPLTVNGKLNTRAL 181
Cdd:cd12116 446 MVPSAFVRLDALPLTANGKLDRKAL 470
|
|
| PRK05691 |
PRK05691 |
peptide synthase; Validated |
5-288 |
1.91e-73 |
|
peptide synthase; Validated
Pssm-ID: 235564 [Multi-domain] Cd Length: 4334 Bit Score: 255.48 E-value: 1.91e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178432446 5 VPIGAPVPGAALVVLDGWLRPVSAGVVGELYVAGRGVGVGYWRRPGLSASRFVACPFGPPGTRMYRTGDRVRWRADGQLE 84
Cdd:PRK05691 1443 SPIGRPLGNVLCRVLDAELNLLPPGVAGELCIGGAGLARGYLGRPALTAERFVPDPLGEDGARLYRTGDRARWNADGALE 1522
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178432446 85 YLGRTDDQVKIRGYRVELGEIRTALAELEGVEHAAVIAREDRPGErRLVGYITGTA----DPATVRAELARRLPAHMVPA 160
Cdd:PRK05691 1523 YLGRLDQQVKLRGFRVEPEEIQARLLAQPGVAQAAVLVREGAAGA-QLVGYYTGEAgqeaEAERLKAALAAELPEYMVPA 1601
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178432446 161 SVMALQALPLTVNGKLNTRALPAPRYADGDrYRAPANSVEKVLADIYAQVLGVERVGVDDSFFDLGGDSISAMRATAAIN 240
Cdd:PRK05691 1602 QLIRLDQMPLGPSGKLDRRALPEPVWQQRE-HVEPRTELQQQIAAIWREVLGLPRVGLRDDFFALGGHSLLATQIVSRTR 1680
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|.
gi 1178432446 241 AALGAGLAVRTLFYAPSVRRLSRQLGTPASAEE---LVPVETLNEGSGVPL 288
Cdd:PRK05691 1681 QACDVELPLRALFEASELGAFAEQVARIQAAGErnsQGAIARVDRSQPVPL 1731
|
|
| PRK05691 |
PRK05691 |
peptide synthase; Validated |
1-278 |
2.34e-72 |
|
peptide synthase; Validated
Pssm-ID: 235564 [Multi-domain] Cd Length: 4334 Bit Score: 252.01 E-value: 2.34e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178432446 1 GSDVVPIGAPVPGAALVVLDGWLRPVSAGVVGELYVAGRGVGVGYWRRPGLSASRFVACPFGPPGTRMYRTGDRVRWRAD 80
Cdd:PRK05691 2502 GAASVPIGRVVGARVAYILDADLALVPQGATGELYVGGAGLAQGYHDRPGLTAERFVADPFAADGGRLYRTGDLVRLRAD 2581
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178432446 81 GQLEYLGRTDDQVKIRGYRVELGEIRTALAELEGVEHAAVIAReDRPGERRLVGYITGTADPAT----------VRAELA 150
Cdd:PRK05691 2582 GLVEYVGRIDHQVKIRGFRIELGEIESRLLEHPAVREAVVLAL-DTPSGKQLAGYLVSAVAGQDdeaqaalreaLKAHLK 2660
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178432446 151 RRLPAHMVPASVMALQALPLTVNGKLNTRALPAPRYA-DGDRYRAPANSVEKVLADIYAQVLGVERVGVDDSFFDLGGDS 229
Cdd:PRK05691 2661 QQLPDYMVPAHLILLDSLPLTANGKLDRRALPAPDPElNRQAYQAPRSELEQQLAQIWREVLNVERVGLGDNFFELGGDS 2740
|
250 260 270 280
....*....|....*....|....*....|....*....|....*....
gi 1178432446 230 ISAMRATAAINaALGAGLAVRTLFYAPSVRRLSRQlgtpASAEELVPVE 278
Cdd:PRK05691 2741 ILSIQVVSRAR-QLGIHFSPRDLFQHQTVQTLAAV----ATHSEAAQAE 2784
|
|
| A_NRPS_PvdJ-like |
cd17649 |
non-ribosomal peptide synthetase; This family of the adenylation (A) domain of nonribosomal ... |
4-182 |
1.75e-71 |
|
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: 235.73 E-value: 1.75e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178432446 4 VVPIGAPVPGAALVVLDGWLRPVSAGVVGELYVAGRGVGVGYWRRPGLSASRFVACPFGPPGTRMYRTGDRVRWRADGQL 83
Cdd:cd17649 267 SMPIGRPLGGRSAYILDADLNPVPVGVTGELYIGGEGLARGYLGRPELTAERFVPDPFGAPGSRLYRTGDLARWRDDGVI 346
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178432446 84 EYLGRTDDQVKIRGYRVELGEIRTALAELEGVEHAAVIAReDRPGERRLVGYI------TGTADPATVRAELARRLPAHM 157
Cdd:cd17649 347 EYLGRVDHQVKIRGFRIELGEIEAALLEHPGVREAAVVAL-DGAGGKQLVAYVvlraaaAQPELRAQLRTALRASLPDYM 425
|
170 180
....*....|....*....|....*
gi 1178432446 158 VPASVMALQALPLTVNGKLNTRALP 182
Cdd:cd17649 426 VPAHLVFLARLPLTPNGKLDRKALP 450
|
|
| A_NRPS_Sfm_like |
cd12115 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including Saframycin A gene ... |
1-181 |
6.17e-70 |
|
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: 231.44 E-value: 6.17e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178432446 1 GSDVVPIGAPVPGAALVVLDGWLRPVSAGVVGELYVAGRGVGVGYWRRPGLSASRFVACPFGPpGTRMYRTGDRVRWRAD 80
Cdd:cd12115 264 ASGEVSIGRPLANTQAYVLDRALQPVPLGVPGELYIGGAGVARGYLGRPGLTAERFLPDPFGP-GARLYRTGDLVRWRPD 342
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178432446 81 GQLEYLGRTDDQVKIRGYRVELGEIRTALAELEGVEHAAVIAREDRPGERRLVGYITGTADPATVRAE----LARRLPAH 156
Cdd:cd12115 343 GLLEFLGRADNQVKVRGFRIELGEIEAALRSIPGVREAVVVAIGDAAGERRLVAYIVAEPGAAGLVEDlrrhLGTRLPAY 422
|
170 180
....*....|....*....|....*
gi 1178432446 157 MVPASVMALQALPLTVNGKLNTRAL 181
Cdd:cd12115 423 MVPSRFVRLDALPLTPNGKIDRSAL 447
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
1-263 |
1.01e-68 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 241.78 E-value: 1.01e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178432446 1 GSDVVPIGAPVPGAALVVLDGWLRPVSAGVVGELYVAGRGVGVGYWRRPGLSASRFVACPFGPpGTRMYRTGDRVRWRAD 80
Cdd:PRK12316 3359 GKDAVPIGRPIANRACYILDGSLEPVPVGALGELYLGGEGLARGYHNRPGLTAERFVPDPFVP-GERLYRTGDLARYRAD 3437
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178432446 81 GQLEYLGRTDDQVKIRGYRVELGEIRTALAELEGVEHAAVIAREDRPGERRLVGYITGTADPATVRAELARRLPAHMVPA 160
Cdd:PRK12316 3438 GVIEYIGRVDHQVKIRGFRIELGEIEARLLEHPWVREAVVLAVDGRQLVAYVVPEDEAGDLREALKAHLKASLPEYMVPA 3517
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178432446 161 SVMALQALPLTVNGKLNTRALPAPRYADGDR-YRAPANSVEKVLADIYAQVLGVERVGVDDSFFDLGGDSISAMRATAAI 239
Cdd:PRK12316 3518 HLLFLERMPLTPNGKLDRKALPRPDAALLQQdYVAPVNELERRLAAIWADVLKLEQVGLTDNFFELGGDSIISLQVVSRA 3597
|
250 260
....*....|....*....|....
gi 1178432446 240 NAAlGAGLAVRTLFYAPSVRRLSR 263
Cdd:PRK12316 3598 RQA-GIRFTPKDLFQHQTIQGLAR 3620
|
|
| A_NRPS_Bac |
cd17655 |
bacitracin synthetase and related proteins; This family of the adenylation (A) domain of ... |
5-184 |
1.57e-68 |
|
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: 229.14 E-value: 1.57e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178432446 5 VPIGAPVPGAALVVLDGWLRPVSAGVVGELYVAGRGVGVGYWRRPGLSASRFVACPFgPPGTRMYRTGDRVRWRADGQLE 84
Cdd:cd17655 309 VPIGKPLGNTRIYILDQYGRPQPVGVAGELYIGGEGVARGYLNRPELTAEKFVDDPF-VPGERMYRTGDLARWLPDGNIE 387
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178432446 85 YLGRTDDQVKIRGYRVELGEIRTALAELEGVEHAAVIAREDRPGERRLVGYITG--TADPATVRAELARRLPAHMVPASV 162
Cdd:cd17655 388 FLGRIDHQVKIRGYRIELGEIEARLLQHPDIKEAVVIARKDEQGQNYLCAYIVSekELPVAQLREFLARELPDYMIPSYF 467
|
170 180
....*....|....*....|..
gi 1178432446 163 MALQALPLTVNGKLNTRALPAP 184
Cdd:cd17655 468 IKLDEIPLTPNGKVDRKALPEP 489
|
|
| A_NRPS_PpsD_like |
cd17650 |
similar to adenylation domain of plipastatin synthase (PpsD); This family of the adenylation ... |
1-181 |
2.25e-67 |
|
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: 225.04 E-value: 2.25e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178432446 1 GSDVVPIGAPVPGAALVVLDGWLRPVSAGVVGELYVAGRGVGVGYWRRPGLSASRFVACPFGPpGTRMYRTGDRVRWRAD 80
Cdd:cd17650 266 DSANVPIGRPLPNTAMYVLDERLQPQPVGVAGELYIGGAGVARGYLNRPELTAERFVENPFAP-GERMYRTGDLARWRAD 344
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178432446 81 GQLEYLGRTDDQVKIRGYRVELGEIRTALAELEGVEHAAVIAREDRPGERRLVGYITGTADPAT--VRAELARRLPAHMV 158
Cdd:cd17650 345 GNVELLGRVDHQVKIRGFRIELGEIESQLARHPAIDEAVVAVREDKGGEARLCAYVVAAATLNTaeLRAFLAKELPSYMI 424
|
170 180
....*....|....*....|...
gi 1178432446 159 PASVMALQALPLTVNGKLNTRAL 181
Cdd:cd17650 425 PSYYVQLDALPLTPNGKVDRRAL 447
|
|
| PRK05691 |
PRK05691 |
peptide synthase; Validated |
5-262 |
5.96e-65 |
|
peptide synthase; Validated
Pssm-ID: 235564 [Multi-domain] Cd Length: 4334 Bit Score: 230.44 E-value: 5.96e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178432446 5 VPIGAPVPGAALVVLDGWLRPVSAGVVGELYVAGRGVGVGYWRRPGLSASRFVACPFGPPGTRMYRTGDRVRWRADGQLE 84
Cdd:PRK05691 4040 LPIGSPTDNNRLYLLDEALELVPLGAVGELCVAGTGVGRGYVGDPLRTALAFVPHPFGAPGERLYRTGDLARRRSDGVLE 4119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178432446 85 YLGRTDDQVKIRGYRVELGEIRTALAELEGVEHAAVIAREdRPGERRLVGYIT---GTADPATVRAELARR----LPAHM 157
Cdd:PRK05691 4120 YVGRIDHQVKIRGYRIELGEIEARLHEQAEVREAAVAVQE-GVNGKHLVGYLVphqTVLAQGALLERIKQRlraeLPDYM 4198
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178432446 158 VPASVMALQALPLTVNGKLNTRALPAPRY--ADGDRYRAPANSVEKVLADIYAQVLGVERVGVDDSFFDLGGDSISAMRA 235
Cdd:PRK05691 4199 VPLHWLWLDRLPLNANGKLDRKALPALDIgqLQSQAYLAPRNELEQTLATIWADVLKVERVGVHDNFFELGGHSLLATQI 4278
|
250 260
....*....|....*....|....*..
gi 1178432446 236 TAAINAALGAGLAVRTLFYAPSVRRLS 262
Cdd:PRK05691 4279 ASRVQKALQRNVPLRAMFECSTVEELA 4305
|
|
| A_NRPS_ApnA-like |
cd17644 |
similar to adenylation domain of anabaenopeptin synthetase (ApnA); This family of the ... |
5-182 |
3.57e-61 |
|
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: 208.83 E-value: 3.57e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178432446 5 VPIGAPVPGAALVVLDGWLRPVSAGVVGELYVAGRGVGVGYWRRPGLSASRFVACPF-GPPGTRMYRTGDRVRWRADGQL 83
Cdd:cd17644 283 VPIGRPIANTQVYILDENLQPVPVGVPGELHIGGVGLARGYLNRPELTAEKFISHPFnSSESERLYKTGDLARYLPDGNI 362
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178432446 84 EYLGRTDDQVKIRGYRVELGEIRTALAELEGVEHAAVIAREDRPGERRLVGYITG----TADPATVRAELARRLPAHMVP 159
Cdd:cd17644 363 EYLGRIDNQVKIRGFRIELGEIEAVLSQHNDVKTAVVIVREDQPGNKRLVAYIVPhyeeSPSTVELRQFLKAKLPDYMIP 442
|
170 180
....*....|....*....|...
gi 1178432446 160 ASVMALQALPLTVNGKLNTRALP 182
Cdd:cd17644 443 SAFVVLEELPLTPNGKIDRRALP 465
|
|
| AA-adenyl-dom |
TIGR01733 |
amino acid adenylation domain; This model represents a domain responsible for the specific ... |
5-120 |
2.39e-58 |
|
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: 199.80 E-value: 2.39e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178432446 5 VPIGAPVPGAALVVLDGWLRPVSAGVVGELYVAGRGVGVGYWRRPGLSASRFVACPF-GPPGTRMYRTGDRVRWRADGQL 83
Cdd:TIGR01733 293 VPIGRPLANTRLYVLDDDLRPVPVGVVGELYIGGPGVARGYLNRPELTAERFVPDPFaGGDGARLYRTGDLVRYLPDGNL 372
|
90 100 110
....*....|....*....|....*....|....*..
gi 1178432446 84 EYLGRTDDQVKIRGYRVELGEIRTALAELEGVEHAAV 120
Cdd:TIGR01733 373 EFLGRIDDQVKIRGYRIELGEIEAALLRHPGVREAVV 409
|
|
| A_NRPS_ACVS-like |
cd17648 |
N-(5-amino-5-carboxypentanoyl)-L-cysteinyl-D-valine synthase; This family contains ACV ... |
7-182 |
5.43e-58 |
|
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: 200.32 E-value: 5.43e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178432446 7 IGAPVPGAALVVLDGWLRPVSAGVVGELYVAGRGVGVGYWRRPGLSASRFVACPFGPPG-------TRMYRTGDRVRWRA 79
Cdd:cd17648 263 LGRPVRNTKCYVLNDAMKRVPVGAVGELYLGGDGVARGYLNRPELTAERFLPNPFQTEQerargrnARLYKTGDLVRWLP 342
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178432446 80 DGQLEYLGRTDDQVKIRGYRVELGEIRTALAELEGVEHAAVIARED-----RPGERRLVGYIT---GTADPATVRAELAR 151
Cdd:cd17648 343 SGELEYLGRNDFQVKIRGQRIEPGEVEAALASYPGVRECAVVAKEDasqaqSRIQKYLVGYYLpepGHVPESDLLSFLRA 422
|
170 180 190
....*....|....*....|....*....|.
gi 1178432446 152 RLPAHMVPASVMALQALPLTVNGKLNTRALP 182
Cdd:cd17648 423 KLPRYMVPARLVRLEGIPVTINGKLDVRALP 453
|
|
| EntF2 |
COG3319 |
Thioesterase domain of type I polyketide synthase or non-ribosomal peptide synthetase ... |
3-554 |
2.82e-56 |
|
Thioesterase domain of type I polyketide synthase or non-ribosomal peptide synthetase [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 442548 [Multi-domain] Cd Length: 855 Bit Score: 203.01 E-value: 2.82e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178432446 3 DVVPIGAPVPGAALVVLDGWLRPVSAGVVGELYVAGRGVGVGYWRRPGLSASRFVACPFGPPGTRMYRTGDRVRWRADGQ 82
Cdd:COG3319 314 ALGPIGGGPGLLVLLVLLVLLLPLLLGVGGGGGGGGGGGGAGGLAGRGLRAAAALRDPAGAGARGRLRRGGDRGRRLGGG 393
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178432446 83 LEYLGRTDDQVKIRGYRVELGEIRTALAELEGVEHAAVIAREDRPGERRLVGYITGTADPATVRAELARRL----PAHMV 158
Cdd:COG3319 394 LLLGLGRLRLQRLRRGLREELEEAEAALAEAAAVAAAVAAAAAAAAAAAALAAAVVAAAALAAAALLLLLLllllPPPLP 473
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178432446 159 PASVMALQALPLTVNGKLNTRALPAPRYADGDRYRAPANSVEKVLADIYAQVLGVERVGVDDSFFDLGGDSISAMRATAA 238
Cdd:COG3319 474 PALLLLLLLLLLLLLAALLLAAAAPAAAAAAAAAPAPAAALELALALLLLLLLGLGLVGDDDDFFGGGGGSLLALLLLLL 553
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178432446 239 INAALGAGLAVRTLFYAPSVRRLSRQLGTPASAEELVPVETLN-EGSGVPLWCIHDGFGLSWPYRALGRYL--DCPVIGI 315
Cdd:COG3319 554 LLALLLRLLLLLALLLAPTLAALAAALAAAAAAAALSPLVPLRaGGSGPPLFCVHPAGGNVLCYRPLARALgpDRPVYGL 633
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178432446 316 NRVPQNGEGEP-ESIRAMAARYADTLQALYPDGPYKLLGWSFGGVVAQELAIELQRRGCVVQSLVLLDAPysatkgVTRL 394
Cdd:COG3319 634 QAPGLDGGEPPpASVEEMAARYVEAIRAVQPEGPYHLLGWSFGGLVAYEMARQLEAQGEEVALLVLLDSY------APGA 707
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178432446 395 GANKIRASAESQILQRILRANGIDAQPGPLTYQRAEELIRQ------KLGSSILPPKELLEFMVNSANASQSFLAEHVPE 468
Cdd:COG3319 708 LARLDEAELLAALLRDLARGVDLPLDAEELRALDPEERLARllerlrEAGLPAGLDAERLRRLLRVFRANLRALRRYRPR 787
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178432446 469 VFDGDMVVFSAARNGHRNGGDPTLLaqmhkmgthlaarsrlkkWKSHTAGSFTAYSIDCSHYDMLSTASLNMYGEHLKFA 548
Cdd:COG3319 788 PYDGPVLLFRAEEDPPGRADDPALG------------------WRPLVAGGLEVHDVPGDHFSMLREPHVAELAAALRAA 849
|
....*.
gi 1178432446 549 LENARR 554
Cdd:COG3319 850 LAAAEA 855
|
|
| A_NRPS_LgrA-like |
cd17645 |
adenylation (A) domain of linear gramicidin synthetase (LgrA) and similar proteins; This ... |
5-182 |
1.77e-55 |
|
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: 193.15 E-value: 1.77e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178432446 5 VPIGAPVPGAALVVLDGWLRPVSAGVVGELYVAGRGVGVGYWRRPGLSASRFVACPFgPPGTRMYRTGDRVRWRADGQLE 84
Cdd:cd17645 262 IPIGKPIDNTRVYILDEALQLQPIGVAGELCIAGEGLARGYLNRPELTAEKFIVHPF-VPGERMYRTGDLAKFLPDGNIE 340
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178432446 85 YLGRTDDQVKIRGYRVELGEIRTALAELEGVEHAAVIAREDRPGERRLVGYITG--TADPATVRAELARRLPAHMVPASV 162
Cdd:cd17645 341 FLGRLDQQVKIRGYRIEPGEIEPFLMNHPLIELAAVLAKEDADGRKYLVAYVTApeEIPHEELREWLKNDLPDYMIPTYF 420
|
170 180
....*....|....*....|
gi 1178432446 163 MALQALPLTVNGKLNTRALP 182
Cdd:cd17645 421 VHLKALPLTANGKVDRKALP 440
|
|
| A_NRPS_GliP_like |
cd17653 |
nonribosomal peptide synthase GliP-like; This family includes the adenylation (A) domain of ... |
5-181 |
1.32e-54 |
|
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: 190.60 E-value: 1.32e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178432446 5 VPIGAPVPGAALVVLDGWLRPVSAGVVGELYVAGRGVGVGYWRRPGLSASRFVACPFGPpGTRMYRTGDRVRWRADGQLE 84
Cdd:cd17653 259 VTIGKPIPNSTCYILDADLQPVPEGVVGEICISGVQVARGYLGNPALTASKFVPDPFWP-GSRMYRTGDYGRWTEDGGLE 337
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178432446 85 YLGRTDDQVKIRGYRVELGEI-RTALAELEGVEHAAVIAREDrpgerRLVGYIT-GTADPATVRAELARRLPAHMVPASV 162
Cdd:cd17653 338 FLGREDNQVKVRGFRINLEEIeEVVLQSQPEVTQAAAIVVNG-----RLVAFVTpETVDVDGLRSELAKHLPSYAVPDRI 412
|
170
....*....|....*....
gi 1178432446 163 MALQALPLTVNGKLNTRAL 181
Cdd:cd17653 413 IALDSFPLTANGKVDRKAL 431
|
|
| A_NRPS_TlmIV_like |
cd12114 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including ... |
4-181 |
1.53e-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: 191.33 E-value: 1.53e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178432446 4 VVPIGAPVPGAALVVLDGWLRPVSAGVVGELYVAGRGVGVGYWRRPGLSASRFVAcpfGPPGTRMYRTGDRVRWRADGQL 83
Cdd:cd12114 299 SIPYGRPLANQRYRVLDPRGRDCPDWVPGELWIGGRGVALGYLGDPELTAARFVT---HPDGERLYRTGDLGRYRPDGTL 375
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178432446 84 EYLGRTDDQVKIRGYRVELGEIRTALAELEGVEHAAVIAReDRPGERRLVGYIT-----GTADPATVRAELARRLPAHMV 158
Cdd:cd12114 376 EFLGRRDGQVKVRGYRIELGEIEAALQAHPGVARAVVVVL-GDPGGKRLAAFVVpdndgTPIAPDALRAFLAQTLPAYMI 454
|
170 180
....*....|....*....|...
gi 1178432446 159 PASVMALQALPLTVNGKLNTRAL 181
Cdd:cd12114 455 PSRVIALEALPLTANGKVDRAAL 477
|
|
| DltA |
cd05945 |
D-alanine:D-alanyl carrier protein ligase (DltA) and similar proteins; This family includes ... |
1-181 |
5.40e-54 |
|
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: 189.38 E-value: 5.40e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178432446 1 GSDVVPIGAPVPGAALVVLDGWLRPVSAGVVGELYVAGRGVGVGYWRRPGLSASRFvacpFGPPGTRMYRTGDRVRWRAD 80
Cdd:cd05945 268 GYDRLPIGYAKPGAKLVILDEDGRPVPPGEKGELVISGPSVSKGYLNNPEKTAAAF----FPDEGQRAYRTGDLVRLEAD 343
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178432446 81 GQLEYLGRTDDQVKIRGYRVELGEIRTALAELEGVEHAAVIAREDRPGERRLVGYITGTA-----DPATVRAELARRLPA 155
Cdd:cd05945 344 GLLFYRGRLDFQVKLNGYRIELEEIEAALRQVPGVKEAVVVPKYKGEKVTELIAFVVPKPgaeagLTKAIKAELAERLPP 423
|
170 180
....*....|....*....|....*.
gi 1178432446 156 HMVPASVMALQALPLTVNGKLNTRAL 181
Cdd:cd05945 424 YMIPRRFVYLDELPLNANGKIDRKAL 449
|
|
| A_NRPS_ProA |
cd17656 |
gramicidin S synthase 2, also known as ATP-dependent proline adenylase; This family of the ... |
6-182 |
1.85e-51 |
|
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: 183.06 E-value: 1.85e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178432446 6 PIGAPVPGAALVVLDGWLRPVSAGVVGELYVAGRGVGVGYWRRPGLSASRFVACPFgPPGTRMYRTGDRVRWRADGQLEY 85
Cdd:cd17656 302 PIGKPISNTWIYILDQEQQLQPQGIVGELYISGASVARGYLNRQELTAEKFFPDPF-DPNERMYRTGDLARYLPDGNIEF 380
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178432446 86 LGRTDDQVKIRGYRVELGEIRTALAELEGVEHAAVIAREDRPGERRLVGYITG--TADPATVRAELARRLPAHMVPASVM 163
Cdd:cd17656 381 LGRADHQVKIRGYRIELGEIEAQLLNHPGVSEAVVLDKADDKGEKYLCAYFVMeqELNISQLREYLAKQLPEYMIPSFFV 460
|
170
....*....|....*....
gi 1178432446 164 ALQALPLTVNGKLNTRALP 182
Cdd:cd17656 461 PLDQLPLTPNGKVDRKALP 479
|
|
| A_NRPS_SidN3_like |
cd05918 |
The adenylation (A) domain of siderophore-synthesizing nonribosomal peptide synthetases (NRPS); ... |
1-181 |
2.32e-43 |
|
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: 161.17 E-value: 2.32e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178432446 1 GSDVVPIGAPVPGAALVV-LDGWLRPVSAGVVGELYVAGRGVGVGYWRRPGLSASRFVACPF------GPPGTRMYRTGD 73
Cdd:cd05918 262 STDPRNIGRPLGATCWVVdPDNHDRLVPIGAVGELLIEGPILARGYLNDPEKTAAAFIEDPAwlkqegSGRGRRLYRTGD 341
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178432446 74 RVRWRADGQLEYLGRTDDQVKIRGYRVELGEIRTALAELEGVEH---AAVIAREDRPGERRLVGYITG------------ 138
Cdd:cd05918 342 LVRYNPDGSLEYVGRKDTQVKIRGQRVELGEIEHHLRQSLPGAKevvVEVVKPKDGSSSPQLVAFVVLdgsssgsgdgds 421
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1178432446 139 ---------TADPATVRAELARRLPAHMVPASVMALQALPLTVNGKLNTRAL 181
Cdd:cd05918 422 lflepsdefRALVAELRSKLRQRLPSYMVPSVFLPLSHLPLTASGKIDRRAL 473
|
|
| alpha_am_amid |
TIGR03443 |
L-aminoadipate-semialdehyde dehydrogenase; Members of this protein family are ... |
3-274 |
3.58e-40 |
|
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: 156.76 E-value: 3.58e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178432446 3 DVVPIGAPVPGAALVVLDGWLRPVSAGV--VGELYVAGRGVGVGYWRRPGLSASRFVACPFGPPGT-------------- 66
Cdd:TIGR03443 591 DVMPAGKGMKNVQLLVVNRNDRTQTCGVgeVGEIYVRAGGLAEGYLGLPELNAEKFVNNWFVDPSHwidldkennkpere 670
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178432446 67 -------RMYRTGDRVRWRADGQLEYLGRTDDQVKIRGYRVELGEIRTALAELEGVEHAAVIAREDRPGERRLVGYITGT 139
Cdd:TIGR03443 671 fwlgprdRLYRTGDLGRYLPDGNVECCGRADDQVKIRGFRIELGEIDTHLSQHPLVRENVTLVRRDKDEEPTLVSYIVPQ 750
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178432446 140 ADPAT------------------------------VRAELARRLPAHMVPASVMALQALPLTVNGKLNTRALPAP----- 184
Cdd:TIGR03443 751 DKSDEleefksevddeessdpvvkglikyrklikdIREYLKKKLPSYAIPTVIVPLKKLPLNPNGKVDKPALPFPdtaql 830
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178432446 185 ----RYADGDRYRAPANSVEKVLADIYAQVL--GVERVGVDDSFFDLGGDSISA------MRATAAINAALGaglavrTL 252
Cdd:TIGR03443 831 aavaKNRSASAADEEFTETEREIRDLWLELLpnRPATISPDDSFFDLGGHSILAtrmifeLRKKLNVELPLG------LI 904
|
330 340
....*....|....*....|..
gi 1178432446 253 FYAPSVRRLSRQLGTPASAEEL 274
Cdd:TIGR03443 905 FKSPTIKGFAKEVDRLKKGEEL 926
|
|
| MenE/FadK |
COG0318 |
O-succinylbenzoic acid-CoA ligase MenE or related acyl-CoA synthetase (AMP-forming) [Lipid ... |
4-189 |
6.40e-39 |
|
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: 148.03 E-value: 6.40e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178432446 4 VVPIGAPVPGAALVVLDGWLRPVSAGVVGELYVAGRGVGVGYWRRPGLSASRFVacpfgppgTRMYRTGDRVRWRADGQL 83
Cdd:COG0318 268 PGSVGRPLPGVEVRIVDEDGRELPPGEVGEIVVRGPNVMKGYWNDPEATAEAFR--------DGWLRTGDLGRLDEDGYL 339
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178432446 84 EYLGRTDDQVKIRGYRVELGEIRTALAELEGVEHAAVIAREDRPGERRLVGYIT----GTADPATVRAELARRLPAHMVP 159
Cdd:COG0318 340 YIVGRKKDMIISGGENVYPAEVEEVLAAHPGVAEAAVVGVPDEKWGERVVAFVVlrpgAELDAEELRAFLRERLARYKVP 419
|
170 180 190
....*....|....*....|....*....|
gi 1178432446 160 ASVMALQALPLTVNGKLNTRALPApRYADG 189
Cdd:COG0318 420 RRVEFVDELPRTASGKIDRRALRE-RYAAG 448
|
|
| AFD_class_I |
cd04433 |
Adenylate forming domain, Class I, also known as the ANL superfamily; This family is known as ... |
5-175 |
1.47e-30 |
|
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: 122.01 E-value: 1.47e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178432446 5 VPIGAPVPGAALVVLDGWLRPVSAGVVGELYVAGRGVGVGYWRRPGLSASRFvacpfgppGTRMYRTGDRVRWRADGQLE 84
Cdd:cd04433 168 GSVGRPVPGVEVRIVDPDGGELPPGEIGELVVRGPSVMKGYWNNPEATAAVD--------EDGWYRTGDLGRLDEDGYLY 239
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178432446 85 YLGRTDDQVKIRGYRVELGEIRTALAELEGVEHAAVIAREDRPGERRLVGYIT----GTADPATVRAELARRLPAHMVPA 160
Cdd:cd04433 240 IVGRLKDMIKSGGENVYPAEVEAVLLGHPGVAEAAVVGVPDPEWGERVVAVVVlrpgADLDAEELRAHVRERLAPYKVPR 319
|
170
....*....|....*
gi 1178432446 161 SVMALQALPLTVNGK 175
Cdd:cd04433 320 RVVFVDALPRTASGK 334
|
|
| PRK04813 |
PRK04813 |
D-alanine--poly(phosphoribitol) ligase subunit DltA; |
6-181 |
5.28e-27 |
|
D-alanine--poly(phosphoribitol) ligase subunit DltA;
Pssm-ID: 235313 [Multi-domain] Cd Length: 503 Bit Score: 114.61 E-value: 5.28e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178432446 6 PIGAPVPGAALVVLDGWLRPVSAGVVGELYVAGRGVGVGYWRRPGLSASRFvacpFGPPGTRMYRTGDRVRWrADGQLEY 85
Cdd:PRK04813 319 PIGYAKPDSPLLIIDEEGTKLPDGEQGEIVISGPSVSKGYLNNPEKTAEAF----FTFDGQPAYHTGDAGYL-EDGLLFY 393
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178432446 86 LGRTDDQVKIRGYRVELGEIRTALAELEGVEHAAVIAREDRPGERRLVGYITGTAD--------PATVRAELARRLPAHM 157
Cdd:PRK04813 394 QGRIDFQIKLNGYRIELEEIEQNLRQSSYVESAVVVPYNKDHKVQYLIAYVVPKEEdferefelTKAIKKELKERLMEYM 473
|
170 180
....*....|....*....|....
gi 1178432446 158 VPASVMALQALPLTVNGKLNTRAL 181
Cdd:PRK04813 474 IPRKFIYRDSLPLTPNGKIDRKAL 497
|
|
| A_NRPS_alphaAR |
cd17647 |
Alpha-aminoadipate reductase; This family contains L-2-aminoadipate reductase, also known as ... |
3-184 |
2.82e-26 |
|
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: 112.61 E-value: 2.82e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178432446 3 DVVPIGAPVPGAALVVLDGWLRPVSAGV--VGELYVAGRGVGVGYWRRPGLSASRFVACPFGPPG--------------- 65
Cdd:cd17647 285 DVMPAGRGMLNVQLLVVNRNDRTQICGIgeVGEIYVRAGGLAEGYRGLPELNKEKFVNNWFVEPDhwnyldkdnnepwrq 364
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178432446 66 ------TRMYRTGDRVRWRADGQLEYLGRTDDQVKIRGYRVELGEIRTALAELEGVEHAAVIAREDRPGERRLVGYITGT 139
Cdd:cd17647 365 fwlgprDRLYRTGDLGRYLPNGDCECCGRADDQVKIRGFRIELGEIDTHISQHPLVRENITLVRRDKDEEPTLVSYIVPR 444
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1178432446 140 ADPAT-------------------------------VRAELARRLPAHMVPASVMALQALPLTVNGKLNTRALPAP 184
Cdd:cd17647 445 FDKPDdesfaqedvpkevstdpivkgligyrklikdIREFLKKRLASYAIPSLIVVLDKLPLNPNGKVDKPKLQFP 520
|
|
| Acs |
COG0365 |
Acyl-coenzyme A synthetase/AMP-(fatty) acid ligase [Lipid transport and metabolism]; |
1-181 |
8.15e-26 |
|
Acyl-coenzyme A synthetase/AMP-(fatty) acid ligase [Lipid transport and metabolism];
Pssm-ID: 440134 [Multi-domain] Cd Length: 565 Bit Score: 111.36 E-value: 8.15e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178432446 1 GSDVVP--IGAPVPGAALVVLDGWLRPVSAGVVGELYVAGRGVG--VGYWRRPglsaSRFVACPFGP-PGtrMYRTGDRV 75
Cdd:COG0365 353 GLPVKPgsMGKPVPGYDVAVVDEDGNPVPPGEEGELVIKGPWPGmfRGYWNDP----ERYRETYFGRfPG--WYRTGDGA 426
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178432446 76 RWRADGQLEYLGRTDDQVKIRGYRVELGEIRTALAELEGVEHAAVIAREDRPGERRLVGYIT---GTADPATVRAEL--- 149
Cdd:COG0365 427 RRDEDGYFWILGRSDDVINVSGHRIGTAEIESALVSHPAVAEAAVVGVPDEIRGQVVKAFVVlkpGVEPSDELAKELqah 506
|
170 180 190
....*....|....*....|....*....|...
gi 1178432446 150 -ARRLPAHMVPASVMALQALPLTVNGKLNTRAL 181
Cdd:COG0365 507 vREELGPYAYPREIEFVDELPKTRSGKIMRRLL 539
|
|
| AMP-binding |
pfam00501 |
AMP-binding enzyme; |
7-96 |
2.55e-24 |
|
AMP-binding enzyme;
Pssm-ID: 459834 [Multi-domain] Cd Length: 417 Bit Score: 105.47 E-value: 2.55e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178432446 7 IGAPVPGAALVVLD-GWLRPVSAGVVGELYVAGRGVGVGYWRRPGLSASRFVAcpfgppgTRMYRTGDRVRWRADGQLEY 85
Cdd:pfam00501 334 VGRPLPGTEVKIVDdETGEPVPPGEPGELCVRGPGVMKGYLNDPELTAEAFDE-------DGWYRTGDLGRRDEDGYLEI 406
|
90
....*....|.
gi 1178432446 86 LGRTDDQVKIR 96
Cdd:pfam00501 407 VGRKKDQIKLG 417
|
|
| FACL_like_6 |
cd05922 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
7-181 |
1.06e-23 |
|
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ATP-dependent activation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions.
Pssm-ID: 341246 [Multi-domain] Cd Length: 457 Bit Score: 104.06 E-value: 1.06e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178432446 7 IGAPVPGAALVVL--DGWLRPVsaGVVGELYVAGRGVGVGYWRRPGLSASRfvacpfGPPGTRMYrTGDRVRWRADGQLE 84
Cdd:cd05922 288 IGLAIPGGEFEILddDGTPTPP--GEPGEIVHRGPNVMKGYWNDPPYRRKE------GRGGGVLH-TGDLARRDEDGFLF 358
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178432446 85 YLGRTDDQVKIRGYRVELGEIRTALAELEGVEHAAVIAREDRPGErRLVGYITGTA--DPATVRAELARRLPAHMVPASV 162
Cdd:cd05922 359 IVGRRDRMIKLFGNRISPTEIEAAARSIGLIIEAAAVGLPDPLGE-KLALFVTAPDkiDPKDVLRSLAERLPPYKVPATV 437
|
170
....*....|....*....
gi 1178432446 163 MALQALPLTVNGKLNTRAL 181
Cdd:cd05922 438 RVVDELPLTASGKVDYAAL 456
|
|
| BCL_4HBCL |
cd05959 |
Benzoate CoA ligase (BCL) and 4-Hydroxybenzoate-Coenzyme A Ligase (4-HBA-CoA ligase); Benzoate ... |
8-181 |
3.99e-23 |
|
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: 102.83 E-value: 3.99e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178432446 8 GAPVPGAALVVLDGWLRPVSAGVVGELYVAGRGVGVGYWRRPGLSASRFVacpfGPpgtrMYRTGDRVRWRADGQLEYLG 87
Cdd:cd05959 335 GKPVPGYEVELRDEDGGDVADGEPGELYVRGPSSATMYWNNRDKTRDTFQ----GE----WTRTGDKYVRDDDGFYTYAG 406
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178432446 88 RTDDQVKIRGYRVELGEIRTALAELEGVEHAAVIAREDRPGERRLVGYIT---GTADPATVRAELAR----RLPAHMVPA 160
Cdd:cd05959 407 RADDMLKVSGIWVSPFEVESALVQHPAVLEAAVVGVEDEDGLTKPKAFVVlrpGYEDSEALEEELKEfvkdRLAPYKYPR 486
|
170 180
....*....|....*....|.
gi 1178432446 161 SVMALQALPLTVNGKLNTRAL 181
Cdd:cd05959 487 WIVFVDELPKTATGKIQRFKL 507
|
|
| PRK05691 |
PRK05691 |
peptide synthase; Validated |
1-267 |
1.61e-22 |
|
peptide synthase; Validated
Pssm-ID: 235564 [Multi-domain] Cd Length: 4334 Bit Score: 102.55 E-value: 1.61e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178432446 1 GSDVVPIGAPVPGAALVVLD-GWLRPVSAGVVGELYVAGRGVGVGYWRRPGLSASRFVACPfgppGTRMYRTGDrVRWRA 79
Cdd:PRK05691 366 GSVLMSCGRSQPGHAVLIVDpQSLEVLGDNRVGEIWASGPSIAHGYWRNPEASAKTFVEHD----GRTWLRTGD-LGFLR 440
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178432446 80 DGQLEYLGRTDDQVKIRGYRVELGEI-RTALAELEGVEHA--AVIAREDRPGE---------RRLVGYITGTADPATVRA 147
Cdd:PRK05691 441 DGELFVTGRLKDMLIVRGHNLYPQDIeKTVEREVEVVRKGrvAAFAVNHQGEEgigiaaeisRSVQKILPPQALIKSIRQ 520
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178432446 148 ELARRLpaHMVPASVMALQ--ALPLTVNGKLNTRA---------------LPAPRYADGDRYRAPANSVEKVLADIYAQV 210
Cdd:PRK05691 521 AVAEAC--QEAPSVVLLLNpgALPKTSSGKLQRSAcrlrladgsldsyalFPALQAVEAAQTAASGDELQARIAAIWCEQ 598
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*..
gi 1178432446 211 LGVERVGVDDSFFDLGGDSISAMRATAAINAALGAGLAVRTLFYAPSVRRLSRQLGT 267
Cdd:PRK05691 599 LKVEQVAADDHFFLLGGNSIAATQVVARLRDELGIDLNLRQLFEAPTLAAFSAAVAR 655
|
|
| BCL_like |
cd05919 |
Benzoate CoA ligase (BCL) and similar adenylate forming enzymes; This family contains benzoate ... |
8-181 |
1.87e-22 |
|
Benzoate CoA ligase (BCL) and similar adenylate forming enzymes; This family contains benzoate CoA ligase (BCL) and related ligases that catalyze the acylation of benzoate derivatives, 2-aminobenzoate and 4-hydroxybenzoate. Aromatic compounds represent the second most abundant class of organic carbon compounds after carbohydrates. Xenobiotic aromatic compounds are also a major class of man-made pollutants. Some bacteria use benzoate as the sole source of carbon and energy through benzoate degradation. Benzoate degradation starts with its activation to benzoyl-CoA by benzoate CoA ligase. The reaction catalyzed by benzoate CoA ligase proceeds via a two-step process; the first ATP-dependent step forms an acyl-AMP intermediate, and the second step forms the acyl-CoA ester with release of the AMP.
Pssm-ID: 341243 [Multi-domain] Cd Length: 436 Bit Score: 100.23 E-value: 1.87e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178432446 8 GAPVPGAALVVLDGWLRPVSAGVVGELYVAGRGVGVGYWRRPGLSASRFVAcpfgppgtRMYRTGDRVRWRADGQLEYLG 87
Cdd:cd05919 263 GRPVPGYEIRLVDEEGHTIPPGEEGDLLVRGPSAAVGYWNNPEKSRATFNG--------GWYRTGDKFCRDADGWYTHAG 334
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178432446 88 RTDDQVKIRGYRVELGEIRTALAELEGVEHAAVIAREDRPGERRLVGYITgTADPATVRAELAR--------RLPAHMVP 159
Cdd:cd05919 335 RADDMLKVGGQWVSPVEVESLIIQHPAVAEAAVVAVPESTGLSRLTAFVV-LKSPAAPQESLARdihrhlleRLSAHKVP 413
|
170 180
....*....|....*....|..
gi 1178432446 160 ASVMALQALPLTVNGKLNTRAL 181
Cdd:cd05919 414 RRIAFVDELPRTATGKLQRFKL 435
|
|
| Thioesterase |
pfam00975 |
Thioesterase domain; Peptide synthetases are involved in the non-ribosomal synthesis of ... |
287-389 |
7.27e-22 |
|
Thioesterase domain; Peptide synthetases are involved in the non-ribosomal synthesis of peptide antibiotics. Next to the operons encoding these enzymes, in almost all cases, are genes that encode proteins that have similarity to the type II fatty acid thioesterases of vertebrates. There are also modules within the peptide synthetases that also share this similarity. With respect to antibiotic production, thioesterases are required for the addition of the last amino acid to the peptide antibiotic, thereby forming a cyclic antibiotic. Thioesterases (non-integrated) have molecular masses of 25-29 kDa.
Pssm-ID: 395776 [Multi-domain] Cd Length: 223 Bit Score: 94.38 E-value: 7.27e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178432446 287 PLWCIHDGFGLSWPYRALGRYL--DCPVIGInRVPQNGEGEP--ESIRAMAARYADTLQALYPDGPYKLLGWSFGGVVAQ 362
Cdd:pfam00975 2 PLFCFPPAGGSASSFRSLARRLppPAEVLAV-QYPGRGRGEPplNSIEALADEYAEALRQIQPEGPYALFGHSMGGMLAF 80
|
90 100
....*....|....*....|....*..
gi 1178432446 363 ELAIELQRRGCVVQSLVLLDAPYSATK 389
Cdd:pfam00975 81 EVARRLERQGEAVRSLFLSDASAPHTV 107
|
|
| A_NRPS_acs4 |
cd17654 |
acyl-CoA synthetase family member 4; This family of the adenylation (A) domain of nonribosomal ... |
5-181 |
1.40e-20 |
|
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: 94.46 E-value: 1.40e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178432446 5 VPIGAPVPGAALVVLDGWLRPVSagvvGELYVAGRgVGVGYWRrpglsasrfvaCPFGPPGTRMYRTGDRVRwRADGQLE 84
Cdd:cd17654 293 VQLGSPLLGTVIEVRDQNGSEGT----GQVFLGGL-NRVCILD-----------DEVTVPKGTMRATGDFVT-VKDGELF 355
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178432446 85 YLGRTDDQVKIRGYRVELGEIRTALAELEGVEHAAVIAREDrpgeRRLVGYITGTADPATVRAELAR-RLPAHMVPASVM 163
Cdd:cd17654 356 FLGRKDSQIKRRGKRINLDLIQQVIESCLGVESCAVTLSDQ----QRLIAFIVGESSSSRIHKELQLtLLSSHAIPDTFV 431
|
170
....*....|....*...
gi 1178432446 164 ALQALPLTVNGKLNTRAL 181
Cdd:cd17654 432 QIDKLPLTSHGKVDKSEL 449
|
|
| benz_CoA_lig |
TIGR02262 |
benzoate-CoA ligase family; Characterized members of this protein family include benzoate-CoA ... |
8-176 |
2.61e-18 |
|
benzoate-CoA ligase family; Characterized members of this protein family include benzoate-CoA ligase, 4-hydroxybenzoate-CoA ligase, 2-aminobenzoate-CoA ligase, etc. Members are related to fatty acid and acetate CoA ligases.
Pssm-ID: 274059 [Multi-domain] Cd Length: 505 Bit Score: 87.97 E-value: 2.61e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178432446 8 GAPVPGAALVVLDGWLRPVSAGVVGELYVAGRGVGVGYWRRPGLSASRFVAcpfgpPGTRmyrTGDRVRWRADGQLEYLG 87
Cdd:TIGR02262 333 GKPVPGYRLRLVGDGGQDVADGEPGELLISGPSSATMYWNNRAKSRDTFQG-----EWTR---SGDKYVRNDDGSYTYAG 404
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178432446 88 RTDDQVKIRGYRVELGEIRTALAELEGVEHAAVIAREDRPGERRLVGYIT----GTADPATVRAELARRLPAHMVPASVM 163
Cdd:TIGR02262 405 RTDDMLKVSGIYVSPFEIESALIQHPAVLEAAVVGVADEDGLIKPKAFVVlrpgQTALETELKEHVKDRLAPYKYPRWIV 484
|
170
....*....|...
gi 1178432446 164 ALQALPLTVNGKL 176
Cdd:TIGR02262 485 FVDDLPKTATGKI 497
|
|
| MACS_like_3 |
cd05971 |
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the ... |
7-181 |
8.36e-18 |
|
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: 85.95 E-value: 8.36e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178432446 7 IGAPVPGAALVVLDGWLRPVSAGVVGELYVAgRGVGV---GYWRRPGLSASRFVacpfgppgTRMYRTGDRVRWRADGQL 83
Cdd:cd05971 262 MGKPIPGHRVAIVDDNGTPLPPGEVGEIAVE-LPDPVaflGYWNNPSATEKKMA--------GDWLLTGDLGRKDSDGYF 332
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178432446 84 EYLGRTDDQVKIRGYRVELGEIRTALAELEGVEHAAVIAREDrPGERRLV--------GYITGTADPATVRAELARRLPA 155
Cdd:cd05971 333 WYVGRDDDVITSSGYRIGPAEIEECLLKHPAVLMAAVVGIPD-PIRGEIVkafvvlnpGETPSDALAREIQELVKTRLAA 411
|
170 180
....*....|....*....|....*.
gi 1178432446 156 HMVPASVMALQALPLTVNGKLNTRAL 181
Cdd:cd05971 412 HEYPREIEFVNELPRTATGKIRRREL 437
|
|
| AcpA |
COG3433 |
Acyl carrier protein/domain [Lipid transport and metabolism, Secondary metabolites ... |
2-273 |
1.06e-17 |
|
Acyl carrier protein/domain [Lipid transport and metabolism, Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 442659 [Multi-domain] Cd Length: 295 Bit Score: 83.65 E-value: 1.06e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178432446 2 SDVVPIGAPVPGAALVVLDGWLRPVSAGVVGELYVAGRGVGVGYWRRPGLSASRFVACPFGPP------GTRMYRTGDRV 75
Cdd:COG3433 9 APPTPDEPPPVIPPAIVQARALLLIVDLQGYFGGFGGEGGLLGAGLLLRIRLLAAAARAPFIPvpypaqPGRQADDLRLL 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178432446 76 RWRADGQLEYLGRTDDQVKIRGYRVELGEIRTALAELEGVEHAAVIAREDRPGERRLVGYITGTADPATVRAELARR--L 153
Cdd:COG3433 89 LRRGLGPGGGLERLVQQVVIRAERGEEEELLLVLRAAAVVRVAVLAALRGAGVGLLLIVGAVAALDGLAAAAALAALdkV 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178432446 154 PAHMVPASVMALQALPLTVNGKLNTRALPAP-------RYADGDRYRAPANSVEKVLADIyAQVLGV--ERVGVDDSFFD 224
Cdd:COG3433 169 PPDVVAASAVVALDALLLLALKVVARAAPALaaaeallAAASPAPALETALTEEELRADV-AELLGVdpEEIDPDDNLFD 247
|
250 260 270 280
....*....|....*....|....*....|....*....|....*....
gi 1178432446 225 LGGDSISAMRATAAINAAlGAGLAVRTLFYAPSVRRLSRQLGTPASAEE 273
Cdd:COG3433 248 LGLDSIRLMQLVERWRKA-GLDVSFADLAEHPTLAAWWALLAAAQAAAA 295
|
|
| MCS |
cd05941 |
Malonyl-CoA synthetase (MCS); MCS catalyzes the formation of malonyl-CoA in a two-step ... |
7-181 |
1.70e-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: 85.03 E-value: 1.70e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178432446 7 IGAPVPGA-ALVVLDGWLRPVSAGVVGELYVAGRGVGVGYWRRPGLSASRFVACPFgppgtrmYRTGDRVRWRADGQLEY 85
Cdd:cd05941 266 VGMPLPGVqARIVDEETGEPLPRGEVGEIQVRGPSVFKEYWNKPEATKEEFTDDGW-------FKTGDLGVVDEDGYYWI 338
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178432446 86 LGRT-DDQVKIRGYRVELGEIRTALAELEGVEHAAVIAREDRPGERRLVGYITGTADPATVRAE-----LARRLPAHMVP 159
Cdd:cd05941 339 LGRSsVDIIKSGGYKVSALEIERVLLAHPGVSECAVIGVPDPDWGERVVAVVVLRAGAAALSLEelkewAKQRLAPYKRP 418
|
170 180
....*....|....*....|..
gi 1178432446 160 ASVMALQALPLTVNGKLNTRAL 181
Cdd:cd05941 419 RRLILVDELPRNAMGKVNKKEL 440
|
|
| PRK09088 |
PRK09088 |
acyl-CoA synthetase; Validated |
8-176 |
1.71e-16 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 181644 [Multi-domain] Cd Length: 488 Bit Score: 82.16 E-value: 1.71e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178432446 8 GAPVPGAALVVLDGWLRPVSAGVVGELYVAGRGVGVGYWRRPGLSASRFVACPFgppgtrmYRTGDRVRWRADGQLEYLG 87
Cdd:PRK09088 309 GIPTPTVQTRVVDDQGNDCPAGVPGELLLRGPNLSPGYWRRPQATARAFTGDGW-------FRTGDIARRDADGFFWVVD 381
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178432446 88 RTDDQVKIRGYRVELGEIRTALAELEGVEHAAVIARED-RPGErrlVGYI-----TGTA-DPATVRAELARRLPAHMVPA 160
Cdd:PRK09088 382 RKKDMFISGGENVYPAEIEAVLADHPGIRECAVVGMADaQWGE---VGYLaivpaDGAPlDLERIRSHLSTRLAKYKVPK 458
|
170
....*....|....*.
gi 1178432446 161 SVMALQALPLTVNGKL 176
Cdd:PRK09088 459 HLRLVDALPRTASGKL 474
|
|
| FACL_DitJ_like |
cd05934 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
6-182 |
2.80e-15 |
|
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: 78.10 E-value: 2.80e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178432446 6 PIGAPVPGAALVVLDGWLRPVSAGVVGELYV-AGRGVGV--GYWRRPGLSASRFvacpfgPPGtrMYRTGDRVRWRADGQ 82
Cdd:cd05934 247 SIGRPAPGYEVRIVDDDGQELPAGEPGELVIrGLRGWGFfkGYYNMPEATAEAM------RNG--WFHTGDLGYRDADGF 318
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178432446 83 LEYLGRTDDQVKIRGYRVELGEIRTALAELEGVEHAAVIAREDRPGERRLVGYIT----GTADPATVRAELARRLPAHMV 158
Cdd:cd05934 319 FYFVDRKKDMIRRRGENISSAEVERAILRHPAVREAAVVAVPDEVGEDEVKAVVVlrpgETLDPEELFAFCEGQLAYFKV 398
|
170 180
....*....|....*....|....
gi 1178432446 159 PASVMALQALPLTVNGKLNTRALP 182
Cdd:cd05934 399 PRYIRFVDDLPKTPTEKVAKAQLR 422
|
|
| PRK06188 |
PRK06188 |
acyl-CoA synthetase; Validated |
8-191 |
5.05e-15 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 235731 [Multi-domain] Cd Length: 524 Bit Score: 77.72 E-value: 5.05e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178432446 8 GAPVPGAALVVLDGWLRPVSAGVVGELYVAGRGVGVGYWRRPGLSASRFvacpfgppGTRMYRTGDRVRWRADGQLEYLG 87
Cdd:PRK06188 342 GRPTPGLRVALLDEDGREVAQGEVGEICVRGPLVMDGYWNRPEETAEAF--------RDGWLHTGDVAREDEDGFYYIVD 413
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178432446 88 RTDDQVKIRGYRVELGEIRTALAELEGVEHAAVIARED-------------RPGErrlvgyitgTADPATVRAELARRLP 154
Cdd:PRK06188 414 RKKDMIVTGGFNVFPREVEDVLAEHPAVAQVAVIGVPDekwgeavtavvvlRPGA---------AVDAAELQAHVKERKG 484
|
170 180 190
....*....|....*....|....*....|....*..
gi 1178432446 155 AHMVPASVMALQALPLTVNGKLNTRALPAPRYADGDR 191
Cdd:PRK06188 485 SVHAPKQVDFVDSLPLTALGKPDKKALRARYWEGRGR 521
|
|
| FACL_FadD13-like |
cd17631 |
fatty acyl-CoA synthetase, including FadD13; This family contains fatty acyl-CoA synthetases, ... |
8-176 |
6.90e-15 |
|
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: 76.88 E-value: 6.90e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178432446 8 GAPVPGAALVVLDGWLRPVSAGVVGELYVAGRGVGVGYWRRPGLSASRFVACPFgppgtrmyRTGDRVRWRADGQLEYLG 87
Cdd:cd17631 269 GRPVFFVEVRIVDPDGREVPPGEVGEIVVRGPHVMAGYWNRPEATAAAFRDGWF--------HTGDLGRLDEDGYLYIVD 340
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178432446 88 RTDDQVKIRGYRVELGEIRTALAELEGVEHAAVIARED-RPGERRL---VGYITGTADPATVRAELARRLPAHMVPASVM 163
Cdd:cd17631 341 RKKDMIISGGENVYPAEVEDVLYEHPAVAEVAVIGVPDeKWGEAVVavvVPRPGAELDEDELIAHCRERLARYKIPKSVE 420
|
170
....*....|...
gi 1178432446 164 ALQALPLTVNGKL 176
Cdd:cd17631 421 FVDALPRNATGKI 433
|
|
| EntE |
COG1021 |
EntE, 2,3-dihydroxybenzoate-AMP synthase component of non-ribosomal peptide synthetase ... |
24-181 |
6.95e-15 |
|
EntE, 2,3-dihydroxybenzoate-AMP synthase component of non-ribosomal peptide synthetase [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 440644 [Multi-domain] Cd Length: 533 Bit Score: 77.49 E-value: 6.95e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178432446 24 RPVSAGVVGELYVAGRGVGVGYWRRPGLSASRFVACPFgppgtrmYRTGDRVRWRADGQLEYLGRTDDQVkIRGyrvelG 103
Cdd:COG1021 373 NPVPPGEVGELLTRGPYTIRGYYRAPEHNARAFTPDGF-------YRTGDLVRRTPDGYLVVEGRAKDQI-NRG-----G 439
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178432446 104 E------IRTALAELEGVEHAAVIARED-RPGErRLVGYITGTA---DPATVRAELARR-LPAHMVPASVMALQALPLTV 172
Cdd:COG1021 440 EkiaaeeVENLLLAHPAVHDAAVVAMPDeYLGE-RSCAFVVPRGeplTLAELRRFLRERgLAAFKLPDRLEFVDALPLTA 518
|
....*....
gi 1178432446 173 NGKLNTRAL 181
Cdd:COG1021 519 VGKIDKKAL 527
|
|
| ACS-like |
cd17634 |
acetate-CoA ligase; This family includes acyl- and aryl-CoA ligases, as well as the ... |
10-176 |
1.23e-14 |
|
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: 76.85 E-value: 1.23e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178432446 10 PVPGAALVVLDGWLRPVSAGVVGELYVAGR--GVGVGYWRRPGLSASRFVACPFGppgtrMYRTGDRVRWRADGQLEYLG 87
Cdd:cd17634 416 PVFGVQPAVVDNEGHPQPGGTEGNLVITDPwpGQTRTLFGDHERFEQTYFSTFKG-----MYFSGDGARRDEDGYYWITG 490
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178432446 88 RTDDQVKIRGYRVELGEIRTALAELEGVEHAAVIAREDRPGERRLVGYIT---GTADPATVRAEL----ARRLPAHMVPA 160
Cdd:cd17634 491 RSDDVINVAGHRLGTAEIESVLVAHPKVAEAAVVGIPHAIKGQAPYAYVVlnhGVEPSPELYAELrnwvRKEIGPLATPD 570
|
170
....*....|....*.
gi 1178432446 161 SVMALQALPLTVNGKL 176
Cdd:cd17634 571 VVHWVDSLPKTRSGKI 586
|
|
| FC-FACS_FadD_like |
cd05936 |
Prokaryotic long-chain fatty acid CoA synthetases similar to Escherichia coli FadD; This ... |
7-181 |
1.26e-14 |
|
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: 76.45 E-value: 1.26e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178432446 7 IGAPVPGAALVVLDGWLRPVSAGVVGELYVAGRGVGVGYWRRPGLSASRFVACPFgppgtrmyRTGDRVRWRADGQLEYL 86
Cdd:cd05936 297 IGIPLPGTEVKIVDDDGEELPPGEVGELWVRGPQVMKGYWNRPEETAEAFVDGWL--------RTGDIGYMDEDGYFFIV 368
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178432446 87 GRTDDQVKIRGYRVELGEIRTALAELEGVEHAAVIAREDRPGERRLVGYIT----GTADPATVRAELARRLPAHMVPASV 162
Cdd:cd05936 369 DRKKDMIIVGGFNVYPREVEEVLYEHPAVAEAAVVGVPDPYSGEAVKAFVVlkegASLTEEEIIAFCREQLAGYKVPRQV 448
|
170
....*....|....*....
gi 1178432446 163 MALQALPLTVNGKLNTRAL 181
Cdd:cd05936 449 EFRDELPKSAVGKILRREL 467
|
|
| MACS_like_2 |
cd05973 |
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the ... |
8-176 |
2.35e-14 |
|
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: 75.25 E-value: 2.35e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178432446 8 GAPVPGAALVVLDGWLRPVSAGVVGELYVAGRGVGV----GYWRRPGLSASrfvacpfgppgTRMYRTGDRVRWRADGQL 83
Cdd:cd05973 262 GRAMPGWRVAVLDDDGDELGPGEPGRLAIDIANSPLmwfrGYQLPDTPAID-----------GGYYLTGDTVEFDPDGSF 330
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178432446 84 EYLGRTDDQVKIRGYRVELGEIRTALAELEGVEHAAVIAREDRPGERRLVGYIT---GTADPATVRAELA----RRLPAH 156
Cdd:cd05973 331 SFIGRADDVITMSGYRIGPFDVESALIEHPAVAEAAVIGVPDPERTEVVKAFVVlrgGHEGTPALADELQlhvkKRLSAH 410
|
170 180
....*....|....*....|
gi 1178432446 157 MVPASVMALQALPLTVNGKL 176
Cdd:cd05973 411 AYPRTIHFVDELPKTPSGKI 430
|
|
| PRK06178 |
PRK06178 |
acyl-CoA synthetase; Validated |
2-175 |
2.95e-14 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 235724 [Multi-domain] Cd Length: 567 Bit Score: 75.46 E-value: 2.95e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178432446 2 SDVVPIGAPVPGAALVVLD---GWLRPVsaGVVGELYVAGRGVGVGYWRRPGLSASRFVacpfgppgTRMYRTGDRVRWR 78
Cdd:PRK06178 384 SQPVFVGLPVPGTEFKICDfetGELLPL--GAEGEIVVRTPSLLKGYWNKPEATAEALR--------DGWLHTGDIGKID 453
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178432446 79 ADGQLEYLGRTDDQVKIRGYRVELGEIRTALAELEGVEHAAVIAREDRPGERRLVGYIT----GTADPATVRAELARRLP 154
Cdd:PRK06178 454 EQGFLHYLGRRKEMLKVNGMSVFPSEVEALLGQHPAVLGSAVVGRPDPDKGQVPVAFVQlkpgADLTAAALQAWCRENMA 533
|
170 180
....*....|....*....|.
gi 1178432446 155 AHMVPaSVMALQALPLTVNGK 175
Cdd:PRK06178 534 VYKVP-EIRIVDALPMTATGK 553
|
|
| A_NRPS_TubE_like |
cd05906 |
The adenylation domain (A domain) of a family of nonribosomal peptide synthetases (NRPSs) ... |
5-189 |
4.94e-14 |
|
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: 74.63 E-value: 4.94e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178432446 5 VPIGAPVPGAALVVLDGWLRPVSAGVVGELYVAGRGVGVGYWRRPGLSASRFVACPFgppgtrmYRTGDrVRWRADGQLE 84
Cdd:cd05906 354 VSLGRPIPGVSMRIVDDEGQLLPEGEVGRLQVRGPVVTKGYYNNPEANAEAFTEDGW-------FRTGD-LGFLDNGNLT 425
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178432446 85 YLGRTDDQVKIRGYRVELGEIRTALAELEGVEH---AAVIAREDRPGERRLVGYITGTADPATVRAELARRL-------- 153
Cdd:cd05906 426 ITGRTKDTIIVNGVNYYSHEIEAAVEEVPGVEPsftAAFAVRDPGAETEELAIFFVPEYDLQDALSETLRAIrsvvsrev 505
|
170 180 190
....*....|....*....|....*....|....*....
gi 1178432446 154 ---PAHMVPasvMALQALPLTVNGKLnTRALPAPRYADG 189
Cdd:cd05906 506 gvsPAYLIP---LPKEEIPKTSLGKI-QRSKLKAAFEAG 540
|
|
| 23DHB-AMP_lg |
cd05920 |
2,3-dihydroxybenzoate-AMP ligase; 2,3-dihydroxybenzoate-AMP ligase activates 2, ... |
8-181 |
7.36e-14 |
|
2,3-dihydroxybenzoate-AMP ligase; 2,3-dihydroxybenzoate-AMP ligase activates 2,3-dihydroxybenzoate (DHB) by ligation of AMP from ATP with the release of pyrophosphate. However, it can also catalyze the ATP-PPi exchange for 2,3-DHB analogs, such as salicyclic acid (o-hydrobenzoate), as well as 2,4-DHB and 2,5-DHB, but with less efficiency. Proteins in this family are the stand-alone adenylation components of non-ribosomal peptide synthases (NRPSs) involved in the biosynthesis of siderophores, which are low molecular weight iron-chelating compounds synthesized by many bacteria to aid in the acquisition of this vital trace elements. In Escherichia coli, the 2,3-dihydroxybenzoate-AMP ligase is called EntE, the adenylation component of the enterobactin NRPS system.
Pssm-ID: 341244 [Multi-domain] Cd Length: 482 Bit Score: 73.90 E-value: 7.36e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178432446 8 GAPV-PGAALVVLDGWLRPVSAGVVGELYVAGRGVGVGYWRRPGLSASRFVACPFgppgtrmYRTGDRVRWRADGQLEYL 86
Cdd:cd05920 311 GRPMsPDDEIRVVDEEGNPVPPGEEGELLTRGPYTIRGYYRAPEHNARAFTPDGF-------YRTGDLVRRTPDGYLVVE 383
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178432446 87 GRTDDQVKIRGYRVELGEIRTALAELEGVEHAAVIARED-RPGERRLVGYITGTADP--ATVRAELARR-LPAHMVPASV 162
Cdd:cd05920 384 GRIKDQINRGGEKIAAEEVENLLLRHPAVHDAAVVAMPDeLLGERSCAFVVLRDPPPsaAQLRRFLRERgLAAYKLPDRI 463
|
170
....*....|....*....
gi 1178432446 163 MALQALPLTVNGKLNTRAL 181
Cdd:cd05920 464 EFVDSLPLTAVGKIDKKAL 482
|
|
| OSB_MenE-like |
cd17630 |
O-succinylbenzoic acid-CoA ligase; This family contains O-succinylbenzoyl-CoA (OSB-CoA) ... |
8-181 |
1.08e-13 |
|
O-succinylbenzoic acid-CoA ligase; This family contains O-succinylbenzoyl-CoA (OSB-CoA) synthetase (also known as O-succinylbenzoic acid CoA ligase) that belongs to the ANL superfamily and catalyzes the ligation of CoA to o-succinylbenzoate (OSB). It includes MenE in the bacterial menaquinone biosynthesis pathway which is a promising target for the development of novel antibacterial agents. MenE catalyzes CoA ligation via an acyl-adenylate intermediate; tight-binding inhibitors of MenE based on stable acyl-sulfonyladenosine analogs of this intermediate provide a pathway toward the development of optimized MenE inhibitors.
Pssm-ID: 341285 [Multi-domain] Cd Length: 325 Bit Score: 72.36 E-value: 1.08e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178432446 8 GAPVPGAALVVLDGwlrpvsagvvGELYVAGRGVGVGYWRRPGLSasrfvacPFGPPGTrmYRTGDRVRWRADGQLEYLG 87
Cdd:cd17630 165 GVLLPGRELRIVED----------GEIWVGGASLAMGYLRGQLVP-------EFNEDGW--FTTKDLGELHADGRLTVLG 225
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178432446 88 RTDDQVKIRGYRVELGEIRTALAELEGVEHAAVIAREDRPGERRLVGYITG--TADPATVRAELARRLPAHMVPASVMAL 165
Cdd:cd17630 226 RADNMIISGGENIQPEEIEAALAAHPAVRDAFVVGVPDEELGQRPVAVIVGrgPADPAELRAWLKDKLARFKLPKRIYPV 305
|
170
....*....|....*.
gi 1178432446 166 QALPLTVNGKLNTRAL 181
Cdd:cd17630 306 PELPRTGGGKVDRRAL 321
|
|
| MACS_like_4 |
cd05969 |
Uncharacterized subfamily of Acetyl-CoA synthetase like family (ACS); This family is most ... |
7-183 |
1.15e-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: 73.31 E-value: 1.15e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178432446 7 IGAPVPGAALVVLDGWLRPVSAGVVGELYVAGR--GVGVGYWRRPGLSASRFVacpfgppgTRMYRTGDRVRWRADGQLE 84
Cdd:cd05969 262 MGKPLPGVKAAVVDENGNELPPGTKGILALKPGwpSMFRGIWNDEERYKNSFI--------DGWYLTGDLAYRDEDGYFW 333
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178432446 85 YLGRTDDQVKIRGYRVELGEIRTALAELEGVEHAAVIAREDRPGERRLVGYIT---GTADPATVRAEL----ARRLPAHM 157
Cdd:cd05969 334 FVGRADDIIKTSGHRVGPFEVESALMEHPAVAEAGVIGKPDPLRGEIIKAFISlkeGFEPSDELKEEIinfvRQKLGAHV 413
|
170 180
....*....|....*....|....*.
gi 1178432446 158 VPASVMALQALPLTVNGKLNTRALPA 183
Cdd:cd05969 414 APREIEFVDNLPKTRSGKIMRRVLKA 439
|
|
| PRK06164 |
PRK06164 |
acyl-CoA synthetase; Validated |
8-174 |
1.23e-13 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 235722 [Multi-domain] Cd Length: 540 Bit Score: 73.62 E-value: 1.23e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178432446 8 GAPVPGAALV----VLDGWLRPvsAGVVGELYVAGRGVGVGYWRRPGLSASRFVACPFgppgtrmYRTGDRVRWRADGQL 83
Cdd:PRK06164 352 GRPASPEARVrardPQDGALLP--DGESGEIEIRAPSLMRGYLDNPDATARALTDDGY-------FRTGDLGYTRGDGQF 422
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178432446 84 EYLGRTDDQVKIRGYRVELGEIRTALAELEGVEHAAVIAREdRPGERRLVGYITGTA----DPATVRAELARRLPAHMVP 159
Cdd:PRK06164 423 VYQTRMGDSLRLGGFLVNPAEIEHALEALPGVAAAQVVGAT-RDGKTVPVAFVIPTDgaspDEAGLMAACREALAGFKVP 501
|
170
....*....|....*
gi 1178432446 160 ASVMALQALPLTVNG 174
Cdd:PRK06164 502 ARVQVVEAFPVTESA 516
|
|
| PRK07787 |
PRK07787 |
acyl-CoA synthetase; Validated |
7-185 |
1.90e-13 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236096 [Multi-domain] Cd Length: 471 Bit Score: 72.72 E-value: 1.90e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178432446 7 IGAPVPGAALVVLDGWLRPVSAGV--VGELYVAGRGVGVGYWRRPGLSASRFVACPFgppgtrmYRTGDRVRWRADGQLE 84
Cdd:PRK07787 295 VGLPLAGVETRLVDEDGGPVPHDGetVGELQVRGPTLFDGYLNRPDATAAAFTADGW-------FRTGDVAVVDPDGMHR 367
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178432446 85 YLGR-TDDQVKIRGYRVELGEIRTALAELEGVEHAAVIAREDRPGERRLVGYITGTADPATvrAEL----ARRLPAHMVP 159
Cdd:PRK07787 368 IVGReSTDLIKSGGYRIGAGEIETALLGHPGVREAAVVGVPDDDLGQRIVAYVVGADDVAA--DELidfvAQQLSVHKRP 445
|
170 180
....*....|....*....|....*.
gi 1178432446 160 ASVMALQALPLTVNGKLNTRALPAPR 185
Cdd:PRK07787 446 REVRFVDALPRNAMGKVLKKQLLSEG 471
|
|
| CHC_CoA_lg |
cd05903 |
Cyclohexanecarboxylate-CoA ligase (also called cyclohex-1-ene-1-carboxylate:CoA ligase); ... |
8-176 |
2.22e-13 |
|
Cyclohexanecarboxylate-CoA ligase (also called cyclohex-1-ene-1-carboxylate:CoA ligase); Cyclohexanecarboxylate-CoA ligase activates the aliphatic ring compound, cyclohexanecarboxylate, for degradation. It catalyzes the synthesis of cyclohexanecarboxylate-CoA thioesters in a two-step reaction involving the formation of cyclohexanecarboxylate-AMP anhydride, followed by the nucleophilic substitution of AMP by CoA.
Pssm-ID: 341229 [Multi-domain] Cd Length: 437 Bit Score: 72.41 E-value: 2.22e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178432446 8 GAPVPGAALVVLDGWLRPVSAGVVGELYVAGRGVGVGYWRRPGLSAsrfVACPFGppgtrMYRTGDRVRWRADGQLEYLG 87
Cdd:cd05903 265 GRPLPGVEIKVVDDTGATLAPGVEGELLSRGPSVFLGYLDRPDLTA---DAAPEG-----WFRTGDLARLDEDGYLRITG 336
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178432446 88 RTDDQVKIRGYRVELGEIRTALAELEGVEHAAVIARED-RPGERR---LVGYITGTADPATVRAELAR-RLPAHMVPASV 162
Cdd:cd05903 337 RSKDIIIRGGENIPVLEVEDLLLGHPGVIEAAVVALPDeRLGERAcavVVTKSGALLTFDELVAYLDRqGVAKQYWPERL 416
|
170
....*....|....
gi 1178432446 163 MALQALPLTVNGKL 176
Cdd:cd05903 417 VHVDDLPRTPSGKV 430
|
|
| AcpP |
COG0236 |
Acyl carrier protein [Lipid transport and metabolism]; Acyl carrier protein is part of the ... |
194-265 |
6.32e-13 |
|
Acyl carrier protein [Lipid transport and metabolism]; Acyl carrier protein is part of the Pathway/BioSystem: Fatty acid biosynthesis
Pssm-ID: 440006 [Multi-domain] Cd Length: 80 Bit Score: 64.10 E-value: 6.32e-13
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1178432446 194 APANSVEKVLADIYAQVLGV--ERVGVDDSFF-DLGGDSISAMRATAAINAALGAGLAVRTLFYAPSVRRLSRQL 265
Cdd:COG0236 1 MPREELEERLAEIIAEVLGVdpEEITPDDSFFeDLGLDSLDAVELIAALEEEFGIELPDTELFEYPTVADLADYL 75
|
|
| FAAL |
cd05931 |
Fatty acyl-AMP ligase (FAAL); FAAL belongs to the class I adenylate forming enzyme family and ... |
1-180 |
1.65e-12 |
|
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: 69.96 E-value: 1.65e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178432446 1 GSDVVPIGAPVPGAALVVLD-GWLRPVSAGVVGELYVAGRGVGVGYWRRPGLSASRFVACPfGPPGTRMYRTGDrVRWRA 79
Cdd:cd05931 351 ARELVSCGRPLPDQEVRIVDpETGRELPDGEVGEIWVRGPSVASGYWGRPEATAETFGALA-ATDEGGWLRTGD-LGFLH 428
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178432446 80 DGQLEYLGRTDDQVKIRGYRVELGEIRTALAELEGVEH---AAVIAREDRPGERRLV-----GYITGTADPAT---VRAE 148
Cdd:cd05931 429 DGELYITGRLKDLIIVRGRNHYPQDIEATAEEAHPALRpgcVAAFSVPDDGEERLVVvaeveRGADPADLAAIaaaIRAA 508
|
170 180 190
....*....|....*....|....*....|....*
gi 1178432446 149 LARRlpaHMVPASVMAL---QALPLTVNGKLNTRA 180
Cdd:cd05931 509 VARE---HGVAPADVVLvrpGSIPRTSSGKIQRRA 540
|
|
| PRK06187 |
PRK06187 |
long-chain-fatty-acid--CoA ligase; Validated |
8-190 |
1.82e-12 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 235730 [Multi-domain] Cd Length: 521 Bit Score: 69.83 E-value: 1.82e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178432446 8 GAPVPGAALVVLDGWLR--PVSAGVVGELYVAGRGVGVGYWRRPGLSASRFVAcpfgppGtrMYRTGDRVRWRADGQLEY 85
Cdd:PRK06187 342 GRPLPGVEARIVDDDGDelPPDGGEVGEIIVRGPWLMQGYWNRPEATAETIDG------G--WLHTGDVGYIDEDGYLYI 413
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178432446 86 LGRTDDQVKIRG---YRVELGEirtALAELEGVEHAAVIARED-RPGERRLVgYITG----TADPATVRAELARRLPAHM 157
Cdd:PRK06187 414 TDRIKDVIISGGeniYPRELED---ALYGHPAVAEVAVIGVPDeKWGERPVA-VVVLkpgaTLDAKELRAFLRGRLAKFK 489
|
170 180 190
....*....|....*....|....*....|...
gi 1178432446 158 VPASVMALQALPLTVNGKLNTRALPAPrYADGD 190
Cdd:PRK06187 490 LPKRIAFVDELPRTSVGKILKRVLREQ-YAEGK 521
|
|
| PP-binding |
pfam00550 |
Phosphopantetheine attachment site; A 4'-phosphopantetheine prosthetic group is attached ... |
201-259 |
2.84e-12 |
|
Phosphopantetheine attachment site; A 4'-phosphopantetheine prosthetic group is attached through a serine. This prosthetic group acts as a a 'swinging arm' for the attachment of activated fatty acid and amino-acid groups. This domain forms a four helix bundle. This family includes members not included in Prosite. The inclusion of these members is supported by sequence analysis and functional evidence. The related domain of Swiss:P19828 has the attachment serine replaced by an alanine.
Pssm-ID: 425746 [Multi-domain] Cd Length: 62 Bit Score: 61.81 E-value: 2.84e-12
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1178432446 201 KVLADIYAQVLGV--ERVGVDDSFFDLGGDSISAMRATAAINAALGAGLAVRTLFYAPSVR 259
Cdd:pfam00550 1 ERLRELLAEVLGVpaEEIDPDTDLFDLGLDSLLAVELIARLEEEFGVEIPPSDLFEHPTLA 61
|
|
| PRK05677 |
PRK05677 |
long-chain-fatty-acid--CoA ligase; Validated |
7-181 |
2.96e-12 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 168170 [Multi-domain] Cd Length: 562 Bit Score: 69.02 E-value: 2.96e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178432446 7 IGAPVPGAALVVLDGWLRPVSAGVVGELYVAGRGVGVGYWRRPGLSASRFVACPFgppgtrmYRTGDRVRWRADGQLEYL 86
Cdd:PRK05677 380 IGIPVPSTLCKVIDDDGNELPLGEVGELCVKGPQVMKGYWQRPEATDEILDSDGW-------LKTGDIALIQEDGYMRIV 452
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178432446 87 GRTDDQVKIRGYRVELGEIRTALAELEGV-EHAAVIAREDRPGE--RRLVGYITG-TADPATVRAELARRLPAHMVPASV 162
Cdd:PRK05677 453 DRKKDMILVSGFNVYPNELEDVLAALPGVlQCAAIGVPDEKSGEaiKVFVVVKPGeTLTKEQVMEHMRANLTGYKVPKAV 532
|
170
....*....|....*....
gi 1178432446 163 MALQALPLTVNGKLNTRAL 181
Cdd:PRK05677 533 EFRDELPTTNVGKILRREL 551
|
|
| ABCL |
cd05958 |
2-aminobenzoate-CoA ligase (ABCL); ABCL catalyzes the initial step in the 2-aminobenzoate ... |
8-181 |
4.46e-12 |
|
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: 68.27 E-value: 4.46e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178432446 8 GAPVPGAALVVLDGWLRPVSAGVVGELYVAGRgvgVGYWRRPGLSASRFVacpfgppGTRMYRTGDRVRWRADGQLEYLG 87
Cdd:cd05958 268 GKPVPGYEAKVVDDEGNPVPDGTIGRLAVRGP---TGCRYLADKRQRTYV-------QGGWNITGDTYSRDPDGYFRHQG 337
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178432446 88 RTDDQVKIRGYRVELGEIRTALAELEGVEHAAVIAREDRPGERRLVGYIT----GTADPATVRA---ELARRLPAHMVPA 160
Cdd:cd05958 338 RSDDMIVSGGYNIAPPEVEDVLLQHPAVAECAVVGHPDESRGVVVKAFVVlrpgVIPGPVLARElqdHAKAHIAPYKYPR 417
|
170 180
....*....|....*....|.
gi 1178432446 161 SVMALQALPLTVNGKLNTRAL 181
Cdd:cd05958 418 AIEFVTELPRTATGKLQRFAL 438
|
|
| MACS_like |
cd05972 |
Medium-chain acyl-CoA synthetase (MACS or ACSM); MACS catalyzes the two-step activation of ... |
7-181 |
4.77e-12 |
|
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: 68.13 E-value: 4.77e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178432446 7 IGAPVPGAALVVLDGWLRPVSAGVVGELYVAGRGVG--VGYWRRPGLSASRFVAcpfgppgtRMYRTGDRVRWRADGQLE 84
Cdd:cd05972 251 MGRPTPGYDVAIIDDDGRELPPGEEGDIAIKLPPPGlfLGYVGDPEKTEASIRG--------DYYLTGDRAYRDEDGYFW 322
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178432446 85 YLGRTDDQVKIRGYRVELGEIRTALAELEGVEHAAVIAREDrPGERRLV-GYI----TGTADPATVRaELA----RRLPA 155
Cdd:cd05972 323 FVGRADDIIKSSGYRIGPFEVESALLEHPAVAEAAVVGSPD-PVRGEVVkAFVvltsGYEPSEELAE-ELQghvkKVLAP 400
|
170 180
....*....|....*....|....*.
gi 1178432446 156 HMVPASVMALQALPLTVNGKLNTRAL 181
Cdd:cd05972 401 YKYPREIEFVEELPKTISGKIRRVEL 426
|
|
| PRK08308 |
PRK08308 |
acyl-CoA synthetase; Validated |
65-183 |
1.02e-11 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236231 [Multi-domain] Cd Length: 414 Bit Score: 66.98 E-value: 1.02e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178432446 65 GTRMYRTGDRVRWRADGQLEYLGRTDDQVKIRGYRVELGEIRTALAELEGVEHAAVIAREDR-PGERRLVGYIT-GTADP 142
Cdd:PRK08308 289 GDKEIFTKDLGYKSERGTLHFMGRMDDVINVSGLNVYPIEVEDVMLRLPGVQEAVVYRGKDPvAGERVKAKVIShEEIDP 368
|
90 100 110 120
....*....|....*....|....*....|....*....|.
gi 1178432446 143 ATVRAELARRLPAHMVPASVMALQALPLTVNGKLNTRALPA 183
Cdd:PRK08308 369 VQLREWCIQHLAPYQVPHEIESVTEIPKNANGKVSRKLLEL 409
|
|
| AAS_C |
cd05909 |
C-terminal domain of the acyl-acyl carrier protein synthetase (also called ... |
7-181 |
1.69e-11 |
|
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: 66.59 E-value: 1.69e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178432446 7 IGAPVPG--AALVVLDGwLRPVSAGVVGELYVAGRGVGVGYWRRPGLSASRFvacpfgppGTRMYRTGDRVRWRADGQLE 84
Cdd:cd05909 316 VGRPLPGmeVKIVSVET-HEEVPIGEGGLLLVRGPNVMLGYLNEPELTSFAF--------GDGWYDTGDIGKIDGEGFLT 386
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178432446 85 YLGRTDDQVKIRGYRVELGEIRTALAELEG--VEHAAVIAREDRPGERRLVGYITGTADPATVRAEL-ARRLPAHMVPAS 161
Cdd:cd05909 387 ITGRLSRFAKIAGEMVSLEAIEDILSEILPedNEVAVVSVPDGRKGEKIVLLTTTTDTDPSSLNDILkNAGISNLAKPSY 466
|
170 180
....*....|....*....|
gi 1178432446 162 VMALQALPLTVNGKLNTRAL 181
Cdd:cd05909 467 IHQVEEIPLLGTGKPDYVTL 486
|
|
| PrpE |
cd05967 |
Propionyl-CoA synthetase (PrpE); EC 6.2.1.17: propanoate:CoA ligase (AMP-forming) or ... |
8-196 |
1.94e-11 |
|
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: 66.57 E-value: 1.94e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178432446 8 GAPVPGAALVVLDGWLRPVSAGVVGELYVAGR---GVGVGYWRRPGlsasRFVACPFGP-PGtrMYRTGDRVRWRADGQL 83
Cdd:cd05967 414 GKPVPGYQVQVLDEDGEPVGPNELGNIVIKLPlppGCLLTLWKNDE----RFKKLYLSKfPG--YYDTGDAGYKDEDGYL 487
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178432446 84 EYLGRTDDQVKIRGYRVELGEIRTALAELEGVEHAAVIAREDR-PGERRLVGYI---TGTADPATVRAELAR----RLPA 155
Cdd:cd05967 488 FIMGRTDDVINVAGHRLSTGEMEESVLSHPAVAECAVVGVRDElKGQVPLGLVVlkeGVKITAEELEKELVAlvreQIGP 567
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 1178432446 156 HMVPASVMALQALPLTVNGKLNTRALPAprYADGDRYRAPA 196
Cdd:cd05967 568 VAAFRLVIFVKRLPKTRSGKILRRTLRK--IADGEDYTIPS 606
|
|
| PRK05605 |
PRK05605 |
long-chain-fatty-acid--CoA ligase; Validated |
24-179 |
2.80e-11 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 235531 [Multi-domain] Cd Length: 573 Bit Score: 66.18 E-value: 2.80e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178432446 24 RPVSAGVVGELYVAGRGVGVGYWRRPGLSASRFVacpfgpPGtrMYRTGDRVRWRADGQLEYLGRTDDQVKIRGYRVELG 103
Cdd:PRK05605 410 ETMPDGEEGELLVRGPQVFKGYWNRPEETAKSFL------DG--WFRTGDVVVMEEDGFIRIVDRIKELIITGGFNVYPA 481
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178432446 104 EIRTALAELEGVEHAAV--IAREDrpGERRLVGYIT---GTA-DPATVRAELARRLPAHMVPASVMALQALPLTVNGKLN 177
Cdd:PRK05605 482 EVEEVLREHPGVEDAAVvgLPRED--GSEEVVAAVVlepGAAlDPEGLRAYCREHLTRYKVPRRFYHVDELPRDQLGKVR 559
|
..
gi 1178432446 178 TR 179
Cdd:PRK05605 560 RR 561
|
|
| PRK07514 |
PRK07514 |
malonyl-CoA synthase; Validated |
7-175 |
3.20e-11 |
|
malonyl-CoA synthase; Validated
Pssm-ID: 181011 [Multi-domain] Cd Length: 504 Bit Score: 65.67 E-value: 3.20e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178432446 7 IGAPVPGAALVVLD---GwlRPVSAGVVGELYVAGRGVGVGYWRRPGLSASRFVACPFgppgtrmYRTGDRVRWRADGQL 83
Cdd:PRK07514 323 VGFPLPGVSLRVTDpetG--AELPPGEIGMIEVKGPNVFKGYWRMPEKTAEEFRADGF-------FITGDLGKIDERGYV 393
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178432446 84 EYLGRTDDQVKIRGYRVELGEIRTALAELEGVEHAAVI--ARED-----------RPGerrlvgyitGTADPATVRAELA 150
Cdd:PRK07514 394 HIVGRGKDLIISGGYNVYPKEVEGEIDELPGVVESAVIgvPHPDfgegvtavvvpKPG---------AALDEAAILAALK 464
|
170 180
....*....|....*....|....*
gi 1178432446 151 RRLPAHMVPASVMALQALPLTVNGK 175
Cdd:PRK07514 465 GRLARFKQPKRVFFVDELPRNTMGK 489
|
|
| PRK13295 |
PRK13295 |
cyclohexanecarboxylate-CoA ligase; Reviewed |
8-176 |
3.40e-11 |
|
cyclohexanecarboxylate-CoA ligase; Reviewed
Pssm-ID: 171961 [Multi-domain] Cd Length: 547 Bit Score: 65.84 E-value: 3.40e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178432446 8 GAPVPGAALVVLDGWLRPVSAGVVGELYVAGRGVGVGYWRRPGLSASRFVAcpfgppgtrMYRTGDRVRWRADGQLEYLG 87
Cdd:PRK13295 369 GCPLPGVEVRVVDADGAPLPAGQIGRLQVRGCSNFGGYLKRPQLNGTDADG---------WFDTGDLARIDADGYIRISG 439
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178432446 88 RTDDqVKIRG-YRVELGEIRTALAELEGVEHAAVIARED-RPGErRLVGYITGTADPATVRAELARRLPAHMV-----PA 160
Cdd:PRK13295 440 RSKD-VIIRGgENIPVVEIEALLYRHPAIAQVAIVAYPDeRLGE-RACAFVVPRPGQSLDFEEMVEFLKAQKVakqyiPE 517
|
170
....*....|....*.
gi 1178432446 161 SVMALQALPLTVNGKL 176
Cdd:PRK13295 518 RLVVRDALPRTPSGKI 533
|
|
| PRK07529 |
PRK07529 |
AMP-binding domain protein; Validated |
7-244 |
5.52e-11 |
|
AMP-binding domain protein; Validated
Pssm-ID: 236043 [Multi-domain] Cd Length: 632 Bit Score: 65.36 E-value: 5.52e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178432446 7 IGAPVPGAAL--VVLDG---WLRPVSAGVVGELYVAGRGVGVGYwRRPGLSASRFVacpfgppGTRMYRTGDRVRWRADG 81
Cdd:PRK07529 388 VGLRLPYQRVrvVILDDagrYLRDCAVDEVGVLCIAGPNVFSGY-LEAAHNKGLWL-------EDGWLNTGDLGRIDADG 459
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178432446 82 QLEYLGRTDDQVkIR-GYRVELGEIRTALAELEGVEHAAVIARED-RPGErrL-VGYIT----GTADPATVRAELARRLP 154
Cdd:PRK07529 460 YFWLTGRAKDLI-IRgGHNIDPAAIEEALLRHPAVALAAAVGRPDaHAGE--LpVAYVQlkpgASATEAELLAFARDHIA 536
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178432446 155 AHM-VPASVMALQALPLTVNGKLNTRALpapryadgdRYRAPANSVEKVLADIYAQVLGVErVGVDDSFFDLGGDSISAM 233
Cdd:PRK07529 537 ERAaVPKHVRILDALPKTAVGKIFKPAL---------RRDAIRRVLRAALRDAGVEAEVVD-VVEDGRRGLVAQVALRGA 606
|
250
....*....|.
gi 1178432446 234 RATAAINAALG 244
Cdd:PRK07529 607 EDREAVAAVLG 617
|
|
| PRK08633 |
PRK08633 |
2-acyl-glycerophospho-ethanolamine acyltransferase; Validated |
7-181 |
5.59e-11 |
|
2-acyl-glycerophospho-ethanolamine acyltransferase; Validated
Pssm-ID: 236315 [Multi-domain] Cd Length: 1146 Bit Score: 65.72 E-value: 5.59e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178432446 7 IGAPVPGAALVVLD-GWLRPVSAGVVGELYVAGRGVGVGYWRRPGLSASRFVACPfgppGTRMYRTGDRVRWRADGQLEY 85
Cdd:PRK08633 962 VGMPLPGVAVRIVDpETFEELPPGEDGLILIGGPQVMKGYLGDPEKTAEVIKDID----GIGWYVTGDKGHLDEDGFLTI 1037
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178432446 86 LGRTDDQVKIRGYRVELGEIRTALAEL---EGVEHAAVIAREDRPGERRLVGYITGTADPATVRAELAR-RLPAHMVPAS 161
Cdd:PRK08633 1038 TDRYSRFAKIGGEMVPLGAVEEELAKAlggEEVVFAVTAVPDEKKGEKLVVLHTCGAEDVEELKRAIKEsGLPNLWKPSR 1117
|
170 180
....*....|....*....|
gi 1178432446 162 VMALQALPLTVNGKLNTRAL 181
Cdd:PRK08633 1118 YFKVEALPLLGSGKLDLKGL 1137
|
|
| LC_FACS_like |
cd05935 |
Putative long-chain fatty acid CoA ligase; The members of this family are putative long-chain ... |
7-181 |
2.21e-10 |
|
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: 62.88 E-value: 2.21e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178432446 7 IGAPVPGAALVVLD-GWLRPVSAGVVGELYVAGRGVGVGYWRRPGLSASRFVACPfgppGTRMYRTGDRVRWRADGQLEY 85
Cdd:cd05935 253 LGIP*FGVDARVIDiETGRELPPNEVGEIVVRGPQIFKGYWNRPEETEESFIEIK----GRRFFRTGDLGYMDEEGYFFF 328
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178432446 86 LGRTDDQVKIRGYRVELGEIRTALAELEGVEHAAVIARED-RPGErRLVGYIT------GTADPATVRAELARRLPAHMV 158
Cdd:cd05935 329 VDRVKRMINVSGFKVWPAEVEAKLYKHPAI*EVCVISVPDeRVGE-EVKAFIVlrpeyrGKVTEEDIIEWAREQMAAYKY 407
|
170 180
....*....|....*....|...
gi 1178432446 159 PASVMALQALPLTVNGKLNTRAL 181
Cdd:cd05935 408 PREVEFVDELPRSASGKILWRLL 430
|
|
| PtmA |
cd17636 |
long-chain fatty acid CoA ligase (FadD); This family contains fatty acid CoA ligases, ... |
8-174 |
2.44e-10 |
|
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: 61.93 E-value: 2.44e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178432446 8 GAPVPGAALVVLDGWLRPVSAGVVGELYVAGRGVGVGYWRRPGLSASRFVAcpfgppgtRMYRTGDRVRWRADGQLEYLG 87
Cdd:cd17636 166 GRPSPLVQVRILDEDGREVPDGEVGEIVARGPTVMAGYWNRPEVNARRTRG--------GWHHTNDLGRREPDGSLSFVG 237
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178432446 88 RTDDQVKIRGYRVELGEIRTALAELEGVEHAAVIARED-------------RPGErrlvgyitgTADPATVRAELARRLP 154
Cdd:cd17636 238 PKTRMIKSGAENIYPAEVERCLRQHPAVADAAVIGVPDprwaqsvkaivvlKPGA---------SVTEAELIEHCRARIA 308
|
170 180
....*....|....*....|
gi 1178432446 155 AHMVPASVMALQALPLTVNG 174
Cdd:cd17636 309 SYKKPKSVEFADALPRTAGG 328
|
|
| AMP-binding_C |
pfam13193 |
AMP-binding enzyme C-terminal domain; This is a small domain that is found C terminal to ... |
104-175 |
3.68e-10 |
|
AMP-binding enzyme C-terminal domain; This is a small domain that is found C terminal to pfam00501. It has a central beta sheet core that is flanked by alpha helices.
Pssm-ID: 463804 [Multi-domain] Cd Length: 76 Bit Score: 56.01 E-value: 3.68e-10
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1178432446 104 EIRTALAELEGVEHAAVIAREDRPGERRLVGYIT----GTADPATVRAELARRLPAHMVPASVMALQALPLTVNGK 175
Cdd:pfam13193 1 EVESALVSHPAVAEAAVVGVPDELKGEAPVAFVVlkpgVELLEEELVAHVREELGPYAVPKEVVFVDELPKTRSGK 76
|
|
| FADD10 |
cd17635 |
adenylate forming domain, fatty acid CoA ligase (FadD10); This family contains long chain ... |
3-176 |
7.22e-10 |
|
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: 60.74 E-value: 7.22e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178432446 3 DVVPIGAPVPGAALVVLDGWLRPVSAGVVGELYVAGRGVGVGYWRRPGLSASRFVACPFgppgtrmyRTGDRVRWRADGQ 82
Cdd:cd17635 168 EINAVGRPYPGVDVYLAATDGIAGPSASFGTIWIKSPANMLGYWNNPERTAEVLIDGWV--------NTGDLGERREDGF 239
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178432446 83 LEYLGRTDDQVKIRGYRVELGEIRTALAELEGVEHAAVIAREDRP-GErrLVG---YITGTADPATVRA---ELARRLPA 155
Cdd:cd17635 240 LFITGRSSESINCGGVKIAPDEVERIAEGVSGVQECACYEISDEEfGE--LVGlavVASAELDENAIRAlkhTIRRELEP 317
|
170 180
....*....|....*....|.
gi 1178432446 156 HMVPASVMALQALPLTVNGKL 176
Cdd:cd17635 318 YARPSTIVIVTDIPRTQSGKV 338
|
|
| AACS_like |
cd05968 |
Uncharacterized acyl-CoA synthetase subfamily similar to Acetoacetyl-CoA synthetase; This ... |
9-183 |
1.57e-09 |
|
Uncharacterized acyl-CoA synthetase subfamily similar to Acetoacetyl-CoA synthetase; This uncharacterized acyl-CoA synthetase family (EC 6.2.1.16, or acetoacetate#CoA ligase or acetoacetate:CoA ligase (AMP-forming)) is highly homologous to acetoacetyl-CoA synthetase. However, the proteins in this family exist in only bacteria and archaea. AACS is a cytosolic ligase that specifically activates acetoacetate to its coenzyme A ester by a two-step reaction. Acetoacetate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This is the first step of the mevalonate pathway of isoprenoid biosynthesis via isopentenyl diphosphate. Isoprenoids are a large class of compounds found in all living organisms.
Pssm-ID: 341272 [Multi-domain] Cd Length: 610 Bit Score: 60.58 E-value: 1.57e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178432446 9 APVPGAALVVLDGWLRPVSaGVVGELYVAGRGVGV--GYWRRPglsaSRFVACPFGP-PGTRMYrtGDRVRWRADGQLEY 85
Cdd:cd05968 417 GPVPGMKADVLDESGKPAR-PEVGELVLLAPWPGMtrGFWRDE----DRYLETYWSRfDNVWVH--GDFAYYDEEGYFYI 489
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178432446 86 LGRTDDQVKIRGYRVELGEIRTALAELEGV-EHAAVIAREDRPGERRLVGYIT--GTADPATVRAELARRLPAHM----V 158
Cdd:cd05968 490 LGRSDDTINVAGKRVGPAEIESVLNAHPAVlESAAIGVPHPVKGEAIVCFVVLkpGVTPTEALAEELMERVADELgkplS 569
|
170 180
....*....|....*....|....*
gi 1178432446 159 PASVMALQALPLTVNGKLNTRALPA 183
Cdd:cd05968 570 PERILFVKDLPKTRNAKVMRRVIRA 594
|
|
| PRK08751 |
PRK08751 |
long-chain fatty acid--CoA ligase; |
7-181 |
1.95e-09 |
|
long-chain fatty acid--CoA ligase;
Pssm-ID: 181546 [Multi-domain] Cd Length: 560 Bit Score: 60.28 E-value: 1.95e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178432446 7 IGAPVPGAALVVLDGWLRPVSAGVVGELYVAGRGVGVGYWRRPGLSASRFVAcpfgppgTRMYRTGDRVRWRADGQLEYL 86
Cdd:PRK08751 384 IGLPIPSTDACIKDDAGTVLAIGEIGELCIKGPQVMKGYWKRPEETAKVMDA-------DGWLHTGDIARMDEQGFVYIV 456
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178432446 87 GRTDDQVKIRGYRVELGEIRTALAELEGV-EHAAVIAREDRPGErrLVGYITGTADPA----TVRAELARRLPAHMVPAS 161
Cdd:PRK08751 457 DRKKDMILVSGFNVYPNEIEDVIAMMPGVlEVAAVGVPDEKSGE--IVKVVIVKKDPAltaeDVKAHARANLTGYKQPRI 534
|
170 180
....*....|....*....|
gi 1178432446 162 VMALQALPLTVNGKLNTRAL 181
Cdd:PRK08751 535 IEFRKELPKTNVGKILRREL 554
|
|
| MACS_like_1 |
cd05974 |
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the ... |
1-125 |
1.99e-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: 341278 [Multi-domain] Cd Length: 432 Bit Score: 59.89 E-value: 1.99e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178432446 1 GSDVVP--IGAPVPGAALVVLDGWLRPVSAGVVGELYVAGRGVGV--GYWRRPGLSAsrfvacpfGPPGTRMYRTGDRVR 76
Cdd:cd05974 246 GQPVKAgsMGRPLPGYRVALLDPDGAPATEGEVALDLGDTRPVGLmkGYAGDPDKTA--------HAMRGGYYRTGDIAM 317
|
90 100 110 120
....*....|....*....|....*....|....*....|....*....
gi 1178432446 77 WRADGQLEYLGRTDDQVKIRGYRVELGEIRTALAELEGVEHAAVIARED 125
Cdd:cd05974 318 RDEDGYLTYVGRADDVFKSSDYRISPFELESVLIEHPAVAEAAVVPSPD 366
|
|
| FACL_like_4 |
cd05944 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
7-181 |
2.68e-09 |
|
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ATP-dependent activation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions.
Pssm-ID: 341266 [Multi-domain] Cd Length: 359 Bit Score: 59.03 E-value: 2.68e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178432446 7 IGAPVPGAA--LVVLDG---WLRPVSAGVVGELYVAGRGVGVGYWRRPGlSASRFVacpfgppGTRMYRTGDRVRWRADG 81
Cdd:cd05944 176 VGLRLPYARvrIKVLDGvgrLLRDCAPDEVGEICVAGPGVFGGYLYTEG-NKNAFV-------ADGWLNTGDLGRLDADG 247
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178432446 82 QLEYLGRTDDQVKIRGYRVELGEIRTALAELEGVEHAAVIAREDRPGERRLVGYIT----GTADPATVRAELARRLPAH- 156
Cdd:cd05944 248 YLFITGRAKDLIIRGGHNIDPALIEEALLRHPAVAFAGAVGQPDAHAGELPVAYVQlkpgAVVEEEELLAWARDHVPERa 327
|
170 180
....*....|....*....|....*
gi 1178432446 157 MVPASVMALQALPLTVNGKLNTRAL 181
Cdd:cd05944 328 AVPKHIEVLEELPVTAVGKVFKPAL 352
|
|
| AACS |
cd05943 |
Acetoacetyl-CoA synthetase (acetoacetate-CoA ligase, AACS); AACS is a cytosolic ligase that ... |
6-175 |
3.23e-09 |
|
Acetoacetyl-CoA synthetase (acetoacetate-CoA ligase, AACS); AACS is a cytosolic ligase that specifically activates acetoacetate to its coenzyme A ester by a two-step reaction. Acetoacetate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This is the first step of the mevalonate pathway of isoprenoid biosynthesis via isopentenyl diphosphate. Isoprenoids are a large class of compounds found in all living organisms. AACS is widely distributed in bacteria, archaea and eukaryotes. In bacteria, AACS is known to exhibit an important role in the metabolism of poly-b-hydroxybutyrate, an intracellular reserve of organic carbon and chemical energy by some microorganisms. In mammals, AACS influences the rate of ketone body utilization for the formation of physiologically important fatty acids and cholesterol.
Pssm-ID: 341265 [Multi-domain] Cd Length: 629 Bit Score: 59.59 E-value: 3.23e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178432446 6 PIGAPVPGAALVVLDGWLRPVSaGVVGELyVAGR---GVGVGYWRRPGlsASRFVACPFGP-PGTrmYRTGDRVRWRADG 81
Cdd:cd05943 425 EIQCRGLGMAVEAFDEEGKPVW-GEKGEL-VCTKpfpSMPVGFWNDPD--GSRYRAAYFAKyPGV--WAHGDWIEITPRG 498
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178432446 82 QLEYLGRTDDQVKIRGYRVELGEIRTALAELEGVEHAAVIAREDRPGERRLVGYIT----GTADPA---TVRAELARRLP 154
Cdd:cd05943 499 GVVILGRSDGTLNPGGVRIGTAEIYRVVEKIPEVEDSLVVGQEWKDGDERVILFVKlregVELDDElrkRIRSTIRSALS 578
|
170 180
....*....|....*....|.
gi 1178432446 155 AHMVPASVMALQALPLTVNGK 175
Cdd:cd05943 579 PRHVPAKIIAVPDIPRTLSGK 599
|
|
| MACS_AAE_MA_like |
cd05970 |
Medium-chain acyl-CoA synthetase (MACS) of AAE_MA like; MACS catalyzes the two-step activation ... |
7-176 |
3.62e-09 |
|
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: 59.43 E-value: 3.62e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178432446 7 IGAPVPGAALVVLDGWLRPVSAGVVGELYV---AGRGVG--VGYWRRPGLSASRFvacpfgppGTRMYRTGDrVRWR-AD 80
Cdd:cd05970 355 MGKPAPGYEIDLIDREGRSCEAGEEGEIVIrtsKGKPVGlfGGYYKDAEKTAEVW--------HDGYYHTGD-AAWMdED 425
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178432446 81 GQLEYLGRTDDQVKIRGYRVELGEIRTALaelegVEHAAVIaredrpgERRLVGY---ITGTADPATV--------RAEL 149
Cdd:cd05970 426 GYLWFVGRTDDLIKSSGYRIGPFEVESAL-----IQHPAVL-------ECAVTGVpdpIRGQVVKATIvlakgyepSEEL 493
|
170 180 190
....*....|....*....|....*....|....*
gi 1178432446 150 ARRLPAHM--------VPASVMALQALPLTVNGKL 176
Cdd:cd05970 494 KKELQDHVkkvtapykYPRIVEFVDELPKTISGKI 528
|
|
| PRK07788 |
PRK07788 |
acyl-CoA synthetase; Validated |
8-183 |
3.77e-09 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236097 [Multi-domain] Cd Length: 549 Bit Score: 59.17 E-value: 3.77e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178432446 8 GAPVPGAALVVLDGWLRPVSAGVVGELYVAGrgvgvgywrrpGLSASRFVAcpfgpPGTR-----MYRTGDRVRWRADGQ 82
Cdd:PRK07788 379 GRPPKGVTVKILDENGNEVPRGVVGRIFVGN-----------GFPFEGYTD-----GRDKqiidgLLSSGDVGYFDEDGL 442
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178432446 83 LEYLGRTDDQVKIRGYRVELGEIRTALAELEGVEHAAVIAREDRPGERRLVGYIT---GTA-DPATVRAELARRLPAHMV 158
Cdd:PRK07788 443 LFVDGRDDDMIVSGGENVFPAEVEDLLAGHPDVVEAAVIGVDDEEFGQRLRAFVVkapGAAlDEDAIKDYVRDNLARYKV 522
|
170 180
....*....|....*....|....*
gi 1178432446 159 PASVMALQALPLTVNGKLNTRALPA 183
Cdd:PRK07788 523 PRDVVFLDELPRNPTGKVLKRELRE 547
|
|
| AFD_YhfT-like |
cd17633 |
fatty acid-CoA ligase VraA; This family of acyl-CoA ligases includes Bacillus subtilis YhfT, ... |
7-176 |
7.99e-09 |
|
fatty acid-CoA ligase VraA; This family of acyl-CoA ligases includes Bacillus subtilis YhfT, as well as long-chain fatty acid-CoA ligase VraA, all of which are as yet to be characterized. These proteins belong to the adenylate-forming enzymes which catalyze an ATP-dependent two-step reaction to first activate a carboxylate substrate as an adenylate and then transfer the carboxylate to the pantetheine group of either coenzyme A or an acyl-carrier protein. The active site of the domain is located at the interface of a large N-terminal subdomain and a smaller C-terminal subdomain
Pssm-ID: 341288 [Multi-domain] Cd Length: 320 Bit Score: 57.42 E-value: 7.99e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178432446 7 IGAPVPGaalvvLDGWLRPVSAGVVGELYVAGRGVGVGYWRRPGLSAsrfvacpfgppgTRMYRTGDRVRWRADGQLEYL 86
Cdd:cd17633 165 VGRPFPN-----VEIEIRNADGGEIGKIFVKSEMVFSGYVRGGFSNP------------DGWMSVGDIGYVDEEGYLYLV 227
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178432446 87 GRTDDQVKIRGYRVELGEIRTALAELEGVEHAAVIAREDRPGERRLVGYITG-TADPATVRAELARRLPAHMVPASVMAL 165
Cdd:cd17633 228 GRESDMIIIGGINIFPTEIESVLKAIPGIEEAIVVGIPDARFGEIAVALYSGdKLTYKQLKRFLKQKLSRYEIPKKIIFV 307
|
170
....*....|.
gi 1178432446 166 QALPLTVNGKL 176
Cdd:cd17633 308 DSLPYTSSGKI 318
|
|
| ttLC_FACS_AlkK_like |
cd12119 |
Fatty acyl-CoA synthetases similar to LC-FACS from Thermus thermophiles; This family includes ... |
8-181 |
1.14e-08 |
|
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: 57.64 E-value: 1.14e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178432446 8 GAPVPG--AALVVLDGWLRPVSAGVVGELYVAGRGVGVGYWRRPGLSASRFVACPFgppgtrmyRTGDRVRWRADGQLEY 85
Cdd:cd12119 345 GRPVPGveLRIVDDDGRELPWDGKAVGELQVRGPWVTKSYYKNDEESEALTEDGWL--------RTGDVATIDEDGYLTI 416
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178432446 86 LGRTDDQVKIRG---YRVELgeiRTALAELEGVEHAAVIARED-RPGERRL---VGYITGTADPATVRAELARRLPAHMV 158
Cdd:cd12119 417 TDRSKDVIKSGGewiSSVEL---ENAIMAHPAVAEAAVIGVPHpKWGERPLavvVLKEGATVTAEELLEFLADKVAKWWL 493
|
170 180
....*....|....*....|...
gi 1178432446 159 PASVMALQALPLTVNGKLNTRAL 181
Cdd:cd12119 494 PDDVVFVDEIPKTSTGKIDKKAL 516
|
|
| FACL_like_2 |
cd05917 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
2-175 |
1.51e-08 |
|
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: 56.52 E-value: 1.51e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178432446 2 SDVVPIGAPVPGAALVVLDGWLRPV-SAGVVGELYVAGRGVGVGYWRRPGLSASRFvacpfgpPGTRMYRTGDRVRWRAD 80
Cdd:cd05917 171 KRVNTVGRIMPHTEAKIVDPEGGIVpPVGVPGELCIRGYSVMKGYWNDPEKTAEAI-------DGDGWLHTGDLAVMDED 243
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178432446 81 GQLEYLGRTDDQVkIRG----YRVELGEIrtaLAELEGVEHAAVIA-REDRPGErRLVGYITGTADP----ATVRAELAR 151
Cdd:cd05917 244 GYCRIVGRIKDMI-IRGgeniYPREIEEF---LHTHPKVSDVQVVGvPDERYGE-EVCAWIRLKEGAelteEDIKAYCKG 318
|
170 180
....*....|....*....|....
gi 1178432446 152 RLPAHMVPASVMALQALPLTVNGK 175
Cdd:cd05917 319 KIAHYKVPRYVFFVDEFPLTVSGK 342
|
|
| PRK06155 |
PRK06155 |
crotonobetaine/carnitine-CoA ligase; Provisional |
5-176 |
1.58e-08 |
|
crotonobetaine/carnitine-CoA ligase; Provisional
Pssm-ID: 235719 [Multi-domain] Cd Length: 542 Bit Score: 57.08 E-value: 1.58e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178432446 5 VPIGAPVPGAAlvvldGWLRP-------------VSAGVVGELYVAGRgvgvgywrRPGLSASRFvacpFGPPGTRM--- 68
Cdd:PRK06155 335 VTHGSQRPGSM-----GRLAPgfearvvdehdqeLPDGEPGELLLRAD--------EPFAFATGY----FGMPEKTVeaw 397
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178432446 69 ----YRTGDRVRWRADGQLEYLGRTDDQVKIRGYRVELGEIRTALAELEGVEHAAVIAREDRPGERRLVGYIT---GTA- 140
Cdd:PRK06155 398 rnlwFHTGDRVVRDADGWFRFVDRIKDAIRRRGENISSFEVEQVLLSHPAVAAAAVFPVPSELGEDEVMAAVVlrdGTAl 477
|
170 180 190
....*....|....*....|....*....|....*.
gi 1178432446 141 DPATVRAELARRLPAHMVPASVMALQALPLTVNGKL 176
Cdd:PRK06155 478 EPVALVRHCEPRLAYFAVPRYVEFVAALPKTENGKV 513
|
|
| ACS |
cd05966 |
Acetyl-CoA synthetase (also known as acetate-CoA ligase and acetyl-activating enzyme); ... |
10-181 |
1.82e-08 |
|
Acetyl-CoA synthetase (also known as acetate-CoA ligase and acetyl-activating enzyme); Acetyl-CoA synthetase (ACS, EC 6.2.1.1, acetate#CoA ligase or acetate:CoA ligase (AMP-forming)) catalyzes the formation of acetyl-CoA from acetate, CoA, and ATP. Synthesis of acetyl-CoA is carried out in a two-step reaction. In the first step, the enzyme catalyzes the synthesis of acetyl-AMP intermediate from acetate and ATP. In the second step, acetyl-AMP reacts with CoA to produce acetyl-CoA. This enzyme is widely present in all living organisms. The activity of this enzyme is crucial for maintaining the required levels of acetyl-CoA, a key intermediate in many important biosynthetic and catabolic processes. Acetyl-CoA is used in the biosynthesis of glucose, fatty acids, and cholesterol. It can also be used in the production of energy in the citric acid cycle. Eukaryotes typically have two isoforms of acetyl-CoA synthetase, a cytosolic form involved in biosynthetic processes and a mitochondrial form primarily involved in energy generation.
Pssm-ID: 341270 [Multi-domain] Cd Length: 608 Bit Score: 57.19 E-value: 1.82e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178432446 10 PVPGAALVVLDGWLRPVSAGVVGELYVAG------RGVgvgyWRRPGlsasRFVACPFGP-PGtrMYRTGDRVRWRADGQ 82
Cdd:cd05966 415 PFFGIEPAILDEEGNEVEGEVEGYLVIKRpwpgmaRTI----YGDHE----RYEDTYFSKfPG--YYFTGDGARRDEDGY 484
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178432446 83 LEYLGRTDDQVKIRGYRVELGEIRTALAELEGVEHAAVIAREDR-PGErRLVGYIT---GTADPATVRAEL----ARRLP 154
Cdd:cd05966 485 YWITGRVDDVINVSGHRLGTAEVESALVAHPAVAEAAVVGRPHDiKGE-AIYAFVTlkdGEEPSDELRKELrkhvRKEIG 563
|
170 180
....*....|....*....|....*..
gi 1178432446 155 AHMVPASVMALQALPLTVNGKLNTRAL 181
Cdd:cd05966 564 PIATPDKIQFVPGLPKTRSGKIMRRIL 590
|
|
| PRK13382 |
PRK13382 |
bile acid CoA ligase; |
8-184 |
2.47e-08 |
|
bile acid CoA ligase;
Pssm-ID: 172019 [Multi-domain] Cd Length: 537 Bit Score: 56.69 E-value: 2.47e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178432446 8 GAPVPGAALVVLDGWLRPVSAGVVGELYVAGRGVGVGYwrRPGlSASRFVAcpfgppgtRMYRTGDRVRWRADGQLEYLG 87
Cdd:PRK13382 368 GRPAEGTEIRILDQDFREVPTGEVGTIFVRNDTQFDGY--TSG-STKDFHD--------GFMASGDVGYLDENGRLFVVG 436
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178432446 88 RTDDQVKIRGYRVELGEIRTALAELEGVEHAAVIAREDRPGERRLVGYITGTADPA--------TVRAELARrlpaHMVP 159
Cdd:PRK13382 437 RDDEMIVSGGENVYPIEVEKTLATHPDVAEAAVIGVDDEQYGQRLAAFVVLKPGASatpetlkqHVRDNLAN----YKVP 512
|
170 180
....*....|....*....|....*
gi 1178432446 160 ASVMALQALPLTVNGKLNTRALPAP 184
Cdd:PRK13382 513 RDIVVLDELPRGATGKILRRELQAR 537
|
|
| FACL_like_5 |
cd05924 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
12-179 |
2.69e-08 |
|
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ATP-dependent activation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions.
Pssm-ID: 341248 [Multi-domain] Cd Length: 364 Bit Score: 55.85 E-value: 2.69e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178432446 12 PGAALVVLDGWLRPVSAGVVGELYVAGRG-VGVGYWRRPGLSASRFVACPfgppGTRMYRTGDRVRWRADGQLEYLGRTD 90
Cdd:cd05924 193 ANPDTVVLDDDGRVVPPGSGGVGWIARRGhIPLGYYGDEAKTAETFPEVD----GVRYAVPGDRATVEADGTVTLLGRGS 268
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178432446 91 DQVKIRGYRVELGEIRTALAELEGVEHAAVIARED-RPGERrlVGYITGTADPATV-----RAELARRLPAHMVPASVMA 164
Cdd:cd05924 269 VCINTGGEKVFPEEVEEALKSHPAVYDVLVVGRPDeRWGQE--VVAVVQLREGAGVdleelREHCRTRIARYKLPKQVVF 346
|
170
....*....|....*
gi 1178432446 165 LQALPLTVNGKLNTR 179
Cdd:cd05924 347 VDEIERSPAGKADYR 361
|
|
| PRK06060 |
PRK06060 |
p-hydroxybenzoic acid--AMP ligase FadD22; |
28-183 |
2.75e-08 |
|
p-hydroxybenzoic acid--AMP ligase FadD22;
Pssm-ID: 180374 [Multi-domain] Cd Length: 705 Bit Score: 56.58 E-value: 2.75e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178432446 28 AGVVGELYVAGRGVGVGYWRRPGlsasrfvacPFGPPGTRMyRTGDRVRWRADGQLEYLGRTDDQVKIRGYRVELGEIRT 107
Cdd:PRK06060 336 PGVEGDLWVRGPAIAKGYWNRPD---------SPVANEGWL-DTRDRVCIDSDGWVTYRCRADDTEVIGGVNVDPREVER 405
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178432446 108 ALAELEGVEHAAVIAREDRPGERRLVGYITGTA----DPATVR---AELARRLPAHMVPASVMALQALPLTVNGKLNTRA 180
Cdd:PRK06060 406 LIIEDEAVAEAAVVAVRESTGASTLQAFLVATSgatiDGSVMRdlhRGLLNRLSAFKVPHRFAVVDRLPRTPNGKLVRGA 485
|
...
gi 1178432446 181 LPA 183
Cdd:PRK06060 486 LRK 488
|
|
| PRK12492 |
PRK12492 |
long-chain-fatty-acid--CoA ligase; Provisional |
7-181 |
2.84e-08 |
|
long-chain-fatty-acid--CoA ligase; Provisional
Pssm-ID: 171539 [Multi-domain] Cd Length: 562 Bit Score: 56.37 E-value: 2.84e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178432446 7 IGAPVPGAALVVLDGWLRPVSAGVVGELYVAGRGVGVGYWRRPGLSASRFVAcpfgppgTRMYRTGDRVRWRADGQLEYL 86
Cdd:PRK12492 388 VGIPVPGTALKVIDDDGNELPLGERGELCIKGPQVMKGYWQQPEATAEALDA-------EGWFKTGDIAVIDPDGFVRIV 460
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178432446 87 GRTDDQVKIRGYRVELGEIRTALAELEGVEHAAVIARED-RPGE--RRLVGYITGTADPATVRAELARRLPAHMVPASVM 163
Cdd:PRK12492 461 DRKKDLIIVSGFNVYPNEIEDVVMAHPKVANCAAIGVPDeRSGEavKLFVVARDPGLSVEELKAYCKENFTGYKVPKHIV 540
|
170
....*....|....*...
gi 1178432446 164 ALQALPLTVNGKLNTRAL 181
Cdd:PRK12492 541 LRDSLPMTPVGKILRREL 558
|
|
| Firefly_Luc_like |
cd05911 |
Firefly luciferase of light emitting insects and 4-Coumarate-CoA Ligase (4CL); This family ... |
8-177 |
4.85e-08 |
|
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: 55.68 E-value: 4.85e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178432446 8 GAPVPG--AALVVLDG--WLRPvsaGVVGELYVAGRGVGVGYWRRPGLSASRFVACPFgppgtrmYRTGDRVRWRADGQL 83
Cdd:cd05911 318 GRLLPNveAKIVDDDGkdSLGP---NEPGEICVRGPQVMKGYYNNPEATKETFDEDGW-------LHTGDIGYFDEDGYL 387
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178432446 84 EYLGRTDDQVKIRGYRVELGEIRTALAELEGVEHAAVIAREDRPGERRLVGYITGTADPATVRAELaRRLPAHMVPAS-- 161
Cdd:cd05911 388 YIVDRKKELIKYKGFQVAPAELEAVLLEHPGVADAAVIGIPDEVSGELPRAYVVRKPGEKLTEKEV-KDYVAKKVASYkq 466
|
170 180
....*....|....*....|
gi 1178432446 162 ----VMALQALPLTVNGKLN 177
Cdd:cd05911 467 lrggVVFVDEIPKSASGKIL 486
|
|
| PRK07867 |
PRK07867 |
acyl-CoA synthetase; Validated |
8-190 |
7.31e-08 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236120 [Multi-domain] Cd Length: 529 Bit Score: 55.07 E-value: 7.31e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178432446 8 GAPVPGAalvVLDGWLRPVSAGVVGELY-VAGRGVGVGYWRRPGLSASRFVAcpfgppgtRMYRTGDRVRWRADGQLEYL 86
Cdd:PRK07867 332 GTECPPA---EDADGRLLNADEAIGELVnTAGPGGFEGYYNDPEADAERMRG--------GVYWSGDLAYRDADGYAYFA 400
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178432446 87 GRTDDQVKIRGYRVELGEIRTALAELEGVEHAAVIAREDRP-GER---RLVGYITGTADPATVRAELARR--LPAHMVPA 160
Cdd:PRK07867 401 GRLGDWMRVDGENLGTAPIERILLRYPDATEVAVYAVPDPVvGDQvmaALVLAPGAKFDPDAFAEFLAAQpdLGPKQWPS 480
|
170 180 190
....*....|....*....|....*....|
gi 1178432446 161 SVMALQALPLTVNGKLNTRALPAPRYADGD 190
Cdd:PRK07867 481 YVRVCAELPRTATFKVLKRQLSAEGVDCAD 510
|
|
| PRK07824 |
PRK07824 |
o-succinylbenzoate--CoA ligase; |
8-181 |
7.70e-08 |
|
o-succinylbenzoate--CoA ligase;
Pssm-ID: 236108 [Multi-domain] Cd Length: 358 Bit Score: 54.67 E-value: 7.70e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178432446 8 GAPVPGAALVVLDGwlrpvsagvvgELYVAGRGVGVGYwRRPGLSAsrfvacPFGPPGtrMYRTGDrVRWRADGQLEYLG 87
Cdd:PRK07824 195 GVPLDGVRVRVEDG-----------RIALGGPTLAKGY-RNPVDPD------PFAEPG--WFRTDD-LGALDDGVLTVLG 253
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178432446 88 RTDDQVKIRGYRVELGEIRTALAELEGVEHAAVIAREDRPGERRLVGYITGTADPATV----RAELARRLPAHMVPASVM 163
Cdd:PRK07824 254 RADDAISTGGLTVLPQVVEAALATHPAVADCAVFGLPDDRLGQRVVAAVVGDGGPAPTlealRAHVARTLDRTAAPRELH 333
|
170
....*....|....*...
gi 1178432446 164 ALQALPLTVNGKLNTRAL 181
Cdd:PRK07824 334 VVDELPRRGIGKVDRRAL 351
|
|
| PKS_PP |
smart00823 |
Phosphopantetheine attachment site; Phosphopantetheine (or pantetheine 4' phosphate) is the ... |
199-267 |
9.85e-08 |
|
Phosphopantetheine attachment site; Phosphopantetheine (or pantetheine 4' phosphate) is the prosthetic group of acyl carrier proteins (ACP) in some multienzyme complexes where it serves as a 'swinging arm' for the attachment of activated fatty acid and amino-acid groups.
Pssm-ID: 214834 [Multi-domain] Cd Length: 86 Bit Score: 49.56 E-value: 9.85e-08
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1178432446 199 VEKVLADIYAQVLGV---ERVGVDDSFFDLGGDSISAMRATAAINAALGAGLAVRTLFYAPSVRRLSRQLGT 267
Cdd:smart00823 13 LLDLVREQVAAVLGHaaaEAIDPDRPFRDLGLDSLMAVELRNRLEAATGLRLPATLVFDHPTPAALAEHLAA 84
|
|
| ACLS-CaiC |
cd17637 |
acyl-CoA synthetase (AMP-forming)/AMP-acid ligase II; This family contains fatty acid CoA ... |
8-121 |
1.94e-07 |
|
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: 53.04 E-value: 1.94e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178432446 8 GAPVPGAALVVLDGWLRPVSAGVVGELYVAGRGVGVGYWRRPGLSASRFvacpfgppgtR--MYRTGDRVRWRADGQLEY 85
Cdd:cd17637 165 GRPGPLVRVRIVDDNDRPVPAGETGEIVVRGPLVFQGYWNLPELTAYTF----------RngWHHTGDLGRFDEDGYLWY 234
|
90 100 110
....*....|....*....|....*....|....*...
gi 1178432446 86 LGRT--DDQVKIRGYRVELGEIRTALAELEGVEHAAVI 121
Cdd:cd17637 235 AGRKpeKELIKPGGENVYPAEVEKVILEHPAIAEVCVI 272
|
|
| PRK12476 |
PRK12476 |
putative fatty-acid--CoA ligase; Provisional |
29-189 |
2.24e-07 |
|
putative fatty-acid--CoA ligase; Provisional
Pssm-ID: 171527 [Multi-domain] Cd Length: 612 Bit Score: 53.59 E-value: 2.24e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178432446 29 GVVGELYVAGRGVGVGYWRRPGLSASRFVA-----CPFG------PPGTRMYRTGDRVRWRaDGQLEYLGRTDDQVKIRG 97
Cdd:PRK12476 427 GEVGEIWLHGDNIGRGYWGRPEETERTFGAklqsrLAEGshadgaADDGTWLRTGDLGVYL-DGELYITGRIADLIVIDG 505
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178432446 98 YRVELGEIRTALAELEGVEHAAVIAREDRPGERRLVGYI-------TGTADPA----TVRAELARRlpaHMVP-ASVMAL 165
Cdd:PRK12476 506 RNHYPQDIEATVAEASPMVRRGYVTAFTVPAEDNERLVIvaeraagTSRADPApaidAIRAAVSRR---HGLAvADVRLV 582
|
170 180
....*....|....*....|....*.
gi 1178432446 166 QA--LPLTVNGKLNTRALPApRYADG 189
Cdd:PRK12476 583 PAgaIPRTTSGKLARRACRA-QYLDG 607
|
|
| PRK06814 |
PRK06814 |
acyl-[ACP]--phospholipid O-acyltransferase; |
10-177 |
2.32e-07 |
|
acyl-[ACP]--phospholipid O-acyltransferase;
Pssm-ID: 235865 [Multi-domain] Cd Length: 1140 Bit Score: 53.82 E-value: 2.32e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178432446 10 PVPGaalvvldgwlrpVSAGvvGELYVAGRGVGVGYWR--RPGLsasrfvacpFGPPGTRMYRTGDRVRWRADGQLEYLG 87
Cdd:PRK06814 974 PVPG------------IDEG--GRLFVRGPNVMLGYLRaeNPGV---------LEPPADGWYDTGDIVTIDEEGFITIKG 1030
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178432446 88 RTDDQVKIRGYRVELGEIRTALAEL-EGVEHAAVIAREDRPGERRLVgyITgTADPATvRAEL-----ARRLPAHMVPAS 161
Cdd:PRK06814 1031 RAKRFAKIAGEMISLAAVEELAAELwPDALHAAVSIPDARKGERIIL--LT-TASDAT-RAAFlahakAAGASELMVPAE 1106
|
170
....*....|....*.
gi 1178432446 162 VMALQALPLTVNGKLN 177
Cdd:PRK06814 1107 IITIDEIPLLGTGKID 1122
|
|
| PRK06145 |
PRK06145 |
acyl-CoA synthetase; Validated |
8-181 |
2.34e-07 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 102207 [Multi-domain] Cd Length: 497 Bit Score: 53.35 E-value: 2.34e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178432446 8 GAPVPGAALVVLDGWLRPVSAGVVGELYVAGRGVGVGYWRRPGLSASRFVACPFgppgtrmyRTGDRVRWRADGQLEYLG 87
Cdd:PRK06145 322 GRALAHVEIRIADGAGRWLPPNMKGEICMRGPKVTKGYWKDPEKTAEAFYGDWF--------RSGDVGYLDEEGFLYLTD 393
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178432446 88 RTDDQVKIRGYRVELGEIRTALAELEGVEHAAVI-AREDRPGERrlVGYITGTADPATVRAELAR-----RLPAHMVPAS 161
Cdd:PRK06145 394 RKKDMIISGGENIASSEVERVIYELPEVAEAAVIgVHDDRWGER--ITAVVVLNPGATLTLEALDrhcrqRLASFKVPRQ 471
|
170 180
....*....|....*....|
gi 1178432446 162 VMALQALPLTVNGKLNTRAL 181
Cdd:PRK06145 472 LKVRDELPRNPSGKVLKRVL 491
|
|
| PRK07059 |
PRK07059 |
Long-chain-fatty-acid--CoA ligase; Validated |
7-181 |
2.86e-07 |
|
Long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 235923 [Multi-domain] Cd Length: 557 Bit Score: 53.10 E-value: 2.86e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178432446 7 IGAPVPGAALVVLDGWLRPVSAGVVGELYVAGRGVGVGYWRRPGLSASRFVACPFgppgtrmYRTGDRVRWRADGQLEYL 86
Cdd:PRK07059 382 IGLPLPSTEVSIRDDDGNDLPLGEPGEICIRGPQVMAGYWNRPDETAKVMTADGF-------FRTGDVGVMDERGYTKIV 454
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178432446 87 GRTDDQVKIRGYRVELGEIRTALAELEGVEHAAVIARED-RPGErrLVGYITGTADPATVRAEL----ARRLPAHMVPAS 161
Cdd:PRK07059 455 DRKKDMILVSGFNVYPNEIEEVVASHPGVLEVAAVGVPDeHSGE--AVKLFVVKKDPALTEEDVkafcKERLTNYKRPKF 532
|
170 180
....*....|....*....|
gi 1178432446 162 VMALQALPLTVNGKLNTRAL 181
Cdd:PRK07059 533 VEFRTELPKTNVGKILRREL 552
|
|
| PRK06839 |
PRK06839 |
o-succinylbenzoate--CoA ligase; |
7-181 |
3.97e-07 |
|
o-succinylbenzoate--CoA ligase;
Pssm-ID: 168698 [Multi-domain] Cd Length: 496 Bit Score: 52.55 E-value: 3.97e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178432446 7 IGAPVPGAALVVLDGWLRPVSAGVVGELYVAGRGVGVGYWRRPGLSASRFvacpfgppGTRMYRTGDRVRWRADGQLEYL 86
Cdd:PRK06839 319 IGKPVLFCDYELIDENKNKVEVGEVGELLIRGPNVMKEYWNRPDATEETI--------QDGWLCTGDLARVDEDGFVYIV 390
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178432446 87 GRTDDQVKIRGYRVELGEIRTALAELEGVEHAAVIARED-RPGERRLVGYITGTADPAT---VRAELARRLPAHMVPASV 162
Cdd:PRK06839 391 GRKKEMIISGGENIYPLEVEQVINKLSDVYEVAVVGRQHvKWGEIPIAFIVKKSSSVLIekdVIEHCRLFLAKYKIPKEI 470
|
170
....*....|....*....
gi 1178432446 163 MALQALPLTVNGKLNTRAL 181
Cdd:PRK06839 471 VFLKELPKNATGKIQKAQL 489
|
|
| PRK07656 |
PRK07656 |
long-chain-fatty-acid--CoA ligase; Validated |
7-181 |
5.91e-07 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236072 [Multi-domain] Cd Length: 513 Bit Score: 52.21 E-value: 5.91e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178432446 7 IGAPVPGAALVVLDGWLRPVSAGVVGELYVAGRGVGVGYWRRPglsasrfvacpfgpPGTRM-------YRTGDRVRWRA 79
Cdd:PRK07656 339 IGTAIAGVENKIVNELGEEVPVGEVGELLVRGPNVMKGYYDDP--------------EATAAaidadgwLHTGDLGRLDE 404
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178432446 80 DGQLEYLGRTDDQVKIRGYRVELGEIRTALAELEGVEHAAVIARED-RPGErrlVG--YIT----GTADPATVRAELARR 152
Cdd:PRK07656 405 EGYLYIVDRKKDMFIVGGFNVYPAEVEEVLYEHPAVAEAAVIGVPDeRLGE---VGkaYVVlkpgAELTEEELIAYCREH 481
|
170 180
....*....|....*....|....*....
gi 1178432446 153 LPAHMVPASVMALQALPLTVNGKLNTRAL 181
Cdd:PRK07656 482 LAKYKVPRSIEFLDELPKNATGKVLKRAL 510
|
|
| PKS_TE |
smart00824 |
Thioesterase; Peptide synthetases are involved in the non-ribosomal synthesis of peptide ... |
322-382 |
6.21e-07 |
|
Thioesterase; Peptide synthetases are involved in the non-ribosomal synthesis of peptide antibiotics. Next to the operons encoding these enzymes, in almost all cases, are genes that encode proteins that have similarity to the type II fatty acid thioesterases of vertebrates. There are also modules within the peptide synthetases that also share this similarity. With respect to antibiotic production, thioesterases are required for the addition of the last amino acid to the peptide antibiotic, thereby forming a cyclic antibiotic. Thioesterases (non-integrated) have molecular masses of 25-29 kDa.
Pssm-ID: 214835 [Multi-domain] Cd Length: 212 Bit Score: 50.30 E-value: 6.21e-07
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1178432446 322 GEGE--PESIRAMAARYADTLQALYPDGPYKLLGWSFGGVVAQELAIELQRRGCVVQSLVLLD 382
Cdd:smart00824 37 GPGEplPASADALVEAQAEAVLRAAGGRPFVLVGHSSGGLLAHAVAARLEARGIPPAAVVLLD 99
|
|
| PRK05852 |
PRK05852 |
fatty acid--CoA ligase family protein; |
25-181 |
8.18e-07 |
|
fatty acid--CoA ligase family protein;
Pssm-ID: 235625 [Multi-domain] Cd Length: 534 Bit Score: 51.81 E-value: 8.18e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178432446 25 PVSAGVVGELYVAGRGVGVGYWRRPGLSASRFVACPFgppgtrmyRTGDRVRWRADGQLEYLGRTDDQVKIRGYRVELGE 104
Cdd:PRK05852 374 PLPAGAVGEVWLRGTTVVRGYLGDPTITAANFTDGWL--------RTGDLGSLSAAGDLSIRGRIKELINRGGEKISPER 445
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178432446 105 IRTALAELEGVEHAAVIAREDRPGERRLVGYITGTADPATVRAELA----RRLPAHMVPASVMALQALPLTVNGKLNTRA 180
Cdd:PRK05852 446 VEGVLASHPNVMEAAVFGVPDQLYGEAVAAVIVPRESAPPTAEELVqfcrERLAAFEIPASFQEASGLPHTAKGSLDRRA 525
|
.
gi 1178432446 181 L 181
Cdd:PRK05852 526 V 526
|
|
| MACS_euk |
cd05928 |
Eukaryotic Medium-chain acyl-CoA synthetase (MACS or ACSM); MACS catalyzes the two-step ... |
69-176 |
8.89e-07 |
|
Eukaryotic Medium-chain acyl-CoA synthetase (MACS or ACSM); MACS catalyzes the two-step activation of medium chain fatty acids (containing 4-12 carbons). The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. The acyl-CoA is a key intermediate in many important biosynthetic and catabolic processes. MACS enzymes are localized to mitochondria. Two murine MACS family proteins are found in liver and kidney. In rodents, a MACS member is detected particularly in the olfactory epithelium and is called O-MACS. O-MACS demonstrates substrate preference for the fatty acid lengths of C6-C12.
Pssm-ID: 341251 [Multi-domain] Cd Length: 530 Bit Score: 51.70 E-value: 8.89e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178432446 69 YRTGDRVRWRADGQLEYLGRTDDQVKIRGYRVELGEIRTALAELEGVEHAAVIAREDrPGERRLV-GYITGTAD-PATVR 146
Cdd:cd05928 404 YLTGDRGIMDEDGYFWFMGRADDVINSSGYRIGPFEVESALIEHPAVVESAVVSSPD-PIRGEVVkAFVVLAPQfLSHDP 482
|
90 100 110
....*....|....*....|....*....|....*...
gi 1178432446 147 AELARRLPAHM--------VPASVMALQALPLTVNGKL 176
Cdd:cd05928 483 EQLTKELQQHVksvtapykYPRKVEFVQELPKTVTGKI 520
|
|
| CBAL |
cd05923 |
4-Chlorobenzoate-CoA ligase (CBAL); CBAL catalyzes the conversion of 4-chlorobenzoate (4-CB) ... |
4-181 |
1.10e-06 |
|
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: 51.36 E-value: 1.10e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178432446 4 VVPIGAPVPGAAlvvldgwlrpvSAGVVGELYVAGRG--VGVGYWRRPGLSASRFVacpfgppgTRMYRTGDRVRWRADG 81
Cdd:cd05923 329 IVRIGGSPDEAL-----------ANGEEGELIVAAAAdaAFTGYLNQPEATAKKLQ--------DGWYRTGDVGYVDPSG 389
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178432446 82 QLEYLGRTDDQVKIRGYRVELGEIRTALAELEGVEHAAVIAREDRPGERRLVGYItgTADPATVRAE------LARRLPA 155
Cdd:cd05923 390 DVRILGRVDDMIISGGENIHPSEIERVLSRHPGVTEVVVIGVADERWGQSVTACV--VPREGTLSADeldqfcRASELAD 467
|
170 180
....*....|....*....|....*.
gi 1178432446 156 HMVPASVMALQALPLTVNGKLNTRAL 181
Cdd:cd05923 468 FKRPRRYFFLDELPKNAMNKVLRRQL 493
|
|
| FCS |
cd05921 |
Feruloyl-CoA synthetase (FCS); Feruloyl-CoA synthetase is an essential enzyme in the feruloyl ... |
7-156 |
1.21e-06 |
|
Feruloyl-CoA synthetase (FCS); Feruloyl-CoA synthetase is an essential enzyme in the feruloyl acid degradation pathway and enables some proteobacteria to grow on media containing feruloyl acid as the sole carbon source. It catalyzes the transfer of CoA to the carboxyl group of ferulic acid, which then forms feruloyl-CoA in the presence of ATP and Mg2. The resulting feruloyl-CoA is further degraded to vanillin and acetyl-CoA. Feruloyl-CoA synthetase (FCS) is a subfamily of the adenylate-forming enzymes superfamily.
Pssm-ID: 341245 [Multi-domain] Cd Length: 561 Bit Score: 51.28 E-value: 1.21e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178432446 7 IGAPVPGAALvvldgwlRPVSAGVVGELYVAGRGVGVGYWRRPGLSASRFVACPFgppgtrmYRTGDRVRWRADGQ---- 82
Cdd:cd05921 350 IGLPAPGTEL-------KLVPSGGKYEVRVKGPNVTPGYWRQPELTAQAFDEEGF-------YCLGDAAKLADPDDpakg 415
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178432446 83 LEYLGRTDDQVKIR-GYRVELGEIRTAL-AELEGVEHAAVIAREDR-----------PGERRLVGyiTGTADPA------ 143
Cdd:cd05921 416 LVFDGRVAEDFKLAsGTWVSVGPLRARAvAACAPLVHDAVVAGEDRaevgalvfpdlLACRRLVG--LQEASDAevlrha 493
|
170
....*....|...
gi 1178432446 144 TVRAELARRLPAH 156
Cdd:cd05921 494 KVRAAFRDRLAAL 506
|
|
| PRK08314 |
PRK08314 |
long-chain-fatty-acid--CoA ligase; Validated |
23-181 |
1.26e-06 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236235 [Multi-domain] Cd Length: 546 Bit Score: 51.11 E-value: 1.26e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178432446 23 LRPVSAGVVGELYVAGRGVGVGYWRRPGLSASRFVACpfgpPGTRMYRTGDRVRWRADGQLEYLGRTDDQVKIRGYRVEL 102
Cdd:PRK08314 376 LEELPPGEVGEIVVHGPQVFKGYWNRPEATAEAFIEI----DGKRFFRTGDLGRMDEEGYFFITDRLKRMINASGFKVWP 451
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178432446 103 GEIRTALAELEGVEHAAVIA-REDRPGErRLVGYITGTAD-PATVRAE----LAR-RLPAHMVPASVMALQALPLTVNGK 175
Cdd:PRK08314 452 AEVENLLYKHPAIQEACVIAtPDPRRGE-TVKAVVVLRPEaRGKTTEEeiiaWAReHMAAYKYPRIVEFVDSLPKSGSGK 530
|
....*.
gi 1178432446 176 LNTRAL 181
Cdd:PRK08314 531 ILWRQL 536
|
|
| PRK07786 |
PRK07786 |
long-chain-fatty-acid--CoA ligase; Validated |
7-176 |
1.63e-06 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 169098 [Multi-domain] Cd Length: 542 Bit Score: 50.93 E-value: 1.63e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178432446 7 IGAPVPGAALVVLDGWLRPVSAGVVGELYVAGRGVGVGYWRRPGLSASRFVACPFgppgtrmyRTGDRVRWRADGQLEYL 86
Cdd:PRK07786 347 VGKVIPTVAARVVDENMNDVPVGEVGEIVYRAPTLMSGYWNNPEATAEAFAGGWF--------HSGDLVRQDEEGYVWVV 418
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178432446 87 GRTDDQVKIRGYRVELGEIRTALAELEGVEHAAVIAREDRPGERRLVGYITGTADPATVRAE-----LARRLPAHMVPAS 161
Cdd:PRK07786 419 DRKKDMIISGGENIYCAEVENVLASHPDIVEVAVIGRADEKWGEVPVAVAAVRNDDAALTLEdlaefLTDRLARYKHPKA 498
|
170
....*....|....*
gi 1178432446 162 VMALQALPLTVNGKL 176
Cdd:PRK07786 499 LEIVDALPRNPAGKV 513
|
|
| FACL_fum10p_like |
cd05926 |
Subfamily of fatty acid CoA ligase (FACL) similar to Fum10p of Gibberella moniliformis; FACL ... |
7-181 |
1.72e-06 |
|
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: 50.77 E-value: 1.72e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178432446 7 IGAPVpGAALVVLDGWLRPVSAGVVGELYVAGRGVGVGYWRRPGLSASRFVACPFgppgtrmYRTGDRVRWRADGQLEYL 86
Cdd:cd05926 321 VGKPV-GVEVRILDEDGEILPPGVVGEICLRGPNVTRGYLNNPEANAEAAFKDGW-------FRTGDLGYLDADGYLFLT 392
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178432446 87 GRTDDQVKIRGYRVELGEIRTALAELEGVEHAAVIAREDRP-GERrLVGYIT----GTADPATVRAELARRLPAHMVPAS 161
Cdd:cd05926 393 GRIKELINRGGEKISPLEVDGVLLSHPAVLEAVAFGVPDEKyGEE-VAAAVVlregASVTEEELRAFCRKHLAAFKVPKK 471
|
170 180
....*....|....*....|
gi 1178432446 162 VMALQALPLTVNGKLNTRAL 181
Cdd:cd05926 472 VYFVDELPKTATGKIQRRKV 491
|
|
| PRK12582 |
PRK12582 |
acyl-CoA synthetase; Provisional |
7-156 |
2.18e-06 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 237144 [Multi-domain] Cd Length: 624 Bit Score: 50.43 E-value: 2.18e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178432446 7 IGAPVPGAALVVLdgwlrPVSAGVvgELYVAGRGVGVGYWRRPGLSASRFVACPFgppgtrmYRTGDRVRW----RADGQ 82
Cdd:PRK12582 406 IGLPLPGVELKLA-----PVGDKY--EVRVKGPNVTPGYHKDPELTAAAFDEEGF-------YRLGDAARFvdpdDPEKG 471
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178432446 83 LEYLGRTDDQVKI-RGYRVELGEIRT-ALAELEGVEHAAVIAREDRP-----------GERRLVGYITGTADPAT----V 145
Cdd:PRK12582 472 LIFDGRVAEDFKLsTGTWVSVGTLRPdAVAACSPVIHDAVVAGQDRAfigllawpnpaACRQLAGDPDAAPEDVVkhpaV 551
|
170
....*....|.
gi 1178432446 146 RAELARRLPAH 156
Cdd:PRK12582 552 LAILREGLSAH 562
|
|
| PRK07470 |
PRK07470 |
acyl-CoA synthetase; Validated |
8-190 |
2.95e-06 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 180988 [Multi-domain] Cd Length: 528 Bit Score: 50.04 E-value: 2.95e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178432446 8 GAPVPGAALVVLDGWLRPVSAGVVGELYVAGRGVGVGYWRRPGLSASRFVACPFgppgtrmyRTGDRVRWRADGQLEYLG 87
Cdd:PRK07470 343 GFERTGMEVQIQDDEGRELPPGETGEICVIGPAVFAGYYNNPEANAKAFRDGWF--------RTGDLGHLDARGFLYITG 414
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178432446 88 RTDDQVKIRGYRVELGEIRTALAELEGVEHAAVIAREDRP-GErrlVGYITGTA------DPATVRAELARRLPAHMVPA 160
Cdd:PRK07470 415 RASDMYISGGSNVYPREIEEKLLTHPAVSEVAVLGVPDPVwGE---VGVAVCVArdgapvDEAELLAWLDGKVARYKLPK 491
|
170 180 190
....*....|....*....|....*....|
gi 1178432446 161 SVMALQALPLTVNGKLNTRALPAPRYADGD 190
Cdd:PRK07470 492 RFFFWDALPKSGYGKITKKMVREELEERGL 521
|
|
| PRK08316 |
PRK08316 |
acyl-CoA synthetase; Validated |
18-181 |
3.02e-06 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 181381 [Multi-domain] Cd Length: 523 Bit Score: 49.93 E-value: 3.02e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178432446 18 VLDGWLRPVSAGVVGElyVAGRG--VGVGYWRRPGLSASRFVACPFgppgtrmyRTGDRVRWRADGQLEYLGRTDDQVKI 95
Cdd:PRK08316 354 VVDDDGNDVAPGEVGE--IVHRSpqLMLGYWDDPEKTAEAFRGGWF--------HSGDLGVMDEEGYITVVDRKKDMIKT 423
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178432446 96 RGYRVELGEIRTALAELEGVEHAAVIARED-------------RPGErrlvgyitgTADPATVRAELARRLPAHMVPASV 162
Cdd:PRK08316 424 GGENVASREVEEALYTHPAVAEVAVIGLPDpkwieavtavvvpKAGA---------TVTEDELIAHCRARLAGFKVPKRV 494
|
170
....*....|....*....
gi 1178432446 163 MALQALPLTVNGKLNTRAL 181
Cdd:PRK08316 495 IFVDELPRNPSGKILKREL 513
|
|
| entE |
PRK10946 |
(2,3-dihydroxybenzoyl)adenylate synthase; |
25-181 |
3.82e-06 |
|
(2,3-dihydroxybenzoyl)adenylate synthase;
Pssm-ID: 236803 [Multi-domain] Cd Length: 536 Bit Score: 49.60 E-value: 3.82e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178432446 25 PVSAGVVGELYVAGRGVGVGYWRRPGLSASRFVACPFgppgtrmYRTGDRVRWRADGQLEYLGRTDDQVKIRGYRVELGE 104
Cdd:PRK10946 374 PLPQGEVGRLMTRGPYTFRGYYKSPQHNASAFDANGF-------YCSGDLVSIDPDGYITVVGREKDQINRGGEKIAAEE 446
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178432446 105 IRTALAELEGVEHAAVIARED-RPGERRlVGYITgTADPatVRA-ELARRLPAHMV-----PASVMALQALPLTVNGKLN 177
Cdd:PRK10946 447 IENLLLRHPAVIHAALVSMEDeLMGEKS-CAFLV-VKEP--LKAvQLRRFLREQGIaefklPDRVECVDSLPLTAVGKVD 522
|
....
gi 1178432446 178 TRAL 181
Cdd:PRK10946 523 KKQL 526
|
|
| PRK13383 |
PRK13383 |
acyl-CoA synthetase; Provisional |
7-183 |
4.29e-06 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 139531 [Multi-domain] Cd Length: 516 Bit Score: 49.61 E-value: 4.29e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178432446 7 IGAPVPGAALVVLDGWLRPVSAGVVGELYVAGRGVGVGYWRRPGLSASrfvacpfgppgTRMYRTGDRVRWRADGQLEYL 86
Cdd:PRK13383 347 VGKPVAGCPVRILDRNNRPVGPRVTGRIFVGGELAGTRYTDGGGKAVV-----------DGMTSTGDMGYLDNAGRLFIV 415
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178432446 87 GRTDDQVKIRGYRVELGEIRTALAELEGVEHAAVIAREDRPGERRLVGYITG----TADPATVRAELARRLPAHMVPASV 162
Cdd:PRK13383 416 GREDDMIISGGENVYPRAVENALAAHPAVADNAVIGVPDERFGHRLAAFVVLhpgsGVDAAQLRDYLKDRVSRFEQPRDI 495
|
170 180
....*....|....*....|.
gi 1178432446 163 MALQALPLTVNGKLNTRALPA 183
Cdd:PRK13383 496 NIVSSIPRNPTGKVLRKELPG 516
|
|
| PRK07798 |
PRK07798 |
acyl-CoA synthetase; Validated |
12-175 |
9.33e-06 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236100 [Multi-domain] Cd Length: 533 Bit Score: 48.34 E-value: 9.33e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178432446 12 PGAALVVLDGWLRPVSAGVVGELYVAGRG-VGVGYWRRPGLSASRFvacpFGPPGTRMYRTGDRVRWRADGQLEYLGRtd 90
Cdd:PRK07798 356 IGPRTVVLDEDGNPVEPGSGEIGWIARRGhIPLGYYKDPEKTAETF----PTIDGVRYAIPGDRARVEADGTITLLGR-- 429
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178432446 91 DQVKIR--GYRVELGEIRTALAELEGVEHAAVIARED-RPGErRLVGYIT----GTADPATVRAELARRLPAHMVPASVM 163
Cdd:PRK07798 430 GSVCINtgGEKVFPEEVEEALKAHPDVADALVVGVPDeRWGQ-EVVAVVQlregARPDLAELRAHCRSSLAGYKVPRAIW 508
|
170
....*....|..
gi 1178432446 164 ALQALPLTVNGK 175
Cdd:PRK07798 509 FVDEVQRSPAGK 520
|
|
| prpE |
PRK10524 |
propionyl-CoA synthetase; Provisional |
55-183 |
1.05e-05 |
|
propionyl-CoA synthetase; Provisional
Pssm-ID: 182517 [Multi-domain] Cd Length: 629 Bit Score: 48.41 E-value: 1.05e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178432446 55 RFVACPFGPPGTRMYRTGDRVRWRADGQLEYLGRTDDQVKIRGYRVELGEIRTALAELEGVEHAAVIARED--------- 125
Cdd:PRK10524 461 RFVKTYWSLFGRQVYSTFDWGIRDADGYYFILGRTDDVINVAGHRLGTREIEESISSHPAVAEVAVVGVKDalkgqvava 540
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1178432446 126 ----RPGERrlvgyITGTADPATVRAEL----ARRLPAHMVPASVMALQALPLTVNGKLNTRALPA 183
Cdd:PRK10524 541 fvvpKDSDS-----LADREARLALEKEImalvDSQLGAVARPARVWFVSALPKTRSGKLLRRAIQA 601
|
|
| PRK07638 |
PRK07638 |
acyl-CoA synthetase; Validated |
80-176 |
1.70e-05 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236071 [Multi-domain] Cd Length: 487 Bit Score: 47.47 E-value: 1.70e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178432446 80 DGQLEYLGRTDDQVKIRGYRVELGEIRTALAELEGVEHAAVIAREDRPGERRLVGYITGTADPATVRAELARRLPAHMVP 159
Cdd:PRK07638 374 EGFIYIVGREKNMILFGGINIFPEEIESVLHEHPAVDEIVVIGVPDSYWGEKPVAIIKGSATKQQLKSFCLQRLSSFKIP 453
|
90
....*....|....*..
gi 1178432446 160 ASVMALQALPLTVNGKL 176
Cdd:PRK07638 454 KEWHFVDEIPYTNSGKI 470
|
|
| PRK08974 |
PRK08974 |
long-chain-fatty-acid--CoA ligase FadD; |
7-181 |
2.17e-05 |
|
long-chain-fatty-acid--CoA ligase FadD;
Pssm-ID: 236359 [Multi-domain] Cd Length: 560 Bit Score: 47.36 E-value: 2.17e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178432446 7 IGAPVPGAALVVLDGWLRPVSAGVVGELYVAGRGVGVGYWRRPGLSAS----RFVAcpfgppgtrmyrTGDRVRWRADGQ 82
Cdd:PRK08974 380 IGLPVPSTEIKLVDDDGNEVPPGEPGELWVKGPQVMLGYWQRPEATDEvikdGWLA------------TGDIAVMDEEGF 447
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178432446 83 LEYLGRTDDQVKIRGYRVELGEIRTALAELEGV-EHAAVIAREDRPGErrLVGYITGTADPATVRAELA----RRLPAHM 157
Cdd:PRK08974 448 LRIVDRKKDMILVSGFNVYPNEIEDVVMLHPKVlEVAAVGVPSEVSGE--AVKIFVVKKDPSLTEEELIthcrRHLTGYK 525
|
170 180
....*....|....*....|....
gi 1178432446 158 VPASVMALQALPLTVNGKLNTRAL 181
Cdd:PRK08974 526 VPKLVEFRDELPKSNVGKILRREL 549
|
|
| GrsT |
COG3208 |
Surfactin synthase thioesterase subunit [Secondary metabolites biosynthesis, transport and ... |
322-419 |
2.83e-05 |
|
Surfactin synthase thioesterase subunit [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 442441 [Multi-domain] Cd Length: 237 Bit Score: 45.61 E-value: 2.83e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178432446 322 GEGEPESIRAMAARYADTLQAlYPDGPYKLLGWSFGGVVAQELAIELQRRGCVVQSLVLLdapySATKGVTRLGANK-IR 400
Cdd:COG3208 48 GEPPLTSLEELADDLAEELAP-LLDRPFALFGHSMGALLAFELARRLERRGRPLPAHLFV----SGRRAPHLPRRRRpLH 122
|
90
....*....|....*....
gi 1178432446 401 ASAESQILQRILRANGIDA 419
Cdd:COG3208 123 DLSDAELLAELRRLGGTPE 141
|
|
| PRK08279 |
PRK08279 |
long-chain-acyl-CoA synthetase; Validated |
8-159 |
2.95e-05 |
|
long-chain-acyl-CoA synthetase; Validated
Pssm-ID: 236217 [Multi-domain] Cd Length: 600 Bit Score: 46.79 E-value: 2.95e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178432446 8 GAPVPGAalvvlDGWLRPVSAGVVGELY--VAGRGVGVGYwRRPGLSASRFVACPFGpPGTRMYRTGDRVRWRADGQLEY 85
Cdd:PRK08279 385 GEPVRDA-----DGRCIKVKPGEVGLLIgrITDRGPFDGY-TDPEASEKKILRDVFK-KGDAWFNTGDLMRDDGFGHAQF 457
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1178432446 86 LGRTDDQVKIRGYRVELGEIRTALAELEGVEHAAV----IARED-RPGERRLVGYITGTADPATVRAELARRLPAHMVP 159
Cdd:PRK08279 458 VDRLGDTFRWKGENVATTEVENALSGFPGVEEAVVygveVPGTDgRAGMAAIVLADGAEFDLAALAAHLYERLPAYAVP 536
|
|
| Abhydrolase_1 |
pfam00561 |
alpha/beta hydrolase fold; This catalytic domain is found in a very wide range of enzymes. |
287-389 |
3.41e-05 |
|
alpha/beta hydrolase fold; This catalytic domain is found in a very wide range of enzymes.
Pssm-ID: 395444 [Multi-domain] Cd Length: 245 Bit Score: 45.57 E-value: 3.41e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178432446 287 PLWCIHDGFGLSWPYRALGRYLD---CPVIGINrVPQNGEGEPES-----IRAMAARYADTLQALYPDGPYKLLGWSFGG 358
Cdd:pfam00561 2 PVLLLHGLPGSSDLWRKLAPALArdgFRVIALD-LRGFGKSSRPKaqddyRTDDLAEDLEYILEALGLEKVNLVGHSMGG 80
|
90 100 110
....*....|....*....|....*....|.
gi 1178432446 359 VVAQELAIELQRRgcvVQSLVLLDAPYSATK 389
Cdd:pfam00561 81 LIALAYAAKYPDR---VKALVLLGALDPPHE 108
|
|
| PRK08180 |
PRK08180 |
feruloyl-CoA synthase; Reviewed |
7-156 |
3.56e-05 |
|
feruloyl-CoA synthase; Reviewed
Pssm-ID: 236175 [Multi-domain] Cd Length: 614 Bit Score: 46.41 E-value: 3.56e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178432446 7 IGAPVPGAA--LVVLDGWLrpvsagvvgELYVAGRGVGVGYWRRPGLSASRFVACPFgppgtrmYRTGDRVRWrADGQ-- 82
Cdd:PRK08180 394 IGLPAPGCEvkLVPVGGKL---------EVRVKGPNVTPGYWRAPELTAEAFDEEGY-------YRSGDAVRF-VDPAdp 456
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178432446 83 ---LEYLGRTDDQVKI-RGYRVELGEIRTAL-AELEGVEHAAVIAREDR-----------PGERRLVG-----YITGTAD 141
Cdd:PRK08180 457 ergLMFDGRIAEDFKLsSGTWVSVGPLRARAvSAGAPLVQDVVITGHDRdeigllvfpnlDACRRLAGlladaSLAEVLA 536
|
170
....*....|....*
gi 1178432446 142 PATVRAELARRLPAH 156
Cdd:PRK08180 537 HPAVRAAFRERLARL 551
|
|
| PRK04319 |
PRK04319 |
acetyl-CoA synthetase; Provisional |
8-183 |
3.69e-05 |
|
acetyl-CoA synthetase; Provisional
Pssm-ID: 235279 [Multi-domain] Cd Length: 570 Bit Score: 46.43 E-value: 3.69e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178432446 8 GAPVPG--AALVVLDGWLRPvsAGVVGELYVAgRG---VGVGYWRRPglsaSRFVACPFGppgtRMYRTGDRVRWRADGQ 82
Cdd:PRK04319 379 GKPLPGieAAIVDDQGNELP--PNRMGNLAIK-KGwpsMMRGIWNNP----EKYESYFAG----DWYVSGDSAYMDEDGY 447
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178432446 83 LEYLGRTDDQVKIRGYRVELGEIRTALAELEGVEHAAVIAREDrPgerrLVGYI--------TGTADPATVRAELA---- 150
Cdd:PRK04319 448 FWFQGRVDDVIKTSGERVGPFEVESKLMEHPAVAEAGVIGKPD-P----VRGEIikafvalrPGYEPSEELKEEIRgfvk 522
|
170 180 190
....*....|....*....|....*....|...
gi 1178432446 151 RRLPAHMVPASVMALQALPLTVNGKLNTRALPA 183
Cdd:PRK04319 523 KGLGAHAAPREIEFKDKLPKTRSGKIMRRVLKA 555
|
|
| PRK06710 |
PRK06710 |
long-chain-fatty-acid--CoA ligase; Validated |
7-181 |
3.73e-05 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 180666 [Multi-domain] Cd Length: 563 Bit Score: 46.56 E-value: 3.73e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178432446 7 IGAPVPG--AALVVLDGW--LRPvsaGVVGELYVAGRGVGVGYWRRPGLSASRFvacpfgppGTRMYRTGDRVRWRADGQ 82
Cdd:PRK06710 378 IGVPWPDteAMIMSLETGeaLPP---GEIGEIVVKGPQIMKGYWNKPEETAAVL--------QDGWLHTGDVGYMDEDGF 446
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178432446 83 LEYLGRTDDQVKIRGYRVELGEIRTALAELEGVEHAAVIAREDRPGERRLVGYITGTADPATVRAEL---ARR-LPAHMV 158
Cdd:PRK06710 447 FYVKDRKKDMIVASGFNVYPREVEEVLYEHEKVQEVVTIGVPDPYRGETVKAFVVLKEGTECSEEELnqfARKyLAAYKV 526
|
170 180
....*....|....*....|...
gi 1178432446 159 PASVMALQALPLTVNGKLNTRAL 181
Cdd:PRK06710 527 PKVYEFRDELPKTTVGKILRRVL 549
|
|
| PRK13388 |
PRK13388 |
acyl-CoA synthetase; Provisional |
31-190 |
3.81e-05 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 237374 [Multi-domain] Cd Length: 540 Bit Score: 46.56 E-value: 3.81e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178432446 31 VGELY-VAGRGVGVGYWRRPGLSASRFvacpfgppgtR--MYRTGDRVRWRADGQLEYLGRTDDQVKIRGYRVELGEIRT 107
Cdd:PRK13388 351 IGELVnTAGAGFFEGYYNNPEATAERM----------RhgMYWSGDLAYRDADGWIYFAGRTADWMRVDGENLSAAPIER 420
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178432446 108 ALAELEGVEHAAVIARED-RPGER---RLVGYITGTADPATVRAELA--RRLPAHMVPASVMALQALPLTVNGKLNTRAL 181
Cdd:PRK13388 421 ILLRHPAINRVAVYAVPDeRVGDQvmaALVLRDGATFDPDAFAAFLAaqPDLGTKAWPRYVRIAADLPSTATNKVLKREL 500
|
....*....
gi 1178432446 182 PAPRYADGD 190
Cdd:PRK13388 501 IAQGWATGD 509
|
|
| PRK06087 |
PRK06087 |
medium-chain fatty-acid--CoA ligase; |
8-177 |
3.88e-05 |
|
medium-chain fatty-acid--CoA ligase;
Pssm-ID: 180393 [Multi-domain] Cd Length: 547 Bit Score: 46.28 E-value: 3.88e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178432446 8 GAPVPGAALVVLDGWLRPVSAGVVGELYVAGRGVGVGYWRRPGLSASRFVAcpfgppgTRMYRTGDRVRWRADGQLEYLG 87
Cdd:PRK06087 358 GYAAAGVEIKVVDEARKTLPPGCEGEEASRGPNVFMGYLDEPELTARALDE-------EGWYYSGDLCRMDEAGYIKITG 430
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178432446 88 RTDDQVKIRGYRVELGEIRTALAELEGVEHAAVIARED-RPGERrLVGYITGTADPAT-----VRAELAR-RLPAHMVPA 160
Cdd:PRK06087 431 RKKDIIVRGGENISSREVEDILLQHPKIHDACVVAMPDeRLGER-SCAYVVLKAPHHSltleeVVAFFSRkRVAKYKYPE 509
|
170
....*....|....*..
gi 1178432446 161 SVMALQALPLTVNGKLN 177
Cdd:PRK06087 510 HIVVIDKLPRTASGKIQ 526
|
|
| FATP_chFAT1_like |
cd05937 |
Uncharacterized subfamily of bifunctional fatty acid transporter/very-long-chain acyl-CoA ... |
44-177 |
4.03e-05 |
|
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: 46.27 E-value: 4.03e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178432446 44 GYWRRPGLSASRFVACPFgPPGTRMYRTGDRVRWRADGQLEYLGRTDDQVKIRGYRVELGEIRTALAELEGVeHAAVIAR 123
Cdd:cd05937 316 GYLHNEDATESKLVRDVF-RKGDIYFRTGDLLRQDADGRWYFLDRLGDTFRWKSENVSTTEVADVLGAHPDI-AEANVYG 393
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1178432446 124 EDRPGERRLVGY--ITGT---ADPATVR----AELAR-RLPAHMVPASVMALQALPLTVNGKLN 177
Cdd:cd05937 394 VKVPGHDGRAGCaaITLEessAVPTEFTksllASLARkNLPSYAVPLFLRLTEEVATTDNHKQQ 457
|
|
| PRK12406 |
PRK12406 |
long-chain-fatty-acid--CoA ligase; Provisional |
7-191 |
4.69e-05 |
|
long-chain-fatty-acid--CoA ligase; Provisional
Pssm-ID: 183506 [Multi-domain] Cd Length: 509 Bit Score: 46.23 E-value: 4.69e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178432446 7 IGAPVPGAALVVLDGWLRPVSAGVVGELYVAGRGVG-VGYWRRPGLSAS----RFVAcpfgppgtrmyrTGDRVRWRADG 81
Cdd:PRK12406 326 VGKAAPGAELRFVDEDGRPLPQGEIGEIYSRIAGNPdFTYHNKPEKRAEidrgGFIT------------SGDVGYLDADG 393
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178432446 82 QLEYLGRTDDQVKIRGYRVELGEIRTALAELEGVEHAAVIAREDRPGERRLVGYIT----GTADPATVRAELARRLPAHM 157
Cdd:PRK12406 394 YLFLCDRKRDMVISGGVNIYPAEIEAVLHAVPGVHDCAVFGIPDAEFGEALMAVVEpqpgATLDEADIRAQLKARLAGYK 473
|
170 180 190
....*....|....*....|....*....|....
gi 1178432446 158 VPASVMALQALPLTVNGKLNTRALPAPRYADGDR 191
Cdd:PRK12406 474 VPKHIEIMAELPREDSGKIFKRRLRDPYWANAGR 507
|
|
| PRK05851 |
PRK05851 |
long-chain-fatty acid--ACP ligase MbtM; |
7-176 |
4.83e-05 |
|
long-chain-fatty acid--ACP ligase MbtM;
Pssm-ID: 180289 [Multi-domain] Cd Length: 525 Bit Score: 45.91 E-value: 4.83e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178432446 7 IGAPVPGAALVVLDG-WLRPVSAGVVGELYVAGRGVGVGYWRRPGLSASRFvacpfgppgtrmYRTGDrVRWRADGQLEY 85
Cdd:PRK05851 347 LGNPIPGMEVRISPGdGAAGVAGREIGEIEIRGASMMSGYLGQAPIDPDDW------------FPTGD-LGYLVDGGLVV 413
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178432446 86 LGRTDDQVKIRGYRVELGEIRTALAELEGVEHAAVIA-----REDRPGerRLVGYITGTADPATVRAELARRLPAH--MV 158
Cdd:PRK05851 414 CGRAKELITVAGRNIFPTEIERVAAQVRGVREGAVVAvgtgeGSARPG--LVIAAEFRGPDEAGARSEVVQRVASEcgVV 491
|
170 180
....*....|....*....|
gi 1178432446 159 PASV--MALQALPLTVNGKL 176
Cdd:PRK05851 492 PSDVvfVAPGSLPRTSSGKL 511
|
|
| LC_FACS_euk1 |
cd17639 |
Eukaryotic long-chain fatty acid CoA synthetase (LC-FACS), including fungal proteins; The ... |
32-161 |
6.02e-05 |
|
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: 45.67 E-value: 6.02e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178432446 32 GELYVAGRGVGVGYWRRPGLSASRFVacpfgppGTRMYRTGDRVRWRADGQLEYLGRTDDQVKIR-GYRVELGEIRTALA 110
Cdd:cd17639 331 GEILIRGPNVFKGYYKNPEKTKEAFD-------GDGWFHTGDIGEFHPDGTLKIIDRKKDLVKLQnGEYIALEKLESIYR 403
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|..
gi 1178432446 111 ELEGVEHAAVIAREDRPgerrlvgYITGTADPATVRAE-LARrlpAHMVPAS 161
Cdd:cd17639 404 SNPLVNNICVYADPDKS-------YPVAIVVPNEKHLTkLAE---KHGVINS 445
|
|
| PRK05850 |
PRK05850 |
acyl-CoA synthetase; Validated |
27-97 |
8.97e-05 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 235624 [Multi-domain] Cd Length: 578 Bit Score: 45.32 E-value: 8.97e-05
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1178432446 27 SAGVVGELYVAGRGVGVGYWRRPGLSASRFVACPFGP-PGTRM---YRTGDrVRWRADGQLEYLGRTDDQVKIRG 97
Cdd:PRK05850 393 PAGTVGEIWVHGDNVAAGYWQKPEETERTFGATLVDPsPGTPEgpwLRTGD-LGFISEGELFIVGRIKDLLIVDG 466
|
|
| PLN02479 |
PLN02479 |
acetate-CoA ligase |
1-183 |
1.48e-04 |
|
acetate-CoA ligase
Pssm-ID: 178097 [Multi-domain] Cd Length: 567 Bit Score: 44.45 E-value: 1.48e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178432446 1 GSDVV--PIGAPVPGaalvvlDGwlrpvsaGVVGELYVAGRGVGVGYWRRPGLSASRFvacpfgppGTRMYRTGDRVRWR 78
Cdd:PLN02479 383 GLDVVdtKTMKPVPA------DG-------KTMGEIVMRGNMVMKGYLKNPKANEEAF--------ANGWFHSGDLGVKH 441
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178432446 79 ADGQLEYLGRTDDQVKIRGYRVELGEIRTALAELEGVEHAAVIAREDRPGERRLVGYIT-----GTADPATVRAELAR-- 151
Cdd:PLN02479 442 PDGYIEIKDRSKDIIISGGENISSLEVENVVYTHPAVLEASVVARPDERWGESPCAFVTlkpgvDKSDEAALAEDIMKfc 521
|
170 180 190
....*....|....*....|....*....|....
gi 1178432446 152 --RLPAHMVPASVMaLQALPLTVNGKLNTRALPA 183
Cdd:PLN02479 522 reRLPAYWVPKSVV-FGPLPKTATGKIQKHVLRA 554
|
|
| OSB_CoA_lg |
cd05912 |
O-succinylbenzoate-CoA ligase (also known as O-succinylbenzoate-CoA synthase, OSB-CoA ... |
8-181 |
1.61e-04 |
|
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: 44.26 E-value: 1.61e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178432446 8 GAPVPGAALVVLDGWLRPvsaGVVGELYVAGRGVGVGYWRRPGLSASRFVACPFgppgtrmyRTGDRVRWRADGQLEYLG 87
Cdd:cd05912 245 GKPLFPVELKIEDDGQPP---YEVGEILLKGPNVTKGYLNRPDATEESFENGWF--------KTGDIGYLDEEGFLYVLD 313
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178432446 88 RTDDQVKIRGYRVELGEIRTALAELEGVEHAAVIAREDRPGERRLVGYITG--TADPATVRAELARRLPAHMVPASVMAL 165
Cdd:cd05912 314 RRSDLIISGGENIYPAEIEEVLLSHPAIKEAGVVGIPDDKWGQVPVAFVVSerPISEEELIAYCSEKLAKYKVPKKIYFV 393
|
170
....*....|....*.
gi 1178432446 166 QALPLTVNGKLNTRAL 181
Cdd:cd05912 394 DELPRTASGKLLRHEL 409
|
|
| PRK03640 |
PRK03640 |
o-succinylbenzoate--CoA ligase; |
23-181 |
3.31e-04 |
|
o-succinylbenzoate--CoA ligase;
Pssm-ID: 235146 [Multi-domain] Cd Length: 483 Bit Score: 43.41 E-value: 3.31e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178432446 23 LRPVSAGVVGELYVAGRGVGVGYWRRPGLSASRFVACPFgppgtrmyRTGDRVRWRADGQLEYLGRTDDQVKIRGYRVEL 102
Cdd:PRK03640 324 GVVVPPFEEGEIVVKGPNVTKGYLNREDATRETFQDGWF--------KTGDIGYLDEEGFLYVLDRRSDLIISGGENIYP 395
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178432446 103 GEIRTALAELEGVEHAAVIAREDRPGERRLVGYI--TGTADPATVRAELARRLPAHMVPASVMALQALPLTVNGKLNTRA 180
Cdd:PRK03640 396 AEIEEVLLSHPGVAEAGVVGVPDDKWGQVPVAFVvkSGEVTEEELRHFCEEKLAKYKVPKRFYFVEELPRNASGKLLRHE 475
|
.
gi 1178432446 181 L 181
Cdd:PRK03640 476 L 476
|
|
| FATP_FACS |
cd05940 |
Fatty acid transport proteins (FATP) play dual roles as fatty acid transporters and its ... |
65-175 |
4.77e-04 |
|
Fatty acid transport proteins (FATP) play dual roles as fatty acid transporters and its activation enzymes; Fatty acid transport protein (FATP) transports long-chain or very-long-chain fatty acids across the plasma membrane. FATPs also have fatty acid CoA synthetase activity, thus playing dual roles as fatty acid transporters and its activation enzymes. At least five copies of FATPs are identified in mammalian cells. This family also includes prokaryotic FATPs. FATPs are the key players in the trafficking of exogenous fatty acids into the cell and in intracellular fatty acid homeostasis.
Pssm-ID: 341263 [Multi-domain] Cd Length: 449 Bit Score: 42.73 E-value: 4.77e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178432446 65 GTRMYRTGDRVRWRADGQLEYLGRTDDQVKIRGYRVELGEIRTALAELEGVEHAAV----IARED-RPGERRLVGYITGT 139
Cdd:cd05940 321 GDAWFNTGDLMRLDGEGFWYFVDRLGDTFRWKGENVSTTEVAAVLGAFPGVEEANVygvqVPGTDgRAGMAAIVLQPNEE 400
|
90 100 110
....*....|....*....|....*....|....*.
gi 1178432446 140 ADPATVRAELARRLPAHMVPASVMALQALPLTVNGK 175
Cdd:cd05940 401 FDLSALAAHLEKNLPGYARPLFLRLQPEMEITGTFK 436
|
|
| VL_LC_FACS_like |
cd05907 |
Long-chain fatty acid CoA synthetases and Bubblegum-like very long-chain fatty acid CoA ... |
7-161 |
5.76e-04 |
|
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: 42.58 E-value: 5.76e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178432446 7 IGAPVPGAALVVldgwlrpvsaGVVGELYVAGRGVGVGYWRRPGLSASRFVAcpfgpPGTrmYRTGDRVRWRADGQLEYL 86
Cdd:cd05907 264 VGKPLPGVEVRI----------ADDGEILVRGPNVMLGYYKNPEATAEALDA-----DGW--LHTGDLGEIDEDGFLHIT 326
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1178432446 87 GRTDD-QVKIRGYRVELGEIRTALAELEGVEHAAVIArEDRPgerRLVGYItgTADPATVRAELARRLPAHMVPAS 161
Cdd:cd05907 327 GRKKDlIITSGGKNISPEPIENALKASPLISQAVVIG-DGRP---FLVALI--VPDPEALEAWAEEHGIAYTDVAE 396
|
|
| MenH |
COG0596 |
2-succinyl-6-hydroxy-2,4-cyclohexadiene-1-carboxylate synthase MenH and related esterases, ... |
284-383 |
6.09e-04 |
|
2-succinyl-6-hydroxy-2,4-cyclohexadiene-1-carboxylate synthase MenH and related esterases, alpha/beta hydrolase fold [Coenzyme transport and metabolism, General function prediction only]; 2-succinyl-6-hydroxy-2,4-cyclohexadiene-1-carboxylate synthase MenH and related esterases, alpha/beta hydrolase fold is part of the Pathway/BioSystem: Menaquinone biosynthesis
Pssm-ID: 440361 [Multi-domain] Cd Length: 221 Bit Score: 41.53 E-value: 6.09e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178432446 284 SGVPLWCIHDGFGLSWPYRALGRYL--DCPVIGINRVpqnGEGE------PESIRAMAARYADTLQALyPDGPYKLLGWS 355
Cdd:COG0596 22 DGPPVVLLHGLPGSSYEWRPLIPALaaGYRVIAPDLR---GHGRsdkpagGYTLDDLADDLAALLDAL-GLERVVLVGHS 97
|
90 100
....*....|....*....|....*...
gi 1178432446 356 FGGVVAQELAIELQRRgcvVQSLVLLDA 383
Cdd:COG0596 98 MGGMVALELAARHPER---VAGLVLVDE 122
|
|
| LC_FACS_like |
cd17640 |
Long-chain fatty acid CoA synthetase; This family includes long-chain fatty acid (C12-C20) CoA ... |
7-126 |
7.82e-04 |
|
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: 41.96 E-value: 7.82e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178432446 7 IGAPVPGAALVVLD----GWLRPvsaGVVGELYVAGRGVGVGYWRRPglSASRFVACPFGppgtrMYRTGDRVRWRADGQ 82
Cdd:cd17640 266 VGRPLPGTEIKIVDpegnVVLPP---GEKGIVWVRGPQVMKGYYKNP--EATSKVLDSDG-----WFNTGDLGWLTCGGE 335
|
90 100 110 120
....*....|....*....|....*....|....*....|....*
gi 1178432446 83 LEYLGRTDDQVKIR-GYRVELGEIRTALAELEGVEHAAVIAREDR 126
Cdd:cd17640 336 LVLTGRAKDTIVLSnGENVEPQPIEEALMRSPFIEQIMVVGQDQK 380
|
|
| PRK07445 |
PRK07445 |
O-succinylbenzoic acid--CoA ligase; Reviewed |
8-182 |
7.99e-04 |
|
O-succinylbenzoic acid--CoA ligase; Reviewed
Pssm-ID: 236019 [Multi-domain] Cd Length: 452 Bit Score: 41.90 E-value: 7.99e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178432446 8 GAPVPGAALVVldgwlrpvSAGVVGELYVAGRGVGVGYWrrPGLSASRfvacpfgppgtRMYRTGDRVRWRADGQLEYLG 87
Cdd:PRK07445 286 GQVLPHAQITI--------PANQTGNITIQAQSLALGYY--PQILDSQ-----------GIFETDDLGYLDAQGYLHILG 344
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178432446 88 RTDDQVKIRGYRVELGEIRTALAELEGVEHAAVIAREDRP-GERRLVGYI--TGTADPATVRAELARRLPAHMVPASVMA 164
Cdd:PRK07445 345 RNSQKIITGGENVYPAEVEAAILATGLVQDVCVLGLPDPHwGEVVTAIYVpkDPSISLEELKTAIKDQLSPFKQPKHWIP 424
|
170
....*....|....*...
gi 1178432446 165 LQALPLTVNGKLNTRALP 182
Cdd:PRK07445 425 VPQLPRNPQGKINRQQLQ 442
|
|
| PRK00174 |
PRK00174 |
acetyl-CoA synthetase; Provisional |
8-181 |
8.82e-04 |
|
acetyl-CoA synthetase; Provisional
Pssm-ID: 234677 [Multi-domain] Cd Length: 637 Bit Score: 42.05 E-value: 8.82e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178432446 8 GAPVPGAA---LVVLDGWlrPvsagvvGELyvagRGVgvgyWRRPglsaSRFVACPFGP-PGtrMYRTGDRVRWRADGQL 83
Cdd:PRK00174 442 GNPLEGGEggnLVIKDPW--P------GMM----RTI----YGDH----ERFVKTYFSTfKG--MYFTGDGARRDEDGYY 499
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178432446 84 EYLGRTDDQVKIRGYRVELGEIRTALAELEGVEHAAViaredrpgerrlVGY---ITGTA--------DPATVRAELARR 152
Cdd:PRK00174 500 WITGRVDDVLNVSGHRLGTAEIESALVAHPKVAEAAV------------VGRpddIKGQGiyafvtlkGGEEPSDELRKE 567
|
170 180 190
....*....|....*....|....*....|....*..
gi 1178432446 153 LPAHMV--------PASVMALQALPLTVNGKLNTRAL 181
Cdd:PRK00174 568 LRNWVRkeigpiakPDVIQFAPGLPKTRSGKIMRRIL 604
|
|
| PRK07769 |
PRK07769 |
long-chain-fatty-acid--CoA ligase; Validated |
5-196 |
1.06e-03 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 181109 [Multi-domain] Cd Length: 631 Bit Score: 42.02 E-value: 1.06e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178432446 5 VPIGAP--VP--GAALVVLDGWLRPVSA--------GVVGELYVAGRGVGVGYWRRPGLSASRF---VACPF-------G 62
Cdd:PRK07769 380 VPADAPnaVAqvSAGKVGVSEWAVIVDPetaselpdGQIGEIWLHGNNIGTGYWGKPEETAATFqniLKSRLseshaegA 459
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178432446 63 PPGTRMYRTGDRVRWrADGQLEYLGRTDDQVKIRG---YRVEL----GEIRTAL----------------AELEGVEHAA 119
Cdd:PRK07769 460 PDDALWVRTGDYGVY-FDGELYITGRVKDLVIIDGrnhYPQDLeytaQEATKALrtgyvaafsvpanqlpQVVFDDSHAG 538
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178432446 120 VIAREDRPGER------RLVGyiTGTADPA----TVRAELARRlpaHMVPA-SVMALQA--LPLTVNGKLNTRALPAPrY 186
Cdd:PRK07769 539 LKFDPEDTSEQlvivaeRAPG--AHKLDPQpiadDIRAAIAVR---HGVTVrDVLLVPAgsIPRTSSGKIARRACRAA-Y 612
|
250
....*....|...
gi 1178432446 187 ADGD---RYRAPA 196
Cdd:PRK07769 613 LDGSlrsGYGQPA 625
|
|
| PRK07768 |
PRK07768 |
long-chain-fatty-acid--CoA ligase; Validated |
4-181 |
1.16e-03 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236091 [Multi-domain] Cd Length: 545 Bit Score: 41.52 E-value: 1.16e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178432446 4 VVPIGAPVPGAALVVLDGWLRPVSAGVVGELYVAGRGVGVGYwrrpgLSASRFVAcpfgppgtrmyrTGDRVRWRADGQL 83
Cdd:PRK07768 359 LATLGPPLPGLEVRVVDEDGQVLPPRGVGVIELRGESVTPGY-----LTMDGFIP------------AQDADGWLDTGDL 421
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178432446 84 EYL---------GRTDDQVKIRGYRVELGEIRTALAELEGVEHAAVIA-REDRPGER---RLVGYITGTADPATVRA--- 147
Cdd:PRK07768 422 GYLteegevvvcGRVKDVIIMAGRNIYPTDIERAAARVEGVRPGNAVAvRLDAGHSRegfAVAVESNAFEDPAEVRRirh 501
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 1178432446 148 ELARRLPAH--MVPASVMALQA--LPLTVNGKL---NTRAL 181
Cdd:PRK07768 502 QVAHEVVAEvgVRPRNVVVLGPgsIPKTPSGKLrraNAAEL 542
|
|
| FAA1 |
COG1022 |
Long-chain acyl-CoA synthetase (AMP-forming) [Lipid transport and metabolism]; |
32-127 |
1.19e-03 |
|
Long-chain acyl-CoA synthetase (AMP-forming) [Lipid transport and metabolism];
Pssm-ID: 440645 [Multi-domain] Cd Length: 603 Bit Score: 41.62 E-value: 1.19e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178432446 32 GELYVAGRGVGVGYWRRPGLSASRFVAcpfgpPGtrMYRTGDRVRWRADGQLEYLGRTDDQVKIR-GYRVELGEIRTALA 110
Cdd:COG1022 415 GEILVRGPNVMKGYYKNPEATAEAFDA-----DG--WLHTGDIGELDEDGFLRITGRKKDLIVTSgGKNVAPQPIENALK 487
|
90
....*....|....*..
gi 1178432446 111 ELEGVEHAAVIArEDRP 127
Cdd:COG1022 488 ASPLIEQAVVVG-DGRP 503
|
|
| ttLC_FACS_AEE21_like |
cd12118 |
Fatty acyl-CoA synthetases similar to LC-FACS from Thermus thermophiles and Arabidopsis; This ... |
31-175 |
2.04e-03 |
|
Fatty acyl-CoA synthetases similar to LC-FACS from Thermus thermophiles and Arabidopsis; This family includes fatty acyl-CoA synthetases that can activate medium to long-chain fatty acids. These enzymes catalyze the ATP-dependent acylation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. Fatty acyl-CoA synthetases are responsible for fatty acid degradation as well as physiological regulation of cellular functions via the production of fatty acyl-CoA esters. The fatty acyl-CoA synthetase from Thermus thermophiles in this family has been shown to catalyze the long-chain fatty acid, myristoyl acid. Also included in this family are acyl activating enzymes from Arabidopsis, which contains a large number of proteins from this family with up to 63 different genes, many of which are uncharacterized.
Pssm-ID: 341283 [Multi-domain] Cd Length: 486 Bit Score: 40.75 E-value: 2.04e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178432446 31 VGELYVAGRGVGVGYWRRPGLSASRFvacpfgppgtR--MYRTGDRVRWRADGQLEYLGRTDDQVKIRGYRVELGEIRTA 108
Cdd:cd12118 339 IGEIVFRGNIVMKGYLKNPEATAEAF----------RggWFHSGDLAVIHPDGYIEIKDRSKDIIISGGENISSVEVEGV 408
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1178432446 109 LAELEGVEHAAVIARED-RPGErRLVGYIT----GTADPATVRAELARRLPAHMVPASVMALQaLPLTVNGK 175
Cdd:cd12118 409 LYKHPAVLEAAVVARPDeKWGE-VPCAFVElkegAKVTEEEIIAFCREHLAGFMVPKTVVFGE-LPKTSTGK 478
|
|
| PaaK |
COG1541 |
Phenylacetate-coenzyme A ligase PaaK, adenylate-forming domain family [Coenzyme transport and ... |
69-153 |
2.73e-03 |
|
Phenylacetate-coenzyme A ligase PaaK, adenylate-forming domain family [Coenzyme transport and metabolism];
Pssm-ID: 441150 [Multi-domain] Cd Length: 423 Bit Score: 40.13 E-value: 2.73e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178432446 69 YRTGDRVRWRADG--------QLEY-LGRTDDQVKIRGYRVELGEIRTALAELEGV--EHAAVIAREDRPGERRLVGYIT 137
Cdd:COG1541 297 YRTGDLTRLLPEPcpcgrthpRIGRiLGRADDMLIIRGVNVFPSQIEEVLLRIPEVgpEYQIVVDREGGLDELTVRVELA 376
|
90
....*....|....*.
gi 1178432446 138 GTADPATVRAELARRL 153
Cdd:COG1541 377 PGASLEALAEAIAAAL 392
|
|
| PLN02387 |
PLN02387 |
long-chain-fatty-acid-CoA ligase family protein |
7-109 |
4.51e-03 |
|
long-chain-fatty-acid-CoA ligase family protein
Pssm-ID: 215217 [Multi-domain] Cd Length: 696 Bit Score: 39.71 E-value: 4.51e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178432446 7 IGAPVPGAALVVLD----GWLRPVSAGVVGELYVAGRGVGVGYWRRPGLSASRFvacPFGPPGTRMYRTGDRVRWRADGQ 82
Cdd:PLN02387 474 VGPPLPCCYVKLVSweegGYLISDKPMPRGEIVIGGPSVTLGYFKNQEKTDEVY---KVDERGMRWFYTGDIGQFHPDGC 550
|
90 100
....*....|....*....|....*...
gi 1178432446 83 LEYLGRTDDQVKIR-GYRVELGEIRTAL 109
Cdd:PLN02387 551 LEIIDRKKDIVKLQhGEYVSLGKVEAAL 578
|
|
| |
