|
Name |
Accession |
Description |
Interval |
E-value |
| PLN02736 |
PLN02736 |
long-chain acyl-CoA synthetase |
41-691 |
0e+00 |
|
long-chain acyl-CoA synthetase
Pssm-ID: 178337 [Multi-domain] Cd Length: 651 Bit Score: 1431.04 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327099 41 PFFKEDSYSVVLPEKLDTGKWNVYRSKRSPTKLVSRFPDHPEIGTLHDNFVHAVETYAENKYLGTRVRSDGTIGEYSWMT 120
Cdd:PLN02736 1 EFVHEQGYSVVLPEKLQTGKWNVYRSARSPLKLVSRFPDHPEIGTLHDNFVYAVETFRDYKYLGTRIRVDGTVGEYKWMT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327099 121 YGEAASERQAIGSGLLFHGVNQGDCVGLYFINRPEWLVVDHACAAYSFVSVPLYDTLGPDAVKFVVNHANLQAIFCVPQT 200
Cdd:PLN02736 81 YGEAGTARTAIGSGLVQHGIPKGACVGLYFINRPEWLIVDHACSAYSYVSVPLYDTLGPDAVKFIVNHAEVAAIFCVPQT 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327099 201 LNILLSFLAEIPSIRLIVVVGGADEHLPSLPRGTGVTIVSYQKLLSQGRSSLHPFSPPKPEDIATICYTSGTTGTPKGVV 280
Cdd:PLN02736 161 LNTLLSCLSEIPSVRLIVVVGGADEPLPSLPSGTGVEIVTYSKLLAQGRSSPQPFRPPKPEDVATICYTSGTTGTPKGVV 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327099 281 LTHGNLIANVAGSSVEAEFFPSDVYISYLPLAHIYERANQIMGVYGGVAVGFYQGDVFKLMDDFAVLRPTIFCSVPRLYN 360
Cdd:PLN02736 241 LTHGNLIANVAGSSLSTKFYPSDVHISYLPLAHIYERVNQIVMLHYGVAVGFYQGDNLKLMDDLAALRPTIFCSVPRLYN 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327099 361 RIYDGITSAVKSSGVVKKRLFEIAYNSKKQAIINGRTPSAFWDKLVFNKIKEKLGGRVRFMGSGASPLSPDVMDFLRICF 440
Cdd:PLN02736 321 RIYDGITNAVKESGGLKERLFNAAYNAKKQALENGKNPSPMWDRLVFNKIKAKLGGRVRFMSSGASPLSPDVMEFLRICF 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327099 441 GCSVREGYGMTETSCVISAMDDGDNLSGHVGSPNPACEVKLVDVPEMNYTSDDQPYPRGEICVRGPIIFKGYYKDEEQTR 520
Cdd:PLN02736 401 GGRVLEGYGMTETSCVISGMDEGDNLSGHVGSPNPACEVKLVDVPEMNYTSEDQPYPRGEICVRGPIIFKGYYKDEVQTR 480
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327099 521 EILDGDGWLHTGDIGLWLPGGRLKIIDRKKNIFKLAQGEYIAPEKIENVYTKCRFVSQCFIHGDSFNSSLVAIVSVDPEV 600
Cdd:PLN02736 481 EVIDEDGWLHTGDIGLWLPGGRLKIIDRKKNIFKLAQGEYIAPEKIENVYAKCKFVAQCFVYGDSLNSSLVAVVVVDPEV 560
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327099 601 MKDWAASEGIKYEHLGQLCNDPRVRKTVLAEMDDLGREAQLRGFEFAKAVTLVPEPFTLENGLLTPTFKIKRPQAKAYFA 680
Cdd:PLN02736 561 LKAWAASEGIKYEDLKQLCNDPRVRAAVLADMDAVGREAQLRGFEFAKAVTLVPEPFTVENGLLTPTFKVKRPQAKAYFA 640
|
650
....*....|.
gi 22327099 681 EAISKMYAEIA 691
Cdd:PLN02736 641 KAISDMYAELA 651
|
|
| LC-FACS_euk |
cd05927 |
Eukaryotic long-chain fatty acid CoA synthetase (LC-FACS); The members of this family are ... |
114-688 |
0e+00 |
|
Eukaryotic long-chain fatty acid CoA synthetase (LC-FACS); The members of this family are eukaryotic fatty acid CoA synthetases that activate fatty acids with chain lengths of 12 to 20. LC-FACS catalyzes the formation of fatty acyl-CoA in a two-step reaction: the formation of a fatty acyl-AMP molecule as an intermediate, and the formation of a fatty acyl-CoA. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions. Organisms tend to have multiple isoforms of LC-FACS genes with multiple splice variants. For example, nine genes are found in Arabidopsis and six genes are expressed in mammalian cells.
Pssm-ID: 341250 [Multi-domain] Cd Length: 545 Bit Score: 837.64 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327099 114 GEYSWMTYGEAASERQAIGSGLLFHGVNQ--GDCVGLYFINRPEWLVVDHACAAYSFVSVPLYDTLGPDAVKFVVNHANL 191
Cdd:cd05927 1 GPYEWISYKEVAERADNIGSALRSLGGKPapASFVGIYSINRPEWIISELACYAYSLVTVPLYDTLGPEAIEYILNHAEI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327099 192 QAIFCVPqtlnillsflaeipsirlivvvggadehlpslprgtGVTIVSYQKLLSQGRSSLHPFSPPKPEDIATICYTSG 271
Cdd:cd05927 81 SIVFCDA------------------------------------GVKVYSLEEFEKLGKKNKVPPPPPKPEDLATICYTSG 124
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327099 272 TTGTPKGVVLTHGNLIANVAGSSVEAE----FFPSDVYISYLPLAHIYERANQIMGVYGGVAVGFYQGDVFKLMDDFAVL 347
Cdd:cd05927 125 TTGNPKGVMLTHGNIVSNVAGVFKILEilnkINPTDVYISYLPLAHIFERVVEALFLYHGAKIGFYSGDIRLLLDDIKAL 204
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327099 348 RPTIFCSVPRLYNRIYDGITSAVKSSGVVKKRLFEIAYNSKKQAIING-RTPSAFWDKLVFNKIKEKLGGRVRFMGSGAS 426
Cdd:cd05927 205 KPTVFPGVPRVLNRIYDKIFNKVQAKGPLKRKLFNFALNYKLAELRSGvVRASPFWDKLVFNKIKQALGGNVRLMLTGSA 284
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327099 427 PLSPDVMDFLRICFGCSVREGYGMTETSCVISAMDDGDNLSGHVGSPNPACEVKLVDVPEMNYTSDDqPYPRGEICVRGP 506
Cdd:cd05927 285 PLSPEVLEFLRVALGCPVLEGYGQTECTAGATLTLPGDTSVGHVGGPLPCAEVKLVDVPEMNYDAKD-PNPRGEVCIRGP 363
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327099 507 IIFKGYYKDEEQTREILDGDGWLHTGDIGLWLPGGRLKIIDRKKNIFKLAQGEYIAPEKIENVYTKCRFVSQCFIHGDSF 586
Cdd:cd05927 364 NVFSGYYKDPEKTAEALDEDGWLHTGDIGEWLPNGTLKIIDRKKNIFKLSQGEYVAPEKIENIYARSPFVAQIFVYGDSL 443
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327099 587 NSSLVAIVSVDPEVMKDWAASEGIKYEHLGQLCNDPRVRKTVLAEMDDLGREAQLRGFEFAKAVTLVPEPFTLENGLLTP 666
Cdd:cd05927 444 KSFLVAIVVPDPDVLKEWAASKGGGTGSFEELCKNPEVKKAILEDLVRLGKENGLKGFEQVKAIHLEPEPFSVENGLLTP 523
|
570 580
....*....|....*....|..
gi 22327099 667 TFKIKRPQAKAYFAEAISKMYA 688
Cdd:cd05927 524 TFKLKRPQLKKYYKKQIDEMYK 545
|
|
| FAA1 |
COG1022 |
Long-chain acyl-CoA synthetase (AMP-forming) [Lipid transport and metabolism]; |
75-689 |
0e+00 |
|
Long-chain acyl-CoA synthetase (AMP-forming) [Lipid transport and metabolism];
Pssm-ID: 440645 [Multi-domain] Cd Length: 603 Bit Score: 573.58 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327099 75 SRFPDHPEIGTLHDNFVHAVETYAENKYLGTRVRsdgtiGEYSWMTYGEAASERQAIGSGLLFHGVNQGDCVGLYFINRP 154
Cdd:COG1022 2 SEFSDVPPADTLPDLLRRRAARFPDRVALREKED-----GIWQSLTWAEFAERVRALAAGLLALGVKPGDRVAILSDNRP 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327099 155 EWLVVDHACAAYSFVSVPLYDTLGPDAVKFVVNHANLQAIFCV-PQTLNILLSFLAEIPSIRLIVVVGGADEHLPSlprg 233
Cdd:COG1022 77 EWVIADLAILAAGAVTVPIYPTSSAEEVAYILNDSGAKVLFVEdQEQLDKLLEVRDELPSLRHIVVLDPRGLRDDP---- 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327099 234 tgvTIVSYQKLLSQGRSSLHPF------SPPKPEDIATICYTSGTTGTPKGVVLTHGNLIANVAGSSVEAEFFPSDVYIS 307
Cdd:COG1022 153 ---RLLSLDELLALGREVADPAelearrAAVKPDDLATIIYTSGTTGRPKGVMLTHRNLLSNARALLERLPLGPGDRTLS 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327099 308 YLPLAHIYERANQIMGVYGGVAVGfYQGDVFKLMDDFAVLRPTIFCSVPRLYNRIYDGITSAVKSSGVVKKRLFEIAYN- 386
Cdd:COG1022 230 FLPLAHVFERTVSYYALAAGATVA-FAESPDTLAEDLREVKPTFMLAVPRVWEKVYAGIQAKAEEAGGLKRKLFRWALAv 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327099 387 --SKKQAIINGRTPS-------AFWDKLVFNKIKEKLGGRVRFMGSGASPLSPDVMDFLRIcFGCSVREGYGMTETSCVI 457
Cdd:COG1022 309 grRYARARLAGKSPSlllrlkhALADKLVFSKLREALGGRLRFAVSGGAALGPELARFFRA-LGIPVLEGYGLTETSPVI 387
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327099 458 SAMDDGDNLSGHVGSPNPACEVKLvdvpemnytSDDqpyprGEICVRGPIIFKGYYKDEEQTREILDGDGWLHTGDIGLW 537
Cdd:COG1022 388 TVNRPGDNRIGTVGPPLPGVEVKI---------AED-----GEILVRGPNVMKGYYKNPEATAEAFDADGWLHTGDIGEL 453
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327099 538 LPGGRLKIIDRKKNIFKLAQGEYIAPEKIENVYTKCRFVSQCFIHGDS--FnssLVAIVSVDPEVMKDWAASEGIKYEHL 615
Cdd:COG1022 454 DEDGFLRITGRKKDLIVTSGGKNVAPQPIENALKASPLIEQAVVVGDGrpF---LAALIVPDFEALGEWAEENGLPYTSY 530
|
570 580 590 600 610 620 630
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 22327099 616 GQLCNDPRVRKTVLAEMDDLgrEAQLRGFEFAKAVTLVPEPFTLENGLLTPTFKIKRPQAKAYFAEAISKMYAE 689
Cdd:COG1022 531 AELAQDPEVRALIQEEVDRA--NAGLSRAEQIKRFRLLPKEFTIENGELTPTLKLKRKVILEKYADLIEALYAG 602
|
|
| PLN02861 |
PLN02861 |
long-chain-fatty-acid-CoA ligase |
63-689 |
0e+00 |
|
long-chain-fatty-acid-CoA ligase
Pssm-ID: 178452 [Multi-domain] Cd Length: 660 Bit Score: 545.59 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327099 63 VYRSKRSPTKLVsrfpDHP-EIGTLHDNFVHAVETYAENKYLGTRVRSDGTIGEYSWMTYGEAASERQAIGSGLLFHGVN 141
Cdd:PLN02861 25 VYRSIYAKDGLL----DLPaDIDSPWQFFSDAVKKYPNNQMLGRRQVTDSKVGPYVWLTYKEVYDAAIRIGSAIRSRGVN 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327099 142 QGDCVGLYFINRPEWLVVDHACAAYSFVSVPLYDTLGPDAVKFVVNHANLQAIFCVPQTLNILLSFLAEIPS-IRLIVVV 220
Cdd:PLN02861 101 PGDRCGIYGSNCPEWIIAMEACNSQGITYVPLYDTLGANAVEFIINHAEVSIAFVQESKISSILSCLPKCSSnLKTIVSF 180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327099 221 GGADEHLPSLPRGTGVTIVSYQKLLSQGrsSLHPFSPPK-PEDIATICYTSGTTGTPKGVVLTHGNLIANVAgsSVEAEF 299
Cdd:PLN02861 181 GDVSSEQKEEAEELGVSCFSWEEFSLMG--SLDCELPPKqKTDICTIMYTSGTTGEPKGVILTNRAIIAEVL--STDHLL 256
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327099 300 F-------PSDVYISYLPLAHIYERANQIMGVYGGVAVGFYQGDVFKLMDDFAVLRPTIFCSVPRLYNRIYDGITSAVKS 372
Cdd:PLN02861 257 KvtdrvatEEDSYFSYLPLAHVYDQVIETYCISKGASIGFWQGDIRYLMEDVQALKPTIFCGVPRVYDRIYTGIMQKISS 336
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327099 373 SGVVKKRLFEIAYNSKKQAIING---RTPSAFWDKLVFNKIKEKLGGRVRFMGSGASPLSPDVMDFLRICFGCSVREGYG 449
Cdd:PLN02861 337 GGMLRKKLFDFAYNYKLGNLRKGlkqEEASPRLDRLVFDKIKEGLGGRVRLLLSGAAPLPRHVEEFLRVTSCSVLSQGYG 416
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327099 450 MTEtSCVISAMDDGDNLS--GHVGSPNPACEVKLVDVPEMNYTSDDQpYPRGEICVRGPIIFKGYYKDEEQTREILDgDG 527
Cdd:PLN02861 417 LTE-SCGGCFTSIANVFSmvGTVGVPMTTIEARLESVPEMGYDALSD-VPRGEICLRGNTLFSGYHKRQDLTEEVLI-DG 493
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327099 528 WLHTGDIGLWLPGGRLKIIDRKKNIFKLAQGEYIAPEKIENVYTKCRFVSQCFIHGDSFNSSLVAIVSVDPEVMKDWAAS 607
Cdd:PLN02861 494 WFHTGDIGEWQPNGAMKIIDRKKNIFKLSQGEYVAVENLENTYSRCPLIASIWVYGNSFESFLVAVVVPDRQALEDWAAN 573
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327099 608 EGiKYEHLGQLCNDPRVRKTVLAEMDDLGREAQLRGFEFAKAVTLVPEPFTLENGLLTPTFKIKRPQAKAYFAEAISKMY 687
Cdd:PLN02861 574 NN-KTGDFKSLCKNLKARKYILDELNSTGKKLQLRGFEMLKAIHLEPNPFDIERDLITPTFKLKRPQLLKYYKDCIDQLY 652
|
..
gi 22327099 688 AE 689
Cdd:PLN02861 653 SE 654
|
|
| LC_FACS_euk1 |
cd17639 |
Eukaryotic long-chain fatty acid CoA synthetase (LC-FACS), including fungal proteins; The ... |
114-672 |
7.60e-180 |
|
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: 521.78 E-value: 7.60e-180
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327099 114 GEYSWMTYGEAASERQAIGSGLLFHGVNQGDCVGLYFINRPEWLVVDHACAAYSFVSVPLYDTLGPDAVKFVVNHANLQA 193
Cdd:cd17639 1 GEYKYMSYAEVWERVLNFGRGLVELGLKPGDKVAIFAETRAEWLITALGCWSQNIPIVTVYATLGEDALIHSLNETECSA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327099 194 IFCVPqtlnillsflaeipsirlivvvggadehlpslprgtgvtivsyqkllsqgrsslhpfsppKPEDIATICYTSGTT 273
Cdd:cd17639 81 IFTDG------------------------------------------------------------KPDDLACIMYTSGST 100
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327099 274 GTPKGVVLTHGNLIANVAGSS--VEAEFFPSDVYISYLPLAHIYERANQIMGVYGGVAVGFyqGDVFKLMD--------D 343
Cdd:cd17639 101 GNPKGVMLTHGNLVAGIAGLGdrVPELLGPDDRYLAYLPLAHIFELAAENVCLYRGGTIGY--GSPRTLTDkskrgckgD 178
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327099 344 FAVLRPTIFCSVPRLYNRIYDGITSAVKSSGVVKKRLFEIAYNSKKQAIINGRTpSAFWDKLVFNKIKEKLGGRVRFMGS 423
Cdd:cd17639 179 LTEFKPTLMVGVPAIWDTIRKGVLAKLNPMGGLKRTLFWTAYQSKLKALKEGPG-TPLLDELVFKKVRAALGGRLRYMLS 257
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327099 424 GASPLSPDVMDFLRICFgCSVREGYGMTETSCVISAMDDGDNLSGHVGSPNPACEVKLVDVPEMNYTSDdQPYPRGEICV 503
Cdd:cd17639 258 GGAPLSADTQEFLNIVL-CPVIQGYGLTETCAGGTVQDPGDLETGRVGPPLPCCEIKLVDWEEGGYSTD-KPPPRGEILI 335
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327099 504 RGPIIFKGYYKDEEQTREILDGDGWLHTGDIGLWLPGGRLKIIDRKKNIFKLAQGEYIAPEKIENVYTKCRFVSQCFIHG 583
Cdd:cd17639 336 RGPNVFKGYYKNPEKTKEAFDGDGWFHTGDIGEFHPDGTLKIIDRKKDLVKLQNGEYIALEKLESIYRSNPLVNNICVYA 415
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327099 584 DSFNSSLVAIVSVDPEVMKDWAASEGIKYEHLGQLCNDPRVRKTVLAEMDDLGREAQLRGFEFAKAVTLVPEPFTLENGL 663
Cdd:cd17639 416 DPDKSYPVAIVVPNEKHLTKLAEKHGVINSEWEELCEDKKLQKAVLKSLAETARAAGLEKFEIPQGVVLLDEEWTPENGL 495
|
....*....
gi 22327099 664 LTPTFKIKR 672
Cdd:cd17639 496 VTAAQKLKR 504
|
|
| PLN02430 |
PLN02430 |
long-chain-fatty-acid-CoA ligase |
63-692 |
1.24e-178 |
|
long-chain-fatty-acid-CoA ligase
Pssm-ID: 178049 [Multi-domain] Cd Length: 660 Bit Score: 524.38 E-value: 1.24e-178
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327099 63 VYRSKRSPtklvSRFPD-HPEIGTLHDNFVHAVETYAENKYLGTRVRSDGTIGEYSWMTYGEAASERQAIGSGLLFHGVN 141
Cdd:PLN02430 24 VYRNLLSK----KGFPPiDSDITTAWDIFSKSVEKYPDNKMLGWRRIVDGKVGPYMWKTYKEVYEEVLQIGSALRASGAE 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327099 142 QGDCVGLYFINRPEWLVVDHACAAYSFVSVPLYDTLGPDAVKFVVNHANLQAIFCVPQTLNILLSF-LAEIPSIRLIVVV 220
Cdd:PLN02430 100 PGSRVGIYGSNCPQWIVAMEACAAHSLICVPLYDTLGPGAVDYIVDHAEIDFVFVQDKKIKELLEPdCKSAKRLKAIVSF 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327099 221 GGADEHLPSLPRGTGVTIVSYQKLLSQGRSSLHPFSPPKPEDIATICYTSGTTGTPKGVVLTHGNLIANVAGSSVEAEFF 300
Cdd:PLN02430 180 TSVTEEESDKASQIGVKTYSWIDFLHMGKENPSETNPPKPLDICTIMYTSGTSGDPKGVVLTHEAVATFVRGVDLFMEQF 259
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327099 301 P-----SDVYISYLPLAHIYERANQIMGVYGGVAVGFYQGDVFKLMDDFAVLRPTIFCSVPRLYNRIYDGITSAVKSSGV 375
Cdd:PLN02430 260 EdkmthDDVYLSFLPLAHILDRMIEEYFFRKGASVGYYHGDLNALRDDLMELKPTLLAGVPRVFERIHEGIQKALQELNP 339
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327099 376 VKKRLFEIAYNSKKQAIING---RTPSAFWDKLVFNKIKEKLGGRVRFMGSGASPLSPDVMDFLRICFGCSVREGYGMTE 452
Cdd:PLN02430 340 RRRLIFNALYKYKLAWMNRGyshKKASPMADFLAFRKVKAKLGGRLRLLISGGAPLSTEIEEFLRVTSCAFVVQGYGLTE 419
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327099 453 TsCVISAMDDGDNLS--GHVGSPNPACEVKLVDVPEMNYTSDDQPyPRGEICVRGPIIFKGYYKDEEQTREILDgDGWLH 530
Cdd:PLN02430 420 T-LGPTTLGFPDEMCmlGTVGAPAVYNELRLEEVPEMGYDPLGEP-PRGEICVRGKCLFSGYYKNPELTEEVMK-DGWFH 496
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327099 531 TGDIGLWLPGGRLKIIDRKKNIFKLAQGEYIAPEKIENVYTKCRFVSQCFIHGDSFNSSLVAIVSVDPEVMKDWAASEGI 610
Cdd:PLN02430 497 TGDIGEILPNGVLKIIDRKKNLIKLSQGEYVALEYLENVYGQNPIVEDIWVYGDSFKSMLVAVVVPNEENTNKWAKDNGF 576
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327099 611 KyEHLGQLCNDPRVRKTVLAEMDDLGREAQLRGFEFAKAVTLVPEPFTLENGLLTPTFKIKRPQAKAYFAEAISKMYAEI 690
Cdd:PLN02430 577 T-GSFEELCSLPELKEHILSELKSTAEKNKLRGFEYIKGVILETKPFDVERDLVTATLKKRRNNLLKYYQVEIDEMYRKL 655
|
..
gi 22327099 691 AA 692
Cdd:PLN02430 656 AE 657
|
|
| PLN02614 |
PLN02614 |
long-chain acyl-CoA synthetase |
63-693 |
5.17e-175 |
|
long-chain acyl-CoA synthetase
Pssm-ID: 166255 [Multi-domain] Cd Length: 666 Bit Score: 515.34 E-value: 5.17e-175
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327099 63 VYRSkrspTKLVSRFPDHPE-IGTLHDNFVHAVETYAENKYLGTRVRSDGTIGEYSWMTYGEAASERQAIGSGLLFHGVN 141
Cdd:PLN02614 27 VYRS----IFAKDGFPNPIEgMDSCWDVFRMSVEKYPNNPMLGRREIVDGKPGKYVWQTYQEVYDIVIKLGNSLRSVGVK 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327099 142 QGDCVGLYFINRPEWLVVDHACAAYSFVSVPLYDTLGPDAVKFVVNHANLQAIFCVPQTLNILLSFLA-EIPSIRLIVVV 220
Cdd:PLN02614 103 DEAKCGIYGANSPEWIISMEACNAHGLYCVPLYDTLGAGAVEFIISHSEVSIVFVEEKKISELFKTCPnSTEYMKTVVSF 182
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327099 221 GGADEHLPSLPRGTGVTIVSYQKLLSQGRSSLHPFSPPKPEDIATICYTSGTTGTPKGVVLTHGNLIANVAG-----SSV 295
Cdd:PLN02614 183 GGVSREQKEEAETFGLVIYAWDEFLKLGEGKQYDLPIKKKSDICTIMYTSGTTGDPKGVMISNESIVTLIAGvirllKSA 262
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327099 296 EAEFFPSDVYISYLPLAHIYERANQIMGVYGGVAVGFYQGDVFKLMDDFAVLRPTIFCSVPRLYNRIYDGITSAVKSSGV 375
Cdd:PLN02614 263 NAALTVKDVYLSYLPLAHIFDRVIEECFIQHGAAIGFWRGDVKLLIEDLGELKPTIFCAVPRVLDRVYSGLQKKLSDGGF 342
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327099 376 VKKRLFEIAYNSKKQAIINGRT---PSAFWDKLVFNKIKEKLGGRVRFMGSGASPLSPDVMDFLRICFGCSVREGYGMTE 452
Cdd:PLN02614 343 LKKFVFDSAFSYKFGNMKKGQShveASPLCDKLVFNKVKQGLGGNVRIILSGAAPLASHVESFLRVVACCHVLQGYGLTE 422
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327099 453 tSC--VISAMDDGDNLSGHVGSPNPACEVKLVDVPEMNYTSDDQPyPRGEICVRGPIIFKGYYKDEEQTREILDgDGWLH 530
Cdd:PLN02614 423 -SCagTFVSLPDELDMLGTVGPPVPNVDIRLESVPEMEYDALAST-PRGEICIRGKTLFSGYYKREDLTKEVLI-DGWLH 499
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327099 531 TGDIGLWLPGGRLKIIDRKKNIFKLAQGEYIAPEKIENVYTKCRFVSQCFIHGDSFNSSLVAIVSVDPEVMKDWAASEGI 610
Cdd:PLN02614 500 TGDVGEWQPNGSMKIIDRKKNIFKLSQGEYVAVENIENIYGEVQAVDSVWVYGNSFESFLVAIANPNQQILERWAAENGV 579
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327099 611 KYEHlGQLCNDPRVRKTVLAEMDDLGREAQLRGFEFAKAVTLVPEPFTLENGLLTPTFKIKRPQAKAYFAEAISKMYAEI 690
Cdd:PLN02614 580 SGDY-NALCQNEKAKEFILGELVKMAKEKKMKGFEIIKAIHLDPVPFDMERDLLTPTFKKKRPQLLKYYQSVIDEMYKTT 658
|
...
gi 22327099 691 AAS 693
Cdd:PLN02614 659 NEK 661
|
|
| PLN02387 |
PLN02387 |
long-chain-fatty-acid-CoA ligase family protein |
75-688 |
1.69e-161 |
|
long-chain-fatty-acid-CoA ligase family protein
Pssm-ID: 215217 [Multi-domain] Cd Length: 696 Bit Score: 481.54 E-value: 1.69e-161
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327099 75 SRFPDHPE-----IGTLHDNFVHAVETYAENKYLGTR--------VRSDG------TIGEYSWMTYGEAASERQAIGSGL 135
Cdd:PLN02387 44 ARFPELVEtpwegATTLAALFEQSCKKYSDKRLLGTRklisrefeTSSDGrkfeklHLGEYEWITYGQVFERVCNFASGL 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327099 136 LFHGVNQGDCVGLYFINRPEWLVVDHACAAYSFVSVPLYDTLGPDAVKFVVNHANLQAIFCVPQTLNILLSFLAEIPSI- 214
Cdd:PLN02387 124 VALGHNKEERVAIFADTRAEWLIALQGCFRQNITVVTIYASLGEEALCHSLNETEVTTVICDSKQLKKLIDISSQLETVk 203
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327099 215 RLIVVVGGADEHLPSLPRGTGVTIVSYQKLLSQGRSSLHPFSPPKPEDIATICYTSGTTGTPKGVVLTHGNLIANVAG-S 293
Cdd:PLN02387 204 RVIYMDDEGVDSDSSLSGSSNWTVSSFSEVEKLGKENPVDPDLPSPNDIAVIMYTSGSTGLPKGVMMTHGNIVATVAGvM 283
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327099 294 SVEAEFFPSDVYISYLPLAHIYERANQIMGVYGGVAVGFyqGDVFKLMD-----------DFAVLRPTIFCSVPRLYNRI 362
Cdd:PLN02387 284 TVVPKLGKNDVYLAYLPLAHILELAAESVMAAVGAAIGY--GSPLTLTDtsnkikkgtkgDASALKPTLMTAVPAILDRV 361
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327099 363 YDGITSAVKSSGVVKKRLFEIAYNsKKQAIINGRTPSA------FWDKLVFNKIKEKLGGRVRFMGSGASPLSPDVMDFL 436
Cdd:PLN02387 362 RDGVRKKVDAKGGLAKKLFDIAYK-RRLAAIEGSWFGAwgleklLWDALVFKKIRAVLGGRIRFMLSGGAPLSGDTQRFI 440
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327099 437 RICFGCSVREGYGMTETsCVISAMDDGDNLS-GHVGSPNPACEVKLVDVPEMNYTSDDQPYPRGEICVRGPIIFKGYYKD 515
Cdd:PLN02387 441 NICLGAPIGQGYGLTET-CAGATFSEWDDTSvGRVGPPLPCCYVKLVSWEEGGYLISDKPMPRGEIVIGGPSVTLGYFKN 519
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327099 516 EEQTREI--LDGDG--WLHTGDIGLWLPGGRLKIIDRKKNIFKLAQGEYIAPEKIENVYTKCRFVSQCFIHGDSFNSSLV 591
Cdd:PLN02387 520 QEKTDEVykVDERGmrWFYTGDIGQFHPDGCLEIIDRKKDIVKLQHGEYVSLGKVEAALSVSPYVDNIMVHADPFHSYCV 599
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327099 592 AIVSVDPEVMKDWAASEGIKYEHLGQLCNDPRVRKTVLAEMDDLGREAQLRGFEFAKAVTLVPEPFTLENGLLTPTFKIK 671
Cdd:PLN02387 600 ALVVPSQQALEKWAKKAGIDYSNFAELCEKEEAVKEVQQSLSKAAKAARLEKFEIPAKIKLLPEPWTPESGLVTAALKLK 679
|
650
....*....|....*..
gi 22327099 672 RPQAKAYFAEAISKMYA 688
Cdd:PLN02387 680 REQIRKKFKDDLKKLYE 696
|
|
| VL_LC_FACS_like |
cd05907 |
Long-chain fatty acid CoA synthetases and Bubblegum-like very long-chain fatty acid CoA ... |
114-674 |
1.46e-156 |
|
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: 460.14 E-value: 1.46e-156
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327099 114 GEYSWMTYGEAASERQAIGSGLLFHGVNQGDCVGLYFINRPEWLVVDHACAAYSFVSVPLYDTLGPDAVKFVVNHANLQA 193
Cdd:cd05907 1 GVWQPITWAEFAEEVRALAKGLIALGVEPGDRVAILSRNRPEWTIADLAILAIGAVPVPIYPTSSAEQIAYILNDSEAKA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327099 194 IFCvpqtlnillsflaeipsirlivvvggadehlpslprgtgvtivsyqkllsqgrsslhpfspPKPEDIATICYTSGTT 273
Cdd:cd05907 81 LFV-------------------------------------------------------------EDPDDLATIIYTSGTT 99
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327099 274 GTPKGVVLTHGNLIANVAGSSVEAEFFPSDVYISYLPLAHIYERanqIMGVYG----GVAVGFYQGDVfKLMDDFAVLRP 349
Cdd:cd05907 100 GRPKGVMLSHRNILSNALALAERLPATEGDRHLSFLPLAHVFER---RAGLYVpllaGARIYFASSAE-TLLDDLSEVRP 175
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327099 350 TIFCSVPRLYNRIYDGItsAVKSSGVVKKRLFEIAYnskkqaiingrtpsafwdklvfnkikeklGGRVRFMGSGASPLS 429
Cdd:cd05907 176 TVFLAVPRVWEKVYAAI--KVKAVPGLKRKLFDLAV-----------------------------GGRLRFAASGGAPLP 224
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327099 430 PDVMDFLRIcFGCSVREGYGMTETSCVISAMDDGDNLSGHVGSPNPACEVKLVDvpemnytsddqpypRGEICVRGPIIF 509
Cdd:cd05907 225 AELLHFFRA-LGIPVYEGYGLTETSAVVTLNPPGDNRIGTVGKPLPGVEVRIAD--------------DGEILVRGPNVM 289
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327099 510 KGYYKDEEQTREILDGDGWLHTGDIGLWLPGGRLKIIDRKKNIFKLAQGEYIAPEKIENVYTKCRFVSQCFIHGDSfNSS 589
Cdd:cd05907 290 LGYYKNPEATAEALDADGWLHTGDLGEIDEDGFLHITGRKKDLIITSGGKNISPEPIENALKASPLISQAVVIGDG-RPF 368
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327099 590 LVAIVSVDPEVMKDWAASEGIKYEHLGQLCNDPRVRKTVLAEMDDLGreAQLRGFEFAKAVTLVPEPFTLENGLLTPTFK 669
Cdd:cd05907 369 LVALIVPDPEALEAWAEEHGIAYTDVAELAANPAVRAEIEAAVEAAN--ARLSRYEQIKKFLLLPEPFTIENGELTPTLK 446
|
....*
gi 22327099 670 IKRPQ 674
Cdd:cd05907 447 LKRPV 451
|
|
| PTZ00216 |
PTZ00216 |
acyl-CoA synthetase; Provisional |
119-689 |
8.69e-134 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 240316 [Multi-domain] Cd Length: 700 Bit Score: 410.52 E-value: 8.69e-134
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327099 119 MTYGEAASERQAIGSGLLFHGVNQGDCVGLYFINRPEWLVVDHACAAYSFVSVPLYDTLGPDAVKFVVNHANLQAIFCVP 198
Cdd:PTZ00216 122 ITYAELWERIVNFGRGLAELGLTKGSNVAIYEETRWEWLASIYGIWSQSMVAATVYANLGEDALAYALRETECKAIVCNG 201
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327099 199 QTLNILLSFL--AEIPSIRLIvvvggadeHLPSLPRGT---GVTIVSYQKLLSQGRSSLHPFSPPKPE---DIATICYTS 270
Cdd:PTZ00216 202 KNVPNLLRLMksGGMPNTTII--------YLDSLPASVdteGCRLVAWTDVVAKGHSAGSHHPLNIPEnndDLALIMYTS 273
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327099 271 GTTGTPKGVVLTHGNLIANVAG-----SSVEAEFFPSDVYISYLPLAHIYERANQIMGVYGGVAVGFyqGDVFKLMDDFA 345
Cdd:PTZ00216 274 GTTGDPKGVMHTHGSLTAGILAledrlNDLIGPPEEDETYCSYLPLAHIMEFGVTNIFLARGALIGF--GSPRTLTDTFA 351
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327099 346 -------VLRPTIFCSVPRlynrIYDGITSAVKSS----GVVKKRLFEIAYNSKKQAIINGR-TPsaFWDKLVFNKIKEK 413
Cdd:PTZ00216 352 rphgdltEFRPVFLIGVPR----IFDTIKKAVEAKlppvGSLKRRVFDHAYQSRLRALKEGKdTP--YWNEKVFSAPRAV 425
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327099 414 LGGRVRFMGSGASPLSPDVMDFLRICFGCsVREGYGMTETSCVISAMDDGDNLSGHVGSPNPACEVKLVDVPEMNYTsdD 493
Cdd:PTZ00216 426 LGGRVRAMLSGGGPLSAATQEFVNVVFGM-VIQGWGLTETVCCGGIQRTGDLEPNAVGQLLKGVEMKLLDTEEYKHT--D 502
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327099 494 QPYPRGEICVRGPIIFKGYYKDEEQTREILDGDGWLHTGDIGLWLPGGRLKIIDRKKNIFKLAQGEYIAPEKIENVYTKC 573
Cdd:PTZ00216 503 TPEPRGEILLRGPFLFKGYYKQEELTREVLDEDGWFHTGDVGSIAANGTLRIIGRVKALAKNCLGEYIALEALEALYGQN 582
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327099 574 RFVSQ---C-FIHGDsfNSSLVAIVSVDPEVMKDWAASEGIKYEhLGQLCNDPRVRKTVLAEMDDLGREAQLRGFEFAKA 649
Cdd:PTZ00216 583 ELVVPngvCvLVHPA--RSYICALVLTDEAKAMAFAKEHGIEGE-YPAILKDPEFQKKATESLQETARAAGRKSFEIVRH 659
|
570 580 590 600
....*....|....*....|....*....|....*....|
gi 22327099 650 VTLVPEPFTLENGLLTPTFKIKRPQAKAYFAEAISKMYAE 689
Cdd:PTZ00216 660 VRVLSDEWTPENGVLTAAMKLKRRVIDERYADLIKELFAD 699
|
|
| AMP-binding |
pfam00501 |
AMP-binding enzyme; |
113-556 |
1.87e-118 |
|
AMP-binding enzyme;
Pssm-ID: 459834 [Multi-domain] Cd Length: 417 Bit Score: 360.86 E-value: 1.87e-118
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327099 113 IGEYSWMTYGEAASERQAIGSGLLFHGVNQGDCVGLYFINRPEWLVVDHACAAYSFVSVPLYDTLGPDAVKFVVNHANLQ 192
Cdd:pfam00501 16 VGEGRRLTYRELDERANRLAAGLRALGVGKGDRVAILLPNSPEWVVAFLACLKAGAVYVPLNPRLPAEELAYILEDSGAK 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327099 193 AIFCVP-QTLNILLSFLAEIPSIRLIVVVGGADEHLPSLPRGTGVTIvsyqkllsqgRSSLHPFSPPKPEDIATICYTSG 271
Cdd:pfam00501 96 VLITDDaLKLEELLEALGKLEVVKLVLVLDRDPVLKEEPLPEEAKPA----------DVPPPPPPPPDPDDLAYIIYTSG 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327099 272 TTGTPKGVVLTHGNLIANVAGSSVEAE----FFPSDVYISYLPLAHIYERANQIMG-VYGGVAVGFYQG----DVFKLMD 342
Cdd:pfam00501 166 TTGKPKGVMLTHRNLVANVLSIKRVRPrgfgLGPDDRVLSTLPLFHDFGLSLGLLGpLLAGATVVLPPGfpalDPAALLE 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327099 343 DFAVLRPTIFCSVPRLYNRIYDgitsavksSGVVKKRLFeiaynskkqaiingrtpsafwdklvfnkikeklgGRVRFMG 422
Cdd:pfam00501 246 LIERYKVTVLYGVPTLLNMLLE--------AGAPKRALL----------------------------------SSLRLVL 283
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327099 423 SGASPLSPDVMDFLRICFGCSVREGYGMTETSCVISAMDDGD---NLSGHVGSPNPACEVKLVDVPEMNYTSDDQPyprG 499
Cdd:pfam00501 284 SGGAPLPPELARRFRELFGGALVNGYGLTETTGVVTTPLPLDedlRSLGSVGRPLPGTEVKIVDDETGEPVPPGEP---G 360
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*..
gi 22327099 500 EICVRGPIIFKGYYKDEEQTREILDGDGWLHTGDIGLWLPGGRLKIIDRKKNIFKLA 556
Cdd:pfam00501 361 ELCVRGPGVMKGYLNDPELTAEAFDEDGWYRTGDLGRRDEDGYLEIVGRKKDQIKLG 417
|
|
| LC_FACS_bac |
cd05932 |
Bacterial long-chain fatty acid CoA synthetase (LC-FACS), including Marinobacter ... |
110-672 |
6.40e-90 |
|
Bacterial long-chain fatty acid CoA synthetase (LC-FACS), including Marinobacter hydrocarbonoclasticus isoprenoid Coenzyme A synthetase; The members of this family are bacterial long-chain fatty acid CoA synthetase. Marinobacter hydrocarbonoclasticus isoprenoid Coenzyme A synthetase in this family is involved in the synthesis of isoprenoid wax ester storage compounds when grown on phytol as the sole carbon source. LC-FACS catalyzes the formation of fatty acyl-CoA in a two-step reaction: the formation of a fatty acyl-AMP molecule as an intermediate, and the formation of a fatty acyl-CoA. Free fatty acids must be "activated" to their CoA thioesters before participating in most catabolic and anabolic reactions.
Pssm-ID: 341255 [Multi-domain] Cd Length: 508 Bit Score: 290.14 E-value: 6.40e-90
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327099 110 DGTIGEYSWmtyGEAASERQAIGSGLLFHGVNQGDCVGLYFINRPEWLVVDHACAAYSFVSVPLYDTLGPDAVKFVVNHA 189
Cdd:cd05932 1 GGQVVEFTW---GEVADKARRLAAALRALGLEPGSKIALISKNCAEWFITDLAIWMAGHISVPLYPTLNPDTIRYVLEHS 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327099 190 NLQAIFcvpqtlnilLSFLAEIPSIRliVVVGGADEHLPSLPRGTGVTIVSYQKLLSQGrSSLHPFSPPKPEDIATICYT 269
Cdd:cd05932 78 ESKALF---------VGKLDDWKAMA--PGVPEGLISISLPPPSAANCQYQWDDLIAQH-PPLEERPTRFPEQLATLIYT 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327099 270 SGTTGTPKGVVLTHGNLIANVAGSSVEAEFFPSDVYISYLPLAHIYERANQIMG-VYGGVAVGFYQG-DVFklMDDFAVL 347
Cdd:cd05932 146 SGTTGQPKGVMLTFGSFAWAAQAGIEHIGTEENDRMLSYLPLAHVTERVFVEGGsLYGGVLVAFAESlDTF--VEDVQRA 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327099 348 RPTIFCSVPRLYNRIYDGITSAVKSSGVvkKRLFEIAynskkqaIINgrtpsafwdKLVFNKIKEKLG-GRVRFMGSGAS 426
Cdd:cd05932 224 RPTLFFSVPRLWTKFQQGVQDKIPQQKL--NLLLKIP-------VVN---------SLVKRKVLKGLGlDQCRLAGCGSA 285
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327099 427 PLSPDVMDFLRiCFGCSVREGYGMTEtSCVISAMD-DGDNLSGHVGSPNPACEVKLvdvpemnytSDDqpyprGEICVRG 505
Cdd:cd05932 286 PVPPALLEWYR-SLGLNILEAYGMTE-NFAYSHLNyPGRDKIGTVGNAGPGVEVRI---------SED-----GEILVRS 349
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327099 506 PIIFKGYYKDEEQTREILDGDGWLHTGDIGLWLPGGRLKIIDRKKNIFKLAQGEYIAPEKIENVYTKCRFVSQCFIHGDS 585
Cdd:cd05932 350 PALMMGYYKDPEATAEAFTADGFLRTGDKGELDADGNLTITGRVKDIFKTSKGKYVAPAPIENKLAEHDRVEMVCVIGSG 429
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327099 586 FNSSL-VAIVSVDPEVMKDWAASEgikyehlgqlcndpRVRKTVLAEMDDLgrEAQLRGFEFAKAVTLVPEPFTLENGLL 664
Cdd:cd05932 430 LPAPLaLVVLSEEARLRADAFARA--------------ELEASLRAHLARV--NSTLDSHEQLAGIVVVKDPWSIDNGIL 493
|
....*...
gi 22327099 665 TPTFKIKR 672
Cdd:cd05932 494 TPTLKIKR 501
|
|
| LC_FACS_like |
cd17640 |
Long-chain fatty acid CoA synthetase; This family includes long-chain fatty acid (C12-C20) CoA ... |
116-673 |
9.14e-86 |
|
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: 277.70 E-value: 9.14e-86
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327099 116 YSWMTYGEAASERQAIGSGLLFHGVNQGDCVGLYFINRPEWLVVDHACAAYSFVSVPLYDTLGPDAVKFVVNHANLQAIF 195
Cdd:cd17640 3 PKRITYKDLYQEILDFAAGLRSLGVKAGEKVALFADNSPRWLIADQGIMALGAVDVVRGSDSSVEELLYILNHSESVALV 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327099 196 cvpqtlnillsflaeipsirlivvvggADEHlpslprgtgvtivsyqkllsqgrsslhpfsppkPEDIATICYTSGTTGT 275
Cdd:cd17640 83 ---------------------------VEND---------------------------------SDDLATIIYTSGTTGN 102
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327099 276 PKGVVLTHGNLIANVAGSSVEAEFFPSDVYISYLPLAHIYERANQIMGVYGGVAVGFYQGDVFKlmDDFAVLRPTIFCSV 355
Cdd:cd17640 103 PKGVMLTHANLLHQIRSLSDIVPPQPGDRFLSILPIWHSYERSAEYFIFACGCSQAYTSIRTLK--DDLKRVKPHYIVSV 180
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327099 356 PRLYNRIYDGITSAVKSSGVVKKRLFEIAynskkqaiingrtpsafwdklvfnkikeKLGGRVRFMGSGASPLSPDVMDF 435
Cdd:cd17640 181 PRLWESLYSGIQKQVSKSSPIKQFLFLFF----------------------------LSGGIFKFGISGGGALPPHVDTF 232
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327099 436 LRIcFGCSVREGYGMTETSCVISAMDDGDNLSGHVGSPNPACEVKLVDVPEMNYTsddqPYP-RGEICVRGPIIFKGYYK 514
Cdd:cd17640 233 FEA-IGIEVLNGYGLTETSPVVSARRLKCNVRGSVGRPLPGTEIKIVDPEGNVVL----PPGeKGIVWVRGPQVMKGYYK 307
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327099 515 DEEQTREILDGDGWLHTGDIGLWLPGGRLKIIDRKKNIFKLAQGEYIAPEKIENVYTKCRFVSQCFIHGDSfNSSLVAIV 594
Cdd:cd17640 308 NPEATSKVLDSDGWFNTGDLGWLTCGGELVLTGRAKDTIVLSNGENVEPQPIEEALMRSPFIEQIMVVGQD-QKRLGALI 386
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327099 595 SVDPEVMKDWAASEGIKY-EHLGQLCNDPRVRKTVLAE-MDDLGREAQLRGFEFAKAVTLVPEPFTlENGLLTPTFKIKR 672
Cdd:cd17640 387 VPNFEELEKWAKESGVKLaNDRSQLLASKKVLKLYKNEiKDEISNRPGFKSFEQIAPFALLEEPFI-ENGEMTQTMKIKR 465
|
.
gi 22327099 673 P 673
Cdd:cd17640 466 N 466
|
|
| LC_FACS_bac1 |
cd17641 |
bacterial long-chain fatty acid CoA synthetase; The members of this family are bacterial ... |
120-672 |
8.99e-82 |
|
bacterial long-chain fatty acid CoA synthetase; The members of this family are bacterial long-chain fatty acid CoA synthetase, most of which are as yet uncharacterized. LC-FACS catalyzes the formation of fatty acyl-CoA in a two-step reaction: the formation of a fatty acyl-AMP molecule as an intermediate, and the formation of a fatty acyl-CoA. Free fatty acids must be "activated" to their CoA thioesters before participating in most catabolic and anabolic reactions.
Pssm-ID: 341296 [Multi-domain] Cd Length: 569 Bit Score: 270.45 E-value: 8.99e-82
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327099 120 TYGEAASERQAIGSGLLFHGVNQGDCVGLYFINRPEWL---VVDHACAAYSfvsVPLYDTLGPDAVKFVVNHANLQAIFC 196
Cdd:cd17641 13 TWADYADRVRAFALGLLALGVGRGDVVAILGDNRPEWVwaeLAAQAIGALS---LGIYQDSMAEEVAYLLNYTGARVVIA 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327099 197 VPQ-TLNILLSFLAEIPSIRLIVVVGGADEHLPSLPRgtgvtIVSYQKLLSQGRS--SLHP------FSPPKPEDIATIC 267
Cdd:cd17641 90 EDEeQVDKLLEIADRIPSVRYVIYCDPRGMRKYDDPR-----LISFEDVVALGRAldRRDPglyereVAAGKGEDVAVLC 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327099 268 YTSGTTGTPKGVVLTHGNLIANVAGSSVEAEFFPSDVYISYLPLAHIYEranQIMGV----YGGVAVGFYQgDVFKLMDD 343
Cdd:cd17641 165 TTSGTTGKPKLAMLSHGNFLGHCAAYLAADPLGPGDEYVSVLPLPWIGE---QMYSVgqalVCGFIVNFPE-EPETMMED 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327099 344 FAVLRPTIFCSVPRLYNRIYDGITSAVKSSGVVKKRLFEIAYNSKKQAIING----------RTPSAFWDKLVFNKIKEK 413
Cdd:cd17641 241 LREIGPTFVLLPPRVWEGIAADVRARMMDATPFKRFMFELGMKLGLRALDRGkrgrpvslwlRLASWLADALLFRPLRDR 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327099 414 LG-GRVRFMGSGASPLSPDVMDFLRiCFGCSVREGYGMTETSCVISAMDDGDNLSGHVGSPNPACEVKLVDVpemnytsd 492
Cdd:cd17641 321 LGfSRLRSAATGGAALGPDTFRFFH-AIGVPLKQLYGQTELAGAYTVHRDGDVDPDTVGVPFPGTEVRIDEV-------- 391
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327099 493 dqpyprGEICVRGPIIFKGYYKDEEQTREILDGDGWLHTGDIGLWLPGGRLKIIDRKKNIFKLAQGEYIAPEKIENVYTK 572
Cdd:cd17641 392 ------GEILVRSPGVFVGYYKNPEATAEDFDEDGWLHTGDAGYFKENGHLVVIDRAKDVGTTSDGTRFSPQFIENKLKF 465
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327099 573 CRFVSQCFIHGDSfNSSLVAIVSVDPEVMKDWAASEGIKYEHLGQLCNDPRV----RKTVLAEMDDLGREAQLRGFefak 648
Cdd:cd17641 466 SPYIAEAVVLGAG-RPYLTAFICIDYAIVGKWAEQRGIAFTTYTDLASRPEVyeliRKEVEKVNASLPEAQRIRRF---- 540
|
570 580
....*....|....*....|....
gi 22327099 649 avTLVPEPFTLENGLLTPTFKIKR 672
Cdd:cd17641 541 --LLLYKELDADDGELTRTRKVRR 562
|
|
| AFD_CAR-like |
cd17632 |
adenylation domain of carboxylic acid reductase (CAR); This family contains the adenylation ... |
97-665 |
9.71e-82 |
|
adenylation domain of carboxylic acid reductase (CAR); This family contains the adenylation domain of carboxylic acid reductase enzymes (CARs), and performs an equivalent function to that of the ANL superfamily of adenylating enzymes. It takes a carboxylic acid substrate and ATP, and produces an AMP-acyl phosphoester intermediate, releasing pyrophosphate. Kinetic analysis using various substrates shows that this enzyme has a broad but similar substrate specificity, preferring electron-rich acids. This suggests that attack by the carboxylate on the alpha-phosphate of adenosine triphosphate (ATP) is the step that determines the substrate specificity and reaction kinetics. CAR is an important enzyme for use as a biocatalyst providing regiospecific route to aldehydes from their respective carboxylic acids.
Pssm-ID: 341287 [Multi-domain] Cd Length: 588 Bit Score: 270.87 E-value: 9.71e-82
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327099 97 YAENKYLGTRVRSDGT-----------IGEYSWMTYGEAASERQAIGSGLLF-HGVNQGDCVGLYFINRPEWLVVDHACA 164
Cdd:cd17632 35 YADRPALGQRATELVTdpatgrttlrlLPRFETITYAELWERVGAVAAAHDPeQPVRPGDFVAVLGFTSPDYATVDLALT 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327099 165 AYSFVSVPLYDTLGPDAVKFVVNHANLQAIFCVPQTLNILLSFLAEIPSIRLIVVVGGA---DEH--------LPSLPRG 233
Cdd:cd17632 115 RLGAVSVPLQAGASAAQLAPILAETEPRLLAVSAEHLDLAVEAVLEGGTPPRLVVFDHRpevDAHraalesarERLAAVG 194
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327099 234 TGVTIVSyqkLLSQGRSSLHPFSPPKPED----IATICYTSGTTGTPKGVVLTHgNLIAN--VAGSSVEAEFFPSDVYIS 307
Cdd:cd17632 195 IPVTTLT---LIAVRGRDLPPAPLFRPEPdddpLALLIYTSGSTGTPKGAMYTE-RLVATfwLKVSSIQDIRPPASITLN 270
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327099 308 YLPLAHIYERANQIMGVY-GGVAVGFYQGDVFKLMDDFAVLRPTIFCSVPRLYNRIYDGITSAVKSSGVVKKRLFEIAYN 386
Cdd:cd17632 271 FMPMSHIAGRISLYGTLArGGTAYFAAASDMSTLFDDLALVRPTELFLVPRVCDMLFQRYQAELDRRSVAGADAETLAER 350
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327099 387 SKKQaiingrtpsafwdklvfnkIKEK-LGGRVRFMGSGASPLSPDVMDFLRICFGCSVREGYGMTETSCVIsamddgdn 465
Cdd:cd17632 351 VKAE-------------------LRERvLGGRLLAAVCGSAPLSAEMKAFMESLLDLDLHDGYGSTEAGAVI-------- 403
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327099 466 LSGHVGSPnPACEVKLVDVPEMNYTSDDQPYPRGEICVRGPIIFKGYYKDEEQTREILDGDGWLHTGDIGLWLPGGRLKI 545
Cdd:cd17632 404 LDGVIVRP-PVLDYKLVDVPELGYFRTDRPHPRGELLVKTDTLFPGYYKRPEVTAEVFDEDGFYRTGDVMAELGPDRLVY 482
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327099 546 IDRKKNIFKLAQGEYIAPEKIENVYTKCRFVSQCFIHGDSFNSSLVAIVSVDPEVMKDWaasegikyehlgqlcNDPRVR 625
Cdd:cd17632 483 VDRRNNVLKLSQGEFVTVARLEAVFAASPLVRQIFVYGNSERAYLLAVVVPTQDALAGE---------------DTARLR 547
|
570 580 590 600
....*....|....*....|....*....|....*....|
gi 22327099 626 KTVLAEMDDLGREAQLRGFEFAKAVTLVPEPFTLENGLLT 665
Cdd:cd17632 548 AALAESLQRIAREAGLQSYEIPRDFLIETEPFTIANGLLS 587
|
|
| ACSBG_like |
cd05933 |
Bubblegum-like very long-chain fatty acid CoA synthetase (VL-FACS); This family of very ... |
117-687 |
8.93e-78 |
|
Bubblegum-like very long-chain fatty acid CoA synthetase (VL-FACS); This family of very long-chain fatty acid CoA synthetase is named bubblegum because Drosophila melanogaster mutant bubblegum (BGM) has elevated levels of very-long-chain fatty acids (VLCFA) caused by a defective gene of this family. The human homolog (hsBG) has been characterized as a very long chain fatty acid CoA synthetase that functions specifically in the brain; hsBG may play a central role in brain VLCFA metabolism and myelinogenesis. VL-FACS is involved in the first reaction step of very long chain fatty acid degradation. It catalyzes the formation of fatty acyl-CoA in a two-step reaction: the formation of a fatty acyl-AMP molecule as an intermediate, and the formation of a fatty acyl-CoA. Free fatty acids must be "activated" to their CoA thioesters before participating in most catabolic and anabolic reactions.
Pssm-ID: 341256 [Multi-domain] Cd Length: 596 Bit Score: 260.37 E-value: 8.93e-78
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327099 117 SW--MTYGEAASE-RQAiGSGLLFHGVNQGDCVGLYFINRPEWLVVDHACAAYSFVSVPLYDTLGPDAVKFVVNHANLQa 193
Cdd:cd05933 5 KWhtLTYKEYYEAcRQA-AKAFLKLGLERFHGVGILGFNSPEWFIAAVGAIFAGGIAVGIYTTNSPEACQYVAETSEAN- 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327099 194 IFCVP--QTLNILLSFLAEIPSIRLIVVVGGA-DEHLPSLprgtgvtiVSYQKLLSQGRSS-----LHPFSPPKPEDIAT 265
Cdd:cd05933 83 ILVVEnqKQLQKILQIQDKLPHLKAIIQYKEPlKEKEPNL--------YSWDEFMELGRSIpdeqlDAIISSQKPNQCCT 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327099 266 ICYTSGTTGTPKGVVLTHGNLIANVAGSSVEAEFFPSDV----YISYLPLAHIyerANQIMGVYGGVAVG----FYQGDV 337
Cdd:cd05933 155 LIYTSGTTGMPKGVMLSHDNITWTAKAASQHMDLRPATVgqesVVSYLPLSHI---AAQILDIWLPIKVGgqvyFAQPDA 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327099 338 FK--LMDDFAVLRPTIFCSVPRLYNRIYDGITSAVKSSGVVKKRLFEIA------YNSKKQAI-INGRTPSAFWDKLVFN 408
Cdd:cd05933 232 LKgtLVKTLREVRPTAFMGVPRVWEKIQEKMKAVGAKSGTLKRKIASWAkgvgleTNLKLMGGeSPSPLFYRLAKKLVFK 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327099 409 KIKEKLG-GRVRFMGSGASPLSPDVMDF---LRIcfgcSVREGYGMTETSCVISAMDDGDNLSGHVGSPNPACEVKLVdv 484
Cdd:cd05933 312 KVRKALGlDRCQKFFTGAAPISRETLEFflsLNI----PIMELYGMSETSGPHTISNPQAYRLLSCGKALPGCKTKIH-- 385
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327099 485 pemNYTSDDQpyprGEICVRGPIIFKGYYKDEEQTREILDGDGWLHTGDIGLWLPGGRLKIIDRKKNIFKLAQGEYIAPE 564
Cdd:cd05933 386 ---NPDADGI----GEICFWGRHVFMGYLNMEDKTEEAIDEDGWLHSGDLGKLDEDGFLYITGRIKELIITAGGENVPPV 458
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327099 565 KIEN-VYTKCRFVSQCFIHGDS--FNSSLVAI-VSVDPE--VMKDWAASEGIKYehlgqlCNDPRVRKTVLAEM----DD 634
Cdd:cd05933 459 PIEDaVKKELPIISNAMLIGDKrkFLSMLLTLkCEVNPEtgEPLDELTEEAIEF------CRKLGSQATRVSEIaggkDP 532
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 22327099 635 LGREAQLRGFEFA--KAV---------TLVPEPFTLENGLLTPTFKIKRPQAKAYFAEAISKMY 687
Cdd:cd05933 533 KVYEAIEEGIKRVnkKAIsnaqkiqkwVILEKDFSVPGGELGPTMKLKRPVVAKKYKDEIDKLY 596
|
|
| MenE/FadK |
COG0318 |
O-succinylbenzoic acid-CoA ligase MenE or related acyl-CoA synthetase (AMP-forming) [Lipid ... |
86-632 |
8.29e-76 |
|
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: 250.88 E-value: 8.29e-76
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327099 86 LHDNFVHAVETYAENKYLgtrVRSDGTIgeyswmTYGEAASERQAIGSGLLFHGVNQGDCVGLYFINRPEWLVVDHACAA 165
Cdd:COG0318 1 LADLLRRAAARHPDRPAL---VFGGRRL------TYAELDARARRLAAALRALGVGPGDRVALLLPNSPEFVVAFLAALR 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327099 166 YSFVSVPLYDTLGPDAVKFVVNHANLQAIFCvpqtlnillsflaeipsirlivvvggadehlpslprgtgvtivsyqkll 245
Cdd:COG0318 72 AGAVVVPLNPRLTAEELAYILEDSGARALVT------------------------------------------------- 102
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327099 246 sqgrsslhpfsppkpediATICYTSGTTGTPKGVVLTHGNLIANVAGSSVEAEFFPSDVYISYLPLAHIYeraNQIMGVY 325
Cdd:COG0318 103 ------------------ALILYTSGTTGRPKGVMLTHRNLLANAAAIAAALGLTPGDVVLVALPLFHVF---GLTVGLL 161
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327099 326 GGVAVG--------FYQGDVFKLMDDFavlRPTIFCSVPRLYNRIYdgitsavkssgvvkkrlfeiaynskkqaiingRT 397
Cdd:COG0318 162 APLLAGatlvllprFDPERVLELIERE---RVTVLFGVPTMLARLL--------------------------------RH 206
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327099 398 PSAFWDKLvfnkikeklgGRVRFMGSGASPLSPDVMDFLRICFGCSVREGYGMTETSCVISA--MDDGDNLSGHVGSPNP 475
Cdd:COG0318 207 PEFARYDL----------SSLRLVVSGGAPLPPELLERFEERFGVRIVEGYGLTETSPVVTVnpEDPGERRPGSVGRPLP 276
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327099 476 ACEVKLVDVpemnytsDDQPYPR---GEICVRGPIIFKGYYKDEEQTREILDgDGWLHTGDIGLWLPGGRLKIIDRKKNI 552
Cdd:COG0318 277 GVEVRIVDE-------DGRELPPgevGEIVVRGPNVMKGYWNDPEATAEAFR-DGWLRTGDLGRLDEDGYLYIVGRKKDM 348
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327099 553 FKLAqGEYIAPEKIENVYTKCRFVSQCF---IHGDSFNSSLVAIV------SVDPEVMKDWAASE--GIK----YEHLGQ 617
Cdd:COG0318 349 IISG-GENVYPAEVEEVLAAHPGVAEAAvvgVPDEKWGERVVAFVvlrpgaELDAEELRAFLRERlaRYKvprrVEFVDE 427
|
570 580
....*....|....*....|
gi 22327099 618 LcndPR-----VRKTVLAEM 632
Cdd:COG0318 428 L---PRtasgkIDRRALRER 444
|
|
| Firefly_Luc_like |
cd05911 |
Firefly luciferase of light emitting insects and 4-Coumarate-CoA Ligase (4CL); This family ... |
110-569 |
4.69e-74 |
|
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: 247.13 E-value: 4.69e-74
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327099 110 DGTIGEYswMTYGEAASERQAIGSGLLFHGVNQGDCVGLYFINRPEWLVVDHAC----AAYSFVSvPLYDtlgPDAVKFV 185
Cdd:cd05911 4 DADTGKE--LTYAQLRTLSRRLAAGLRKLGLKKGDVVGIISPNSTYYPPVFLGClfagGIFSAAN-PIYT---ADELAHQ 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327099 186 VNHANLQAIFCVPQTLNILLSFLAEIPSIRLIVVVGGADEhlpslprgtgvTIVSYQKLLSQGRSSLHPFSPP----KPE 261
Cdd:cd05911 78 LKISKPKVIFTDPDGLEKVKEAAKELGPKDKIIVLDDKPD-----------GVLSIEDLLSPTLGEEDEDLPPplkdGKD 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327099 262 DIATICYTSGTTGTPKGVVLTHGNLIANV--AGSSVEAEFFPSDVYISYLPLAHIYERANQIMGVYGGVAV----GFYQG 335
Cdd:cd05911 147 DTAAILYSSGTTGLPKGVCLSHRNLIANLsqVQTFLYGNDGSNDVILGFLPLYHIYGLFTTLASLLNGATViimpKFDSE 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327099 336 DVFKLMDDFAVlrpTIFCSVPRLYNRIydgitsaVKSSGVVKKRLfeiaynskkqaiingrtPSafwdklvfnkikeklg 415
Cdd:cd05911 227 LFLDLIEKYKI---TFLYLVPPIAAAL-------AKSPLLDKYDL-----------------SS---------------- 263
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327099 416 grVRFMGSGASPLSPDVMDFLRICFG-CSVREGYGMTETSCVISAMDDGDNLSGHVGSPNPACEVKLVDVPEMNYTSDDQ 494
Cdd:cd05911 264 --LRVILSGGAPLSKELQELLAKRFPnATIKQGYGMTETGGILTVNPDGDDKPGSVGRLLPNVEAKIVDDDGKDSLGPNE 341
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 22327099 495 PyprGEICVRGPIIFKGYYKDEEQTREILDGDGWLHTGDIGLWLPGGRLKIIDRKKNIFKLaQGEYIAPEKIENV 569
Cdd:cd05911 342 P---GEICVRGPQVMKGYYNNPEATKETFDEDGWLHTGDIGYFDEDGYLYIVDRKKELIKY-KGFQVAPAELEAV 412
|
|
| LC_FACL_like |
cd05914 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); The members of this family are ... |
120-672 |
7.03e-68 |
|
Uncharacterized subfamily of fatty acid CoA ligase (FACL); The members of this family are bacterial long-chain fatty acid CoA synthetase, most of which are as yet uncharacterized. LC-FACS catalyzes the formation of fatty acyl-CoA in a two-step reaction: the formation of a fatty acyl-AMP molecule as an intermediate, and the formation of a fatty acyl-CoA. Free fatty acids must be "activated" to their CoA thioesters before participating in most catabolic and anabolic reactions.
Pssm-ID: 341240 [Multi-domain] Cd Length: 463 Bit Score: 230.02 E-value: 7.03e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327099 120 TYGEAASERQAIGSGLLFHGVNQGDCVGLYFINRPEWLVVDHACAAYSFVSVPLYDTLGPDAVKFVVNHANLQAIFCvpq 199
Cdd:cd05914 9 TYKDLADNIAKFALLLKINGVGTGDRVALMGENRPEWGIAFFAIWTYGAIAVPILAEFTADEVHHILNHSEAKAIFV--- 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327099 200 tlnillsflaeipsirlivvvggadehlpslprgtgvtivsyqkllsqgrsslhpfspPKPEDIATICYTSGTTGTPKGV 279
Cdd:cd05914 86 ----------------------------------------------------------SDEDDVALINYTSGTTGNSKGV 107
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327099 280 VLTHGNLIANVAGSSVEAEFFPSDVYISYLPLAHIYERA-NQIMGVYGGVAVGFYQ---GDVFKLMDdFAVLRPTIFCSV 355
Cdd:cd05914 108 MLTYRNIVSNVDGVKEVVLLGKGDKILSILPLHHIYPLTfTLLLPLLNGAHVVFLDkipSAKIIALA-FAQVTPTLGVPV 186
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327099 356 PRLYNRIYDGITSAVKSSGVVKKRLFEIAYNSKKQaiingrtpsafwdKLVFNKIKEKLGGRVRFMGSGASPLSPDVMDF 435
Cdd:cd05914 187 PLVIEKIFKMDIIPKLTLKKFKFKLAKKINNRKIR-------------KLAFKKVHEAFGGNIKEFVIGGAKINPDVEEF 253
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327099 436 LRIcFGCSVREGYGMTETSCVISAMDDGDNLSGHVGSPNPACEVKLvdvpemnyTSDDQPYPRGEICVRGPIIFKGYYKD 515
Cdd:cd05914 254 LRT-IGFPYTIGYGMTETAPIISYSPPNRIRLGSAGKVIDGVEVRI--------DSPDPATGEGEIIVRGPNVMKGYYKN 324
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327099 516 EEQTREILDGDGWLHTGDIGLWLPGGRLKIIDRKKNIFKLAQGEYIAPEKIENVYTKCRFVSQCFIHgdSFNSSLVAIVS 595
Cdd:cd05914 325 PEATAEAFDKDGWFHTGDLGKIDAEGYLYIRGRKKEMIVLSSGKNIYPEEIEAKINNMPFVLESLVV--VQEKKLVALAY 402
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 22327099 596 VDPEVMKDwaasegikyEHLGQLCNDPRVRKTVLAEMDDlgreaQLRGFEFAKAVTLVPEPFTlenglLTPTFKIKR 672
Cdd:cd05914 403 IDPDFLDV---------KALKQRNIIDAIKWEVRDKVNQ-----KVPNYKKISKVKIVKEEFE-----KTPKGKIKR 460
|
|
| PRK06187 |
PRK06187 |
long-chain-fatty-acid--CoA ligase; Validated |
104-569 |
1.55e-66 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 235730 [Multi-domain] Cd Length: 521 Bit Score: 228.15 E-value: 1.55e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327099 104 GTRVRSDGTIgeYSW----MTYGEAASERQAIGSGLLFHGVNQGDCVGLYFINRPEWLVVDHACAAYSFVSVPLYDTLGP 179
Cdd:PRK06187 15 GARKHPDKEA--VYFdgrrTTYAELDERVNRLANALRALGVKKGDRVAVFDWNSHEYLEAYFAVPKIGAVLHPINIRLKP 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327099 180 DAVKFVVNHANLQAIFCVPQTLNILLSFLAEIPSIRLIVVVGGADEHlpslprGTGVTIVSYQKLLSqGRSSLHPFSPPK 259
Cdd:PRK06187 93 EEIAYILNDAEDRVVLVDSEFVPLLAAILPQLPTVRTVIVEGDGPAA------PLAPEVGEYEELLA-AASDTFDFPDID 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327099 260 PEDIATICYTSGTTGTPKGVVLTHGNLIANVAGSSVEAEFFPSDVYISYLPLAHIYERANQIMGVYGG---VAVGFYQGD 336
Cdd:PRK06187 166 ENDAAAMLYTSGTTGHPKGVVLSHRNLFLHSLAVCAWLKLSRDDVYLVIVPMFHVHAWGLPYLALMAGakqVIPRRFDPE 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327099 337 vfKLMDDFAVLRPTIFCSVPRLYnriydgitsavkssgvvkkrlfeiaynskkQAIINGRTPSAFWdklvFNkikeklgg 416
Cdd:PRK06187 246 --NLLDLIETERVTFFFAVPTIW------------------------------QMLLKAPRAYFVD----FS-------- 281
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327099 417 RVRFMGSGASPLSPDVM-DFLRIcFGCSVREGYGMTETSCVISA------MDDGDNLSGHVGSPNPACEVKLVDvpemny 489
Cdd:PRK06187 282 SLRLVIYGGAALPPALLrEFKEK-FGIDLVQGYGMTETSPVVSVlppedqLPGQWTKRRSAGRPLPGVEARIVD------ 354
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327099 490 tSDDQPYPR-----GEICVRGPIIFKGYYKDEEQTREILDGdGWLHTGDIGLWLPGGRLKIIDRKKNIFKLAqGEYIAPE 564
Cdd:PRK06187 355 -DDGDELPPdggevGEIIVRGPWLMQGYWNRPEATAETIDG-GWLHTGDVGYIDEDGYLYITDRIKDVIISG-GENIYPR 431
|
....*
gi 22327099 565 KIENV 569
Cdd:PRK06187 432 ELEDA 436
|
|
| AFD_class_I |
cd04433 |
Adenylate forming domain, Class I, also known as the ANL superfamily; This family is known as ... |
262-612 |
2.63e-64 |
|
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: 216.38 E-value: 2.63e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327099 262 DIATICYTSGTTGTPKGVVLTHGNLIANVAGSSVEAEFFPSDVYISYLPLAHIyeraNQIMGVYGGVAVG--------FY 333
Cdd:cd04433 1 DPALILYTSGTTGKPKGVVLSHRNLLAAAAALAASGGLTEGDVFLSTLPLFHI----GGLFGLLGALLAGgtvvllpkFD 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327099 334 QGDVFKLMDDFavlRPTIFCSVPRLYNRI--YDGITSAVKSSgvvkkrlfeiaynskkqaiingrtpsafwdklvfnkik 411
Cdd:cd04433 77 PEAALELIERE---KVTILLGVPTLLARLlkAPESAGYDLSS-------------------------------------- 115
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327099 412 eklggrVRFMGSGASPLSPDVMDFLRICFGCSVREGYGMTETSCVISAM--DDGDNLSGHVGSPNPACEVKLVDVPemny 489
Cdd:cd04433 116 ------LRALVSGGAPLPPELLERFEEAPGIKLVNGYGLTETGGTVATGppDDDARKPGSVGRPVPGVEVRIVDPD---- 185
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327099 490 TSDDQPYPRGEICVRGPIIFKGYYKDEEQTREIlDGDGWLHTGDIGLWLPGGRLKIIDRKKNIFKlAQGEYIAPEKIENV 569
Cdd:cd04433 186 GGELPPGEIGELVVRGPSVMKGYWNNPEATAAV-DEDGWYRTGDLGRLDEDGYLYIVGRLKDMIK-SGGENVYPAEVEAV 263
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|..
gi 22327099 570 YTKCRFVSQCFIHG---DSFNSSLVAIV------SVDPEVMKDWAASEGIKY 612
Cdd:cd04433 264 LLGHPGVAEAAVVGvpdPEWGERVVAVVvlrpgaDLDAEELRAHVRERLAPY 315
|
|
| FC-FACS_FadD_like |
cd05936 |
Prokaryotic long-chain fatty acid CoA synthetases similar to Escherichia coli FadD; This ... |
118-579 |
4.11e-60 |
|
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: 209.34 E-value: 4.11e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327099 118 WMTYGEAASERQAIGSGLLFHGVNQGDCVGLYFINRPEWLVVDHACAAYSFVSVPLYDTLGPDAVKFVVNHANLQAIFCv 197
Cdd:cd05936 24 KLTYRELDALAEAFAAGLQNLGVQPGDRVALMLPNCPQFPIAYFGALKAGAVVVPLNPLYTPRELEHILNDSGAKALIV- 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327099 198 pqtlnillsflaeipsirlivvvggadehlpslprgtgvtIVSYQKLLSQGRSSLHPFSPPkPEDIATICYTSGTTGTPK 277
Cdd:cd05936 103 ----------------------------------------AVSFTDLLAAGAPLGERVALT-PEDVAVLQYTSGTTGVPK 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327099 278 GVVLTHGNLIANV--AGSSVEAEFFPSDVYISYLPLAHIYerANQIMGVY----GGVAVGFYQGDVFKLMDDFAVLRPTI 351
Cdd:cd05936 142 GAMLTHRNLVANAlqIKAWLEDLLEGDDVVLAALPLFHVF--GLTVALLLplalGATIVLIPRFRPIGVLKEIRKHRVTI 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327099 352 FCSVPRLYNriydgitsavkssgvvkkrlfeiaynskkqAIINgrtpsafwdklvfNKIKEKLG-GRVRFMGSGASPLSP 430
Cdd:cd05936 220 FPGVPTMYI------------------------------ALLN-------------APEFKKRDfSSLRLCISGGAPLPV 256
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327099 431 DVMDFLRICFGCSVREGYGMTETSCVISAMD-DGDNLSGHVGSPNPACEVKLVDvpemnytSDDQPYPR---GEICVRGP 506
Cdd:cd05936 257 EVAERFEELTGVPIVEGYGLTETSPVVAVNPlDGPRKPGSIGIPLPGTEVKIVD-------DDGEELPPgevGELWVRGP 329
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 22327099 507 IIFKGYYKDEEQTREILDgDGWLHTGDIGLWLPGGRLKIIDRKKNIFkLAQGEYIAPEKIENVYTKCRFVSQC 579
Cdd:cd05936 330 QVMKGYWNRPEETAEAFV-DGWLRTGDIGYMDEDGYFFIVDRKKDMI-IVGGFNVYPREVEEVLYEHPAVAEA 400
|
|
| PTZ00342 |
PTZ00342 |
acyl-CoA synthetase; Provisional |
259-687 |
4.82e-56 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 240370 [Multi-domain] Cd Length: 746 Bit Score: 204.18 E-value: 4.82e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327099 259 KPEDIATICYTSGTTGTPKGVVLTHGNL---IANVAGSSVEAEFFPsDVYISYLPLAHIYERANQIMGVYGGVAVGFYQG 335
Cdd:PTZ00342 302 DPDFITSIVYTSGTSGKPKGVMLSNKNLyntVVPLCKHSIFKKYNP-KTHLSYLPISHIYERVIAYLSFMLGGTINIWSK 380
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327099 336 DVFKLMDDFAVLRPTIFCSVPRLYNRIYDGITSAVKSSGVVKKRLFEIAYNSKKQAiiNGRTPSAFWDKL--VFNKIKEK 413
Cdd:PTZ00342 381 DINYFSKDIYNSKGNILAGVPKVFNRIYTNIMTEINNLPPLKRFLVKKILSLRKSN--NNGGFSKFLEGIthISSKIKDK 458
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327099 414 LGGRVRFMGSGASPLSPDVMDFLRICFGCSVREGYGMTETSCVISAMDDGDNLSGHVGSP-NPACEVKLVDVPemNYTSD 492
Cdd:PTZ00342 459 VNPNLEVILNGGGKLSPKIAEELSVLLNVNYYQGYGLTETTGPIFVQHADDNNTESIGGPiSPNTKYKVRTWE--TYKAT 536
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327099 493 DQPyPRGEICVRGPIIFKGYYKDEEQTREILDGDGWLHTGDIGLWLPGGRLKIIDRKKNIFKLAQGEYIAPEKIENVYTK 572
Cdd:PTZ00342 537 DTL-PKGELLIKSDSIFSGYFLEKEQTKNAFTEDGYFKTGDIVQINKNGSLTFLDRSKGLVKLSQGEYIETDMLNNLYSQ 615
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327099 573 CRFVSQCFIHGDSFNSSLVAIVSVDPEV----MKD--WAASEGIKYEHLGQLCNDPRVRKTVLAE-----MDDLGREAQL 641
Cdd:PTZ00342 616 ISFINFCVVYGDDSMDGPLAIISVDKYLlfkcLKDdnMLESTGINEKNYLEKLTDETINNNIYVDyvkgkMLEVYKKTNL 695
|
410 420 430 440
....*....|....*....|....*....|....*....|....*....
gi 22327099 642 RGFEFAKAVTLVPEPFTLENgLLTPTFKIKR---PQAKAYFAEAISKMY 687
Cdd:PTZ00342 696 NRYNIINDIYLTSKVWDTNN-YLTPTFKVKRfyvFKDYAFFIDQVKKIY 743
|
|
| PRK07656 |
PRK07656 |
long-chain-fatty-acid--CoA ligase; Validated |
119-553 |
2.27e-53 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236072 [Multi-domain] Cd Length: 513 Bit Score: 192.04 E-value: 2.27e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327099 119 MTYGEAASERQAIGSGLLFHGVNQGDCVGLYFINRPEWLVvdhacAAYSFVS-----VPLYDTLGPDAVKFVVNHANLQA 193
Cdd:PRK07656 31 LTYAELNARVRRAAAALAALGIGKGDRVAIWAPNSPHWVI-----AALGALKagavvVPLNTRYTADEAAYILARGDAKA 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327099 194 IFCVPQTLNILLSFLAEIPSIRLIVVVGGADehlpslPRGTGVTIVSYQKLLSQGRSSLhpFSPP-KPEDIATICYTSGT 272
Cdd:PRK07656 106 LFVLGLFLGVDYSATTRLPALEHVVICETEE------DDPHTEKMKTFTDFLAAGDPAE--RAPEvDPDDVADILFTSGT 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327099 273 TGTPKGVVLTHGNLIANVAGSSVEAEFFPSDVYISYLPLAHIYeranqimgvygGVAVG----------------FYQGD 336
Cdd:PRK07656 178 TGRPKGAMLTHRQLLSNAADWAEYLGLTEGDRYLAANPFFHVF-----------GYKAGvnaplmrgatilplpvFDPDE 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327099 337 VFKLMDDFavlRPTIFCSVPRLYNRIYDgitsavkssgVVKKRLFEIAynskkqaiingrtpsafwdklvfnkikeklgg 416
Cdd:PRK07656 247 VFRLIETE---RITVLPGPPTMYNSLLQ----------HPDRSAEDLS-------------------------------- 281
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327099 417 RVRFMGSGASPLSPDVMDFLRICFGCS-VREGYGMTETS---CVISAMDDGDNLSGHVGSPNPACEVKLVDVPEMNYTSD 492
Cdd:PRK07656 282 SLRLAVTGAASMPVALLERFESELGVDiVLTGYGLSEASgvtTFNRLDDDRKTVAGTIGTAIAGVENKIVNELGEEVPVG 361
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 22327099 493 DQpyprGEICVRGPIIFKGYYKDEEQTREILDGDGWLHTGDIGLWLPGGRLKIIDRKKNIF 553
Cdd:PRK07656 362 EV----GELLVRGPNVMKGYYDDPEATAAAIDADGWLHTGDLGRLDEEGYLYIVDRKKDMF 418
|
|
| 4CL |
cd05904 |
4-Coumarate-CoA Ligase (4CL); 4-Coumarate:coenzyme A ligase is a key enzyme in the ... |
120-569 |
1.67e-52 |
|
4-Coumarate-CoA Ligase (4CL); 4-Coumarate:coenzyme A ligase is a key enzyme in the phenylpropanoid metabolic pathway for monolignol and flavonoid biosynthesis. It catalyzes the synthesis of hydroxycinnamate-CoA thioesters in a two-step reaction, involving the formation of hydroxycinnamate-AMP anhydride and the nucleophilic substitution of AMP by CoA. The phenylpropanoid pathway is one of the most important secondary metabolism pathways in plants and hydroxycinnamate-CoA thioesters are the precursors of lignin and other important phenylpropanoids.
Pssm-ID: 341230 [Multi-domain] Cd Length: 505 Bit Score: 189.37 E-value: 1.67e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327099 120 TYGEAASERQAIGSGLLFHGVNQGDCVGLYFINRPEWLVVDHACAAYSFVSVPLYDTLGPDAVKFVVNHANLQAIFCVPQ 199
Cdd:cd05904 34 TYAELERRVRRLAAGLAKRGGRKGDVVLLLSPNSIEFPVAFLAVLSLGAVVTTANPLSTPAEIAKQVKDSGAKLAFTTAE 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327099 200 TLnillsflAEIPSIRLIVVVGGADEHLPSLPRgtgvtivsyqKLLSQGRSSLHPFSPPKPEDIATICYTSGTTGTPKGV 279
Cdd:cd05904 114 LA-------EKLASLALPVVLLDSAEFDSLSFS----------DLLFEADEAEPPVVVIKQDDVAALLYSSGTTGRSKGV 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327099 280 VLTHGNLIANVAG--SSVEAEFFPSDVYISYLPLAHIYERANQIMGV--YGGVAV---GFYQGDVFKLMDDFAVlrpTIF 352
Cdd:cd05904 177 MLTHRNLIAMVAQfvAGEGSNSDSEDVFLCVLPMFHIYGLSSFALGLlrLGATVVvmpRFDLEELLAAIERYKV---THL 253
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327099 353 CSVPRLynriydgITSAVKSSGVVKKRLfeiaynskkqaiingrtpsafwdklvfnkikeklgGRVRFMGSGASPLSPDV 432
Cdd:cd05904 254 PVVPPI-------VLALVKSPIVDKYDL-----------------------------------SSLRQIMSGAAPLGKEL 291
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327099 433 MDFLRICF-GCSVREGYGMTETSCVISAMDDGDNLSGHVGS-----PNpaCEVKLVDvPEmnyTSDDQPYPR-GEICVRG 505
Cdd:cd05904 292 IEAFRAKFpNVDLGQGYGMTESTGVVAMCFAPEKDRAKYGSvgrlvPN--VEAKIVD-PE---TGESLPPNQtGELWIRG 365
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 22327099 506 PIIFKGYYKDEEQTREILDGDGWLHTGDIGLWLPGGRLKIIDRKKNIFKLaQGEYIAPEKIENV 569
Cdd:cd05904 366 PSIMKGYLNNPEATAATIDKEGWLHTGDLCYIDEDGYLFIVDRLKELIKY-KGFQVAPAELEAL 428
|
|
| FACL_FadD13-like |
cd17631 |
fatty acyl-CoA synthetase, including FadD13; This family contains fatty acyl-CoA synthetases, ... |
119-569 |
8.15e-49 |
|
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: 177.42 E-value: 8.15e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327099 119 MTYGEAASERQAIGSGLLFHGVNQGDCVGLYFINRPEWLVVDHACAAYSFVSVPLYDTLGPDAVKFVVNHAnlqaifcvp 198
Cdd:cd17631 21 LTYAELDERVNRLAHALRALGVAKGDRVAVLSKNSPEFLELLFAAARLGAVFVPLNFRLTPPEVAYILADS--------- 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327099 199 qtlnillsflaeipsirlivvvggadehlpslprGTGVTIvsyqkllsqgrsslhpfsppkpEDIATICYTSGTTGTPKG 278
Cdd:cd17631 92 ----------------------------------GAKVLF----------------------DDLALLMYTSGTTGRPKG 115
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327099 279 VVLTHGNLIANVAGSSVEAEFFPSDVYISYLPLAHIYErANQIMGVY---GGVAV---GFyqgDVFKLMDDFAVLRPTIF 352
Cdd:cd17631 116 AMLTHRNLLWNAVNALAALDLGPDDVLLVVAPLFHIGG-LGVFTLPTllrGGTVVilrKF---DPETVLDLIERHRVTSF 191
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327099 353 CSVPRLYnriydgitsavkssgvvkkrlfeiaynskkQAIIngRTPSafWDKLVFNkikeklggRVRFMGSGASPLSPDV 432
Cdd:cd17631 192 FLVPTMI------------------------------QALL--QHPR--FATTDLS--------SLRAVIYGGAPMPERL 229
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327099 433 mdfLRIC--FGCSVREGYGMTETSCVISAM--DDGDNLSGHVGSPNPACEVKLVDvpemnytSDDQPYP---RGEICVRG 505
Cdd:cd17631 230 ---LRALqaRGVKFVQGYGMTETSPGVTFLspEDHRRKLGSAGRPVFFVEVRIVD-------PDGREVPpgeVGEIVVRG 299
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 22327099 506 PIIFKGYYKDEEQTREILdGDGWLHTGDIGLWLPGGRLKIIDRKKNIFKlAQGEYIAPEKIENV 569
Cdd:cd17631 300 PHVMAGYWNRPEATAAAF-RDGWFHTGDLGRLDEDGYLYIVDRKKDMII-SGGENVYPAEVEDV 361
|
|
| MCS |
cd05941 |
Malonyl-CoA synthetase (MCS); MCS catalyzes the formation of malonyl-CoA in a two-step ... |
262-612 |
7.25e-48 |
|
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: 174.79 E-value: 7.25e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327099 262 DIATICYTSGTTGTPKGVVLTHGNLIANVAGSSVEAEFFPSDVYISYLPLAHIYeranqimGVYGGVAVGFYQGDVFKLM 341
Cdd:cd05941 90 DPALILYTSGTTGRPKGVVLTHANLAANVRALVDAWRWTEDDVLLHVLPLHHVH-------GLVNALLCPLFAGASVEFL 162
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327099 342 DDFAVLRP---------TIFCSVPRLYNRIydgitsavkssgvvkkrlfeIAYNSKKQAIINGRTPSAFwdklvfnkike 412
Cdd:cd05941 163 PKFDPKEVaisrlmpsiTVFMGVPTIYTRL--------------------LQYYEAHFTDPQFARAAAA----------- 211
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327099 413 klgGRVRFMGSGASPLSPDVMDFLRICFGCSVREGYGMTETSCVISAMDDGDNLSGHVGSPNPACEVKLVDVPEMNYTSD 492
Cdd:cd05941 212 ---ERLRLMVSGSAALPVPTLEEWEAITGHTLLERYGMTEIGMALSNPLDGERRPGTVGMPLPGVQARIVDEETGEPLPR 288
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327099 493 DQPyprGEICVRGPIIFKGYYKDEEQTREILDGDGWLHTGDIGLWLPGGRLKIIDRKK-NIFKlAQGEYIAPEKIENVYT 571
Cdd:cd05941 289 GEV---GEIQVRGPSVFKEYWNKPEATKEEFTDDGWFKTGDLGVVDEDGYYWILGRSSvDIIK-SGGYKVSALEIERVLL 364
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|.
gi 22327099 572 KCRFVSQCFIHG---DSFNSSLVAIV-------SVDPEVMKDWAASEGIKY 612
Cdd:cd05941 365 AHPGVSECAVIGvpdPDWGERVVAVVvlragaaALSLEELKEWAKQRLAPY 415
|
|
| FACL_DitJ_like |
cd05934 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
120-569 |
3.31e-47 |
|
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: 172.48 E-value: 3.31e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327099 120 TYGEAASERQAIGSGLLFHGVNQGDCVGLYFINRPEWLVVDHACAAYSFVSVPLYDTLGPDAVKFVVNHANLQAIFCvpq 199
Cdd:cd05934 5 TYAELLRESARIAAALAALGIRPGDRVALMLDNCPEFLFAWFALAKLGAVLVPINTALRGDELAYIIDHSGAQLVVV--- 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327099 200 tlnillsflaeipsirlivvvggadehlpslprgtgvtivsyqkllsqgrsslhpfsppkpeDIATICYTSGTTGTPKGV 279
Cdd:cd05934 82 --------------------------------------------------------------DPASILYTSGTTGPPKGV 99
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327099 280 VLTHGNLiANVAGSSVEAEFFPS-DVYISYLPLAHIyeraN-QIMGVYGGVAVGfyqgDVFKLMDDFAVLRptiFCSVPR 357
Cdd:cd05934 100 VITHANL-TFAGYYSARRFGLGEdDVYLTVLPLFHI----NaQAVSVLAALSVG----ATLVLLPRFSASR---FWSDVR 167
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327099 358 LYNRIYdgiTSAVkssGVVKKRLFeiaynskkqaiingRTPSAFWDKlvfnkikeklGGRVRFmGSGASPLSPDVMDFLR 437
Cdd:cd05934 168 RYGATV---TNYL---GAMLSYLL--------------AQPPSPDDR----------AHRLRA-AYGAPNPPELHEEFEE 216
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327099 438 IcFGCSVREGYGMTETSCVISAMDDGDNLSGHVGSPNPACEVKLVDvpemnytSDDQPYPR---GEICVR---GPIIFKG 511
Cdd:cd05934 217 R-FGVRLLEGYGMTETIVGVIGPRDEPRRPGSIGRPAPGYEVRIVD-------DDGQELPAgepGELVIRglrGWGFFKG 288
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*...
gi 22327099 512 YYKDEEQTREILDGdGWLHTGDIGLWLPGGRLKIIDRKKNIFKlAQGEYIAPEKIENV 569
Cdd:cd05934 289 YYNMPEATAEAMRN-GWFHTGDLGYRDADGFFYFVDRKKDMIR-RRGENISSAEVERA 344
|
|
| FACL_fum10p_like |
cd05926 |
Subfamily of fatty acid CoA ligase (FACL) similar to Fum10p of Gibberella moniliformis; FACL ... |
118-579 |
4.98e-47 |
|
Subfamily of fatty acid CoA ligase (FACL) similar to Fum10p of Gibberella moniliformis; FACL catalyzes the formation of fatty acyl-CoA in a two-step reaction: the formation of a fatty acyl-AMP molecule as an intermediate, followed by the formation of a fatty acyl-CoA. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions. Fum10p is a fatty acid CoA ligase involved in the synthesis of fumonisin, a polyketide mycotoxin, in Gibberella moniliformis.
Pssm-ID: 341249 [Multi-domain] Cd Length: 493 Bit Score: 173.65 E-value: 4.98e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327099 118 WMTYGEAASERQAIGSGLLFHGVNQGDCVGLYFINRPEWLVVDHACAAYSFVSVPLYDTLGPDAVKFVVNHANLQAIfcv 197
Cdd:cd05926 14 ALTYADLAELVDDLARQLAALGIKKGDRVAIALPNGLEFVVAFLAAARAGAVVAPLNPAYKKAEFEFYLADLGSKLV--- 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327099 198 pqtlniLLSFLAEIPSIRLIVVVGGADEHLpSLPRGTGVTIVSYQKL--LSQGRSSLHPFSPPKPEDIATICYTSGTTGT 275
Cdd:cd05926 91 ------LTPKGELGPASRAASKLGLAILEL-ALDVGVLIRAPSAESLsnLLADKKNAKSEGVPLPDDLALILHTSGTTGR 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327099 276 PKGVVLTHGNLIANVAGSSVEAEFFPSDVYISYLPLAHIyeraNQIMGVY------GGVAV---GFyqgDVFKLMDDFAV 346
Cdd:cd05926 164 PKGVPLTHRNLAASATNITNTYKLTPDDRTLVVMPLFHV----HGLVASLlstlaaGGSVVlppRF---SASTFWPDVRD 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327099 347 LRPTIFCSVPRLYnriydgitsavkssgvvkkrlfeiaynskkQAIINgRTPSafwdklvfNKIKEKlgGRVRFMGSGAS 426
Cdd:cd05926 237 YNATWYTAVPTIH------------------------------QILLN-RPEP--------NPESPP--PKLRFIRSCSA 275
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327099 427 PLSPDVMDFLRICFGCSVREGYGMTETSCVISA--MDDGDNLSGHVGSPNpACEVKLVDvpemnytSDDQPYP---RGEI 501
Cdd:cd05926 276 SLPPAVLEALEATFGAPVLEAYGMTEAAHQMTSnpLPPGPRKPGSVGKPV-GVEVRILD-------EDGEILPpgvVGEI 347
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 22327099 502 CVRGPIIFKGYYKDEEQTREILDGDGWLHTGDIGLWLPGGRLKIIDRKKNIFKLAqGEYIAPEKIENVYTKCRFVSQC 579
Cdd:cd05926 348 CLRGPNVTRGYLNNPEANAEAAFKDGWFRTGDLGYLDADGYLFLTGRIKELINRG-GEKISPLEVDGVLLSHPAVLEA 424
|
|
| menE |
TIGR01923 |
O-succinylbenzoate-CoA ligase; This model represents an enzyme, O-succinylbenzoate-CoA ligase, ... |
138-618 |
7.64e-44 |
|
O-succinylbenzoate-CoA ligase; This model represents an enzyme, O-succinylbenzoate-CoA ligase, which is involved in the fourth step of the menaquinone biosynthesis pathway. O-succinylbenzoate-CoA ligase, together with menB - naphtoate synthase, take 2-succinylbenzoate and convert it into 1,4-di-hydroxy-2- naphtoate. [Biosynthesis of cofactors, prosthetic groups, and carriers, Menaquinone and ubiquinone]
Pssm-ID: 162605 [Multi-domain] Cd Length: 436 Bit Score: 163.39 E-value: 7.64e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327099 138 HGVNQGDCVGLYFINRPEWLVVDHACAAYSFVSVPLYDTLGPDAVKFVVNHANLQAIFCvpqtlnillsflaeipsirli 217
Cdd:TIGR01923 19 QGIRSGSRVALVGQNSIEMVLLLHACLLLGAEIAMLNTRLTENERTNQLEDLDVQLLLT--------------------- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327099 218 vvvggadehlPSLPRGTGVTIVSYQKLLSQGRSSLHPFSPPKPEDIATICYTSGTTGTPKGVVLTHGNLIANVAGSSVEA 297
Cdd:TIGR01923 78 ----------DSLLEEKDFQADSLDRIEAAGRYETSLSASFNMDQIATLMFTSGTTGKPKAVPHTFRNHYASAVGSKENL 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327099 298 EFFPSDVYISYLPLAHIYERANQIMGVYGGVAVGFYQGDVfKLMDDFAVLRPTIFCSVPRLYNRIYDgitsavKSSGVVK 377
Cdd:TIGR01923 148 GFTEDDNWLLSLPLYHISGLSILFRWLIEGATLRIVDKFN-QLLEMIANERVTHISLVPTQLNRLLD------EGGHNEN 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327099 378 KRLFeiaynskkqaiingrtpsafwdklvfnkikeKLGGrvrfmgsgaSPLSPDVMDfLRICFGCSVREGYGMTET-SCV 456
Cdd:TIGR01923 221 LRKI-------------------------------LLGG---------SAIPAPLIE-EAQQYGLPIYLSYGMTETcSQV 259
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327099 457 ISAMDDGDNLSGHVGSPNPACEVKLvdvpemnytSDDQPYPRGEICVRGPIIFKGYYkDEEQTREILDGDGWLHTGDIGL 536
Cdd:TIGR01923 260 TTATPEMLHARPDVGRPLAGREIKI---------KVDNKEGHGEIMVKGANLMKGYL-YQGELTPAFEQQGWFNTGDIGE 329
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327099 537 WLPGGRLKIIDRKKNIFkLAQGEYIAPEKIENVYTKCRFVSQCFIHG---DSFNSSLVAIVSVDpevmKDWAASEGIKY- 612
Cdd:TIGR01923 330 LDGEGFLYVLGRRDDLI-ISGGENIYPEEIETVLYQHPGIQEAVVVPkpdAEWGQVPVAYIVSE----SDISQAKLIAYl 404
|
....*..
gi 22327099 613 -EHLGQL 618
Cdd:TIGR01923 405 tEKLAKY 411
|
|
| PRK05605 |
PRK05605 |
long-chain-fatty-acid--CoA ligase; Validated |
81-615 |
1.45e-41 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 235531 [Multi-domain] Cd Length: 573 Bit Score: 159.78 E-value: 1.45e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327099 81 PEIGTLHDNFVHAVETYAEN---KYLGTRvrsdgtigeyswMTYGEAASERQAIGSGLLFHGVNQGDCVGLYFINRPEWL 157
Cdd:PRK05605 29 YGDTTLVDLYDNAVARFGDRpalDFFGAT------------TTYAELGKQVRRAAAGLRALGVRPGDRVAIVLPNCPQHI 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327099 158 VVDHACAAYSFVSV---PLY--------------------DTLGPDAVKFVVNHAnLQAIFCV------PQTLNILLSFl 208
Cdd:PRK05605 97 VAFYAVLRLGAVVVehnPLYtahelehpfedhgarvaivwDKVAPTVERLRRTTP-LETIVSVnmiaamPLLQRLALRL- 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327099 209 aEIPSIRlivvvgGADEHLPSLPRGTgvtiVSYQKLLS-----QGRSSLHPfsPPKPEDIATICYTSGTTGTPKGVVLTH 283
Cdd:PRK05605 175 -PIPALR------KARAALTGPAPGT----VPWETLVDaaiggDGSDVSHP--RPTPDDVALILYTSGTTGKPKGAQLTH 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327099 284 GNLIANVA---------GSSVEaeffpsdVYISYLPLAHIYERA-NQIMGVY-GGVAVGFYQGDVFKLMDDFAVLRPTIF 352
Cdd:PRK05605 242 RNLFANAAqgkawvpglGDGPE-------RVLAALPMFHAYGLTlCLTLAVSiGGELVLLPAPDIDLILDAMKKHPPTWL 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327099 353 CSVPRLYNRIYDGitsavkssgvvkkrlfeiaynSKKQAI-INGrtpsafwdklvfnkikeklggrVRFMGSGASPLSPD 431
Cdd:PRK05605 315 PGVPPLYEKIAEA---------------------AEERGVdLSG----------------------VRNAFSGAMALPVS 351
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327099 432 VMDFLRICFGCSVREGYGMTETSCVISA--MDDgDNLSGHVGSPNPACEVKLVDvPEmNYTSDDQPYPRGEICVRGPIIF 509
Cdd:PRK05605 352 TVELWEKLTGGLLVEGYGLTETSPIIVGnpMSD-DRRPGYVGVPFPDTEVRIVD-PE-DPDETMPDGEEGELLVRGPQVF 428
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327099 510 KGYYKDEEQTREILDgDGWLHTGDIGLWLPGGRLKIIDRKKNIFkLAQGEYIAPEKIENVYTKCRFVSQCFIHG---DSF 586
Cdd:PRK05605 429 KGYWNRPEETAKSFL-DGWFRTGDVVVMEEDGFIRIVDRIKELI-ITGGFNVYPAEVEEVLREHPGVEDAAVVGlprEDG 506
|
570 580 590
....*....|....*....|....*....|....*
gi 22327099 587 NSSLVAIVS------VDPEVMKDWAasegikYEHL 615
Cdd:PRK05605 507 SEEVVAAVVlepgaaLDPEGLRAYC------REHL 535
|
|
| PRK05677 |
PRK05677 |
long-chain-fatty-acid--CoA ligase; Validated |
239-579 |
1.12e-40 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 168170 [Multi-domain] Cd Length: 562 Bit Score: 157.23 E-value: 1.12e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327099 239 VSYQKLLSQGRSslHPFSP--PKPEDIATICYTSGTTGTPKGVVLTHGNLIANVA------GSSVEAEffpSDVYISYLP 310
Cdd:PRK05677 185 VKFNDALAKGAG--QPVTEanPQADDVAVLQYTGGTTGVAKGAMLTHRNLVANMLqcralmGSNLNEG---CEILIAPLP 259
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327099 311 LAHIYeranqimgvyggvavGFyqgdVFKLMDDFAVLRPTIFCSVPRlynriydGITSAVKSSGVVKKRLFeIAYNSKKQ 390
Cdd:PRK05677 260 LYHIY---------------AF----TFHCMAMMLIGNHNILISNPR-------DLPAMVKELGKWKFSGF-VGLNTLFV 312
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327099 391 AIINGRTpsafWDKLVFNKIKEKLggrvrfmgSGASPLSPDVMDFLRICFGCSVREGYGMTETSCVISAMDDGDNLSGHV 470
Cdd:PRK05677 313 ALCNNEA----FRKLDFSALKLTL--------SGGMALQLATAERWKEVTGCAICEGYGMTETSPVVSVNPSQAIQVGTI 380
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327099 471 GSPNPACEVKLVDvpemnytSDDQPYPRGEI---CVRGPIIFKGYYKDEEQTREILDGDGWLHTGDIGLWLPGGRLKIID 547
Cdd:PRK05677 381 GIPVPSTLCKVID-------DDGNELPLGEVgelCVKGPQVMKGYWQRPEATDEILDSDGWLKTGDIALIQEDGYMRIVD 453
|
330 340 350
....*....|....*....|....*....|..
gi 22327099 548 RKKNIFkLAQGEYIAPEKIENVYTKCRFVSQC 579
Cdd:PRK05677 454 RKKDMI-LVSGFNVYPNELEDVLAALPGVLQC 484
|
|
| Acs |
COG0365 |
Acyl-coenzyme A synthetase/AMP-(fatty) acid ligase [Lipid transport and metabolism]; |
120-569 |
1.28e-40 |
|
Acyl-coenzyme A synthetase/AMP-(fatty) acid ligase [Lipid transport and metabolism];
Pssm-ID: 440134 [Multi-domain] Cd Length: 565 Bit Score: 156.81 E-value: 1.28e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327099 120 TYGEAASERQAIGSGLLFHGVNQGDCVGLYFINRPEWLVVDHACA---AysfVSVPLYDTLGPDAVKFVVNHANLQAIFC 196
Cdd:COG0365 41 TYAELRREVNRFANALRALGVKKGDRVAIYLPNIPEAVIAMLACArigA---VHSPVFPGFGAEALADRIEDAEAKVLIT 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327099 197 VPQTLNILLSF---------LAEIPSIRLIVVVGGADEHLPslPRGTgvtiVSYQKLLsQGRSSLHPFSPPKPEDIATIC 267
Cdd:COG0365 118 ADGGLRGGKVIdlkekvdeaLEELPSLEHVIVVGRTGADVP--MEGD----LDWDELL-AAASAEFEPEPTDADDPLFIL 190
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327099 268 YTSGTTGTPKGVVLTHGNLIANVAGSS-----VEAE---FFPSDV-------YISYLPLAHiyeRANQIMgvYGGVAVGF 332
Cdd:COG0365 191 YTSGTTGKPKGVVHTHGGYLVHAATTAkyvldLKPGdvfWCTADIgwatghsYIVYGPLLN---GATVVL--YEGRPDFP 265
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327099 333 YQGDVFKLMDDFavlRPTIFCSVPRLYnriydgitsavkssgvvkkRLFeiaynsKKQaiinGRTPSAFWDkLVfnkike 412
Cdd:COG0365 266 DPGRLWELIEKY---GVTVFFTAPTAI-------------------RAL------MKA----GDEPLKKYD-LS------ 306
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327099 413 klggRVRFMGSGASPLSPDVMDFLRICFGCSVREGYGMTET-SCVISAMDDGDNLSGHVGSPNPACEVKLVDvpemnytS 491
Cdd:COG0365 307 ----SLRLLGSAGEPLNPEVWEWWYEAVGVPIVDGWGQTETgGIFISNLPGLPVKPGSMGKPVPGYDVAVVD-------E 375
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327099 492 DDQPYPR---GEICVRGPI--IFKGYYKDEEQTREILDG--DGWLHTGDIGLWLPGGRLKIIDRKKNIFKLAqGEYIAPE 564
Cdd:COG0365 376 DGNPVPPgeeGELVIKGPWpgMFRGYWNDPERYRETYFGrfPGWYRTGDGARRDEDGYFWILGRSDDVINVS-GHRIGTA 454
|
....*
gi 22327099 565 KIENV 569
Cdd:COG0365 455 EIESA 459
|
|
| PLN02246 |
PLN02246 |
4-coumarate--CoA ligase |
110-567 |
1.51e-40 |
|
4-coumarate--CoA ligase
Pssm-ID: 215137 [Multi-domain] Cd Length: 537 Bit Score: 156.29 E-value: 1.51e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327099 110 DGTIGEYswMTYGEAASERQAIGSGLLFHGVNQGDCVGLYFINRPEWlvvdhacaAYSFvsvplydtLGPDAVKFVVNHA 189
Cdd:PLN02246 44 DGATGRV--YTYADVELLSRRVAAGLHKLGIRQGDVVMLLLPNCPEF--------VLAF--------LGASRRGAVTTTA 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327099 190 NlqaIFCVPQTLnillSFLAEIPSIRLIVVVGGADEHLPSLPRGTGVTIVSYQKL---------LSQGRSSLHPFSPPKP 260
Cdd:PLN02246 106 N---PFYTPAEI----AKQAKASGAKLIITQSCYVDKLKGLAEDDGVTVVTIDDPpegclhfseLTQADENELPEVEISP 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327099 261 EDIATICYTSGTTGTPKGVVLTHGNLIANVAgSSVEAE-----FFPSDVYISYLPLAHIYErANQIM--GVYGGVAVGFY 333
Cdd:PLN02246 179 DDVVALPYSSGTTGLPKGVMLTHKGLVTSVA-QQVDGEnpnlyFHSDDVILCVLPMFHIYS-LNSVLlcGLRVGAAILIM 256
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327099 334 QG-DVFKLMDDFAVLRPTIFCSVPRLynriydgITSAVKSSGVVKKRLFEIaynskkqaiingrtpsafwdklvfnkike 412
Cdd:PLN02246 257 PKfEIGALLELIQRHKVTIAPFVPPI-------VLAIAKSPVVEKYDLSSI----------------------------- 300
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327099 413 klggrvRFMGSGASPLSPDVMDFLRICF-GCSVREGYGMTETSCVIS-----AMDDGDNLSGHVGSPNPACEVKLVDvPE 486
Cdd:PLN02246 301 ------RMVLSGAAPLGKELEDAFRAKLpNAVLGQGYGMTEAGPVLAmclafAKEPFPVKSGSCGTVVRNAELKIVD-PE 373
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327099 487 mnyTSDDQPYPR-GEICVRGPIIFKGYYKDEEQTREILDGDGWLHTGDIGLWLPGGRLKIIDRKKNIFKLaQGEYIAPEK 565
Cdd:PLN02246 374 ---TGASLPRNQpGEICIRGPQIMKGYLNDPEATANTIDKDGWLHTGDIGYIDDDDELFIVDRLKELIKY-KGFQVAPAE 449
|
..
gi 22327099 566 IE 567
Cdd:PLN02246 450 LE 451
|
|
| PRK12583 |
PRK12583 |
acyl-CoA synthetase; Provisional |
74-567 |
5.25e-40 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 237145 [Multi-domain] Cd Length: 558 Bit Score: 154.93 E-value: 5.25e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327099 74 VSRFPDHPEIGTLHdnfvhavetyaenkyLGTRvrsdgtigeYSWMTYGEAASErqaIGSGLLFHGVNQGDCVGLYFINR 153
Cdd:PRK12583 28 VARFPDREALVVRH---------------QALR---------YTWRQLADAVDR---LARGLLALGVQPGDRVGIWAPNC 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327099 154 PEWLVVDHACAAYSFVSVPLYDTLGPDAVKFVVNHANLQAIFCVP-----QTLNILLSFL-------------AEIPSIR 215
Cdd:PRK12583 81 AEWLLTQFATARIGAILVNINPAYRASELEYALGQSGVRWVICADafktsDYHAMLQELLpglaegqpgalacERLPELR 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327099 216 LIVVVGGAD-EHLPSLP----RGTGVTivsyQKLLSQGRSSLHPfsppkpEDIATICYTSGTTGTPKGVVLTHGNLIANV 290
Cdd:PRK12583 161 GVVSLAPAPpPGFLAWHelqaRGETVS----REALAERQASLDR------DDPINIQYTSGTTGFPKGATLSHHNILNNG 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327099 291 AGSSVEAEFFPSDVYISYLPLAHIYeraNQIMGVYGGVAVG---FYQGDVFklmDDFAVLRptifcsvprlynriydgit 367
Cdd:PRK12583 231 YFVAESLGLTEHDRLCVPVPLYHCF---GMVLANLGCMTVGaclVYPNEAF---DPLATLQ------------------- 285
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327099 368 savkssgvvkkrlfeiAYNSKKQAIINGrTPSAFWDKLVFNKIKEKLGGRVRFMGSGASPLSPDVMDFLRICFGCS-VRE 446
Cdd:PRK12583 286 ----------------AVEEERCTALYG-VPTMFIAELDHPQRGNFDLSSLRTGIMAGAPCPIEVMRRVMDEMHMAeVQI 348
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327099 447 GYGMTETSCVI---SAMDDGDNLSGHVGSPNPACEVKLVDvpemnytSDDQPYPRGEI---CVRGPIIFKGYYKDEEQTR 520
Cdd:PRK12583 349 AYGMTETSPVSlqtTAADDLERRVETVGRTQPHLEVKVVD-------PDGATVPRGEIgelCTRGYSVMKGYWNNPEATA 421
|
490 500 510 520
....*....|....*....|....*....|....*....|....*..
gi 22327099 521 EILDGDGWLHTGDIGLWLPGGRLKIIDRKKNIFkLAQGEYIAPEKIE 567
Cdd:PRK12583 422 ESIDEDGWMHTGDLATMDEQGYVRIVGRSKDMI-IRGGENIYPREIE 467
|
|
| AAS_C |
cd05909 |
C-terminal domain of the acyl-acyl carrier protein synthetase (also called ... |
119-567 |
1.22e-37 |
|
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: 147.09 E-value: 1.22e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327099 119 MTYGEAASERQAIGSgLLFHGVNQGDCVGLYFINRPEWLVVDHACAAYSFVSVPLYDTLGPDAVKFVVNHANLQAIFCVP 198
Cdd:cd05909 8 LTYRKLLTGAIALAR-KLAKMTKEGENVGVMLPPSAGGALANFALALSGKVPVMLNYTAGLRELRACIKLAGIKTVLTSK 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327099 199 Q---TLNILLSFLAEIPsIRLIVV------VGGADEhlpsLPRGTGVTIVSYQKLLSQGRSslhpfsPPKPEDIATICYT 269
Cdd:cd05909 87 QfieKLKLHHLFDVEYD-ARIVYLedlrakISKADK----CKAFLAGKFPPKWLLRIFGVA------PVQPDDPAVILFT 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327099 270 SGTTGTPKGVVLTHGNLIANVAGSSVEAEFFPSDVYISYLPLAHIYeranqimgvyggvavGFYQGDVFKLMDDFAVL-- 347
Cdd:cd05909 156 SGSEGLPKGVVLSHKNLLANVEQITAIFDPNPEDVVFGALPFFHSF---------------GLTGCLWLPLLSGIKVVfh 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327099 348 -RPTIFCSVPRLynrIYDgitsavkssgvvkkrlfeiaynskKQAIINGRTPSaFWDKLVFNKIKEKLGgRVRFMGSGAS 426
Cdd:cd05909 221 pNPLDYKKIPEL---IYD------------------------KKATILLGTPT-FLRGYARAAHPEDFS-SLRLVVAGAE 271
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327099 427 PLSPDVMDFLRICFGCSVREGYGMTETSCVISA-MDDGDNLSGHVGSPNPACEVKLVDVPemnytsDDQPYPRGE---IC 502
Cdd:cd05909 272 KLKDTLRQEFQEKFGIRILEGYGTTECSPVISVnTPQSPNKEGTVGRPLPGMEVKIVSVE------THEEVPIGEgglLL 345
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 22327099 503 VRGPIIFKGYYKDEEQTREILdGDGWLHTGDIGLWLPGGRLKIIDRKKNIFKLAqGEYIAPEKIE 567
Cdd:cd05909 346 VRGPNVMLGYLNEPELTSFAF-GDGWYDTGDIGKIDGEGFLTITGRLSRFAKIA-GEMVSLEAIE 408
|
|
| ttLC_FACS_AlkK_like |
cd12119 |
Fatty acyl-CoA synthetases similar to LC-FACS from Thermus thermophiles; This family includes ... |
110-569 |
4.51e-37 |
|
Fatty acyl-CoA synthetases similar to LC-FACS from Thermus thermophiles; This family includes fatty acyl-CoA synthetases that can activate medium-chain to long-chain fatty acids. They catalyze the ATP-dependent acylation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. The fatty acyl-CoA synthetases are responsible for fatty acid degradation as well as physiological regulation of cellular functions via the production of fatty acyl-CoA esters. The fatty acyl-CoA synthetase from Thermus thermophiles in this family catalyzes the long-chain fatty acid, myristoyl acid, while another member in this family, the AlkK protein identified from Pseudomonas oleovorans, targets medium chain fatty acids. This family also includes uncharacterized FACS proteins.
Pssm-ID: 341284 [Multi-domain] Cd Length: 518 Bit Score: 145.85 E-value: 4.51e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327099 110 DGTIGEYSWMTYGEAAseRQaIGSGLLFHGVNQGDCVGLYFINRPEWLVVDHACAAYSFVSVPLYDTLGPDAVKFVVNHA 189
Cdd:cd12119 20 EGEVHRYTYAEVAERA--RR-LANALRRLGVKPGDRVATLAWNTHRHLELYYAVPGMGAVLHTINPRLFPEQIAYIINHA 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327099 190 NLQAIFCVPQTLNILLSFLAEIPSIRLIVVVGGADEHLPSlprgTGVTIVSYQKLLSQGrSSLHPFsPPKPE-DIATICY 268
Cdd:cd12119 97 EDRVVFVDRDFLPLLEAIAPRLPTVEHVVVMTDDAAMPEP----AGVGVLAYEELLAAE-SPEYDW-PDFDEnTAAAICY 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327099 269 TSGTTGTPKGVVLTHGNLI------ANVAGSSVEAeffpSDVYISYLPLAHiyerANQiMGV-YGGVAVG--------FY 333
Cdd:cd12119 171 TSGTTGNPKGVVYSHRSLVlhamaaLLTDGLGLSE----SDVVLPVVPMFH----VNA-WGLpYAAAMVGaklvlpgpYL 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327099 334 QGDV-FKLMDDfavLRPTIFCSVPRlynrIYDGITSAVKSsgvvkkrlfeiaynskkqaiiNGRTPSAFWdKLVfnkike 412
Cdd:cd12119 242 DPASlAELIER---EGVTFAAGVPT----VWQGLLDHLEA---------------------NGRDLSSLR-RVV------ 286
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327099 413 klggrvrfmgSGASPLSPDVMD-FLRIcfGCSVREGYGMTETSCVISA-----------MDDGDNLSGHVGSPNPACEVK 480
Cdd:cd12119 287 ----------IGGSAVPRSLIEaFEER--GVRVIHAWGMTETSPLGTVarppsehsnlsEDEQLALRAKQGRPVPGVELR 354
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327099 481 LVDVpemnytsDDQPYPR-----GEICVRGPIIFKGYYKDEEQTREiLDGDGWLHTGDIGLWLPGGRLKIIDRKKNIFKL 555
Cdd:cd12119 355 IVDD-------DGRELPWdgkavGELQVRGPWVTKSYYKNDEESEA-LTEDGWLRTGDVATIDEDGYLTITDRSKDVIKS 426
|
490
....*....|....
gi 22327099 556 AqGEYIAPEKIENV 569
Cdd:cd12119 427 G-GEWISSVELENA 439
|
|
| Firefly_Luc |
cd17642 |
insect luciferase, similar to plant 4-coumarate: CoA ligases; This family contains insect ... |
78-569 |
5.79e-36 |
|
insect luciferase, similar to plant 4-coumarate: CoA ligases; This family contains insect firefly luciferases that share significant sequence similarity to plant 4-coumarate:coenzyme A ligases, despite their functional diversity. Luciferase catalyzes the production of light in the presence of MgATP, molecular oxygen, and luciferin. In the first step, luciferin is activated by acylation of its carboxylate group with ATP, resulting in an enzyme-bound luciferyl adenylate. In the second step, luciferyl adenylate reacts with molecular oxygen, producing an enzyme-bound excited state product (Luc=O*) and releasing AMP. This excited-state product then decays to the ground state (Luc=O), emitting a quantum of visible light.
Pssm-ID: 341297 [Multi-domain] Cd Length: 532 Bit Score: 142.67 E-value: 5.79e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327099 78 PDHP-EIGTLHDNFVHAVETYAenKYLGTRVRSDGTIG-EYSWMTYGEAASErqaIGSGLLFHGVNQGDCVGLYFINRPE 155
Cdd:cd17642 7 PFYPlEDGTAGEQLHKAMKRYA--SVPGTIAFTDAHTGvNYSYAEYLEMSVR---LAEALKKYGLKQNDRIAVCSENSLQ 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327099 156 WLVVDHACAAYSFVSVPLYDTLGPDAVKFVVNHANLQAIFCVPQTLNILLSFLAEIPSIRLIVVVGGADEHlpslpRGtg 235
Cdd:cd17642 82 FFLPVIAGLFIGVGVAPTNDIYNERELDHSLNISKPTIVFCSKKGLQKVLNVQKKLKIIKTIIILDSKEDY-----KG-- 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327099 236 vtivsYQKLLSQGRSSLHP------FSPP---KPEDIATICYTSGTTGTPKGVVLTHGNLIANVAGS---SVEAEFFPSD 303
Cdd:cd17642 155 -----YQCLYTFITQNLPPgfneydFKPPsfdRDEQVALIMNSSGSTGLPKGVQLTHKNIVARFSHArdpIFGNQIIPDT 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327099 304 VYISYLPLAHIYERANQImgvyGGVAVGF-------YQGDVF-KLMDDF----AVLRPTIFCSVPRlynriydgitsavk 371
Cdd:cd17642 230 AILTVIPFHHGFGMFTTL----GYLICGFrvvlmykFEEELFlRSLQDYkvqsALLVPTLFAFFAK-------------- 291
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327099 372 ssgvvkkrlfeiaynskkqaiingrtpSAFWDKLVFNKIKEklggrvrfMGSGASPLSPDVMDFLRICFGCS-VREGYGM 450
Cdd:cd17642 292 ---------------------------STLVDKYDLSNLHE--------IASGGAPLSKEVGEAVAKRFKLPgIRQGYGL 336
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327099 451 TETSCVISAMDDGDNLSGHVGSPNPACEVKLVDvPEMNYTSDdqPYPRGEICVRGPIIFKGYYKDEEQTREILDGDGWLH 530
Cdd:cd17642 337 TETTSAILITPEGDDKPGAVGKVVPFFYAKVVD-LDTGKTLG--PNERGELCVKGPMIMKGYVNNPEATKALIDKDGWLH 413
|
490 500 510
....*....|....*....|....*....|....*....
gi 22327099 531 TGDIGLWLPGGRLKIIDRKKNIFKLaQGEYIAPEKIENV 569
Cdd:cd17642 414 SGDIAYYDEDGHFFIVDRLKSLIKY-KGYQVPPAELESI 451
|
|
| PRK13295 |
PRK13295 |
cyclohexanecarboxylate-CoA ligase; Reviewed |
85-596 |
3.30e-35 |
|
cyclohexanecarboxylate-CoA ligase; Reviewed
Pssm-ID: 171961 [Multi-domain] Cd Length: 547 Bit Score: 140.57 E-value: 3.30e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327099 85 TLHDNFVHAVETyAENKYLGTRVRSDGtiGEYSWMTYGEAASERQAIGSGLLFHGVNQGDCVGLYFINRPEWLVVDHACA 164
Cdd:PRK13295 25 TINDDLDACVAS-CPDKTAVTAVRLGT--GAPRRFTYRELAALVDRVAVGLARLGVGRGDVVSCQLPNWWEFTVLYLACS 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327099 165 AYSFVSVPLYDTLGPDAVKFVVNHANlQAIFCVPQTLN------ILLSFLAEIPSIRLIVVVGGADEhlpslprgtgvti 238
Cdd:PRK13295 102 RIGAVLNPLMPIFRERELSFMLKHAE-SKVLVVPKTFRgfdhaaMARRLRPELPALRHVVVVGGDGA------------- 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327099 239 VSYQKLLSQGRSSLHPFSP-------PKPEDIATICYTSGTTGTPKGVVLTHGNLIANVAGSSVEAEFFPSDVYISYLPL 311
Cdd:PRK13295 168 DSFEALLITPAWEQEPDAPailarlrPGPDDVTQLIYTSGTTGEPKGVMHTANTLMANIVPYAERLGLGADDVILMASPM 247
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327099 312 AHIyeranqimgvyggvaVGFYQGDVFKLMddfavLRPTIfcsvprLYNRIYDGITSA--VKSSGVVkkrlFEIAynskk 389
Cdd:PRK13295 248 AHQ---------------TGFMYGLMMPVM-----LGATA------VLQDIWDPARAAelIRTEGVT----FTMA----- 292
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327099 390 qaiingRTPsaFWDKLVFNkikEKLGGRV-----RFMGSGAsPLSPDVMDFLRICFGCSVREGYGMTETSCV--ISAMDD 462
Cdd:PRK13295 293 ------STP--FLTDLTRA---VKESGRPvsslrTFLCAGA-PIPGALVERARAALGAKIVSAWGMTENGAVtlTKLDDP 360
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327099 463 GDNLSGHVGSPNPACEVKLVDvpemnytSDDQPYPRGEI---CVRGPIIFKGYYKDEEQTREilDGDGWLHTGDIGLWLP 539
Cdd:PRK13295 361 DERASTTDGCPLPGVEVRVVD-------ADGAPLPAGQIgrlQVRGCSNFGGYLKRPQLNGT--DADGWFDTGDLARIDA 431
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*..
gi 22327099 540 GGRLKIIDRKKNIFkLAQGEYIAPEKIENVYTKCRFVSQcfihgdsfnsslVAIVSV 596
Cdd:PRK13295 432 DGYIRISGRSKDVI-IRGGENIPVVEIEALLYRHPAIAQ------------VAIVAY 475
|
|
| PRK07786 |
PRK07786 |
long-chain-fatty-acid--CoA ligase; Validated |
89-569 |
3.86e-35 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 169098 [Multi-domain] Cd Length: 542 Bit Score: 140.30 E-value: 3.86e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327099 89 NFVHAVETYAENKYLGTRVRSDGTIgeyswMTYGEAASERQAIGSGLLFHGVNQGDCVGLYFINRPEWLVVDHACAAYSF 168
Cdd:PRK07786 18 NWVNQLARHALMQPDAPALRFLGNT-----TTWRELDDRVAALAGALSRRGVGFGDRVLILMLNRTEFVESVLAANMLGA 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327099 169 VSVPLYDTLGPDAVKFVVNHANLQAIFCVPQTLNILLSFLAEIPSIRLIVVVGGADEHlpslprgtgvTIVSYQKLLSQg 248
Cdd:PRK07786 93 IAVPVNFRLTPPEIAFLVSDCGAHVVVTEAALAPVATAVRDIVPLLSTVVVAGGSSDD----------SVLGYEDLLAE- 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327099 249 rsslhPFSPPKPEDI-----ATICYTSGTTGTPKGVVLTHGNLIAN-VAGSSVEAEFFPSDVYISYLPLAHIYERANQIM 322
Cdd:PRK07786 162 -----AGPAHAPVDIpndspALIMYTSGTTGRPKGAVLTHANLTGQaMTCLRTNGADINSDVGFVGVPLFHIAGIGSMLP 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327099 323 GVYGGVAVGFYQGDVF---KLMDDFAVLRPT-IFCsVPrlynriydgitsavkssgvvkkrlfeiaynSKKQAIINGRTP 398
Cdd:PRK07786 237 GLLLGAPTVIYPLGAFdpgQLLDVLEAEKVTgIFL-VP------------------------------AQWQAVCAEQQA 285
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327099 399 SAfwdklvfnkikEKLggRVRFMGSGASPLSPDVMDFLRICF-GCSVREGYGMTETSCVISAMDDGDNLS--GHVGSPNP 475
Cdd:PRK07786 286 RP-----------RDL--ALRVLSWGAAPASDTLLRQMAATFpEAQILAAFGQTEMSPVTCMLLGEDAIRklGSVGKVIP 352
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327099 476 ACEVKLVDvPEMNytsDDQPYPRGEICVRGPIIFKGYYKDEEQTREILDGdGWLHTGDIGLWLPGGRLKIIDRKKNIFkL 555
Cdd:PRK07786 353 TVAARVVD-ENMN---DVPVGEVGEIVYRAPTLMSGYWNNPEATAEAFAG-GWFHSGDLVRQDEEGYVWVVDRKKDMI-I 426
|
490
....*....|....
gi 22327099 556 AQGEYIAPEKIENV 569
Cdd:PRK07786 427 SGGENIYCAEVENV 440
|
|
| PRK12492 |
PRK12492 |
long-chain-fatty-acid--CoA ligase; Provisional |
229-579 |
1.21e-34 |
|
long-chain-fatty-acid--CoA ligase; Provisional
Pssm-ID: 171539 [Multi-domain] Cd Length: 562 Bit Score: 139.19 E-value: 1.21e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327099 229 SLPRGtgvtiVSYQKLLSQGRSSLHPFSPPKPEDIATICYTSGTTGTPKGVVLTHGNLIANVA------------GSSVE 296
Cdd:PRK12492 180 HLPQA-----VPFKQALRQGRGLSLKPVPVGLDDIAVLQYTGGTTGLAKGAMLTHGNLVANMLqvraclsqlgpdGQPLM 254
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327099 297 AEffPSDVYISYLPLAHIYE-RAN-QIMGVYGGvavgfyqgdvfklmddfavlrPTIFCSVPRlynriydGITSAVKSsg 374
Cdd:PRK12492 255 KE--GQEVMIAPLPLYHIYAfTANcMCMMVSGN---------------------HNVLITNPR-------DIPGFIKE-- 302
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327099 375 vVKKRLFE--IAYNSKKQAIINgrTPSafWDKLVFNKIKeklggrvrFMGSGASPLSPDVMDFLRICFGCSVREGYGMTE 452
Cdd:PRK12492 303 -LGKWRFSalLGLNTLFVALMD--HPG--FKDLDFSALK--------LTNSGGTALVKATAERWEQLTGCTIVEGYGLTE 369
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327099 453 TSCVISAMDDGdNLS--GHVGSPNPACEVKLVDvpemnYTSDDQPY-PRGEICVRGPIIFKGYYKDEEQTREILDGDGWL 529
Cdd:PRK12492 370 TSPVASTNPYG-ELArlGTVGIPVPGTALKVID-----DDGNELPLgERGELCIKGPQVMKGYWQQPEATAEALDAEGWF 443
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|
gi 22327099 530 HTGDIGLWLPGGRLKIIDRKKNIFkLAQGEYIAPEKIENVYTKCRFVSQC 579
Cdd:PRK12492 444 KTGDIAVIDPDGFVRIVDRKKDLI-IVSGFNVYPNEIEDVVMAHPKVANC 492
|
|
| PRK08315 |
PRK08315 |
AMP-binding domain protein; Validated |
85-568 |
1.63e-34 |
|
AMP-binding domain protein; Validated
Pssm-ID: 236236 [Multi-domain] Cd Length: 559 Bit Score: 138.79 E-value: 1.63e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327099 85 TLHDNFVHAVETYAENKYLGTRVRsdgtigEYSWmTYGEAASERQAIGSGLLFHGVNQGDCVGLYFINRPEWLVVDHACA 164
Cdd:PRK08315 17 TIGQLLDRTAARYPDREALVYRDQ------GLRW-TYREFNEEVDALAKGLLALGIEKGDRVGIWAPNVPEWVLTQFATA 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327099 165 AYSFVSV---PLYDTlgpDAVKFVVNHANLQAIFCVP--------QTLNILLSFLAE----------IPSIRLIVVVGGA 223
Cdd:PRK08315 90 KIGAILVtinPAYRL---SELEYALNQSGCKALIAADgfkdsdyvAMLYELAPELATcepgqlqsarLPELRRVIFLGDE 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327099 224 DehlpslPRGTgvtiVSYQKLLSQGR-----------SSLHPfsppkpEDIATICYTSGTTGTPKGVVLTHGNLIANvaG 292
Cdd:PRK08315 167 K------HPGM----LNFDELLALGRavddaelaarqATLDP------DDPINIQYTSGTTGFPKGATLTHRNILNN--G 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327099 293 SSV-EA-EFFPSD-VYISyLPLAHIYeraNQIMGVYGGVAVG---FYQGDVFklmDDFAVLR-------------PTIFC 353
Cdd:PRK08315 229 YFIgEAmKLTEEDrLCIP-VPLYHCF---GMVLGNLACVTHGatmVYPGEGF---DPLATLAaveeerctalygvPTMFI 301
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327099 354 SV---PRLYNriYDgitsavkssgvvkkrlfeiaYNSKKQAIINGRT-PSAfwdklVFNKIKEKLGgrvrfmgsgaspls 429
Cdd:PRK08315 302 AEldhPDFAR--FD--------------------LSSLRTGIMAGSPcPIE-----VMKRVIDKMH-------------- 340
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327099 430 pdvMDFLRICfgcsvregYGMTETSCVI--SAMDDG-DNLSGHVGSPNPACEVKLVDvPEMNytsddQPYPR---GEICV 503
Cdd:PRK08315 341 ---MSEVTIA--------YGMTETSPVStqTRTDDPlEKRVTTVGRALPHLEVKIVD-PETG-----ETVPRgeqGELCT 403
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 22327099 504 RGPIIFKGYYKDEEQTREILDGDGWLHTGDIGLWLPGGRLKIIDRKKNIFkLAQGEYIAPEKIEN 568
Cdd:PRK08315 404 RGYSVMKGYWNDPEKTAEAIDADGWMHTGDLAVMDEEGYVNIVGRIKDMI-IRGGENIYPREIEE 467
|
|
| PRK07059 |
PRK07059 |
Long-chain-fatty-acid--CoA ligase; Validated |
119-579 |
2.96e-34 |
|
Long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 235923 [Multi-domain] Cd Length: 557 Bit Score: 137.84 E-value: 2.96e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327099 119 MTYGEAASERQAIGSGLLFHGVNQGDCVGLYFINRPEWLVVDHAC--AAYSFVSV-PLY----------DTlGPDAVKFV 185
Cdd:PRK07059 49 ITYGELDELSRALAAWLQSRGLAKGARVAIMMPNVLQYPVAIAAVlrAGYVVVNVnPLYtprelehqlkDS-GAEAIVVL 127
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327099 186 VNHAN-LQAIFCVPQTLNILLSFLAEIPSIR-LIV--VVGGADEHLP--SLPRGtgvtiVSYQKLLSQGRSSlhPFSPPK 259
Cdd:PRK07059 128 ENFATtVQQVLAKTAVKHVVVASMGDLLGFKgHIVnfVVRRVKKMVPawSLPGH-----VRFNDALAEGARQ--TFKPVK 200
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327099 260 --PEDIATICYTSGTTGTPKGVVLTHGNLIANVAGSSV---EAEFFPSDV----YISYLPLAHIYE-RANQIMGV-YGGV 328
Cdd:PRK07059 201 lgPDDVAFLQYTGGTTGVSKGATLLHRNIVANVLQMEAwlqPAFEKKPRPdqlnFVCALPLYHIFAlTVCGLLGMrTGGR 280
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327099 329 AVgfyqgdvfklmddfavLRPTifcsvPRlynriydGITSAVKSSGVVKKRLFeIAYNSKKQAIINgrtpSAFWDKLVFN 408
Cdd:PRK07059 281 NI----------------LIPN-----PR-------DIPGFIKELKKYQVHIF-PAVNTLYNALLN----NPDFDKLDFS 327
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327099 409 KIKEKLGGrvrfmgsGASPLSPDVMDFLRICfGCSVREGYGMTETSCVISAMD-DGDNLSGHVGSPNPACEVKLVDvPEM 487
Cdd:PRK07059 328 KLIVANGG-------GMAVQRPVAERWLEMT-GCPITEGYGLSETSPVATCNPvDATEFSGTIGLPLPSTEVSIRD-DDG 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327099 488 NYTSDDQPyprGEICVRGPIIFKGYYKDEEQTREILDGDGWLHTGDIGLWLPGGRLKIIDRKKNIFkLAQGEYIAPEKIE 567
Cdd:PRK07059 399 NDLPLGEP---GEICIRGPQVMAGYWNRPDETAKVMTADGFFRTGDVGVMDERGYTKIVDRKKDMI-LVSGFNVYPNEIE 474
|
490
....*....|..
gi 22327099 568 NVYTKCRFVSQC 579
Cdd:PRK07059 475 EVVASHPGVLEV 486
|
|
| OSB_CoA_lg |
cd05912 |
O-succinylbenzoate-CoA ligase (also known as O-succinylbenzoate-CoA synthase, OSB-CoA ... |
256-570 |
1.62e-33 |
|
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: 133.24 E-value: 1.62e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327099 256 SPPKPEDIATICYTSGTTGTPKGVVLTHGNLIANVAGSSVEAEFFPSDVYISYLPLAHIYERANQIMGVYGGVAVGFYQG 335
Cdd:cd05912 72 SDVKLDDIATIMYTSGTTGKPKGVQQTFGNHWWSAIGSALNLGLTEDDNWLCALPLFHISGLSILMRSVIYGMTVYLVDK 151
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327099 336 -DVFKLMDDFAVLRPTIFCSVPRLYNRIYDgitsavkssgvvkkrlfeiaynskkqaIINGRTPSAFwdklvfnkikekl 414
Cdd:cd05912 152 fDAEQVLHLINSGKVTIISVVPTMLQRLLE---------------------------ILGEGYPNNL------------- 191
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327099 415 ggrvRFMGSGASPLSPDVmdfLRIC--FGCSVREGYGMTETSCVISAM--DDGDNLSGHVGSPNPACEVKLVDvpemnyt 490
Cdd:cd05912 192 ----RCILLGGGPAPKPL---LEQCkeKGIPVYQSYGMTETCSQIVTLspEDALNKIGSAGKPLFPVELKIED------- 257
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327099 491 SDDQPYPRGEICVRGPIIFKGYYKDEEQTREILDgDGWLHTGDIGLWLPGGRLKIIDRKKNIFkLAQGEYIAPEKIENVY 570
Cdd:cd05912 258 DGQPPYEVGEILLKGPNVTKGYLNRPDATEESFE-NGWFKTGDIGYLDEEGFLYVLDRRSDLI-ISGGENIYPAEIEEVL 335
|
|
| CHC_CoA_lg |
cd05903 |
Cyclohexanecarboxylate-CoA ligase (also called cyclohex-1-ene-1-carboxylate:CoA ligase); ... |
120-569 |
4.50e-33 |
|
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: 132.50 E-value: 4.50e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327099 120 TYGEAASERQAIGSGLLFHGVNQGDCVGLYFINRPEWLVVDHACAAYSFVSVPLYDTLGPDAVKFVVNHAnlQAifcvpq 199
Cdd:cd05903 3 TYSELDTRADRLAAGLAALGVGPGDVVAFQLPNWWEFAVLYLACLRIGAVTNPILPFFREHELAFILRRA--KA------ 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327099 200 tlnillsflaeipsiRLIVVvggadehlPSLPRGTgvtivSYQkllsqgrsslhpfspPKPEDIATICYTSGTTGTPKGV 279
Cdd:cd05903 75 ---------------KVFVV--------PERFRQF-----DPA---------------AMPDAVALLLFTSGTTGEPKGV 111
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327099 280 VLTHGNLIANVAGSSVEAEFFPSDVYISYLPLAHIyeranqiMGVYGGVAVGFYQGDVFKLMDDFavlRPTifcsvprly 359
Cdd:cd05903 112 MHSHNTLSASIRQYAERLGLGPGDVFLVASPMAHQ-------TGFVYGFTLPLLLGAPVVLQDIW---DPD--------- 172
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327099 360 nriyDGITSaVKSSGVvkkrlfeiaynskkqAIINGRTPsaFWDKLVfnKIKEKLGGRV---RFMGSGASPLSPDVMDFL 436
Cdd:cd05903 173 ----KALAL-MREHGV---------------TFMMGATP--FLTDLL--NAVEEAGEPLsrlRTFVCGGATVPRSLARRA 228
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327099 437 RICFGCSVREGYGMTETSCVISAMDDGD-NLSGHV-GSPNPACEVKLVDvpemNYTSDDQPYPRGEICVRGPIIFKGYYK 514
Cdd:cd05903 229 AELLGAKVCSAYGSTECPGAVTSITPAPeDRRLYTdGRPLPGVEIKVVD----DTGATLAPGVEGELLSRGPSVFLGYLD 304
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*
gi 22327099 515 DEEQTREILDgDGWLHTGDIGLWLPGGRLKIIDRKKNIFkLAQGEYIAPEKIENV 569
Cdd:cd05903 305 RPDLTADAAP-EGWFRTGDLARLDEDGYLRITGRSKDII-IRGGENIPVLEVEDL 357
|
|
| PRK07529 |
PRK07529 |
AMP-binding domain protein; Validated |
136-552 |
7.53e-33 |
|
AMP-binding domain protein; Validated
Pssm-ID: 236043 [Multi-domain] Cd Length: 632 Bit Score: 134.70 E-value: 7.53e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327099 136 LFH--GVNQGDCVGLYFINRPEWLVVDHACAAYSFVsVPLYDTLGPDAVKFVVNHANLQAIFCV---PQTlNI---LLSF 207
Cdd:PRK07529 74 LLHslGVGPGDVVAFLLPNLPETHFALWGGEAAGIA-NPINPLLEPEQIAELLRAAGAKVLVTLgpfPGT-DIwqkVAEV 151
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327099 208 LAEIPSIRLIVVVGGAD-------EHLPSLPRGTGVTIVSYQKLLSQGRSSLHPF-SPPKPEDIATICYTSGTTGTPKGV 279
Cdd:PRK07529 152 LAALPELRTVVEVDLARylpgpkrLAVPLIRRKAHARILDFDAELARQPGDRLFSgRPIGPDDVAAYFHTGGTTGMPKLA 231
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327099 280 VLTHGNLIANvAGSSVEAEFF-PSDVYISYLPLAHIYeranqimGVYGGVAVGFYQGD--VF---------KLMDDFAVL 347
Cdd:PRK07529 232 QHTHGNEVAN-AWLGALLLGLgPGDTVFCGLPLFHVN-------ALLVTGLAPLARGAhvVLatpqgyrgpGVIANFWKI 303
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327099 348 ----RPTIFCSVPrlynriydgitsavkssgvvkkrlfeIAYNSKKQAIINGRTPSAfwdklvfnkikeklggrVRFMGS 423
Cdd:PRK07529 304 veryRINFLSGVP--------------------------TVYAALLQVPVDGHDISS-----------------LRYALC 340
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327099 424 GASPLSPDVMDFLRICFGCSVREGYGMTETSCViSAMD--DGDNLSGHVGSPNPACEVKLVDV-PEMNYTSDDQPYPRGE 500
Cdd:PRK07529 341 GAAPLPVEVFRRFEAATGVRIVEGYGLTEATCV-SSVNppDGERRIGSVGLRLPYQRVRVVILdDAGRYLRDCAVDEVGV 419
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 22327099 501 ICVRGPIIFKGYYkDEEQTREILDGDGWLHTGDIG-------LWLPgGRLK--IIDRKKNI 552
Cdd:PRK07529 420 LCIAGPNVFSGYL-EAAHNKGLWLEDGWLNTGDLGridadgyFWLT-GRAKdlIIRGGHNI 478
|
|
| PLN02330 |
PLN02330 |
4-coumarate--CoA ligase-like 1 |
75-569 |
1.61e-32 |
|
4-coumarate--CoA ligase-like 1
Pssm-ID: 215189 [Multi-domain] Cd Length: 546 Bit Score: 132.80 E-value: 1.61e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327099 75 SRFPDH--PEIGTLHDNFVHAVETYAENKYLGTRVRSDGtigeyswMTYGEAASERQAIGSGLLFHGVNQGDCVGLYFIN 152
Cdd:PLN02330 17 SRYPSVpvPDKLTLPDFVLQDAELYADKVAFVEAVTGKA-------VTYGEVVRDTRRFAKALRSLGLRKGQVVVVVLPN 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327099 153 RPEWLVVdhacaaysfvsvplydTLGPDAVKFVVNHANlqaifcvPQTLNILLSFLAEIPSIRLIVV-------VGGADE 225
Cdd:PLN02330 90 VAEYGIV----------------ALGIMAAGGVFSGAN-------PTALESEIKKQAEAAGAKLIVTndtnygkVKGLGL 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327099 226 HLPSLPRGTGVTIVSYQKLLSQGR--SSLHPFSPPKPEDIATICYTSGTTGTPKGVVLTHGNLIANVAGS--SVEAEFFP 301
Cdd:PLN02330 147 PVIVLGEEKIEGAVNWKELLEAADraGDTSDNEEILQTDLCALPFSSGTTGISKGVMLTHRNLVANLCSSlfSVGPEMIG 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327099 302 SDVYISYLPLAHIYeranQIMGVYggvavgfyqgdvfklmddFAVLR-PTIFCSVPRLYNRIYDG--ITSAVKSSGVVKK 378
Cdd:PLN02330 227 QVVTLGLIPFFHIY----GITGIC------------------CATLRnKGKVVVMSRFELRTFLNalITQEVSFAPIVPP 284
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327099 379 rlfeIAYNSKKQAIIngrtpsafwDKLVFNKIKeklggrVRFMGSGASPLSPDVMDFLRICF-GCSVREGYGMTETSCVi 457
Cdd:PLN02330 285 ----IILNLVKNPIV---------EEFDLSKLK------LQAIMTAAAPLAPELLTAFEAKFpGVQVQEAYGLTEHSCI- 344
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327099 458 sAMDDGDNLSGH-------VGSPNPACEVKLVDvPEmnytsDDQPYPR---GEICVRGPIIFKGYYKDEEQTREILDGDG 527
Cdd:PLN02330 345 -TLTHGDPEKGHgiakknsVGFILPNLEVKFID-PD-----TGRSLPKntpGELCVRSQCVMQGYYNNKEETDRTIDEDG 417
|
490 500 510 520
....*....|....*....|....*....|....*....|..
gi 22327099 528 WLHTGDIGLWLPGGRLKIIDRKKNIFKLaQGEYIAPEKIENV 569
Cdd:PLN02330 418 WLHTGDIGYIDDDGDIFIVDRIKELIKY-KGFQVAPAELEAI 458
|
|
| PRK07787 |
PRK07787 |
acyl-CoA synthetase; Validated |
219-569 |
2.89e-32 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236096 [Multi-domain] Cd Length: 471 Bit Score: 130.88 E-value: 2.89e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327099 219 VVGGADEHLPSLPRgtgVTIVSYqkllsqGRSSlHPFSPPKPEDIATICYTSGTTGTPKGVVLTHGNLIANVAGSSVEAE 298
Cdd:PRK07787 96 WLGPAPDDPAGLPH---VPVRLH------ARSW-HRYPEPDPDAPALIVYTSGTTGPPKGVVLSRRAIAADLDALAEAWQ 165
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327099 299 FFPSDVYISYLPLAHIYeraNQIMGVYGGVAVGfyqGDVFKLM----DDFA---VLRPTIFCSVPRLYNRIYDGITSAvk 371
Cdd:PRK07787 166 WTADDVLVHGLPLFHVH---GLVLGVLGPLRIG---NRFVHTGrptpEAYAqalSEGGTLYFGVPTVWSRIAADPEAA-- 237
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327099 372 ssgvvkkrlfeiaynskkqaiingrtpsafwdklvfnkikEKLGGrVRFMGSGASPLSPDVMDFLRICFGCSVREGYGMT 451
Cdd:PRK07787 238 ----------------------------------------RALRG-ARLLVSGSAALPVPVFDRLAALTGHRPVERYGMT 276
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327099 452 ETSCVISAMDDGDNLSGHVGSPNPACEVKLVDVPEMNYTSDDQPYprGEICVRGPIIFKGYYKDEEQTREILDGDGWLHT 531
Cdd:PRK07787 277 ETLITLSTRADGERRPGWVGLPLAGVETRLVDEDGGPVPHDGETV--GELQVRGPTLFDGYLNRPDATAAAFTADGWFRT 354
|
330 340 350 360
....*....|....*....|....*....|....*....|....
gi 22327099 532 GDIGLWLPGGRLKIIDR------KKNIFKLAQGEyiapekIENV 569
Cdd:PRK07787 355 GDVAVVDPDGMHRIVGRestdliKSGGYRIGAGE------IETA 392
|
|
| PRK06087 |
PRK06087 |
medium-chain fatty-acid--CoA ligase; |
85-581 |
3.40e-32 |
|
medium-chain fatty-acid--CoA ligase;
Pssm-ID: 180393 [Multi-domain] Cd Length: 547 Bit Score: 131.79 E-value: 3.40e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327099 85 TLHDNFVHAVETYAENKYLgtrvrSDGTIGEYswmTYGEAASERQAIGSGLLFHGVNQGDCVGLYFINRPEWLVVDHACA 164
Cdd:PRK06087 24 SLADYWQQTARAMPDKIAV-----VDNHGASY---TYSALDHAASRLANWLLAKGIEPGDRVAFQLPGWCEFTIIYLACL 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327099 165 AYSFVSVPLYDTLGPDAVKFVVNHANLQAIFC---VPQT--LNILLSFLAEIPSIRLIVVVggaDEHLPSLPRgtgvtiV 239
Cdd:PRK06087 96 KVGAVSVPLLPSWREAELVWVLNKCQAKMFFAptlFKQTrpVDLILPLQNQLPQLQQIVGV---DKLAPATSS------L 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327099 240 SYQKLLSQGrSSLHPFSPPKPEDIATICYTSGTTGTPKGVVLTHGNLIANVAGSSVEAEFFPSDVYISYLPLAHiyeran 319
Cdd:PRK06087 167 SLSQIIADY-EPLTTAITTHGDELAAVLFTSGTEGLPKGVMLTHNNILASERAYCARLNLTWQDVFMMPAPLGH------ 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327099 320 qIMGVYGGVAVGFYQGDVFKLMDDFavlRPTifcSVPRLYNRiydgitsavkssgvvkkrlfeiaynsKKQAIINGRTPS 399
Cdd:PRK06087 240 -ATGFLHGVTAPFLIGARSVLLDIF---TPD---ACLALLEQ--------------------------QRCTCMLGATPF 286
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327099 400 AFwDKLvfnKIKEKLGGRV---RFMGSGASPLSPDVmdfLRICFGCSVR--EGYGMTEtSCVISAMDDGDNLSGHV---G 471
Cdd:PRK06087 287 IY-DLL---NLLEKQPADLsalRFFLCGGTTIPKKV---ARECQQRGIKllSVYGSTE-SSPHAVVNLDDPLSRFMhtdG 358
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327099 472 SPNPACEVKLVDvpemnytSDDQPYPR---GEICVRGPIIFKGYYKDEEQTREILDGDGWLHTGDIGLWLPGGRLKIIDR 548
Cdd:PRK06087 359 YAAAGVEIKVVD-------EARKTLPPgceGEEASRGPNVFMGYLDEPELTARALDEEGWYYSGDLCRMDEAGYIKITGR 431
|
490 500 510
....*....|....*....|....*....|....
gi 22327099 549 KKNIFkLAQGEYIAPEKIENVYTKC-RFVSQCFI 581
Cdd:PRK06087 432 KKDII-VRGGENISSREVEDILLQHpKIHDACVV 464
|
|
| PRK08751 |
PRK08751 |
long-chain fatty acid--CoA ligase; |
119-569 |
5.30e-32 |
|
long-chain fatty acid--CoA ligase;
Pssm-ID: 181546 [Multi-domain] Cd Length: 560 Bit Score: 131.15 E-value: 5.30e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327099 119 MTYGEAASERQAIGSGLLFH-GVNQGDCVGLYFINRPEWLVVDHA--CAAYSFVSV-PLYDtlgPDAVKFVVNHANLQAI 194
Cdd:PRK08751 51 ITYREADQLVEQFAAYLLGElQLKKGDRVALMMPNCLQYPIATFGvlRAGLTVVNVnPLYT---PRELKHQLIDSGASVL 127
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327099 195 FCVPQTLNILLSFLAEIPsIRLIVVVGGADehLPSLPRGTGVTIV-----------------SYQKLLSQGRSSLHPFSP 257
Cdd:PRK08751 128 VVIDNFGTTVQQVIADTP-VKQVITTGLGD--MLGFPKAALVNFVvkyvkklvpeyringaiRFREALALGRKHSMPTLQ 204
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327099 258 PKPEDIATICYTSGTTGTPKGVVLTHGNLIAN-------VAGSSVEAEffPSDVYISYLPLAHIYE-RANQI--MGVYGG 327
Cdd:PRK08751 205 IEPDDIAFLQYTGGTTGVAKGAMLTHRNLVANmqqahqwLAGTGKLEE--GCEVVITALPLYHIFAlTANGLvfMKIGGC 282
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327099 328 VAVGFYQGDVFKLMDDFAVLRPTIFCSVPRLYNRIYDgitsavkssgvvkkrlfeiaynskkqaiingrTPSafWDKLVF 407
Cdd:PRK08751 283 NHLISNPRDMPGFVKELKKTRFTAFTGVNTLFNGLLN--------------------------------TPG--FDQIDF 328
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327099 408 NKIKEKLGGRVRFMGSgasplspdVMDFLRICFGCSVREGYGMTETS--CVISAMDDGDNlSGHVGSPNPACEVKLVDvp 485
Cdd:PRK08751 329 SSLKMTLGGGMAVQRS--------VAERWKQVTGLTLVEAYGLTETSpaACINPLTLKEY-NGSIGLPIPSTDACIKD-- 397
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327099 486 emnytSDDQPYPRGEI---CVRGPIIFKGYYKDEEQTREILDGDGWLHTGDIGLWLPGGRLKIIDRKKNIFkLAQGEYIA 562
Cdd:PRK08751 398 -----DAGTVLAIGEIgelCIKGPQVMKGYWKRPEETAKVMDADGWLHTGDIARMDEQGFVYIVDRKKDMI-LVSGFNVY 471
|
....*..
gi 22327099 563 PEKIENV 569
Cdd:PRK08751 472 PNEIEDV 478
|
|
| FAAL |
cd05931 |
Fatty acyl-AMP ligase (FAAL); FAAL belongs to the class I adenylate forming enzyme family and ... |
110-567 |
6.73e-32 |
|
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: 130.82 E-value: 6.73e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327099 110 DGTIGEYSWMTYGEAASERQAIGSGLLFHGvNQGDCVGLYFINRPEWLVVDHACAAYSFVSVPLYDTLGPDAvkfvvnHA 189
Cdd:cd05931 16 DDEGGREETLTYAELDRRARAIAARLQAVG-KPGDRVLLLAPPGLDFVAAFLGCLYAGAIAVPLPPPTPGRH------AE 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327099 190 NLQAIF--CVPqtlNILLSFLAEIPSIRLIVVVGGADEHLPslprgtgvTIVSYQKLLSQGRSSLHPfsPPKPEDIATIC 267
Cdd:cd05931 89 RLAAILadAGP---RVVLTTAAALAAVRAFAASRPAAGTPR--------LLVVDLLPDTSAADWPPP--SPDPDDIAYLQ 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327099 268 YTSGTTGTPKGVVLTHGNLIANVAGSSVEAEFFPSDVYISYLPLAHiyeranqIMGVYGGVAVGFYQGDVFKLMDDFA-V 346
Cdd:cd05931 156 YTSGSTGTPKGVVVTHRNLLANVRQIRRAYGLDPGDVVVSWLPLYH-------DMGLIGGLLTPLYSGGPSVLMSPAAfL 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327099 347 LRPTIFcsvPRLYNRiYDGITSAVKSsgvvkkrlFeiAYNskkqaiingrtpsafwdkLVFNKIK-EKLGG----RVRFM 421
Cdd:cd05931 229 RRPLRW---LRLISR-YRATISAAPN--------F--AYD------------------LCVRRVRdEDLEGldlsSWRVA 276
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327099 422 GSGASPLSPDVMD-FLRiCF-GC-----SVREGYGMTETSCVISA----------MDDGDNLSGHV-------------- 470
Cdd:cd05931 277 LNGAEPVRPATLRrFAE-AFaPFgfrpeAFRPSYGLAEATLFVSGgppgtgpvvlRVDRDALAGRAvavaaddpaarelv 355
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327099 471 --GSPNPACEVKLVDvPEMNytsddQPYPR---GEICVRGPIIFKGYYKDEEQTREI------LDGDGWLHTGDIGLWLP 539
Cdd:cd05931 356 scGRPLPDQEVRIVD-PETG-----RELPDgevGEIWVRGPSVASGYWGRPEATAETfgalaaTDEGGWLRTGDLGFLHD 429
|
490 500 510
....*....|....*....|....*....|....*
gi 22327099 540 G-----GRLK--IIDRKKNIFklaqgeyiaPEKIE 567
Cdd:cd05931 430 GelyitGRLKdlIIVRGRNHY---------PQDIE 455
|
|
| A_NRPS_TubE_like |
cd05906 |
The adenylation domain (A domain) of a family of nonribosomal peptide synthetases (NRPSs) ... |
78-550 |
8.12e-32 |
|
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: 130.48 E-value: 8.12e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327099 78 PDHPEIG---TLHDNFVHAVETYaENKYLgTRVRSDGTigEYSWmTYGEAASERQAIGSGLLFHGVNQGDCVGLYFINRP 154
Cdd:cd05906 1 PLHRPEGaprTLLELLLRAAERG-PTKGI-TYIDADGS--EEFQ-SYQDLLEDARRLAAGLRQLGLRPGDSVILQFDDNE 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327099 155 EWLVVDHACAAYSFVSVPLydtlGPDAVKFVVNHANLQaIFCVPQTLN--ILLSflaeipSIRLIVVVGGADEHLPSLpr 232
Cdd:cd05906 76 DFIPAFWACVLAGFVPAPL----TVPPTYDEPNARLRK-LRHIWQLLGspVVLT------DAELVAEFAGLETLSGLP-- 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327099 233 gtGVTIVSYQKLLSQGRssLHPFSPPKPEDIATICYTSGTTGTPKGVVLTHGNLIANVAGSSVEAEFFPSDVYISYLPLA 312
Cdd:cd05906 143 --GIRVLSIEELLDTAA--DHDLPQSRPDDLALLMLTSGSTGFPKAVPLTHRNILARSAGKIQHNGLTPQDVFLNWVPLD 218
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327099 313 HIyeranqimgvygGVAVGFYQGDVFKLMDDFAVLRPTIFCSVPRLYNRIydgitsavkssgvvkkrlfeiaynSKKQAI 392
Cdd:cd05906 219 HV------------GGLVELHLRAVYLGCQQVHVPTEEILADPLRWLDLI------------------------DRYRVT 262
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327099 393 IngrtpsAFWDKLVFNKIKEKLG---------GRVRFMGSGASPLS-PDVMDFLRICFGCSVRE-----GYGMTETS--C 455
Cdd:cd05906 263 I------TWAPNFAFALLNDLLEeiedgtwdlSSLRYLVNAGEAVVaKTIRRLLRLLEPYGLPPdairpAFGMTETCsgV 336
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327099 456 VISAMDDGDNLSG-----HVGSPNPACEVKLVDvPEMNYTSDDQPyprGEICVRGPIIFKGYYKDEEQTREILDGDGWLH 530
Cdd:cd05906 337 IYSRSFPTYDHSQalefvSLGRPIPGVSMRIVD-DEGQLLPEGEV---GRLQVRGPVVTKGYYNNPEANAEAFTEDGWFR 412
|
490 500
....*....|....*....|
gi 22327099 531 TGDIGlWLPGGRLKIIDRKK 550
Cdd:cd05906 413 TGDLG-FLDNGNLTITGRTK 431
|
|
| caiC |
PRK08008 |
putative crotonobetaine/carnitine-CoA ligase; Validated |
136-569 |
2.66e-31 |
|
putative crotonobetaine/carnitine-CoA ligase; Validated
Pssm-ID: 181195 [Multi-domain] Cd Length: 517 Bit Score: 128.65 E-value: 2.66e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327099 136 LFH--GVNQGDCVGLYFINRPEWLVVDHACAAYSFVSVPLYDTLGPDAVKFVVNHANLQAIFCVPQTLNILLSFLAEIP- 212
Cdd:PRK08008 53 LFYslGIRKGDKVALHLDNCPEFIFCWFGLAKIGAIMVPINARLLREESAWILQNSQASLLVTSAQFYPMYRQIQQEDAt 132
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327099 213 SIRLIVVvggADEHLPSLprgTGVtiVSYQKLLSQGRSSLHPFSPPKPEDIATICYTSGTTGTPKGVVLTHGNLIanVAG 292
Cdd:PRK08008 133 PLRHICL---TRVALPAD---DGV--SSFTQLKAQQPATLCYAPPLSTDDTAEILFTSGTTSRPKGVVITHYNLR--FAG 202
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327099 293 --SSVEAEFFPSDVYISYLPLAHIYERANQIMGVyggvavgFYQGDVFKLMDDFavlrptifcsvprlynriydgitSAv 370
Cdd:PRK08008 203 yySAWQCALRDDDVYLTVMPAFHIDCQCTAAMAA-------FSAGATFVLLEKY-----------------------SA- 251
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327099 371 kssgvvkkrlfeiaynskkqaiingrtpSAFWDKLVFNK--IKEKLGGRVRFMGsgASPLSP--------DVMDFLRIC- 439
Cdd:PRK08008 252 ----------------------------RAFWGQVCKYRatITECIPMMIRTLM--VQPPSAndrqhclrEVMFYLNLSd 301
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327099 440 ---------FGCSVREGYGMTETscVISAMddGDNLSGH-----VGSPNPACEVKLVDVpemnytsDDQPYPR---GEIC 502
Cdd:PRK08008 302 qekdafeerFGVRLLTSYGMTET--IVGII--GDRPGDKrrwpsIGRPGFCYEAEIRDD-------HNRPLPAgeiGEIC 370
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327099 503 VRG---PIIFKGYYKDEEQTREILDGDGWLHTGDIGLWLPGGRLKIIDRKKNIFKLAqGEYIAPEKIENV 569
Cdd:PRK08008 371 IKGvpgKTIFKEYYLDPKATAKVLEADGWLHTGDTGYVDEEGFFYFVDRRCNMIKRG-GENVSCVELENI 439
|
|
| PRK08162 |
PRK08162 |
acyl-CoA synthetase; Validated |
120-569 |
4.06e-31 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236169 [Multi-domain] Cd Length: 545 Bit Score: 128.53 E-value: 4.06e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327099 120 TYGEAASERQAIGSGLLFHGVNQGDCVGLYFINRPEWLVVDHACAAYSFVSVPLYDTLGPDAVKFVVNHANLQAIFCVPQ 199
Cdd:PRK08162 45 TWAETYARCRRLASALARRGIGRGDTVAVLLPNIPAMVEAHFGVPMAGAVLNTLNTRLDAASIAFMLRHGEAKVLIVDTE 124
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327099 200 TLNILLSFLAEIPSIRLIVVvggaDEHLPSLPRGTGVTIVSYQKLLSQGRSSLhPFSPPKPE-DIATICYTSGTTGTPKG 278
Cdd:PRK08162 125 FAEVAREALALLPGPKPLVI----DVDDPEYPGGRFIGALDYEAFLASGDPDF-AWTLPADEwDAIALNYTSGTTGNPKG 199
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327099 279 VVLTHGNLIANVAGSSVEAEFFPSDVYISYLPLAHiyerANQ-----IMGVYGGVAVGFYQGDVFKLMDDFAVLRPTIFC 353
Cdd:PRK08162 200 VVYHHRGAYLNALSNILAWGMPKHPVYLWTLPMFH----CNGwcfpwTVAARAGTNVCLRKVDPKLIFDLIREHGVTHYC 275
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327099 354 SVPrlynriydgitsavkssgvvkkrlfeIAYNskkqAIINGrtPSAFwdklvfnkiKEKLGGRVRFMGSGASPLSPDVM 433
Cdd:PRK08162 276 GAP--------------------------IVLS----ALINA--PAEW---------RAGIDHPVHAMVAGAAPPAAVIA 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327099 434 DFLRIcfGCSVREGYGMTET---SCVISAMDDGDNLS--------GHVGSPNPACE-VKLVDVPEMnytsddQPYPR--- 498
Cdd:PRK08162 315 KMEEI--GFDLTHVYGLTETygpATVCAWQPEWDALPlderaqlkARQGVRYPLQEgVTVLDPDTM------QPVPAdge 386
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 22327099 499 --GEICVRGPIIFKGYYKDEEQTREILDGdGWLHTGDIGLWLPGGRLKIIDRKKNIFkLAQGEYIAPEKIENV 569
Cdd:PRK08162 387 tiGEIMFRGNIVMKGYLKNPKATEEAFAG-GWFHTGDLAVLHPDGYIKIKDRSKDII-ISGGENISSIEVEDV 457
|
|
| PRK08180 |
PRK08180 |
feruloyl-CoA synthase; Reviewed |
68-533 |
7.19e-31 |
|
feruloyl-CoA synthase; Reviewed
Pssm-ID: 236175 [Multi-domain] Cd Length: 614 Bit Score: 128.46 E-value: 7.19e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327099 68 RSPTKLvsrfPDHPEigTLHDNFVHAVETYAENKYLGTRvrsdGTIGEYSWMTYGEAASERQAIGSGLLFHGVNQGdcvg 147
Cdd:PRK08180 29 RSAEPL----GDYPR--RLTDRLVHWAQEAPDRVFLAER----GADGGWRRLTYAEALERVRAIAQALLDRGLSAE---- 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327099 148 lyfinRPewLVV------DHA---CAAYS----FVSV-PLYDTLGPDavkfvvnHANLQAIFcvpQTLNILLSF------ 207
Cdd:PRK08180 95 -----RP--LMIlsgnsiEHAllaLAAMYagvpYAPVsPAYSLVSQD-------FGKLRHVL---ELLTPGLVFaddgaa 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327099 208 -----LAEIPSIRLIVVVGGADEhlpslprgtGVTIVSYQKLLSQGRSSLHP--FSPPKPEDIATICYTSGTTGTPKGVV 280
Cdd:PRK08180 158 faralAAVVPADVEVVAVRGAVP---------GRAATPFAALLATPPTAAVDaaHAAVGPDTIAKFLFTSGSTGLPKAVI 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327099 281 LTHGNLIANVAgsSVEAEF-FPSD---VYISYLPLAHIYErANQIMG--VY-GGVavgFYQGD---VFKLMDD-FAVLR- 348
Cdd:PRK08180 229 NTHRMLCANQQ--MLAQTFpFLAEeppVLVDWLPWNHTFG-GNHNLGivLYnGGT---LYIDDgkpTPGGFDEtLRNLRe 302
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327099 349 --PTIFCSVPRLYnriyDGITSAVKSSGVVKKRLFEiaynskkqaiingrtpsafwdklvfnkikeklggRVRFMGSGAS 426
Cdd:PRK08180 303 isPTVYFNVPKGW----EMLVPALERDAALRRRFFS----------------------------------RLKLLFYAGA 344
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327099 427 PLSPDVMDFL----------RICFGCsvreGYGMTETSCVISAMDDGDNLSGHVGSPNPACEVKLVDVpemnytsDDqpy 496
Cdd:PRK08180 345 ALSQDVWDRLdrvaeatcgeRIRMMT----GLGMTETAPSATFTTGPLSRAGNIGLPAPGCEVKLVPV-------GG--- 410
|
490 500 510
....*....|....*....|....*....|....*..
gi 22327099 497 pRGEICVRGPIIFKGYYKDEEQTREILDGDGWLHTGD 533
Cdd:PRK08180 411 -KLEVRVKGPNVTPGYWRAPELTAEAFDEEGYYRSGD 446
|
|
| LC_FACS_like |
cd05935 |
Putative long-chain fatty acid CoA ligase; The members of this family are putative long-chain ... |
119-599 |
9.43e-31 |
|
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: 125.67 E-value: 9.43e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327099 119 MTYGEAASERQAIGSGLLFHGVNQGDCVGLYFINRPEWLVVDHACAAYSFVSVPLYDTLGPDAVKFVVNHANLQAifcvp 198
Cdd:cd05935 2 LTYLELLEVVKKLASFLSNKGVRKGDRVGICLQNSPQYVIAYFAIWRANAVVVPINPMLKERELEYILNDSGAKV----- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327099 199 qtlnillsflaeipsirliVVVGgadehlpslprgtgvtivsyqkllsqgrSSLhpfsppkpEDIATICYTSGTTGTPKG 278
Cdd:cd05935 77 -------------------AVVG----------------------------SEL--------DDLALIPYTSGTTGLPKG 101
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327099 279 VVLTHGNLIANVAGSSVEAEFFPSDVYISYLPLAHIYERANQIM-GVYGG---VAVGFYQGDVfkLMDDFAVLRPTIFCS 354
Cdd:cd05935 102 CMHTHFSAAANALQSAVWTGLTPSDVILACLPLFHVTGFVGSLNtAVYVGgtyVLMARWDRET--ALELIEKYKVTFWTN 179
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327099 355 VPRLYNriydgitsavkssgvvkkrlfeiaynskkqaiingrtpsafwDKLVFNKIKEKLGGRVRFMGSGASPLSPDVMD 434
Cdd:cd05935 180 IPTMLV------------------------------------------DLLATPEFKTRDLSSLKVLTGGGAPMPPAVAE 217
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327099 435 FLRICFGCSVREGYGMTETsCVISAMDDGDNL-SGHVGSPNPACEVKLVDVPEMNYTSDDQpypRGEICVRGPIIFKGYY 513
Cdd:cd05935 218 KLLKLTGLRFVEGYGLTET-MSQTHTNPPLRPkLQCLGIP*FGVDARVIDIETGRELPPNE---VGEIVVRGPQIFKGYW 293
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327099 514 KDEEQTREI---LDGDGWLHTGDIGLWLPGGRLKIIDRKKNIFKLAqGEYIAPEKIENVYTKCRFVSQCFIHG--DSFNS 588
Cdd:cd05935 294 NRPEETEESfieIKGRRFFRTGDLGYMDEEGYFFFVDRVKRMINVS-GFKVWPAEVEAKLYKHPAI*EVCVISvpDERVG 372
|
490
....*....|..
gi 22327099 589 SLV-AIVSVDPE 599
Cdd:cd05935 373 EEVkAFIVLRPE 384
|
|
| PRK07514 |
PRK07514 |
malonyl-CoA synthase; Validated |
119-572 |
9.70e-31 |
|
malonyl-CoA synthase; Validated
Pssm-ID: 181011 [Multi-domain] Cd Length: 504 Bit Score: 126.91 E-value: 9.70e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327099 119 MTYGE--AASERQAigsGLLFH-GVNQGDCVGLYFINRPEWLVVDHACAAYSFVSVPLydtlgpdavkfvvNHAnlqaif 195
Cdd:PRK07514 29 YTYGDldAASARLA---NLLVAlGVKPGDRVAVQVEKSPEALALYLATLRAGAVFLPL-------------NTA------ 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327099 196 cvpQTLNILLSFL--AEiPsiRLIVVVGGADEHLPSLPRGTGVTIVsyQKLLSQGRSSL----------HPFSPPKPEDI 263
Cdd:PRK07514 87 ---YTLAELDYFIgdAE-P--ALVVCDPANFAWLSKIAAAAGAPHV--ETLDADGTGSLleaaaaapddFETVPRGADDL 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327099 264 ATICYTSGTTGTPKGVVLTHGNLIANVAGSSVEAEFFPSDVYISYLPLAHIYeranqimGVYggVAV------------- 330
Cdd:PRK07514 159 AAILYTSGTTGRSKGAMLSHGNLLSNALTLVDYWRFTPDDVLIHALPIFHTH-------GLF--VATnvallagasmifl 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327099 331 -GFYQGDVFKLMDdfavlRPTIFCSVPRLYNRIYD--GITSAVkssgVVKKRLFeiaynskkqaiingrtpsafwdklvf 407
Cdd:PRK07514 230 pKFDPDAVLALMP-----RATVMMGVPTFYTRLLQepRLTREA----AAHMRLF-------------------------- 274
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327099 408 nkIkeklggrvrfmgSGASPLSPDVMDFLRICFGCSVREGYGMTETSCVISAMDDGDNLSGHVGSPNPACEVKLVDvPEm 487
Cdd:PRK07514 275 --I------------SGSAPLLAETHREFQERTGHAILERYGMTETNMNTSNPYDGERRAGTVGFPLPGVSLRVTD-PE- 338
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327099 488 nytsDDQPYPRGEIC---VRGPIIFKGYYKDEEQTREILDGDGWLHTGDIGLWLPGGRLKIIDRKKNIfkLAQGEYiape 564
Cdd:PRK07514 339 ----TGAELPPGEIGmieVKGPNVFKGYWRMPEKTAEEFRADGFFITGDLGKIDERGYVHIVGRGKDL--IISGGY---- 408
|
....*...
gi 22327099 565 kieNVYTK 572
Cdd:PRK07514 409 ---NVYPK 413
|
|
| ttLC_FACS_AEE21_like |
cd12118 |
Fatty acyl-CoA synthetases similar to LC-FACS from Thermus thermophiles and Arabidopsis; This ... |
115-569 |
1.45e-30 |
|
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: 125.87 E-value: 1.45e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327099 115 EYSWMTYGEAASeRQAigSGLLFHGVNQGDCVGLYFINRPEWLVVDHACAAYSFVSVPLYDTLGPDAVKFVVNHANLQAI 194
Cdd:cd12118 29 RYTWRQTYDRCR-RLA--SALAALGISRGDTVAVLAPNTPAMYELHFGVPMAGAVLNALNTRLDAEEIAFILRHSEAKVL 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327099 195 FCvpqtlnillsflaeipsirlivvvggaDEHLpslprgtgvtivSYQKLLSQGRSSLHPFsPPKPE-DIATICYTSGTT 273
Cdd:cd12118 106 FV---------------------------DREF------------EYEDLLAEGDPDFEWI-PPADEwDPIALNYTSGTT 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327099 274 GTPKGVVLTHGNLIANVAGSSVEAEFFPSDVYISYLPLAHiyerANQIMGVYGGVAVG--------FYQGDVFKLMDDFA 345
Cdd:cd12118 146 GRPKGVVYHHRGAYLNALANILEWEMKQHPVYLWTLPMFH----CNGWCFPWTVAAVGgtnvclrkVDAKAIYDLIEKHK 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327099 346 VlrpTIFCSVPRLYNriydgitsavkssgvvkkrlfeiaynskkqAIINGRTPSafwdklvfnkiKEKLGGRVRFMGSGA 425
Cdd:cd12118 222 V---THFCGAPTVLN------------------------------MLANAPPSD-----------ARPLPHRVHVMTAGA 257
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327099 426 SPlsPDVMDFLRICFGCSVREGYGMTETSCVISA---MDDGDNLS-------------GHVGSPnpacEVKLVDVPEMny 489
Cdd:cd12118 258 PP--PAAVLAKMEELGFDVTHVYGLTETYGPATVcawKPEWDELPteerarlkarqgvRYVGLE----EVDVLDPETM-- 329
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327099 490 tsddQPYPR-----GEICVRGPIIFKGYYKDEEQTREILDGdGWLHTGDIGLWLPGGRLKIIDRKKNIFkLAQGEYIAPE 564
Cdd:cd12118 330 ----KPVPRdgktiGEIVFRGNIVMKGYLKNPEATAEAFRG-GWFHSGDLAVIHPDGYIEIKDRSKDII-ISGGENISSV 403
|
....*
gi 22327099 565 KIENV 569
Cdd:cd12118 404 EVEGV 408
|
|
| PRK06839 |
PRK06839 |
o-succinylbenzoate--CoA ligase; |
113-569 |
1.54e-30 |
|
o-succinylbenzoate--CoA ligase;
Pssm-ID: 168698 [Multi-domain] Cd Length: 496 Bit Score: 126.13 E-value: 1.54e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327099 113 IGEYSWMTYGEAASERQAIGSGLLFH-GVNQGDCVGLYFINRPEWLVVDHACAAYSFVSVPLYDTLGPDAVKFVVNHANL 191
Cdd:PRK06839 22 ITEEEEMTYKQLHEYVSKVAAYLIYElNVKKGERIAILSQNSLEYIVLLFAIAKVECIAVPLNIRLTENELIFQLKDSGT 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327099 192 QAIFCVPQTLNILLSFLAEIPSIRLIvvvggadehlpslprgtgvTIVSYQKLLSQGRSSlhpFSPPKPEDIATICYTSG 271
Cdd:PRK06839 102 TVLFVEKTFQNMALSMQKVSYVQRVI-------------------SITSLKEIEDRKIDN---FVEKNESASFIICYTSG 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327099 272 TTGTPKGVVLTHGNLIANVAGSSVEAEFFPSDVYISYLPLAHIyeranqimgvyGGVAVgfyqgdvfklmddFAVlrPTI 351
Cdd:PRK06839 160 TTGKPKGAVLTQENMFWNALNNTFAIDLTMHDRSIVLLPLFHI-----------GGIGL-------------FAF--PTL 213
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327099 352 FCS----VPRLYNRiydgiTSAVKssgVVKKRLFEIAYN--SKKQAIINgrtpSAFWDKLVFNKikeklggrVRFMGSGA 425
Cdd:PRK06839 214 FAGgviiVPRKFEP-----TKALS---MIEKHKVTVVMGvpTIHQALIN----CSKFETTNLQS--------VRWFYNGG 273
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327099 426 SPLSPDVMDFLR---ICFGcsvrEGYGMTETSCVIS--AMDDGDNLSGHVGSPNPACEVKLVDvpemNYTSDDQPYPRGE 500
Cdd:PRK06839 274 APCPEELMREFIdrgFLFG----QGFGMTETSPTVFmlSEEDARRKVGSIGKPVLFCDYELID----ENKNKVEVGEVGE 345
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 22327099 501 ICVRGPIIFKGYYKDEEQTREILDgDGWLHTGDIGLWLPGGRLKIIDRKKNIFkLAQGEYIAPEKIENV 569
Cdd:PRK06839 346 LLIRGPNVMKEYWNRPDATEETIQ-DGWLCTGDLARVDEDGFVYIVGRKKEMI-ISGGENIYPLEVEQV 412
|
|
| FACL_like_2 |
cd05917 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
260-568 |
2.51e-30 |
|
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: 122.77 E-value: 2.51e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327099 260 PEDIATICYTSGTTGTPKGVVLTHGNLIANVAGSSVEAEFFPSDVYISYLPLAHIYeraNQIMGVYGGVAVG---FYQGD 336
Cdd:cd05917 1 PDDVINIQFTSGTTGSPKGATLTHHNIVNNGYFIGERLGLTEQDRLCIPVPLFHCF---GSVLGVLACLTHGatmVFPSP 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327099 337 VFklmDDFAVLR-------------PTIFCSV---PRLynRIYDgitsavkssgvvkkrlfeiaYNSKKQAIINGrtpsa 400
Cdd:cd05917 78 SF---DPLAVLEaiekekctalhgvPTMFIAElehPDF--DKFD--------------------LSSLRTGIMAG----- 127
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327099 401 fwdklvfnkikeklggrvrfmgsgaSPLSPDVMDFLRICFGCS-VREGYGMTETSCVI---SAMDDGDNLSGHVGSPNPA 476
Cdd:cd05917 128 -------------------------APCPPELMKRVIEVMNMKdVTIAYGMTETSPVStqtRTDDSIEKRVNTVGRIMPH 182
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327099 477 CEVKLVDVpemnyTSDDQPYP--RGEICVRGPIIFKGYYKDEEQTREILDGDGWLHTGDIGLWLPGGRLKIIDRKKNIFk 554
Cdd:cd05917 183 TEAKIVDP-----EGGIVPPVgvPGELCIRGYSVMKGYWNDPEKTAEAIDGDGWLHTGDLAVMDEDGYCRIVGRIKDMI- 256
|
330
....*....|....
gi 22327099 555 LAQGEYIAPEKIEN 568
Cdd:cd05917 257 IRGGENIYPREIEE 270
|
|
| PRK03640 |
PRK03640 |
o-succinylbenzoate--CoA ligase; |
119-572 |
4.45e-30 |
|
o-succinylbenzoate--CoA ligase;
Pssm-ID: 235146 [Multi-domain] Cd Length: 483 Bit Score: 124.30 E-value: 4.45e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327099 119 MTYGEAASERQAIGSGLLFHGVNQGDCVGLYFINRPEWLVVDHACAAYSFVSVPLYDTLGPDAVKFVVNHANLQAIFCVP 198
Cdd:PRK03640 28 VTFMELHEAVVSVAGKLAALGVKKGDRVALLMKNGMEMILVIHALQQLGAVAVLLNTRLSREELLWQLDDAEVKCLITDD 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327099 199 qtlnillSFLAEI-PSIRLIVvvggadEHLPSLPRGTgVTIVSYQKLlsqgrsslhpfsppkpEDIATICYTSGTTGTPK 277
Cdd:PRK03640 108 -------DFEAKLiPGISVKF------AELMNGPKEE-AEIQEEFDL----------------DEVATIMYTSGTTGKPK 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327099 278 GVVLTHGNLIANVAGSSVEAEFFPSDVYISYLPLAHIyeranqimgvyGGVAvgfyqgdvfklmddfAVLRPTIF-CSVp 356
Cdd:PRK03640 158 GVIQTYGNHWWSAVGSALNLGLTEDDCWLAAVPIFHI-----------SGLS---------------ILMRSVIYgMRV- 210
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327099 357 RLYNRiYDG--ITSAVKSSG-----VVKKRLFEIAynskkQAIINGRTPSAFwdklvfnkikeklggrvRFMGSGASPLS 429
Cdd:PRK03640 211 VLVEK-FDAekINKLLQTGGvtiisVVSTMLQRLL-----ERLGEGTYPSSF-----------------RCMLLGGGPAP 267
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327099 430 PDVmdfLRIC--FGCSVREGYGMTETSCVISAMDDGDNLS--GHVGSPNPACEVKLVDvpemnYTSDDQPYPRGEICVRG 505
Cdd:PRK03640 268 KPL---LEQCkeKGIPVYQSYGMTETASQIVTLSPEDALTklGSAGKPLFPCELKIEK-----DGVVVPPFEEGEIVVKG 339
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 22327099 506 PIIFKGYYKDEEQTREILDgDGWLHTGDIGLWLPGGRLKIIDRKKNIFkLAQGEYIAPEKIENVYTK 572
Cdd:PRK03640 340 PNVTKGYLNREDATRETFQ-DGWFKTGDIGYLDEEGFLYVLDRRSDLI-ISGGENIYPAEIEEVLLS 404
|
|
| PRK06188 |
PRK06188 |
acyl-CoA synthetase; Validated |
119-599 |
1.56e-29 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 235731 [Multi-domain] Cd Length: 524 Bit Score: 123.56 E-value: 1.56e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327099 119 MTYGEAASE-RQAIGsglLFH--GVNQGDCVGLYFINRPE-WLVVDHACAAySFVSVPLYDTLGPDAVKFVVNHANLQAI 194
Cdd:PRK06188 38 LTYGQLADRiSRYIQ---AFEalGLGTGDAVALLSLNRPEvLMAIGAAQLA-GLRRTALHPLGSLDDHAYVLEDAGISTL 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327099 195 FCVPQT-LNILLSFLAEIPSIRLIVVVGgadehlpslPRGTGVtivsyqKLLSQGRS----SLHPFSppKPEDIATICYT 269
Cdd:PRK06188 114 IVDPAPfVERALALLARVPSLKHVLTLG---------PVPDGV------DLLAAAAKfgpaPLVAAA--LPPDIAGLAYT 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327099 270 SGTTGTPKGVVLTHGNLIANVAgsSVEAEF-FPSDvyISYL---PLAHIyeranqimgvyGG--VAVGFYQGDVFKLMDD 343
Cdd:PRK06188 177 GGTTGKPKGVMGTHRSIATMAQ--IQLAEWeWPAD--PRFLmctPLSHA-----------GGafFLPTLLRGGTVIVLAK 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327099 344 F---AVLR--------PTIFcsVPRLYNRIYD--GITSAVKSSgvvkkrLFEIAYnskkqaiingrtpsafwdklvfnki 410
Cdd:PRK06188 242 FdpaEVLRaieeqritATFL--VPTMIYALLDhpDLRTRDLSS------LETVYY------------------------- 288
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327099 411 keklggrvrfmgsGASPLSPDvmdflRIC-----FGCSVREGYGMTETSCVISAMDDGDNLSGHV------GSPNPACEV 479
Cdd:PRK06188 289 -------------GASPMSPV-----RLAeaierFGPIFAQYYGQTEAPMVITYLRKRDHDPDDPkrltscGRPTPGLRV 350
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327099 480 KLVDvpemnytSDDQPYPR---GEICVRGPIIFKGYYKDEEQTREILDgDGWLHTGDIGLWLPGGRLKIIDRKK------ 550
Cdd:PRK06188 351 ALLD-------EDGREVAQgevGEICVRGPLVMDGYWNRPEETAEAFR-DGWLHTGDVAREDEDGFYYIVDRKKdmivtg 422
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327099 551 --NIFklaqgeyiaPEKIENVYTKCRFVSQCFIHG---DSFNSSLVAIV------SVDPE 599
Cdd:PRK06188 423 gfNVF---------PREVEDVLAEHPAVAQVAVIGvpdEKWGEAVTAVVvlrpgaAVDAA 473
|
|
| PLN02574 |
PLN02574 |
4-coumarate--CoA ligase-like |
80-581 |
2.43e-29 |
|
4-coumarate--CoA ligase-like
Pssm-ID: 215312 [Multi-domain] Cd Length: 560 Bit Score: 123.03 E-value: 2.43e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327099 80 HPEIGTLHDNFVHAVE-TYAENKYLGTRVRSDGTIGEYswMTYGEAASERQAIGSGLL-FHGVNQGDCVGLYFINRPEWL 157
Cdd:PLN02574 29 HPPVPLPSDPNLDAVSfIFSHHNHNGDTALIDSSTGFS--ISYSELQPLVKSMAAGLYhVMGVRQGDVVLLLLPNSVYFP 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327099 158 VVDHACAAYSFVSVPLYDTLGPDAVKFVVNHANLQAIFCVPQTLnillsflAEIPSIRLIVVV----GGADEHLPSLPRg 233
Cdd:PLN02574 107 VIFLAVLSLGGIVTTMNPSSSLGEIKKRVVDCSVGLAFTSPENV-------EKLSPLGVPVIGvpenYDFDSKRIEFPK- 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327099 234 tgvtivSYQKLLSQGRSSLHPfsPPKPEDIATICYTSGTTGTPKGVVLTHGNLIANVA-----GSSVEAEFFPSDVYISY 308
Cdd:PLN02574 179 ------FYELIKEDFDFVPKP--VIKQDDVAAIMYSSGTTGASKGVVLTHRNLIAMVElfvrfEASQYEYPGSDNVYLAA 250
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327099 309 LPLAHIYERANQIMGVYG-GVAV----GFYQGDVFKLMDDFAVlrpTIFCSVPRLynriydgITSAVKSSGVVKKRLFEi 383
Cdd:PLN02574 251 LPMFHIYGLSLFVVGLLSlGSTIvvmrRFDASDMVKVIDRFKV---THFPVVPPI-------LMALTKKAKGVCGEVLK- 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327099 384 aynSKKQaiingrtpsafwdklvfnkikeklggrvrfMGSGASPLSPD-VMDFLRICFGCSVREGYGMTETSCVISAMDD 462
Cdd:PLN02574 320 ---SLKQ------------------------------VSCGAAPLSGKfIQDFVQTLPHVDFIQGYGMTESTAVGTRGFN 366
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327099 463 GDNLSGH--VGSPNPACEVKLVDvpeMNYTSDDQPYPRGEICVRGPIIFKGYYKDEEQTREILDGDGWLHTGDIGLWLPG 540
Cdd:PLN02574 367 TEKLSKYssVGLLAPNMQAKVVD---WSTGCLLPPGNCGELWIQGPGVMKGYLNNPKATQSTIDKDGWLRTGDIAYFDED 443
|
490 500 510 520
....*....|....*....|....*....|....*....|.
gi 22327099 541 GRLKIIDRKKNIFKLaQGEYIAPEKIENVytkcrFVSQCFI 581
Cdd:PLN02574 444 GYLYIVDRLKEIIKY-KGFQIAPADLEAV-----LISHPEI 478
|
|
| OSB_MenE-like |
cd17630 |
O-succinylbenzoic acid-CoA ligase; This family contains O-succinylbenzoyl-CoA (OSB-CoA) ... |
262-679 |
2.69e-29 |
|
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: 118.97 E-value: 2.69e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327099 262 DIATICYTSGTTGTPKGVVLTHGNLIANVAGSSVEAEFFPSDVYISYLPLAHIyeranqimgvyGGVAV---GFYQGDVF 338
Cdd:cd17630 1 RLATVILTSGSTGTPKAVVHTAANLLASAAGLHSRLGFGGGDSWLLSLPLYHV-----------GGLAIlvrSLLAGAEL 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327099 339 KLMD-------DFAVLRPTIFCSVPRLYNRIYDgitsavkssgvvkkrlfeiaynskkqaiiNGRTPSAFwdklvfnkik 411
Cdd:cd17630 70 VLLErnqalaeDLAPPGVTHVSLVPTQLQRLLD-----------------------------SGQGPAAL---------- 110
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327099 412 eklgGRVRFMGSGASPLSPDVMDFLRiCFGCSVREGYGMTETSCVISAMDDGDNLSGHVGSPNPACEVKLVDvpemnyts 491
Cdd:cd17630 111 ----KSLRAVLLGGAPIPPELLERAA-DRGIPLYTTYGMTETASQVATKRPDGFGRGGVGVLLPGRELRIVE-------- 177
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327099 492 ddqpypRGEICVRGPIIFKGYYKDeeQTREILDGDGWLHTGDIGLWLPGGRLKIIDRKKNIFkLAQGEYIAPEKIENVYT 571
Cdd:cd17630 178 ------DGEIWVGGASLAMGYLRG--QLVPEFNEDGWFTTKDLGELHADGRLTVLGRADNMI-ISGGENIQPEEIEAALA 248
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327099 572 KCRFVSQCFIHG---DSFNSSLVAIVSVDPEVmkdwaasegikyehlgqlcnDPrvrKTVLAEMDDlgreaQLRGFEFAK 648
Cdd:cd17630 249 AHPAVRDAFVVGvpdEELGQRPVAVIVGRGPA--------------------DP---AELRAWLKD-----KLARFKLPK 300
|
410 420 430
....*....|....*....|....*....|.
gi 22327099 649 AVTLVPEPftlengLLTPTFKIKRPQAKAYF 679
Cdd:cd17630 301 RIYPVPEL------PRTGGGKVDRRALRAWL 325
|
|
| PRK08974 |
PRK08974 |
long-chain-fatty-acid--CoA ligase FadD; |
239-569 |
2.89e-29 |
|
long-chain-fatty-acid--CoA ligase FadD;
Pssm-ID: 236359 [Multi-domain] Cd Length: 560 Bit Score: 122.86 E-value: 2.89e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327099 239 VSYQKLLSQGRSSLHPFSPPKPEDIATICYTSGTTGTPKGVVLTHGNLIANVAgsSVEAEFFP-----SDVYISYLPLAH 313
Cdd:PRK08974 184 ISFRSALHKGRRMQYVKPELVPEDLAFLQYTGGTTGVAKGAMLTHRNMLANLE--QAKAAYGPllhpgKELVVTALPLYH 261
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327099 314 IYE-RANQIMGVYGGVAvgfyqgdvfklmddfavlrpTIFCSVPRlynriydGITSAVKSsgvVKKRLFE--IAYNSKKQ 390
Cdd:PRK08974 262 IFAlTVNCLLFIELGGQ--------------------NLLITNPR-------DIPGFVKE---LKKYPFTaiTGVNTLFN 311
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327099 391 AIINGRTpsafWDKLVFNKIKEKLGGrvrfmgsgASPLSPDVMDFLRICFGCSVREGYGMTETSCVISAMD-DGDNLSGH 469
Cdd:PRK08974 312 ALLNNEE----FQELDFSSLKLSVGG--------GMAVQQAVAERWVKLTGQYLLEGYGLTECSPLVSVNPyDLDYYSGS 379
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327099 470 VGSPNPACEVKLVDvPEMNYTSDDQPyprGEICVRGPIIFKGYYKDEEQTREILDgDGWLHTGDIGLWLPGGRLKIIDRK 549
Cdd:PRK08974 380 IGLPVPSTEIKLVD-DDGNEVPPGEP---GELWVKGPQVMLGYWQRPEATDEVIK-DGWLATGDIAVMDEEGFLRIVDRK 454
|
330 340
....*....|....*....|
gi 22327099 550 KNIFkLAQGEYIAPEKIENV 569
Cdd:PRK08974 455 KDMI-LVSGFNVYPNEIEDV 473
|
|
| BCL_4HBCL |
cd05959 |
Benzoate CoA ligase (BCL) and 4-Hydroxybenzoate-Coenzyme A Ligase (4-HBA-CoA ligase); Benzoate ... |
106-569 |
5.77e-29 |
|
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: 121.32 E-value: 5.77e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327099 106 RVRSDGT--IGEYSWMTYGEAASERQAIGSGLLFHGVNQGDCVGLYFINRPEWLVVDHACAAYSFVSVPLYDTLGPDAVK 183
Cdd:cd05959 15 EGRGDKTafIDDAGSLTYAELEAEARRVAGALRALGVKREERVLLIMLDTVDFPTAFLGAIRAGIVPVPVNTLLTPDDYA 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327099 184 FVVNHANLQAIFCVPQTLNILLSFLAEI-PSIRLIVVVGGADEHLPSLprgtgvtivSYQKLLSQGRSSLHPfSPPKPED 262
Cdd:cd05959 95 YYLEDSRARVVVVSGELAPVLAAALTKSeHTLVVLIVSGGAGPEAGAL---------LLAELVAAEAEQLKP-AATHADD 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327099 263 IATICYTSGTTGTPKGVVLTHGNLIA-------NVAGSSveaeffPSDVYISYLPLAHIYERANQI---MGVyGGVAV-- 330
Cdd:cd05959 165 PAFWLYSSGSTGRPKGVVHLHADIYWtaelyarNVLGIR------EDDVCFSAAKLFFAYGLGNSLtfpLSV-GATTVlm 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327099 331 -GFYQGD-VFKLMDDFavlRPTIFCSVPRLYNriydgitsAVKSSGVVKKRLFEiaynskkqaiingrtpsafwdklvfn 408
Cdd:cd05959 238 pERPTPAaVFKRIRRY---RPTVFFGVPTLYA--------AMLAAPNLPSRDLS-------------------------- 280
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327099 409 kikeklggRVRFMGSGASPLSPDVMDFLRICFGCSVREGYGMTETSCVISAMDDGDNLSGHVGSPNPACEVKLVDvPEMN 488
Cdd:cd05959 281 --------SLRLCVSAGEALPAEVGERWKARFGLDILDGIGSTEMLHIFLSNRPGRVRYGTTGKPVPGYEVELRD-EDGG 351
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327099 489 YTSDDQPyprGEICVRGPIIFKGYYKDEEQTREILDGdGWLHTGDIGLWLPGGRLKIIDRKKNIFKlAQGEYIAPEKIEN 568
Cdd:cd05959 352 DVADGEP---GELYVRGPSSATMYWNNRDKTRDTFQG-EWTRTGDKYVRDDDGFYTYAGRADDMLK-VSGIWVSPFEVES 426
|
.
gi 22327099 569 V 569
Cdd:cd05959 427 A 427
|
|
| PRK05620 |
PRK05620 |
long-chain fatty-acid--CoA ligase; |
104-568 |
5.86e-29 |
|
long-chain fatty-acid--CoA ligase;
Pssm-ID: 180167 [Multi-domain] Cd Length: 576 Bit Score: 122.20 E-value: 5.86e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327099 104 GTRVRSDGTIgeyswMTYGEAASERQ---AIG--SGLLFH------GVNQGDCVGLYFINRPEWLVVDHACAAYSFVSVP 172
Cdd:PRK05620 19 GSTVHGDTTV-----TTWGGAEQEQTtfaAIGarAAALAHalhdelGITGDQRVGSMMYNCAEHLEVLFAVACMGAVFNP 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327099 173 LYDTLGPDAVKFVVNHANLQAIFCVPQTLNILLSFLAEIPSIRLIVVVGGADEHLPSLPRGTGVTIVSYQKLLSqGRSSL 252
Cdd:PRK05620 94 LNKQLMNDQIVHIINHAEDEVIVADPRLAEQLGEILKECPCVRAVVFIGPSDADSAAAHMPEGIKVYSYEALLD-GRSTV 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327099 253 HPFsPPKPEDI-ATICYTSGTTGTPKGVVLTHGNLianvagssveaeffpsdvyisylplahiyeranqimgvyggvavg 331
Cdd:PRK05620 173 YDW-PELDETTaAAICYSTGTTGAPKGVVYSHRSL--------------------------------------------- 206
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327099 332 FYQGDVFKLMDDFAVLRPTIF-CSVPrLYNRIYDGITSAVKSSG---------VVKKRLFE-IAYNSKKQAiingRTPSA 400
Cdd:PRK05620 207 YLQSLSLRTTDSLAVTHGESFlCCVP-IYHVLSWGVPLAAFMSGtplvfpgpdLSAPTLAKiIATAMPRVA----HGVPT 281
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327099 401 FWDKLVFNKIK---EKLGGRVRFmgSGASPLSPDVMDFLRICFGCSVREGYGMTETSCVISAMDDGDNLSGHV------- 470
Cdd:PRK05620 282 LWIQLMVHYLKnppERMSLQEIY--VGGSAVPPILIKAWEERYGVDVVHVWGMTETSPVGTVARPPSGVSGEArwayrvs 359
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327099 471 -GSPNPACEVKLVDVPE-MNYTSDDQpyprGEICVRGPIIFKGYYKDEEQT----------REILDG------DGWLHTG 532
Cdd:PRK05620 360 qGRFPASLEYRIVNDGQvMESTDRNE----GEIQVRGNWVTASYYHSPTEEgggaastfrgEDVEDAndrftaDGWLRTG 435
|
490 500 510
....*....|....*....|....*....|....*.
gi 22327099 533 DIGLWLPGGRLKIIDRKKNIFKlAQGEYIAPEKIEN 568
Cdd:PRK05620 436 DVGSVTRDGFLTIHDRARDVIR-SGGEWIYSAQLEN 470
|
|
| PRK07768 |
PRK07768 |
long-chain-fatty-acid--CoA ligase; Validated |
218-567 |
9.11e-29 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236091 [Multi-domain] Cd Length: 545 Bit Score: 121.26 E-value: 9.11e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327099 218 VVVGGADEHLPSLPRGTGVTIVSYQKLLSQGrsslhPFSPPK--PEDIATICYTSGTTGTPKGVVLTHGNLIANVAGSSV 295
Cdd:PRK07768 112 VVVGEPFLAAAPVLEEKGIRVLTVADLLAAD-----PIDPVEtgEDDLALMQLTSGSTGSPKAVQITHGNLYANAEAMFV 186
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327099 296 EAEFFP-SDVYISYLPLAHiyeranqIMGVYGGVAVGFYQG-DVFKlmddfavLRPTIFCSVPRLYNRI---YDG-ITSA 369
Cdd:PRK07768 187 AAEFDVeTDVMVSWLPLFH-------DMGMVGFLTVPMYFGaELVK-------VTPMDFLRDPLLWAELiskYRGtMTAA 252
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327099 370 VKSS-GVVKKRLfeiaynsKKQAiingrTPSAFwdklvfnkikeKLGGrVRFMGSGASPLSPDVM-DFLRIC--FGC--- 442
Cdd:PRK07768 253 PNFAyALLARRL-------RRQA-----KPGAF-----------DLSS-LRFALNGAEPIDPADVeDLLDAGarFGLrpe 308
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327099 443 SVREGYGMTETSCVISAMD----------DGDNLS----------GHV------GSPNPACEVKLVDvpemnytSDDQPY 496
Cdd:PRK07768 309 AILPAYGMAEATLAVSFSPcgaglvvdevDADLLAalrravpatkGNTrrlatlGPPLPGLEVRVVD-------EDGQVL 381
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 22327099 497 PR---GEICVRGPIIFKGyYKDEEQTREILDGDGWLHTGDIGLWLPGGRLKIIDRKKNIFKLAqGEYIAPEKIE 567
Cdd:PRK07768 382 PPrgvGVIELRGESVTPG-YLTMDGFIPAQDADGWLDTGDLGYLTEEGEVVVCGRVKDVIIMA-GRNIYPTDIE 453
|
|
| PLN02860 |
PLN02860 |
o-succinylbenzoate-CoA ligase |
260-677 |
1.61e-28 |
|
o-succinylbenzoate-CoA ligase
Pssm-ID: 215464 [Multi-domain] Cd Length: 563 Bit Score: 120.67 E-value: 1.61e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327099 260 PEDIATICYTSGTTGTPKGVVLTHGNLIANVAGSSVEAEFFPSDVYISYLPLAHIYERANQI-MGVYGGVAV---GFYQG 335
Cdd:PLN02860 171 PDDAVLICFTSGTTGRPKGVTISHSALIVQSLAKIAIVGYGEDDVYLHTAPLCHIGGLSSALaMLMVGACHVllpKFDAK 250
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327099 336 DVFKLMDDFAVlrpTIFCSVPRLYNRIydgitsavkssgvvkkrlfeIAYNSKKQAIINGRTpsafwdklvfnkikeklg 415
Cdd:PLN02860 251 AALQAIKQHNV---TSMITVPAMMADL--------------------ISLTRKSMTWKVFPS------------------ 289
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327099 416 grVRFMGSGASPLSPDVMDFLRICFGCS-VREGYGMTETSCVISAM-----------------DDGDNLSGH------VG 471
Cdd:PLN02860 290 --VRKILNGGGSLSSRLLPDAKKLFPNAkLFSAYGMTEACSSLTFMtlhdptlespkqtlqtvNQTKSSSVHqpqgvcVG 367
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327099 472 SPNPACEVKLvdvpemnytSDDQPYPRGEICVRGPIIFKGYYKDEEQTREILDGDGWLHTGDIGLWLPGGRLKIIDRKKN 551
Cdd:PLN02860 368 KPAPHVELKI---------GLDESSRVGRILTRGPHVMLGYWGQNSETASVLSNDGWLDTGDIGWIDKAGNLWLIGRSND 438
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327099 552 IFKlAQGEYIAPEKIENVYTKCRFVSQCFIHG--DS-FNSSLVAIVSvdpevMKD---WAASEGIKYEHLGQLCNDprvr 625
Cdd:PLN02860 439 RIK-TGGENVYPEEVEAVLSQHPGVASVVVVGvpDSrLTEMVVACVR-----LRDgwiWSDNEKENAKKNLTLSSE---- 508
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|..
gi 22327099 626 ktvlaEMDDLGREAQLRGFEFAKAVTLVPEPFTlenglLTPTFKIKRPQAKA 677
Cdd:PLN02860 509 -----TLRHHCREKNLSRFKIPKLFVQWRKPFP-----LTTTGKIRRDEVRR 550
|
|
| MACS_like |
cd05972 |
Medium-chain acyl-CoA synthetase (MACS or ACSM); MACS catalyzes the two-step activation of ... |
120-568 |
6.59e-28 |
|
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: 117.05 E-value: 6.59e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327099 120 TYGEAASERQAIGSGLLFHGVNQGDCVGLYFINRPEWLVVDHACAAYSFVSVPLYDTLGPDAVKFVVNHANLQAIFCvpq 199
Cdd:cd05972 2 SFRELKRESAKAANVLAKLGLRKGDRVAVLLPRVPELWAVILAVIKLGAVYVPLTTLLGPKDIEYRLEAAGAKAIVT--- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327099 200 tlnillsflaeipsirlivvvggaDEhlpslprgtgvtivsyqkllsqgrsslhpfsppkpEDIATICYTSGTTGTPKGV 279
Cdd:cd05972 79 ------------------------DA-----------------------------------EDPALIYFTSGTTGLPKGV 99
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327099 280 VLTHGNLIANVAGSSVEAEFFPSDVYISYLPLAHIYERANQIMGVYG-GVAVGFYQGDVF------KLMDDFAVlrpTIF 352
Cdd:cd05972 100 LHTHSYPLGHIPTAAYWLGLRPDDIHWNIADPGWAKGAWSSFFGPWLlGATVFVYEGPRFdaerilELLERYGV---TSF 176
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327099 353 CSVPRLYNRIydgitSAVKSSGVVKKRLfeiaynskkqaiingrtpsafwdklvfnkikeklggrvRFMGSGASPLSPDV 432
Cdd:cd05972 177 CGPPTAYRML-----IKQDLSSYKFSHL--------------------------------------RLVVSAGEPLNPEV 213
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327099 433 MDFLRICFGCSVREGYGMTETSCVISAMDDGDNLSGHVGSPNPACEVKLVDvpemnytsDD----QPYPRGEICVR-GPI 507
Cdd:cd05972 214 IEWWRAATGLPIRDGYGQTETGLTVGNFPDMPVKPGSMGRPTPGYDVAIID--------DDgrelPPGEEGDIAIKlPPP 285
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 22327099 508 -IFKGYYKDEEQTREILdGDGWLHTGDIGLWLPGGRLKIIDRKKNIFKlAQGEYIAPEKIEN 568
Cdd:cd05972 286 gLFLGYVGDPEKTEASI-RGDYYLTGDRAYRDEDGYFWFVGRADDIIK-SSGYRIGPFEVES 345
|
|
| EntE |
COG1021 |
EntE, 2,3-dihydroxybenzoate-AMP synthase component of non-ribosomal peptide synthetase ... |
114-593 |
9.08e-28 |
|
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: 117.94 E-value: 9.08e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327099 114 GEYSWmTYGEAASERQAIGSGLLFHGVNQGDCVGLYFINRPEWLVVDHAC----AaysfvsVPLYdTLgP---------- 179
Cdd:COG1021 47 GERRL-SYAELDRRADRLAAGLLALGLRPGDRVVVQLPNVAEFVIVFFALfragA------IPVF-AL-Pahrraeishf 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327099 180 ----DAVKFVV-------NHANLQAifcvpqtlnillSFLAEIPSIRLIVVVGGADEHlpslprgtgvtiVSYQKLLSQG 248
Cdd:COG1021 118 aeqsEAVAYIIpdrhrgfDYRALAR------------ELQAEVPSLRHVLVVGDAGEF------------TSLDALLAAP 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327099 249 RSSLHPfsPPKPEDIATICYTSGTTGTPKGVVLTHGNLIANVAGSSVEAEFFPSDVYISYLPLAHiyeraNQIMGVYGGV 328
Cdd:COG1021 174 ADLSEP--RPDPDDVAFFQLSGGTTGLPKLIPRTHDDYLYSVRASAEICGLDADTVYLAALPAAH-----NFPLSSPGVL 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327099 329 AVgFYQG------------DVFKLMDDFAVlrpTIFCSVPRLYNRIYDgitsavkssgvvkkrlfeiaynskkQAIINGR 396
Cdd:COG1021 247 GV-LYAGgtvvlapdpspdTAFPLIERERV---TVTALVPPLALLWLD-------------------------AAERSRY 297
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327099 397 TPSAfwdklvfnkikeklggrVRFMGSGASPLSPDVMDFLRICFGCSVREGYGMTETSCVISAMDDGDNLSGH-VGSP-N 474
Cdd:COG1021 298 DLSS-----------------LRVLQVGGAKLSPELARRVRPALGCTLQQVFGMAEGLVNYTRLDDPEEVILTtQGRPiS 360
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327099 475 PACEVKLVDvpemnytSDDQPYPRGEI---CVRGPIIFKGYYKDEEQTREILDGDGWLHTGDIGLWLPGGRLKIIDRKKN 551
Cdd:COG1021 361 PDDEVRIVD-------EDGNPVPPGEVgelLTRGPYTIRGYYRAPEHNARAFTPDGFYRTGDLVRRTPDGYLVVEGRAKD 433
|
490 500 510 520
....*....|....*....|....*....|....*....|....*.
gi 22327099 552 ifklaQ----GEYIAPEKIENVYTKcrfvsqcfiHGDSFNSSLVAI 593
Cdd:COG1021 434 -----QinrgGEKIAAEEVENLLLA---------HPAVHDAAVVAM 465
|
|
| PRK06178 |
PRK06178 |
acyl-CoA synthetase; Validated |
120-567 |
9.26e-28 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 235724 [Multi-domain] Cd Length: 567 Bit Score: 118.61 E-value: 9.26e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327099 120 TYGE--AASERQAigSGLLFHGVNQGDCVGLYFINRPEWLVVDHAC----AAYSFVSvPLYDTLgpdAVKFVVNHANLQA 193
Cdd:PRK06178 60 TYAEldELSDRFA--ALLRQRGVGAGDRVAVFLPNCPQFHIVFFGIlklgAVHVPVS-PLFREH---ELSYELNDAGAEV 133
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327099 194 IFCVPQTLNILLSFLAEIpSIRLIVVVGGAD--EHLPSLP-----RGTGVTIVSYQKLLS--QGRSSLHPFSPPKPEDIA 264
Cdd:PRK06178 134 LLALDQLAPVVEQVRAET-SLRHVIVTSLADvlPAEPTLPlpdslRAPRLAAAGAIDLLPalRACTAPVPLPPPALDALA 212
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327099 265 TICYTSGTTGTPKGVVLTHGNLI----ANVAGSSVEAEffpSDVYISYLPLAHIyeranqimgvyGGvavgfyqgdvfkl 340
Cdd:PRK06178 213 ALNYTGGTTGMPKGCEHTQRDMVytaaAAYAVAVVGGE---DSVFLSFLPEFWI-----------AG------------- 265
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327099 341 mDDFAVLRPTIFCSVPRLYNRiYD--GITSAVKSSGVVK--------------KRLFEIAYNSKKQAiingrtpsafwdk 404
Cdd:PRK06178 266 -ENFGLLFPLFSGATLVLLAR-WDavAFMAAVERYRVTRtvmlvdnavelmdhPRFAEYDLSSLRQV------------- 330
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327099 405 lvfnkikeklgGRVRFMgsgaSPLSPDVMDFLRICFGCSVREG-YGMTET-SC--VISAMDDGD-NLSGH---VGSPNPA 476
Cdd:PRK06178 331 -----------RVVSFV----KKLNPDYRQRWRALTGSVLAEAaWGMTEThTCdtFTAGFQDDDfDLLSQpvfVGLPVPG 395
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327099 477 CEVKLVDVPemnyTSDDQPY-PRGEICVRGPIIFKGYYKDEEQTREILDgDGWLHTGDIGLWLPGGRLKIIDRKKNIFKL 555
Cdd:PRK06178 396 TEFKICDFE----TGELLPLgAEGEIVVRTPSLLKGYWNKPEATAEALR-DGWLHTGDIGKIDEQGFLHYLGRRKEMLKV 470
|
490
....*....|..
gi 22327099 556 aQGEYIAPEKIE 567
Cdd:PRK06178 471 -NGMSVFPSEVE 481
|
|
| PRK08633 |
PRK08633 |
2-acyl-glycerophospho-ethanolamine acyltransferase; Validated |
255-548 |
1.94e-27 |
|
2-acyl-glycerophospho-ethanolamine acyltransferase; Validated
Pssm-ID: 236315 [Multi-domain] Cd Length: 1146 Bit Score: 118.87 E-value: 1.94e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327099 255 FSPPKPEDIATICYTSGTTGTPKGVVLTHGNLIANVAGSSVEAEFFPSDVYISYLPLAHIYE-RANQIMGVYGGVAVGFY 333
Cdd:PRK08633 776 GPTFKPDDTATIIFSSGSEGEPKGVMLSHHNILSNIEQISDVFNLRNDDVILSSLPFFHSFGlTVTLWLPLLEGIKVVYH 855
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327099 334 QG--DVFKLMDDFAVLRPTIFCSVP---RLYNRiydgitsavkssgvvKKRLfeiaynskkqaiingrtpsafwDKLVFN 408
Cdd:PRK08633 856 PDptDALGIAKLVAKHRATILLGTPtflRLYLR---------------NKKL----------------------HPLMFA 898
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327099 409 KIkeklggrvRFMGSGASPLSPDVMDFLRICFGCSVREGYGMTETSCVIS-----AMDDGD-----NLSGHVGSPNPACE 478
Cdd:PRK08633 899 SL--------RLVVAGAEKLKPEVADAFEEKFGIRILEGYGATETSPVASvnlpdVLAADFkrqtgSKEGSVGMPLPGVA 970
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 22327099 479 VKLVDvPEmNYtsddQPYPRGE---ICVRGPIIFKGYYKDEEQTREIL---DGDGWLHTGDIGLWLPGGRLKIIDR 548
Cdd:PRK08633 971 VRIVD-PE-TF----EELPPGEdglILIGGPQVMKGYLGDPEKTAEVIkdiDGIGWYVTGDKGHLDEDGFLTITDR 1040
|
|
| AA-adenyl-dom |
TIGR01733 |
amino acid adenylation domain; This model represents a domain responsible for the specific ... |
120-579 |
4.71e-27 |
|
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: 114.28 E-value: 4.71e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327099 120 TYGEAASERQAIGSGLL-FHGVNQGDCVGLYFiNRPEWLVVD-HAC----AAYsfvsVPLyDTLGPDAvkfvvnhanlqa 193
Cdd:TIGR01733 1 TYRELDERANRLARHLRaAGGVGPGDRVAVLL-ERSAELVVAiLAVlkagAAY----VPL-DPAYPAE------------ 62
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327099 194 ifcvpqtlniLLSFLAEIPSIRLIVVvggaDEHLPSLPRGTGVTIVSYQ----KLLSQGRSSLHPFSPPKPEDIATICYT 269
Cdd:TIGR01733 63 ----------RLAFILEDAGARLLLT----DSALASRLAGLVLPVILLDplelAALDDAPAPPPPDAPSGPDDLAYVIYT 128
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327099 270 SGTTGTPKGVVLTHGNLIANVAGSSVEAEFFPSDVYISYLPLAHiyeranqimgvyggvavgfyqgdvfklmdDFAVLrp 349
Cdd:TIGR01733 129 SGSTGRPKGVVVTHRSLVNLLAWLARRYGLDPDDRVLQFASLSF-----------------------------DASVE-- 177
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327099 350 TIFcsvPRLYNriydGITSAVKSSGVVKKRLFEIAYNSKKQAI--INGrTPSAF--WDKLvfnkiKEKLGGRVRFMGSGA 425
Cdd:TIGR01733 178 EIF---GALLA----GATLVVPPEDEERDDAALLAALIAEHPVtvLNL-TPSLLalLAAA-----LPPALASLRLVILGG 244
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327099 426 SPLSPDVMD-FLRICFGCSVREGYGMTETSCV-----ISAMDDGDNLSGHVGSPNPACEVKLVDvpemnytSDDQPYPR- 498
Cdd:TIGR01733 245 EALTPALVDrWRARGPGARLINLYGPTETTVWstatlVDPDDAPRESPVPIGRPLANTRLYVLD-------DDLRPVPVg 317
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327099 499 --GEICVRGPIIFKGYYKDEEQTRE--------ILDGDGWLHTGDIGLWLPGGRLKIIDRKKNIFKLaQGEYIAPEKIEN 568
Cdd:TIGR01733 318 vvGELYIGGPGVARGYLNRPELTAErfvpdpfaGGDGARLYRTGDLVRYLPDGNLEFLGRIDDQVKI-RGYRIELGEIEA 396
|
490
....*....|.
gi 22327099 569 VYTKCRFVSQC 579
Cdd:TIGR01733 397 ALLRHPGVREA 407
|
|
| PRK08316 |
PRK08316 |
acyl-CoA synthetase; Validated |
114-571 |
1.25e-26 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 181381 [Multi-domain] Cd Length: 523 Bit Score: 114.64 E-value: 1.25e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327099 114 GEYSWmTYGE--AASERQAigSGLLFHGVNQGDCVGLYFINRPEWLVVDHACAAYSFVSVPLYDTLGPDAVKFVVNHANL 191
Cdd:PRK08316 33 GDRSW-TYAEldAAVNRVA--AALLDLGLKKGDRVAALGHNSDAYALLWLACARAGAVHVPVNFMLTGEELAYILDHSGA 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327099 192 QAIFCVPQTLNILLSFLAEIPSIRLIVVVGGAdehlPSLPRGTGVTIVSyqklLSQGRSSLHPFSPPKPEDIATICYTSG 271
Cdd:PRK08316 110 RAFLVDPALAPTAEAALALLPVDTLILSLVLG----GREAPGGWLDFAD----WAEAGSVAEPDVELADDDLAQILYTSG 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327099 272 TTGTPKGVVLTHGNLIANVAGSSVEAEFFPSDVYISYLPLAHiyeranqimgvyggVAvgfyQGDVFkLMDDFAVLRPTI 351
Cdd:PRK08316 182 TESLPKGAMLTHRALIAEYVSCIVAGDMSADDIPLHALPLYH--------------CA----QLDVF-LGPYLYVGATNV 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327099 352 FCSVP---RLYNRI-YDGITSavkssgvvkkrLFeiaynskkqaiingrTPSAFWDKL----VFNKikeklggrvRFMGS 423
Cdd:PRK08316 243 ILDAPdpeLILRTIeAERITS-----------FF---------------APPTVWISLlrhpDFDT---------RDLSS 287
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327099 424 ------GASPLSPDVMDFLRICF-GCSVREGYGMTETSCVISAM--DDGDNLSGHVGSPNPACEVKLVDvPEMNYTSDDQ 494
Cdd:PRK08316 288 lrkgyyGASIMPVEVLKELRERLpGLRFYNCYGQTEIAPLATVLgpEEHLRRPGSAGRPVLNVETRVVD-DDGNDVAPGE 366
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 22327099 495 PyprGEICVRGPIIFKGYYKDEEQTREILDGdGWLHTGDIGLWLPGGRLKIIDRKKNIFKLAqGEYIAPEKIEN-VYT 571
Cdd:PRK08316 367 V---GEIVHRSPQLMLGYWDDPEKTAEAFRG-GWFHSGDLGVMDEEGYITVVDRKKDMIKTG-GENVASREVEEaLYT 439
|
|
| MACS_AAE_MA_like |
cd05970 |
Medium-chain acyl-CoA synthetase (MACS) of AAE_MA like; MACS catalyzes the two-step activation ... |
114-613 |
1.27e-26 |
|
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: 114.51 E-value: 1.27e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327099 114 GEYSWMTYGEAASERQAIGSGLLFHGVNQGDCVGLYFINRPEWLVVDHACAAYSFVSVPLYDTLGPDAVKFVVNHANLQA 193
Cdd:cd05970 43 GEERIFTFAELADYSDKTANFFKAMGIGKGDTVMLTLKRRYEFWYSLLALHKLGAIAIPATHQLTAKDIVYRIESADIKM 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327099 194 IFCVpQTLNILLSF---LAEIPSIRLIVVVGGadehlpSLPRGtgvtIVSYQKLLSQGRSSLHP---FSPPKPEDIATIC 267
Cdd:cd05970 123 IVAI-AEDNIPEEIekaAPECPSKPKLVWVGD------PVPEG----WIDFRKLIKNASPDFERptaNSYPCGEDILLVY 191
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327099 268 YTSGTTGTPKGVVLTHGNLIANVAGSSVEAEFFPSDVYISYLPLAHIYERANQIMGVY-GGVAVGFYQGDVF---KLMDD 343
Cdd:cd05970 192 FSSGTTGMPKMVEHDFTYPLGHIVTAKYWQNVREGGLHLTVADTGWGKAVWGKIYGQWiAGAAVFVYDYDKFdpkALLEK 271
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327099 344 FAVLRPTIFCSVPRLYNRIydgitsavkssgvVKKRLFEIAYNSKKQAIINGRtpsafwdklvfnkikeklggrvrfmgs 423
Cdd:cd05970 272 LSKYGVTTFCAPPTIYRFL-------------IREDLSRYDLSSLRYCTTAGE--------------------------- 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327099 424 gasPLSPDVMDFLRICFGCSVREGYGMTETSCVISAMDDGDNLSGHVGSPNPACEVKLVDvpemnytSDDQPYP---RGE 500
Cdd:cd05970 312 ---ALNPEVFNTFKEKTGIKLMEGFGQTETTLTIATFPWMEPKPGSMGKPAPGYEIDLID-------REGRSCEageEGE 381
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327099 501 ICVR----GPI-IFKGYYKDEEQTREILDgDGWLHTGDIGLWLPGGRLKIIDRKKNIFKlAQGEYIAPEKIENVYTKCRF 575
Cdd:cd05970 382 IVIRtskgKPVgLFGGYYKDAEKTAEVWH-DGYYHTGDAAWMDEDGYLWFVGRTDDLIK-SSGYRIGPFEVESALIQHPA 459
|
490 500 510 520
....*....|....*....|....*....|....*....|
gi 22327099 576 VSQCFIHG--DSFNSSLVAIVSVdpeVMKDWAASEGIKYE 613
Cdd:cd05970 460 VLECAVTGvpDPIRGQVVKATIV---LAKGYEPSEELKKE 496
|
|
| FadD3 |
cd17638 |
acyl-CoA synthetase FadD3 and similar proteins; This family contains long chain fatty acid CoA ... |
262-601 |
1.79e-26 |
|
acyl-CoA synthetase FadD3 and similar proteins; This family contains long chain fatty acid CoA ligases, including FadD3 which is an acyl-CoA synthetase that initiates catabolism of cholesterol rings C and D in actinobacteria. The cholesterol catabolic pathway occurs in most mycolic acid-containing actinobacteria, such as Rhodococcus jostii RHA1, and is critical for Mycobacterium tuberculosis (Mtb) during infection. FadD3 catalyzes the ATP-dependent CoA thioesterification of 3a-alpha-H-4alpha(3'-propanoate)-7a-beta-methylhexahydro-1,5-indanedione (HIP) to yield HIP-CoA. Hydroxylated analogs of HIP, 5alpha-OH HIP and 1beta-OH HIP, can also be used.
Pssm-ID: 341293 [Multi-domain] Cd Length: 330 Bit Score: 111.05 E-value: 1.79e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327099 262 DIATICYTSGTTGTPKGVVLTHGNLIANVAGSSVEAEFFPSDVYISYLPLAHIYeranqimGVYGGVAVGFYQG------ 335
Cdd:cd17638 1 DVSDIMFTSGTTGRSKGVMCAHRQTLRAAAAWADCADLTEDDRYLIINPFFHTF-------GYKAGIVACLLTGatvvpv 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327099 336 ---DVFKLMDDFAVLRPTIFCSVPRLYNRIYDgitsavkssgVVKKRLFEIAynSKKQAIingrTPSAFWDKLVFNKIKE 412
Cdd:cd17638 74 avfDVDAILEAIERERITVLPGPPTLFQSLLD----------HPGRKKFDLS--SLRAAV----TGAATVPVELVRRMRS 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327099 413 KLGgrvrFMgsgasplspdvmdflricfgcSVREGYGMTEtsCVISAM----DDGDNLSGHVGSPNPACEVKLVDvpemn 488
Cdd:cd17638 138 ELG----FE---------------------TVLTAYGLTE--AGVATMcrpgDDAETVATTCGRACPGFEVRIAD----- 185
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327099 489 ytsddqpypRGEICVRGPIIFKGYYKDEEQTREILDGDGWLHTGDIGLWLPGGRLKIIDRKKNIFkLAQGEYIAPEKIEN 568
Cdd:cd17638 186 ---------DGEVLVRGYNVMQGYLDDPEATAEAIDADGWLHTGDVGELDERGYLRITDRLKDMY-IVGGFNVYPAEVEG 255
|
330 340 350
....*....|....*....|....*....|...
gi 22327099 569 VYTKCRFVSQcfihgdsfnsslVAIVSVDPEVM 601
Cdd:cd17638 256 ALAEHPGVAQ------------VAVIGVPDERM 276
|
|
| PTZ00297 |
PTZ00297 |
pantothenate kinase; Provisional |
113-698 |
4.20e-26 |
|
pantothenate kinase; Provisional
Pssm-ID: 140318 [Multi-domain] Cd Length: 1452 Bit Score: 114.95 E-value: 4.20e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327099 113 IGEYSWMTYGEAASERQAIGSGLLFHGVNQGDCVGLYFINRPEWLVVDHACAAYSFVSVPLYDTlgPDAVKFVVNHANLQ 192
Cdd:PTZ00297 452 SGESEWLTYGTVDARARELGSGLLALGVRPGDVIGVDCEASRNIVILEVACALYGFTTLPLVGK--GSTMRTLIDEHKIK 529
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327099 193 AIFCVPQTLNILLSflaeIPSIRLIVVV---GGADEHLPSLPRGTGVTIVSYQKLLSQGRSSLHPFsPPKPEDIATICYT 269
Cdd:PTZ00297 530 VVFADRNSVAAILT----CRSRKLETVVythSFYDEDDHAVARDLNITLIPYEFVEQKGRLCPVPL-KEHVTTDTVFTYV 604
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327099 270 SGTTGTPKG-----VVLTHGNL---IANVAGSSVEAEFFPSDVYISYLPLAHIYERANqIMGVYG-GVAVGfyQGDVFKL 340
Cdd:PTZ00297 605 VDNTTSASGdglavVRVTHADVlrdISTLVMTGVLPSSFKKHLMVHFTPFAMLFNRVF-VLGLFAhGSAVA--TVDAAHL 681
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327099 341 MDDFAVLRPTIFCSVPRLYNriydgiTSAVKSS------GVVKKRLFEIAYNSKKQAIINGRTPSAFWDKLVFNKIKEKL 414
Cdd:PTZ00297 682 QRAFVKFQPTILVAAPSLFS------TSRLQLSranerySAVYSWLFERAFQLRSRLINIHRRDSSLLRFIFFRATQELL 755
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327099 415 GGRVR--FMGSGASPLSPDVMDFLRICFGCSVRE-GYGMTETSCVISamddgdnlsghvGSPNPACEVKLVDVPEMnytS 491
Cdd:PTZ00297 756 GGCVEkiVLCVSEESTSFSLLEHISVCYVPCLREvFFLPSEGVFCVD------------GTPAPSLQVDLEPFDEP---S 820
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327099 492 DDQPYPRGEICVRGpiifkgyykDEEQTREIldgdgwlhtgdIGLWLPGGRLKIIDRKKNIFKLAQGEYIAPEKIENVYT 571
Cdd:PTZ00297 821 DGAGIGQLVLAKKG---------EPRRTLPI-----------AAQWKRDRTLRLLGPPLGILLPVAYEYVIAAELERIFS 880
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327099 572 KCRFVSQCFIHGDSfNSSLVAIVSVDPEVMK-DWAASegikyeHLGQLCNDPRVR-----------KTVLAEMDDLGREA 639
Cdd:PTZ00297 881 QSRYVNDIFLYADP-SRPIIAIVSPNRDTVEfEWRQS------HCMGEGGGPARQlgwtelvayasSLLTADFACIAKEN 953
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|....*....
gi 22327099 640 QLRGFEFAKAVTLVPEPFTLENGLLTPTFKIKRPQAKAYFAEAISKMYAEiAASNPIPS 698
Cdd:PTZ00297 954 GLHPSNVPEYVHLHPHAFKDHSTFLTPYGKIRRDAVHSYFSSVIERFYSD-VETTPLPT 1011
|
|
| MACS_like_3 |
cd05971 |
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the ... |
110-572 |
5.59e-26 |
|
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: 111.37 E-value: 5.59e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327099 110 DGTIGEYswmTYGEAASERQAIGSGLLFHGVNQGDCVGLYFINRPEWLVVDHACAAYSFVSVPLYDTLGPDAVKFVVNHA 189
Cdd:cd05971 1 KGTPEKV---TFKELKTASNRFANVLKEIGLEKGDRVGVFLSQGPECAIAHIAILRSGAIAVPLFALFGPEALEYRLSNS 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327099 190 NLQAIfcvpqtlnillsflaeipsirlivVVGGADehlpslprgtgvtivsyqkllsqgrsslhpfsppkpeDIATICYT 269
Cdd:cd05971 78 GASAL------------------------VTDGSD-------------------------------------DPALIIYT 96
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327099 270 SGTTGTPKGVVLTHGNLIANVAGSSVEAEFFPSDVYISYLPL--AHIyeranqimgvyGGVavgfyqgdvfklmddFAVL 347
Cdd:cd05971 97 SGTTGPPKGALHAHRVLLGHLPGVQFPFNLFPRDGDLYWTPAdwAWI-----------GGL---------------LDVL 150
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327099 348 RPTIFCSVPRLynriydgitsAVKSSGVVKKRLFEI-AYNSKKQAIIngrTPSAFwdKLV--FNKIKEKLGGRVRFMGSG 424
Cdd:cd05971 151 LPSLYFGVPVL----------AHRMTKFDPKAALDLmSRYGVTTAFL---PPTAL--KMMrqQGEQLKHAQVKLRAIATG 215
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327099 425 ASPLSPDVMDFLRICFGCSVREGYGMTETSCVISAMDD-GDNLSGHVGSPNPACEVKLVDvpemnytSDDQPYP---RGE 500
Cdd:cd05971 216 GESLGEELLGWAREQFGVEVNEFYGQTECNLVIGNCSAlFPIKPGSMGKPIPGHRVAIVD-------DNGTPLPpgeVGE 288
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 22327099 501 ICVR--GPIIFKGYYKDEEQTREILDGDgWLHTGDIGLWLPGGRLKIIDRKKNIFKLAqGEYIAPEKIENVYTK 572
Cdd:cd05971 289 IAVElpDPVAFLGYWNNPSATEKKMAGD-WLLTGDLGRKDSDGYFWYVGRDDDVITSS-GYRIGPAEIEECLLK 360
|
|
| PRK09088 |
PRK09088 |
acyl-CoA synthetase; Validated |
117-569 |
6.07e-26 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 181644 [Multi-domain] Cd Length: 488 Bit Score: 112.21 E-value: 6.07e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327099 117 SWmTYGEAASERQAIGSGLLFHGVNQGDCVGLYFINRPeWLVVDH-ACAAYSFVSVPLYDTLGPdavkfvvnhANLQAIF 195
Cdd:PRK09088 22 RW-TYAELDALVGRLAAVLRRRGCVDGERLAVLARNSV-WLVALHfACARVGAIYVPLNWRLSA---------SELDALL 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327099 196 --CVPqtlnillsflaeipsiRLIVvvggADEHLPSLpRGTGVTIVSYQKLLSQGRSSLHPFSPPkpEDIATICYTSGTT 273
Cdd:PRK09088 91 qdAEP----------------RLLL----GDDAVAAG-RTDVEDLAAFIASADALEPADTPSIPP--ERVSLILFTSGTS 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327099 274 GTPKGVVLTHGNLIANVAGSSVEAEFFPSDVYISYLPLAHIYERANQIMGV--YGG---VAVGFYQGDVFKLMDDFAVLR 348
Cdd:PRK09088 148 GQPKGVMLSERNLQQTAHNFGVLGRVDAHSSFLCDAPMFHIIGLITSVRPVlaVGGsilVSNGFEPKRTLGRLGDPALGI 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327099 349 PTIFCsVPRLYNRIYDGITsavkssgvvkkrlFEIAYNSKKQAIINGrtpsafwdklvfnkikeklggrvrfmgsGASPL 428
Cdd:PRK09088 228 THYFC-VPQMAQAFRAQPG-------------FDAAALRHLTALFTG----------------------------GAPHA 265
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327099 429 SPDVMDFLRIcfGCSVREGYGMTETSCVISAMDDGDNLSGHVGS---PNPACEVKLVDvpemNYTSDDQPYPRGEICVRG 505
Cdd:PRK09088 266 AEDILGWLDD--GIPMVDGFGMSEAGTVFGMSVDCDVIRAKAGAagiPTPTVQTRVVD----DQGNDCPAGVPGELLLRG 339
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 22327099 506 PIIFKGYYKDEEQTREILDGDGWLHTGDIGLWLPGGRLKIIDRKKNIFkLAQGEYIAPEKIENV 569
Cdd:PRK09088 340 PNLSPGYWRRPQATARAFTGDGWFRTGDIARRDADGFFWVVDRKKDMF-ISGGENVYPAEIEAV 402
|
|
| PRK06155 |
PRK06155 |
crotonobetaine/carnitine-CoA ligase; Provisional |
94-569 |
6.12e-26 |
|
crotonobetaine/carnitine-CoA ligase; Provisional
Pssm-ID: 235719 [Multi-domain] Cd Length: 542 Bit Score: 112.54 E-value: 6.12e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327099 94 VETYAEnkylGTRVRSDGTigeysWMTYGEAASERQAIGSGLLFHGVNQGDCVGLYFINRPEWLVVDHACAAYSFVSVPL 173
Cdd:PRK06155 31 AERYPD----RPLLVFGGT-----RWTYAEAARAAAAAAHALAAAGVKRGDRVALMCGNRIEFLDVFLGCAWLGAIAVPI 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327099 174 -YDTLGPDAVKFVVNhANLQAIFCVPQTLNILLSFLAEIPSIRLIVVVGGADEhlPSLPRGTGVTIvsyqklLSQGRSSL 252
Cdd:PRK06155 102 nTALRGPQLEHILRN-SGARLLVVEAALLAALEAADPGDLPLPAVWLLDAPAS--VSVPAGWSTAP------LPPLDAPA 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327099 253 hPFSPPKPEDIATICYTSGTTGTPKGVVLTHGNLIANVAGSSVEAEFFPSDVYISYLPLAHIYERAnqimgvyggvavGF 332
Cdd:PRK06155 173 -PAAAVQPGDTAAILYTSGTTGPSKGVCCPHAQFYWWGRNSAEDLEIGADDVLYTTLPLFHTNALN------------AF 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327099 333 YQGdvfKLMDDFAVLRPTIFCSvprlynRIYDgitSAVKSSGVVKKRLFEIAynskkqAIINGRTPSAfwdklvfnkikE 412
Cdd:PRK06155 240 FQA---LLAGATYVLEPRFSAS------GFWP---AVRRHGATVTYLLGAMV------SILLSQPARE-----------S 290
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327099 413 KLGGRVRFMGSGASPlsPDVMDFLRICFGCSVREGYGMTETSCVIsAMDDGDNLSGHVGSPNPACEVKLVD-----VPem 487
Cdd:PRK06155 291 DRAHRVRVALGPGVP--AALHAAFRERFGVDLLDGYGSTETNFVI-AVTHGSQRPGSMGRLAPGFEARVVDehdqeLP-- 365
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327099 488 nytsDDQPyprGEICVRG--PIIF-KGYYKDEEQTREILDgDGWLHTGDIGLWLPGGRLKIIDRKKNIFKlAQGEYIAPE 564
Cdd:PRK06155 366 ----DGEP---GELLLRAdePFAFaTGYFGMPEKTVEAWR-NLWFHTGDRVVRDADGWFRFVDRIKDAIR-RRGENISSF 436
|
....*
gi 22327099 565 KIENV 569
Cdd:PRK06155 437 EVEQV 441
|
|
| PRK06710 |
PRK06710 |
long-chain-fatty-acid--CoA ligase; Validated |
257-569 |
2.70e-25 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 180666 [Multi-domain] Cd Length: 563 Bit Score: 110.89 E-value: 2.70e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327099 257 PPKPE-DIATICYTSGTTGTPKGVVLTHGNLIANVAG------SSVEAEffpsDVYISYLPLAHIYeranqimGVYGGVA 329
Cdd:PRK06710 201 PCDPEnDLALLQYTGGTTGFPKGVMLTHKNLVSNTLMgvqwlyNCKEGE----EVVLGVLPFFHVY-------GMTAVMN 269
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327099 330 VGFYQGDVFKLMDDFAVlrptifcsvprlynriydgitsavkssgvvkKRLFEiAYNSKKQAIINGrTPSAFWDKLVFNK 409
Cdd:PRK06710 270 LSIMQGYKMVLIPKFDM-------------------------------KMVFE-AIKKHKVTLFPG-APTIYIALLNSPL 316
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327099 410 IKEKLGGRVRFMGSGASPLSPDVMDFLRICFGCSVREGYGMTETSCVI-SAMDDGDNLSGHVGSPNPACEVKLVDVPEMN 488
Cdd:PRK06710 317 LKEYDISSIRACISGSAPLPVEVQEKFETVTGGKLVEGYGLTESSPVThSNFLWEKRVPGSIGVPWPDTEAMIMSLETGE 396
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327099 489 YTsddQPYPRGEICVRGPIIFKGYYKDEEQTREILDgDGWLHTGDIGLWLPGGRLKIIDRKKNIFkLAQGEYIAPEKIEN 568
Cdd:PRK06710 397 AL---PPGEIGEIVVKGPQIMKGYWNKPEETAAVLQ-DGWLHTGDVGYMDEDGFFYVKDRKKDMI-VASGFNVYPREVEE 471
|
.
gi 22327099 569 V 569
Cdd:PRK06710 472 V 472
|
|
| PRK06145 |
PRK06145 |
acyl-CoA synthetase; Validated |
119-598 |
4.96e-25 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 102207 [Multi-domain] Cd Length: 497 Bit Score: 109.21 E-value: 4.96e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327099 119 MTYGEAASERQAIGSGLLFHGVNQGDCVGLYFINRPEWLVVDHACAAYSFVSVPLYDTLGPDAVKFVVNHANLQAIFCVP 198
Cdd:PRK06145 28 ISYAEFHQRILQAAGMLHARGIGQGDVVALLMKNSAAFLELAFAASYLGAVFLPINYRLAADEVAYILGDAGAKLLLVDE 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327099 199 QtlnillsfLAEIPSIRLIVVVGGADEHLPSlprgtgvtivsyqKLLSQGRSSLHPFSPPKPEDIATICYTSGTTGTPKG 278
Cdd:PRK06145 108 E--------FDAIVALETPKIVIDAAAQADS-------------RRLAQGGLEIPPQAAVAPTDLVRLMYTSGTTDRPKG 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327099 279 VVLTHGNLIANVAGSSVEAEFFPSDVYISYLPLAHIyeranqimGVYG--GVAVgFYQGDVFKLMDDFAVlrPTIFCSVP 356
Cdd:PRK06145 167 VMHSYGNLHWKSIDHVIALGLTASERLLVVGPLYHV--------GAFDlpGIAV-LWVGGTLRIHREFDP--EAVLAAIE 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327099 357 RlyNRIYDGITSAVKSSGVV---KKRLFEIayNSKKQAIING-RTPSAfwdklvfnkikeklggRVRfmgsgasplspdv 432
Cdd:PRK06145 236 R--HRLTCAWMAPVMLSRVLtvpDRDRFDL--DSLAWCIGGGeKTPES----------------RIR------------- 282
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327099 433 mDFLRICFGCSVREGYGMTETSCVISAMDDGDNLS--GHVGSPNPACEVKLVDvpemnytsDD----QPYPRGEICVRGP 506
Cdd:PRK06145 283 -DFTRVFTRARYIDAYGLTETCSGDTLMEAGREIEkiGSTGRALAHVEIRIAD--------GAgrwlPPNMKGEICMRGP 353
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327099 507 IIFKGYYKDEEQTREILDGDgWLHTGDIGLWLPGGRLKIIDRKKNIFkLAQGEYIAPEKIENVYTKCRFVSQCFI---HG 583
Cdd:PRK06145 354 KVTKGYWKDPEKTAEAFYGD-WFRSGDVGYLDEEGFLYLTDRKKDMI-ISGGENIASSEVERVIYELPEVAEAAVigvHD 431
|
490
....*....|....*
gi 22327099 584 DSFNSSLVAIVSVDP 598
Cdd:PRK06145 432 DRWGERITAVVVLNP 446
|
|
| ACLS-CaiC |
cd17637 |
acyl-CoA synthetase (AMP-forming)/AMP-acid ligase II; This family contains fatty acid CoA ... |
266-569 |
5.39e-25 |
|
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: 106.59 E-value: 5.39e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327099 266 ICYTSGTTGTPKGVVLTHGNLIANVAGSSVEAEFFPSDVYISYLPLAHIyeranqiMGVYGGVAVgFYQGDVFKLMDDFA 345
Cdd:cd17637 5 IIHTAAVAGRPRGAVLSHGNLIAANLQLIHAMGLTEADVYLNMLPLFHI-------AGLNLALAT-FHAGGANVVMEKFD 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327099 346 VL---------RPTIFCSVPRLYNRIYDgitsavkssgvvkkrlfeiaynskkQAIINGRTPSAFwdKLVfnkikeklgg 416
Cdd:cd17637 77 PAealelieeeKVTLMGSFPPILSNLLD-------------------------AAEKSGVDLSSL--RHV---------- 119
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327099 417 rvrfmgSGASplSPDVMDFLRICFGCSVREGYGMTETSCVISaMDDGDNLSGHVGSPNPACEVKLVDvpemnytSDDQPY 496
Cdd:cd17637 120 ------LGLD--APETIQRFEETTGATFWSLYGQTETSGLVT-LSPYRERPGSAGRPGPLVRVRIVD-------DNDRPV 183
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 22327099 497 PR---GEICVRGPIIFKGYYKDEEQTREILDGdGWLHTGDIGLWLPGGRLKIIDRK--KNIFKlAQGEYIAPEKIENV 569
Cdd:cd17637 184 PAgetGEIVVRGPLVFQGYWNLPELTAYTFRN-GWHHTGDLGRFDEDGYLWYAGRKpeKELIK-PGGENVYPAEVEKV 259
|
|
| PRK05852 |
PRK05852 |
fatty acid--CoA ligase family protein; |
131-600 |
5.44e-25 |
|
fatty acid--CoA ligase family protein;
Pssm-ID: 235625 [Multi-domain] Cd Length: 534 Bit Score: 109.59 E-value: 5.44e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327099 131 IGSGLLFHGVNQGDCVGLYFINRPEWLVVDHACAAYSFVSVPLyDTLGPDAVKFVvnhaNLQAIFCvpqtlnillsflae 210
Cdd:PRK05852 56 LAGQLTRSGLLPGDRVALRMGSNAEFVVALLAASRADLVVVPL-DPALPIAEQRV----RSQAAGA-------------- 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327099 211 ipSIRLIVVVGGADEHLPSLPRGTGVTIVSYQKLLSQGRSSLHPFSPPKP-----------EDIATICYTSGTTGTPKGV 279
Cdd:PRK05852 117 --RVVLIDADGPHDRAEPTTRWWPLTVNVGGDSGPSGGTLSVHLDAATEPtpatstpeglrPDDAMIMFTGGTTGLPKMV 194
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327099 280 VLTHGNLIANVAGSSVEAEFFPSDVYISYLPLAHIYERANQIMG--VYGGV----AVGFYQGDVFklMDDFAVLRPTIFC 353
Cdd:PRK05852 195 PWTHANIASSVRAIITGYRLSPRDATVAVMPLYHGHGLIAALLAtlASGGAvllpARGRFSAHTF--WDDIKAVGATWYT 272
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327099 354 SVPRLYnRIydgitsavkssgvvkkrLFEIAYNSKkqaiiNGRTPSAfwdklvfnkikeklggrVRFMGSGASPLSPDVM 433
Cdd:PRK05852 273 AVPTIH-QI-----------------LLERAATEP-----SGRKPAA-----------------LRFIRSCSAPLTAETA 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327099 434 DFLRICFGCSVREGYGMTETSCVISAMddgdNLSGHVGSPNPACEVKLVDV---PEMNYT-SDDQPYPR---GEICVRGP 506
Cdd:PRK05852 313 QALQTEFAAPVVCAFGMTEATHQVTTT----QIEGIGQTENPVVSTGLVGRstgAQIRIVgSDGLPLPAgavGEVWLRGT 388
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327099 507 IIFKGYYKDEEQTREILDgDGWLHTGDIGLWLPGGRLKIIDRKKNIFKLAqGEYIAPEKIENVYTKCRFVSQCFIHG--D 584
Cdd:PRK05852 389 TVVRGYLGDPTITAANFT-DGWLRTGDLGSLSAAGDLSIRGRIKELINRG-GEKISPERVEGVLASHPNVMEAAVFGvpD 466
|
490
....*....|....*.
gi 22327099 585 SFNSSLVAIVSVDPEV 600
Cdd:PRK05852 467 QLYGEAVAAVIVPRES 482
|
|
| ligase_PEP_1 |
TIGR03098 |
acyl-CoA ligase (AMP-forming), exosortase A-associated; This group of proteins contains an ... |
119-583 |
6.51e-25 |
|
acyl-CoA ligase (AMP-forming), exosortase A-associated; This group of proteins contains an AMP-binding domain (pfam00501) associated with acyl CoA-ligases. These proteins are generally found in genomes containing the exosortase/PEP-CTERM protein expoert system, specifically the type 1 variant of this system described by the Genome Property GenProp0652. When found in this context they are invariably present next to a decarboxylase enzyme. A number of sequences from Burkholderia species also hit this model, but the genomic context is obviously different. The hypothesis of a constant substrate for this family is only strong where the exosortase context is present.
Pssm-ID: 211788 [Multi-domain] Cd Length: 517 Bit Score: 109.10 E-value: 6.51e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327099 119 MTYgEAASER-QAIGSGLLFHGVNQGDCVGLYFINRPEWLVVDHACAAYSFVSVPLYDTLGPDAVKFVVNHANLQAIFCV 197
Cdd:TIGR03098 26 LTY-AALSERvLALASGLRGLGLARGERVAIYLDKRLETVTAMFGAALAGGVFVPINPLLKAEQVAHILADCNVRLLVTS 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327099 198 PQTLNILLSFLAEIPSIRLIVVVGGADEHLPSLPrgtGVTIVSYQKLLSQGRSSlhPFSPPKPEDIATICYTSGTTGTPK 277
Cdd:TIGR03098 105 SERLDLLHPALPGCHDLRTLIIVGDPAHASEGHP---GEEPASWPKLLALGDAD--PPHPVIDSDMAAILYTSGSTGRPK 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327099 278 GVVLTHGNLIANVAGSSVEAEFFPSDVYISYLPLAHIYERaNQIMgvyggvaVGFYQGDVFKLMDDFavlrptifcsVPR 357
Cdd:TIGR03098 180 GVVLSHRNLVAGAQSVATYLENRPDDRLLAVLPLSFDYGF-NQLT-------TAFYVGATVVLHDYL----------LPR 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327099 358 lynriyDGITSavkssgVVKKRLFEIAynskkqaiinGRTPsaFWDKLVFNKIKEKLGGRVRFMGSGASPLSPDVMDFLR 437
Cdd:TIGR03098 242 ------DVLKA------LEKHGITGLA----------AVPP--LWAQLAQLDWPESAAPSLRYLTNSGGAMPRATLSRLR 297
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327099 438 ICFGCS-VREGYGMTET--SCVISAmDDGDNLSGHVGSPNPACEVkLVDVPEMNYTSDDQPyprGEICVRGPIIFKGYYK 514
Cdd:TIGR03098 298 SFLPNArLFLMYGLTEAfrSTYLPP-EEVDRRPDSIGKAIPNAEV-LVLREDGSECAPGEE---GELVHRGALVAMGYWN 372
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327099 515 DEEQTREILDG----DGWLHTGDIGLWlPG--------GRLKIIDRKKNIFKLAqGEYIAPEKIENVYTKCRFVSQCFIH 582
Cdd:TIGR03098 373 DPEKTAERFRPlppfPGELHLPELAVW-SGdtvrrdeeGFLYFVGRRDEMIKTS-GYRVSPTEVEEVAYATGLVAEAVAF 450
|
.
gi 22327099 583 G 583
Cdd:TIGR03098 451 G 451
|
|
| PRK06814 |
PRK06814 |
acyl-[ACP]--phospholipid O-acyltransferase; |
119-568 |
8.18e-25 |
|
acyl-[ACP]--phospholipid O-acyltransferase;
Pssm-ID: 235865 [Multi-domain] Cd Length: 1140 Bit Score: 110.83 E-value: 8.18e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327099 119 MTYGEAASERQAIGsGLLFHGVNQGDCVGLYFINRPEWLVVDHACAAYSFVSVPLYDTLGPDAVKFVVNHANLQAIFCVP 198
Cdd:PRK06814 659 LTYRKLLTGAFVLG-RKLKKNTPPGENVGVMLPNANGAAVTFFALQSAGRVPAMINFSAGIANILSACKAAQVKTVLTSR 737
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327099 199 Q-----TLNILLSFLAEipSIRLIvvvggadeHLPSLPRGtgVTIVSYQKLLSQGRSSLHPFSPPKPEDIATICYTSGTT 273
Cdd:PRK06814 738 AfiekaRLGPLIEALEF--GIRII--------YLEDVRAQ--IGLADKIKGLLAGRFPLVYFCNRDPDDPAVILFTSGSE 805
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327099 274 GTPKGVVLTHGNLIANVAGSSVEAEFFPSDVYISYLPLAHIYE-RANQIMGVYGGVAVGFYQGdvfklmddfavlrPTIF 352
Cdd:PRK06814 806 GTPKGVVLSHRNLLANRAQVAARIDFSPEDKVFNALPVFHSFGlTGGLVLPLLSGVKVFLYPS-------------PLHY 872
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327099 353 CSVPRLynrIYDgitsaVKSSGVVKKRLFEIAYnskkqaiinGRT--PSAFWdklvfnkikeklggRVRFMGSGASPLSP 430
Cdd:PRK06814 873 RIIPEL---IYD-----TNATILFGTDTFLNGY---------ARYahPYDFR--------------SLRYVFAGAEKVKE 921
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327099 431 DVMDFLRICFGCSVREGYGMTETSCVISAMDDGDNLSGHVGSPNPACEVKLVDVPEMNytsddqpyPRGEICVRGPIIFK 510
Cdd:PRK06814 922 ETRQTWMEKFGIRILEGYGVTETAPVIALNTPMHNKAGTVGRLLPGIEYRLEPVPGID--------EGGRLFVRGPNVML 993
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*...
gi 22327099 511 GYYKDEEQTREILDGDGWLHTGDIGLWLPGGRLKIIDRKKNIFKLAqGEYIAPEKIEN 568
Cdd:PRK06814 994 GYLRAENPGVLEPPADGWYDTGDIVTIDEEGFITIKGRAKRFAKIA-GEMISLAAVEE 1050
|
|
| FCS |
cd05921 |
Feruloyl-CoA synthetase (FCS); Feruloyl-CoA synthetase is an essential enzyme in the feruloyl ... |
114-533 |
9.38e-25 |
|
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: 109.06 E-value: 9.38e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327099 114 GEYSW--MTYGEAASERQAIGSGLLFHGVNQGDCVGLYFINRpewlvVDHACAAYSFVSV--------PLYDTLGPDavk 183
Cdd:cd05921 19 GNGGWrrVTYAEALRQVRAIAQGLLDLGLSAERPLLILSGNS-----IEHALMALAAMYAgvpaapvsPAYSLMSQD--- 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327099 184 fvvnHANLQAIFCVPQTLNILLS----F---LAEIPSIRLIVVVGGADehlpslprGTGVTIVSYQKLLSQ--GRSSLHP 254
Cdd:cd05921 91 ----LAKLKHLFELLKPGLVFAQdaapFaraLAAIFPLGTPLVVSRNA--------VAGRGAISFAELAATppTAAVDAA 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327099 255 FSPPKPEDIATICYTSGTTGTPKGVVLTHGNLIANVAG-SSVEAEFFPSD-VYISYLPLAHIYErANQIMG--VYGGvav 330
Cdd:cd05921 159 FAAVGPDTVAKFLFTSGSTGLPKAVINTQRMLCANQAMlEQTYPFFGEEPpVLVDWLPWNHTFG-GNHNFNlvLYNG--- 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327099 331 GFYQGDVFKLM--------DDFAVLRPTIFCSVPRLynriYDGITSAVKSSGVVKKRLFEiaynskkqaiingrtpsafw 402
Cdd:cd05921 235 GTLYIDDGKPMpggfeetlRNLREISPTVYFNVPAG----WEMLVAALEKDEALRRRFFK-------------------- 290
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327099 403 dklvfnkikeklggRVRFMGSGASPLSPDVMDFL----------RICFGCsvreGYGMTETSCVISAMDDGDNLSGHVGS 472
Cdd:cd05921 291 --------------RLKLMFYAGAGLSQDVWDRLqalavatvgeRIPMMA----GLGATETAPTATFTHWPTERSGLIGL 352
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 22327099 473 PNPACEVKLVdvpemnyTSDDqpypRGEICVRGPIIFKGYYKDEEQTREILDGDGWLHTGD 533
Cdd:cd05921 353 PAPGTELKLV-------PSGG----KYEVRVKGPNVTPGYWRQPELTAQAFDEEGFYCLGD 402
|
|
| FACL_like_6 |
cd05922 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
133-600 |
1.28e-24 |
|
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ATP-dependent activation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions.
Pssm-ID: 341246 [Multi-domain] Cd Length: 457 Bit Score: 107.53 E-value: 1.28e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327099 133 SGLLFHGVNQGDCVGLYFINRPE--WLV--VDHACAAYSFVSVPLYDTLGPDAVKFVVNHANLQAIFCVPQTLNILLSFL 208
Cdd:cd05922 8 SALLEAGGVRGERVVLILPNRFTyiELSfaVAYAGGRLGLVFVPLNPTLKESVLRYLVADAGGRIVLADAGAADRLRDAL 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327099 209 AEIPSIRLIVVVGGADehlpslprgtgvtivsyqkllsqGRSSLHPFSPPKPEDIATICYTSGTTGTPKGVVLTHGNLIA 288
Cdd:cd05922 88 PASPDPGTVLDADGIR-----------------------AARASAPAHEVSHEDLALLLYTSGSTGSPKLVRLSHQNLLA 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327099 289 NVAGSSVEAEFFPSDVYISYLPLAHIYeranqimGVY--------GGVAV---GFYQGDVFklMDDFAVLRPTIFCSVPR 357
Cdd:cd05922 145 NARSIAEYLGITADDRALTVLPLSYDY-------GLSvlnthllrGATLVltnDGVLDDAF--WEDLREHGATGLAGVPS 215
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327099 358 LYNRIydgITSAVKSSGVVKKRLFEIAynskkqaiiNGRTPSAFWDKLvfnkiKEKL-GGRVRFMgsgasplspdvmdfl 436
Cdd:cd05922 216 TYAML---TRLGFDPAKLPSLRYLTQA---------GGRLPQETIARL-----RELLpGAQVYVM--------------- 263
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327099 437 ricfgcsvregYGMTETSCVISAM--DDGDNLSGHVGSPNPACEVKLVDvpemnytSDDQPYPR---GEICVRGPIIFKG 511
Cdd:cd05922 264 -----------YGQTEATRRMTYLppERILEKPGSIGLAIPGGEFEILD-------DDGTPTPPgepGEIVHRGPNVMKG 325
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327099 512 YYKDEEQTREILDGDGWLHTGDIGLWLPGGRLKIIDRKKNIFKLAqGEYIAPEKIENVY--TKCRFVSQCFIHGDSFNSS 589
Cdd:cd05922 326 YWNDPPYRRKEGRGGGVLHTGDLARRDEDGFLFIVGRRDRMIKLF-GNRISPTEIEAAArsIGLIIEAAAVGLPDPLGEK 404
|
490
....*....|.
gi 22327099 590 LVAIVSVDPEV 600
Cdd:cd05922 405 LALFVTAPDKI 415
|
|
| FACL_like_4 |
cd05944 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
260-567 |
3.26e-24 |
|
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: 104.87 E-value: 3.26e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327099 260 PEDIATICYTSGTTGTPKGVVLTHGNLIANVAGSSVEAEFFPSDVYISYLPLAHIYERANQIMG-VYGGVAVGF-----Y 333
Cdd:cd05944 1 SDDVAAYFHTGGTTGTPKLAQHTHSNEVYNAWMLALNSLFDPDDVLLCGLPLFHVNGSVVTLLTpLASGAHVVLagpagY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327099 334 QG-----DVFKLMDDFavlRPTIFCSVPrlynriydgitsavkssgvvkkrlfeIAYNSKKQAIINGRTPSafwdklvfn 408
Cdd:cd05944 81 RNpglfdNFWKLVERY---RITSLSTVP--------------------------TVYAALLQVPVNADISS--------- 122
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327099 409 kikeklggrVRFMGSGASPLSPDVMDFLRICFGCSVREGYGMTETSCVIS-AMDDGDNLSGHVGSPNPACEVKLVDV-PE 486
Cdd:cd05944 123 ---------LRFAMSGAAPLPVELRARFEDATGLPVVEGYGLTEATCLVAvNPPDGPKRPGSVGLRLPYARVRIKVLdGV 193
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327099 487 MNYTSDDQPYPRGEICVRGPIIFKGYYkDEEQTREILDGDGWLHTGDIGLWLPGGRLKIIDRKKNIFkLAQGEYIAPEKI 566
Cdd:cd05944 194 GRLLRDCAPDEVGEICVAGPGVFGGYL-YTEGNKNAFVADGWLNTGDLGRLDADGYLFITGRAKDLI-IRGGHNIDPALI 271
|
.
gi 22327099 567 E 567
Cdd:cd05944 272 E 272
|
|
| PRK08314 |
PRK08314 |
long-chain-fatty-acid--CoA ligase; Validated |
47-569 |
5.42e-24 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236235 [Multi-domain] Cd Length: 546 Bit Score: 106.58 E-value: 5.42e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327099 47 SYSVVLPEkldTGKW-NVYRSKRsptklvsRFPDHPEIgtlhdnfvhavetyaenKYLGTRVrsdgtigeyswmTYGEAA 125
Cdd:PRK08314 2 PKSLTLPE---TSLFhNLEVSAR-------RYPDKTAI-----------------VFYGRAI------------SYRELL 42
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327099 126 SERQAIgSGLLFH--GVNQGDCVGLYFINRPEWLVVDHACAAYSFVSVPLYDTLGPDAVKFVVNHANLQAIFCVPQTLNI 203
Cdd:PRK08314 43 EEAERL-AGYLQQecGVRKGDRVLLYMQNSPQFVIAYYAILRANAVVVPVNPMNREEELAHYVTDSGARVAIVGSELAPK 121
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327099 204 LLSFLAEIPsIRLIVVVGGAD--------------EHLPSLPRGTGVTIVSYQKLLSQGRsslhpfSPPK----PEDIAT 265
Cdd:PRK08314 122 VAPAVGNLR-LRHVIVAQYSDylpaepeiavpawlRAEPPLQALAPGGVVAWKEALAAGL------APPPhtagPDDLAV 194
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327099 266 ICYTSGTTGTPKGVVLTHGNLIANVAGSSVEAEFFPSDVYISYLPLAHiyeranqIMGVYGGVAVGFYQGDVFKLMddfa 345
Cdd:PRK08314 195 LPYTSGTTGVPKGCMHTHRTVMANAVGSVLWSNSTPESVVLAVLPLFH-------VTGMVHSMNAPIYAGATVVLM---- 263
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327099 346 vlrptifcsvPRlynriYDGITSAvkssgvvkkRLFEiaynsKKQAIINGRTPSAFWDKLVFNKIKEKLGGRVRFMGSGA 425
Cdd:PRK08314 264 ----------PR-----WDREAAA---------RLIE-----RYRVTHWTNIPTMVVDFLASPGLAERDLSSLRYIGGGG 314
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327099 426 SPLSPDVMDFLRICFGCSVREGYGMTETscvISAMddgdnlsgHVgspNPACEVKL--VDVPEMNYTS---DD---QPYP 497
Cdd:PRK08314 315 AAMPEAVAERLKELTGLDYVEGYGLTET---MAQT--------HS---NPPDRPKLqcLGIPTFGVDArviDPetlEELP 380
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 22327099 498 R---GEICVRGPIIFKGYYKDEEQTREI---LDGDGWLHTGDIGLWLPGGRLKIIDRKKNIFKlAQGEYIAPEKIENV 569
Cdd:PRK08314 381 PgevGEIVVHGPQVFKGYWNRPEATAEAfieIDGKRFFRTGDLGRMDEEGYFFITDRLKRMIN-ASGFKVWPAEVENL 457
|
|
| A_NRPS_Srf_like |
cd12117 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including Bacillus subtilis ... |
119-606 |
3.59e-23 |
|
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: 103.43 E-value: 3.59e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327099 119 MTYGE--AASERQAigSGLLFHGVNQGDCVGLYFINRPEWLV----VDHACAAYsfvsVPLYDTLgPDAVkfvvnhanlq 192
Cdd:cd12117 23 LTYAElnERANRLA--RRLRAAGVGPGDVVGVLAERSPELVVallaVLKAGAAY----VPLDPEL-PAER---------- 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327099 193 aifcvpqtlnilLSFLAEIPSIRLIVvvggADEHLPSLPRGTGVTIVSYQKLLSQGRSSLHPfsPPKPEDIATICYTSGT 272
Cdd:cd12117 86 ------------LAFMLADAGAKVLL----TDRSLAGRAGGLEVAVVIDEALDAGPAGNPAV--PVSPDDLAYVMYTSGS 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327099 273 TGTPKGVVLTHGNLIANVAGSSVeAEFFPSDVYISYLPL---AHIYEranqIMG--VYGGVAVgfyqgdvfkLMDDFAVL 347
Cdd:cd12117 148 TGRPKGVAVTHRGVVRLVKNTNY-VTLGPDDRVLQTSPLafdASTFE----IWGalLNGARLV---------LAPKGTLL 213
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327099 348 RPTIFCSVPRLynriyDGITSAVKSSGvvkkrLFeiaynskkQAIINGRtPSAFwdklvfnkikeklgGRVRFMGSGASP 427
Cdd:cd12117 214 DPDALGALIAE-----EGVTVLWLTAA-----LF--------NQLADED-PECF--------------AGLRELLTGGEV 260
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327099 428 LSPDVMD-FLRICFGCSVREGYGMTE-----TSCVISAMDDGDnlsGHV--GSPNPACEVKLVDVpemnytsDDQPYPR- 498
Cdd:cd12117 261 VSPPHVRrVLAACPGLRLVNGYGPTEnttftTSHVVTELDEVA---GSIpiGRPIANTRVYVLDE-------DGRPVPPg 330
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327099 499 --GEICVRGPIIFKGYYKDEEQTRE------ILDGDGWLHTGDIGLWLPGGRLKIIDRKKNIFKLaQGEYIAPEKIENVY 570
Cdd:cd12117 331 vpGELYVGGDGLALGYLNRPALTAErfvadpFGPGERLYRTGDLARWLPDGRLEFLGRIDDQVKI-RGFRIELGEIEAAL 409
|
490 500 510 520
....*....|....*....|....*....|....*....|...
gi 22327099 571 TKCRFVSQCFI---HGDSFNSSLVAIVS----VDPEVMKDWAA 606
Cdd:cd12117 410 RAHPGVREAVVvvrEDAGGDKRLVAYVVaegaLDAAELRAFLR 452
|
|
| BCL_like |
cd05919 |
Benzoate CoA ligase (BCL) and similar adenylate forming enzymes; This family contains benzoate ... |
119-639 |
8.67e-23 |
|
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: 101.77 E-value: 8.67e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327099 119 MTYGEAASERQAIGSGLLFHGVNQGDCVGLYFINRPEWLVVDHACAAYSFVSVPLYDTLGPDAVKFVVNHanlqaifCVP 198
Cdd:cd05919 11 VTYGQLHDGANRLGSALRNLGVSSGDRVLLLMLDSPELVQLFLGCLARGAIAVVINPLLHPDDYAYIARD-------CEA 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327099 199 qtlnillsflaeipsiRLIVVVGgadehlpslprgtgvtivsyqkllsqgrsslhpfsppkpEDIATICYTSGTTGTPKG 278
Cdd:cd05919 84 ----------------RLVVTSA---------------------------------------DDIAYLLYSSGTTGPPKG 108
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327099 279 VVLTHGNLIANVAGSSVEA-EFFPSDVYISYLPLAHIYERANQIMGVY--GGVAVGFYQG-DVFKLMDDFAVLRPTIFCS 354
Cdd:cd05919 109 VMHAHRDPLLFADAMAREAlGLTPGDRVFSSAKMFFGYGLGNSLWFPLavGASAVLNPGWpTAERVLATLARFRPTVLYG 188
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327099 355 VPRLYNRIYDgitsavksSGVVKKRLFEiaynskkqaiingrtpsafwdklvfnkikeklggRVRFMGSGASPLSPDVMD 434
Cdd:cd05919 189 VPTFYANLLD--------SCAGSPDALR----------------------------------SLRLCVSAGEALPRGLGE 226
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327099 435 FLRICFGCSVREGYGMTETSCVISAMDDGDNLSGHVGSPNPACEVKLVDvPEMNYTSDDQPyprGEICVRGPIIFKGYYK 514
Cdd:cd05919 227 RWMEHFGGPILDGIGATEVGHIFLSNRPGAWRLGSTGRPVPGYEIRLVD-EEGHTIPPGEE---GDLLVRGPSAAVGYWN 302
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327099 515 DEEQTREILDGdGWLHTGDIGLWLPGGRLKIIDRKKNIFKLAqGEYIAPEKIENVYTKCRFVSQCFIHG---DSFNSSLV 591
Cdd:cd05919 303 NPEKSRATFNG-GWYRTGDKFCRDADGWYTHAGRADDMLKVG-GQWVSPVEVESLIIQHPAVAEAAVVAvpeSTGLSRLT 380
|
490 500 510 520
....*....|....*....|....*....|....*....|....*...
gi 22327099 592 AIVSVDPEVMKDWAASEGIKYEHLGQLCNDPRVRKtvLAEMDDLGREA 639
Cdd:cd05919 381 AFVVLKSPAAPQESLARDIHRHLLERLSAHKVPRR--IAFVDELPRTA 426
|
|
| PRK12406 |
PRK12406 |
long-chain-fatty-acid--CoA ligase; Provisional |
102-638 |
1.25e-22 |
|
long-chain-fatty-acid--CoA ligase; Provisional
Pssm-ID: 183506 [Multi-domain] Cd Length: 509 Bit Score: 102.08 E-value: 1.25e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327099 102 YLGTRVRSdgtigeyswmtYGEAASERQAIGSGLLFHGVNQGDCVGLYFINRPEWLVVDHACAAYSFVSVPLYDTLGPDA 181
Cdd:PRK12406 6 ISGDRRRS-----------FDELAQRAARAAGGLAALGVRPGDCVALLMRNDFAFFEAAYAAMRLGAYAVPVNWHFKPEE 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327099 182 VKFVVN---------HANL--QAIFCVPQTLNILlsflaEIPSIRLIVVVGGADEHLPSLPRGTgvtiVSYQKLLSQGRs 250
Cdd:PRK12406 75 IAYILEdsgarvliaHADLlhGLASALPAGVTVL-----SVPTPPEIAAAYRISPALLTPPAGA----IDWEGWLAQQE- 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327099 251 slhPFSPPKPEDIATICYTSGTTGTPKGV---------VLTHGNLIANVAGssveaeFFPSDVYISYLPLAHIYERANQI 321
Cdd:PRK12406 145 ---PYDGPPVPQPQSMIYTSGTTGHPKGVrraaptpeqAAAAEQMRALIYG------LKPGIRALLTGPLYHSAPNAYGL 215
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327099 322 M-GVYGGVAVGFYQGDVFKLMDDFAVLRPTIFCSVPRLYNRIYDgITSAVKSSGVVKKrlfeiaynskkqaiingrtpsa 400
Cdd:PRK12406 216 RaGRLGGVLVLQPRFDPEELLQLIERHRITHMHMVPTMFIRLLK-LPEEVRAKYDVSS---------------------- 272
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327099 401 fwdklvfnkikeklggrVRFMGSGASPLSPDVMDFLRICFGCSVREGYGMTETSCVISAMDDgDNLS--GHVGSPNPACE 478
Cdd:PRK12406 273 -----------------LRHVIHAAAPCPADVKRAMIEWWGPVIYEYYGSTESGAVTFATSE-DALShpGTVGKAAPGAE 334
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327099 479 VKLVDvpemnytSDDQPYPR---GEICVRGPII--FKgYYKDEEQTREIlDGDGWLHTGDIGLWLPGGRLKIIDRKKNIF 553
Cdd:PRK12406 335 LRFVD-------EDGRPLPQgeiGEIYSRIAGNpdFT-YHNKPEKRAEI-DRGGFITSGDVGYLDADGYLFLCDRKRDMV 405
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327099 554 kLAQGEYIAPEKIENVYTKCRFVSQCFIHG--DS-FNSSLVAIVSVDPEVMKDwaaSEGIKyEHLGQLCNDPRVRKTVLA 630
Cdd:PRK12406 406 -ISGGVNIYPAEIEAVLHAVPGVHDCAVFGipDAeFGEALMAVVEPQPGATLD---EADIR-AQLKARLAGYKVPKHIEI 480
|
....*...
gi 22327099 631 eMDDLGRE 638
Cdd:PRK12406 481 -MAELPRE 487
|
|
| DltA |
cd05945 |
D-alanine:D-alanyl carrier protein ligase (DltA) and similar proteins; This family includes ... |
260-579 |
5.84e-22 |
|
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: 99.24 E-value: 5.84e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327099 260 PEDIATICYTSGTTGTPKGVVLTHGNLIANVAGSSVEAEFFPSDVYISYLPLAHIYeranQIMGVYGGVAVGfyqGDVFk 339
Cdd:cd05945 96 GDDNAYIIFTSGSTGRPKGVQISHDNLVSFTNWMLSDFPLGPGDVFLNQAPFSFDL----SVMDLYPALASG---ATLV- 167
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327099 340 lmddfaVLRPTIFCSVPRLYNRIYD-GITSAVKssgvvkkrlfeiaynskkqaiingrTPSaFWDKLV----FNKikEKL 414
Cdd:cd05945 168 ------PVPRDATADPKQLFRFLAEhGITVWVS-------------------------TPS-FAAMCLlsptFTP--ESL 213
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327099 415 GGRVRFMGSGaSPLSPDVMDFLRICF-GCSVREGYGMTETSCVISAMD-DGDNLSGH----VGSPNPACEVKLVDvpemn 488
Cdd:cd05945 214 PSLRHFLFCG-EVLPHKTARALQQRFpDARIYNTYGPTEATVAVTYIEvTPEVLDGYdrlpIGYAKPGAKLVILD----- 287
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327099 489 ytSDDQPYP---RGEICVRGPIIFKGYYKDEEQTREIL---DGDGWLHTGDIGLWLPGGRLKIIDRKKNIFKLaQGEYIA 562
Cdd:cd05945 288 --EDGRPVPpgeKGELVISGPSVSKGYLNNPEKTAAAFfpdEGQRAYRTGDLVRLEADGLLFYRGRLDFQVKL-NGYRIE 364
|
330
....*....|....*..
gi 22327099 563 PEKIENVYTKCRFVSQC 579
Cdd:cd05945 365 LEEIEAALRQVPGVKEA 381
|
|
| PRK06018 |
PRK06018 |
putative acyl-CoA synthetase; Provisional |
177-569 |
1.74e-21 |
|
putative acyl-CoA synthetase; Provisional
Pssm-ID: 235673 [Multi-domain] Cd Length: 542 Bit Score: 98.67 E-value: 1.74e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327099 177 LGPDAVKFVVNHANLQAIFCVPQTLNILLSFLAEIPSIRLIVVVGGADEhlpsLPRGTGVTIVSYQKLLSQ--GRSSLHP 254
Cdd:PRK06018 98 LFPEQIAWIINHAEDRVVITDLTFVPILEKIADKLPSVERYVVLTDAAH----MPQTTLKNAVAYEEWIAEadGDFAWKT 173
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327099 255 FsppkPEDIAT-ICYTSGTTGTPKGVVLTHGN-----LIANVAGSSVEAEffpSDVYISYLPLAHiyerANQIMGVYGGV 328
Cdd:PRK06018 174 F----DENTAAgMCYTSGTTGDPKGVLYSHRSnvlhaLMANNGDALGTSA---ADTMLPVVPLFH----ANSWGIAFSAP 242
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327099 329 AVG---------FYQGDVFKLMDDFAVlrpTIFCSVPRLYnriydgitsavkssgvvkkrLFEIAYNSKkqaiingrtps 399
Cdd:PRK06018 243 SMGtklvmpgakLDGASVYELLDTEKV---TFTAGVPTVW--------------------LMLLQYMEK----------- 288
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327099 400 afwDKLVFNKIKeklggrVRFMGSGASPLSPdVMDFLRicFGCSVREGYGMTETSCV--ISAMDDG-DNLSGHV------ 470
Cdd:PRK06018 289 ---EGLKLPHLK------MVVCGGSAMPRSM-IKAFED--MGVEVRHAWGMTEMSPLgtLAALKPPfSKLPGDArldvlq 356
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327099 471 --GSPNPACEVKLVDVPEMNYTSDDQPYprGEICVRGPIIFKGYYKDEEqtrEILDGDGWLHTGDIGLWLPGGRLKIIDR 548
Cdd:PRK06018 357 kqGYPPFGVEMKITDDAGKELPWDGKTF--GRLKVRGPAVAAAYYRVDG---EILDDDGFFDTGDVATIDAYGYMRITDR 431
|
410 420
....*....|....*....|.
gi 22327099 549 KKNIFKlAQGEYIAPEKIENV 569
Cdd:PRK06018 432 SKDVIK-SGGEWISSIDLENL 451
|
|
| FADD10 |
cd17635 |
adenylate forming domain, fatty acid CoA ligase (FadD10); This family contains long chain ... |
261-618 |
2.46e-21 |
|
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: 95.79 E-value: 2.46e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327099 261 EDIATICYTSGTTGTPKGVVLTHG-------NLIANVAGSSVEaeffpsDVYISYLPLAHIYERANQIMGV-YGGVAVGF 332
Cdd:cd17635 1 EDPLAVIFTSGTTGEPKAVLLANKtffavpdILQKEGLNWVVG------DVTYLPLPATHIGGLWWILTCLiHGGLCVTG 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327099 333 ----YQGDVFKLMDDFAVlrpTIFCSVPRLYNRIYDGITSAVKSSgvvkKRLFEIAYNSKKqaIINGRTPSAFWDKLVfn 408
Cdd:cd17635 75 gentTYKSLFKILTTNAV---TTTCLVPTLLSKLVSELKSANATV----PSLRLIGYGGSR--AIAADVRFIEATGLT-- 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327099 409 kikeklggrvrfmgsgasplspdvmdflricfgcSVREGYGMTETS--CVISAMDDGDNLsGHVGSPNPACEVKLVDVPE 486
Cdd:cd17635 144 ----------------------------------NTAQVYGLSETGtaLCLPTDDDSIEI-NAVGRPYPGVDVYLAATDG 188
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327099 487 MNYTSDDQpyprGEICVRGPIIFKGYYKDEEQTREILDgDGWLHTGDIGLWLPGGRLKIIDRKKNIFKLAqGEYIAPEKI 566
Cdd:cd17635 189 IAGPSASF----GTIWIKSPANMLGYWNNPERTAEVLI-DGWVNTGDLGERREDGFLFITGRSSESINCG-GVKIAPDEV 262
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|...
gi 22327099 567 ENVYTKCRFVSQCFIHGDSFNS-SLVAIVSVDPEVMKDWAASEGIKYEHLGQL 618
Cdd:cd17635 263 ERIAEGVSGVQECACYEISDEEfGELVGLAVVASAELDENAIRALKHTIRREL 315
|
|
| A_NRPS |
cd05930 |
The adenylation domain of nonribosomal peptide synthetases (NRPS); The adenylation (A) domain ... |
260-617 |
3.02e-21 |
|
The adenylation domain of nonribosomal peptide synthetases (NRPS); The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester bond to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.
Pssm-ID: 341253 [Multi-domain] Cd Length: 444 Bit Score: 97.21 E-value: 3.02e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327099 260 PEDIATICYTSGTTGTPKGVVLTHGNLIANVAGSSVEAEFFPSDVYISYLPLA---HIYEranqimgVYGGVAVGfyqGD 336
Cdd:cd05930 92 PDDLAYVIYTSGSTGKPKGVMVEHRGLVNLLLWMQEAYPLTPGDRVLQFTSFSfdvSVWE-------IFGALLAG---AT 161
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327099 337 VFkLMDDFAVLRPtifcsvprlynriyDGITSAVKSSGVVkkrlfeiaynskkqaIINGrTPSAFwdKLVFNKIKEKLGG 416
Cdd:cd05930 162 LV-VLPEEVRKDP--------------EALADLLAEEGIT---------------VLHL-TPSLL--RLLLQELELAALP 208
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327099 417 RVRFMGSGASPLSPDVMD-FLRICFGCSVREGYGMTETSCVISAM--DDGDNLSGHV--GSPNPACEVKLVDvpemnytS 491
Cdd:cd05930 209 SLRLVLVGGEALPPDLVRrWRELLPGARLVNLYGPTEATVDATYYrvPPDDEEDGRVpiGRPIPNTRVYVLD-------E 281
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327099 492 DDQPYPR---GEICVRGPIIFKGYYKDEEQTRE-----ILDGDGWLH-TGDIGLWLPGGRLKIIDRKKNIFKLAqGEYIA 562
Cdd:cd05930 282 NLRPVPPgvpGELYIGGAGLARGYLNRPELTAErfvpnPFGPGERMYrTGDLVRWLPDGNLEFLGRIDDQVKIR-GYRIE 360
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*...
gi 22327099 563 PEKIENVYTKCRFVSQCFI---HGDSFNSSLVAIVSVDPEVMKDwaaSEGIKyEHLGQ 617
Cdd:cd05930 361 LGEIEAALLAHPGVREAAVvarEDGDGEKRLVAYVVPDEGGELD---EEELR-AHLAE 414
|
|
| PRK09192 |
PRK09192 |
fatty acyl-AMP ligase; |
254-567 |
4.61e-21 |
|
fatty acyl-AMP ligase;
Pssm-ID: 236403 [Multi-domain] Cd Length: 579 Bit Score: 97.77 E-value: 4.61e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327099 254 PFSPPKPEDIATICYTSGTTGTPKGVVLTHGNLIANVAGSSVEA-EFFPSDVYISYLPLAHIyeranqiMGVyggvaVGF 332
Cdd:PRK09192 169 ALPRPTPDDIAYLQYSSGSTRFPRGVIITHRALMANLRAISHDGlKVRPGDRCVSWLPFYHD-------MGL-----VGF 236
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327099 333 Y------QGDVFKL-MDDFAVlRPTIFcsvprlynriYDGITsavKSSGVvkkrlfeIAYnskkqaiingrTPSaFWDKL 405
Cdd:PRK09192 237 LltpvatQLSVDYLpTRDFAR-RPLQW----------LDLIS---RNRGT-------ISY-----------SPP-FGYEL 283
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327099 406 VFNKIKEK-LGG----RVRFMGSGASPLSPDVMDFLRICF---GCSVRE---GYGMTETSCVISAMD----------DGD 464
Cdd:PRK09192 284 CARRVNSKdLAEldlsCWRVAGIGADMIRPDVLHQFAEAFapaGFDDKAfmpSYGLAEATLAVSFSPlgsgivveevDRD 363
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327099 465 NLSGH------------------VGSPNPACEVKLVDvpemnytSDDQPYPR---GEICVRGPIIFKGYYKDEEQTREiL 523
Cdd:PRK09192 364 RLEYQgkavapgaetrrvrtfvnCGKALPGHEIEIRN-------EAGMPLPErvvGHICVRGPSLMSGYFRDEESQDV-L 435
|
330 340 350 360
....*....|....*....|....*....|....*....|....
gi 22327099 524 DGDGWLHTGDIGlWLPGGRLKIIDRKKNIFkLAQGEYIAPEKIE 567
Cdd:PRK09192 436 AADGWLDTGDLG-YLLDGYLYITGRAKDLI-IINGRNIWPQDIE 477
|
|
| A_NRPS_MycA_like |
cd05908 |
The adenylation domain of nonribosomal peptide synthetases (NRPS) similar to mycosubtilin ... |
260-569 |
5.22e-21 |
|
The adenylation domain of nonribosomal peptide synthetases (NRPS) similar to mycosubtilin synthase subunit A (MycA); The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as (amino)-acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms thioester to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. This family includes NRPS similar to mycosubtilin synthase subunit A (MycA). Mycosubtilin, which is characterized by a beta-amino fatty acid moiety linked to the circular heptapeptide Asn-Tyr-Asn-Gln-Pro-Ser-Asn, belongs to the iturin family of lipopeptide antibiotics. The mycosubtilin synthase subunit A (MycA) combines functional domains derived from peptide synthetases, amino transferases, and fatty acid synthases. Nonribosomal peptide synthetases are large multifunction enzymes that synthesize many therapeutically useful peptides. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and, in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.
Pssm-ID: 341234 [Multi-domain] Cd Length: 499 Bit Score: 97.17 E-value: 5.22e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327099 260 PEDIATICYTSGTTGTPKGVVLTHGNLIANVAGSSVEAEFFPSDVYISYLPLAHIyeranqiMGVYGGVAVGFYQGDVFK 339
Cdd:cd05908 105 ADELAFIQFSSGSTGDPKGVMLTHENLVHNMFAILNSTEWKTKDRILSWMPLTHD-------MGLIAFHLAPLIAGMNQY 177
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327099 340 LMddfavlrPT-IFCSVPRLYNRIYDGITSAVKSSGVVKKRLFEIAYNSKKqaiingrtpSAFWDKlvfnkikeklgGRV 418
Cdd:cd05908 178 LM-------PTrLFIRRPILWLKKASEHKATIVSSPNFGYKYFLKTLKPEK---------ANDWDL-----------SSI 230
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327099 419 RFMGSGASPLSPDVMD-FLRICFGCSVREG-----YGMTETSCVISAMDDGDNLS----GH------------------- 469
Cdd:cd05908 231 RMILNGAEPIDYELCHeFLDHMSKYGLKRNailpvYGLAEASVGASLPKAQSPFKtitlGRrhvthgepepevdkkdsec 310
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327099 470 -----VGSPNPACEVKLVDvpEMNYTSDDQPYprGEICVRGPIIFKGYYKDEEQTREILDGDGWLHTGDIGLwLPGGRLK 544
Cdd:cd05908 311 ltfveVGKPIDETDIRICD--EDNKILPDGYI--GHIQIRGKNVTPGYYNNPEATAKVFTDDGWLKTGDLGF-IRNGRLV 385
|
330 340
....*....|....*....|....*
gi 22327099 545 IIDRKKNIFkLAQGEYIAPEKIENV 569
Cdd:cd05908 386 ITGREKDII-FVNGQNVYPHDIERI 409
|
|
| EntF |
COG1020 |
EntF, seryl-AMP synthase component of non-ribosomal peptide synthetase [Secondary metabolites ... |
79-543 |
2.10e-20 |
|
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: 96.85 E-value: 2.10e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327099 79 DHPEIGTLHDNFVHAVETYAENkylgTRVRSDGTigeysWMTYGE--AASERqaIGSGLLFHGVNQGDCVGLYfINR-PE 155
Cdd:COG1020 471 PYPADATLHELFEAQAARTPDA----VAVVFGDQ-----SLTYAElnARANR--LAHHLRALGVGPGDLVGVC-LERsLE 538
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327099 156 WLV----VDHACAAYsfvsVPLyDTLGPDA-VKFVVNHANlqaifcvpqtlnillsflaeipsIRLIVVVGGADEHLPSL 230
Cdd:COG1020 539 MVVallaVLKAGAAY----VPL-DPAYPAErLAYMLEDAG-----------------------ARLVLTQSALAARLPEL 590
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327099 231 prgtGVTIVSYQKLLSQGRSSLHPFSPPKPEDIATICYTSGTTGTPKGVVLTHGNLIANVAGSSVEAEFFPSDVYISYLP 310
Cdd:COG1020 591 ----GVPVLALDALALAAEPATNPPVPVTPDDLAYVIYTSGSTGRPKGVMVEHRALVNLLAWMQRRYGLGPGDRVLQFAS 666
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327099 311 LAH---IYEranqIMG--VYGGVAVgFYQGDVFKLMDDFAVL----RPTIFCSVPRLYNRIYDGITSAVKSsgvvkkrLf 381
Cdd:COG1020 667 LSFdasVWE----IFGalLSGATLV-LAPPEARRDPAALAELlarhRVTVLNLTPSLLRALLDAAPEALPS-------L- 733
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327099 382 eiaynskkqaiingrtpsafwdKLVFnkikekLGGRVrfmgsgaspLSPDVMD-FLRICFGCSVREGYGMTETS--CVIS 458
Cdd:COG1020 734 ----------------------RLVL------VGGEA---------LPPELVRrWRARLPGARLVNLYGPTETTvdSTYY 776
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327099 459 AMDDGDNLSGHV--GSPNPACEVKLVDvpemnytSDDQPYP---RGEICVRGPIIFKGYYKDEEQTRE-------ILDGD 526
Cdd:COG1020 777 EVTPPDADGGSVpiGRPIANTRVYVLD-------AHLQPVPvgvPGELYIGGAGLARGYLNRPELTAErfvadpfGFPGA 849
|
490
....*....|....*..
gi 22327099 527 GWLHTGDIGLWLPGGRL 543
Cdd:COG1020 850 RLYRTGDLARWLPDGNL 866
|
|
| PRK12582 |
PRK12582 |
acyl-CoA synthetase; Provisional |
75-561 |
2.19e-20 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 237144 [Multi-domain] Cd Length: 624 Bit Score: 95.88 E-value: 2.19e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327099 75 SRFP--DHPEigtlhdNFVHAVETYA----ENKYLGTRvrsDGTIGEYSWMTYGEAASERQAIGSGLLFHGVNQGDCVGL 148
Cdd:PRK12582 40 SRHPlgPYPR------SIPHLLAKWAaeapDRPWLAQR---EPGHGQWRKVTYGEAKRAVDALAQALLDLGLDPGRPVMI 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327099 149 YFINRPEWLVVdhACAAYSF------VSvPLYDTLGPDavkfvvnHANLQAIFCVPQTLNILLS----FLAEIPSIRL-- 216
Cdd:PRK12582 111 LSGNSIEHALM--TLAAMQAgvpaapVS-PAYSLMSHD-------HAKLKHLFDLVKPRVVFAQsgapFARALAALDLld 180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327099 217 --IVVVGGAdehlpslprGTGVTIVSYQKLLS--------QGRSSLHPfsppkpEDIATICYTSGTTGTPKGVVLTHGNL 286
Cdd:PRK12582 181 vtVVHVTGP---------GEGIASIAFADLAAtpptaavaAAIAAITP------DTVAKYLFTSGSTGMPKAVINTQRMM 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327099 287 IANVAGSSVEAEFFPSD---VYISYLPLAHIYErANQIMG--VYGGvavGFYQGDVFKLM-----DDFAVLR---PTIFC 353
Cdd:PRK12582 246 CANIAMQEQLRPREPDPpppVSLDWMPWNHTMG-GNANFNglLWGG---GTLYIDDGKPLpgmfeETIRNLReisPTVYG 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327099 354 SVPRLYNriydGITSAVKSSGVVKKRLFEiaynskkqaiingrtpsafwdklvfnkikeklggRVRFMGSGASPLSPDVM 433
Cdd:PRK12582 322 NVPAGYA----MLAEAMEKDDALRRSFFK----------------------------------NLRLMAYGGATLSDDLY 363
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327099 434 DFLRicfGCSVRE---------GYGMTETSCVISAMDDGDNLSGHVGSPNPACEVKLVdvpemnytsddqpyPRG---EI 501
Cdd:PRK12582 364 ERMQ---ALAVRTtghripfytGYGATETAPTTTGTHWDTERVGLIGLPLPGVELKLA--------------PVGdkyEV 426
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 22327099 502 CVRGPIIFKGYYKDEEQTREILDGDGWLHTGDIGLWL----PGGRLKIIDRKKNIFKLAQGEYI 561
Cdd:PRK12582 427 RVKGPNVTPGYHKDPELTAAAFDEEGFYRLGDAARFVdpddPEKGLIFDGRVAEDFKLSTGTWV 490
|
|
| 23DHB-AMP_lg |
cd05920 |
2,3-dihydroxybenzoate-AMP ligase; 2,3-dihydroxybenzoate-AMP ligase activates 2, ... |
262-568 |
1.45e-19 |
|
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: 92.39 E-value: 1.45e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327099 262 DIATICYTSGTTGTPKGVVLTHGNLIANVAGSSVEAEFFPSDVYISYLPLAHIYerANQIMGVYGGVAVG----FYQ--- 334
Cdd:cd05920 140 EVALFLLSGGTTGTPKLIPRTHNDYAYNVRASAEVCGLDQDTVYLAVLPAAHNF--PLACPGVLGTLLAGgrvvLAPdps 217
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327099 335 -GDVFKLMDDFAVlrpTIFCSVPRLYNRIYDgitsavkssgvvkkrlfeiaynskkQAIINGRTPSAfwdklvfnkikek 413
Cdd:cd05920 218 pDAAFPLIEREGV---TVTALVPALVSLWLD-------------------------AAASRRADLSS------------- 256
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327099 414 lggrVRFMGSGASPLSPDVMDFLRICFGCSVREGYGMTETSCVISAMDDGDNLSGHV-GSP-NPACEVKLVDvpemnytS 491
Cdd:cd05920 257 ----LRLLQVGGARLSPALARRVPPVLGCTLQQVFGMAEGLLNYTRLDDPDEVIIHTqGRPmSPDDEIRVVD-------E 325
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327099 492 DDQPYPRGEI---CVRGPIIFKGYYKDEEQTREILDGDGWLHTGDIGLWLPGGRLKIIDRKKNIFKLAqGEYIAPEKIEN 568
Cdd:cd05920 326 EGNPVPPGEEgelLTRGPYTIRGYYRAPEHNARAFTPDGFYRTGDLVRRTPDGYLVVEGRIKDQINRG-GEKIAAEEVEN 404
|
|
| A_NRPS_GliP_like |
cd17653 |
nonribosomal peptide synthase GliP-like; This family includes the adenylation (A) domain of ... |
119-597 |
4.37e-19 |
|
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: 90.45 E-value: 4.37e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327099 119 MTYGEAASERQAIGSGLLFHGVNQGDCVGLYFINRPEWLV----VDHACAAYsfvsVPLydtlgpdavkfvvnhanlqai 194
Cdd:cd17653 23 LTYGELDAASNALANRLLQLGVVPGDVVPLLSDRSLEMLVailaILKAGAAY----VPL--------------------- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327099 195 fcvpqtlnillsflaeipsirlivvvggaDEHLPSlprgtgvtiVSYQKLLSQGRSSLhPFSPPKPEDIATICYTSGTTG 274
Cdd:cd17653 78 -----------------------------DAKLPS---------ARIQAILRTSGATL-LLTTDSPDDLAYIIFTSGSTG 118
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327099 275 TPKGVVLTHGNLIANVagSSVEAEFF--PSDvyisylplahiyeRANQIMGVyggvavGFyqgDVFKLMddfavlrptif 352
Cdd:cd17653 119 IPKGVMVPHRGVLNYV--SQPPARLDvgPGS-------------RVAQVLSI------AF---DACIGE----------- 163
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327099 353 csvprlynriydgITSAVKSSG--VVKKRLFEIAYNSKKQAIINGrTPSafwdklVFNKIKEKLGGRVRFMGSGASPLSP 430
Cdd:cd17653 164 -------------IFSTLCNGGtlVLADPSDPFAHVARTVDALMS-TPS------ILSTLSPQDFPNLKTIFLGGEAVPP 223
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327099 431 DVMDflRICFGCSVREGYGMTETSCVIS--AMDDGDNLsgHVGSPNPACEVKLVDvpemnytSDDQPYP---RGEICVRG 505
Cdd:cd17653 224 SLLD--RWSPGRRLYNAYGPTECTISSTmtELLPGQPV--TIGKPIPNSTCYILD-------ADLQPVPegvVGEICISG 292
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327099 506 PIIFKGYYKDEEQT----REILDGDGWLH--TGDIGLWLPGGRLKIIDRKKNIFKLaQGEYIAPEKIEN-VYTKCRFVSQ 578
Cdd:cd17653 293 VQVARGYLGNPALTaskfVPDPFWPGSRMyrTGDYGRWTEDGGLEFLGREDNQVKV-RGFRINLEEIEEvVLQSQPEVTQ 371
|
490 500
....*....|....*....|....
gi 22327099 579 --CFIHGDsfnsSLVAIV---SVD 597
Cdd:cd17653 372 aaAIVVNG----RLVAFVtpeTVD 391
|
|
| PRK08043 |
PRK08043 |
bifunctional acyl-ACP--phospholipid O-acyltransferase/long-chain-fatty-acid--ACP ligase; |
257-567 |
1.13e-18 |
|
bifunctional acyl-ACP--phospholipid O-acyltransferase/long-chain-fatty-acid--ACP ligase;
Pssm-ID: 181207 [Multi-domain] Cd Length: 718 Bit Score: 90.54 E-value: 1.13e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327099 257 PPKPEDIATICYTSGTTGTPKGVVLTHGNLIANVAGSSVEAEFFPSDVYISYLPLAHIYeranqimgvygGVAVGFYQgd 336
Cdd:PRK08043 361 KQQPEDAALILFTSGSEGHPKGVVHSHKSLLANVEQIKTIADFTPNDRFMSALPLFHSF-----------GLTVGLFT-- 427
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327099 337 vfKLMDDFAVL---RPTIFCSVPRLynrIYDgitsavKSSGVvkkrLFEIAY---NSKKQAiingrTPSAFwdklvfnki 410
Cdd:PRK08043 428 --PLLTGAEVFlypSPLHYRIVPEL---VYD------RNCTV----LFGTSTflgNYARFA-----NPYDF--------- 478
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327099 411 keklgGRVRFMGSGASPLSPDVMDFLRICFGCSVREGYGMTETSCVISAMDDGDNLSGHVGSPNPACEVKLVDVPEMNYT 490
Cdd:PRK08043 479 -----ARLRYVVAGAEKLQESTKQLWQDKFGLRILEGYGVTECAPVVSINVPMAAKPGTVGRILPGMDARLLSVPGIEQG 553
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327099 491 sddqpyprGEICVRGPIIFKGY------YKDEEQTREILDGD---GWLHTGDIGLWLPGGRLKIIDRKKNIFKLAqGEYI 561
Cdd:PRK08043 554 --------GRLQLKGPNIMNGYlrvekpGVLEVPTAENARGEmerGWYDTGDIVRFDEQGFVQIQGRAKRFAKIA-GEMV 624
|
....*.
gi 22327099 562 APEKIE 567
Cdd:PRK08043 625 SLEMVE 630
|
|
| PRK07008 |
PRK07008 |
long-chain-fatty-acid--CoA ligase; Validated |
92-569 |
1.68e-18 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 235908 [Multi-domain] Cd Length: 539 Bit Score: 89.38 E-value: 1.68e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327099 92 HAVETYAENKYLGTRVrsDGTIGEYswmTYGEAASERQAIGSGLLFHGVNQGDCVGLYFINRPEWLVVDHACAAYSFVSV 171
Cdd:PRK07008 18 HAARHAGDTEIVSRRV--EGDIHRY---TYRDCERRAKQLAQALAALGVEPGDRVGTLAWNGYRHLEAYYGVSGSGAVCH 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327099 172 PLYDTLGPDAVKFVVNHANLQAIFCVPQTLNILLSFLAEIPSIRLIVVVGGADeHLP--SLPrgtgvtIVSYQKLLSqGR 249
Cdd:PRK07008 93 TINPRLFPEQIAYIVNHAEDRYVLFDLTFLPLVDALAPQCPNVKGWVAMTDAA-HLPagSTP------LLCYETLVG-AQ 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327099 250 SSLHPFsPPKPEDIAT-ICYTSGTTGTPKGVVLTHGNLIANVAGSSVEAEFFPS--DVYISYLPLAHI------YERAnq 320
Cdd:PRK07008 165 DGDYDW-PRFDENQASsLCYTSGTTGNPKGALYSHRSTVLHAYGAALPDAMGLSarDAVLPVVPMFHVnawglpYSAP-- 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327099 321 IMG---VYGGVAVgfyQG-DVFKLMDDFAVlrpTIFCSVPrlynRIYDGITSAVKSSGVvkkrlfeiAYNSKKQAIIngr 396
Cdd:PRK07008 242 LTGaklVLPGPDL---DGkSLYELIEAERV---TFSAGVP----TVWLGLLNHMREAGL--------RFSTLRRTVI--- 300
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327099 397 tpsafwdklvfnkikeklggrvrfmgsGASPLSPDVMDFLRICFGCSVREGYGMTE-----TSCVISA--MDDGDNLSGH 469
Cdd:PRK07008 301 ---------------------------GGSACPPAMIRTFEDEYGVEVIHAWGMTEmsplgTLCKLKWkhSQLPLDEQRK 353
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327099 470 V----GSPNPACEVKLVDvpemnytSDDQPYP-----RGEICVRGPIIFKGYYKDEEQTreiLDgDGWLHTGDIGLWLPG 540
Cdd:PRK07008 354 LlekqGRVIYGVDMKIVG-------DDGRELPwdgkaFGDLQVRGPWVIDRYFRGDASP---LV-DGWFPTGDVATIDAD 422
|
490 500
....*....|....*....|....*....
gi 22327099 541 GRLKIIDRKKNIFKlAQGEYIAPEKIENV 569
Cdd:PRK07008 423 GFMQITDRSKDVIK-SGGEWISSIDIENV 450
|
|
| PRK06164 |
PRK06164 |
acyl-CoA synthetase; Validated |
112-579 |
1.90e-18 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 235722 [Multi-domain] Cd Length: 540 Bit Score: 89.42 E-value: 1.90e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327099 112 TIGEYSWMTYGEAASERQAIGSGLLFHGVNQGDCVGLYFINRPEWLVVDHACAAYS---------FVSVPLYDTLGPDAV 182
Cdd:PRK06164 29 LIDEDRPLSRAELRALVDRLAAWLAAQGVRRGDRVAVWLPNCIEWVVLFLACARLGatviavntrYRSHEVAHILGRGRA 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327099 183 KFVVNHANLQAIfcvpqtlnILLSFLAEI-----PSIRLIVVVGGADEHLPSLPRGTGVTIVSyqklLSQGRSSLHPFSP 257
Cdd:PRK06164 109 RWLVVWPGFKGI--------DFAAILAAVppdalPPLRAIAVVDDAADATPAPAPGARVQLFA----LPDPAPPAAAGER 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327099 258 PKPEDIATICYT-SGTTGTPKGV------VLTHGNLIANVAGSSveaeffPSDVYISYLPLAhiyeranqimGVYG--GV 328
Cdd:PRK06164 177 AADPDAGALLFTtSGTTSGPKLVlhrqatLLRHARAIARAYGYD------PGAVLLAALPFC----------GVFGfsTL 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327099 329 AVGFYQGDVFKLMDDFavlrptifcSVPRLYNRIYD-GITSAVKSSGVVKkRLFEIAYNSkkqaiinGRTPSAfwdklvf 407
Cdd:PRK06164 241 LGALAGGAPLVCEPVF---------DAARTARALRRhRVTHTFGNDEMLR-RILDTAGER-------ADFPSA------- 296
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327099 408 nkikeklggrvRFMGSGA-SPLSPDVMDFLRIcFGCSVREGYGMTETSCVISAMDDGDNLSGHV---GSP-NPACEVKLV 482
Cdd:PRK06164 297 -----------RLFGFASfAPALGELAALARA-RGVPLTGLYGSSEVQALVALQPATDPVSVRIeggGRPaSPEARVRAR 364
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327099 483 DVPEMNYTSDDQPyprGEICVRGPIIFKGYYKDEEQTREILDGDGWLHTGDIGLWLPGGRLKIIDRKKNIFKLAqGEYIA 562
Cdd:PRK06164 365 DPQDGALLPDGES---GEIEIRAPSLMRGYLDNPDATARALTDDGYFRTGDLGYTRGDGQFVYQTRMGDSLRLG-GFLVN 440
|
490
....*....|....*..
gi 22327099 563 PEKIENVYTKCRFVSQC 579
Cdd:PRK06164 441 PAEIEHALEALPGVAAA 457
|
|
| PRK07867 |
PRK07867 |
acyl-CoA synthetase; Validated |
117-534 |
2.41e-18 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236120 [Multi-domain] Cd Length: 529 Bit Score: 88.97 E-value: 2.41e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327099 117 SWMTYGEAASERQAIGSGLLF-----HgvnqgdcVGLYFINRPEWLVVDHACAAYSFVSVPLYDTLGPDAVKFVVNHANL 191
Cdd:PRK07867 30 SWREHIRGSAARAAALRARLDptrppH-------VGVLLDNTPEFSLLLGAAALSGIVPVGLNPTRRGAALARDIAHADC 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327099 192 QAIfcvpqtlnillsfLAEIPSIRLIVVVGGADEHLpslprgtGVTIVSYQKLLSQGRSSLHPFSPPKPEDIATICYTSG 271
Cdd:PRK07867 103 QLV-------------LTESAHAELLDGLDPGVRVI-------NVDSPAWADELAAHRDAEPPFRVADPDDLFMLIFTSG 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327099 272 TTGTPKGVVLTHGNLIanVAGSSVEAEFF--PSDV-YISyLPLAHiyerANQIMgvyGGVAVGFYQGDVFKLMDDFAVLR 348
Cdd:PRK07867 163 TSGDPKAVRCTHRKVA--SAGVMLAQRFGlgPDDVcYVS-MPLFH----SNAVM---AGWAVALAAGASIALRRKFSASG 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327099 349 ptiFCSVPRLYnriydGITSAvkssGVVKKRLFEIAynskkqaiingRTPSAFWD-----KLVFnkikeklggrvrfmGS 423
Cdd:PRK07867 233 ---FLPDVRRY-----GATYA----NYVGKPLSYVL-----------ATPERPDDadnplRIVY--------------GN 275
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327099 424 GASPlsPDVMDFLRIcFGCSVREGYGMTETSCVISAMDDGDnlSGHVGSPNPAceVKLVDvPEMNytsddQPYPRGEIC- 502
Cdd:PRK07867 276 EGAP--GDIARFARR-FGCVVVDGFGSTEGGVAITRTPDTP--PGALGPLPPG--VAIVD-PDTG-----TECPPAEDAd 342
|
410 420 430 440
....*....|....*....|....*....|....*....|....*..
gi 22327099 503 ---------------VRGPIIFKGYYKDEEQTREILDgDGWLHTGDI 534
Cdd:PRK07867 343 grllnadeaigelvnTAGPGGFEGYYNDPEADAERMR-GGVYWSGDL 388
|
|
| PRK06334 |
PRK06334 |
long chain fatty acid--[acyl-carrier-protein] ligase; Validated |
260-569 |
8.85e-18 |
|
long chain fatty acid--[acyl-carrier-protein] ligase; Validated
Pssm-ID: 180533 [Multi-domain] Cd Length: 539 Bit Score: 87.18 E-value: 8.85e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327099 260 PEDIATICYTSGTTGTPKGVVLTHGNLIANVAGSsveAEFF---PSDVYISYLPLAHIYE-RANQIMGVYGGVAVGF--- 332
Cdd:PRK06334 182 PEDVAVILFTSGTEKLPKGVPLTHANLLANQRAC---LKFFspkEDDVMMSFLPPFHAYGfNSCTLFPLLSGVPVVFayn 258
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327099 333 --YQGDVFKLMDDFAVlrpTIFCSVPRLYNRIydgITSAVKSsgvvkkrlfEIAYNSKKQAIINGrtpSAFWDKLvFNKI 410
Cdd:PRK06334 259 plYPKKIVEMIDEAKV---TFLGSTPVFFDYI---LKTAKKQ---------ESCLPSLRFVVIGG---DAFKDSL-YQEA 319
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327099 411 KEklggrvrfmgsgasplspdvmDFLRIcfgcSVREGYGMTETSCVISAMD-DGDNLSGHVGSPNPACEVKLVDvpEMNY 489
Cdd:PRK06334 320 LK---------------------TFPHI----QLRQGYGTTECSPVITINTvNSPKHESCVGMPIRGMDVLIVS--EETK 372
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327099 490 TsddqPYPRGE---ICVRGPIIFKGYY-KDEEQTREILDGDGWLHTGDIGLWLPGGRLKIIDRKKNIFKLAqGEYIAPEK 565
Cdd:PRK06334 373 V----PVSSGEtglVLTRGTSLFSGYLgEDFGQGFVELGGETWYVTGDLGYVDRHGELFLKGRLSRFVKIG-AEMVSLEA 447
|
....
gi 22327099 566 IENV 569
Cdd:PRK06334 448 LESI 451
|
|
| ABCL |
cd05958 |
2-aminobenzoate-CoA ligase (ABCL); ABCL catalyzes the initial step in the 2-aminobenzoate ... |
261-614 |
2.22e-17 |
|
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: 85.22 E-value: 2.22e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327099 261 EDIATICYTSGTTGTPKGVVLTHGNLIANVAGSSVEA-EFFPSDVYISYLPLAHIYERANQI---MGVyGGVAVGFYQGD 336
Cdd:cd05958 97 DDICILAFTSGTTGAPKATMHFHRDPLASADRYAVNVlRLREDDRFVGSPPLAFTFGLGGVLlfpFGV-GASGVLLEEAT 175
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327099 337 VFKLMDDFAVLRPTIFCSVPRLYnriydgitsavkssgvvkkrlfeiaynskkQAIINGRTPSafwdklvfnkikEKLGG 416
Cdd:cd05958 176 PDLLLSAIARYKPTVLFTAPTAY------------------------------RAMLAHPDAA------------GPDLS 213
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327099 417 RVRFMGSGASPLSPDVMDFLRICFGCSVREGYGMTETSCVISAMDDGDNLSGHVGSPNPACEVKLVDvpemnytSDDQPY 496
Cdd:cd05958 214 SLRKCVSAGEALPAALHRAWKEATGIPIIDGIGSTEMFHIFISARPGDARPGATGKPVPGYEAKVVD-------DEGNPV 286
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327099 497 PRGEI---CVRGPIIFKgyYKDEEQTREILDGdGWLHTGDIGLWLPGGRLKIIDRKKNIFKLAqGEYIAPEKIENVYTKC 573
Cdd:cd05958 287 PDGTIgrlAVRGPTGCR--YLADKRQRTYVQG-GWNITGDTYSRDPDGYFRHQGRSDDMIVSG-GYNIAPPEVEDVLLQH 362
|
330 340 350 360
....*....|....*....|....*....|....*....|....
gi 22327099 574 RFVSQCFIHGDSFNSSLV---AIVSVDPEVMKDWAASEGIKyEH 614
Cdd:cd05958 363 PAVAECAVVGHPDESRGVvvkAFVVLRPGVIPGPVLARELQ-DH 405
|
|
| PRK07798 |
PRK07798 |
acyl-CoA synthetase; Validated |
119-569 |
5.21e-17 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236100 [Multi-domain] Cd Length: 533 Bit Score: 84.55 E-value: 5.21e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327099 119 MTYGEAASERQAIGSGLLFHGVNQGDCVGLYFINRPEWlvVDHACAAYSFVSVPL-----YDtlgPDAVKFVVNHANLQA 193
Cdd:PRK07798 29 LTYAELEERANRLAHYLIAQGLGPGDHVGIYARNRIEY--VEAMLGAFKARAVPVnvnyrYV---EDELRYLLDDSDAVA 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327099 194 IFCVPQTLNILLSFLAEIPSIRLIVVVGGADEhLPSLPRGtgvtiVSYQKLLSQGrSSLHPFSPPKPEDIATIcYTSGTT 273
Cdd:PRK07798 104 LVYEREFAPRVAEVLPRLPKLRTLVVVEDGSG-NDLLPGA-----VDYEDALAAG-SPERDFGERSPDDLYLL-YTGGTT 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327099 274 GTPKGVVLTHGNL-------IANVAGSSVEAE--------------FFPsdvyISylPLAHIYERANQIMGVYGGVAVGF 332
Cdd:PRK07798 176 GMPKGVMWRQEDIfrvllggRDFATGEPIEDEeelakraaagpgmrRFP----AP--PLMHGAGQWAAFAALFSGQTVVL 249
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327099 333 YQGDVFklmDDFAVLRptifcSVPRlynriyDGITSAVKSSGVVKKRLFEiaynskkqAIINGRTpsafWDklvfnkike 412
Cdd:PRK07798 250 LPDVRF---DADEVWR-----TIER------EKVNVITIVGDAMARPLLD--------ALEARGP----YD--------- 294
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327099 413 klGGRVRFMGSGASPLSPDVMD-FLRICFGCSVREGYGMTET-SCVISAMDDGdnlSGHVGSP--NPACEVKLVDVpemn 488
Cdd:PRK07798 295 --LSSLFAIASGGALFSPSVKEaLLELLPNVVLTDSIGSSETgFGGSGTVAKG---AVHTGGPrfTIGPRTVVLDE---- 365
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327099 489 ytsDDQPYP-----RGEICVRGPIIFkGYYKDEEQTREIL---DGDGWLHTGDIGLWLPGGRLKIIDRKKNIFKLAqGEY 560
Cdd:PRK07798 366 ---DGNPVEpgsgeIGWIARRGHIPL-GYYKDPEKTAETFptiDGVRYAIPGDRARVEADGTITLLGRGSVCINTG-GEK 440
|
....*....
gi 22327099 561 IAPEKIENV 569
Cdd:PRK07798 441 VFPEEVEEA 449
|
|
| A_NRPS_Ta1_like |
cd12116 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including salinosporamide A ... |
107-594 |
1.20e-16 |
|
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: 83.11 E-value: 1.20e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327099 107 VRSDGTigeysWMTYGEAASERQAIGSGLLFHGVNQGDCVGLYFINRPEWLVVDHACAAYSFVSVPLYDTLGPDAVKFVV 186
Cdd:cd12116 6 VRDDDR-----SLSYAELDERANRLAARLRARGVGPGDRVAVYLPRSARLVAAMLAVLKAGAAYVPLDPDYPADRLRYIL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327099 187 NHANLQAIFCVPQTLNILlsflaeiPSIRLIVVVGGADEHLPSLPRGTgvtivsyqkllsqgrsslhpfsPPKPEDIATI 266
Cdd:cd12116 81 EDAEPALVLTDDALPDRL-------PAGLPVLLLALAAAAAAPAAPRT----------------------PVSPDDLAYV 131
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327099 267 CYTSGTTGTPKGVVLTHGNLIANVAGSSVEAEFFPSDVY---------IS----YLPLahiyeranqimgVYGG---VAV 330
Cdd:cd12116 132 IYTSGSTGRPKGVVVSHRNLVNFLHSMRERLGLGPGDRLlavttyafdISllelLLPL------------LAGArvvIAP 199
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327099 331 GFYQGDVFKLMDDFAVLRPTIFcsvprlynriydgitsavkssgvvkkrlfeiaynskkQAiingrTPsAFWDKLVFNKI 410
Cdd:cd12116 200 RETQRDPEALARLIEAHSITVM-------------------------------------QA-----TP-ATWRMLLDAGW 236
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327099 411 KEKLGGRVRfmgSGASPLSPDVMDFLrICFGCSVREGYGMTETSCVISAMDDGDNLSG-HVGSPNPACEVKLVDvpemny 489
Cdd:cd12116 237 QGRAGLTAL---CGGEALPPDLAARL-LSRVGSLWNLYGPTETTIWSTAARVTAAAGPiPIGRPLANTQVYVLD------ 306
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327099 490 tSDDQPYPR---GEICVRGPIIFKGYYKDEEQTREIL-------DGDGWLHTGDIGLWLPGGRLKIIDRKKNIFKLaQGE 559
Cdd:cd12116 307 -AALRPVPPgvpGELYIGGDGVAQGYLGRPALTAERFvpdpfagPGSRLYRTGDLVRRRADGRLEYLGRADGQVKI-RGH 384
|
490 500 510
....*....|....*....|....*....|....*..
gi 22327099 560 YIAPEKIENVYTKCRFVSQC--FIHGDSFNSSLVAIV 594
Cdd:cd12116 385 RIELGEIEAALAAHPGVAQAavVVREDGGDRRLVAYV 421
|
|
| entE |
PRK10946 |
(2,3-dihydroxybenzoyl)adenylate synthase; |
206-593 |
2.12e-16 |
|
(2,3-dihydroxybenzoyl)adenylate synthase;
Pssm-ID: 236803 [Multi-domain] Cd Length: 536 Bit Score: 82.73 E-value: 2.12e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327099 206 SFLAEIPSIRLIVVVGGADEHlpslprgtgvtivSYQKLLSQGRSSLhPFSPPKPEDIATICYTSGTTGTPKGVVLTHGN 285
Cdd:PRK10946 141 TLVAEHSSLRVVLLLNDDGEH-------------SLDDAINHPAEDF-TATPSPADEVAFFQLSGGSTGTPKLIPRTHND 206
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327099 286 LIANVAGSSVEAEFFPSDVYISYLPLAHiyeraNQIMGVYGGVAVgFYQGDVFKLMDDfavlrPTIFCSVPrLYNRIYDG 365
Cdd:PRK10946 207 YYYSVRRSVEICGFTPQTRYLCALPAAH-----NYPMSSPGALGV-FLAGGTVVLAPD-----PSATLCFP-LIEKHQVN 274
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327099 366 ITSAVKSSGVV-KKRLFEIAYNSKKQAIingrtpsafwdKLVfnkikeKLGGrVRFMGSGASPLsPDVMdflricfGCSV 444
Cdd:PRK10946 275 VTALVPPAVSLwLQAIAEGGSRAQLASL-----------KLL------QVGG-ARLSETLARRI-PAEL-------GCQL 328
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327099 445 REGYGMTETSCVISAMDDGDNlsgHV----GSP-NPACEVKLVDvpemnytSDDQPYPRGEI---CVRGPIIFKGYYKDE 516
Cdd:PRK10946 329 QQVFGMAEGLVNYTRLDDSDE---RIfttqGRPmSPDDEVWVAD-------ADGNPLPQGEVgrlMTRGPYTFRGYYKSP 398
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327099 517 EQTREILDGDGWLHTGDIGLWLPGGRLKIIDRKKNifklaQ----GEYIAPEKIENVYTKcrfvsqcfiHGDSFNSSLVA 592
Cdd:PRK10946 399 QHNASAFDANGFYCSGDLVSIDPDGYITVVGREKD-----QinrgGEKIAAEEIENLLLR---------HPAVIHAALVS 464
|
.
gi 22327099 593 I 593
Cdd:PRK10946 465 M 465
|
|
| A_NRPS_Bac |
cd17655 |
bacitracin synthetase and related proteins; This family of the adenylation (A) domain of ... |
223-572 |
2.31e-16 |
|
bacitracin synthetase and related proteins; This family of the adenylation (A) domain of nonribosomal peptide synthases (NRPS) includes bacitracin synthetases 1, 2, and 3 (BA1, also known as ATP-dependent cysteine adenylase or cysteine activase, BA2, also known as ATP-dependent lysine adenylase or lysine activase, and BA3, also known as ATP-dependent isoleucine adenylase or isoleucine activase) in Bacilli. Bacitracin is a mixture of related cyclic peptides used as a polypeptide antibiotic. This family also includes gramicidin synthetase 1 involved in synthesis of the cyclic peptide antibiotic gramicidin S via activation of phenylalanine. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.
Pssm-ID: 341310 [Multi-domain] Cd Length: 490 Bit Score: 82.38 E-value: 2.31e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327099 223 ADEHLPSLPRGTG-VTIVSYQKLLSQGRSSLHPfsPPKPEDIATICYTSGTTGTPKGVVLTHGNLIanvagssveaeffp 301
Cdd:cd17655 100 TQSHLQPPIAFIGlIDLLDEDTIYHEESENLEP--VSKSDDLAYVIYTSGSTGKPKGVMIEHRGVV-------------- 163
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327099 302 sdvyisylplaHIYERANQIMgvyggvavgfYQGDVfklmDDFAVLRPTIF-CSVPRLY------NRIYdgitsAVKSSG 374
Cdd:cd17655 164 -----------NLVEWANKVI----------YQGEH----LRVALFASISFdASVTEIFasllsgNTLY-----IVRKET 213
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327099 375 VVKKRLFEIAYNSKKQAIINGrTPSAFwdKLVfNKIKEKLGGRVRFMGSGASPLSPDVMDFLRICFGCSVR--EGYGMTE 452
Cdd:cd17655 214 VLDGQALTQYIRQNRITIIDL-TPAHL--KLL-DAADDSEGLSLKHLIVGGEALSTELAKKIIELFGTNPTitNAYGPTE 289
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327099 453 TS--CVISAMDDGDNLSGHV--GSPNPACEVKLVDvpemnytSDDQPYP---RGEICVRGPIIFKGYYKDEEQTRE---- 521
Cdd:cd17655 290 TTvdASIYQYEPETDQQVSVpiGKPLGNTRIYILD-------QYGRPQPvgvAGELYIGGEGVARGYLNRPELTAEkfvd 362
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|...
gi 22327099 522 --ILDGDGWLHTGDIGLWLPGGRLKIIDRKKNIFKLaQGEYIAPEKIENVYTK 572
Cdd:cd17655 363 dpFVPGERMYRTGDLARWLPDGNIEFLGRIDHQVKI-RGYRIELGEIEARLLQ 414
|
|
| PRK09029 |
PRK09029 |
O-succinylbenzoic acid--CoA ligase; Provisional |
447-581 |
2.44e-16 |
|
O-succinylbenzoic acid--CoA ligase; Provisional
Pssm-ID: 236363 [Multi-domain] Cd Length: 458 Bit Score: 82.23 E-value: 2.44e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327099 447 GYGMTE---TSCVISAmddgDNLSGhVGSPNPACEVKLVDvpemnytsddqpyprGEICVRGPIIFKGYYKDEeQTREIL 523
Cdd:PRK09029 270 GYGLTEmasTVCAKRA----DGLAG-VGSPLPGREVKLVD---------------GEIWLRGASLALGYWRQG-QLVPLV 328
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*...
gi 22327099 524 DGDGWLHTGDIGLWLpGGRLKIIDRKKNIFkLAQGEYIAPEKIENVYTKCRFVSQCFI 581
Cdd:PRK09029 329 NDEGWFATRDRGEWQ-NGELTILGRLDNLF-FSGGEGIQPEEIERVINQHPLVQQVFV 384
|
|
| PRK05691 |
PRK05691 |
peptide synthase; Validated |
259-573 |
3.80e-16 |
|
peptide synthase; Validated
Pssm-ID: 235564 [Multi-domain] Cd Length: 4334 Bit Score: 83.29 E-value: 3.80e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327099 259 KPEDIATICYTSGTTGTPKGVVLTHGNLIAN--VAGSSVEAEFFPSDVYISYLPLAHiyeranqIMGVYGGVAVGFYQGD 336
Cdd:PRK05691 164 QPDDIAFLQYTSGSTALPKGVQVSHGNLVANeqLIRHGFGIDLNPDDVIVSWLPLYH-------DMGLIGGLLQPIFSGV 236
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327099 337 VFKLMDdfavlrPTIFCSVP-RLYNRI--YDGITSAVKssgvvkkrlfEIAYNskkqaIINGRTPSAFWDKLVFNkikek 413
Cdd:PRK05691 237 PCVLMS------PAYFLERPlRWLEAIseYGGTISGGP----------DFAYR-----LCSERVSESALERLDLS----- 290
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327099 414 lGGRVRFmgSGASPLSPDVMDFLRICF-GCSVRE-----GYGMTETSCV---------ISAMD-DGDNLSGHV------- 470
Cdd:PRK05691 291 -RWRVAY--SGSEPIRQDSLERFAEKFaACGFDPdsffaSYGLAEATLFvsggrrgqgIPALElDAEALARNRaepgtgs 367
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327099 471 -----GSPNPACEVKLVDVPEMNYTSDDQPyprGEICVRGPIIFKGYYKDEEQTREI---LDGDGWLHTGDIGlWLPGGR 542
Cdd:PRK05691 368 vlmscGRSQPGHAVLIVDPQSLEVLGDNRV---GEIWASGPSIAHGYWRNPEASAKTfveHDGRTWLRTGDLG-FLRDGE 443
|
330 340 350
....*....|....*....|....*....|.
gi 22327099 543 LKIIDRKKNIFkLAQGEYIAPEKIENVYTKC 573
Cdd:PRK05691 444 LFVTGRLKDML-IVRGHNLYPQDIEKTVERE 473
|
|
| PLN02479 |
PLN02479 |
acetate-CoA ligase |
216-569 |
5.32e-16 |
|
acetate-CoA ligase
Pssm-ID: 178097 [Multi-domain] Cd Length: 567 Bit Score: 81.81 E-value: 5.32e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327099 216 LIVVVGGADEHLPSLPRGTGVTIVSYQKLLSQGRSSLhPFSPPKPE--DIAtICYTSGTTGTPKGVVLTH-GNLIANVAG 292
Cdd:PLN02479 150 LLIVIGDPTCDPKSLQYALGKGAIEYEKFLETGDPEF-AWKPPADEwqSIA-LGYTSGTTASPKGVVLHHrGAYLMALSN 227
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327099 293 SSVeAEFFPSDVYISYLPLAH-----------------IYERANQIMGVYGGVAvgfYQGdvfklmddfavlrPTIFCSV 355
Cdd:PLN02479 228 ALI-WGMNEGAVYLWTLPMFHcngwcftwtlaalcgtnICLRQVTAKAIYSAIA---NYG-------------VTHFCAA 290
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327099 356 PRLYNRIYDGitsavkssgvvkkrlfeiaynSKKQAIIngrtpsafwdklvfnkikeKLGGRVRFMGSGASPlSPDVMDF 435
Cdd:PLN02479 291 PVVLNTIVNA---------------------PKSETIL-------------------PLPRVVHVMTAGAAP-PPSVLFA 329
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327099 436 LRIcFGCSVREGYGMTET---SCVISAMDDGDNLSGHVGSP-NPACEVKLVDVPEMNY--TSDDQPYPR-----GEICVR 504
Cdd:PLN02479 330 MSE-KGFRVTHTYGLSETygpSTVCAWKPEWDSLPPEEQARlNARQGVRYIGLEGLDVvdTKTMKPVPAdgktmGEIVMR 408
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 22327099 505 GPIIFKGYYKDEEQTREILDGdGWLHTGDIGLWLPGGRLKIIDRKKNIFkLAQGEYIAPEKIENV 569
Cdd:PLN02479 409 GNMVMKGYLKNPKANEEAFAN-GWFHSGDLGVKHPDGYIEIKDRSKDII-ISGGENISSLEVENV 471
|
|
| PLN03102 |
PLN03102 |
acyl-activating enzyme; Provisional |
131-572 |
1.69e-15 |
|
acyl-activating enzyme; Provisional
Pssm-ID: 215576 [Multi-domain] Cd Length: 579 Bit Score: 80.06 E-value: 1.69e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327099 131 IGSGLLFHGVNQGDCVGLYFINRPEWLVVDHACAAYSFVSVPLYDTLGPDAVKFVVNHANlqaifcvPQTLNILLSFLAE 210
Cdd:PLN03102 52 LAASLISLNITKNDVVSVLAPNTPAMYEMHFAVPMAGAVLNPINTRLDATSIAAILRHAK-------PKILFVDRSFEPL 124
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327099 211 IPSIRLIVVVGGADEHLPSL-------PRGTGVTIVSYQKLLSQGR----SSLHPFSPPKPEDIATICYTSGTTGTPKGV 279
Cdd:PLN03102 125 AREVLHLLSSEDSNLNLPVIfiheidfPKRPSSEELDYECLIQRGEptpsLVARMFRIQDEHDPISLNYTSGTTADPKGV 204
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327099 280 VLTHGNLIANVAGSSVEAEFFPSDVYISYLPLAHIYERANQI-MGVYGGVAVGFYQGDVFKLMDDFAVLRPTIFCSVPRL 358
Cdd:PLN03102 205 VISHRGAYLSTLSAIIGWEMGTCPVYLWTLPMFHCNGWTFTWgTAARGGTSVCMRHVTAPEIYKNIEMHNVTHMCCVPTV 284
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327099 359 YNRIYDGitsavkssgvvkKRLFEIAYNSKKQAIINGRTPSAFWDKLVfnkikEKLGGRVRfmgsgasplspdvmdflri 438
Cdd:PLN03102 285 FNILLKG------------NSLDLSPRSGPVHVLTGGSPPPAALVKKV-----QRLGFQVM------------------- 328
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327099 439 cfgcsvrEGYGMTETSCVI---SAMDDGDNLSGH----VGSPNPACEVKLVDVPEMNyTSDDQPYPR-----GEICVRGP 506
Cdd:PLN03102 329 -------HAYGLTEATGPVlfcEWQDEWNRLPENqqmeLKARQGVSILGLADVDVKN-KETQESVPRdgktmGEIVIKGS 400
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 22327099 507 IIFKGYYKDEEQTREILDgDGWLHTGDIGLWLPGGRLKIIDRKKNIFkLAQGEYIAPEKIENVYTK 572
Cdd:PLN03102 401 SIMKGYLKNPKATSEAFK-HGWLNTGDVGVIHPDGHVEIKDRSKDII-ISGGENISSVEVENVLYK 464
|
|
| A_NRPS_Cytc1-like |
cd17643 |
similar to adenylation domain of cytotrienin synthetase CytC1; This family of the adenylation ... |
260-567 |
3.56e-15 |
|
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: 78.50 E-value: 3.56e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327099 260 PEDIATICYTSGTTGTPKGVVLTHGNLIANVAGSSVEAEFFPSDVYI---SY----------LPLAHiyeranqimgvyG 326
Cdd:cd17643 92 PDDLAYVIYTSGSTGRPKGVVVSHANVLALFAATQRWFGFNEDDVWTlfhSYafdfsvweiwGALLH------------G 159
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327099 327 G--VAVgfyqgdvfklmdDFAVLRPtifcsvPRLYNRIydgitsaVKSSGVvkkrlfeiaynskkqAIINgRTPSAFwdk 404
Cdd:cd17643 160 GrlVVV------------PYEVARS------PEDFARL-------LRDEGV---------------TVLN-QTPSAF--- 195
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327099 405 LVFNKIKEKLGGRV---RFMGSGASPLSPDVMDFLRICFGCS---VREGYGMTETsCV------ISAMDDGDNLSGHVGS 472
Cdd:cd17643 196 YQLVEAADRDGRDPlalRYVIFGGEALEAAMLRPWAGRFGLDrpqLVNMYGITET-TVhvtfrpLDAADLPAAAASPIGR 274
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327099 473 PNPACEVKLVDvpemnytSDDQPYPR---GEICVRGPIIFKGYYKDEEQTRE-------ILDGDGWLHTGDIGLWLPGGR 542
Cdd:cd17643 275 PLPGLRVYVLD-------ADGRPVPPgvvGELYVSGAGVARGYLGRPELTAErfvanpfGGPGSRMYRTGDLARRLPDGE 347
|
330 340
....*....|....*....|....*
gi 22327099 543 LKIIDRKKNIFKLaQGEYIAPEKIE 567
Cdd:cd17643 348 LEYLGRADEQVKI-RGFRIELGEIE 371
|
|
| CBAL |
cd05923 |
4-Chlorobenzoate-CoA ligase (CBAL); CBAL catalyzes the conversion of 4-chlorobenzoate (4-CB) ... |
119-569 |
6.58e-15 |
|
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: 77.93 E-value: 6.58e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327099 119 MTYGEAASERQAIGSGLLFHGVNQGDCVGLYFINRPEWLVVDHACAAYSFVSVPLYDTLGPDAVKFVVNHANLQAIFCVP 198
Cdd:cd05923 29 LTYSELRARIEAVAARLHARGLRPGQRVAVVLPNSVEAVIALLALHRLGAVPALINPRLKAAELAELIERGEMTAAVIAV 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327099 199 QTLNILLSFLAEIPSIRLIVVVGgadehlpslprgTGVTiVSYQKLLsqgrsslhPFSPPKPEDIATICYTSGTTGTPKG 278
Cdd:cd05923 109 DAQVMDAIFQSGVRVLALSDLVG------------LGEP-ESAGPLI--------EDPPREPEQPAFVFYTSGTTGLPKG 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327099 279 VVLTHGNLIANVAGSSVEAE--FFPSDVYISYLPLAHiyeranqIMGVYGGVAV-----GFY-------QGDVFKLMDDf 344
Cdd:cd05923 168 AVIPQRAAESRVLFMSTQAGlrHGRHNVVLGLMPLYH-------VIGFFAVLVAalaldGTYvvveefdPADALKLIEQ- 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327099 345 avLRPTIFCSVPRLynriYDGITSAVKSSGVVKKRLfeiaynskkqaiingrtpsafwDKLVFnkikeklggrvrfmgSG 424
Cdd:cd05923 240 --ERVTSLFATPTH----LDALAAAAEFAGLKLSSL----------------------RHVTF---------------AG 276
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327099 425 ASplSPD-VMDFLRICFGCSVREGYGMTETscvISAMDDGDNLSGHVGSPNPACEVKLVDVPEmnytSDDQPYPRGEicv 503
Cdd:cd05923 277 AT--MPDaVLERVNQHLPGEKVNIYGTTEA---MNSLYMRDARTGTEMRPGFFSEVRIVRIGG----SPDEALANGE--- 344
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 22327099 504 RGPII--------FKGYYKDEEQTREILDgDGWLHTGDIGLWLPGGRLKIIDRKKNIFkLAQGEYIAPEKIENV 569
Cdd:cd05923 345 EGELIvaaaadaaFTGYLNQPEATAKKLQ-DGWYRTGDVGYVDPSGDVRILGRVDDMI-ISGGENIHPSEIERV 416
|
|
| MACS_like_4 |
cd05969 |
Uncharacterized subfamily of Acetyl-CoA synthetase like family (ACS); This family is most ... |
120-569 |
7.26e-15 |
|
Uncharacterized subfamily of Acetyl-CoA synthetase like family (ACS); This family is most similar to acetyl-CoA synthetase. Acetyl-CoA synthetase (ACS) catalyzes the formation of acetyl-CoA from acetate, CoA, and ATP. Synthesis of acetyl-CoA is carried out in a two-step reaction. In the first step, the enzyme catalyzes the synthesis of acetyl-AMP intermediate from acetate and ATP. In the second step, acetyl-AMP reacts with CoA to produce acetyl-CoA. This enzyme is only present in bacteria.
Pssm-ID: 341273 [Multi-domain] Cd Length: 442 Bit Score: 77.54 E-value: 7.26e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327099 120 TYGEAASERQAIGSGLLFHGVNQGDCVGLYFINRPEWLVVDHACAAYSFVSVPLYDTLGPDAVKFVVnhanlqaifcvpq 199
Cdd:cd05969 2 TFAQLKVLSARFANVLKSLGVGKGDRVFVLSPRSPELYFSMLGIGKIGAVICPLFSAFGPEAIRDRL------------- 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327099 200 tlnillsflaEIPSIRLIVVVggadehlPSLPRGTgvtivsyqkllsqgrsslhpfsppKPEDIATICYTSGTTGTPKGV 279
Cdd:cd05969 69 ----------ENSEAKVLITT-------EELYERT------------------------DPEDPTLLHYTSGTTGTPKGV 107
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327099 280 VLTHGNLIANVAGSSVEAEFFPSDVYISYLPLAHIyerANQIMGVYGGVAVGfyqgdvfklmddfavlrptifCSvprly 359
Cdd:cd05969 108 LHVHDAMIFYYFTGKYVLDLHPDDIYWCTADPGWV---TGTVYGIWAPWLNG---------------------VT----- 158
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327099 360 NRIYDGITSAVKSSGVVKKRLFEIAYNskkqaiingrTPSAFwdklvfnKIKEKLG---------GRVRFMGSGASPLSP 430
Cdd:cd05969 159 NVVYEGRFDAESWYGIIERVKVTVWYT----------APTAI-------RMLMKEGdelarkydlSSLRFIHSVGEPLNP 221
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327099 431 DVMDFLRICFGCSVREGYGMTET-SCVISAMDDGDNLSGHVGSPNPACEVKLVDvpemNYTSDDQPYPRGEICVRG--PI 507
Cdd:cd05969 222 EAIRWGMEVFGVPIHDTWWQTETgSIMIANYPCMPIKPGSMGKPLPGVKAAVVD----ENGNELPPGTKGILALKPgwPS 297
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 22327099 508 IFKGYYKDEEQTREILDgDGWLHTGDIGLWLPGGRLKIIDRKKNIFKLAqGEYIAPEKIENV 569
Cdd:cd05969 298 MFRGIWNDEERYKNSFI-DGWYLTGDLAYRDEDGYFWFVGRADDIIKTS-GHRVGPFEVESA 357
|
|
| PRK09274 |
PRK09274 |
peptide synthase; Provisional |
212-593 |
2.25e-14 |
|
peptide synthase; Provisional
Pssm-ID: 236443 [Multi-domain] Cd Length: 552 Bit Score: 76.48 E-value: 2.25e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327099 212 PSIRLIVVVGGAdehlpSLPRGTgvtivSYQKLLSQGRssLHPFSPP--KPEDIATICYTSGTTGTPKGVVLTHGNLIAN 289
Cdd:PRK09274 135 PSVRRLVTVGGR-----LLWGGT-----TLATLLRDGA--AAPFPMAdlAPDDMAAILFTSGSTGTPKGVVYTHGMFEAQ 202
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327099 290 vagssVEA--EFF---PSDVYISYLPLahiyeranqiMGVYgGVAVGFyqGDVFKLMdDFAvlRPtIFCSVPRLYNRIYD 364
Cdd:PRK09274 203 -----IEAlrEDYgiePGEIDLPTFPL----------FALF-GPALGM--TSVIPDM-DPT--RP-ATVDPAKLFAAIER 260
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327099 365 -GITSAVKSSgvvkkrlfeiaynskkqAIINGRTPSAFWDKLVFNKIKeklggRVRfmgSGASPLSPDVMDFLRICF--G 441
Cdd:PRK09274 261 yGVTNLFGSP-----------------ALLERLGRYGEANGIKLPSLR-----RVI---SAGAPVPIAVIERFRAMLppD 315
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327099 442 CSVREGYGMTET--SCVIS----------AMDDGDnlsGH-VGSPNPACEVKLVDVPE--MNYTSDDQPYPR---GEICV 503
Cdd:PRK09274 316 AEILTPYGATEAlpISSIEsreilfatraATDNGA---GIcVGRPVDGVEVRIIAISDapIPEWDDALRLATgeiGEIVV 392
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327099 504 RGPIIFKGYYKDEEQTRE--ILDGDG--WLHTGDIGlWL-PGGRLKIIDRKKNIFKLAQGEY--IAPEKIENVytkcrfv 576
Cdd:PRK09274 393 AGPMVTRSYYNRPEATRLakIPDGQGdvWHRMGDLG-YLdAQGRLWFCGRKAHRVETAGGTLytIPCERIFNT------- 464
|
410
....*....|....*..
gi 22327099 577 sqcfiHGDSFNSSLVAI 593
Cdd:PRK09274 465 -----HPGVKRSALVGV 476
|
|
| PRK05851 |
PRK05851 |
long-chain-fatty acid--ACP ligase MbtM; |
225-576 |
4.16e-14 |
|
long-chain-fatty acid--ACP ligase MbtM;
Pssm-ID: 180289 [Multi-domain] Cd Length: 525 Bit Score: 75.57 E-value: 4.16e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327099 225 EHLPSL-PRGTGVTIVSYQKLLSQGRSSlhPFSPPKPEDIATICYTSGTTGTPKGVVLTHGNLIANVAG----SSVEAef 299
Cdd:PRK05851 117 SHLERLrAVDSSVTVHDLATAAHTNRSA--SLTPPDSGGPAVLQGTAGSTGTPRTAILSPGAVLSNLRGlnarVGLDA-- 192
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327099 300 fPSDVYISYLPLAHIYERANQIMGVYGGVAVGfyqgdvfklmddfavLRPT-IFCSVP-RLYNRIYD---GITSAVKssg 374
Cdd:PRK05851 193 -ATDVGCSWLPLYHDMGLAFLLTAALAGAPLW---------------LAPTtAFSASPfRWLSWLSDsraTLTAAPN--- 253
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327099 375 vvkkrlfeIAYNskkqaiINGRTPSafwdklvfnKIKEKLGGRVRFMGSGASPLspDVMDFLRIC-----FGC---SVRE 446
Cdd:PRK05851 254 --------FAYN------LIGKYAR---------RVSDVDLGALRVALNGGEPV--DCDGFERFAtamapFGFdagAAAP 308
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327099 447 GYGMTETSCVISA-------------MDDGDNLSGH--VGSPNPACEVKLvdvpemnyTSDDQPYPR-----GEICVRGP 506
Cdd:PRK05851 309 SYGLAESTCAVTVpvpgiglrvdevtTDDGSGARRHavLGNPIPGMEVRI--------SPGDGAAGVagreiGEIEIRGA 380
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327099 507 IIFKGYYKDEEqtreiLDGDGWLHTGDIGLWLPGGrLKIIDRKKNIFKLAqGEYIAPEKIENVYTKCRFV 576
Cdd:PRK05851 381 SMMSGYLGQAP-----IDPDDWFPTGDLGYLVDGG-LVVCGRAKELITVA-GRNIFPTEIERVAAQVRGV 443
|
|
| AACS_like |
cd05968 |
Uncharacterized acyl-CoA synthetase subfamily similar to Acetoacetyl-CoA synthetase; This ... |
26-569 |
4.46e-14 |
|
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: 75.60 E-value: 4.46e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327099 26 QSSSLFLNATASsASPFFKEDSYSVVLPEKLDTGKWNVYRSKRSPtklvsrFPDHPEIGTLhdNFVHAVEtyaeNKYLGT 105
Cdd:cd05968 7 PDLEAFLERSAE-DNAWFWGEFVKDVGIEWYEPPYQTLDLSGGKP------WAAWFVGGRM--NIVEQLL----DKWLAD 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327099 106 R-----VRSDGTIGEYSWMTYGEAASERQAIGSGLLFHGVNQGDCVGLYFINRPEWLVVDHACAAYSFVSVPLYDTLGPD 180
Cdd:cd05968 74 TrtrpaLRWEGEDGTSRTLTYGELLYEVKRLANGLRALGVGKGDRVGIYLPMIPEIVPAFLAVARIGGIVVPIFSGFGKE 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327099 181 AVKFVVNHANLQAIFCVPQTL--NILLSFLAEI-------PSIRLIVVVGGADEHLPSlprgtgvTIVSYQKLLSQGRSS 251
Cdd:cd05968 154 AAATRLQDAEAKALITADGFTrrGREVNLKEEAdkacaqcPTVEKVVVVRHLGNDFTP-------AKGRDLSYDEEKETA 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327099 252 LHPFSPPKPEDIATICYTSGTTGTPKGVVLTHgnlianvAGSSVEAEF---FPSDV-------YISYLplahiyeraNQI 321
Cdd:cd05968 227 GDGAERTESEDPLMIIYTSGTTGKPKGTVHVH-------AGFPLKAAQdmyFQFDLkpgdlltWFTDL---------GWM 290
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327099 322 MG---VYGGVavgfyqgdvfklmddfaVLRPTIFcsvprlynrIYDGI---TSAVKSSGVVKKrlFEIAYNSKKQAIIng 395
Cdd:cd05968 291 MGpwlIFGGL-----------------ILGATMV---------LYDGApdhPKADRLWRMVED--HEITHLGLSPTLI-- 340
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327099 396 RTPSAFWDKLVFNKIKEKLggrvRFMGSGASPLSPDVMDFLRICFG---CSVREGYGMTETScvisamddGDNLSGHVGS 472
Cdd:cd05968 341 RALKPRGDAPVNAHDLSSL----RVLGSTGEPWNPEPWNWLFETVGkgrNPIINYSGGTEIS--------GGILGNVLIK 408
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327099 473 PNPACEVKLVdVPEMNYTS-DDQPYP----RGEICVRGPII--FKGYYKDEEQTREI----LDGDgWLHtGDIGLWLPGG 541
Cdd:cd05968 409 PIKPSSFNGP-VPGMKADVlDESGKParpeVGELVLLAPWPgmTRGFWRDEDRYLETywsrFDNV-WVH-GDFAYYDEEG 485
|
570 580
....*....|....*....|....*...
gi 22327099 542 RLKIIDRKKNIFKLAqGEYIAPEKIENV 569
Cdd:cd05968 486 YFYILGRSDDTINVA-GKRVGPAEIESV 512
|
|
| PRK08276 |
PRK08276 |
long-chain-fatty-acid--CoA ligase; Validated |
119-569 |
6.12e-14 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236215 [Multi-domain] Cd Length: 502 Bit Score: 74.94 E-value: 6.12e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327099 119 MTYGEAASERQAIGSGLLFHGVNQGDCVGLYFINRPEWLVVDHACAAYSFVSVPLYDTLGPDAVKFVVNHANLQAIFCVP 198
Cdd:PRK08276 12 VTYGELEARSNRLAHGLRALGLREGDVVAILLENNPEFFEVYWAARRSGLYYTPINWHLTAAEIAYIVDDSGAKVLIVSA 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327099 199 QTLNILLSFLAEIPS-IRLIVVVGGADEhlpslprgtGVTivSYQKLLSQgrsslHPFSPPKPEDI-ATICYTSGTTGTP 276
Cdd:PRK08276 92 ALADTAAELAAELPAgVPLLLVVAGPVP---------GFR--SYEEALAA-----QPDTPIADETAgADMLYSSGTTGRP 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327099 277 KGVV--LTHGNLIANVAGSSVEAEFF----PSDVYISYLPLAHIYE-RANQIMGVYGGVAVgfyqgdvfkLMDDF----- 344
Cdd:PRK08276 156 KGIKrpLPGLDPDEAPGMMLALLGFGmyggPDSVYLSPAPLYHTAPlRFGMSALALGGTVV---------VMEKFdaeea 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327099 345 --AVLRPTIFCS--VPRLYNRIydgitsaVKSSGVVKKRlfeiaYNSKKqaiingrtpsafwdklvfnkikeklggrVRF 420
Cdd:PRK08276 227 laLIERYRVTHSqlVPTMFVRM-------LKLPEEVRAR-----YDVSS----------------------------LRV 266
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327099 421 MGSGASPLSPDV----MDFlricFGCSVREGYGMTET--SCVISAmddGDNLS--GHVGSPnPACEVKLVDvpemnytSD 492
Cdd:PRK08276 267 AIHAAAPCPVEVkramIDW----WGPIIHEYYASSEGggVTVITS---EDWLAhpGSVGKA-VLGEVRILD-------ED 331
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327099 493 DQPYPRGEIcvrGPIIFKG------YYKDEEQTREILDGDGWLHTGDIGlWLPG-GRLKIIDRKKNIFkLAQGEYIAPEK 565
Cdd:PRK08276 332 GNELPPGEI---GTVYFEMdgypfeYHNDPEKTAAARNPHGWVTVGDVG-YLDEdGYLYLTDRKSDMI-ISGGVNIYPQE 406
|
....
gi 22327099 566 IENV 569
Cdd:PRK08276 407 IENL 410
|
|
| PRK05857 |
PRK05857 |
fatty acid--CoA ligase; |
108-569 |
7.74e-14 |
|
fatty acid--CoA ligase;
Pssm-ID: 180293 [Multi-domain] Cd Length: 540 Bit Score: 74.66 E-value: 7.74e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327099 108 RSDGTigeySWMTYGEAASERQAIGSGLLFHGVNQGDCVGLYFINRPEWLVVDHACAAYSFVSVPLYDTLGPDAVKFVVN 187
Cdd:PRK05857 35 RCDGT----SALRYRELVAEVGGLAADLRAQSVSRGSRVLVISDNGPETYLSVLACAKLGAIAVMADGNLPIAAIERFCQ 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327099 188 HANLQAIFCVPQT---LNILLSFLAEIPSIRlIVVVGGADEHLPSLPRGtgvtivsyqkllsqgrsslHPFSPPK--PED 262
Cdd:PRK05857 111 ITDPAAALVAPGSkmaSSAVPEALHSIPVIA-VDIAAVTRESEHSLDAA-------------------SLAGNADqgSED 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327099 263 IATICYTSGTTGTPKGVVLTHGNLIANVAGSSVEA----EFFPSDVYISYLPLAHI---YERANQIMgvYGGVAV--GFY 333
Cdd:PRK05857 171 PLAMIFTSGTTGEPKAVLLANRTFFAVPDILQKEGlnwvTWVVGETTYSPLPATHIgglWWILTCLM--HGGLCVtgGEN 248
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327099 334 QGDVFKLMDDFAVlrpTIFCSVPRLYNRIydgiTSAVKSSGVVKKRLFEIAYNSKKqaiingrtpsafwdklvfnkikeK 413
Cdd:PRK05857 249 TTSLLEILTTNAV---ATTCLVPTLLSKL----VSELKSANATVPSLRLVGYGGSR-----------------------A 298
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327099 414 LGGRVRFMGSGasplspdvmdflricfGCSVREGYGMTETSCVISAM-DDGDNLS----GHVGSPNPACEVKLVDV---- 484
Cdd:PRK05857 299 IAADVRFIEAT----------------GVRTAQVYGLSETGCTALCLpTDDGSIVkieaGAVGRPYPGVDVYLAATdgig 362
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327099 485 PEMNYTSDDQPYprGEICVRGPIIFKGYYKDEEQTREILdGDGWLHTGDIGLWLPGGRLKIIDRKKNIFkLAQGEYIAPE 564
Cdd:PRK05857 363 PTAPGAGPSASF--GTLWIKSPANMLGYWNNPERTAEVL-IDGWVNTGDLLERREDGFFYIKGRSSEMI-ICGGVNIAPD 438
|
....*
gi 22327099 565 KIENV 569
Cdd:PRK05857 439 EVDRI 443
|
|
| MACS_like_2 |
cd05973 |
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the ... |
119-583 |
1.36e-13 |
|
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the two-step activation of medium chain fatty acids (containing 4-12 carbons). The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. MACS enzymes are localized to mitochondria.
Pssm-ID: 341277 [Multi-domain] Cd Length: 437 Bit Score: 73.32 E-value: 1.36e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327099 119 MTYGEAASERQAIGSGLLFHGVNQGDCVGLYFINRPEWLVVDHACAAYSFVSVPLYDTLGPDAVKFVVNHANLQaifcvp 198
Cdd:cd05973 1 LTFGELRALSARFANALQELGVGPGDVVAGLLPRTPELVVTILGIWRLGAVYQPLFTAFGPKAIEHRLRTSGAR------ 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327099 199 qtlnillsflaeipsirlIVVVGGADEHlpslprgtgvtivsyqKLlsqgrsslhpfsppkPEDIATICYTSGTTGTPKG 278
Cdd:cd05973 75 ------------------LVVTDAANRH----------------KL---------------DSDPFVMMFTSGTTGLPKG 105
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327099 279 VVLTHGNLIANVAGSSVEAEFFPSDVYisylplahiYERANQimgvygGVAVGFYqgdvFKLMDDFAVLRPTIFC----S 354
Cdd:cd05973 106 VPVPLRALAAFGAYLRDAVDLRPEDSF---------WNAADP------GWAYGLY----YAITGPLALGHPTILLeggfS 166
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327099 355 VPRLYNRIYD-GITSAVKSSgvvkkrlfeIAYNSkkqaIINGRTPSAfwdklvfnkikEKLGGRVRFMGSGASPLSPDVM 433
Cdd:cd05973 167 VESTWRVIERlGVTNLAGSP---------TAYRL----LMAAGAEVP-----------ARPKGRLRRVSSAGEPLTPEVI 222
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327099 434 DFLRICFGCSVREGYGMTETSCVIS-AMDDGDNL-SGHVGSPNPACEVKLVDvpemnyTSDDQPYPR--GEICV---RGP 506
Cdd:cd05973 223 RWFDAALGVPIHDHYGQTELGMVLAnHHALEHPVhAGSAGRAMPGWRVAVLD------DDGDELGPGepGRLAIdiaNSP 296
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 22327099 507 II-FKGYYKDEEQTreiLDGdGWLHTGDIGLWLPGGRLKIIDRKKNIFKLAqGEYIAPEKIENVYTKCRFVSQCFIHG 583
Cdd:cd05973 297 LMwFRGYQLPDTPA---IDG-GYYLTGDTVEFDPDGSFSFIGRADDVITMS-GYRIGPFDVESALIEHPAVAEAAVIG 369
|
|
| MACS_like_1 |
cd05974 |
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the ... |
422-569 |
1.37e-13 |
|
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the two-step activation of medium chain fatty acids (containing 4-12 carbons). The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. MACS enzymes are localized to mitochondria.
Pssm-ID: 341278 [Multi-domain] Cd Length: 432 Bit Score: 73.37 E-value: 1.37e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327099 422 GSGaSPLSPDVMDFLRICFGCSVREGYGMTETSCVISAMDDGDNLSGHVGSPNPACEVKLVDvpemnytSDDQPYPRGEI 501
Cdd:cd05974 207 GAG-EPLNPEVIEQVRRAWGLTIRDGYGQTETTALVGNSPGQPVKAGSMGRPLPGYRVALLD-------PDGAPATEGEV 278
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 22327099 502 CV-----RGPIIFKGYYKDEEQTREILdGDGWLHTGDIGLWLPGGRLKIIDRKKNIFKlAQGEYIAPEKIENV 569
Cdd:cd05974 279 ALdlgdtRPVGLMKGYAGDPDKTAHAM-RGGYYRTGDIAMRDEDGYLTYVGRADDVFK-SSDYRISPFELESV 349
|
|
| A_NRPS_SidN3_like |
cd05918 |
The adenylation (A) domain of siderophore-synthesizing nonribosomal peptide synthetases (NRPS); ... |
259-599 |
3.53e-13 |
|
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: 72.19 E-value: 3.53e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327099 259 KPEDIATICYTSGTTGTPKGVVLTHGNLIANVagssveaeffpsdvyisylpLAHIYeranqIMGVYGGVAV------GF 332
Cdd:cd05918 104 SPSDAAYVIFTSGSTGKPKGVVIEHRALSTSA--------------------LAHGR-----ALGLTSESRVlqfasyTF 158
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327099 333 yqgDVFkLMDDFAVLRP--TIfCsVPRLYNRIyDGITSAVKSSGVvkkrlfeiayNskkQAIIngrTPSafwdklVFNKI 410
Cdd:cd05918 159 ---DVS-ILEIFTTLAAggCL-C-IPSEEDRL-NDLAGFINRLRV----------T---WAFL---TPS------VARLL 209
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327099 411 KEKLGGRVRFMGSGASPLSPDVMDflRICFGCSVREGYGMTETS--CVISAMDDGDNlSGHVGSPNPACeVKLVDvpEMN 488
Cdd:cd05918 210 DPEDVPSLRTLVLGGEALTQSDVD--TWADRVRLINAYGPAECTiaATVSPVVPSTD-PRNIGRPLGAT-CWVVD--PDN 283
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327099 489 YtsdDQPYPR---GEICVRGPIIFKGYYKDEEQTREI-LDGDGWLH------------TGDIGLWLPGGRLKIIDRKKNI 552
Cdd:cd05918 284 H---DRLVPIgavGELLIEGPILARGYLNDPEKTAAAfIEDPAWLKqegsgrgrrlyrTGDLVRYNPDGSLEYVGRKDTQ 360
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*....
gi 22327099 553 FKLaQGEYIAPEKIENVytkcrfVSQCF------------IHGDSFNSSLVAIVSVDPE 599
Cdd:cd05918 361 VKI-RGQRVELGEIEHH------LRQSLpgakevvvevvkPKDGSSSPQLVAFVVLDGS 412
|
|
| PRK07470 |
PRK07470 |
acyl-CoA synthetase; Validated |
114-567 |
3.98e-13 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 180988 [Multi-domain] Cd Length: 528 Bit Score: 72.38 E-value: 3.98e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327099 114 GEYSWmTYGEAASERQAIGSGLLFHGVNQGDCVGLYFINRPEWLVVDHACAAYSFVSVPLYDTLGPDAVKFVVNHANLQA 193
Cdd:PRK07470 29 GDRSW-TWREIDARVDALAAALAARGVRKGDRILVHSRNCNQMFESMFAAFRLGAVWVPTNFRQTPDEVAYLAEASGARA 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327099 194 IFCVPQTLNILLSFLAEIPSIRLIVVVGGADEHLpslprgtgvtivSYQKLLSQGRSSLHPFSPPKPEDIATICYTSGTT 273
Cdd:PRK07470 108 MICHADFPEHAAAVRAASPDLTHVVAIGGARAGL------------DYEALVARHLGARVANAAVDHDDPCWFFFTSGTT 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327099 274 GTPKGVVLTHGNL---IANVAgssveAEFFP----SDVYISYLPLAH---IYeranQIMGVYGGVAVGFYQGDVFKLMDD 343
Cdd:PRK07470 176 GRPKAAVLTHGQMafvITNHL-----ADLMPgtteQDASLVVAPLSHgagIH----QLCQVARGAATVLLPSERFDPAEV 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327099 344 FAVL---RPTIFCSVPRlynriydgITSAVKSSGVVKKRlfeiAYNSKKQAIINGrTPSAFWD-KLVFNKIKEKLggrVR 419
Cdd:PRK07470 247 WALVerhRVTNLFTVPT--------ILKMLVEHPAVDRY----DHSSLRYVIYAG-APMYRADqKRALAKLGKVL---VQ 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327099 420 FMGSGAsplspdvmdflriCFGCsvregygMTETSCVISAMDDGDNLS-GHVGSPNPACEVKLVDvpemnytSDDQPYP- 497
Cdd:PRK07470 311 YFGLGE-------------VTGN-------ITVLPPALHDAEDGPDARiGTCGFERTGMEVQIQD-------DEGRELPp 363
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 22327099 498 --RGEICVRGPIIFKGYYKDEEQTREILDgDGWLHTGDIGLWLPGGRLKIIDRKKNIFkLAQGEYIAPEKIE 567
Cdd:PRK07470 364 geTGEICVIGPAVFAGYYNNPEANAKAFR-DGWFRTGDLGHLDARGFLYITGRASDMY-ISGGSNVYPREIE 433
|
|
| PRK13388 |
PRK13388 |
acyl-CoA synthetase; Provisional |
103-535 |
4.84e-13 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 237374 [Multi-domain] Cd Length: 540 Bit Score: 71.98 E-value: 4.84e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327099 103 LGTRVrSDGTIG------EYSWMTYGEAASERQAIGSGLL-----FHgvnqgdcVGLYFINRPEWLVVDHACAAYSFVSV 171
Cdd:PRK13388 9 LRDRA-GDDTIAvrygdrTWTWREVLAEAAARAAALIALAdpdrpLH-------VGVLLGNTPEMLFWLAAAALGGYVLV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327099 172 PLYDTLGPDAVKFVVNHANLQAIFCVPQTLNiLLSFLaEIPSIRLIVVvggadehlpSLPRgtgvtivsYQKLLsQGRSS 251
Cdd:PRK13388 81 GLNTTRRGAALAADIRRADCQLLVTDAEHRP-LLDGL-DLPGVRVLDV---------DTPA--------YAELV-AAAGA 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327099 252 LHPFSPPKPEDIATICYTSGTTGTPKGVVLTHGNLIanVAGSSVEAEF--FPSDV-YISyLPLAHiyerANQIMGVYgGV 328
Cdd:PRK13388 141 LTPHREVDAMDPFMLIFTSGTTGAPKAVRCSHGRLA--FAGRALTERFglTRDDVcYVS-MPLFH----SNAVMAGW-AP 212
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327099 329 AVGfyQGDVFKLMDDFAVLRptiFCSVPRLYNRIYdgitsavkssgvvkkrlfeIAYNSKKQAIINGrTPSAFWDklvfn 408
Cdd:PRK13388 213 AVA--SGAAVALPAKFSASG---FLDDVRRYGATY-------------------FNYVGKPLAYILA-TPERPDD----- 262
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327099 409 kIKEKLggRVRFmGSGASPlsPDVMDFLRIcFGCSVREGYGMTETSCVISAmdDGDNLSGHVGSPNPAceVKLVDvPEmn 488
Cdd:PRK13388 263 -ADNPL--RVAF-GNEASP--RDIAEFSRR-FGCQVEDGYGSSEGAVIVVR--EPGTPPGSIGRGAPG--VAIYN-PE-- 328
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 22327099 489 yTSDDQPYPR--------------GEICVR-GPIIFKGYYKDEEQTREILDgDGWLHTGDIG 535
Cdd:PRK13388 329 -TLTECAVARfdahgallnadeaiGELVNTaGAGFFEGYYNNPEATAERMR-HGMYWSGDLA 388
|
|
| ttLC_FACS_like |
cd05915 |
Fatty acyl-CoA synthetases similar to LC-FACS from Thermus thermophiles; This family includes ... |
241-569 |
7.76e-13 |
|
Fatty acyl-CoA synthetases similar to LC-FACS from Thermus thermophiles; This family includes fatty acyl-CoA synthetases that can activate medium-chain to long-chain fatty acids. They catalyze the ATP-dependent acylation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. Fatty acyl-CoA synthetases are responsible for fatty acid degradation as well as physiological regulation of cellular functions via the production of fatty acyl-CoA esters. The fatty acyl-CoA synthetase from Thermus thermophiles in this family has been shown to catalyze the long-chain fatty acid, myristoyl acid, while another member in this family, the AlkK protein identified in Pseudomonas oleovorans, targets medium chain fatty acids. This family also includes an uncharacterized subgroup of FACS.
Pssm-ID: 213283 [Multi-domain] Cd Length: 509 Bit Score: 71.31 E-value: 7.76e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327099 241 YQKLLSQGRSSLHPFSPPKPEDIATICYTSGTTGTPKGVVLTH--GNLIANVAGSSVEAEFFPSDVYISYLPLAHIYERA 318
Cdd:cd05915 133 GYLAYEEALGEEADPVRVPERAACGMAYTTGTTGLPKGVVYSHraLVLHSLAASLVDGTALSEKDVVLPVVPMFHVNAWC 212
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327099 319 N-QIMGVYGGVAVGFYQ-GDVFKLMDDFAVLRPTIFCSVPRLYNriydgitsavkssgvvkkrlfeiaynskkqAIINGR 396
Cdd:cd05915 213 LpYAATLVGAKQVLPGPrLDPASLVELFDGEGVTFTAGVPTVWL------------------------------ALADYL 262
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327099 397 tpsafwdklvfNKIKEKLGGRVRFMGSGASPlsPDVMDFLR--------ICFGCSvrEGYGMTeTSCV------ISAMDD 462
Cdd:cd05915 263 -----------ESTGHRLKTLRRLVVGGSAA--PRSLIARFermgvevrQGYGLT--ETSPVV-VQNFvkshleSLSEEE 326
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327099 463 GDNLSGHVGSPNPACEVKLVDVPEMNYTSDDQPYPrgEICVRGPIIFKGYYKDEEQTREILDGDGWLHTGDIGLWLPGGR 542
Cdd:cd05915 327 KLTLKAKTGLPIPLVRLRVADEEGRPVPKDGKALG--EVQLKGPWITGGYYGNEEATRSALTPDGFFRTGDIAVWDEEGY 404
|
330 340
....*....|....*....|....*..
gi 22327099 543 LKIIDRKKNIFKLAqGEYIAPEKIENV 569
Cdd:cd05915 405 VEIKDRLKDLIKSG-GEWISSVDLENA 430
|
|
| PRK07788 |
PRK07788 |
acyl-CoA synthetase; Validated |
119-569 |
9.97e-13 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236097 [Multi-domain] Cd Length: 549 Bit Score: 71.11 E-value: 9.97e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327099 119 MTYGEAASERQAIGSGLLFHGVNQGDCVGLYFINRpEWLVVDHACAAYSFVSVPLYDT-LGPDAVKFVVNHANLQAIFcV 197
Cdd:PRK07788 75 LTYAELDEQSNALARGLLALGVRAGDGVAVLARNH-RGFVLALYAAGKVGARIILLNTgFSGPQLAEVAAREGVKALV-Y 152
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327099 198 PQTLNILLSFLAEiPSIRLIVVVGGADEHLPSLPrgtgvTIVSYQKLLSQGRSSLHPfSPPKPEDIatICYTSGTTGTPK 277
Cdd:PRK07788 153 DDEFTDLLSALPP-DLGRLRAWGGNPDDDEPSGS-----TDETLDDLIAGSSTAPLP-KPPKPGGI--VILTSGTTGTPK 223
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327099 278 GVVLTHGNLIANVAGssveaeffpsdvYISYLPLahiyeRANQIMGV---------YGGVAVGFYQG---------DVFK 339
Cdd:PRK07788 224 GAPRPEPSPLAPLAG------------LLSRVPF-----RAGETTLLpapmfhatgWAHLTLAMALGstvvlrrrfDPEA 286
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327099 340 LMDDFAVLRPTIFCSVPrlynriydgitsavkssgVVKKRLFEIAynskkQAIINGRTPSAfwdklvfnkikeklggrVR 419
Cdd:PRK07788 287 TLEDIAKHKATALVVVP------------------VMLSRILDLG-----PEVLAKYDTSS-----------------LK 326
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327099 420 FMGSGASPLSPDVMDFLRICFGCSVREGYGMTETS-CVISAMDDGDNLSGHVGSPNPACEVKLVDvpemnytSDDQPYPR 498
Cdd:PRK07788 327 IIFVSGSALSPELATRALEAFGPVLYNLYGSTEVAfATIATPEDLAEAPGTVGRPPKGVTVKILD-------ENGNEVPR 399
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 22327099 499 GE---ICVRGPIIFKGYYKDeeQTREILDGdgWLHTGDIGLWLPGGRLKIIDRKKNIFkLAQGEYIAPEKIENV 569
Cdd:PRK07788 400 GVvgrIFVGNGFPFEGYTDG--RDKQIIDG--LLSSGDVGYFDEDGLLFVDGRDDDMI-VSGGENVFPAEVEDL 468
|
|
| MACS_euk |
cd05928 |
Eukaryotic Medium-chain acyl-CoA synthetase (MACS or ACSM); MACS catalyzes the two-step ... |
139-568 |
2.34e-12 |
|
Eukaryotic Medium-chain acyl-CoA synthetase (MACS or ACSM); MACS catalyzes the two-step activation of medium chain fatty acids (containing 4-12 carbons). The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. The acyl-CoA is a key intermediate in many important biosynthetic and catabolic processes. MACS enzymes are localized to mitochondria. Two murine MACS family proteins are found in liver and kidney. In rodents, a MACS member is detected particularly in the olfactory epithelium and is called O-MACS. O-MACS demonstrates substrate preference for the fatty acid lengths of C6-C12.
Pssm-ID: 341251 [Multi-domain] Cd Length: 530 Bit Score: 69.80 E-value: 2.34e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327099 139 GVNQGDCVGLYFINRPEWLVVDHACAAYSFVSVPLYDTLGPDAVKFVVNHANLQAIFCVPQTLNILLSFLAEIPSIRLIV 218
Cdd:cd05928 63 GLQRGDRVAVILPRVPEWWLVNVACIRTGLVFIPGTIQLTAKDILYRLQASKAKCIVTSDELAPEVDSVASECPSLKTKL 142
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327099 219 VVGgadehlPSLPRGTGvtivSYQKLLsQGRSSLHPFSPPKPEDIATICYTSGTTGTPKGVVLTHGNLIAnvaGSSVEAE 298
Cdd:cd05928 143 LVS------EKSRDGWL----NFKELL-NEASTEHHCVETGSQEPMAIYFTSGTTGSPKMAEHSHSSLGL---GLKVNGR 208
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327099 299 FF----PSDVYISYLPLAHIYERANQIMGVYGGVAVGFY----QGDVFKLMDDFAVLRPTIFCSVPRLYNRIydgitsav 370
Cdd:cd05928 209 YWldltASDIMWNTSDTGWIKSAWSSLFEPWIQGACVFVhhlpRFDPLVILKTLSSYPITTFCGAPTVYRML-------- 280
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327099 371 kssgvVKKRLFEIAYNSKKQAIingrtpsafwdklvfnkikeklggrvrfmgSGASPLSPDVMDFLRICFGCSVREGYGM 450
Cdd:cd05928 281 -----VQQDLSSYKFPSLQHCV------------------------------TGGEPLNPEVLEKWKAQTGLDIYEGYGQ 325
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327099 451 TETScVISAMDDGDNL-SGHVGSPNPACEVKLVD-----VPemnytsddqPYPRGEICVR-GPI----IFKGYYKDEEQT 519
Cdd:cd05928 326 TETG-LICANFKGMKIkPGSMGKASPPYDVQIIDdngnvLP---------PGTEGDIGIRvKPIrpfgLFSGYVDNPEKT 395
|
410 420 430 440
....*....|....*....|....*....|....*....|....*....
gi 22327099 520 REILDGDGWLhTGDIGLWLPGGRLKIIDRKKNIFkLAQGEYIAPEKIEN 568
Cdd:cd05928 396 AATIRGDFYL-TGDRGIMDEDGYFWFMGRADDVI-NSSGYRIGPFEVES 442
|
|
| PRK04319 |
PRK04319 |
acetyl-CoA synthetase; Provisional |
120-533 |
3.17e-12 |
|
acetyl-CoA synthetase; Provisional
Pssm-ID: 235279 [Multi-domain] Cd Length: 570 Bit Score: 69.54 E-value: 3.17e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327099 120 TYGEAASERQAIGSGLLFHGVNQGDCVGLYFINRPEWLVVDHACAAYSFVSVPLYDTLGPDAVKFVVNHANLQAIFcvpq 199
Cdd:PRK04319 75 TYKELKELSNKFANVLKELGVEKGDRVFIFMPRIPELYFALLGALKNGAIVGPLFEAFMEEAVRDRLEDSEAKVLI---- 150
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327099 200 TLNILLSFL--AEIPSIRLIVVVGGADEHLPslprgtgvTIVSYQKLLSQGRSSLhPFSPPKPEDIATICYTSGTTGTPK 277
Cdd:PRK04319 151 TTPALLERKpaDDLPSLKHVLLVGEDVEEGP--------GTLDFNALMEQASDEF-DIEWTDREDGAILHYTSGSTGKPK 221
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327099 278 GVVLTHGNLIANVAGSSVEAEFFPSDVY-----------ISY---LPLAHiyeRANQImgVYGGvavGFYQGDVFKLMDD 343
Cdd:PRK04319 222 GVLHVHNAMLQHYQTGKYVLDLHEDDVYwctadpgwvtgTSYgifAPWLN---GATNV--IDGG---RFSPERWYRILED 293
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327099 344 FAVlrpTIFCSVP---RLYNRIYDgitsavkssGVVKKrlfeiaYNSKkqaiingrtpsafwdklvfnkikeklggRVRF 420
Cdd:PRK04319 294 YKV---TVWYTAPtaiRMLMGAGD---------DLVKK------YDLS----------------------------SLRH 327
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327099 421 MGSGASPLSPDVMDFLRICFGCSVREGYGMTETSC-VIS---AMDDGdnlSGHVGSPNPACEVKLVDvpemNYTSDDQPY 496
Cdd:PRK04319 328 ILSVGEPLNPEVVRWGMKVFGLPIHDNWWMTETGGiMIAnypAMDIK---PGSMGKPLPGIEAAIVD----DQGNELPPN 400
|
410 420 430
....*....|....*....|....*....|....*....
gi 22327099 497 PRGEICVRG--PIIFKGYYKDEEQTREILDGdGWLHTGD 533
Cdd:PRK04319 401 RMGNLAIKKgwPSMMRGIWNNPEKYESYFAG-DWYVSGD 438
|
|
| A_NRPS_VisG_like |
cd17651 |
similar to adenylation domain of virginiamycin S synthetase; This family of the adenylation (A) ... |
120-567 |
5.04e-12 |
|
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: 68.91 E-value: 5.04e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327099 120 TYGEAASERQAIGSGLLFHGVNQGDCVGLYFINRPEWLV----VDHACAAYsfvsVPLyDTLGPDA-VKFVVNHANLqai 194
Cdd:cd17651 22 TYAELDRRANRLAHRLRARGVGPGDLVALCARRSAELVVallaILKAGAAY----VPL-DPAYPAErLAFMLADAGP--- 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327099 195 fcvpqtlnillsflaeipsirliVVVGGADEHLPSLP-RGTGVTIVSYQKLLSQGRSSlhPFSPPKPEDIATICYTSGTT 273
Cdd:cd17651 94 -----------------------VLVLTHPALAGELAvELVAVTLLDQPGAAAGADAE--PDPALDADDLAYVIYTSGST 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327099 274 GTPKGVVLTHGNLIANVAGSSVEAEFFPSDvyisylplahiyeRANQIMGvyggvaVGFyqgdvfklmdDFAVLRptIFc 353
Cdd:cd17651 149 GRPKGVVMPHRSLANLVAWQARASSLGPGA-------------RTLQFAG------LGF----------DVSVQE--IF- 196
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327099 354 svprlynriydgitSAVKSSGVVKKRLFEIaynskkqaiinGRTPSAFWDKLVFNKIKE-------------------KL 414
Cdd:cd17651 197 --------------STLCAGATLVLPPEEV-----------RTDPPALAAWLDEQRISRvflptvalralaehgrplgVR 251
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327099 415 GGRVRFMGSGASPLS--PDVMDFLRICFGCSVREGYGMTETSCVISAMDDGDN----LSGHVGSPNPACEVKLVDvpemn 488
Cdd:cd17651 252 LAALRYLLTGGEQLVltEDLREFCAGLPGLRLHNHYGPTETHVVTALSLPGDPaawpAPPPIGRPIDNTRVYVLD----- 326
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327099 489 ytSDDQPYPR---GEICVRGPIIFKGYYKDEEQTREILDGDGWL------HTGDIGLWLPGGRLKIIDRKKNIFKLaQGE 559
Cdd:cd17651 327 --AALRPVPPgvpGELYIGGAGLARGYLNRPELTAERFVPDPFVpgarmyRTGDLARWLPDGELEFLGRADDQVKI-RGF 403
|
....*...
gi 22327099 560 YIAPEKIE 567
Cdd:cd17651 404 RIELGEIE 411
|
|
| PtmA |
cd17636 |
long-chain fatty acid CoA ligase (FadD); This family contains fatty acid CoA ligases, ... |
447-598 |
5.22e-12 |
|
long-chain fatty acid CoA ligase (FadD); This family contains fatty acid CoA ligases, including acyl-CoA synthetase (AMP-forming)/AMP-acid ligase II, most of which are yet to be characterized. Fatty acyl-CoA ligases catalyze the ATP-dependent activation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions.
Pssm-ID: 341291 [Multi-domain] Cd Length: 331 Bit Score: 67.71 E-value: 5.22e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327099 447 GYGMTETS--CVISAMDdGDNLSGHvGSPNPACEVKLVDvpemnytSDDQPYPRG---EICVRGPIIFKGYY-KDEEQTR 520
Cdd:cd17636 142 GYGQTEVMglATFAALG-GGAIGGA-GRPSPLVQVRILD-------EDGREVPDGevgEIVARGPTVMAGYWnRPEVNAR 212
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327099 521 EIldGDGWLHTGDIGLWLPGGRLKIIDRKKNIFKLAqGEYIAPEKIENVYTKCRFVSQCFIHG---DSFNSSLVAIVSVD 597
Cdd:cd17636 213 RT--RGGWHHTNDLGRREPDGSLSFVGPKTRMIKSG-AENIYPAEVERCLRQHPAVADAAVIGvpdPRWAQSVKAIVVLK 289
|
.
gi 22327099 598 P 598
Cdd:cd17636 290 P 290
|
|
| A_NRPS_PpsD_like |
cd17650 |
similar to adenylation domain of plipastatin synthase (PpsD); This family of the adenylation ... |
260-606 |
9.08e-12 |
|
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: 67.88 E-value: 9.08e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327099 260 PEDIATICYTSGTTGTPKGVVLTHGNLIANVAGSSVEAEffpsdvyISYLPLAHIyERANQIMGVYGG-VAVGFYQGDVF 338
Cdd:cd17650 92 PEDLAYVIYTSGTTGKPKGVMVEHRNVAHAAHAWRREYE-------LDSFPVRLL-QMASFSFDVFAGdFARSLLNGGTL 163
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327099 339 KLMDDFAVLRPtifcsvprlyNRIYD-----GITSAVKSSGVVKKRLFEIAYnskkqaiiNGRTPSAFwdklvfnkikek 413
Cdd:cd17650 164 VICPDEVKLDP----------AALYDlilksRITLMESTPALIRPVMAYVYR--------NGLDLSAM------------ 213
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327099 414 lggRVRFMGSGASPLSPDVMDFLRICFGCSVREGYGMTET---SCVISAMDDGDNLSGHV--GSPNPACEVKLVDvpemn 488
Cdd:cd17650 214 ---RLLIVGSDGCKAQDFKTLAARFGQGMRIINSYGVTEAtidSTYYEEGRDPLGDSANVpiGRPLPNTAMYVLD----- 285
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327099 489 ytSDDQPYP---RGEICVRGPIIFKGYYKDEEQTRE------ILDGDGWLHTGDIGLWLPGGRLKIIDRKKNIFKLaQGE 559
Cdd:cd17650 286 --ERLQPQPvgvAGELYIGGAGVARGYLNRPELTAErfvenpFAPGERMYRTGDLARWRADGNVELLGRVDHQVKI-RGF 362
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|
gi 22327099 560 YIAPEKIENVYTKCRFVSQCFI---HGDSFNSSLVAIVSVDPEVmkDWAA 606
Cdd:cd17650 363 RIELGEIESQLARHPAIDEAVVavrEDKGGEARLCAYVVAAATL--NTAE 410
|
|
| PRK13391 |
PRK13391 |
acyl-CoA synthetase; Provisional |
120-569 |
2.27e-11 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 184022 [Multi-domain] Cd Length: 511 Bit Score: 66.64 E-value: 2.27e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327099 120 TYGE--AASERQAigsgLLF--HGVNQGDCVGLYFINRPEWLVVDHACAAYSFVSVPLYDTLGPDAVKFVVNHANLQAIF 195
Cdd:PRK13391 26 TYREldERSNRLA----HLFrsLGLKRGDHVAIFMENNLRYLEVCWAAERSGLYYTCVNSHLTPAEAAYIVDDSGARALI 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327099 196 CVPQTLNILLSFLAEIPSIRLIVVVGGADEhlpsLPRgtgvtIVSYQKLLSQgrsslHPFSPPKPEDIAT-ICYTSGTTG 274
Cdd:PRK13391 102 TSAAKLDVARALLKQCPGVRHRLVLDGDGE----LEG-----FVGYAEAVAG-----LPATPIADESLGTdMLYSSGTTG 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327099 275 TPKGVV--LTHGNLianVAGSSVEAEF-----FPSD-VYISYLPLAHIY-ERANQIMGVYGGVAV---GFYQGDVFKLMD 342
Cdd:PRK13391 168 RPKGIKrpLPEQPP---DTPLPLTAFLqrlwgFRSDmVYLSPAPLYHSApQRAVMLVIRLGGTVIvmeHFDAEQYLALIE 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327099 343 DFAV----LRPTIFCSVPRLYNRI---YDgitsavkssgvvkkrlfeiaYNSKKQAIingrtpsafwdklvfnkikeklg 415
Cdd:PRK13391 245 EYGVthtqLVPTMFSRMLKLPEEVrdkYD--------------------LSSLEVAI----------------------- 281
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327099 416 grvrfmgSGASPLSPDVMDFLRICFGCSVREGYGMTETSCViSAMDDGDNLS--GHVGSPnpacevkLVDVPEMnytSDD 493
Cdd:PRK13391 282 -------HAAAPCPPQVKEQMIDWWGPIIHEYYAATEGLGF-TACDSEEWLAhpGTVGRA-------MFGDLHI---LDD 343
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327099 494 --QPYPRGEIcvrGPIIFKG-----YYKDEEQTREILDGDG-WLHTGDIGLWLPGGRLKIIDRKKNIFkLAQGEYIAPEK 565
Cdd:PRK13391 344 dgAELPPGEP---GTIWFEGgrpfeYLNDPAKTAEARHPDGtWSTVGDIGYVDEDGYLYLTDRAAFMI-ISGGVNIYPQE 419
|
....
gi 22327099 566 IENV 569
Cdd:PRK13391 420 AENL 423
|
|
| A_NRPS_ProA |
cd17656 |
gramicidin S synthase 2, also known as ATP-dependent proline adenylase; This family of the ... |
226-612 |
7.13e-11 |
|
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: 65.19 E-value: 7.13e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327099 226 HLPSLPRGTGVTIVSYQKLLSQGRSSLHPFSPpKPEDIATICYTSGTTGTPKGVVLTHGNlIANVagssveaeffpsdvy 305
Cdd:cd17656 94 HLKSKLSFNKSTILLEDPSISQEDTSNIDYIN-NSDDLLYIIYTSGTTGKPKGVQLEHKN-MVNL--------------- 156
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327099 306 isylpLAHIYERANQIMGvyggvavgfyqGDVFKlmddFAVlrptifCSvprlYNRIYDGITSAVKSSGVVK-------- 377
Cdd:cd17656 157 -----LHFEREKTNINFS-----------DKVLQ----FAT------CS----FDVCYQEIFSTLLSGGTLYiireetkr 206
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327099 378 --KRLFEIAYNSKKQAIIngrTPSAFWdKLVFN--KIKEKLGGRVRFMGSGASPLSpdVMDFLRICF---GCSVREGYGM 450
Cdd:cd17656 207 dvEQLFDLVKRHNIEVVF---LPVAFL-KFIFSerEFINRFPTCVKHIITAGEQLV--ITNEFKEMLhehNVHLHNHYGP 280
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327099 451 TE----TSCVISAMDDGDNLSGhVGSPNPACEVKLVDvpemnytSDDQPYPRG---EICVRGPIIFKGYYKDEEQTREIL 523
Cdd:cd17656 281 SEthvvTTYTINPEAEIPELPP-IGKPISNTWIYILD-------QEQQLQPQGivgELYISGASVARGYLNRQELTAEKF 352
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327099 524 DGDGW------LHTGDIGLWLPGGRLKIIDRKKNIFKLaQGEYIAPEKIENVYTKCRFVSQCfihgdsfnsslvaivsvd 597
Cdd:cd17656 353 FPDPFdpnermYRTGDLARYLPDGNIEFLGRADHQVKI-RGYRIELGEIEAQLLNHPGVSEA------------------ 413
|
410
....*....|....*
gi 22327099 598 peVMKDWAASEGIKY 612
Cdd:cd17656 414 --VVLDKADDKGEKY 426
|
|
| A_NRPS_AB3403-like |
cd17646 |
Peptide Synthetase; The adenylation (A) domain of NRPS recognizes a specific amino acid or ... |
218-578 |
7.21e-11 |
|
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: 64.99 E-value: 7.21e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327099 218 VVVGGADEhLPSLPRGTGVTIVSYQKLLSqgRSSLHPFSPPKPEDIATICYTSGTTGTPKGVVLTHGNLIANVAGSSVEA 297
Cdd:cd17646 98 VVLTTADL-AARLPAGGDVALLGDEALAA--PPATPPLVPPRPDNLAYVIYTSGSTGRPKGVMVTHAGIVNRLLWMQDEY 174
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327099 298 EFFPSDVYISYLPLA---HIYER-------ANQIMGVYGGVAVGFYqgdVFKLMDDFAVlrpTIFCSVPrlynriydgit 367
Cdd:cd17646 175 PLGPGDRVLQKTPLSfdvSVWELfwplvagARLVVARPGGHRDPAY---LAALIREHGV---TTCHFVP----------- 237
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327099 368 savkssgvvkkrlfeiaynSKKQAIINGRTPSAfwdklvfnkikeklGGRVRFMGSGASPLSPDVMDFLRICFGCSVREG 447
Cdd:cd17646 238 -------------------SMLRVFLAEPAAGS--------------CASLRRVFCSGEALPPELAARFLALPGAELHNL 284
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327099 448 YGMTETS-----CVISAMDDGDNLSghVGSPNPACEVKLVDvPEMNytsddqPYPR---GEICVRGPIIFKGYYKDEEQT 519
Cdd:cd17646 285 YGPTEAAidvthWPVRGPAETPSVP--IGRPVPNTRLYVLD-DALR------PVPVgvpGELYLGGVQLARGYLGRPALT 355
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 22327099 520 REIL------DGDGWLHTGDIGLWLPGGRLKIIDRKKNIFKLaQGEYIAPEKIENVYTKCRFVSQ 578
Cdd:cd17646 356 AERFvpdpfgPGSRMYRTGDLARWRPDGALEFLGRSDDQVKI-RGFRVEPGEIEAALAAHPAVTH 419
|
|
| FACL_like_1 |
cd05910 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
258-549 |
1.16e-10 |
|
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ATP-dependent activation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions.
Pssm-ID: 341236 [Multi-domain] Cd Length: 457 Bit Score: 64.40 E-value: 1.16e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327099 258 PKPEDIATICYTSGTTGTPKGVVLTHGNLIANVAGSSVEAEFFPSDVYISYLPLAHIYeraNQIMGVyggvavgfyqGDV 337
Cdd:cd05910 82 PKADEPAAILFTSGSTGTPKGVVYRHGTFAAQIDALRQLYGIRPGEVDLATFPLFALF---GPALGL----------TSV 148
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327099 338 FKLMDDfavLRPtIFCSVPRLYNRIYD-GITSAVKSSGVVKKrlfeIAynskKQAIINGRT-PSafwdklvfnkikeklg 415
Cdd:cd05910 149 IPDMDP---TRP-ARADPQKLVGAIRQyGVSIVFGSPALLER----VA----RYCAQHGITlPS---------------- 200
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327099 416 grVRFMGSGASPLSPDVMDFLR--ICFGCSVREGYGMTEtSCVISAMDDGDNLSGH-----------VGSPNPACEVKLV 482
Cdd:cd05910 201 --LRRVLSAGAPVPIALAARLRkmLSDEAEILTPYGATE-ALPVSSIGSRELLATTtaatsggagtcVGRPIPGVRVRII 277
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 22327099 483 -----DVPEMNYTSDDQPYPRGEICVRGPIIFKGYYKDEEQTR--EILDGDG--WLHTGDIGLWLPGGRLKIIDRK 549
Cdd:cd05910 278 eiddePIAEWDDTLELPRGEIGEITVTGPTVTPTYVNRPVATAlaKIDDNSEgfWHRMGDLGYLDDEGRLWFCGRK 353
|
|
| A_NRPS_TlmIV_like |
cd12114 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including ... |
119-569 |
1.53e-10 |
|
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: 63.83 E-value: 1.53e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327099 119 MTYGEAASERQAIGSGLLFHGVNQGDCVGLYFINRPEWLV----VDHACAAYsfvsVPLydtlGPDAVKfvvnhANLQAI 194
Cdd:cd12114 13 LTYGELAERARRVAGALKAAGVRPGDLVAVTLPKGPEQVVavlgILAAGAAY----VPV----DIDQPA-----ARREAI 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327099 195 FcvpqtlnillsflaEIPSIRLIVVVGGADEHLPSLPRgtgVTIVSyqkLLSQGRSSLHPFSPPKPEDIATICYTSGTTG 274
Cdd:cd12114 80 L--------------ADAGARLVLTDGPDAQLDVAVFD---VLILD---LDALAAPAPPPPVDVAPDDLAYVIFTSGSTG 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327099 275 TPKGVVLTHGNLIANVAgsSVEAEFF--PSDVYISYLPLAH---IYEranqimgVYGGVAVG--------FYQGDVF--- 338
Cdd:cd12114 140 TPKGVMISHRAALNTIL--DINRRFAvgPDDRVLALSSLSFdlsVYD-------IFGALSAGatlvlpdeARRRDPAhwa 210
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327099 339 KLMDDFAVlrpTIFCSVPRLYNRIYDGITSAvkssgvvkkrlfEIAYNSKKQAIINGRtpsafWdklvfnkIKEKLGGRV 418
Cdd:cd12114 211 ELIERHGV---TLWNSVPALLEMLLDVLEAA------------QALLPSLRLVLLSGD-----W-------IPLDLPARL 263
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327099 419 RfmgsgasplspdvmdflRICFGCSVREGYGMTETS-----CVISAMDDgdnlsgHVGS-------PNPACEVklVDvpe 486
Cdd:cd12114 264 R-----------------ALAPDARLISLGGATEASiwsiyHPIDEVPP------DWRSipygrplANQRYRV--LD--- 315
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327099 487 mnytSDDQPYP---RGEICVRGPIIFKGYYKDEEQTRE----ILDGDGWLHTGDIGLWLPGGRLKIIDRKKNIFKLaQGE 559
Cdd:cd12114 316 ----PRGRDCPdwvPGELWIGGRGVALGYLGDPELTAArfvtHPDGERLYRTGDLGRYRPDGTLEFLGRRDGQVKV-RGY 390
|
490
....*....|
gi 22327099 560 YIAPEKIENV 569
Cdd:cd12114 391 RIELGEIEAA 400
|
|
| A_NRPS_Sfm_like |
cd12115 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including Saframycin A gene ... |
260-599 |
3.34e-10 |
|
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: 62.72 E-value: 3.34e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327099 260 PEDIATICYTSGTTGTPKGVVLTHGNLIANVAGSsveAEFFPSDvyisylplahiyeranQIMGVYGGVAVGFyqgD--V 337
Cdd:cd12115 104 PDDLAYVIYTSGSTGRPKGVAIEHRNAAAFLQWA---AAAFSAE----------------ELAGVLASTSICF---DlsV 161
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327099 338 FKLmddFAVLrpTIFCSVprlynriydgitsaVKSSGVVKKRLFEIAynsKKQAIINgRTPSAFWDKLVFNKIKEKlggr 417
Cdd:cd12115 162 FEL---FGPL--ATGGKV--------------VLADNVLALPDLPAA---AEVTLIN-TVPSAAAELLRHDALPAS---- 214
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327099 418 VRFMGSGASPLSPDVMDFL-RICFGCSVREGYGMTE-----TSCVISAMDDGDNlsgHVGSPNPACEVKLVDvpemnytS 491
Cdd:cd12115 215 VRVVNLAGEPLPRDLVQRLyARLQVERVVNLYGPSEdttysTVAPVPPGASGEV---SIGRPLANTQAYVLD-------R 284
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327099 492 DDQPYP---RGEICVRGPIIFKGYYKDEEQTRE------ILDGDGWLHTGDIGLWLPGGRLKIIDRKKNIFKLaQGEYIA 562
Cdd:cd12115 285 ALQPVPlgvPGELYIGGAGVARGYLGRPGLTAErflpdpFGPGARLYRTGDLVRWRPDGLLEFLGRADNQVKV-RGFRIE 363
|
330 340 350 360
....*....|....*....|....*....|....*....|
gi 22327099 563 PEKIENVYTKCRFVSQCFI--HGDSFNS-SLVAIVSVDPE 599
Cdd:cd12115 364 LGEIEAALRSIPGVREAVVvaIGDAAGErRLVAYIVAEPG 403
|
|
| A_NRPS_PvdJ-like |
cd17649 |
non-ribosomal peptide synthetase; This family of the adenylation (A) domain of nonribosomal ... |
260-567 |
5.95e-10 |
|
non-ribosomal peptide synthetase; This family of the adenylation (A) domain of nonribosomal peptide synthases (NRPS) includes pyoverdine biosynthesis protein PvdJ involved in the synthesis of pyoverdine, which consists of a chromophore group attached to a variable peptide chain and comprises around 6-12 amino acids that are specific for each Pseudomonas species, and for which the peptide might be first synthesized before the chromophore assembly. Also included is ornibactin biosynthesis protein OrbI; ornibactin is a tetrapeptide siderophore with an l-ornithine-d-hydroxyaspartate-l-serine-l-ornithine backbone. The adenylation domain at the N-terminal of OrbI possibly initiates the ornibactin with the binding of N5-hydroxyornithine. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.
Pssm-ID: 341304 [Multi-domain] Cd Length: 450 Bit Score: 62.00 E-value: 5.95e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327099 260 PEDIATICYTSGTTGTPKGVVLTHGNLIANVAGSSVEAEFFPSDVYISYLPL----AHiyERanqimgVYGGVAVGfyqG 335
Cdd:cd17649 93 PRQLAYVIYTSGSTGTPKGVAVSHGPLAAHCQATAERYGLTPGDRELQFASFnfdgAH--EQ------LLPPLICG---A 161
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327099 336 DVfklmddfaVLRP-TIFCSVPRLYNRIydgitsavkssgvvkkrlfeiaynsKKQAIINGRTPSAFWDKLV--FNKIKE 412
Cdd:cd17649 162 CV--------VLRPdELWASADELAEMV-------------------------RELGVTVLDLPPAYLQQLAeeADRTGD 208
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327099 413 KLGGRVRFMGSGASPLSPdvmDFLRICFGCSVR--EGYGMTETscVISAM---------DDGDNLSghVGSPNPACEVKL 481
Cdd:cd17649 209 GRPPSLRLYIFGGEALSP---ELLRRWLKAPVRlfNAYGPTEA--TVTPLvwkceagaaRAGASMP--IGRPLGGRSAYI 281
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327099 482 VDvPEMNYTSDDQPyprGEICVRGPIIFKGYYKDEEQTRE--ILDGDG-----WLHTGDIGLWLPGGRLKIIDRKKNIFK 554
Cdd:cd17649 282 LD-ADLNPVPVGVT---GELYIGGEGLARGYLGRPELTAErfVPDPFGapgsrLYRTGDLARWRDDGVIEYLGRVDHQVK 357
|
330
....*....|...
gi 22327099 555 LaQGEYIAPEKIE 567
Cdd:cd17649 358 I-RGFRIELGEIE 369
|
|
| PRK13382 |
PRK13382 |
bile acid CoA ligase; |
257-639 |
1.00e-09 |
|
bile acid CoA ligase;
Pssm-ID: 172019 [Multi-domain] Cd Length: 537 Bit Score: 61.70 E-value: 1.00e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327099 257 PPKPEDIATICYTSGTTGTPKGV----VLTHGNLIANVAGSSVEAEffpSDVYISyLPLAHIYERAN-QIMGVYGGVAV- 330
Cdd:PRK13382 192 EPTGRKGRVILLTSGTTGTPKGArrsgPGGIGTLKAILDRTPWRAE---EPTVIV-APMFHAWGFSQlVLAASLACTIVt 267
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327099 331 --GFYQGDVFKLMDDFavlRPTIFCSVPRLYNRIYDGITSavkssgvvkkrlfeiaynskkqaiingrtpsafwdklVFN 408
Cdd:PRK13382 268 rrRFDPEATLDLIDRH---RATGLAVVPVMFDRIMDLPAE-------------------------------------VRN 307
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327099 409 KIKeklGGRVRFMGSGASPLSPDVMDFLRICFGCSVREGYGMTETSCVISAMDDgdNLSGH---VGSPNPACEVKLVDvp 485
Cdd:PRK13382 308 RYS---GRSLRFAAASGSRMRPDVVIAFMDQFGDVIYNNYNATEAGMIATATPA--DLRAApdtAGRPAEGTEIRILD-- 380
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327099 486 emnytSDDQPYPRGE---ICVRGPIIFKGYYKDeeQTREILDGdgWLHTGDIGLWLPGGRLKIIDRKKNIFkLAQGEYIA 562
Cdd:PRK13382 381 -----QDFREVPTGEvgtIFVRNDTQFDGYTSG--STKDFHDG--FMASGDVGYLDENGRLFVVGRDDEMI-VSGGENVY 450
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327099 563 PEKIENVYTKCRFVSQCFIHG---DSFNSSLVAIVSVDPEVMkdwAASEGIKYEHLGQLCNDPRVRKTVLaeMDDLGREA 639
Cdd:PRK13382 451 PIEVEKTLATHPDVAEAAVIGvddEQYGQRLAAFVVLKPGAS---ATPETLKQHVRDNLANYKVPRDIVV--LDELPRGA 525
|
|
| PRK07445 |
PRK07445 |
O-succinylbenzoic acid--CoA ligase; Reviewed |
385-569 |
1.15e-09 |
|
O-succinylbenzoic acid--CoA ligase; Reviewed
Pssm-ID: 236019 [Multi-domain] Cd Length: 452 Bit Score: 61.16 E-value: 1.15e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327099 385 YNSKKQAIINGRTPSAFWDKLVFNKIKEKLGGRVRFMGS------GASPLSPDVMD---FLRICFGCSvregYGMTETSC 455
Cdd:PRK07445 193 YKRLKSGQELPPNPSDFFLSLVPTQLQRLLQLRPQWLAQfrtillGGAPAWPSLLEqarQLQLRLAPT----YGMTETAS 268
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327099 456 VISAMDDGDNLSG--HVGSPNPACEVKLVdvpemnytsddqPYPRGEICVRGPIIFKGYYKdeeqtrEILDGDGWLHTGD 533
Cdd:PRK07445 269 QIATLKPDDFLAGnnSSGQVLPHAQITIP------------ANQTGNITIQAQSLALGYYP------QILDSQGIFETDD 330
|
170 180 190
....*....|....*....|....*....|....*.
gi 22327099 534 IGLWLPGGRLKIIDRKKNIFkLAQGEYIAPEKIENV 569
Cdd:PRK07445 331 LGYLDAQGYLHILGRNSQKI-ITGGENVYPAEVEAA 365
|
|
| FATP_chFAT1_like |
cd05937 |
Uncharacterized subfamily of bifunctional fatty acid transporter/very-long-chain acyl-CoA ... |
138-571 |
2.32e-09 |
|
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: 60.14 E-value: 2.32e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327099 138 HGVNQGDCVGLYFINRPEwlvvdhacaaysfvsvplydtlgpdavkFVVNHANLQAIFCVPQTLNILLSFLAEIPSIRLi 217
Cdd:cd05937 26 LGVQAGDFVAIDLTNSPE----------------------------FVFLWLGLWSIGAAPAFINYNLSGDPLIHCLKL- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327099 218 vvvggadehlpslprgTGVTIVSYQkllsqgrsslhpfsppkPEDIATICYTSGTTGTPKGVV------LTHGNLIANVA 291
Cdd:cd05937 77 ----------------SGSRFVIVD-----------------PDDPAILIYTSGTTGLPKAAAiswrrtLVTSNLLSHDL 123
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327099 292 GSSveaefFPSDVYiSYLPLAHiyeranqimgvyggvAVGFYQGDVFKLMDDFAV-LRPTIfcSVPRLYNRIYDGITSAV 370
Cdd:cd05937 124 NLK-----NGDRTY-TCMPLYH---------------GTAAFLGACNCLMSGGTLaLSRKF--SASQFWKDVRDSGATII 180
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327099 371 KSSGVVKKRLFEiaynskkqaiingrTPSAFWDKLvfnkikeklgGRVRFM-GSGaspLSPDVMDFLRICFGCS-VREGY 448
Cdd:cd05937 181 QYVGELCRYLLS--------------TPPSPYDRD----------HKVRVAwGNG---LRPDIWERFRERFNVPeIGEFY 233
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327099 449 GMTETscvISAMDD---GDNLSGHVGSPNPACEVKLVD--VPEMNYTSDDQPY--PRGEICVRGPI-------------- 507
Cdd:cd05937 234 AATEG---VFALTNhnvGDFGAGAIGHHGLIRRWKFENqvVLVKMDPETDDPIrdPKTGFCVRAPVgepgemlgrvpfkn 310
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 22327099 508 --IFKGYYKDEEQT-----REILD-GDGWLHTGDIGLWLPGGRLKIIDRKKNIFKLaqgeyiapeKIENVYT 571
Cdd:cd05937 311 reAFQGYLHNEDATesklvRDVFRkGDIYFRTGDLLRQDADGRWYFLDRLGDTFRW---------KSENVST 373
|
|
| PRK12467 |
PRK12467 |
peptide synthase; Provisional |
205-312 |
3.02e-09 |
|
peptide synthase; Provisional
Pssm-ID: 237108 [Multi-domain] Cd Length: 3956 Bit Score: 60.95 E-value: 3.02e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327099 205 LSFLAEIPSIRLIVvvggADEH-LPSLPRGTGVTIVSYQKL--LSQGRSSLHPFSPPKPEDIATICYTSGTTGTPKGVVL 281
Cdd:PRK12467 601 LAYMLDDSGVRLLL----TQSHlLAQLPVPAGLRSLCLDEPadLLCGYSGHNPEVALDPDNLAYVIYTSGSTGQPKGVAI 676
|
90 100 110
....*....|....*....|....*....|.
gi 22327099 282 THGNLIANVAGSSVEAEFFPSDVYISYLPLA 312
Cdd:PRK12467 677 SHGALANYVCVIAERLQLAADDSMLMVSTFA 707
|
|
| A_NRPS_ApnA-like |
cd17644 |
similar to adenylation domain of anabaenopeptin synthetase (ApnA); This family of the ... |
196-672 |
3.20e-09 |
|
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: 59.76 E-value: 3.20e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327099 196 CVPQTLNILLSFLAeipsirlIVVVGGADEHL-PSLPRGTGVTIVS---YQKLLSQgrsslhpfsppkPEDIATICYTSG 271
Cdd:cd17644 56 CVERSLEMIIGLLA-------ILKAGGAYVPLdPNYPQERLTYILEdaqISVLLTQ------------PENLAYVIYTSG 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327099 272 TTGTPKGVVLTHGNLIaNVAGSSVEAEFFPSDVYISYLplahiyeranqimgvyggVAVGFyqgDVfklmddfavlrpti 351
Cdd:cd17644 117 STGKPKGVMIEHQSLV-NLSHGLIKEYGITSSDRVLQF------------------ASIAF---DV-------------- 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327099 352 fcSVPRLYNRIYDGITSAVKSSGVVKKRLFEIAYNSKKQ-AIINgrTPSAFWDKLVFNKIKEKLGG--RVRFMGSGASPL 428
Cdd:cd17644 161 --AAEEIYVTLLSGATLVLRPEEMRSSLEDFVQYIQQWQlTVLS--LPPAYWHLLVLELLLSTIDLpsSLRLVIVGGEAV 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327099 429 SPDVMDFLRICFGCSVR--EGYGMTE-----TSCVISAMDDGDNLSGHVGSPNPACEVKLVDvpemnytSDDQPYP---R 498
Cdd:cd17644 237 QPELVRQWQKNVGNFIQliNVYGPTEatiaaTVCRLTQLTERNITSVPIGRPIANTQVYILD-------ENLQPVPvgvP 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327099 499 GEICVRGPIIFKGYYKDEEQTREILDGDGWLH--------TGDIGLWLPGGRLKIIDRKKNIFKLaQGEYIAPEKIENVY 570
Cdd:cd17644 310 GELHIGGVGLARGYLNRPELTAEKFISHPFNSseserlykTGDLARYLPDGNIEYLGRIDNQVKI-RGFRIELGEIEAVL 388
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327099 571 TKCRFVSQCfihgdsfnsslVAIVSVDPEvmkdwaasegikyehlgqlcNDPRVRKTVLAEMDDLGREAQLRGFEFAK-A 649
Cdd:cd17644 389 SQHNDVKTA-----------VVIVREDQP--------------------GNKRLVAYIVPHYEESPSTVELRQFLKAKlP 437
|
490 500
....*....|....*....|....
gi 22327099 650 VTLVPEPF-TLENGLLTPTFKIKR 672
Cdd:cd17644 438 DYMIPSAFvVLEELPLTPNGKIDR 461
|
|
| ACS-like |
cd17634 |
acetate-CoA ligase; This family includes acyl- and aryl-CoA ligases, as well as the ... |
120-331 |
6.08e-09 |
|
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: 59.13 E-value: 6.08e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327099 120 TYGEAASERQAIGSGLLFHGVNQGDCVGLYFINRPEWLVVDHACAAYSFVSVPLYDTLGPDAVK----------FVVNHA 189
Cdd:cd17634 86 SYRELHREVCRFAGTLLDLGVKKGDRVAIYMPMIPEAAVAMLACARIGAVHSVIFGGFAPEAVAgriidsssrlLITADG 165
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327099 190 NLQAIFCVPQTLNILLSFLAEIPSIRLIVVVG--GADEhlpslpRGTGVTIVSYQKLLSQGRSSLHPfSPPKPEDIATIC 267
Cdd:cd17634 166 GVRAGRSVPLKKNVDDALNPNVTSVEHVIVLKrtGSDI------DWQEGRDLWWRDLIAKASPEHQP-EAMNAEDPLFIL 238
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 22327099 268 YTSGTTGTPKGVVLTHGNLIANVAGSSVEA-EFFPSDVYISYLPLAhiyeranQIMG----VYGGVAVG 331
Cdd:cd17634 239 YTSGTTGKPKGVLHTTGGYLVYAATTMKYVfDYGPGDIYWCTADVG-------WVTGhsylLYGPLACG 300
|
|
| FACL_like_5 |
cd05924 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
258-626 |
1.12e-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: 57.78 E-value: 1.12e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327099 258 PKPEDIaTICYTSGTTGTPKGVVLTHGNLIANVAGSS--VEAEFFPSD------------VYISYLPLAHIYERANQIMG 323
Cdd:cd05924 1 RSADDL-YILYTGGTTGMPKGVMWRQEDIFRMLMGGAdfGTGEFTPSEdahkaaaaaagtVMFPAPPLMHGTGSWTAFGG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327099 324 VYGGVAVgFYQGDVFklmDDFAVLRptifcSVPRlynriyDGITSAVKSSGVVKKRLFEiaynskkqAIINGRT---PSa 400
Cdd:cd05924 80 LLGGQTV-VLPDDRF---DPEEVWR-----TIEK------HKVTSMTIVGDAMARPLID--------ALRDAGPydlSS- 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327099 401 fwdklvfnkikeklggrVRFMGSGASPLSPDVMD-FLRICFGCSVREGYGMTETSCVISAMDDGdnlSGHVGSP--NPAC 477
Cdd:cd05924 136 -----------------LFAISSGGALLSPEVKQgLLELVPNITLVDAFGSSETGFTGSGHSAG---SGPETGPftRANP 195
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327099 478 EVKLVDvPEMNYTSDDQPYPrGEICVRGpIIFKGYYKDEEQTREI---LDGDGWLHTGDIGLWLPGGRLKIIDRKKNIFK 554
Cdd:cd05924 196 DTVVLD-DDGRVVPPGSGGV-GWIARRG-HIPLGYYGDEAKTAETfpeVDGVRYAVPGDRATVEADGTVTLLGRGSVCIN 272
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327099 555 LAqGEYIAPEKIENVYTKCRFVSQCFIHG---DSFNSSLVAIVSVDP------EVMKDWAASEGIKYEHLGQLCNDPRVR 625
Cdd:cd05924 273 TG-GEKVFPEEVEEALKSHPAVYDVLVVGrpdERWGQEVVAVVQLREgagvdlEELREHCRTRIARYKLPKQVVFVDEIE 351
|
.
gi 22327099 626 K 626
Cdd:cd05924 352 R 352
|
|
| FATP_FACS |
cd05940 |
Fatty acid transport proteins (FATP) play dual roles as fatty acid transporters and its ... |
262-583 |
1.70e-08 |
|
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: 57.36 E-value: 1.70e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327099 262 DIATICYTSGTTGTPKGVVLTHGNLIANVAGSSVEAEFFPSDVYISYLPLahiYERANQIMGVYGGVAVGfyqgdvfklm 341
Cdd:cd05940 82 DAALYIYTSGTTGLPKAAIISHRRAWRGGAFFAGSGGALPSDVLYTCLPL---YHSTALIVGWSACLASG---------- 148
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327099 342 ddfavlrptifcsvprlynriydgitsavksSGVVKKRLFeiaynskkqaiingrTPSAFWDKLVFN------------- 408
Cdd:cd05940 149 -------------------------------ATLVIRKKF---------------SASNFWDDIRKYqatifqyigelcr 182
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327099 409 -------KIKEKlGGRVRFM-GSGaspLSPDVMDFLRICFGC-SVREGYGMTETSCVISAMDDGDNLSGHVGSPN----P 475
Cdd:cd05940 183 yllnqppKPTER-KHKVRMIfGNG---LRPDIWEEFKERFGVpRIAEFYAATEGNSGFINFFGKPGAIGRNPSLLrkvaP 258
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327099 476 ACEVKlVDVPEMNYTSDDQPY----PRGE----ICVRGPI-IFKGYYKDEEQTREIL-----DGDGWLHTGDIGLWLPGG 541
Cdd:cd05940 259 LALVK-YDLESGEPIRDAEGRcikvPRGEpgllISRINPLePFDGYTDPAATEKKILrdvfkKGDAWFNTGDLMRLDGEG 337
|
330 340 350 360
....*....|....*....|....*....|....*....|..
gi 22327099 542 RLKIIDRKKNIFKLaQGEYIAPEKIENVYTKCRFVSQCFIHG 583
Cdd:cd05940 338 FWYFVDRLGDTFRW-KGENVSTTEVAAVLGAFPGVEEANVYG 378
|
|
| PRK12467 |
PRK12467 |
peptide synthase; Provisional |
205-312 |
2.58e-08 |
|
peptide synthase; Provisional
Pssm-ID: 237108 [Multi-domain] Cd Length: 3956 Bit Score: 57.86 E-value: 2.58e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327099 205 LSFLAEIPSIRLIVvvggADEHL-PSLPRGTGVTIVsyqkLLSQ------GRSSLHPFSPPKPEDIATICYTSGTTGTPK 277
Cdd:PRK12467 1663 LAYMIEDSGIELLL----TQSHLqARLPLPDGLRSL----VLDQeddwleGYSDSNPAVNLAPQNLAYVIYTSGSTGRPK 1734
|
90 100 110
....*....|....*....|....*....|....*
gi 22327099 278 GVVLTHGNLIANVAGSSVEAEFFPSDVYISYLPLA 312
Cdd:PRK12467 1735 GAGNRHGALVNRLCATQEAYQLSAADVVLQFTSFA 1769
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
197-312 |
3.06e-08 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 57.66 E-value: 3.06e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327099 197 VPQTLNILLSFLA-------------EIPSIRLIVVVGGADEHL--------PSLPRGTGVTIVSYQKLLS-QGRSSLHP 254
Cdd:PRK12316 4608 MERSAEMMVGLLAvlkaggayvpldpEYPRERLAYMMEDSGAALlltqshllQRLPIPDGLASLALDRDEDwEGFPAHDP 4687
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*...
gi 22327099 255 FSPPKPEDIATICYTSGTTGTPKGVVLTHGNLIANVAGSSVEAEFFPSDVYISYLPLA 312
Cdd:PRK12316 4688 AVRLHPDNLAYVIYTSGSTGRPKGVAVSHGSLVNHLHATGERYELTPDDRVLQFMSFS 4745
|
|
| AFD_YhfT-like |
cd17633 |
fatty acid-CoA ligase VraA; This family of acyl-CoA ligases includes Bacillus subtilis YhfT, ... |
418-597 |
4.45e-08 |
|
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: 55.49 E-value: 4.45e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327099 418 VRFMGSGASPLSPDVMDFLRICFGCSVR-EGYGMTETSCVISAMDDGDNLSGHVGSPNPACEVKLvdvpeMNYTSDDQpy 496
Cdd:cd17633 112 IKSIFSSGQKLFESTKKKLKNIFPKANLiEFYGTSELSFITYNFNQESRPPNSVGRPFPNVEIEI-----RNADGGEI-- 184
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327099 497 prGEICVRGPIIFKGYYKDEEQTReildgDGWLHTGDIGLWLPGGRLKIIDRKKNIFkLAQGEYIAPEKIENVYTKCRFV 576
Cdd:cd17633 185 --GKIFVKSEMVFSGYVRGGFSNP-----DGWMSVGDIGYVDEEGYLYLVGRESDMI-IIGGINIFPTEIESVLKAIPGI 256
|
170 180
....*....|....*....|....
gi 22327099 577 SQCFIHGDS---FNSSLVAIVSVD 597
Cdd:cd17633 257 EEAIVVGIPdarFGEIAVALYSGD 280
|
|
| A_NRPS_LgrA-like |
cd17645 |
adenylation (A) domain of linear gramicidin synthetase (LgrA) and similar proteins; This ... |
260-604 |
5.08e-08 |
|
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: 56.02 E-value: 5.08e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327099 260 PEDIATICYTSGTTGTPKGVVLTHGNLIaNVAgssveaeffpsDVYISYLPLAhiyerANQIMGVYGGVAVGFYQGDVFK 339
Cdd:cd17645 103 PDDLAYVIYTSGSTGLPKGVMIEHHNLV-NLC-----------EWHRPYFGVT-----PADKSLVYASFSFDASAWEIFP 165
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327099 340 LMDDFA---VLRPTIFCSVPRLyNRIYD--GITSAVKSSGVVKKrlFEIAYNSKKQAIINGRtpsafwDKLvfNKIKEKl 414
Cdd:cd17645 166 HLTAGAalhVVPSERRLDLDAL-NDYFNqeGITISFLPTGAAEQ--FMQLDNQSLRVLLTGG------DKL--KKIERK- 233
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327099 415 ggrvrfmgsgasplspdvmdflricfGCSVREGYGMTETSCVISAMD-DGDNLSGHVGSPNPACEVKLVDvpemnytSDD 493
Cdd:cd17645 234 --------------------------GYKLVNNYGPTENTVVATSFEiDKPYANIPIGKPIDNTRVYILD-------EAL 280
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327099 494 QPYP---RGEICVRGPIIFKGYYKDEEQTRE------ILDGDGWLHTGDIGLWLPGGRLKIIDRKKNIFKLaQGEYIAPE 564
Cdd:cd17645 281 QLQPigvAGELCIAGEGLARGYLNRPELTAEkfivhpFVPGERMYRTGDLAKFLPDGNIEFLGRLDQQVKI-RGYRIEPG 359
|
330 340 350 360
....*....|....*....|....*....|....*....|....*...
gi 22327099 565 KIENVYTKCRFVSQCFI----HGDSfNSSLVAIVS----VDPEVMKDW 604
Cdd:cd17645 360 EIEPFLMNHPLIELAAVlakeDADG-RKYLVAYVTapeeIPHEELREW 406
|
|
| hsFATP2a_ACSVL_like |
cd05938 |
Fatty acid transport proteins (FATP) including hsFATP2, hsFATP5, and hsFATP6, and similar ... |
120-583 |
5.60e-08 |
|
Fatty acid transport proteins (FATP) including hsFATP2, hsFATP5, and hsFATP6, and similar proteins; Fatty acid transport proteins (FATP) of this family transport long-chain or very-long-chain fatty acids across the plasma membrane. At least five copies of FATPs are identified in mammalian cells. This family includes hsFATP2, hsFATP5, and hsFATP6, and similar proteins. Each FATP has unique patterns of tissue distribution. These FATPs also have fatty acid CoA synthetase activity, thus playing dual roles as fatty acid transporters and its activation enzymes. The hsFATP proteins exist in two splice variants; the b variant, lacking exon 3, has no acyl-CoA synthetase activity. FATPs are key players in the trafficking of exogenous fatty acids into the cell and in intracellular fatty acid homeostasis.
Pssm-ID: 341261 [Multi-domain] Cd Length: 537 Bit Score: 56.15 E-value: 5.60e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327099 120 TYGEAASERQAIGSGLLFH-GVNQGDCVGLYFINRPE----WLVVDH-----ACAAYSFVSVPLYDTLGPDAVKFVVNHA 189
Cdd:cd05938 7 TYRDVDRRSNQAARALLAHaGLRPGDTVALLLGNEPAflwiWLGLAKlgcpvAFLNTNIRSKSLLHCFRCCGAKVLVVAP 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327099 190 NLQaifcvPQTLNILLSFLAEIpsIRLIVVVGGadehlpSLPRGtgvtIVSYQKLLSQGRSSLHPFSPPKPEDIATIC-- 267
Cdd:cd05938 87 ELQ-----EAVEEVLPALRADG--VSVWYLSHT------SNTEG----VISLLDKVDAASDEPVPASLRAHVTIKSPAly 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327099 268 -YTSGTTGTPKGVVLTHGNLIA--NVAGSS-VEAEffpsDVYISYLPLAHIyerANQIMGVYGGVAVGfyqgdvfklmdd 343
Cdd:cd05938 150 iYTSGTTGLPKAARISHLRVLQcsGFLSLCgVTAD----DVIYITLPLYHS---SGFLLGIGGCIELG------------ 210
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327099 344 favlrptifcsvprlynriydgitsavksSGVVKKRLFeiaynskkqaiingrTPSAFWDK------LVFNKIKEKL--- 414
Cdd:cd05938 211 -----------------------------ATCVLKPKF---------------SASQFWDDcrkhnvTVIQYIGELLryl 246
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327099 415 ----------GGRVRF-MGSGaspLSPDVM-DFLRIcFG-CSVREGYGMTETScvISAMddgdNLSGHVGSPNPA-CEVK 480
Cdd:cd05938 247 cnqpqspndrDHKVRLaIGNG---LRADVWrEFLRR-FGpIRIREFYGSTEGN--IGFF----NYTGKIGAVGRVsYLYK 316
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327099 481 LV--------DVPEMNYTSDDQ----PYPRGE----IC-VRGPIIFKGYYKDEEQT-REIL-----DGDGWLHTGDIGLW 537
Cdd:cd05938 317 LLfpfelikfDVEKEEPVRDAQgfciPVAKGEpgllVAkITQQSPFLGYAGDKEQTeKKLLrdvfkKGDVYFNTGDLLVQ 396
|
490 500 510 520
....*....|....*....|....*....|....*....|....*.
gi 22327099 538 LPGGRLKIIDRKKNIFKLaQGEYIAPEKIENVYTKCRFVSQCFIHG 583
Cdd:cd05938 397 DQQNFLYFHDRVGDTFRW-KGENVATTEVADVLGLLDFLQEVNVYG 441
|
|
| BACL_like |
cd05929 |
Bacterial Bile acid CoA ligases and similar proteins; Bile acid-Coenzyme A ligase catalyzes ... |
257-617 |
6.88e-08 |
|
Bacterial Bile acid CoA ligases and similar proteins; Bile acid-Coenzyme A ligase catalyzes the formation of bile acid-CoA conjugates in a two-step reaction: the formation of a bile acid-AMP molecule as an intermediate, followed by the formation of a bile acid-CoA. This ligase requires a bile acid with a free carboxyl group, ATP, Mg2+, and CoA for synthesis of the final bile acid-CoA conjugate. The bile acid-CoA ligation is believed to be the initial step in the bile acid 7alpha-dehydroxylation pathway in the intestinal bacterium Eubacterium sp.
Pssm-ID: 341252 [Multi-domain] Cd Length: 473 Bit Score: 55.46 E-value: 6.88e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327099 257 PPKPEDIAT--ICYTSGTTGTPKGVVLTH-GNLIAN--VAGSSVEAEFFPSDVYISYLPLAHIY-ERANQIMGVYGGVAV 330
Cdd:cd05929 119 TPIEDEAAGwkMLYSGGTTGRPKGIKRGLpGGPPDNdtLMAAALGFGPGADSVYLSPAPLYHAApFRWSMTALFMGGTLV 198
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327099 331 G---FYQGDVFKLMDDFAVlrpTIFCSVPRLYNRIydgitsaVKSSGVVKKRlfeiaYN-SKKQAIINGRTPSAFWdklv 406
Cdd:cd05929 199 LmekFDPEEFLRLIERYRV---TFAQFVPTMFVRL-------LKLPEAVRNA-----YDlSSLKRVIHAAAPCPPW---- 259
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327099 407 fnkIKEK---LGGRVrfmgsgasplspdvmdflricfgcsVREGYGMTET--SCVISamddGDNLSGHVGSPNPAC--EV 479
Cdd:cd05929 260 ---VKEQwidWGGPI-------------------------IWEYYGGTEGqgLTIIN----GEEWLTHPGSVGRAVlgKV 307
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327099 480 KLVDvpemnytSDDQPYPRGEIcvrGPIIFKG-----YYKDEEQTREILDGDGWLHTGDIGlWLPG-GRLKIIDRKKNIF 553
Cdd:cd05929 308 HILD-------EDGNEVPPGEI---GEVYFANgpgfeYTNDPEKTAAARNEGGWSTLGDVG-YLDEdGYLYLTDRRSDMI 376
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 22327099 554 kLAQGEYIAPEKIENVYTKCRFVSQCFIHG---DSFNSSLVAIVSVDPEVMKDWAASEGIKyEHLGQ 617
Cdd:cd05929 377 -ISGGVNIYPQEIENALIAHPKVLDAAVVGvpdEELGQRVHAVVQPAPGADAGTALAEELI-AFLRD 441
|
|
| A_NRPS_ACVS-like |
cd17648 |
N-(5-amino-5-carboxypentanoyl)-L-cysteinyl-D-valine synthase; This family contains ACV ... |
260-579 |
1.39e-07 |
|
N-(5-amino-5-carboxypentanoyl)-L-cysteinyl-D-valine synthase; This family contains ACV synthetase (ACVS, EC 6.3.2.26; also known as N-(5-amino-5-carboxypentanoyl)-L-cysteinyl-D-valine synthase or delta-(L-alpha-aminoadipyl)-L-cysteinyl-D-valine synthetase) is involved in medically important antibiotic biosynthesis. ACV synthetase is active in an early step in the penicillin G biosynthesis pathway which involves the formation of the tripeptide 6-(L-alpha-aminoadipyl)-L-cysteinyl-D-valine (ACV); each of the constituent amino acids of the tripeptide ACV are activated as aminoacyl-adenylates with peptide bonds formed through the participation of amino acid thioester intermediates. ACV is then cyclized by the action of isopenicillin N synthase.
Pssm-ID: 341303 [Multi-domain] Cd Length: 453 Bit Score: 54.33 E-value: 1.39e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327099 260 PEDIATICYTSGTTGTPKGVVLTHG---NLIAnvagsSVEAEFFPSDvyisylplaHIYEranqimgvyggvAVGFYQGD 336
Cdd:cd17648 93 STDLAYAIYTSGTTGKPKGVLVEHGsvvNLRT-----SLSERYFGRD---------NGDE------------AVLFFSNY 146
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327099 337 VFklmdDFavlrptifcSVPRLYNRIYDGITSAVKSSGVV--KKRLFEIAyNSKKQAIINGrTPSafwdklVFNKIKEKL 414
Cdd:cd17648 147 VF----DF---------FVEQMTLALLNGQKLVVPPDEMRfdPDRFYAYI-NREKVTYLSG-TPS------VLQQYDLAR 205
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327099 415 GGRVRFMGSGASPLSPDVMDFLRICFGCSVREGYGMTETSCV-----ISAMDDGDNLSGHvGSPNPACEVklvdvpemnY 489
Cdd:cd17648 206 LPHLKRVDAAGEEFTAPVFEKLRSRFAGLIINAYGPTETTVTnhkrfFPGDQRFDKSLGR-PVRNTKCYV---------L 275
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327099 490 TSDDQPYP---RGEICVRGPIIFKGYYKDEEQTRE------------ILDG-DGWLH-TGDIGLWLPGGRLKIIDRKKNI 552
Cdd:cd17648 276 NDAMKRVPvgaVGELYLGGDGVARGYLNRPELTAErflpnpfqteqeRARGrNARLYkTGDLVRWLPSGELEYLGRNDFQ 355
|
330 340
....*....|....*....|....*..
gi 22327099 553 FKLaQGEYIAPEKIENVYTKCRFVSQC 579
Cdd:cd17648 356 VKI-RGQRIEPGEVEAALASYPGVREC 381
|
|
| entF |
PRK10252 |
enterobactin non-ribosomal peptide synthetase EntF; |
223-283 |
1.43e-07 |
|
enterobactin non-ribosomal peptide synthetase EntF;
Pssm-ID: 236668 [Multi-domain] Cd Length: 1296 Bit Score: 55.05 E-value: 1.43e-07
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 22327099 223 ADEHLPSLPRGTGVTIVSYQKLLSqgRSSLHPFSPPKPEDIATICYTSGTTGTPKGVVLTH 283
Cdd:PRK10252 562 TADQLPRFADVPDLTSLCYNAPLA--PQGAAPLQLSQPHHTAYIIFTSGSTGRPKGVMVGQ 620
|
|
| PRK04813 |
PRK04813 |
D-alanine--poly(phosphoribitol) ligase subunit DltA; |
234-579 |
2.01e-07 |
|
D-alanine--poly(phosphoribitol) ligase subunit DltA;
Pssm-ID: 235313 [Multi-domain] Cd Length: 503 Bit Score: 54.13 E-value: 2.01e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327099 234 TGVTIVSYQKLLSQGR--SSLHPFSPPKPEDIATICYTSGTTGTPKGVVLTHGNLIanvagssveaEFfpSDVYISYLPL 311
Cdd:PRK04813 114 LGIPVITLDELKDIFAtgNPYDFDHAVKGDDNYYIIFTSGTTGKPKGVQISHDNLV----------SF--TNWMLEDFAL 181
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327099 312 AHIYERANQ--------IMGVYGGVAVGfyqGDVFKL----MDDFavlrptifcsvprlynriydgitsavkssgvvkKR 379
Cdd:PRK04813 182 PEGPQFLNQapysfdlsVMDLYPTLASG---GTLVALpkdmTANF---------------------------------KQ 225
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327099 380 LFEiaynSKKQAIIN--GRTPS----AFWDKlVFNKikEKLGGRVRFMGSGASpLSPDVMDFLRICFGCS-VREGYGMTE 452
Cdd:PRK04813 226 LFE----TLPQLPINvwVSTPSfadmCLLDP-SFNE--EHLPNLTHFLFCGEE-LPHKTAKKLLERFPSAtIYNTYGPTE 297
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327099 453 TSCVISA-------MDDGDNLSghVGSPNPACEVKLVDvPEMNYTSDDQPyprGEICVRGPIIFKGYYKDEEQTREI--- 522
Cdd:PRK04813 298 ATVAVTSieitdemLDQYKRLP--IGYAKPDSPLLIID-EEGTKLPDGEQ---GEIVISGPSVSKGYLNNPEKTAEAfft 371
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 22327099 523 LDGDGWLHTGDIG-----LWLPGGRlkiIDrkkniF--KLAqGEYIAPEKIENVYTKCRFVSQC 579
Cdd:PRK04813 372 FDGQPAYHTGDAGyledgLLFYQGR---ID-----FqiKLN-GYRIELEEIEQNLRQSSYVESA 426
|
|
| PRK07769 |
PRK07769 |
long-chain-fatty-acid--CoA ligase; Validated |
76-547 |
2.50e-07 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 181109 [Multi-domain] Cd Length: 631 Bit Score: 53.96 E-value: 2.50e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327099 76 RFPDHpeiGTLHDNFVHAVETYAEN---KYLGTRVRSDGTIGEYSWMTYGeaaSERQAIGSGLlfHGVNQ-GDCVGlyfI 151
Cdd:PRK07769 16 RFPPN---TNLVRHVERWAKVRGDKlayRFLDFSTERDGVARDLTWSQFG---ARNRAVGARL--QQVTKpGDRVA---I 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327099 152 NRPEWL--VVDHACAAYS-FVSVPLYDTLGPdavkfvvNHAN-LQAIF--CVPQTlnILLS---------FLAEIPSI-- 214
Cdd:PRK07769 85 LAPQNLdyLIAFFGALYAgRIAVPLFDPAEP-------GHVGrLHAVLddCTPSA--ILTTtdsaegvrkFFRARPAKer 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327099 215 -RLIVVvggadehlPSLPRGTGVTIVsyqkllsqgrsslhpfsPPKP--EDIATICYTSGTTGTPKGVVLTHGNLIANVA 291
Cdd:PRK07769 156 pRVIAV--------DAVPDEVGATWV-----------------PPEAneDTIAYLQYTSGSTRIPAGVQITHLNLPTNVL 210
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327099 292 G--SSVEAEffPSDVYISYLPLAHiyeranqIMGVYgGVAVGFYQGDVFKLMDdfavlrPTIFCSVPRLYNRiydgiTSA 369
Cdd:PRK07769 211 QviDALEGQ--EGDRGVSWLPFFH-------DMGLI-TVLLPALLGHYITFMS------PAAFVRRPGRWIR-----ELA 269
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327099 370 VKSSGVvkKRLFEIAYN-SKKQAIINGrTPSAFWDKLVFNKIKEKLggrvrfmgSGASPLSPDVMDFLRICFG------C 442
Cdd:PRK07769 270 RKPGGT--GGTFSAAPNfAFEHAAARG-LPKDGEPPLDLSNVKGLL--------NGSEPVSPASMRKFNEAFApyglppT 338
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327099 443 SVREGYGMTETSCVISA--MD--------DGDNL-SGHV-----GSPNPACEVK-----------LVDvPEmnyTSDDQP 495
Cdd:PRK07769 339 AIKPSYGMAEATLFVSTtpMDeeptviyvDRDELnAGRFvevpaDAPNAVAQVSagkvgvsewavIVD-PE---TASELP 414
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 22327099 496 YPR-GEICVRGPIIFKGYYKDEEQTREIL-----------------DGDGWLHTGDIGLWLPG-----GRLK---IID 547
Cdd:PRK07769 415 DGQiGEIWLHGNNIGTGYWGKPEETAATFqnilksrlseshaegapDDALWVRTGDYGVYFDGelyitGRVKdlvIID 492
|
|
| hsFATP4_like |
cd05939 |
Fatty acid transport proteins (FATP), including FATP4 and FATP1, and similar proteins; Fatty ... |
120-583 |
3.53e-07 |
|
Fatty acid transport proteins (FATP), including FATP4 and FATP1, and similar proteins; Fatty acid transport protein (FATP) transports long-chain or very-long-chain fatty acids across the plasma membrane. At least five copies of FATPs are identified in mammalian cells. This family includes FATP4, FATP1, and homologous proteins. Each FATP has unique patterns of tissue distribution. FATP4 is mainly expressed in the brain, testis, colon and kidney. FATPs also have fatty acid CoA synthetase activity, thus playing dual roles as fatty acid transporters and its activation enzymes. FATPs are the key players in the trafficking of exogenous fatty acids into the cell and in intracellular fatty acid homeostasis.
Pssm-ID: 341262 [Multi-domain] Cd Length: 474 Bit Score: 53.20 E-value: 3.53e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327099 120 TYGEAASERQAIGSGLLFHGVNQGDCVGLYFINRPEWLVVDHACAAYSFVSVPLYDTLGPDAVKFVVNHANLQAifCVPQ 199
Cdd:cd05939 5 TFRELNEYSNKVANFFQAQGYRSGDVVALFMENRLEFVALWLGLAKIGVETALINSNLRLESLLHCITVSKAKA--LIFN 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327099 200 TLNILLSFlaeipsirlivvvggADEHLPSLPRGTGVTIVSYqkllsqgrsslhpfsppkpediatiCYTSGTTGTPKGV 279
Cdd:cd05939 83 LLDPLLTQ---------------SSTEPPSQDDVNFRDKLFY-------------------------IYTSGTTGLPKAA 122
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327099 280 VLTHGNLIANVAGSSVEAEFFPSDVYISYLPLahiYERANQIMGVYGGVAVGfyqgdvfklmddfavlrptifcsvprly 359
Cdd:cd05939 123 VIVHSRYYRIAAGAYYAFGMRPEDVVYDCLPL---YHSAGGIMGVGQALLHG---------------------------- 171
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327099 360 nriydgitsavkSSGVVKKRLfeiaynskkqaiingrTPSAFWDKLV-FN-KIKEKLGGRVRFMgsGASPLSPDVMDF-L 436
Cdd:cd05939 172 ------------STVVIRKKF----------------SASNFWDDCVkYNcTIVQYIGEICRYL--LAQPPSEEEQKHnV 221
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327099 437 RICFGCSVR-----------------EGYGMTETSCVISamddgdNLSGHVGspnpAC-----------EVKLVDVPEmn 488
Cdd:cd05939 222 RLAVGNGLRpqiweqfvrrfgipqigEFYGATEGNSSLV------NIDNHVG----ACgfnsrilpsvyPIRLIKVDE-- 289
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327099 489 YTSDDQPYPRGeICVR----------GPII-------FKGYYKDEEQTREIL-----DGDGWLHTGDIGLWLPGGRLKII 546
Cdd:cd05939 290 DTGELIRDSDG-LCIPcqpgepgllvGKIIqndplrrFDGYVNEGATNKKIArdvfkKGDSAFLSGDVLVMDELGYLYFK 368
|
490 500 510
....*....|....*....|....*....|....*..
gi 22327099 547 DRKKNIFKLaQGEYIAPEKIENVYTKCRFVSQCFIHG 583
Cdd:cd05939 369 DRTGDTFRW-KGENVSTTEVEGILSNVLGLEDVVVYG 404
|
|
| PRK05850 |
PRK05850 |
acyl-CoA synthetase; Validated |
219-568 |
3.92e-07 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 235624 [Multi-domain] Cd Length: 578 Bit Score: 53.41 E-value: 3.92e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327099 219 VVGGADEHLPSLPRGTGVTIVSYQKLLSQGRSSLHPFSPPKPeDIATICYTSGTTGTPKGVVLTHGNLIANVagSSVEAE 298
Cdd:PRK05850 119 VVDDVTEYVAPQPGQSAPPVIEVDLLDLDSPRGSDARPRDLP-STAYLQYTSGSTRTPAGVMVSHRNVIANF--EQLMSD 195
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327099 299 FF-------PSDVYI-SYLPLAHiyeranqIMGVYGGVAVGFYQGDVFKLMDDFAVLR------------PTIFCSVPRL 358
Cdd:PRK05850 196 YFgdtggvpPPDTTVvSWLPFYH-------DMGLVLGVCAPILGGCPAVLTSPVAFLQrparwmqllasnPHAFSAAPNF 268
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327099 359 ynriydgitsavkssgvvkkrLFEIAYNSKKQAIINGRtpsafwdklvfnkikeKLGGrVRFMGSGASPLSPDVMD---- 434
Cdd:PRK05850 269 ---------------------AFELAVRKTSDDDMAGL----------------DLGG-VLGIISGSERVHPATLKrfad 310
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327099 435 -FLRicFGCS---VREGYGMTE-TSCVISAMD---------DGDNLS-GHVGSPNPACEVKLVdvpemNYTSDDQPYPR- 498
Cdd:PRK05850 311 rFAP--FNLRetaIRPSYGLAEaTVYVATREPgqppesvrfDYEKLSaGHAKRCETGGGTPLV-----SYGSPRSPTVRi 383
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327099 499 --------------GEICVRGPIIFKGYYKDEEQTREILDG----------DG-WLHTGDIGLwLPGGRLKIIDRKKNIF 553
Cdd:PRK05850 384 vdpdtciecpagtvGEIWVHGDNVAAGYWQKPEETERTFGAtlvdpspgtpEGpWLRTGDLGF-ISEGELFIVGRIKDLL 462
|
410
....*....|....*
gi 22327099 554 kLAQGEYIAPEKIEN 568
Cdd:PRK05850 463 -IVDGRNHYPDDIEA 476
|
|
| A_NRPS_CmdD_like |
cd17652 |
similar to adenylation domain of chondramide synthase cmdD; This family of the adenylation (A) ... |
260-297 |
8.05e-07 |
|
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: 51.87 E-value: 8.05e-07
10 20 30
....*....|....*....|....*....|....*...
gi 22327099 260 PEDIATICYTSGTTGTPKGVVLTHGNLiANVAGSSVEA 297
Cdd:cd17652 92 PDNLAYVIYTSGSTGRPKGVVVTHRGL-ANLAAAQIAA 128
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
205-312 |
2.58e-06 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 51.11 E-value: 2.58e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327099 205 LSFLAEIPSIRLIVVVGGADEHLPsLPRGTGVTIVSYQKLLsQGRSSLHPFSPPKPEDIATICYTSGTTGTPKGVVLTHG 284
Cdd:PRK12316 2092 LAYMLEDSGAALLLTQRHLLERLP-LPAGVARLPLDRDAEW-ADYPDTAPAVQLAGENLAYVIYTSGSTGLPKGVAVSHG 2169
|
90 100
....*....|....*....|....*...
gi 22327099 285 NLIANVAGSSVEAEFFPSDVYISYLPLA 312
Cdd:PRK12316 2170 ALVAHCQAAGERYELSPADCELQFMSFS 2197
|
|
| PRK07638 |
PRK07638 |
acyl-CoA synthetase; Validated |
446-594 |
4.68e-06 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236071 [Multi-domain] Cd Length: 487 Bit Score: 49.78 E-value: 4.68e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327099 446 EGYGMTETSCVISAMDDGDNLSGH-VGSP--NPACEVKLVDVPEMnytsddQPYPRGEICVRGPIIFKGYYKDEEQTREi 522
Cdd:PRK07638 284 EFYGASELSFVTALVDEESERRPNsVGRPfhNVQVRICNEAGEEV------QKGEIGTVYVKSPQFFMGYIIGGVLARE- 356
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 22327099 523 LDGDGWLHTGDIGLWLPGGRLKIIDRKKNIFkLAQGEYIAPEKIENVYTKCRFVSQCFIHG--DSF-NSSLVAIV 594
Cdd:PRK07638 357 LNADGWMTVRDVGYEDEEGFIYIVGREKNMI-LFGGINIFPEEIESVLHEHPAVDEIVVIGvpDSYwGEKPVAII 430
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
205-290 |
4.95e-06 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 50.34 E-value: 4.95e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327099 205 LSFLAEIPSIRLIVvvggADEHL-PSLPRGTGVTIVSYQK--LLSQGRSSLHPFSPPKPEDIATICYTSGTTGTPKGVVL 281
Cdd:PRK12316 600 LAYMLEDSGVQLLL----SQSHLgRKLPLAAGVQVLDLDRpaAWLEGYSEENPGTELNPENLAYVIYTSGSTGKPKGAGN 675
|
....*....
gi 22327099 282 THGNLIANV 290
Cdd:PRK12316 676 RHRALSNRL 684
|
|
| PRK08279 |
PRK08279 |
long-chain-acyl-CoA synthetase; Validated |
120-313 |
5.89e-06 |
|
long-chain-acyl-CoA synthetase; Validated
Pssm-ID: 236217 [Multi-domain] Cd Length: 600 Bit Score: 49.49 E-value: 5.89e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327099 120 TYGEAASERQAIGSGLLFHGVNQGDCVGLYFINRPE----WLVVDH--ACAA---YSFVSVPL---YDTLGPDAVkfVVN 187
Cdd:PRK08279 64 SYAELNARANRYAHWAAARGVGKGDVVALLMENRPEylaaWLGLAKlgAVVAllnTQQRGAVLahsLNLVDAKHL--IVG 141
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327099 188 HANLQAIFCVPQTLNILlsflaeipsiRLIVVVGGADEHLPSLprgtgvtivsYQKL--LSQGRSSLHPFSPPK--PEDI 263
Cdd:PRK08279 142 EELVEAFEEARADLARP----------PRLWVAGGDTLDDPEG----------YEDLaaAAAGAPTTNPASRSGvtAKDT 201
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 22327099 264 ATICYTSGTTGTPKGVVLTHGNLIANVAGSSVEAEFFPSDVYISYLPLAH 313
Cdd:PRK08279 202 AFYIYTSGTTGLPKAAVMSHMRWLKAMGGFGGLLRLTPDDVLYCCLPLYH 251
|
|
| A_NRPS_acs4 |
cd17654 |
acyl-CoA synthetase family member 4; This family of the adenylation (A) domain of nonribosomal ... |
175-311 |
1.08e-05 |
|
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: 48.62 E-value: 1.08e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327099 175 DTLGPDAVKFVVNHANLQAIFCVPqTLNILLSFLAeipsirlIVVVGGA----DEHLPS-----LPRGTGVTIVSYQKLL 245
Cdd:cd17654 27 SNLSNFLRKKFQTEERAIGLRCDR-GTESPVAILA-------ILFLGAAyapiDPASPEqrsltVMKKCHVSYLLQNKEL 98
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327099 246 SQGRSSLHP----FSPPKPEDIATICYTSGTTGTPKGVVLTHGNLIANVAGSSVEAEFFPSDVYISYLPL 311
Cdd:cd17654 99 DNAPLSFTPehrhFNIRTDECLAYVIHTSGTTGTPKIVAVPHKCILPNIQHFRSLFNITSEDILFLTSPL 168
|
|
| AACS |
cd05943 |
Acetoacetyl-CoA synthetase (acetoacetate-CoA ligase, AACS); AACS is a cytosolic ligase that ... |
107-284 |
1.12e-05 |
|
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: 48.81 E-value: 1.12e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327099 107 VRSDGTIGEYSWmtyGEAASERQAIGSGLLFHGVNQGDCVGLYFINRPEWLVvdhAC-------AAYSFVSVplyDTlGP 179
Cdd:cd05943 90 AAEDGERTEVTW---AELRRRVARLAAALRALGVKPGDRVAGYLPNIPEAVV---AMlatasigAIWSSCSP---DF-GV 159
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327099 180 DAVK-----------FVVNHANLQA-IFCVPQTLNILLsflAEIPSIRLIVVV----GGADEHLPSLPRgtgvtIVSYQK 243
Cdd:cd05943 160 PGVLdrfgqiepkvlFAVDAYTYNGkRHDVREKVAELV---KGLPSLLAVVVVpytvAAGQPDLSKIAK-----ALTLED 231
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 22327099 244 LLSQGRSSLHPFSPPKPEDIATICYTSGTTGTPKGVVLTHG 284
Cdd:cd05943 232 FLATGAAGELEFEPLPFDHPLYILYSSGTTGLPKCIVHGAG 272
|
|
| PRK07824 |
PRK07824 |
o-succinylbenzoate--CoA ligase; |
249-598 |
2.47e-05 |
|
o-succinylbenzoate--CoA ligase;
Pssm-ID: 236108 [Multi-domain] Cd Length: 358 Bit Score: 46.96 E-value: 2.47e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327099 249 RSSLHPFSPPKPeDIATICYTSGTTGTPKGVVLTHGNLIAnvAGSSVEAEFFPSDVYISYLPLAHIYERANQIMGVYGG- 327
Cdd:PRK07824 24 RDALRVGEPIDD-DVALVVATSGTTGTPKGAMLTAAALTA--SADATHDRLGGPGQWLLALPAHHIAGLQVLVRSVIAGs 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327099 328 ------VAVGFyqgDVFKLMDDFAVLRPtifcsvprlyNRIYDGITSAvkssgvvkkrlfeiaynskkQAIINGRTPSAF 401
Cdd:PRK07824 101 epveldVSAGF---DPTALPRAVAELGG----------GRRYTSLVPM--------------------QLAKALDDPAAT 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327099 402 WDKLVFNKIkeKLGGrvrfmgsgaSPLSPDVMDFLRiCFGCSVREGYGMTETS--CVisamddgdnlsgHVGSPNPACEV 479
Cdd:PRK07824 148 AALAELDAV--LVGG---------GPAPAPVLDAAA-AAGINVVRTYGMSETSggCV------------YDGVPLDGVRV 203
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327099 480 KLVDvpemnytsddqpyprGEICVRGPIIFKGYykdeeqtREILDGD-----GWLHTGDIGLwLPGGRLKIIDRKKNIFK 554
Cdd:PRK07824 204 RVED---------------GRIALGGPTLAKGY-------RNPVDPDpfaepGWFRTDDLGA-LDDGVLTVLGRADDAIS 260
|
330 340 350 360
....*....|....*....|....*....|....*....|....*..
gi 22327099 555 LAqGEYIAPEKIENVYTKCRFVSQCFIHG---DSFNSSLVAIVSVDP 598
Cdd:PRK07824 261 TG-GLTVLPQVVEAALATHPAVADCAVFGlpdDRLGQRVVAAVVGDG 306
|
|
| PRK12467 |
PRK12467 |
peptide synthase; Provisional |
227-286 |
7.55e-05 |
|
peptide synthase; Provisional
Pssm-ID: 237108 [Multi-domain] Cd Length: 3956 Bit Score: 46.31 E-value: 7.55e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327099 227 LPSLPRGTGVTIVSYQKLLSQGRSSLHPFSPPKPEDIATICYTSGTTGTPKGVVLTHGNL 286
Cdd:PRK12467 3203 LEQLPAPAGDTALTLDRLDLNGYSENNPSTRVMGENLAYVIYTSGSTGKPKGVGVRHGAL 3262
|
|
| Ac_CoA_lig_AcsA |
TIGR02188 |
acetate--CoA ligase; This model describes acetate-CoA ligase (EC 6.2.1.1), also called ... |
114-284 |
1.58e-04 |
|
acetate--CoA ligase; This model describes acetate-CoA ligase (EC 6.2.1.1), also called acetyl-CoA synthetase and acetyl-activating enzyme. It catalyzes the reaction ATP + acetate + CoA = AMP + diphosphate + acetyl-CoA and belongs to the family of AMP-binding enzymes described by pfam00501.
Pssm-ID: 274022 [Multi-domain] Cd Length: 626 Bit Score: 44.93 E-value: 1.58e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327099 114 GEYSWMTYGEAASERQAIGSGLLFHGVNQGDCVGLYFINRPEWLVVDHACAAYSFVSVPLYDTLGPDAVKFVVNHANLQA 193
Cdd:TIGR02188 84 GEVRKITYRELHREVCRFANVLKSLGVKKGDRVAIYMPMIPEAAIAMLACARIGAIHSVVFGGFSAEALADRINDAGAKL 163
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327099 194 IFCVPQTL---------NILLSFLAEIP-SIRLIVVVggadehlpslpRGTGVTIVSYQKllsqGR--------SSLHPF 255
Cdd:TIGR02188 164 VITADEGLrggkviplkAIVDEALEKCPvSVEHVLVV-----------RRTGNPVVPWVE----GRdvwwhdlmAKASAY 228
|
170 180 190
....*....|....*....|....*....|..
gi 22327099 256 SPPKP---EDIATICYTSGTTGTPKGVVLTHG 284
Cdd:TIGR02188 229 CEPEPmdsEDPLFILYTSGSTGKPKGVLHTTG 260
|
|
| ACS |
cd05966 |
Acetyl-CoA synthetase (also known as acetate-CoA ligase and acetyl-activating enzyme); ... |
254-284 |
1.70e-04 |
|
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: 44.86 E-value: 1.70e-04
10 20 30
....*....|....*....|....*....|....
gi 22327099 254 PFSPPKP---EDIATICYTSGTTGTPKGVVLTHG 284
Cdd:cd05966 221 PECEPEWmdsEDPLFILYTSGSTGKPKGVVHTTG 254
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
198-599 |
3.31e-04 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 44.18 E-value: 3.31e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327099 198 PQTLNILLSFLAEIPSIRLIVvvggADEHLpSLPRGTGVTIVSYQKLlSQGRSSLHPFSPPKPEDIATICYTSGTTGTPK 277
Cdd:PRK12316 3139 PEYPEERLAYMLEDSGAQLLL----SQSHL-RLPLAQGVQVLDLDRG-DENYAEANPAIRTMPENLAYVIYTSGSTGKPK 3212
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327099 278 GVVLTHGNLIANVAGSsveaeffpsdvyisylplahiyeranqimgvyggvavgfyqGDVFKLMDDFAVLRPTIF---CS 354
Cdd:PRK12316 3213 GVGIRHSALSNHLCWM-----------------------------------------QQAYGLGVGDRVLQFTTFsfdVF 3251
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327099 355 VPRLYNRIYDGitSAVKSSGVVKKRLFEIAYNSKKQAIINgrTPSAFWDKL--VFNKIKEKLGGRVRFMGSGASPLSPDV 432
Cdd:PRK12316 3252 VEELFWPLMSG--ARVVLAGPEDWRDPALLVELINSEGVD--VLHAYPSMLqaFLEEEDAHRCTSLKRIVCGGEALPADL 3327
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327099 433 MDflRICFGCSVREGYGMTETSCVISAMDDGDNLSGH--VGSPNPACEVKLVDvpemnytSDDQPYPRG---EICVRGPI 507
Cdd:PRK12316 3328 QQ--QVFAGLPLYNLYGPTEATITVTHWQCVEEGKDAvpIGRPIANRACYILD-------GSLEPVPVGalgELYLGGEG 3398
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327099 508 IFKGYYKDEEQTRE------ILDGDGWLHTGDIGLWLPGGRLKIIDRKKNIFKLaQGEYIAPEKIENVYTKCRFVSQCFI 581
Cdd:PRK12316 3399 LARGYHNRPGLTAErfvpdpFVPGERLYRTGDLARYRADGVIEYIGRVDHQVKI-RGFRIELGEIEARLLEHPWVREAVV 3477
|
410
....*....|....*...
gi 22327099 582 HGDSFNSSLVAIVSVDPE 599
Cdd:PRK12316 3478 LAVDGRQLVAYVVPEDEA 3495
|
|
| PrpE |
cd05967 |
Propionyl-CoA synthetase (PrpE); EC 6.2.1.17: propanoate:CoA ligase (AMP-forming) or ... |
120-316 |
1.49e-03 |
|
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: 41.92 E-value: 1.49e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327099 120 TYGEAASERQAIGSGLLFHGVNQGDCVGLYFINRPEWLVVDHAC----AAYSFV----SVPLYDTLGPDAVKFVVNHANL 191
Cdd:cd05967 84 TYAELLDEVSRLAGVLRKLGVVKGDRVIIYMPMIPEAAIAMLACarigAIHSVVfggfAAKELASRIDDAKPKLIVTASC 163
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327099 192 QA----IFCVPQTLNILLSfLAEIPSIRLIVVvggaDEHLPSLPRGTGVTIVSYQKLLSQGRSslHPFSPPKPEDIATIC 267
Cdd:cd05967 164 GIepgkVVPYKPLLDKALE-LSGHKPHHVLVL----NRPQVPADLTKPGRDLDWSELLAKAEP--VDCVPVAATDPLYIL 236
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 22327099 268 YTSGTTGTPKGVVL-THGNLIA------NVAGSSVEAEFFP-SDV-------YISYLPLAH-----IYE 316
Cdd:cd05967 237 YTSGTTGKPKGVVRdNGGHAVAlnwsmrNIYGIKPGDVWWAaSDVgwvvghsYIVYGPLLHgattvLYE 305
|
|
| PRK00174 |
PRK00174 |
acetyl-CoA synthetase; Provisional |
208-328 |
1.91e-03 |
|
acetyl-CoA synthetase; Provisional
Pssm-ID: 234677 [Multi-domain] Cd Length: 637 Bit Score: 41.28 E-value: 1.91e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327099 208 LAEIPSIRLIVVVggadehlpslpRGTGVTI-------VSYQKLLsQGRSSLHPFSPPKPEDIATICYTSGTTGTPKGVV 280
Cdd:PRK00174 197 LANCPSVEKVIVV-----------RRTGGDVdwvegrdLWWHELV-AGASDECEPEPMDAEDPLFILYTSGSTGKPKGVL 264
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 22327099 281 LTHGNLIANVAgSSVEAEF--FPSDV--------------YISYLPLAhiyERANQIMgvYGGV 328
Cdd:PRK00174 265 HTTGGYLVYAA-MTMKYVFdyKDGDVywctadvgwvtghsYIVYGPLA---NGATTLM--FEGV 322
|
|
| PRK05691 |
PRK05691 |
peptide synthase; Validated |
260-286 |
3.19e-03 |
|
peptide synthase; Validated
Pssm-ID: 235564 [Multi-domain] Cd Length: 4334 Bit Score: 40.92 E-value: 3.19e-03
10 20
....*....|....*....|....*..
gi 22327099 260 PEDIATICYTSGTTGTPKGVVLTHGNL 286
Cdd:PRK05691 2332 PQHQAYLIYTSGSTGKPKGVVVSHGEI 2358
|
|
| PRK03584 |
PRK03584 |
acetoacetate--CoA ligase; |
97-284 |
5.55e-03 |
|
acetoacetate--CoA ligase;
Pssm-ID: 235134 [Multi-domain] Cd Length: 655 Bit Score: 40.16 E-value: 5.55e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327099 97 YAENKYLGTR--------VRSDGTIGEYSWmtyGEAASERQAIGSGLLFHGVNQGDCVGLYFINRPEWLVVDHACAA--- 165
Cdd:PRK03584 88 YAENLLRHRRddrpaiifRGEDGPRRELSW---AELRRQVAALAAALRALGVGPGDRVAAYLPNIPETVVAMLATASlga 164
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327099 166 -YSFVSvPLYdtlGPDAV---------K--FVVN--HANLQAIFCVPQTLNILlsflAEIPSIRLIVVVGGADehlPSLP 231
Cdd:PRK03584 165 iWSSCS-PDF---GVQGVldrfgqiepKvlIAVDgyRYGGKAFDRRAKVAELR----AALPSLEHVVVVPYLG---PAAA 233
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 22327099 232 RGTGVTIVSYQKLLSQGRSSlhpfsPPKPEDIAT-----ICYTSGTTGTPKGVVLTHG 284
Cdd:PRK03584 234 AAALPGALLWEDFLAPAEAA-----ELEFEPVPFdhplwILYSSGTTGLPKCIVHGHG 286
|
|
| PRK05691 |
PRK05691 |
peptide synthase; Validated |
227-286 |
6.88e-03 |
|
peptide synthase; Validated
Pssm-ID: 235564 [Multi-domain] Cd Length: 4334 Bit Score: 40.15 E-value: 6.88e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 22327099 227 LPSLPRGTGVTIVSYQKLLSQGrsslHPFSPP----KPEDIATICYTSGTTGTPKGVVLTHGNL 286
Cdd:PRK05691 1239 LERLPQAEGVSAIALDSLHLDS----WPSQAPglhlHGDNLAYVIYTSGSTGQPKGVGNTHAAL 1298
|
|
| |
