|
Name |
Accession |
Description |
Interval |
E-value |
| MACS_euk |
cd05928 |
Eukaryotic Medium-chain acyl-CoA synthetase (MACS or ACSM); MACS catalyzes the two-step ... |
54-596 |
0e+00 |
|
Eukaryotic Medium-chain acyl-CoA synthetase (MACS or ACSM); MACS catalyzes the two-step activation of medium chain fatty acids (containing 4-12 carbons). The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. The acyl-CoA is a key intermediate in many important biosynthetic and catabolic processes. MACS enzymes are localized to mitochondria. Two murine MACS family proteins are found in liver and kidney. In rodents, a MACS member is detected particularly in the olfactory epithelium and is called O-MACS. O-MACS demonstrates substrate preference for the fatty acid lengths of C6-C12.
Pssm-ID: 341251 [Multi-domain] Cd Length: 530 Bit Score: 1043.97 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217306889 54 IPEYFNFAKDVLDQWTDKEKAGKKPSNPAFWWINRNGEEMRWSFEELGSLSRKFANILSEACSLQRGDRVILILPRVPEW 133
Cdd:cd05928 1 VPEYFNFASDVLDQWADKEKAGKRPPNPALWWVNGKGDEVKWSFRELGSLSRKAANVLSGACGLQRGDRVAVILPRVPEW 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217306889 134 WLANVACLRTGTVLIPGTTQLTQKDILYRLQSSKANCIITNDVLAPAVDAVASKCENLHSKLIVSENSREGWGNLKELMk 213
Cdd:cd05928 81 WLVNVACIRTGLVFIPGTIQLTAKDILYRLQASKAKCIVTSDELAPEVDSVASECPSLKTKLLVSEKSRDGWLNFKELL- 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217306889 214 vflchpgwstvarswltatstslvqailsllsswdyRHASDSHTCVKTKHNEIMAIFFTSGTSGYPKMTAHTHSSFGLGL 293
Cdd:cd05928 160 ------------------------------------NEASTEHHCVETGSQEPMAIYFTSGTTGSPKMAEHSHSSLGLGL 203
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217306889 294 SVNGRFWLDLTPSDVMWNTSDTGWAKSAWSSVFSPWIQGACVFTHHLPRFEPTSILQTLSKYPITVFCSAPTVYRMLVQN 373
Cdd:cd05928 204 KVNGRYWLDLTASDIMWNTSDTGWIKSAWSSLFEPWIQGACVFVHHLPRFDPLVILKTLSSYPITTFCGAPTVYRMLVQQ 283
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217306889 374 DITSYKFKSLKHCVSAGEPITPDVTEKWRNKTGLDIYEGYGQTETVLICGNFKGMKIKPGSMGKPSPAFDVKIVDVNGNV 453
Cdd:cd05928 284 DLSSYKFPSLQHCVTGGEPLNPEVLEKWKAQTGLDIYEGYGQTETGLICANFKGMKIKPGSMGKASPPYDVQIIDDNGNV 363
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217306889 454 LPPGQEGDIGIQVLPNRPFGLFTHYVDNPSKTASTLRGNFYITGDRGYMDKDGYFWFVARADDVILSSGYRIGPFEVENA 533
Cdd:cd05928 364 LPPGTEGDIGIRVKPIRPFGLFSGYVDNPEKTAATIRGDFYLTGDRGIMDEDGYFWFMGRADDVINSSGYRIGPFEVESA 443
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2217306889 534 LNEHPSVAESAVVSSPDPIRGEVVKAFVVLNPDYKSHDQEQLIKEIQEHVKKTTAPYKYPRKV 596
Cdd:cd05928 444 LIEHPAVVESAVVSSPDPIRGEVVKAFVVLAPQFLSHDPEQLTKELQQHVKSVTAPYKYPRKV 506
|
|
| MACS_like |
cd05972 |
Medium-chain acyl-CoA synthetase (MACS or ACSM); MACS catalyzes the two-step activation of ... |
95-596 |
0e+00 |
|
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: 577.37 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217306889 95 WSFEELGSLSRKFANILSEACsLQRGDRVILILPRVPEWWLANVACLRTGTVLIPGTTQLTQKDILYRLQSSKANCIITN 174
Cdd:cd05972 1 WSFRELKRESAKAANVLAKLG-LRKGDRVAVLLPRVPELWAVILAVIKLGAVYVPLTTLLGPKDIEYRLEAAGAKAIVTD 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217306889 175 Dvlapavdavaskcenlhsklivsensregwgnlkelmkvflchpgwstvarswltatstslvqailsllsswdyrhasd 254
Cdd:cd05972 80 A------------------------------------------------------------------------------- 80
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217306889 255 shtcvktkhNEIMAIFFTSGTSGYPKMTAHTHSsFGLGLSVNGRFWLDLTPSDVMWNTSDTGWAKSAWSSVFSPWIQGAC 334
Cdd:cd05972 81 ---------EDPALIYFTSGTTGLPKGVLHTHS-YPLGHIPTAAYWLGLRPDDIHWNIADPGWAKGAWSSFFGPWLLGAT 150
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217306889 335 VFTHHLPRFEPTSILQTLSKYPITVFCSAPTVYRMLVQNDITSYKFKSLKHCVSAGEPITPDVTEKWRNKTGLDIYEGYG 414
Cdd:cd05972 151 VFVYEGPRFDAERILELLERYGVTSFCGPPTAYRMLIKQDLSSYKFSHLRLVVSAGEPLNPEVIEWWRAATGLPIRDGYG 230
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217306889 415 QTETVLICGNFKGMKIKPGSMGKPSPAFDVKIVDVNGNVLPPGQEGDIGIQVLPNrpfGLFTHYVDNPSKTASTLRGNFY 494
Cdd:cd05972 231 QTETGLTVGNFPDMPVKPGSMGRPTPGYDVAIIDDDGRELPPGEEGDIAIKLPPP---GLFLGYVGDPEKTEASIRGDYY 307
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217306889 495 ITGDRGYMDKDGYFWFVARADDVILSSGYRIGPFEVENALNEHPSVAESAVVSSPDPIRGEVVKAFVVLNPDYKshDQEQ 574
Cdd:cd05972 308 LTGDRAYRDEDGYFWFVGRADDIIKSSGYRIGPFEVESALLEHPAVAEAAVVGSPDPVRGEVVKAFVVLTSGYE--PSEE 385
|
490 500
....*....|....*....|..
gi 2217306889 575 LIKEIQEHVKKTTAPYKYPRKV 596
Cdd:cd05972 386 LAEELQGHVKKVLAPYKYPREI 407
|
|
| Acs |
COG0365 |
Acyl-coenzyme A synthetase/AMP-(fatty) acid ligase [Lipid transport and metabolism]; |
54-596 |
0e+00 |
|
Acyl-coenzyme A synthetase/AMP-(fatty) acid ligase [Lipid transport and metabolism];
Pssm-ID: 440134 [Multi-domain] Cd Length: 565 Bit Score: 545.86 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217306889 54 IPEYFNFAKDVLDQWtdkekAGKKPSNPAFWWINRNGEEMRWSFEELGSLSRKFANILsEACSLQRGDRVILILPRVPEW 133
Cdd:COG0365 4 VGGRLNIAYNCLDRH-----AEGRGDKVALIWEGEDGEERTLTYAELRREVNRFANAL-RALGVKKGDRVAIYLPNIPEA 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217306889 134 WLANVACLRTGTVLIPGTTQLTQKDILYRLQSSKANCIITNDV---------LAPAVDAVASKCENLHSKLIV----SEN 200
Cdd:COG0365 78 VIAMLACARIGAVHSPVFPGFGAEALADRIEDAEAKVLITADGglrggkvidLKEKVDEALEELPSLEHVIVVgrtgADV 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217306889 201 SREGWGNLKELMKvflchpgwstvarswltatstslvqailsllsswdyrHASDSHTCVKTKHNEIMAIFFTSGTSGYPK 280
Cdd:COG0365 158 PMEGDLDWDELLA-------------------------------------AASAEFEPEPTDADDPLFILYTSGTTGKPK 200
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217306889 281 MTAHTHSSFGLGLSVNGRFWLDLTPSDVMWNTSDTGWAKSAWSSVFSPWIQGACVFTHH-LPRF-EPTSILQTLSKYPIT 358
Cdd:COG0365 201 GVVHTHGGYLVHAATTAKYVLDLKPGDVFWCTADIGWATGHSYIVYGPLLNGATVVLYEgRPDFpDPGRLWELIEKYGVT 280
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217306889 359 VFCSAPTVYRMLVQND---ITSYKFKSLKHCVSAGEPITPDVTEKWRNKTGLDIYEGYGQTETV-LICGNFKGMKIKPGS 434
Cdd:COG0365 281 VFFTAPTAIRALMKAGdepLKKYDLSSLRLLGSAGEPLNPEVWEWWYEAVGVPIVDGWGQTETGgIFISNLPGLPVKPGS 360
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217306889 435 MGKPSPAFDVKIVDVNGNVLPPGQEGDIGIQvlpnRPF-GLFTHYVDNPSKTASTLRGNF---YITGDRGYMDKDGYFWF 510
Cdd:COG0365 361 MGKPVPGYDVAVVDEDGNPVPPGEEGELVIK----GPWpGMFRGYWNDPERYRETYFGRFpgwYRTGDGARRDEDGYFWI 436
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217306889 511 VARADDVILSSGYRIGPFEVENALNEHPSVAESAVVSSPDPIRGEVVKAFVVLNPDYKSHDqeQLIKEIQEHVKKTTAPY 590
Cdd:COG0365 437 LGRSDDVINVSGHRIGTAEIESALVSHPAVAEAAVVGVPDEIRGQVVKAFVVLKPGVEPSD--ELAKELQAHVREELGPY 514
|
....*.
gi 2217306889 591 KYPRKV 596
Cdd:COG0365 515 AYPREI 520
|
|
| MACS_AAE_MA_like |
cd05970 |
Medium-chain acyl-CoA synthetase (MACS) of AAE_MA like; MACS catalyzes the two-step activation ... |
43-596 |
0e+00 |
|
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: 544.01 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217306889 43 YESMKQDFKLGIPEYFNFAKDVLDQWtdkekAGKKPSNPAFWWINRNGEEMRWSFEELGSLSRKFANILsEACSLQRGDR 122
Cdd:cd05970 1 YEDFHNNFSINVPENFNFAYDVVDAM-----AKEYPDKLALVWCDDAGEERIFTFAELADYSDKTANFF-KAMGIGKGDT 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217306889 123 VILILPRVPEWWLANVACLRTGTVLIPGTTQLTQKDILYRLQSS--KANCIITNDVLAPAVDAVASKCENLHSKLIVSEN 200
Cdd:cd05970 75 VMLTLKRRYEFWYSLLALHKLGAIAIPATHQLTAKDIVYRIESAdiKMIVAIAEDNIPEEIEKAAPECPSKPKLVWVGDP 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217306889 201 SREGWGNLKELMKVflchpgwstvarswltatstslvqailsllSSWDYRHasdSHTCVKTKHNEIMAIFFTSGTSGYPK 280
Cdd:cd05970 155 VPEGWIDFRKLIKN------------------------------ASPDFER---PTANSYPCGEDILLVYFSSGTTGMPK 201
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217306889 281 MTAHTHSsFGLGLSVNGRFWLDLTPSDVMWNTSDTGWAKSAWSSVFSPWIQGACVFTHHLPRFEPTSILQTLSKYPITVF 360
Cdd:cd05970 202 MVEHDFT-YPLGHIVTAKYWQNVREGGLHLTVADTGWGKAVWGKIYGQWIAGAAVFVYDYDKFDPKALLEKLSKYGVTTF 280
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217306889 361 CSAPTVYRMLVQNDITSYKFKSLKHCVSAGEPITPDVTEKWRNKTGLDIYEGYGQTETVLICGNFKGMKIKPGSMGKPSP 440
Cdd:cd05970 281 CAPPTIYRFLIREDLSRYDLSSLRYCTTAGEALNPEVFNTFKEKTGIKLMEGFGQTETTLTIATFPWMEPKPGSMGKPAP 360
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217306889 441 AFDVKIVDVNGNVLPPGQEGDIGIQVLPNRPFGLFTHYVDNPSKTASTLRGNFYITGDRGYMDKDGYFWFVARADDVILS 520
Cdd:cd05970 361 GYEIDLIDREGRSCEAGEEGEIVIRTSKGKPVGLFGGYYKDAEKTAEVWHDGYYHTGDAAWMDEDGYLWFVGRTDDLIKS 440
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2217306889 521 SGYRIGPFEVENALNEHPSVAESAVVSSPDPIRGEVVKAFVVLNPDYKShdQEQLIKEIQEHVKKTTAPYKYPRKV 596
Cdd:cd05970 441 SGYRIGPFEVESALIQHPAVLECAVTGVPDPIRGQVVKATIVLAKGYEP--SEELKKELQDHVKKVTAPYKYPRIV 514
|
|
| MACS_like_1 |
cd05974 |
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the ... |
96-598 |
5.18e-126 |
|
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: 378.83 E-value: 5.18e-126
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217306889 96 SFEELGSLSRKFANILsEACSLQRGDRVILILPRVPEWWLANVACLRTGTVLIPGTTQLTQKDILYRLQSSKAnciitnd 175
Cdd:cd05974 2 SFAEMSARSSRVANFL-RSIGVGRGDRILLMLGNVVELWEAMLAAMKLGAVVIPATTLLTPDDLRDRVDRGGA------- 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217306889 176 VLAPAVDAVaskcenlhsklivsensregwgnlkelmkvflchpgwstvarswltatstslvqailsllsswdyrHASDS 255
Cdd:cd05974 74 VYAAVDENT------------------------------------------------------------------HADDP 87
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217306889 256 htcvktkhneiMAIFFTSGTSGYPKMTAHTHSSFGLGlSVNGRFWLDLTPSDVMWNTSDTGWAKSAWSSVFSPWIQGACV 335
Cdd:cd05974 88 -----------MLLYFTSGTTSKPKLVEHTHRSYPVG-HLSTMYWIGLKPGDVHWNISSPGWAKHAWSCFFAPWNAGATV 155
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217306889 336 FTHHLPRFEPTSILQTLSKYPITVFCSAPTVYRMLVQNDITSYKFKsLKHCVSAGEPITPDVTEKWRNKTGLDIYEGYGQ 415
Cdd:cd05974 156 FLFNYARFDAKRVLAALVRYGVTTLCAPPTVWRMLIQQDLASFDVK-LREVVGAGEPLNPEVIEQVRRAWGLTIRDGYGQ 234
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217306889 416 TETVLICGNFKGMKIKPGSMGKPSPAFDVKIVDVNGNvlpPGQEGDIGIQVLPNRPFGLFTHYVDNPSKTASTLRGNFYI 495
Cdd:cd05974 235 TETTALVGNSPGQPVKAGSMGRPLPGYRVALLDPDGA---PATEGEVALDLGDTRPVGLMKGYAGDPDKTAHAMRGGYYR 311
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217306889 496 TGDRGYMDKDGYFWFVARADDVILSSGYRIGPFEVENALNEHPSVAESAVVSSPDPIRGEVVKAFVVLNPDYKshDQEQL 575
Cdd:cd05974 312 TGDIAMRDEDGYLTYVGRADDVFKSSDYRISPFELESVLIEHPAVAEAAVVPSPDPVRLSVPKAFIVLRAGYE--PSPET 389
|
490 500
....*....|....*....|...
gi 2217306889 576 IKEIQEHVKKTTAPYKYPRKVGI 598
Cdd:cd05974 390 ALEIFRFSRERLAPYKRIRRLEF 412
|
|
| PRK04319 |
PRK04319 |
acetyl-CoA synthetase; Provisional |
35-594 |
3.20e-124 |
|
acetyl-CoA synthetase; Provisional
Pssm-ID: 235279 [Multi-domain] Cd Length: 570 Bit Score: 379.24 E-value: 3.20e-124
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217306889 35 ATPQNFSnYESMKQDFKLGIPEYFNFAKDVLDQWTDKEKAGKkpsnPAFWWINRNGEEmRWSFEELGSLSRKFANILSEA 114
Cdd:PRK04319 20 ETYATFS-WEEVEKEFSWLETGKVNIAYEAIDRHADGGRKDK----VALRYLDASRKE-KYTYKELKELSNKFANVLKEL 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217306889 115 cSLQRGDRVILILPRVPEWWLANVACLRTGTVLIPGTTQLTQKDILYRLQSSKANCIITNDVLAPAVdaVASKCENLHSK 194
Cdd:PRK04319 94 -GVEKGDRVFIFMPRIPELYFALLGALKNGAIVGPLFEAFMEEAVRDRLEDSEAKVLITTPALLERK--PADDLPSLKHV 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217306889 195 LIVSENSREGWG--NLKELMKvflchpgwstvarswltatstslvqailsllsswdyrHASDSHTCVKTKHNEIMAIFFT 272
Cdd:PRK04319 171 LLVGEDVEEGPGtlDFNALME-------------------------------------QASDEFDIEWTDREDGAILHYT 213
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217306889 273 SGTSGYPKMTAHTHSSFgLGLSVNGRFWLDLTPSDVMWNTSDTGWAKSAWSSVFSPWIQGA--CVFThhlPRFEPTSILQ 350
Cdd:PRK04319 214 SGSTGKPKGVLHVHNAM-LQHYQTGKYVLDLHEDDVYWCTADPGWVTGTSYGIFAPWLNGAtnVIDG---GRFSPERWYR 289
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217306889 351 TLSKYPITVFCSAPTVYRMLVQND---ITSYKFKSLKHCVSAGEPITPDVTeKWRNKT-GLDIYEGYGQTET--VLICgN 424
Cdd:PRK04319 290 ILEDYKVTVWYTAPTAIRMLMGAGddlVKKYDLSSLRHILSVGEPLNPEVV-RWGMKVfGLPIHDNWWMTETggIMIA-N 367
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217306889 425 FKGMKIKPGSMGKPSPAFDVKIVDVNGNVLPPGQEGDIGIQvlPNRPfGLFTHYVDNPSKTASTLRGNFYITGDRGYMDK 504
Cdd:PRK04319 368 YPAMDIKPGSMGKPLPGIEAAIVDDQGNELPPNRMGNLAIK--KGWP-SMMRGIWNNPEKYESYFAGDWYVSGDSAYMDE 444
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217306889 505 DGYFWFVARADDVILSSGYRIGPFEVENALNEHPSVAESAVVSSPDPIRGEVVKAFVVLNPDYKshDQEQLIKEIQEHVK 584
Cdd:PRK04319 445 DGYFWFQGRVDDVIKTSGERVGPFEVESKLMEHPAVAEAGVIGKPDPVRGEIIKAFVALRPGYE--PSEELKEEIRGFVK 522
|
570
....*....|
gi 2217306889 585 KTTAPYKYPR 594
Cdd:PRK04319 523 KGLGAHAAPR 532
|
|
| MACS_like_4 |
cd05969 |
Uncharacterized subfamily of Acetyl-CoA synthetase like family (ACS); This family is most ... |
95-596 |
9.99e-111 |
|
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: 339.86 E-value: 9.99e-111
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217306889 95 WSFEELGSLSRKFANILsEACSLQRGDRVILILPRVPEWWLANVACLRTGTVLIPGTTQLTQKDILYRLQSSKANCIITN 174
Cdd:cd05969 1 YTFAQLKVLSARFANVL-KSLGVGKGDRVFVLSPRSPELYFSMLGIGKIGAVICPLFSAFGPEAIRDRLENSEAKVLITT 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217306889 175 DVLAPavdavaskcenlhsklivsensregwgnlkelmkvflchpgwstvarswltatstslvqailsllsswdyrhasd 254
Cdd:cd05969 80 EELYE--------------------------------------------------------------------------- 84
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217306889 255 shtcvKTKHNEIMAIFFTSGTSGYPKMTAHTHSSFgLGLSVNGRFWLDLTPSDVMWNTSDTGWAKSAWSSVFSPWIQGAC 334
Cdd:cd05969 85 -----RTDPEDPTLLHYTSGTTGTPKGVLHVHDAM-IFYYFTGKYVLDLHPDDIYWCTADPGWVTGTVYGIWAPWLNGVT 158
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217306889 335 VFTHHlPRFEPTSILQTLSKYPITVFCSAPTVYRMLVQNDI---TSYKFKSLKHCVSAGEPITPDVTEKWRNKTGLDIYE 411
Cdd:cd05969 159 NVVYE-GRFDAESWYGIIERVKVTVWYTAPTAIRMLMKEGDelaRKYDLSSLRFIHSVGEPLNPEAIRWGMEVFGVPIHD 237
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217306889 412 GYGQTET--VLICgNFKGMKIKPGSMGKPSPAFDVKIVDVNGNVLPPGQEGDIGIQvlPNRPfGLFTHYVDNPSKTASTL 489
Cdd:cd05969 238 TWWQTETgsIMIA-NYPCMPIKPGSMGKPLPGVKAAVVDENGNELPPGTKGILALK--PGWP-SMFRGIWNDEERYKNSF 313
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217306889 490 RGNFYITGDRGYMDKDGYFWFVARADDVILSSGYRIGPFEVENALNEHPSVAESAVVSSPDPIRGEVVKAFVVLNPDYKS 569
Cdd:cd05969 314 IDGWYLTGDLAYRDEDGYFWFVGRADDIIKTSGHRVGPFEVESALMEHPAVAEAGVIGKPDPLRGEIIKAFISLKEGFEP 393
|
490 500
....*....|....*....|....*..
gi 2217306889 570 hdQEQLIKEIQEHVKKTTAPYKYPRKV 596
Cdd:cd05969 394 --SDELKEEIINFVRQKLGAHVAPREI 418
|
|
| MenE/FadK |
COG0318 |
O-succinylbenzoic acid-CoA ligase MenE or related acyl-CoA synthetase (AMP-forming) [Lipid ... |
63-596 |
3.51e-106 |
|
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: 328.31 E-value: 3.51e-106
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217306889 63 DVLDQWtdkekAGKKPSNPAFWWINRngeemRWSFEELGSLSRKFANILSEACsLQRGDRVILILPRVPEWWLANVACLR 142
Cdd:COG0318 3 DLLRRA-----AARHPDRPALVFGGR-----RLTYAELDARARRLAAALRALG-VGPGDRVALLLPNSPEFVVAFLAALR 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217306889 143 TGTVLIPGTTQLTQKDILYRLQSSKANCIITndvlapavdavaskcenlhsklivsensregwgnlkelmkvflchpgws 222
Cdd:COG0318 72 AGAVVVPLNPRLTAEELAYILEDSGARALVT------------------------------------------------- 102
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217306889 223 tvarswltatstslvqailsllsswdyrhasdshtcvktkhneiMAIFFTSGTSGYPKMTAHTHSSFgLGLSVNGRFWLD 302
Cdd:COG0318 103 --------------------------------------------ALILYTSGTTGRPKGVMLTHRNL-LANAAAIAAALG 137
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217306889 303 LTPSDVMWNTS----DTGWaksaWSSVFSPWIQGACVftHHLPRFEPTSILQTLSKYPITVFCSAPTVYRMLVQN-DITS 377
Cdd:COG0318 138 LTPGDVVLVALplfhVFGL----TVGLLAPLLAGATL--VLLPRFDPERVLELIERERVTVLFGVPTMLARLLRHpEFAR 211
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217306889 378 YKFKSLKHCVSAGEPITPDVTEKWRNKTGLDIYEGYGQTET-VLICGNFKGMK-IKPGSMGKPSPAFDVKIVDVNGNVLP 455
Cdd:COG0318 212 YDLSSLRLVVSGGAPLPPELLERFEERFGVRIVEGYGLTETsPVVTVNPEDPGeRRPGSVGRPLPGVEVRIVDEDGRELP 291
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217306889 456 PGQEGDIGIqvlpnRPFGLFTHYVDNPSKTASTLRGNFYITGDRGYMDKDGYFWFVARADDVILSSGYRIGPFEVENALN 535
Cdd:COG0318 292 PGEVGEIVV-----RGPNVMKGYWNDPEATAEAFRDGWLRTGDLGRLDEDGYLYIVGRKKDMIISGGENVYPAEVEEVLA 366
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2217306889 536 EHPSVAESAVVSSPDPIRGEVVKAFVVLNPDyKSHDQEQLIKEIQEHVkkttAPYKYPRKV 596
Cdd:COG0318 367 AHPGVAEAAVVGVPDEKWGERVVAFVVLRPG-AELDAEELRAFLRERL----ARYKVPRRV 422
|
|
| MACS_like_3 |
cd05971 |
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the ... |
89-596 |
4.42e-103 |
|
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: 320.15 E-value: 4.42e-103
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217306889 89 NGEEMRWSFEELGSLSRKFANILSEAcSLQRGDRVILILPRVPEWWLANVACLRTGTVLIPGTTQLTQKDILYRLQSSKA 168
Cdd:cd05971 1 KGTPEKVTFKELKTASNRFANVLKEI-GLEKGDRVGVFLSQGPECAIAHIAILRSGAIAVPLFALFGPEALEYRLSNSGA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217306889 169 NCIITNDVLAPAVdavaskcenlhsklivsensregwgnlkelmkvflchpgwstvarswltatstslvqailsllsswd 248
Cdd:cd05971 80 SALVTDGSDDPAL------------------------------------------------------------------- 92
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217306889 249 yrhasdshtcvktkhneimaIFFTSGTSGYPKMTAHTHSsFGLGLSVNGRFWLDLTP--SDVMWNTSDTGWAKSAWSSVF 326
Cdd:cd05971 93 --------------------IIYTSGTTGPPKGALHAHR-VLLGHLPGVQFPFNLFPrdGDLYWTPADWAWIGGLLDVLL 151
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217306889 327 SPWIQGACVFTHHLPRFEPTSILQTLSKYPITVFCSAPTVYRML-VQNDITSYKFKSLKHCVSAGEPITPDVTEKWRNKT 405
Cdd:cd05971 152 PSLYFGVPVLAHRMTKFDPKAALDLMSRYGVTTAFLPPTALKMMrQQGEQLKHAQVKLRAIATGGESLGEELLGWAREQF 231
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217306889 406 GLDIYEGYGQTETVLICGNFKG-MKIKPGSMGKPSPAFDVKIVDVNGNVLPPGQEGDIGIQvLPNrPFGLFThYVDNPSK 484
Cdd:cd05971 232 GVEVNEFYGQTECNLVIGNCSAlFPIKPGSMGKPIPGHRVAIVDDNGTPLPPGEVGEIAVE-LPD-PVAFLG-YWNNPSA 308
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217306889 485 TASTLRGNFYITGDRGYMDKDGYFWFVARADDVILSSGYRIGPFEVENALNEHPSVAESAVVSSPDPIRGEVVKAFVVLN 564
Cdd:cd05971 309 TEKKMAGDWLLTGDLGRKDSDGYFWYVGRDDDVITSSGYRIGPAEIEECLLKHPAVLMAAVVGIPDPIRGEIVKAFVVLN 388
|
490 500 510
....*....|....*....|....*....|..
gi 2217306889 565 PDYKshDQEQLIKEIQEHVKKTTAPYKYPRKV 596
Cdd:cd05971 389 PGET--PSDALAREIQELVKTRLAAHEYPREI 418
|
|
| AFD_class_I |
cd04433 |
Adenylate forming domain, Class I, also known as the ANL superfamily; This family is known as ... |
265-596 |
5.85e-97 |
|
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: 300.36 E-value: 5.85e-97
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217306889 265 EIMAIFFTSGTSGYPKMTAHTHSSFgLGLSVNGRFWLDLTPSDVMWNTSDTGWAkSAWSSVFSPWIQGACVFTHhlPRFE 344
Cdd:cd04433 1 DPALILYTSGTTGKPKGVVLSHRNL-LAAAAALAASGGLTEGDVFLSTLPLFHI-GGLFGLLGALLAGGTVVLL--PKFD 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217306889 345 PTSILQTLSKYPITVFCSAPTVYRMLVQND-ITSYKFKSLKHCVSAGEPITPDVTEKWRNKTGLDIYEGYGQTET--VLI 421
Cdd:cd04433 77 PEAALELIEREKVTILLGVPTLLARLLKAPeSAGYDLSSLRALVSGGAPLPPELLERFEEAPGIKLVNGYGLTETggTVA 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217306889 422 CGNFKGMKIKPGSMGKPSPAFDVKIVDVNGNVLPPGQEGDIGIQvLPNRPFGlfthYVDNPSKTASTLRGNFYITGDRGY 501
Cdd:cd04433 157 TGPPDDDARKPGSVGRPVPGVEVRIVDPDGGELPPGEIGELVVR-GPSVMKG----YWNNPEATAAVDEDGWYRTGDLGR 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217306889 502 MDKDGYFWFVARADDVILSSGYRIGPFEVENALNEHPSVAESAVVSSPDPIRGEVVKAFVVLNPdykshDQEQLIKEIQE 581
Cdd:cd04433 232 LDEDGYLYIVGRLKDMIKSGGENVYPAEVEAVLLGHPGVAEAAVVGVPDPEWGERVVAVVVLRP-----GADLDAEELRA 306
|
330
....*....|....*
gi 2217306889 582 HVKKTTAPYKYPRKV 596
Cdd:cd04433 307 HVRERLAPYKVPRRV 321
|
|
| MACS_like_2 |
cd05973 |
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the ... |
96-596 |
8.05e-93 |
|
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: 293.27 E-value: 8.05e-93
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217306889 96 SFEELGSLSRKFANILSEAcSLQRGDRVILILPRVPEWWLANVACLRTGTVLIPGTTQLTQKDILYRLQSSKANCIITND 175
Cdd:cd05973 2 TFGELRALSARFANALQEL-GVGPGDVVAGLLPRTPELVVTILGIWRLGAVYQPLFTAFGPKAIEHRLRTSGARLVVTDA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217306889 176 vlapavdavaskcenlhsklivsensregwgnlkelmkvflchpgwstvarswltatstslvqailsllsswDYRHASDS 255
Cdd:cd05973 81 ------------------------------------------------------------------------ANRHKLDS 88
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217306889 256 HTCVktkhneimaIFFTSGTSGYPKMTAHTHSSFgLGLSVNGRFWLDLTPSDVMWNTSDTGWAKSAWSSVFSPWIQGACV 335
Cdd:cd05973 89 DPFV---------MMFTSGTTGLPKGVPVPLRAL-AAFGAYLRDAVDLRPEDSFWNAADPGWAYGLYYAITGPLALGHPT 158
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217306889 336 FTHHLPrFEPTSILQTLSKYPITVFCSAPTVYRMLVQNDITSYKFK--SLKHCVSAGEPITPDVTEKWRNKTGLDIYEGY 413
Cdd:cd05973 159 ILLEGG-FSVESTWRVIERLGVTNLAGSPTAYRLLMAAGAEVPARPkgRLRRVSSAGEPLTPEVIRWFDAALGVPIHDHY 237
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217306889 414 GQTETVLICGNFKGMK--IKPGSMGKPSPAFDVKIVDVNGNVLPPGQEGDIGIQVlPNRPFGLFTHYVDNPSKTAStlrG 491
Cdd:cd05973 238 GQTELGMVLANHHALEhpVHAGSAGRAMPGWRVAVLDDDGDELGPGEPGRLAIDI-ANSPLMWFRGYQLPDTPAID---G 313
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217306889 492 NFYITGDRGYMDKDGYFWFVARADDVILSSGYRIGPFEVENALNEHPSVAESAVVSSPDPIRGEVVKAFVVLNPDYKShd 571
Cdd:cd05973 314 GYYLTGDTVEFDPDGSFSFIGRADDVITMSGYRIGPFDVESALIEHPAVAEAAVIGVPDPERTEVVKAFVVLRGGHEG-- 391
|
490 500
....*....|....*....|....*
gi 2217306889 572 QEQLIKEIQEHVKKTTAPYKYPRKV 596
Cdd:cd05973 392 TPALADELQLHVKKRLSAHAYPRTI 416
|
|
| FC-FACS_FadD_like |
cd05936 |
Prokaryotic long-chain fatty acid CoA synthetases similar to Escherichia coli FadD; This ... |
63-596 |
3.71e-92 |
|
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: 292.54 E-value: 3.71e-92
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217306889 63 DVLDqwtdkEKAGKKPSNPAFWWINRngeemRWSFEELGSLSRKFANILSEAcSLQRGDRVILILPRVPEWWLANVACLR 142
Cdd:cd05936 3 DLLE-----EAARRFPDKTALIFMGR-----KLTYRELDALAEAFAAGLQNL-GVQPGDRVALMLPNCPQFPIAYFGALK 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217306889 143 TGTVLIPGTTQLTQKDILYRLQSSKANCIItndvlapavdavaskcenlhsklivsensregwgnlkelmkvflchpgws 222
Cdd:cd05936 72 AGAVVVPLNPLYTPRELEHILNDSGAKALI-------------------------------------------------- 101
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217306889 223 tVARSWLTATSTslvqaiLSLLSSWDYRHASDshtcvktkhneIMAIFFTSGTSGYPKMTAHTHSSFGLGLSVNgRFWL- 301
Cdd:cd05936 102 -VAVSFTDLLAA------GAPLGERVALTPED-----------VAVLQYTSGTTGVPKGAMLTHRNLVANALQI-KAWLe 162
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217306889 302 -DLTPSDVMWNT-------SDTgwaksawSSVFSPWIQGACVFThhLPRFEPTSILQTLSKYPITVFCSAPTVYRMLVQN 373
Cdd:cd05936 163 dLLEGDDVVLAAlplfhvfGLT-------VALLLPLALGATIVL--IPRFRPIGVLKEIRKHRVTIFPGVPTMYIALLNA 233
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217306889 374 -DITSYKFKSLKHCVSAGEPITPDVTEKWRNKTGLDIYEGYGQTETV-LICGNFKGMKIKPGSMGKPSPAFDVKIVDVNG 451
Cdd:cd05936 234 pEFKKRDFSSLRLCISGGAPLPVEVAERFEELTGVPIVEGYGLTETSpVVAVNPLDGPRKPGSIGIPLPGTEVKIVDDDG 313
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217306889 452 NVLPPGQEGDI---GIQVlpnrpfglFTHYVDNPSKTASTLRGNFYITGDRGYMDKDGYFWFVARADDVILSSGYRIGPF 528
Cdd:cd05936 314 EELPPGEVGELwvrGPQV--------MKGYWNRPEETAEAFVDGWLRTGDIGYMDEDGYFFIVDRKKDMIIVGGFNVYPR 385
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2217306889 529 EVENALNEHPSVAESAVVSSPDPIRGEVVKAFVVLNPDykshdqEQLIK-EIQEHVKKTTAPYKYPRKV 596
Cdd:cd05936 386 EVEEVLYEHPAVAEAAVVGVPDPYSGEAVKAFVVLKEG------ASLTEeEIIAFCREQLAGYKVPRQV 448
|
|
| BCL_4HBCL |
cd05959 |
Benzoate CoA ligase (BCL) and 4-Hydroxybenzoate-Coenzyme A Ligase (4-HBA-CoA ligase); Benzoate ... |
56-596 |
1.90e-89 |
|
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: 286.96 E-value: 1.90e-89
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217306889 56 EYFNFAKDVLDQwTDKEKAGKkpsnPAFwwINRNGEemrWSFEELGSLSRKFANILSEAcSLQRGDRVILILPRVPEWWL 135
Cdd:cd05959 1 EKYNAATLVDLN-LNEGRGDK----TAF--IDDAGS---LTYAELEAEARRVAGALRAL-GVKREERVLLIMLDTVDFPT 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217306889 136 ANVACLRTGTVLIPGTTQLTQKDILYRLQSSKANCIITNDVLAPAVDAVASKCENLHSKLIVSENSREGWGnlkelmkvf 215
Cdd:cd05959 70 AFLGAIRAGIVPVPVNTLLTPDDYAYYLEDSRARVVVVSGELAPVLAAALTKSEHTLVVLIVSGGAGPEAG--------- 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217306889 216 lchpgwstvaRSWLTAtstslvqailsllsswDYRHASDSHTCVKTKHNEIMAIFFTSGTSGYPKMTAHTHSSFGLGLSV 295
Cdd:cd05959 141 ----------ALLLAE----------------LVAAEAEQLKPAATHADDPAFWLYSSGSTGRPKGVVHLHADIYWTAEL 194
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217306889 296 NGRFWLDLTPSDVMWNTSDTGWAKSAWSSVFSP-WIQGACVFthhLP-RFEPTSILQTLSKYPITVFCSAPTVYR-MLVQ 372
Cdd:cd05959 195 YARNVLGIREDDVCFSAAKLFFAYGLGNSLTFPlSVGATTVL---MPeRPTPAAVFKRIRRYRPTVFFGVPTLYAaMLAA 271
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217306889 373 NDITSYKFKSLKHCVSAGEPITPDVTEKWRNKTGLDIYEGYGQTETVLI-CGNFKGmKIKPGSMGKPSPAFDVKIVDVNG 451
Cdd:cd05959 272 PNLPSRDLSSLRLCVSAGEALPAEVGERWKARFGLDILDGIGSTEMLHIfLSNRPG-RVRYGTTGKPVPGYEVELRDEDG 350
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217306889 452 NVLPPGQEGDIGIqvlpnRPFGLFTHYVDNPSKTASTLRGNFYITGDRGYMDKDGYFWFVARADDVILSSGYRIGPFEVE 531
Cdd:cd05959 351 GDVADGEPGELYV-----RGPSSATMYWNNRDKTRDTFQGEWTRTGDKYVRDDDGFYTYAGRADDMLKVSGIWVSPFEVE 425
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2217306889 532 NALNEHPSVAESAVVSSPDPIRGEVVKAFVVLNPDYKshDQEQLIKEIQEHVKKTTAPYKYPRKV 596
Cdd:cd05959 426 SALVQHPAVLEAAVVGVEDEDGLTKPKAFVVLRPGYE--DSEALEEELKEFVKDRLAPYKYPRWI 488
|
|
| ABCL |
cd05958 |
2-aminobenzoate-CoA ligase (ABCL); ABCL catalyzes the initial step in the 2-aminobenzoate ... |
92-596 |
7.36e-81 |
|
2-aminobenzoate-CoA ligase (ABCL); ABCL catalyzes the initial step in the 2-aminobenzoate aerobic degradation pathway by activating 2-aminobenzoate to 2-aminobenzoyl-CoA. The reaction is carried out via a two-step process; the first step is ATP-dependent and forms a 2-aminobenzoyl-AMP intermediate, and the second step forms the 2-aminobenzoyl-CoA ester and releases the AMP. 2-Aminobenzoyl-CoA is further converted to 2-amino-5-oxo-cyclohex-1-ene-1-carbonyl-CoA catalyzed by 2-aminobenzoyl-CoA monooxygenase/reductase. ABCL has been purified from cells aerobically grown with 2-aminobenzoate as sole carbon, energy, and nitrogen source, and has been characterized as a monomer.
Pssm-ID: 341268 [Multi-domain] Cd Length: 439 Bit Score: 262.03 E-value: 7.36e-81
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217306889 92 EMRWSFEELGSLSRKFANILSEACSLQRGDRVILILPRVPEWWLANVACLRTGTVLIPGTTQLTQKDILYRLQsskaNCI 171
Cdd:cd05958 8 EREWTYRDLLALANRIANVLVGELGIVPGNRVLLRGSNSPELVACWFGIQKAGAIAVATMPLLRPKELAYILD----KAR 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217306889 172 ITNDVLAPAVDAVaskcenlhsklivsensregwgnlkelmkvflchpgwstvarswltatstslvqailsllsswdyrh 251
Cdd:cd05958 84 ITVALCAHALTAS------------------------------------------------------------------- 96
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217306889 252 asdshtcvktkhNEIMAIFFTSGTSGYPKMTAHTHSSFGLGLSVNGRFWLDLTPSDVMWNTSDTGWAKSAWSSVFSPWIQ 331
Cdd:cd05958 97 ------------DDICILAFTSGTTGAPKATMHFHRDPLASADRYAVNVLRLREDDRFVGSPPLAFTFGLGGVLLFPFGV 164
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217306889 332 GACVFThhLPRFEPTSILQTLSKYPITVFCSAPTVYR-MLVQNDITSYKFKSLKHCVSAGEPITPDVTEKWRNKTGLDIY 410
Cdd:cd05958 165 GASGVL--LEEATPDLLLSAIARYKPTVLFTAPTAYRaMLAHPDAAGPDLSSLRKCVSAGEALPAALHRAWKEATGIPII 242
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217306889 411 EGYGQTETVLICGNFKGMKIKPGSMGKPSPAFDVKIVDVNGNVLPPGQEGDIGIQvlpnRPFGLftHYVDNPSKtASTLR 490
Cdd:cd05958 243 DGIGSTEMFHIFISARPGDARPGATGKPVPGYEAKVVDDEGNPVPDGTIGRLAVR----GPTGC--RYLADKRQ-RTYVQ 315
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217306889 491 GNFYITGDRGYMDKDGYFWFVARADDVILSSGYRIGPFEVENALNEHPSVAESAVVSSPDPIRGEVVKAFVVLNPDYKSh 570
Cdd:cd05958 316 GGWNITGDTYSRDPDGYFRHQGRSDDMIVSGGYNIAPPEVEDVLLQHPAVAECAVVGHPDESRGVVVKAFVVLRPGVIP- 394
|
490 500
....*....|....*....|....*.
gi 2217306889 571 dQEQLIKEIQEHVKKTTAPYKYPRKV 596
Cdd:cd05958 395 -GPVLARELQDHAKAHIAPYKYPRAI 419
|
|
| PRK06187 |
PRK06187 |
long-chain-fatty-acid--CoA ligase; Validated |
62-596 |
9.17e-76 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 235730 [Multi-domain] Cd Length: 521 Bit Score: 251.26 E-value: 9.17e-76
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217306889 62 KDVLDQWtdkekAGKKPSNPAFWWinrngEEMRWSFEELGSLSRKFANILsEACSLQRGDRVILILPRVPEWWLANVACL 141
Cdd:PRK06187 9 GRILRHG-----ARKHPDKEAVYF-----DGRRTTYAELDERVNRLANAL-RALGVKKGDRVAVFDWNSHEYLEAYFAVP 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217306889 142 RTGTVLIPGTTQLTQKDILYRLQSSKANCIITNDVLAPAVDAVASKCENLHSKLIVSENSREG----WGNLKELMKvflc 217
Cdd:PRK06187 78 KIGAVLHPINIRLKPEEIAYILNDAEDRVVLVDSEFVPLLAAILPQLPTVRTVIVEGDGPAAPlapeVGEYEELLA---- 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217306889 218 hpgwstvarswltatstslvqailsllsswdyrHASDSHTCVKTKHNEIMAIFFTSGTSGYPKMTAHTHSSFgLGLSVNG 297
Cdd:PRK06187 154 ---------------------------------AASDTFDFPDIDENDAAAMLYTSGTTGHPKGVVLSHRNL-FLHSLAV 199
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217306889 298 RFWLDLTPSDV------MWNTSDTGWAksawssvFSPWIQGAcvfTHHLP-RFEPTSILQTLSKYPITVFCSAPTVYRML 370
Cdd:PRK06187 200 CAWLKLSRDDVylvivpMFHVHAWGLP-------YLALMAGA---KQVIPrRFDPENLLDLIETERVTFFFAVPTIWQML 269
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217306889 371 VQNDITS-YKFKSLKHCVSAGEPITPDVTEKWRNKTGLDIYEGYGQTETV-LICGNF-----KGMKIKPGSMGKPSPAFD 443
Cdd:PRK06187 270 LKAPRAYfVDFSSLRLVIYGGAALPPALLREFKEKFGIDLVQGYGMTETSpVVSVLPpedqlPGQWTKRRSAGRPLPGVE 349
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217306889 444 VKIVDVNGNVLPPGqEGDIG-IQVL-PNRPFGlfthYVDNPSKTASTLRGNFYITGDRGYMDKDGYFWFVARADDVILSS 521
Cdd:PRK06187 350 ARIVDDDGDELPPD-GGEVGeIIVRgPWLMQG----YWNRPEATAETIDGGWLHTGDVGYIDEDGYLYITDRIKDVIISG 424
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2217306889 522 GYRIGPFEVENALNEHPSVAESAVVSSPDPIRGEVVKAFVVLNPDyKSHDQEQLIKEIQEHVkkttAPYKYPRKV 596
Cdd:PRK06187 425 GENIYPRELEDALYGHPAVAEVAVIGVPDEKWGERPVAVVVLKPG-ATLDAKELRAFLRGRL----AKFKLPKRI 494
|
|
| AMP-binding |
pfam00501 |
AMP-binding enzyme; |
72-521 |
3.04e-71 |
|
AMP-binding enzyme;
Pssm-ID: 459834 [Multi-domain] Cd Length: 417 Bit Score: 236.05 E-value: 3.04e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217306889 72 EKAGKKPSNPAFwwinRNGEEMRWSFEELGSLSRKFANILsEACSLQRGDRVILILPRVPEWWLANVACLRTGTVLIPGT 151
Cdd:pfam00501 3 RQAARTPDKTAL----EVGEGRRLTYRELDERANRLAAGL-RALGVGKGDRVAILLPNSPEWVVAFLACLKAGAVYVPLN 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217306889 152 TQLTQKDILYRLQSSKANCIITNDVL-APAVDAVASKCENLHSKLIVSENSREGWGNLKElmkvflchpgwstvarswlt 230
Cdd:pfam00501 78 PRLPAEELAYILEDSGAKVLITDDALkLEELLEALGKLEVVKLVLVLDRDPVLKEEPLPE-------------------- 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217306889 231 atstslvqailsllssWDYRHASDSHTCVKTKHNEIMAIFFTSGTSGYPKMTAHTH---SSFGLGLSVNGRFWLDLTPSD 307
Cdd:pfam00501 138 ----------------EAKPADVPPPPPPPPDPDDLAYIIYTSGTTGKPKGVMLTHrnlVANVLSIKRVRPRGFGLGPDD 201
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217306889 308 VMWNTSDTGWAKSAWSSVFSPWIQGA-CVFTHHLPRFEPTSILQTLSKYPITVFCSAPTVYRMLVQN-DITSYKFKSLKH 385
Cdd:pfam00501 202 RVLSTLPLFHDFGLSLGLLGPLLAGAtVVLPPGFPALDPAALLELIERYKVTVLYGVPTLLNMLLEAgAPKRALLSSLRL 281
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217306889 386 CVSAGEPITPDVTEKWRNKTGLDIYEGYGQTET---VLICGNFKGMKIKPGSMGKPSPAFDVKIVDVN-GNVLPPGQEGD 461
Cdd:pfam00501 282 VLSGGAPLPPELARRFRELFGGALVNGYGLTETtgvVTTPLPLDEDLRSLGSVGRPLPGTEVKIVDDEtGEPVPPGEPGE 361
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2217306889 462 I---GIQVLPnrpfGlfthYVDNPSKTASTL-RGNFYITGDRGYMDKDGYFWFVARADDVILSS 521
Cdd:pfam00501 362 LcvrGPGVMK----G----YLNDPELTAEAFdEDGWYRTGDLGRRDEDGYLEIVGRKKDQIKLG 417
|
|
| FACL_FadD13-like |
cd17631 |
fatty acyl-CoA synthetase, including FadD13; This family contains fatty acyl-CoA synthetases, ... |
74-596 |
9.12e-69 |
|
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: 230.19 E-value: 9.12e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217306889 74 AGKKPSNPAFWWINRngeemRWSFEELGSLSRKFANILSEAcSLQRGDRVILILPRVPEWWLANVACLRTGTVLIPGTTQ 153
Cdd:cd17631 5 ARRHPDRTALVFGGR-----SLTYAELDERVNRLAHALRAL-GVAKGDRVAVLSKNSPEFLELLFAAARLGAVFVPLNFR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217306889 154 LTQKDILYRLQSSKAnciitndvlapavdavaskcenlhsKLIVSENSRegwgnlkelmkvflchpgwstvarswltats 233
Cdd:cd17631 79 LTPPEVAYILADSGA-------------------------KVLFDDLAL------------------------------- 102
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217306889 234 tslvqailsllsswdyrhasdshtcvktkhneimaIFFTSGTSGYPKMTAHTHSSFgLGLSVNGRFWLDLTPSDV----- 308
Cdd:cd17631 103 -----------------------------------LMYTSGTTGRPKGAMLTHRNL-LWNAVNALAALDLGPDDVllvva 146
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217306889 309 -MWNTSDTGwaksawssVFSPWIQGACVFTHHLPRFEPTSILQTLSKYPITVFCSAPTVYRMLVQN-DITSYKFKSLKHC 386
Cdd:cd17631 147 pLFHIGGLG--------VFTLPTLLRGGTVVILRKFDPETVLDLIERHRVTSFFLVPTMIQALLQHpRFATTDLSSLRAV 218
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217306889 387 VSAGEPITPDVTEKWRnKTGLDIYEGYGQTETV-LICGNFKGMKI-KPGSMGKPSPAFDVKIVDVNGNVLPPGQEGDIGI 464
Cdd:cd17631 219 IYGGAPMPERLLRALQ-ARGVKFVQGYGMTETSpGVTFLSPEDHRrKLGSAGRPVFFVEVRIVDPDGREVPPGEVGEIVV 297
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217306889 465 QVlPNrpfgLFTHYVDNPSKTASTLRGNFYITGDRGYMDKDGYFWFVARADDVILSSGYRIGPFEVENALNEHPSVAESA 544
Cdd:cd17631 298 RG-PH----VMAGYWNRPEATAAAFRDGWFHTGDLGRLDEDGYLYIVDRKKDMIISGGENVYPAEVEDVLYEHPAVAEVA 372
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|..
gi 2217306889 545 VVSSPDPIRGEVVKAFVVLNPDyKSHDQEQLIkeiqEHVKKTTAPYKYPRKV 596
Cdd:cd17631 373 VIGVPDEKWGEAVVAVVVPRPG-AELDEDELI----AHCRERLARYKIPKSV 419
|
|
| BCL_like |
cd05919 |
Benzoate CoA ligase (BCL) and similar adenylate forming enzymes; This family contains benzoate ... |
96-599 |
3.89e-68 |
|
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: 228.50 E-value: 3.89e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217306889 96 SFEELGSLSRKFANILsEACSLQRGDRVILILPRVPEWWLANVACLRTGTVLIPGTTQLTQKDILYRLQSSKANCIITND 175
Cdd:cd05919 12 TYGQLHDGANRLGSAL-RNLGVSSGDRVLLLMLDSPELVQLFLGCLARGAIAVVINPLLHPDDYAYIARDCEARLVVTSA 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217306889 176 vlapavDAVASkcenlhsklivsensregwgnlkelmkvflchpgwstvarswltatstslvqailsllssWDYrhasds 255
Cdd:cd05919 91 ------DDIAY------------------------------------------------------------LLY------ 98
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217306889 256 htcvktkhneimaiffTSGTSGYPKMTAHTHSSFGLGLSVNGRFWLDLTPSDVMWNTSDTGWAKSAWSSVFSPWIQGACV 335
Cdd:cd05919 99 ----------------SSGTTGPPKGVMHAHRDPLLFADAMAREALGLTPGDRVFSSAKMFFGYGLGNSLWFPLAVGASA 162
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217306889 336 FTHHLPRfEPTSILQTLSKYPITVFCSAPTVY-RMLVQNDITSYKFKSLKHCVSAGEPITPDVTEKWRNKTGLDIYEGYG 414
Cdd:cd05919 163 VLNPGWP-TAERVLATLARFRPTVLYGVPTFYaNLLDSCAGSPDALRSLRLCVSAGEALPRGLGERWMEHFGGPILDGIG 241
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217306889 415 QTETVLICGNFKGMKIKPGSMGKPSPAFDVKIVDVNGNVLPPGQEGDIGIqvlpnRPFGLFTHYVDNPSKTASTLRGNFY 494
Cdd:cd05919 242 ATEVGHIFLSNRPGAWRLGSTGRPVPGYEIRLVDEEGHTIPPGEEGDLLV-----RGPSAAVGYWNNPEKSRATFNGGWY 316
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217306889 495 ITGDRGYMDKDGYFWFVARADDVILSSGYRIGPFEVENALNEHPSVAESAVVSSPDPIRGEVVKAFVVLNPDYKShdQEQ 574
Cdd:cd05919 317 RTGDKFCRDADGWYTHAGRADDMLKVGGQWVSPVEVESLIIQHPAVAEAAVVAVPESTGLSRLTAFVVLKSPAAP--QES 394
|
490 500
....*....|....*....|....*
gi 2217306889 575 LIKEIQEHVKKTTAPYKYPRKVGIL 599
Cdd:cd05919 395 LARDIHRHLLERLSAHKVPRRIAFV 419
|
|
| PRK07656 |
PRK07656 |
long-chain-fatty-acid--CoA ligase; Validated |
74-599 |
8.36e-68 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236072 [Multi-domain] Cd Length: 513 Bit Score: 229.79 E-value: 8.36e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217306889 74 AGKKPSNPAFWWinrngEEMRWSFEELGSLSRKFANILsEACSLQRGDRVILILPRVPEWWLANVACLRTGTVLIPGTTQ 153
Cdd:PRK07656 15 ARRFGDKEAYVF-----GDQRLTYAELNARVRRAAAAL-AALGIGKGDRVAIWAPNSPHWVIAALGALKAGAVVVPLNTR 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217306889 154 LTQKDILYRLQSSKANCIITNDVLAPAVDAVASKCENLHSKLIVSENSREGwgnLKELMKVFlchpgwstvaRSWLTATS 233
Cdd:PRK07656 89 YTADEAAYILARGDAKALFVLGLFLGVDYSATTRLPALEHVVICETEEDDP---HTEKMKTF----------TDFLAAGD 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217306889 234 TSLVQAILsllsswdyrHASDshtcvktkhneIMAIFFTSGTSGYPK--MTAHTHSsfglgLSvNGRFW---LDLTPSD- 307
Cdd:PRK07656 156 PAERAPEV---------DPDD-----------VADILFTSGTTGRPKgaMLTHRQL-----LS-NAADWaeyLGLTEGDr 209
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217306889 308 --------------VMWNTsdtgwaksawssvfsPWIQGACVFTHhlPRFEPTSILQTLSKYPITVFCSAPTVYRMLVQN 373
Cdd:PRK07656 210 ylaanpffhvfgykAGVNA---------------PLMRGATILPL--PVFDPDEVFRLIETERITVLPGPPTMYNSLLQH 272
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217306889 374 -DITSYKFKSLKHCVSAGEPITPDVTEKWRNKTGLDIY-EGYGQTE---TVLICGNFKGMKIKPGSMGKPSPAFDVKIVD 448
Cdd:PRK07656 273 pDRSAEDLSSLRLAVTGAASMPVALLERFESELGVDIVlTGYGLSEasgVTTFNRLDDDRKTVAGTIGTAIAGVENKIVN 352
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217306889 449 VNGNVLPPGQEGDIGIqvlpnRPFGLFTHYVDNPSKTASTLRGNFYI-TGDRGYMDKDGYFWFVARADDVILSSGYRIGP 527
Cdd:PRK07656 353 ELGEEVPVGEVGELLV-----RGPNVMKGYYDDPEATAAAIDADGWLhTGDLGRLDEEGYLYIVDRKKDMFIVGGFNVYP 427
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2217306889 528 FEVENALNEHPSVAESAVVSSPDPIRGEVVKAFVVLNPDyKSHDQEQLIKEIQEHVkkttAPYKYPRKVGIL 599
Cdd:PRK07656 428 AEVEEVLYEHPAVAEAAVIGVPDERLGEVGKAYVVLKPG-AELTEEELIAYCREHL----AKYKVPRSIEFL 494
|
|
| PRK08314 |
PRK08314 |
long-chain-fatty-acid--CoA ligase; Validated |
78-596 |
1.27e-67 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236235 [Multi-domain] Cd Length: 546 Bit Score: 230.23 E-value: 1.27e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217306889 78 PSNPAFWWINRngeemRWSFEELGSLSRKFANILSEACSLQRGDRVILILPRVPEWWLANVACLRTGTVLIPGTTQLTQK 157
Cdd:PRK08314 24 PDKTAIVFYGR-----AISYRELLEEAERLAGYLQQECGVRKGDRVLLYMQNSPQFVIAYYAILRANAVVVPVNPMNREE 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217306889 158 DILYRLQSSKANCIITNDVLAPAVDAVASKCENLHskLIVSENSregwGNLKELMKVFLchPGWSTVARSwLTATSTSLV 237
Cdd:PRK08314 99 ELAHYVTDSGARVAIVGSELAPKVAPAVGNLRLRH--VIVAQYS----DYLPAEPEIAV--PAWLRAEPP-LQALAPGGV 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217306889 238 QAILSLLSSwdyRHASDSHTcvkTKHNEIMAIFFTSGTSGYPKMTAHTHSSFgLGLSVNGRFWLDLTPSDVMWNTSD--- 314
Cdd:PRK08314 170 VAWKEALAA---GLAPPPHT---AGPDDLAVLPYTSGTTGVPKGCMHTHRTV-MANAVGSVLWSNSTPESVVLAVLPlfh 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217306889 315 -TGWAKSAWSSVFSpwiqGACVFThhLPRFEPTSILQTLSKYPITVFCSAPTvyrMLV----QNDITSYKFKSLKHCVSA 389
Cdd:PRK08314 243 vTGMVHSMNAPIYA----GATVVL--MPRWDREAAARLIERYRVTHWTNIPT---MVVdflaSPGLAERDLSSLRYIGGG 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217306889 390 GEPITPDVTEKWRNKTGLDIYEGYGQTETV-LICGNFKGmKIKPGSMGKPSPAFDVKIVD-VNGNVLPPGQEGDI---GI 464
Cdd:PRK08314 314 GAAMPEAVAERLKELTGLDYVEGYGLTETMaQTHSNPPD-RPKLQCLGIPTFGVDARVIDpETLEELPPGEVGEIvvhGP 392
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217306889 465 QVlpnrpfglFTHYVDNPSKTAS---TLRGN-FYITGDRGYMDKDGYFWFVARADDVILSSGYRIGPFEVENALNEHPSV 540
Cdd:PRK08314 393 QV--------FKGYWNRPEATAEafiEIDGKrFFRTGDLGRMDEEGYFFITDRLKRMINASGFKVWPAEVENLLYKHPAI 464
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*.
gi 2217306889 541 AESAVVSSPDPIRGEVVKAFVVLNPDYKSHDQEQlikEIQEHVKKTTAPYKYPRKV 596
Cdd:PRK08314 465 QEACVIATPDPRRGETVKAVVVLRPEARGKTTEE---EIIAWAREHMAAYKYPRIV 517
|
|
| ACS |
cd05966 |
Acetyl-CoA synthetase (also known as acetate-CoA ligase and acetyl-activating enzyme); ... |
59-596 |
1.42e-67 |
|
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: 231.68 E-value: 1.42e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217306889 59 NFAKDVLDQWtdkekAGKKPSNPAFWWINRNGEEMR-WSFEELGSLSRKFANILSEAcSLQRGDRVILILPRVPEWWLAN 137
Cdd:cd05966 53 NISYNCLDRH-----LKERGDKVAIIWEGDEPDQSRtITYRELLREVCRFANVLKSL-GVKKGDRVAIYMPMIPELVIAM 126
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217306889 138 VACLRTG---TVLIPGttqLTQKDILYRLQSSKANCIITND---------VLAPAVDAVASKCENLHsKLIVSENSregw 205
Cdd:cd05966 127 LACARIGavhSVVFAG---FSAESLADRINDAQCKLVITADggyrggkviPLKEIVDEALEKCPSVE-KVLVVKRT---- 198
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217306889 206 gNLKELMkvflcHPG----WSTVARSwltatstslvqailsllsswdyrhASDSHTCVKTKHNEIMAIFFTSGTSGYPKM 281
Cdd:cd05966 199 -GGEVPM-----TEGrdlwWHDLMAK------------------------QSPECEPEWMDSEDPLFILYTSGSTGKPKG 248
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217306889 282 TAHTHSSFGLGLSVNGRFWLDLTPSDVMWNTSDTGWAKSAWSSVFSPWIQGACVFThhlprFE--PT--------SILQt 351
Cdd:cd05966 249 VVHTTGGYLLYAATTFKYVFDYHPDDIYWCTADIGWITGHSYIVYGPLANGATTVM-----FEgtPTypdpgrywDIVE- 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217306889 352 lsKYPITVFCSAPTVYRMLVQ---NDITSYKFKSLKHCVSAGEPITPdvtEKWR---NKTG---LDIYEGYGQTETVLIC 422
Cdd:cd05966 323 --KHKVTIFYTAPTAIRALMKfgdEWVKKHDLSSLRVLGSVGEPINP---EAWMwyyEVIGkerCPIVDTWWQTETGGIM 397
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217306889 423 -----GnfkGMKIKPGSMGKPSPAFDVKIVDVNGNVLPPGQEGDIGIQvlpnRPFglfthyvdnPSkTASTLRGN----- 492
Cdd:cd05966 398 itplpG---ATPLKPGSATRPFFGIEPAILDEEGNEVEGEVEGYLVIK----RPW---------PG-MARTIYGDherye 460
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217306889 493 ---------FYITGDRGYMDKDGYFWFVARADDVILSSGYRIGPFEVENALNEHPSVAESAVVSSPDPIRGEVVKAFVVL 563
Cdd:cd05966 461 dtyfskfpgYYFTGDGARRDEDGYYWITGRVDDVINVSGHRLGTAEVESALVAHPAVAEAAVVGRPHDIKGEAIYAFVTL 540
|
570 580 590
....*....|....*....|....*....|...
gi 2217306889 564 NPDYKSHDqeQLIKEIQEHVKKTTAPYKYPRKV 596
Cdd:cd05966 541 KDGEEPSD--ELRKELRKHVRKEIGPIATPDKI 571
|
|
| ACS-like |
cd17634 |
acetate-CoA ligase; This family includes acyl- and aryl-CoA ligases, as well as the ... |
95-596 |
1.51e-67 |
|
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: 230.93 E-value: 1.51e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217306889 95 WSFEELGSLSRKFANILsEACSLQRGDRVILILPRVPEWWLANVACLRTGTVLIPGTTQLTQKDILYRLQSSKANCIITN 174
Cdd:cd17634 85 ISYRELHREVCRFAGTL-LDLGVKKGDRVAIYMPMIPEAAVAMLACARIGAVHSVIFGGFAPEAVAGRIIDSSSRLLITA 163
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217306889 175 D----------VLAPAVDAVASKCENLHSKLIVSensREGwgnlkelmkvflCHPGWSTVARSWLTAtstsLVQAilsll 244
Cdd:cd17634 164 DggvragrsvpLKKNVDDALNPNVTSVEHVIVLK---RTG------------SDIDWQEGRDLWWRD----LIAK----- 219
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217306889 245 sswdyrhASDSHTCVKTKHNEIMAIFFTSGTSGYPKMTAHTHSSFGLGLSVNGRFWLDLTPSDVMWNTSDTGWAKSAWSS 324
Cdd:cd17634 220 -------ASPEHQPEAMNAEDPLFILYTSGTTGKPKGVLHTTGGYLVYAATTMKYVFDYGPGDIYWCTADVGWVTGHSYL 292
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217306889 325 VFSPWIQGACVFTHH-LPRF-EPTSILQTLSKYPITVFCSAPTVYRMLVQND---ITSYKFKSLKHCVSAGEPITPDVTE 399
Cdd:cd17634 293 LYGPLACGATTLLYEgVPNWpTPARMWQVVDKHGVNILYTAPTAIRALMAAGddaIEGTDRSSLRILGSVGEPINPEAYE 372
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217306889 400 -KWR--NKTGLDIYEGYGQTETV-LICGNFKGM-KIKPGSMGKPSPAFDVKIVDVNGNVLPPGQEGDIGIQV-LPNRPFG 473
Cdd:cd17634 373 wYWKkiGKEKCPVVDTWWQTETGgFMITPLPGAiELKAGSATRPVFGVQPAVVDNEGHPQPGGTEGNLVITDpWPGQTRT 452
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217306889 474 LFThyvDNPSKTASTLR--GNFYITGDRGYMDKDGYFWFVARADDVILSSGYRIGPFEVENALNEHPSVAESAVVSSPDP 551
Cdd:cd17634 453 LFG---DHERFEQTYFStfKGMYFSGDGARRDEDGYYWITGRSDDVINVAGHRLGTAEIESVLVAHPKVAEAAVVGIPHA 529
|
490 500 510 520
....*....|....*....|....*....|....*....|....*
gi 2217306889 552 IRGEVVKAFVVLNPDYKshDQEQLIKEIQEHVKKTTAPYKYPRKV 596
Cdd:cd17634 530 IKGQAPYAYVVLNHGVE--PSPELYAELRNWVRKEIGPLATPDVV 572
|
|
| Firefly_Luc_like |
cd05911 |
Firefly luciferase of light emitting insects and 4-Coumarate-CoA Ligase (4CL); This family ... |
95-604 |
2.14e-67 |
|
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: 227.87 E-value: 2.14e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217306889 95 WSFEELGSLSRKFANILSEAcSLQRGDRVILILPRVPEWWLANVACLRTGTVLIPGTTQLTQKDILYRLQSSKANCIIT- 173
Cdd:cd05911 11 LTYAQLRTLSRRLAAGLRKL-GLKKGDVVGIISPNSTYYPPVFLGCLFAGGIFSAANPIYTADELAHQLKISKPKVIFTd 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217306889 174 NDVLAPAVDAVASkcenlhsklivsensregwgnlkelmkvflchpgWSTVARSWLTATSTSLVQAILSLLSSWDYRHAS 253
Cdd:cd05911 90 PDGLEKVKEAAKE----------------------------------LGPKDKIIVLDDKPDGVLSIEDLLSPTLGEEDE 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217306889 254 DSHTCVKTKHNEIMAIFFTSGTSGYPKMTAHTHSSFGLGL-SVNGRFWLDLTPSDVMWNTSDTGWAKSAWSSVFSPWiQG 332
Cdd:cd05911 136 DLPPPLKDGKDDTAAILYSSGTTGLPKGVCLSHRNLIANLsQVQTFLYGNDGSNDVILGFLPLYHIYGLFTTLASLL-NG 214
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217306889 333 ACVFTHhlPRFEPTSILQTLSKYPITVFCSAPTVYRMLVQN-DITSYKFKSLKHCVSAGEPITPDVTEKWRNKTGL-DIY 410
Cdd:cd05911 215 ATVIIM--PKFDSELFLDLIEKYKITFLYLVPPIAAALAKSpLLDKYDLSSLRVILSGGAPLSKELQELLAKRFPNaTIK 292
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217306889 411 EGYGQTETVLICGNFKGMKIKPGSMGKPSPAFDVKIVDVNGN-VLPPGQEGDI---GIQVLPnrpfGlfthYVDNPSKTA 486
Cdd:cd05911 293 QGYGMTETGGILTVNPDGDDKPGSVGRLLPNVEAKIVDDDGKdSLGPNEPGEIcvrGPQVMK----G----YYNNPEATK 364
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217306889 487 STL-RGNFYITGDRGYMDKDGYFWFVARADDVILSSGYRIGPFEVENALNEHPSVAESAVVSSPDPIRGEVVKAFVVLNP 565
Cdd:cd05911 365 ETFdEDGWLHTGDIGYFDEDGYLYIVDRKKELIKYKGFQVAPAELEAVLLEHPGVADAAVIGIPDEVSGELPRAYVVRKP 444
|
490 500 510
....*....|....*....|....*....|....*....
gi 2217306889 566 DYKSHDqeqliKEIQEHVKKTTAPYKYPRKvGILIITNI 604
Cdd:cd05911 445 GEKLTE-----KEVKDYVAKKVASYKQLRG-GVVFVDEI 477
|
|
| benz_CoA_lig |
TIGR02262 |
benzoate-CoA ligase family; Characterized members of this protein family include benzoate-CoA ... |
80-594 |
2.93e-64 |
|
benzoate-CoA ligase family; Characterized members of this protein family include benzoate-CoA ligase, 4-hydroxybenzoate-CoA ligase, 2-aminobenzoate-CoA ligase, etc. Members are related to fatty acid and acetate CoA ligases.
Pssm-ID: 274059 [Multi-domain] Cd Length: 505 Bit Score: 220.10 E-value: 2.93e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217306889 80 NPAFWWINRNGEEMR------------WSFEELGSLSRKFANILSeACSLQRGDRVILILPRVPEWWLANVACLRTGTVL 147
Cdd:TIGR02262 4 NAAEDLLDRNVVEGRggktafiddissLSYGELEAQVRRLAAALR-RLGVKREERVLLLMLDGVDFPIAFLGAIRAGIVP 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217306889 148 IPGTTQLTQKDILYRLQSSKANCIITNDVLAPAVDAVASKCENLHSkLIVSENSREGWGNLKELMkvflchpgwstvars 227
Cdd:TIGR02262 83 VALNTLLTADDYAYMLEDSRARVVFVSGALLPVIKAALGKSPHLEH-RVVVGRPEAGEVQLAELL--------------- 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217306889 228 wltATStslvqailsllsswdyrhaSDSHTCVKTKHNEIMAIFFTSGTSGYPKMTAHTHSSFGLGLSVNGRFWLDLTPSD 307
Cdd:TIGR02262 147 ---ATE-------------------SEQFKPAATQADDPAFWLYSSGSTGMPKGVVHTHSNPYWTAELYARNTLGIREDD 204
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217306889 308 VMWNTSDTGWAKSAWSSVFSPWIQGACVFTHHlPRFEPTSILQTLSKYPITVFCSAPTVYR-MLVQNDITSYKFKSLKHC 386
Cdd:TIGR02262 205 VCFSAAKLFFAYGLGNALTFPMSVGATTVLMG-ERPTPDAVFDRLRRHQPTIFYGVPTLYAaMLADPNLPSEDQVRLRLC 283
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217306889 387 VSAGEPITPDVTEKWRNKTGLDIYEGYGQTETVLICGNFKGMKIKPGSMGKPSPAFDVKIVDVNGNVLPPGQEGDIGIQV 466
Cdd:TIGR02262 284 TSAGEALPAEVGQRWQARFGVDIVDGIGSTEMLHIFLSNLPGDVRYGTSGKPVPGYRLRLVGDGGQDVADGEPGELLISG 363
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217306889 467 lPNRPFGlfthYVDNPSKTASTLRGNFYITGDRGYMDKDGYFWFVARADDVILSSGYRIGPFEVENALNEHPSVAESAVV 546
Cdd:TIGR02262 364 -PSSATM----YWNNRAKSRDTFQGEWTRSGDKYVRNDDGSYTYAGRTDDMLKVSGIYVSPFEIESALIQHPAVLEAAVV 438
|
490 500 510 520
....*....|....*....|....*....|....*....|....*...
gi 2217306889 547 SSPDPIRGEVVKAFVVLNPDYKShdqeqLIKEIQEHVKKTTAPYKYPR 594
Cdd:TIGR02262 439 GVADEDGLIKPKAFVVLRPGQTA-----LETELKEHVKDRLAPYKYPR 481
|
|
| PrpE |
cd05967 |
Propionyl-CoA synthetase (PrpE); EC 6.2.1.17: propanoate:CoA ligase (AMP-forming) or ... |
90-596 |
6.29e-63 |
|
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: 219.11 E-value: 6.29e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217306889 90 GEEMRWSFEELGSLSRKFANILsEACSLQRGDRVILILPRVPEWWLANVACLRTGTV--LIPG---TTQLTQkdilyRLQ 164
Cdd:cd05967 78 GTERTYTYAELLDEVSRLAGVL-RKLGVVKGDRVIIYMPMIPEAAIAMLACARIGAIhsVVFGgfaAKELAS-----RID 151
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217306889 165 SSKANCIITNDV---------LAPAVDAVASKCENLHSKLIVSEnsregwgnlKELMKVFLCHPG----WSTVarswlta 231
Cdd:cd05967 152 DAKPKLIVTASCgiepgkvvpYKPLLDKALELSGHKPHHVLVLN---------RPQVPADLTKPGrdldWSEL------- 215
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217306889 232 tstslvqailsllsswdyRHASDSHTCVKTKHNEIMAIFFTSGTSGYPKMTAHTHSSFGLGLSVNGRFWLDLTPSDVMWN 311
Cdd:cd05967 216 ------------------LAKAEPVDCVPVAATDPLYILYTSGTTGKPKGVVRDNGGHAVALNWSMRNIYGIKPGDVWWA 277
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217306889 312 TSDTGWAKSAWSSVFSPWIQGA-CVFTHHLPRF--EPTSILQTLSKYPITVFCSAPTVYRMLVQND-----ITSYKFKSL 383
Cdd:cd05967 278 ASDVGWVVGHSYIVYGPLLHGAtTVLYEGKPVGtpDPGAFWRVIEKYQVNALFTAPTAIRAIRKEDpdgkyIKKYDLSSL 357
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217306889 384 KHCVSAGEPITPDVTEKWRNKTGLDIYEGYGQTET----VLICGNFKGMKIKPGSMGKPSPAFDVKIVDVNGNVLPPGQE 459
Cdd:cd05967 358 RTLFLAGERLDPPTLEWAENTLGVPVIDHWWQTETgwpiTANPVGLEPLPIKAGSPGKPVPGYQVQVLDEDGEPVGPNEL 437
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217306889 460 GDIGIQvLPNRPFGLFTHYVDNP---SKTASTLRGnFYITGDRGYMDKDGYFWFVARADDVILSSGYRIGPFEVENALNE 536
Cdd:cd05967 438 GNIVIK-LPLPPGCLLTLWKNDErfkKLYLSKFPG-YYDTGDAGYKDEDGYLFIMGRTDDVINVAGHRLSTGEMEESVLS 515
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217306889 537 HPSVAESAVVSSPDPIRGEVVKAFVVLNPDYKShDQEQLIKEIQEHVKKTTAPYKYPRKV 596
Cdd:cd05967 516 HPAVAECAVVGVRDELKGQVPLGLVVLKEGVKI-TAEELEKELVALVREQIGPVAAFRLV 574
|
|
| LC_FACS_like |
cd05935 |
Putative long-chain fatty acid CoA ligase; The members of this family are putative long-chain ... |
96-596 |
6.85e-63 |
|
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: 214.27 E-value: 6.85e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217306889 96 SFEELGSLSRKFANILSeACSLQRGDRVILILPRVPEWWLANVACLRTGTVLIPGTTQLTQKDILYRLQSSKANCIITnd 175
Cdd:cd05935 3 TYLELLEVVKKLASFLS-NKGVRKGDRVGICLQNSPQYVIAYFAIWRANAVVVPINPMLKERELEYILNDSGAKVAVV-- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217306889 176 vlapavdavaskcenlHSKLivsensregwgnlkelmkvflchpgwstvarswltatstslvqailsllsswdyrhasds 255
Cdd:cd05935 80 ----------------GSEL------------------------------------------------------------ 83
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217306889 256 htcvktkhNEIMAIFFTSGTSGYPKMTAHTHSSFgLGLSVNGRFWLDLTPSDVMWNTSDTGWAKSAWSSVFSPWIQGACV 335
Cdd:cd05935 84 --------DDLALIPYTSGTTGLPKGCMHTHFSA-AANALQSAVWTGLTPSDVILACLPLFHVTGFVGSLNTAVYVGGTY 154
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217306889 336 FThhLPRFEPTSILQTLSKYPITVFCSAPTVYRMLVQN-DITSYKFKSLKHCVSAGEPITPDVTEKWRNKTGLDIYEGYG 414
Cdd:cd05935 155 VL--MARWDRETALELIEKYKVTFWTNIPTMLVDLLATpEFKTRDLSSLKVLTGGGAPMPPAVAEKLLKLTGLRFVEGYG 232
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217306889 415 QTETVLICGNFKGMKIKPGSMGKPSPAFDVKIVDV-NGNVLPPGQEGDIGIQVlPNrpfgLFTHYVDNPSKTAS---TLR 490
Cdd:cd05935 233 LTETMSQTHTNPPLRPKLQCLGIP*FGVDARVIDIeTGRELPPNEVGEIVVRG-PQ----IFKGYWNRPEETEEsfiEIK 307
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217306889 491 GN-FYITGDRGYMDKDGYFWFVARADDVILSSGYRIGPFEVENALNEHPSVAESAVVSSPDPIRGEVVKAFVVLNPDYKS 569
Cdd:cd05935 308 GRrFFRTGDLGYMDEEGYFFFVDRVKRMINVSGFKVWPAEVEAKLYKHPAI*EVCVISVPDERVGEEVKAFIVLRPEYRG 387
|
490 500
....*....|....*....|....*..
gi 2217306889 570 HDQEQlikEIQEHVKKTTAPYKYPRKV 596
Cdd:cd05935 388 KVTEE---DIIEWAREQMAAYKYPREV 411
|
|
| FACL_DitJ_like |
cd05934 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
268-599 |
5.55e-59 |
|
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: 203.68 E-value: 5.55e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217306889 268 AIFFTSGTSGYPKMTAHTHSSFGLGLSVNGRfWLDLTPSDVMW--------NTSDTGWAkSAWSSvfspwiQGACVFthh 339
Cdd:cd05934 85 SILYTSGTTGPPKGVVITHANLTFAGYYSAR-RFGLGEDDVYLtvlplfhiNAQAVSVL-AALSV------GATLVL--- 153
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217306889 340 LPRFEPTSILQTLSKYPITVFCSAPTVYRMLVQNDItsyKFKSLKHCVSA--GEPITPDVTEKWRNKTGLDIYEGYGQTE 417
Cdd:cd05934 154 LPRFSASRFWSDVRRYGATVTNYLGAMLSYLLAQPP---SPDDRAHRLRAayGAPNPPELHEEFEERFGVRLLEGYGMTE 230
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217306889 418 TVLICGNFKGMKIKPGSMGKPSPAFDVKIVDVNGNVLPPGQEGDIGIQvlPNRPFGLFTHYVDNPSKTASTLRGNFYITG 497
Cdd:cd05934 231 TIVGVIGPRDEPRRPGSIGRPAPGYEVRIVDDDGQELPAGEPGELVIR--GLRGWGFFKGYYNMPEATAEAMRNGWFHTG 308
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217306889 498 DRGYMDKDGYFWFVARADDVILSSGYRIGPFEVENALNEHPSVAESAVVSSPDPIRGEVVKAFVVLNPDYK-SHDqeqli 576
Cdd:cd05934 309 DLGYRDADGFFYFVDRKKDMIRRRGENISSAEVERAILRHPAVREAAVVAVPDEVGEDEVKAVVVLRPGETlDPE----- 383
|
330 340
....*....|....*....|...
gi 2217306889 577 kEIQEHVKKTTAPYKYPRKVGIL 599
Cdd:cd05934 384 -ELFAFCEGQLAYFKVPRYIRFV 405
|
|
| PRK06710 |
PRK06710 |
long-chain-fatty-acid--CoA ligase; Validated |
96-594 |
3.47e-58 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 180666 [Multi-domain] Cd Length: 563 Bit Score: 205.27 E-value: 3.47e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217306889 96 SFEELGSLSRKFANILsEACSLQRGDRVILILPRVPEWWLANVACLRTGTVLIPGTTQLTQKDILYRLQSSKANCIITND 175
Cdd:PRK06710 51 TFSVFHDKVKRFANYL-QKLGVEKGDRVAIMLPNCPQAVIGYYGTLLAGGIVVQTNPLYTERELEYQLHDSGAKVILCLD 129
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217306889 176 VLAPAVDAVASKCENLHskLIVSEnsregwgnlkelMKVFLCHPgwSTVARSWLTATSTSLVQAILS--LLSSWDYRHaS 253
Cdd:PRK06710 130 LVFPRVTNVQSATKIEH--VIVTR------------IADFLPFP--KNLLYPFVQKKQSNLVVKVSEseTIHLWNSVE-K 192
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217306889 254 DSHTCVKT---KHNEIMAIFFTSGTSGYPKMTAHTHSSFgLGLSVNGRFWLD--LTPSDVMWNTSDTGWAKSAWSSVFSP 328
Cdd:PRK06710 193 EVNTGVEVpcdPENDLALLQYTGGTTGFPKGVMLTHKNL-VSNTLMGVQWLYncKEGEEVVLGVLPFFHVYGMTAVMNLS 271
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217306889 329 WIQGACVFThhLPRFEPTSILQTLSKYPITVFCSAPTVYRMLVQNDI-TSYKFKSLKHCVSAGEPITPDVTEKWRNKTGL 407
Cdd:PRK06710 272 IMQGYKMVL--IPKFDMKMVFEAIKKHKVTLFPGAPTIYIALLNSPLlKEYDISSIRACISGSAPLPVEVQEKFETVTGG 349
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217306889 408 DIYEGYGQTETVLIC-GNFKGMKIKPGSMGKPSPAFDVKIVDV-NGNVLPPGQEGDI---GIQVLPNrpfglfthYVDNP 482
Cdd:PRK06710 350 KLVEGYGLTESSPVThSNFLWEKRVPGSIGVPWPDTEAMIMSLeTGEALPPGEIGEIvvkGPQIMKG--------YWNKP 421
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217306889 483 SKTASTLRGNFYITGDRGYMDKDGYFWFVARADDVILSSGYRIGPFEVENALNEHPSVAESAVVSSPDPIRGEVVKAFVV 562
Cdd:PRK06710 422 EETAAVLQDGWLHTGDVGYMDEDGFFYVKDRKKDMIVASGFNVYPREVEEVLYEHEKVQEVVTIGVPDPYRGETVKAFVV 501
|
490 500 510
....*....|....*....|....*....|..
gi 2217306889 563 LNPDYKSHDQeqlikEIQEHVKKTTAPYKYPR 594
Cdd:PRK06710 502 LKEGTECSEE-----ELNQFARKYLAAYKVPK 528
|
|
| AACS_like |
cd05968 |
Uncharacterized acyl-CoA synthetase subfamily similar to Acetoacetyl-CoA synthetase; This ... |
59-589 |
5.37e-57 |
|
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: 203.11 E-value: 5.37e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217306889 59 NFAKDVLDQWTdkekaGKKPSNPAFWWINRNGEEMRWSFEELGSLSRKFANILsEACSLQRGDRVILILPRVPEWWLANV 138
Cdd:cd05968 61 NIVEQLLDKWL-----ADTRTRPALRWEGEDGTSRTLTYGELLYEVKRLANGL-RALGVGKGDRVGIYLPMIPEIVPAFL 134
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217306889 139 ACLRTGTVLIPGTTQLTQKDILYRLQSSKANCIITNDV---------LAPAVDAVASKCENLHSKLIVSENSREgwgnlk 209
Cdd:cd05968 135 AVARIGGIVVPIFSGFGKEAAATRLQDAEAKALITADGftrrgrevnLKEEADKACAQCPTVEKVVVVRHLGND------ 208
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217306889 210 elmkvflchPGWSTVARSWltatstslvqailsllssWDYRHASDSHTCVKTKHNEIMAIFFTSGTSGYPKMTAHTHSSF 289
Cdd:cd05968 209 ---------FTPAKGRDLS------------------YDEEKETAGDGAERTESEDPLMIIYTSGTTGKPKGTVHVHAGF 261
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217306889 290 GLGLSVNGRFWLDLTPSDVMWNTSDTGWAKSAWsSVFSPWIQGACVFTHH-LPRF-EPTSILQTLSKYPITVFCSAPTVY 367
Cdd:cd05968 262 PLKAAQDMYFQFDLKPGDLLTWFTDLGWMMGPW-LIFGGLILGATMVLYDgAPDHpKADRLWRMVEDHEITHLGLSPTLI 340
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217306889 368 RMLV---QNDITSYKFKSLKHCVSAGEPITPdvtEKW------RNKTGLDIYEGYGQTETV-LICGNFKGMKIKPGSMGK 437
Cdd:cd05968 341 RALKprgDAPVNAHDLSSLRVLGSTGEPWNP---EPWnwlfetVGKGRNPIINYSGGTEISgGILGNVLIKPIKPSSFNG 417
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217306889 438 PSPAFDVKIVDVNGNVLPPgQEGDIGIQ-VLPNRPFGLF---THYVDnpskTASTLRGNFYITGDRGYMDKDGYFWFVAR 513
Cdd:cd05968 418 PVPGMKADVLDESGKPARP-EVGELVLLaPWPGMTRGFWrdeDRYLE----TYWSRFDNVWVHGDFAYYDEEGYFYILGR 492
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2217306889 514 ADDVILSSGYRIGPFEVENALNEHPSVAESAVVSSPDPIRGEVVKAFVVLNPDYKSHD--QEQLIKEIQEHVKKTTAP 589
Cdd:cd05968 493 SDDTINVAGKRVGPAEIESVLNAHPAVLESAAIGVPHPVKGEAIVCFVVLKPGVTPTEalAEELMERVADELGKPLSP 570
|
|
| MCS |
cd05941 |
Malonyl-CoA synthetase (MCS); MCS catalyzes the formation of malonyl-CoA in a two-step ... |
268-596 |
1.71e-55 |
|
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: 194.82 E-value: 1.71e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217306889 268 AIFFTSGTSGYPKMTAHTHSSFGLGLSVNGRFWlDLTPSDV------------MWNtsdtgwaksawsSVFSPWIQGACV 335
Cdd:cd05941 93 LILYTSGTTGRPKGVVLTHANLAANVRALVDAW-RWTEDDVllhvlplhhvhgLVN------------ALLCPLFAGASV 159
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217306889 336 ftHHLPRFEPTSILQTLSKYPITVFCSAPTVYRMLVQ---------NDITSYKFKSLKHCVSAGEPITPDVTEKWRNKTG 406
Cdd:cd05941 160 --EFLPKFDPKEVAISRLMPSITVFMGVPTIYTRLLQyyeahftdpQFARAAAAERLRLMVSGSAALPVPTLEEWEAITG 237
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217306889 407 LDIYEGYGQTETVLICGN-FKGmKIKPGSMGKPSPAFDVKIVDVNGNvlPPGQEGDIG-IQVlpnRPFGLFTHYVDNPSK 484
Cdd:cd05941 238 HTLLERYGMTEIGMALSNpLDG-ERRPGTVGMPLPGVQARIVDEETG--EPLPRGEVGeIQV---RGPSVFKEYWNKPEA 311
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217306889 485 TASTLRG-NFYITGDRGYMDKDGYFWFVAR-ADDVILSSGYRIGPFEVENALNEHPSVAESAVVSSPDPIRGEVVKAFVV 562
Cdd:cd05941 312 TKEEFTDdGWFKTGDLGVVDEDGYYWILGRsSVDIIKSGGYKVSALEIERVLLAHPGVSECAVIGVPDPDWGERVVAVVV 391
|
330 340 350
....*....|....*....|....*....|....
gi 2217306889 563 LNPDYKSHDQEQLIkeiqEHVKKTTAPYKYPRKV 596
Cdd:cd05941 392 LRAGAAALSLEELK----EWAKQRLAPYKRPRRL 421
|
|
| PRK00174 |
PRK00174 |
acetyl-CoA synthetase; Provisional |
106-596 |
1.50e-54 |
|
acetyl-CoA synthetase; Provisional
Pssm-ID: 234677 [Multi-domain] Cd Length: 637 Bit Score: 196.51 E-value: 1.50e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217306889 106 KFANILSEAcSLQRGDRVILILPRVPEWWLANVACLRTG---TVLIPGttqLTQKDILYRLQSSKANCIITND------- 175
Cdd:PRK00174 110 RFANALKSL-GVKKGDRVAIYMPMIPEAAVAMLACARIGavhSVVFGG---FSAEALADRIIDAGAKLVITADegvrggk 185
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217306889 176 --VLAPAVDAVASKCENLHSKLIVS--------ENSREGWGNlkELMKvflchpgwstvarswltatstslvqailslls 245
Cdd:PRK00174 186 piPLKANVDEALANCPSVEKVIVVRrtggdvdwVEGRDLWWH--ELVA-------------------------------- 231
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217306889 246 swdyrHASDSHTCVKTKHNEIMAIFFTSGTSGYPKMTAHTHSSFGLGLSVNGRFWLDLTPSDVMWNTSDTGWAKSAWSSV 325
Cdd:PRK00174 232 -----GASDECEPEPMDAEDPLFILYTSGSTGKPKGVLHTTGGYLVYAAMTMKYVFDYKDGDVYWCTADVGWVTGHSYIV 306
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217306889 326 FSPWIQGACVFTHH-LPRF-EPTSILQTLSKYPITVFCSAPTVYRMLVQ---NDITSYKFKSLKHCVSAGEPITPdvtEK 400
Cdd:PRK00174 307 YGPLANGATTLMFEgVPNYpDPGRFWEVIDKHKVTIFYTAPTAIRALMKegdEHPKKYDLSSLRLLGSVGEPINP---EA 383
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217306889 401 WR---NKTGLD---IYEGYGQTET--VLIC---GnfkGMKIKPGSMGKPSPAFDVKIVDVNGNVLPPGQEGDIGIqvlpN 469
Cdd:PRK00174 384 WEwyyKVVGGErcpIVDTWWQTETggIMITplpG---ATPLKPGSATRPLPGIQPAVVDEEGNPLEGGEGGNLVI----K 456
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217306889 470 RPFglfthyvdnPS-------------KTA-STLRGNfYITGDRGYMDKDGYFWFVARADDVILSSGYRIGPFEVENALN 535
Cdd:PRK00174 457 DPW---------PGmmrtiygdherfvKTYfSTFKGM-YFTGDGARRDEDGYYWITGRVDDVLNVSGHRLGTAEIESALV 526
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2217306889 536 EHPSVAESAVVSSPDPIRGEVVKAFVVLNPDYKSHDqeQLIKEIQEHVKKTTAPYKYPRKV 596
Cdd:PRK00174 527 AHPKVAEAAVVGRPDDIKGQGIYAFVTLKGGEEPSD--ELRKELRNWVRKEIGPIAKPDVI 585
|
|
| FACL_fum10p_like |
cd05926 |
Subfamily of fatty acid CoA ligase (FACL) similar to Fum10p of Gibberella moniliformis; FACL ... |
95-596 |
8.46e-54 |
|
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: 191.37 E-value: 8.46e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217306889 95 WSFEELGSLSRKFANILSEAcSLQRGDRVILILPRVPEWWLANVACLRTGTVLIPGTTQLTQKDILYRLQSSKANCIIT- 173
Cdd:cd05926 15 LTYADLAELVDDLARQLAAL-GIKKGDRVAIALPNGLEFVVAFLAAARAGAVVAPLNPAYKKAEFEFYLADLGSKLVLTp 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217306889 174 NDVLAPAVDAVAskcenlhsklivsensregwgnlkelmkvflcHPGWSTVARSWLTATSTSLVQAilSLLSSWDYRHAS 253
Cdd:cd05926 94 KGELGPASRAAS--------------------------------KLGLAILELALDVGVLIRAPSA--ESLSNLLADKKN 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217306889 254 DSHTCVKTKhNEIMAIFFTSGTSGYPKMTAHTHSSfgLGLSV-NGRFWLDLTPSD----VMWNTSDTGWAKSAWSSVFSp 328
Cdd:cd05926 140 AKSEGVPLP-DDLALILHTSGTTGRPKGVPLTHRN--LAASAtNITNTYKLTPDDrtlvVMPLFHVHGLVASLLSTLAA- 215
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217306889 329 wiQGACVFThhlPRFEPTSILQTLSKYPITVFCSAPTVYRMLVQNDITSY--KFKSLKHCVSAGEPITPDVTEKWRNKTG 406
Cdd:cd05926 216 --GGSVVLP---PRFSASTFWPDVRDYNATWYTAVPTIHQILLNRPEPNPesPPPKLRFIRSCSASLPPAVLEALEATFG 290
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217306889 407 LDIYEGYGQTETV--LICGNFKGMKIKPGSMGKPSPAfDVKIVDVNGNVLPPGQEGDIGIQVlPNRPFGlfthYVDNPSK 484
Cdd:cd05926 291 APVLEAYGMTEAAhqMTSNPLPPGPRKPGSVGKPVGV-EVRILDEDGEILPPGVVGEICLRG-PNVTRG----YLNNPEA 364
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217306889 485 TA-STLRGNFYITGDRGYMDKDGYFWFVARADDVILSSGYRIGPFEVENALNEHPSVAESAVVSSPDPIRGEVVKAFVVL 563
Cdd:cd05926 365 NAeAAFKDGWFRTGDLGYLDADGYLFLTGRIKELINRGGEKISPLEVDGVLLSHPAVLEAVAFGVPDEKYGEEVAAAVVL 444
|
490 500 510
....*....|....*....|....*....|...
gi 2217306889 564 NPDYKShdqeqLIKEIQEHVKKTTAPYKYPRKV 596
Cdd:cd05926 445 REGASV-----TEEELRAFCRKHLAAFKVPKKV 472
|
|
| PRK08316 |
PRK08316 |
acyl-CoA synthetase; Validated |
91-596 |
1.64e-53 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 181381 [Multi-domain] Cd Length: 523 Bit Score: 191.30 E-value: 1.64e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217306889 91 EEMRWSFEELGSLSRKFANILSEAcSLQRGDRVILILPRVPEWWLANVACLRTGTVLIPGTTQLTQKDILYRLQSSKANC 170
Cdd:PRK08316 33 GDRSWTYAELDAAVNRVAAALLDL-GLKKGDRVAALGHNSDAYALLWLACARAGAVHVPVNFMLTGEELAYILDHSGARA 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217306889 171 IITNDVLAPAVDAVASKCENLHSKLIVSENSREGWGnlkelmkvflchpGWSTVARsWLTATSTSLVQAILsllsswdyr 250
Cdd:PRK08316 112 FLVDPALAPTAEAALALLPVDTLILSLVLGGREAPG-------------GWLDFAD-WAEAGSVAEPDVEL--------- 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217306889 251 hasdshtcvktkHNEIMA-IFFTSGTSGYPKMTAHTHSSFgLGLSVNGRFWLDLTPSDVMWNtsdtgwA----KSAWSSV 325
Cdd:PRK08316 169 ------------ADDDLAqILYTSGTESLPKGAMLTHRAL-IAEYVSCIVAGDMSADDIPLH------AlplyHCAQLDV 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217306889 326 F-SPWIQ-GACvfTHHLPRFEPTSILQTLSKYPITVFCSAPTVYRMLVQN-DITSYKFKSLKHCVSaGEPITP-DVTEKW 401
Cdd:PRK08316 230 FlGPYLYvGAT--NVILDAPDPELILRTIEAERITSFFAPPTVWISLLRHpDFDTRDLSSLRKGYY-GASIMPvEVLKEL 306
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217306889 402 RNK-TGLDIYEGYGQTE-----TVLicgNFKGMKIKPGSMGKPSPAFDVKIVDVNGNVLPPGQEGDIgiqvlPNRPFGLF 475
Cdd:PRK08316 307 RERlPGLRFYNCYGQTEiaplaTVL---GPEEHLRRPGSAGRPVLNVETRVVDDDGNDVAPGEVGEI-----VHRSPQLM 378
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217306889 476 THYVDNPSKTASTLRGNFYITGDRGYMDKDGYFWFVARADDVILSSGYRIGPFEVENALNEHPSVAESAVVSSPDPIRGE 555
Cdd:PRK08316 379 LGYWDDPEKTAEAFRGGWFHSGDLGVMDEEGYITVVDRKKDMIKTGGENVASREVEEALYTHPAVAEVAVIGLPDPKWIE 458
|
490 500 510 520
....*....|....*....|....*....|....*....|.
gi 2217306889 556 VVKAFVVLNPDyKSHDQEQLIkeiqEHVKKTTAPYKYPRKV 596
Cdd:PRK08316 459 AVTAVVVPKAG-ATVTEDELI----AHCRARLAGFKVPKRV 494
|
|
| 4CL |
cd05904 |
4-Coumarate-CoA Ligase (4CL); 4-Coumarate:coenzyme A ligase is a key enzyme in the ... |
72-596 |
1.30e-51 |
|
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: 185.90 E-value: 1.30e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217306889 72 EKAGKKPSNPAFwwIN-RNGEEMrwSFEELGSLSRKFANILSeACSLQRGDRVILILPRVPEWWLANVACLRTGTVLIPG 150
Cdd:cd05904 13 LFASAHPSRPAL--IDaATGRAL--TYAELERRVRRLAAGLA-KRGGRKGDVVLLLSPNSIEFPVAFLAVLSLGAVVTTA 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217306889 151 TTQLTQKDILYRLQSSKANCIITndvlapaVDAVASKCENLHSKLIVSENsregwgnlkelmKVFLCHPGWSTVArswlT 230
Cdd:cd05904 88 NPLSTPAEIAKQVKDSGAKLAFT-------TAELAEKLASLALPVVLLDS------------AEFDSLSFSDLLF----E 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217306889 231 ATSTSLVQAILSllsswdyrhasDSHTCvktkhneimAIFFTSGTSGYPKMTAHTHSSF-GLGLSVNGRFWLDLTPSDVM 309
Cdd:cd05904 145 ADEAEPPVVVIK-----------QDDVA---------ALLYSSGTTGRSKGVMLTHRNLiAMVAQFVAGEGSNSDSEDVF 204
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217306889 310 WntsdtgwaksawssVFSPW--IQGACVFTHH----------LPRFEPTSILQTLSKYPITVFCSAPTVYRMLVQNDIT- 376
Cdd:cd05904 205 L--------------CVLPMfhIYGLSSFALGllrlgatvvvMPRFDLEELLAAIERYKVTHLPVVPPIVLALVKSPIVd 270
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217306889 377 SYKFKSLKHCVSAGEPITPDVTEKWRNK-TGLDIYEGYGQTET---VLICGNFKGMKIKPGSMGKPSPAFDVKIVDVN-G 451
Cdd:cd05904 271 KYDLSSLRQIMSGAAPLGKELIEAFRAKfPNVDLGQGYGMTEStgvVAMCFAPEKDRAKYGSVGRLVPNVEAKIVDPEtG 350
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217306889 452 NVLPPGQEGDIGIqvlpnRPFGLFTHYVDNPSKTASTLRGNFYI-TGDRGYMDKDGYFWFVARADDVILSSGYRIGPFEV 530
Cdd:cd05904 351 ESLPPNQTGELWI-----RGPSIMKGYLNNPEATAATIDKEGWLhTGDLCYIDEDGYLFIVDRLKELIKYKGFQVAPAEL 425
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2217306889 531 ENALNEHPSVAESAVVSSPDPIRGEVVKAFVVLNPDykSHDQEQlikEIQEHVKKTTAPYKYPRKV 596
Cdd:cd05904 426 EALLLSHPEILDAAVIPYPDEEAGEVPMAFVVRKPG--SSLTED---EIMDFVAKQVAPYKKVRKV 486
|
|
| PRK07514 |
PRK07514 |
malonyl-CoA synthase; Validated |
94-596 |
1.24e-49 |
|
malonyl-CoA synthase; Validated
Pssm-ID: 181011 [Multi-domain] Cd Length: 504 Bit Score: 180.46 E-value: 1.24e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217306889 94 RWSFEELGSLSRKFANILSeACSLQRGDRVILILPRVPEWWLANVACLRTGTVLIPGTTQLTQKDILYRLQSSKANCIIT 173
Cdd:PRK07514 28 RYTYGDLDAASARLANLLV-ALGVKPGDRVAVQVEKSPEALALYLATLRAGAVFLPLNTAYTLAELDYFIGDAEPALVVC 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217306889 174 NDVLAPAVDAVASKCenlhsklivsensreGWGNLKELMkvflchpgwstvarswlTATSTSLVQAIlsllsswdyRHAS 253
Cdd:PRK07514 107 DPANFAWLSKIAAAA---------------GAPHVETLD-----------------ADGTGSLLEAA---------AAAP 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217306889 254 DSHTCVKTKHNEIMAIFFTSGTSGYPK--MTAHTH-SSFGLGLSVNGRFwldlTPSDVMwntsdtgwaksawssvfspwI 330
Cdd:PRK07514 146 DDFETVPRGADDLAAILYTSGTTGRSKgaMLSHGNlLSNALTLVDYWRF----TPDDVL--------------------I 201
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217306889 331 QGACVFTHH------------------LPRFEPTSILQTLSKypITVFCSAPTVY-RMLVQNDITSYKFKSLKHCVSAGE 391
Cdd:PRK07514 202 HALPIFHTHglfvatnvallagasmifLPKFDPDAVLALMPR--ATVMMGVPTFYtRLLQEPRLTREAAAHMRLFISGSA 279
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217306889 392 PITPDVTEKWRNKTGLDIYEGYGQTETVLICGN-FKGMKIkPGSMGKPSPAFDVKIVD-VNGNVLPPGQEGDIGIQVlPN 469
Cdd:PRK07514 280 PLLAETHREFQERTGHAILERYGMTETNMNTSNpYDGERR-AGTVGFPLPGVSLRVTDpETGAELPPGEIGMIEVKG-PN 357
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217306889 470 rpfgLFTHYVDNPSKTASTLRGN-FYITGDRGYMDKDGYFWFVARADDVILSSGYRIGPFEVENALNEHPSVAESAVVSS 548
Cdd:PRK07514 358 ----VFKGYWRMPEKTAEEFRADgFFITGDLGKIDERGYVHIVGRGKDLIISGGYNVYPKEVEGEIDELPGVVESAVIGV 433
|
490 500 510 520
....*....|....*....|....*....|....*....|....*...
gi 2217306889 549 PDPIRGEVVKAFVVLNPDyKSHDQEQLIKEIQEHVkkttAPYKYPRKV 596
Cdd:PRK07514 434 PHPDFGEGVTAVVVPKPG-AALDEAAILAALKGRL----ARFKQPKRV 476
|
|
| PRK05605 |
PRK05605 |
long-chain-fatty-acid--CoA ligase; Validated |
63-596 |
1.47e-48 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 235531 [Multi-domain] Cd Length: 573 Bit Score: 178.66 E-value: 1.47e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217306889 63 DVLDqwtdkEKAGKKPSNPAFWWInrnGEEMrwSFEELGSLSRKFANILsEACSLQRGDRVILILPRVPEWWLANVACLR 142
Cdd:PRK05605 36 DLYD-----NAVARFGDRPALDFF---GATT--TYAELGKQVRRAAAGL-RALGVRPGDRVAIVLPNCPQHIVAFYAVLR 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217306889 143 TGTVLIPGTTQLTQKDILYRLQSSKANCIItndvlapAVDAVASKCENLHSKL----IVSENSREGWGNLKELmKVFLCH 218
Cdd:PRK05605 105 LGAVVVEHNPLYTAHELEHPFEDHGARVAI-------VWDKVAPTVERLRRTTpletIVSVNMIAAMPLLQRL-ALRLPI 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217306889 219 PGWSTvARSWLTATSTSLVqailsllsSWDYRHAS------DSHTCVKTKHNEIMAIFFTSGTSGYPKMTAHTHSsfglG 292
Cdd:PRK05605 177 PALRK-ARAALTGPAPGTV--------PWETLVDAaiggdgSDVSHPRPTPDDVALILYTSGTTGKPKGAQLTHR----N 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217306889 293 LSVN---GRFWLDLTPSD----------------VMWNTsdtgwaksawssvFSPWIQGACVFthhLPRFEPTSILQTLS 353
Cdd:PRK05605 244 LFANaaqGKAWVPGLGDGpervlaalpmfhayglTLCLT-------------LAVSIGGELVL---LPAPDIDLILDAMK 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217306889 354 KYPITVFCSAPTVYRMLVQN------DITSykfksLKHCVSAGEPITPDVTEKWRNKTGLDIYEGYGQTETV-LICGNFK 426
Cdd:PRK05605 308 KHPPTWLPGVPPLYEKIAEAaeergvDLSG-----VRNAFSGAMALPVSTVELWEKLTGGLLVEGYGLTETSpIIVGNPM 382
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217306889 427 GMKIKPGSMGKPSPAFDVKIVDVN--GNVLPPGQEGDI---GIQVlpnrpfglFTHYVDNPSKTASTLRGNFYITGDRGY 501
Cdd:PRK05605 383 SDDRRPGYVGVPFPDTEVRIVDPEdpDETMPDGEEGELlvrGPQV--------FKGYWNRPEETAKSFLDGWFRTGDVVV 454
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217306889 502 MDKDGYFWFVARADDVILSSGYRIGPFEVENALNEHPSVAESAVVSSPDPIRGEVVKAFVVLNPDyKSHDQEQLikeiQE 581
Cdd:PRK05605 455 MEEDGFIRIVDRIKELIITGGFNVYPAEVEEVLREHPGVEDAAVVGLPREDGSEEVVAAVVLEPG-AALDPEGL----RA 529
|
570
....*....|....*
gi 2217306889 582 HVKKTTAPYKYPRKV 596
Cdd:PRK05605 530 YCREHLTRYKVPRRF 544
|
|
| prpE |
PRK10524 |
propionyl-CoA synthetase; Provisional |
76-596 |
1.25e-47 |
|
propionyl-CoA synthetase; Provisional
Pssm-ID: 182517 [Multi-domain] Cd Length: 629 Bit Score: 177.06 E-value: 1.25e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217306889 76 KKPSNPAFWWIN-RNGEEMRWSFEELGSLSRKFANILsEACSLQRGDRVILILPRVPEWWLANVACLRTG---TVLIPG- 150
Cdd:PRK10524 65 KRPEQLALIAVStETDEERTYTFRQLHDEVNRMAAML-RSLGVQRGDRVLIYMPMIAEAAFAMLACARIGaihSVVFGGf 143
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217306889 151 -TTQLTQkdilyRLQSSKANCIITNDVLAPAVDAVASKCEnLHSKLIVSENSREgwgnlkelmKVFLCHPGWSTVARswl 229
Cdd:PRK10524 144 aSHSLAA-----RIDDAKPVLIVSADAGSRGGKVVPYKPL-LDEAIALAQHKPR---------HVLLVDRGLAPMAR--- 205
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217306889 230 tatstslVQAILSLLSSWDYRHASDSHTCVKTKHNEIMAIFFTSGTSGYPKMTAHTHSSFGLGLSVNGRFWLDLTPSDVM 309
Cdd:PRK10524 206 -------VAGRDVDYATLRAQHLGARVPVEWLESNEPSYILYTSGTTGKPKGVQRDTGGYAVALATSMDTIFGGKAGETF 278
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217306889 310 WNTSDTGWAKSAWSSVFSPWIQG-ACVFTHHLP-RFEPTSILQTLSKYPITVFCSAPTVYRMLVQND---ITSYKFKSLK 384
Cdd:PRK10524 279 FCASDIGWVVGHSYIVYAPLLAGmATIMYEGLPtRPDAGIWWRIVEKYKVNRMFSAPTAIRVLKKQDpalLRKHDLSSLR 358
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217306889 385 HCVSAGEPITpDVTEKWRNKT-GLDIYEGYGQTET----VLICGNFKGMKIKPGSMGKPSPAFDVKIVD-VNGNVLPPGQ 458
Cdd:PRK10524 359 ALFLAGEPLD-EPTASWISEAlGVPVIDNYWQTETgwpiLAIARGVEDRPTRLGSPGVPMYGYNVKLLNeVTGEPCGPNE 437
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217306889 459 EGDIGIQV-LPnrPFGLFTHYVDNP---SKTASTLRGNFYITGDRGYMDKDGYFWFVARADDVILSSGYRIGPFEVENAL 534
Cdd:PRK10524 438 KGVLVIEGpLP--PGCMQTVWGDDDrfvKTYWSLFGRQVYSTFDWGIRDADGYYFILGRTDDVINVAGHRLGTREIEESI 515
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2217306889 535 NEHPSVAESAVVSSPDPIRGEVVKAFVVLNPDYKSHDQEQ---LIKEIQEHVKKTTAPYKYPRKV 596
Cdd:PRK10524 516 SSHPAVAEVAVVGVKDALKGQVAVAFVVPKDSDSLADREArlaLEKEIMALVDSQLGAVARPARV 580
|
|
| PRK06178 |
PRK06178 |
acyl-CoA synthetase; Validated |
63-593 |
9.03e-47 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 235724 [Multi-domain] Cd Length: 567 Bit Score: 173.69 E-value: 9.03e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217306889 63 DVLDQWtdkekAGKKPSNPAFWWINRngeemRWSFEELGSLSRKFANILsEACSLQRGDRVILILPRVPEWWLANVACLR 142
Cdd:PRK06178 37 EYLRAW-----ARERPQRPAIIFYGH-----VITYAELDELSDRFAALL-RQRGVGAGDRVAVFLPNCPQFHIVFFGILK 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217306889 143 TGTVLIPGTTQLTQKDILYRLQSSKANCIITNDVLAPAVDAVASKCEnlhsklivsensregwgnLKELMKVFLCH--PG 220
Cdd:PRK06178 106 LGAVHVPVSPLFREHELSYELNDAGAEVLLALDQLAPVVEQVRAETS------------------LRHVIVTSLADvlPA 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217306889 221 WSTVARSWLTATSTSLVQAILSLLSSwdYRHASDSHTCVKTKHNEIMAIFFTSGTSGYPKMTAHTHSSFGLGLSVNGRFW 300
Cdd:PRK06178 168 EPTLPLPDSLRAPRLAAAGAIDLLPA--LRACTAPVPLPPPALDALAALNYTGGTTGMPKGCEHTQRDMVYTAAAAYAVA 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217306889 301 LDLTPSDVMWNTSDTGWAKSAWSSVFSPWIQGACVFThhLPRFEPTSILQTLSKYPITVfcsapTVyrMLVQN------- 373
Cdd:PRK06178 246 VVGGEDSVFLSFLPEFWIAGENFGLLFPLFSGATLVL--LARWDAVAFMAAVERYRVTR-----TV--MLVDNavelmdh 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217306889 374 -DITSYKFKSLKH--CVSAGEPITPDVTEKWRNKTGLDIYEG-YGQTETvLICGNF-KGM-------KIKPGSMGKPSPA 441
Cdd:PRK06178 317 pRFAEYDLSSLRQvrVVSFVKKLNPDYRQRWRALTGSVLAEAaWGMTET-HTCDTFtAGFqdddfdlLSQPVFVGLPVPG 395
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217306889 442 FDVKIVD-VNGNVLPPGQEGDIGIqvlpnRPFGLFTHYVDNPSKTASTLRGNFYITGDRGYMDKDGYFWFVARADDVILS 520
Cdd:PRK06178 396 TEFKICDfETGELLPLGAEGEIVV-----RTPSLLKGYWNKPEATAEALRDGWLHTGDIGKIDEQGFLHYLGRRKEMLKV 470
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2217306889 521 SGYRIGPFEVENALNEHPSVAESAVVSSPDPIRGEVVKAFVVLNPDyksHDQEQliKEIQEHVKKTTAPYKYP 593
Cdd:PRK06178 471 NGMSVFPSEVEALLGQHPAVLGSAVVGRPDPDKGQVPVAFVQLKPG---ADLTA--AALQAWCRENMAVYKVP 538
|
|
| ACLS-CaiC |
cd17637 |
acyl-CoA synthetase (AMP-forming)/AMP-acid ligase II; This family contains fatty acid CoA ... |
340-596 |
1.67e-46 |
|
acyl-CoA synthetase (AMP-forming)/AMP-acid ligase II; This family contains fatty acid CoA ligases, including acyl-CoA synthetase (AMP-forming)/AMP-acid ligase II, most of which are yet to be characterized, but may be similar to Carnitine-CoA ligase (CaiC) which catalyzes the transfer of CoA to carnitine. Fatty acyl-CoA ligases catalyze the ATP-dependent activation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions.
Pssm-ID: 341292 [Multi-domain] Cd Length: 333 Bit Score: 167.06 E-value: 1.67e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217306889 340 LPRFEPTSILQTLSKYPITVFCS-APTVYRMLVQNDITSYKFKSLKHcVSAGEpiTPDVTEKWRNKTGLDIYEGYGQTET 418
Cdd:cd17637 72 MEKFDPAEALELIEEEKVTLMGSfPPILSNLLDAAEKSGVDLSSLRH-VLGLD--APETIQRFEETTGATFWSLYGQTET 148
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217306889 419 ---VLICGNFKgmkiKPGSMGKPSPAFDVKIVDVNGNVLPPGQEGDIGIqvlpnRPFGLFTHYVDNPSKTASTLRGNFYI 495
Cdd:cd17637 149 sglVTLSPYRE----RPGSAGRPGPLVRVRIVDDNDRPVPAGETGEIVV-----RGPLVFQGYWNLPELTAYTFRNGWHH 219
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217306889 496 TGDRGYMDKDGYFWFVAR--ADDVILSSGYRIGPFEVENALNEHPSVAESAVVSSPDPIRGEVVKAFVVLNPDyKSHDQE 573
Cdd:cd17637 220 TGDLGRFDEDGYLWYAGRkpEKELIKPGGENVYPAEVEKVILEHPAIAEVCVIGVPDPKWGEGIKAVCVLKPG-ATLTAD 298
|
250 260
....*....|....*....|...
gi 2217306889 574 QLIkeiqEHVKKTTAPYKYPRKV 596
Cdd:cd17637 299 ELI----EFVGSRIARYKKPRYV 317
|
|
| PRK06839 |
PRK06839 |
o-succinylbenzoate--CoA ligase; |
90-599 |
2.95e-46 |
|
o-succinylbenzoate--CoA ligase;
Pssm-ID: 168698 [Multi-domain] Cd Length: 496 Bit Score: 170.81 E-value: 2.95e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217306889 90 GEEMRWSFEELGSLSRKFANILSEACSLQRGDRVILILPRVPEWWLANVACLRTGTVLIPGTTQLTQKDILYRLQSSKAN 169
Cdd:PRK06839 23 TEEEEMTYKQLHEYVSKVAAYLIYELNVKKGERIAILSQNSLEYIVLLFAIAKVECIAVPLNIRLTENELIFQLKDSGTT 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217306889 170 CIITNDVLApavdavaskcenlhsklivsensregwgNLKELMKvflchpGWSTVARS-WLTATSTSLVQAIlsllSSWD 248
Cdd:PRK06839 103 VLFVEKTFQ----------------------------NMALSMQ------KVSYVQRViSITSLKEIEDRKI----DNFV 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217306889 249 YRHASDShtcvktkhneiMAIFFTSGTSGYPKMTAHTHSSFGLGlSVNGRFWLDLTPSDV------MWNTSDTGWAksaw 322
Cdd:PRK06839 145 EKNESAS-----------FIICYTSGTTGKPKGAVLTQENMFWN-ALNNTFAIDLTMHDRsivllpLFHIGGIGLF---- 208
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217306889 323 ssVFSPWIQGACVFTHHlpRFEPTSILQTLSKYPITVFCSAPTVYRMLVQN-DITSYKFKSLKHCVSAGEPITPDVTEKW 401
Cdd:PRK06839 209 --AFPTLFAGGVIIVPR--KFEPTKALSMIEKHKVTVVMGVPTIHQALINCsKFETTNLQSVRWFYNGGAPCPEELMREF 284
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217306889 402 RNKtGLDIYEGYGQTET-----VLICGNFKGmkiKPGSMGKPSPAFDVKIVDVNGNVLPPGQEGDIGIQVlPNrpfgLFT 476
Cdd:PRK06839 285 IDR-GFLFGQGFGMTETsptvfMLSEEDARR---KVGSIGKPVLFCDYELIDENKNKVEVGEVGELLIRG-PN----VMK 355
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217306889 477 HYVDNPSKTASTLRGNFYITGDRGYMDKDGYFWFVARADDVILSSGYRIGPFEVENALNEHPSVAESAVVSSPDPIRGEV 556
Cdd:PRK06839 356 EYWNRPDATEETIQDGWLCTGDLARVDEDGFVYIVGRKKEMIISGGENIYPLEVEQVINKLSDVYEVAVVGRQHVKWGEI 435
|
490 500 510 520
....*....|....*....|....*....|....*....|...
gi 2217306889 557 VKAFVVLNPDYKSHDqeqliKEIQEHVKKTTAPYKYPRKVGIL 599
Cdd:PRK06839 436 PIAFIVKKSSSVLIE-----KDVIEHCRLFLAKYKIPKEIVFL 473
|
|
| PRK08276 |
PRK08276 |
long-chain-fatty-acid--CoA ligase; Validated |
90-596 |
3.18e-46 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236215 [Multi-domain] Cd Length: 502 Bit Score: 170.85 E-value: 3.18e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217306889 90 GEEMRWSFEELGSLSRKFANILSEAcSLQRGDRVILILPRVPEWWLANVACLRTGTVLIPGTTQLTQKDILYRLQSSKAN 169
Cdd:PRK08276 7 PSGEVVTYGELEARSNRLAHGLRAL-GLREGDVVAILLENNPEFFEVYWAARRSGLYYTPINWHLTAAEIAYIVDDSGAK 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217306889 170 CIITNDVLAPAVDAVASKCENlhsklivsensregwgNLKELMKVFLCHPGWstvaRSWLTATSTSLVQAILSLLSSWDy 249
Cdd:PRK08276 86 VLIVSAALADTAAELAAELPA----------------GVPLLLVVAGPVPGF----RSYEEALAAQPDTPIADETAGAD- 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217306889 250 rhasdshtcvktkhneiMAifFTSGTSGYPK------MTAHTHSSFGLGLSVNGrFWLDLTPSDV------MWNTSDTGW 317
Cdd:PRK08276 145 -----------------ML--YSSGTTGRPKgikrplPGLDPDEAPGMMLALLG-FGMYGGPDSVylspapLYHTAPLRF 204
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217306889 318 AKSAwssvfspwiqgacvftHHL-------PRFEPTSILQTLSKYPITVFCSAPTVY-RML-----VQNditSYKFKSLK 384
Cdd:PRK08276 205 GMSA----------------LALggtvvvmEKFDAEEALALIERYRVTHSQLVPTMFvRMLklpeeVRA---RYDVSSLR 265
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217306889 385 HCVSAGEPITPDVTEK----WrnktGLDIYEGYGQTE----TVLICGNFKGmkiKPGSMGKPSPAfDVKIVDVNGNVLPP 456
Cdd:PRK08276 266 VAIHAAAPCPVEVKRAmidwW----GPIIHEYYASSEgggvTVITSEDWLA---HPGSVGKAVLG-EVRILDEDGNELPP 337
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217306889 457 GQEGDIGIQvLPNRPFglftHYVDNPSKTASTLRGNFYIT-GDRGYMDKDGYFWFVARADDVILSSGYRIGPFEVENALN 535
Cdd:PRK08276 338 GEIGTVYFE-MDGYPF----EYHNDPEKTAAARNPHGWVTvGDVGYLDEDGYLYLTDRKSDMIISGGVNIYPQEIENLLV 412
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2217306889 536 EHPSVAESAVVSSPDPIRGEVVKAFVVLNPDYKshDQEQLIKEIQEHVKKTTAPYKYPRKV 596
Cdd:PRK08276 413 THPKVADVAVFGVPDEEMGERVKAVVQPADGAD--AGDALAAELIAWLRGRLAHYKCPRSI 471
|
|
| PRK08974 |
PRK08974 |
long-chain-fatty-acid--CoA ligase FadD; |
72-596 |
5.52e-45 |
|
long-chain-fatty-acid--CoA ligase FadD;
Pssm-ID: 236359 [Multi-domain] Cd Length: 560 Bit Score: 168.31 E-value: 5.52e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217306889 72 EKAGKK-PSNPAFwwINRnGEEMrwSFEELGSLSRKFANILSEACSLQRGDRVILILPRVPEWWLANVACLRTGTVLIPG 150
Cdd:PRK08974 30 EQAVARyADQPAF--INM-GEVM--TFRKLEERSRAFAAYLQNGLGLKKGDRVALMMPNLLQYPIALFGILRAGMIVVNV 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217306889 151 TTQLTQKDILYRLQSSKANCIITndvlapaVDAVASKCENlhskliVSENSregwgnlkELMKVFLCHPGwstvarSWLT 230
Cdd:PRK08974 105 NPLYTPRELEHQLNDSGAKAIVI-------VSNFAHTLEK------VVFKT--------PVKHVILTRMG------DQLS 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217306889 231 ATSTSLV----QAILSLLSSWDYRHASdSHTCVKTK-----------HNEIMAIF-FTSGTSGYPKMTAHTHSsfglgls 294
Cdd:PRK08974 158 TAKGTLVnfvvKYIKRLVPKYHLPDAI-SFRSALHKgrrmqyvkpelVPEDLAFLqYTGGTTGVAKGAMLTHR------- 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217306889 295 vngrfwldltpsDVMWNTSDTGWAKSAWSSVFSPWIQGA------------CVFTHHL---------PRFEPTSIlQTLS 353
Cdd:PRK08974 230 ------------NMLANLEQAKAAYGPLLHPGKELVVTAlplyhifaltvnCLLFIELggqnllitnPRDIPGFV-KELK 296
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217306889 354 KYPITVFCSAPTVYRMLVQN-DITSYKFKSLKHCVSAGEPITPDVTEKWRNKTGLDIYEGYGQTE-TVLICGNFKGMKIK 431
Cdd:PRK08974 297 KYPFTAITGVNTLFNALLNNeEFQELDFSSLKLSVGGGMAVQQAVAERWVKLTGQYLLEGYGLTEcSPLVSVNPYDLDYY 376
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217306889 432 PGSMGKPSPAFDVKIVDVNGNVLPPGQEGDI---GIQVLPNrpfglfthYVDNPSKTASTLRGNFYITGDRGYMDKDGYF 508
Cdd:PRK08974 377 SGSIGLPVPSTEIKLVDDDGNEVPPGEPGELwvkGPQVMLG--------YWQRPEATDEVIKDGWLATGDIAVMDEEGFL 448
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217306889 509 WFVARADDVILSSGYRIGPFEVENALNEHPSVAESAVVSSPDPIRGEVVKAFVVLNPdyKSHDQEQLIKEIQEHVkkttA 588
Cdd:PRK08974 449 RIVDRKKDMILVSGFNVYPNEIEDVVMLHPKVLEVAAVGVPSEVSGEAVKIFVVKKD--PSLTEEELITHCRRHL----T 522
|
....*...
gi 2217306889 589 PYKYPRKV 596
Cdd:PRK08974 523 GYKVPKLV 530
|
|
| PRK07470 |
PRK07470 |
acyl-CoA synthetase; Validated |
74-596 |
6.95e-44 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 180988 [Multi-domain] Cd Length: 528 Bit Score: 164.83 E-value: 6.95e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217306889 74 AGKKPSNPAFWWinrnGEEmRWSFEELGSLSRKFANILsEACSLQRGDRVILILPRVPEWWLANVACLRTGTVLIPGTTQ 153
Cdd:PRK07470 17 ARRFPDRIALVW----GDR-SWTWREIDARVDALAAAL-AARGVRKGDRILVHSRNCNQMFESMFAAFRLGAVWVPTNFR 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217306889 154 LTQKDILYRLQSSKANCIITNDVLAPAVDAVASKCENLHSKLIVSEnsregwgnlkelmkvflchpgwstvarswltATS 233
Cdd:PRK07470 91 QTPDEVAYLAEASGARAMICHADFPEHAAAVRAASPDLTHVVAIGG-------------------------------ARA 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217306889 234 TSLVQAILSllsswdyRHASDSHTCVKTKHNEIMAIFFTSGTSGYPKMTAHTHSSfgLGLSVNGRFwLDLTPsdvmwnts 313
Cdd:PRK07470 140 GLDYEALVA-------RHLGARVANAAVDHDDPCWFFFTSGTTGRPKAAVLTHGQ--MAFVITNHL-ADLMP-------- 201
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217306889 314 dtGWAKSAWSSVFSPWIQGACVftHHL--------------PRFEPTSILQTLSKYPITVFCSAPTVYRMLVQN-DITSY 378
Cdd:PRK07470 202 --GTTEQDASLVVAPLSHGAGI--HQLcqvargaatvllpsERFDPAEVWALVERHRVTNLFTVPTILKMLVEHpAVDRY 277
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217306889 379 KFKSLKHCVSAGEPITPDVTEKWRNKTGLDIYEGYGQTE-----TVL-ICGNF--KGMKIKPGSMGKPSPAFDVKIVDVN 450
Cdd:PRK07470 278 DHSSLRYVIYAGAPMYRADQKRALAKLGKVLVQYFGLGEvtgniTVLpPALHDaeDGPDARIGTCGFERTGMEVQIQDDE 357
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217306889 451 GNVLPPGQEGDI---GIQVlpnrpfglFTHYVDNPSKTASTLRGNFYITGDRGYMDKDGYFWFVARADDVILSSGYRIGP 527
Cdd:PRK07470 358 GRELPPGETGEIcviGPAV--------FAGYYNNPEANAKAFRDGWFRTGDLGHLDARGFLYITGRASDMYISGGSNVYP 429
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2217306889 528 FEVENALNEHPSVAESAVVSSPDPIRGEVVKAFVVLNpDYKSHDQEqlikEIQEHVKKTTAPYKYPRKV 596
Cdd:PRK07470 430 REIEEKLLTHPAVSEVAVLGVPDPVWGEVGVAVCVAR-DGAPVDEA----ELLAWLDGKVARYKLPKRF 493
|
|
| OSB_CoA_lg |
cd05912 |
O-succinylbenzoate-CoA ligase (also known as O-succinylbenzoate-CoA synthase, OSB-CoA ... |
260-596 |
7.99e-44 |
|
O-succinylbenzoate-CoA ligase (also known as O-succinylbenzoate-CoA synthase, OSB-CoA synthetase, or MenE); O-succinylbenzoic acid-CoA synthase catalyzes the coenzyme A (CoA)- and ATP-dependent conversion of o-succinylbenzoic acid to o-succinylbenzoyl-CoA. The reaction is the fourth step of the biosynthesis pathway of menaquinone (vitamin K2). In certain bacteria, menaquinone is used during fumarate reduction in anaerobic respiration. In cyanobacteria, the product of the menaquinone pathway is phylloquinone (2-methyl-3-phytyl-1,4-naphthoquinone), a molecule used exclusively as an electron transfer cofactor in Photosystem 1. In green sulfur bacteria and heliobacteria, menaquinones are used as loosely bound secondary electron acceptors in the photosynthetic reaction center.
Pssm-ID: 341238 [Multi-domain] Cd Length: 411 Bit Score: 162.13 E-value: 7.99e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217306889 260 KTKHNEIMAIFFTSGTSGYPK---MTAHTH------SSFGLGLSVNGRfWLDLTPsdvMWNTSdtgwaksAWSSVFSPWI 330
Cdd:cd05912 73 DVKLDDIATIMYTSGTTGKPKgvqQTFGNHwwsaigSALNLGLTEDDN-WLCALP---LFHIS-------GLSILMRSVI 141
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217306889 331 QGACVFTHhlPRFEPTSILQTLSKYPITVFCSAPTVYRMLVQNDITSYKfKSLKHCVSAGEPITPDVTEKWRNKtGLDIY 410
Cdd:cd05912 142 YGMTVYLV--DKFDAEQVLHLINSGKVTIISVVPTMLQRLLEILGEGYP-NNLRCILLGGGPAPKPLLEQCKEK-GIPVY 217
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217306889 411 EGYGQTETV--LICGNFKGMKIKPGSMGKPSPAFDVKIVDVNGnvlPPGQEGDIGIQVlPNRPFGlfthYVDNPSKTAST 488
Cdd:cd05912 218 QSYGMTETCsqIVTLSPEDALNKIGSAGKPLFPVELKIEDDGQ---PPYEVGEILLKG-PNVTKG----YLNRPDATEES 289
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217306889 489 LRGNFYITGDRGYMDKDGYFWFVARADDVILSSGYRIGPFEVENALNEHPSVAESAVVSSPDPIRGEVVKAFVVLNPDYk 568
Cdd:cd05912 290 FENGWFKTGDIGYLDEEGFLYVLDRRSDLIISGGENIYPAEIEEVLLSHPAIKEAGVVGIPDDKWGQVPVAFVVSERPI- 368
|
330 340
....*....|....*....|....*...
gi 2217306889 569 shDQEQLIKEIQEHVKKttapYKYPRKV 596
Cdd:cd05912 369 --SEEELIAYCSEKLAK----YKVPKKI 390
|
|
| A_NRPS |
cd05930 |
The adenylation domain of nonribosomal peptide synthetases (NRPS); The adenylation (A) domain ... |
253-594 |
1.59e-43 |
|
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: 161.93 E-value: 1.59e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217306889 253 SDSH-TCVKTKHNEIMAIFFTSGTSGYPKMTAHTHSSFglglsVNGRFW----LDLTPSDVMWNTSDTGWAKSAWSsVFS 327
Cdd:cd05930 81 EDSGaKLVLTDPDDLAYVIYTSGSTGKPKGVMVEHRGL-----VNLLLWmqeaYPLTPGDRVLQFTSFSFDVSVWE-IFG 154
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217306889 328 PWIQGACVftHHLP---RFEPTSILQTLSKYPITVFCSAPTVYRMLVQNDITSyKFKSLKHCVSAGEPITPDVTEKWR-N 403
Cdd:cd05930 155 ALLAGATL--VVLPeevRKDPEALADLLAEEGITVLHLTPSLLRLLLQELELA-ALPSLRLVLVGGEALPPDLVRRWReL 231
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217306889 404 KTGLDIYEGYGQTETVLICGNF--KGMKIKPGSM--GKPSPAFDVKIVDVNGNVLPPGQEGDI---GIQVlpNRpfGlft 476
Cdd:cd05930 232 LPGARLVNLYGPTEATVDATYYrvPPDDEEDGRVpiGRPIPNTRVYVLDENLRPVPPGVPGELyigGAGL--AR--G--- 304
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217306889 477 hYVDNPSKTASTLRGN-------FYITGDRGYMDKDGYFWFVARADDVILSSGYRIGPFEVENALNEHPSVAESAVVSSP 549
Cdd:cd05930 305 -YLNRPELTAERFVPNpfgpgerMYRTGDLVRWLPDGNLEFLGRIDDQVKIRGYRIELGEIEAALLAHPGVREAAVVARE 383
|
330 340 350 360
....*....|....*....|....*....|....*....|....*
gi 2217306889 550 DPIRGEVVKAFVVLNPdykshDQEQLIKEIQEHVKKTTAPYKYPR 594
Cdd:cd05930 384 DGDGEKRLVAYVVPDE-----GGELDEEELRAHLAERLPDYMVPS 423
|
|
| PRK06155 |
PRK06155 |
crotonobetaine/carnitine-CoA ligase; Provisional |
92-599 |
2.13e-43 |
|
crotonobetaine/carnitine-CoA ligase; Provisional
Pssm-ID: 235719 [Multi-domain] Cd Length: 542 Bit Score: 163.78 E-value: 2.13e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217306889 92 EMRWSFEELGSLSRKFANILSEAcSLQRGDRVILILPRVPEWWLANVACLRTGTVLIPGTTQLTQKDILYRLQSSKANCI 171
Cdd:PRK06155 44 GTRWTYAEAARAAAAAAHALAAA-GVKRGDRVALMCGNRIEFLDVFLGCAWLGAIAVPINTALRGPQLEHILRNSGARLL 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217306889 172 ITNDVLAPAVDAVASKCENLHSKLIVSENsregwgnlkelmkvflchPGWStVARSWLTATSTSLVQAIlsllsswdyrh 251
Cdd:PRK06155 123 VVEAALLAALEAADPGDLPLPAVWLLDAP------------------ASVS-VPAGWSTAPLPPLDAPA----------- 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217306889 252 asdshTCVKTKHNEIMAIFFTSGTSGYPKMTAHTHSSFglglsvngrFW--------LDLTPSDVMWNTSDTgWAKSAWS 323
Cdd:PRK06155 173 -----PAAAVQPGDTAAILYTSGTTGPSKGVCCPHAQF---------YWwgrnsaedLEIGADDVLYTTLPL-FHTNALN 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217306889 324 SVFSPWIQGAcvfTHHL-PRFEPTSILQTLSKYPITVFCSAPTVYRMLVQNDIT-SYKFKSLKHCVSAGEPitPDVTEKW 401
Cdd:PRK06155 238 AFFQALLAGA---TYVLePRFSASGFWPAVRRHGATVTYLLGAMVSILLSQPAReSDRAHRVRVALGPGVP--AALHAAF 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217306889 402 RNKTGLDIYEGYGQTETVLICGNFKGMKiKPGSMGKPSPAFDVKIVDVNGNVLPPGQEGDIGIQVlpNRPFGLFTHYVDN 481
Cdd:PRK06155 313 RERFGVDLLDGYGSTETNFVIAVTHGSQ-RPGSMGRLAPGFEARVVDEHDQELPDGEPGELLLRA--DEPFAFATGYFGM 389
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217306889 482 PSKTASTLRGNFYITGDRGYMDKDGYFWFVARADDVILSSGYRIGPFEVENALNEHPSVAESAVVSSPDPIRGEVVKAFV 561
Cdd:PRK06155 390 PEKTVEAWRNLWFHTGDRVVRDADGWFRFVDRIKDAIRRRGENISSFEVEQVLLSHPAVAAAAVFPVPSELGEDEVMAAV 469
|
490 500 510
....*....|....*....|....*....|....*...
gi 2217306889 562 VLNPDyKSHDQEQLIkeiqEHVKKTTAPYKYPRKVGIL 599
Cdd:PRK06155 470 VLRDG-TALEPVALV----RHCEPRLAYFAVPRYVEFV 502
|
|
| PRK06188 |
PRK06188 |
acyl-CoA synthetase; Validated |
78-596 |
2.87e-43 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 235731 [Multi-domain] Cd Length: 524 Bit Score: 162.85 E-value: 2.87e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217306889 78 PSNPAFWWINRngeemRWSFEELGSLSRKFANILsEACSLQRGDRVILILPRVPEWWLANVACLRTG---TVLIP-GTTQ 153
Cdd:PRK06188 26 PDRPALVLGDT-----RLTYGQLADRISRYIQAF-EALGLGTGDAVALLSLNRPEVLMAIGAAQLAGlrrTALHPlGSLD 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217306889 154 ltqkDILYRLQSSKANCIITNDvlAPAVD---AVASKCENLhsklivsensregwgnlkelmkvflchpgwstvaRSWLT 230
Cdd:PRK06188 100 ----DHAYVLEDAGISTLIVDP--APFVEralALLARVPSL----------------------------------KHVLT 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217306889 231 ATSTSLVQAILSLLSSWDYRHASDSHTcvktkHNEIMAIFFTSGTSGYPKMTAHTHSSFG---------LGLSVNGRFwL 301
Cdd:PRK06188 140 LGPVPDGVDLLAAAAKFGPAPLVAAAL-----PPDIAGLAYTGGTTGKPKGVMGTHRSIAtmaqiqlaeWEWPADPRF-L 213
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217306889 302 DLTPsdvmwnTSDTGWAKsawssvFSPWIQ-GACVftHHLPRFEPTSILQTLSKYPITVFCSAPT-VYRMLVQNDITSYK 379
Cdd:PRK06188 214 MCTP------LSHAGGAF------FLPTLLrGGTV--IVLAKFDPAEVLRAIEEQRITATFLVPTmIYALLDHPDLRTRD 279
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217306889 380 FKSLKHCVSAGEPITPDvtekwRNKTGLDIY-----EGYGQTE-----TVLICGNFKGMKIKP-GSMGKPSPAFDVKIVD 448
Cdd:PRK06188 280 LSSLETVYYGASPMSPV-----RLAEAIERFgpifaQYYGQTEapmviTYLRKRDHDPDDPKRlTSCGRPTPGLRVALLD 354
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217306889 449 VNGNVLPPGQEGDIGIqvlpnRPFGLFTHYVDNPSKTASTLRGNFYITGDRGYMDKDGYFWFVARADDVILSSGYRIGPF 528
Cdd:PRK06188 355 EDGREVAQGEVGEICV-----RGPLVMDGYWNRPEETAEAFRDGWLHTGDVAREDEDGFYYIVDRKKDMIVTGGFNVFPR 429
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2217306889 529 EVENALNEHPSVAESAVVSSPDPIRGEVVKAFVVLNPDyKSHDQEqlikEIQEHVKKTTAPYKYPRKV 596
Cdd:PRK06188 430 EVEDVLAEHPAVAQVAVIGVPDEKWGEAVTAVVVLRPG-AAVDAA----ELQAHVKERKGSVHAPKQV 492
|
|
| AA-adenyl-dom |
TIGR01733 |
amino acid adenylation domain; This model represents a domain responsible for the specific ... |
96-545 |
1.50e-42 |
|
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: 158.20 E-value: 1.50e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217306889 96 SFEELGSLSRKFANILSEACSLQRGDRVILILPRVPEWWLANVACLRTGTVLIPgttqLtqkDILY---RLQS----SKA 168
Cdd:TIGR01733 1 TYRELDERANRLARHLRAAGGVGPGDRVAVLLERSAELVVAILAVLKAGAAYVP----L---DPAYpaeRLAFiledAGA 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217306889 169 NCIITNDVLAPAVDAVASKCENlhsklivsensregwgnlkelmkvflchpgwstVARSWLTATSTSLVqailsllsswd 248
Cdd:TIGR01733 74 RLLLTDSALASRLAGLVLPVIL---------------------------------LDPLELAALDDAPA----------- 109
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217306889 249 yrhasDSHTCVKTKHNEIMAIFFTSGTSGYPKMTAHTHSSFGLGLSVNGRFWlDLTPSDVMWNTSDTGWAKSAWSsVFSP 328
Cdd:TIGR01733 110 -----PPPPDAPSGPDDLAYVIYTSGSTGRPKGVVVTHRSLVNLLAWLARRY-GLDPDDRVLQFASLSFDASVEE-IFGA 182
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217306889 329 WIQGACVF--THHLPRFEPTSILQTLSKYPITVFCSAPTVYRMLVQNDITSykFKSLKHCVSAGEPITPDVTEKWRNKTG 406
Cdd:TIGR01733 183 LLAGATLVvpPEDEERDDAALLAALIAEHPVTVLNLTPSLLALLAAALPPA--LASLRLVILGGEALTPALVDRWRARGP 260
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217306889 407 -LDIYEGYGQTETVLICGnfkgMKIKPGSM---------GKPSPAFDVKIVDVNGNVLPPGQEGDIGIqvlpnRPFGLFT 476
Cdd:TIGR01733 261 gARLINLYGPTETTVWST----ATLVDPDDaprespvpiGRPLANTRLYVLDDDLRPVPVGVVGELYI-----GGPGVAR 331
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2217306889 477 HYVDNPSKTA---------STLRGNFYITGDRGYMDKDGYFWFVARADDVILSSGYRIGPFEVENALNEHPSVAESAV 545
Cdd:TIGR01733 332 GYLNRPELTAerfvpdpfaGGDGARLYRTGDLVRYLPDGNLEFLGRIDDQVKIRGYRIELGEIEAALLRHPGVREAVV 409
|
|
| PRK07529 |
PRK07529 |
AMP-binding domain protein; Validated |
74-583 |
3.41e-42 |
|
AMP-binding domain protein; Validated
Pssm-ID: 236043 [Multi-domain] Cd Length: 632 Bit Score: 161.66 E-value: 3.41e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217306889 74 AGKKPSNPAFWWI---NRNGEEMRWSFEELgsLSR--KFANILSeACSLQRGDRVILILPRVPEWWLANVACLRTGTVlI 148
Cdd:PRK07529 35 AARHPDAPALSFLldaDPLDRPETWTYAEL--LADvtRTANLLH-SLGVGPGDVVAFLLPNLPETHFALWGGEAAGIA-N 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217306889 149 PGTTQLTQKDILYRLQSSKANCIITndvLAPAVDA-VASKCENLHSKLivsensregwGNLKELMKVFL--CHPGWSTVA 225
Cdd:PRK07529 111 PINPLLEPEQIAELLRAAGAKVLVT---LGPFPGTdIWQKVAEVLAAL----------PELRTVVEVDLarYLPGPKRLA 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217306889 226 RSWLTATSTSLVQAILSLLSswdyRHASDSHTCVKTKHNEIMAIFF-TSGTSGYPKMTAHTHSsfglGLSVNGrfW---- 300
Cdd:PRK07529 178 VPLIRRKAHARILDFDAELA----RQPGDRLFSGRPIGPDDVAAYFhTGGTTGMPKLAQHTHG----NEVANA--Wlgal 247
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217306889 301 -LDLTPSDVMW--------NTSDTGwaksawssVFSPWIQGACVFThhlprfePTS-----------ILQTLSKYPITVF 360
Cdd:PRK07529 248 lLGLGPGDTVFcglplfhvNALLVT--------GLAPLARGAHVVL-------ATPqgyrgpgvianFWKIVERYRINFL 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217306889 361 CSAPTVYRMLVQNDITSYKFKSLKHCVSAGEPITPDVTEKWRNKTGLDIYEGYGQTE-TVLICGNFKGMKIKPGSMGKPS 439
Cdd:PRK07529 313 SGVPTVYAALLQVPVDGHDISSLRYALCGAAPLPVEVFRRFEAATGVRIVEGYGLTEaTCVSSVNPPDGERRIGSVGLRL 392
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217306889 440 PAFDVKIV--DVNGNVLPPGQEGDIGIQVLPNrPfGLFTHYVDNPSKTASTLRGNFYITGDRGYMDKDGYFWFVARADDV 517
Cdd:PRK07529 393 PYQRVRVVilDDAGRYLRDCAVDEVGVLCIAG-P-NVFSGYLEAAHNKGLWLEDGWLNTGDLGRIDADGYFWLTGRAKDL 470
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2217306889 518 ILSSGYRIGPFEVENALNEHPSVAESAVVSSPDPIRGEVVKAFVVLNPDyKSHDQEQLIKEIQEHV 583
Cdd:PRK07529 471 IIRGGHNIDPAAIEEALLRHPAVALAAAVGRPDAHAGELPVAYVQLKPG-ASATEAELLAFARDHI 535
|
|
| PRK03640 |
PRK03640 |
o-succinylbenzoate--CoA ligase; |
91-596 |
8.18e-42 |
|
o-succinylbenzoate--CoA ligase;
Pssm-ID: 235146 [Multi-domain] Cd Length: 483 Bit Score: 157.82 E-value: 8.18e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217306889 91 EEMRWSFEELGSLSRKFANILSEACsLQRGDRVILILPRVPEWWLANVACLRTGTVLIPGTTQLTQKDILYRLQSSKANC 170
Cdd:PRK03640 24 EEKKVTFMELHEAVVSVAGKLAALG-VKKGDRVALLMKNGMEMILVIHALQQLGAVAVLLNTRLSREELLWQLDDAEVKC 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217306889 171 IITNDVLAPAVDAVASkcenlhskLIVSEnsregwgnlkeLMKVFLCHPgwstvarswltatstslvqailSLLSSWDYr 250
Cdd:PRK03640 103 LITDDDFEAKLIPGIS--------VKFAE-----------LMNGPKEEA----------------------EIQEEFDL- 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217306889 251 hasdshtcvktkhNEIMAIFFTSGTSGYPK---MTAHTH------SSFGLGLSVNGRfWLDLTPsdvMWNTSdtgwaksA 321
Cdd:PRK03640 141 -------------DEVATIMYTSGTTGKPKgviQTYGNHwwsavgSALNLGLTEDDC-WLAAVP---IFHIS-------G 196
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217306889 322 WSSVFSPWIQGACVFTHhlPRFEPTSILQTLSKYPITVFCSAPT-VYRMLVQNDITSYKfKSLKHCVSAGEPITPDVTEK 400
Cdd:PRK03640 197 LSILMRSVIYGMRVVLV--EKFDAEKINKLLQTGGVTIISVVSTmLQRLLERLGEGTYP-SSFRCMLLGGGPAPKPLLEQ 273
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217306889 401 WRNKtGLDIYEGYGQTETV-LICG-NFKGMKIKPGSMGKPSPAFDVKIVDvNGNVLPPGQEGDIGIQVlPNrpfgLFTHY 478
Cdd:PRK03640 274 CKEK-GIPVYQSYGMTETAsQIVTlSPEDALTKLGSAGKPLFPCELKIEK-DGVVVPPFEEGEIVVKG-PN----VTKGY 346
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217306889 479 VDNPSKTASTLRGNFYITGDRGYMDKDGYFWFVARADDVILSSGYRIGPFEVENALNEHPSVAESAVVSSPDPIRGEVVK 558
Cdd:PRK03640 347 LNREDATRETFQDGWFKTGDIGYLDEEGFLYVLDRRSDLIISGGENIYPAEIEEVLLSHPGVAEAGVVGVPDDKWGQVPV 426
|
490 500 510
....*....|....*....|....*....|....*...
gi 2217306889 559 AFVVLNpdyKSHDQEQLIKEIQEHVkkttAPYKYPRKV 596
Cdd:PRK03640 427 AFVVKS---GEVTEEELRHFCEEKL----AKYKVPKRF 457
|
|
| PRK07786 |
PRK07786 |
long-chain-fatty-acid--CoA ligase; Validated |
77-599 |
1.30e-41 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 169098 [Multi-domain] Cd Length: 542 Bit Score: 158.40 E-value: 1.30e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217306889 77 KPSNPAFWWInrnGEEMRWSfeELGSLSRKFANILSEAcSLQRGDRVILILPRVPEWWLANVACLRTGTVLIPGTTQLTQ 156
Cdd:PRK07786 30 QPDAPALRFL---GNTTTWR--ELDDRVAALAGALSRR-GVGFGDRVLILMLNRTEFVESVLAANMLGAIAVPVNFRLTP 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217306889 157 KDILYRLQSSKANCIITNDVLAPAVDAVASKCENLHSKLIVSENSREGWGNLKELMkvflchpgwstvarswltatstsl 236
Cdd:PRK07786 104 PEIAFLVSDCGAHVVVTEAALAPVATAVRDIVPLLSTVVVAGGSSDDSVLGYEDLL------------------------ 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217306889 237 vqailsllsswdyRHASDSHTCVKTKHNEIMAIFFTSGTSGYPKMTAHTHSSFGlGLSVNG-RFWLDLTPSDVMWNTSDT 315
Cdd:PRK07786 160 -------------AEAGPAHAPVDIPNDSPALIMYTSGTTGRPKGAVLTHANLT-GQAMTClRTNGADINSDVGFVGVPL 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217306889 316 gWAKSAWSSVFSPWIQGACVFTHHLPRFEPTSILQTLSKYPIT-VFCsAPTVYRMLVQNDITSYKFKSLKhCVSAGEPIT 394
Cdd:PRK07786 226 -FHIAGIGSMLPGLLLGAPTVIYPLGAFDPGQLLDVLEAEKVTgIFL-VPAQWQAVCAEQQARPRDLALR-VLSWGAAPA 302
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217306889 395 PDVTEKWRNKT--GLDIYEGYGQTE----TVLICGNFKGMKIkpGSMGKPSPAFDVKIVDVNGNVLPPGQEGDIgiqvlP 468
Cdd:PRK07786 303 SDTLLRQMAATfpEAQILAAFGQTEmspvTCMLLGEDAIRKL--GSVGKVIPTVAARVVDENMNDVPVGEVGEI-----V 375
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217306889 469 NRPFGLFTHYVDNPSKTASTLRGNFYITGDRGYMDKDGYFWFVARADDVILSSGYRIGPFEVENALNEHPSVAESAVVSS 548
Cdd:PRK07786 376 YRAPTLMSGYWNNPEATAEAFAGGWFHSGDLVRQDEEGYVWVVDRKKDMIISGGENIYCAEVENVLASHPDIVEVAVIGR 455
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|.
gi 2217306889 549 PDPIRGEVVKAFVVLNPDykshDQEQLIKEIQEHVKKTTAPYKYPRKVGIL 599
Cdd:PRK07786 456 ADEKWGEVPVAVAAVRND----DAALTLEDLAEFLTDRLARYKHPKALEIV 502
|
|
| caiC |
PRK08008 |
putative crotonobetaine/carnitine-CoA ligase; Validated |
72-598 |
1.66e-41 |
|
putative crotonobetaine/carnitine-CoA ligase; Validated
Pssm-ID: 181195 [Multi-domain] Cd Length: 517 Bit Score: 157.92 E-value: 1.66e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217306889 72 EKAGKKPSNPAFWWINRNGEEMRWSFEELGSLSRKFANiLSEACSLQRGDRVILILPRVPEW---WLAnVACLrtGTVLI 148
Cdd:PRK08008 15 DLADVYGHKTALIFESSGGVVRRYSYLELNEEINRTAN-LFYSLGIRKGDKVALHLDNCPEFifcWFG-LAKI--GAIMV 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217306889 149 PGTTQLTQKDILYRLQSSKANCIITNDVLAPAVDAVASKCEN-LHSKLIVSENSREGWG-----NLKELMKVFLCHpgws 222
Cdd:PRK08008 91 PINARLLREESAWILQNSQASLLVTSAQFYPMYRQIQQEDATpLRHICLTRVALPADDGvssftQLKAQQPATLCY---- 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217306889 223 tvarswltatstslvqaiLSLLSSWDyrhasdshtcvktkhneIMAIFFTSGTSGYPKMTAHTHSsfglglsvNGRF--- 299
Cdd:PRK08008 167 ------------------APPLSTDD-----------------TAEILFTSGTTSRPKGVVITHY--------NLRFagy 203
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217306889 300 ---W-LDLTPSDVMWNTSdtgwaksawssvfsPWIQGACVFTHHLPRFEPTSILQTLSKYPITVFCSAPTVYRMLVQNDI 375
Cdd:PRK08008 204 ysaWqCALRDDDVYLTVM--------------PAFHIDCQCTAAMAAFSAGATFVLLEKYSARAFWGQVCKYRATITECI 269
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217306889 376 TSYKFKSLKHCVSAGE------------PITPDVTEKWRNKTGLDIYEGYGQTETVL-ICGNFKGMKIKPGSMGKPSPAF 442
Cdd:PRK08008 270 PMMIRTLMVQPPSANDrqhclrevmfylNLSDQEKDAFEERFGVRLLTSYGMTETIVgIIGDRPGDKRRWPSIGRPGFCY 349
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217306889 443 DVKIVDVNGNVLPPGQEGDIGIQVLPNRPfgLFTHYVDNPSKTASTLRGNFYI-TGDRGYMDKDGYFWFVARADDVILSS 521
Cdd:PRK08008 350 EAEIRDDHNRPLPAGEIGEICIKGVPGKT--IFKEYYLDPKATAKVLEADGWLhTGDTGYVDEEGFFYFVDRRCNMIKRG 427
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2217306889 522 GYRIGPFEVENALNEHPSVAESAVVSSPDPIRGEVVKAFVVLNPDykshdqEQL-IKEIQEHVKKTTAPYKYPRKVGI 598
Cdd:PRK08008 428 GENVSCVELENIIATHPKIQDIVVVGIKDSIRDEAIKAFVVLNEG------ETLsEEEFFAFCEQNMAKFKVPSYLEI 499
|
|
| PRK07059 |
PRK07059 |
Long-chain-fatty-acid--CoA ligase; Validated |
96-596 |
2.91e-41 |
|
Long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 235923 [Multi-domain] Cd Length: 557 Bit Score: 157.87 E-value: 2.91e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217306889 96 SFEELGSLSRKFANILsEACSLQRGDRVILILPRVPEWWLANVACLRTGTVLIPGTTQLTQKDILYRLQSSKANCIITND 175
Cdd:PRK07059 50 TYGELDELSRALAAWL-QSRGLAKGARVAIMMPNVLQYPVAIAAVLRAGYVVVNVNPLYTPRELEHQLKDSGAEAIVVLE 128
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217306889 176 VLAPAVDAVASKCENLHsklIVSENSREGWGnLKELMKVFLCH------PGWSTV-ARSWLTATSTSlvqailsllsswd 248
Cdd:PRK07059 129 NFATTVQQVLAKTAVKH---VVVASMGDLLG-FKGHIVNFVVRrvkkmvPAWSLPgHVRFNDALAEG------------- 191
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217306889 249 yrhASDSHTCVKTKHNEIMAIFFTSGTSGYPKMTAHTHSSFglglsvngrfwldltPSDVMWNTSdtgWAKSAWSSvfsP 328
Cdd:PRK07059 192 ---ARQTFKPVKLGPDDVAFLQYTGGTTGVSKGATLLHRNI---------------VANVLQMEA---WLQPAFEK---K 247
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217306889 329 WIQGACVFTHHLP---------------RFEPTSIL-----------QTLSKYPITVFCSAPTVYRMLVQN-DITSYKFK 381
Cdd:PRK07059 248 PRPDQLNFVCALPlyhifaltvcgllgmRTGGRNILipnprdipgfiKELKKYQVHIFPAVNTLYNALLNNpDFDKLDFS 327
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217306889 382 SLKHCVSAGEPITPDVTEKWRNKTGLDIYEGYGQTET--VLICGNFKGMKIKpGSMGKPSPAFDVKIVDVNGNVLPPGQE 459
Cdd:PRK07059 328 KLIVANGGGMAVQRPVAERWLEMTGCPITEGYGLSETspVATCNPVDATEFS-GTIGLPLPSTEVSIRDDDGNDLPLGEP 406
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217306889 460 GDI---GIQVLPNrpfglfthYVDNPSKTASTLRGN-FYITGDRGYMDKDGYFWFVARADDVILSSGYRIGPFEVENALN 535
Cdd:PRK07059 407 GEIcirGPQVMAG--------YWNRPDETAKVMTADgFFRTGDVGVMDERGYTKIVDRKKDMILVSGFNVYPNEIEEVVA 478
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2217306889 536 EHPSVAESAVVSSPDPIRGEVVKAFVVlnpdykSHDQEQLIKEIQEHVKKTTAPYKYPRKV 596
Cdd:PRK07059 479 SHPGVLEVAAVGVPDEHSGEAVKLFVV------KKDPALTEEDVKAFCKERLTNYKRPKFV 533
|
|
| CHC_CoA_lg |
cd05903 |
Cyclohexanecarboxylate-CoA ligase (also called cyclohex-1-ene-1-carboxylate:CoA ligase); ... |
94-599 |
8.85e-41 |
|
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: 154.08 E-value: 8.85e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217306889 94 RWSFEELGSLSRKFANILSEAcSLQRGDRVILILPrvpEWWLANV---ACLRTGTVLIPGTTQLTQKDILYRLQSSKAnc 170
Cdd:cd05903 1 RLTYSELDTRADRLAAGLAAL-GVGPGDVVAFQLP---NWWEFAVlylACLRIGAVTNPILPFFREHELAFILRRAKA-- 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217306889 171 iitndvlapavdavaskcenlhsklivsensregwgnlkelmKVFLchpgwstVARSWLTatstslvqailsllsswdYR 250
Cdd:cd05903 75 ------------------------------------------KVFV-------VPERFRQ------------------FD 87
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217306889 251 HASDShtcvktkhNEIMAIFFTSGTSGYPKMTAHTHSSfglgLSVNGRFW---LDLTPSDVMWNTSDTGWAKSAWSSVFS 327
Cdd:cd05903 88 PAAMP--------DAVALLLFTSGTTGEPKGVMHSHNT----LSASIRQYaerLGLGPGDVFLVASPMAHQTGFVYGFTL 155
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217306889 328 PWIQGACVftHHLPRFEPTSILQTLSKYPITVFCSAPT-VYRMLVQNDITSYKFKSLKHCVSAGEPITPDVTEKWRNKTG 406
Cdd:cd05903 156 PLLLGAPV--VLQDIWDPDKALALMREHGVTFMMGATPfLTDLLNAVEEAGEPLSRLRTFVCGGATVPRSLARRAAELLG 233
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217306889 407 LDIYEGYGQTETVLICGNfkgmkIKPG-------SMGKPSPAFDVKIVDVNGNVLPPGQEGDIGIqvlpnRPFGLFTHYV 479
Cdd:cd05903 234 AKVCSAYGSTECPGAVTS-----ITPApedrrlyTDGRPLPGVEIKVVDDTGATLAPGVEGELLS-----RGPSVFLGYL 303
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217306889 480 DNPSKTASTLRGNFYITGDRGYMDKDGYFWFVARADDVILSSGYRIGPFEVENALNEHPSVAESAVVSSPDPIRGEVVKA 559
Cdd:cd05903 304 DRPDLTADAAPEGWFRTGDLARLDEDGYLRITGRSKDIIIRGGENIPVLEVEDLLLGHPGVIEAAVVALPDERLGERACA 383
|
490 500 510 520
....*....|....*....|....*....|....*....|.
gi 2217306889 560 FVVLNPdykshDQEQLIKEIQEHV-KKTTAPYKYPRKVGIL 599
Cdd:cd05903 384 VVVTKS-----GALLTFDELVAYLdRQGVAKQYWPERLVHV 419
|
|
| FACL_like_4 |
cd05944 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
263-599 |
2.49e-40 |
|
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: 151.09 E-value: 2.49e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217306889 263 HNEIMAIFFTSGTSGYPKMTAHTHSsfglGLSVNGrfW-----LDLTPSDVMWNTSDTGWAKSAWSSVFSPWIQGA-CVF 336
Cdd:cd05944 1 SDDVAAYFHTGGTTGTPKLAQHTHS----NEVYNA--WmlalnSLFDPDDVLLCGLPLFHVNGSVVTLLTPLASGAhVVL 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217306889 337 THHLPRFEPT---SILQTLSKYPITVFCSAPTVYRMLVQNDITSyKFKSLKHCVSAGEPITPDVTEKWRNKTGLDIYEGY 413
Cdd:cd05944 75 AGPAGYRNPGlfdNFWKLVERYRITSLSTVPTVYAALLQVPVNA-DISSLRFAMSGAAPLPVELRARFEDATGLPVVEGY 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217306889 414 GQTE-TVLICGNFKGMKIKPGSMGKPSPAFDVKIV--DVNGNVLPPGQEGDIGIQVLPNRpfGLFTHYVDNPSKTASTLR 490
Cdd:cd05944 154 GLTEaTCLVAVNPPDGPKRPGSVGLRLPYARVRIKvlDGVGRLLRDCAPDEVGEICVAGP--GVFGGYLYTEGNKNAFVA 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217306889 491 GNFYITGDRGYMDKDGYFWFVARADDVILSSGYRIGPFEVENALNEHPSVAESAVVSSPDPIRGEVVKAFVVLNPDYKSh 570
Cdd:cd05944 232 DGWLNTGDLGRLDADGYLFITGRAKDLIIRGGHNIDPALIEEALLRHPAVAFAGAVGQPDAHAGELPVAYVQLKPGAVV- 310
|
330 340
....*....|....*....|....*....
gi 2217306889 571 DQEQLIKEIQEHVKKTTApykYPRKVGIL 599
Cdd:cd05944 311 EEEELLAWARDHVPERAA---VPKHIEVL 336
|
|
| PLN02654 |
PLN02654 |
acetate-CoA ligase |
83-591 |
3.14e-40 |
|
acetate-CoA ligase
Pssm-ID: 215353 [Multi-domain] Cd Length: 666 Bit Score: 156.21 E-value: 3.14e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217306889 83 FWWINRNGEEMRWSFEELGSLSRKFANILsEACSLQRGDRVILILPRVPEWWLANVACLRTGTVLIPGTTQLTQKDILYR 162
Cdd:PLN02654 109 YWEGNEPGFDASLTYSELLDRVCQLANYL-KDVGVKKGDAVVIYLPMLMELPIAMLACARIGAVHSVVFAGFSAESLAQR 187
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217306889 163 LQSSKANCIIT-NDV--------LAPAVDAVASKCENLHSKL---IVSENS----REG--WGNLKELMkvflchpgWSTV 224
Cdd:PLN02654 188 IVDCKPKVVITcNAVkrgpktinLKDIVDAALDESAKNGVSVgicLTYENQlamkREDtkWQEGRDVW--------WQDV 259
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217306889 225 ARSWLTATSTSLVQAilsllsswdyrhasdshtcvktkhNEIMAIFFTSGTSGYPKMTAHTHSSFGLGLSVNGRFWLDLT 304
Cdd:PLN02654 260 VPNYPTKCEVEWVDA------------------------EDPLFLLYTSGSTGKPKGVLHTTGGYMVYTATTFKYAFDYK 315
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217306889 305 PSDVMWNTSDTGWAKSAWSSVFSPWIQGACVFTHH-LPRF-EPTSILQTLSKYPITVFCSAPTVYRMLVQND---ITSYK 379
Cdd:PLN02654 316 PTDVYWCTADCGWITGHSYVTYGPMLNGATVLVFEgAPNYpDSGRCWDIVDKYKVTIFYTAPTLVRSLMRDGdeyVTRHS 395
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217306889 380 FKSLKHCVSAGEPITPDVTEKWRNKTG---LDIYEGYGQTETvlicGNFKGMKI------KPGSMGKPSPAFDVKIVDVN 450
Cdd:PLN02654 396 RKSLRVLGSVGEPINPSAWRWFFNVVGdsrCPISDTWWQTET----GGFMITPLpgawpqKPGSATFPFFGVQPVIVDEK 471
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217306889 451 GNVLPPGQEGDIGIQvlPNRPFGLFTHYVDNPSKTASTLR--GNFYITGDRGYMDKDGYFWFVARADDVILSSGYRIGPF 528
Cdd:PLN02654 472 GKEIEGECSGYLCVK--KSWPGAFRTLYGDHERYETTYFKpfAGYYFSGDGCSRDKDGYYWLTGRVDDVINVSGHRIGTA 549
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2217306889 529 EVENALNEHPSVAESAVVSSPDPIRGEVVKAFVVLNP--DYKSHDQEQLIKEIQEHVKKTTAPYK 591
Cdd:PLN02654 550 EVESALVSHPQCAEAAVVGIEHEVKGQGIYAFVTLVEgvPYSEELRKSLILTVRNQIGAFAAPDK 614
|
|
| PRK12583 |
PRK12583 |
acyl-CoA synthetase; Provisional |
91-594 |
3.29e-40 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 237145 [Multi-domain] Cd Length: 558 Bit Score: 154.93 E-value: 3.29e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217306889 91 EEMRWSFEELGSLSRKFANILSeACSLQRGDRVILILPRVPEWWLANVACLRTGTVLIPGTTQLTQKDILYRLQSSKANC 170
Cdd:PRK12583 42 QALRYTWRQLADAVDRLARGLL-ALGVQPGDRVGIWAPNCAEWLLTQFATARIGAILVNINPAYRASELEYALGQSGVRW 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217306889 171 IITNDvlapavdavASKCENLHSKL--IVSENSREGWGNLK-----ELMKVFLCHP-------GWSTVARSWLTATSTSL 236
Cdd:PRK12583 121 VICAD---------AFKTSDYHAMLqeLLPGLAEGQPGALAcerlpELRGVVSLAPapppgflAWHELQARGETVSREAL 191
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217306889 237 VQAILSLlsswdyrhasdshtcvktKHNEIMAIFFTSGTSGYPKMTAHTHSSfglgLSVNGRF---WLDLTPSDVM---- 309
Cdd:PRK12583 192 AERQASL------------------DRDDPINIQYTSGTTGFPKGATLSHHN----ILNNGYFvaeSLGLTEHDRLcvpv 249
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217306889 310 --WNTSDTGWAKSAWSSVfspwiqGACVFthhLPR--FEPTSILQTLSKYPITVFCSAPTVY-RMLVQNDITSYKFKSLK 384
Cdd:PRK12583 250 plYHCFGMVLANLGCMTV------GACLV---YPNeaFDPLATLQAVEEERCTALYGVPTMFiAELDHPQRGNFDLSSLR 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217306889 385 HCVSAGEPITPDVTEKWRNKTGL-DIYEGYGQTET---VLICGNFKGMKIKPGSMGKPSPAFDVKIVDVNGNVLPPGQEG 460
Cdd:PRK12583 321 TGIMAGAPCPIEVMRRVMDEMHMaEVQIAYGMTETspvSLQTTAADDLERRVETVGRTQPHLEVKVVDPDGATVPRGEIG 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217306889 461 DigiqvLPNRPFGLFTHYVDNPSKTASTLRGNFYI-TGDRGYMDKDGYFWFVARADDVILSSGYRIGPFEVENALNEHPS 539
Cdd:PRK12583 401 E-----LCTRGYSVMKGYWNNPEATAESIDEDGWMhTGDLATMDEQGYVRIVGRSKDMIIRGGENIYPREIEEFLFTHPA 475
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*
gi 2217306889 540 VAESAVVSSPDPIRGEVVKAFVVLNPDYKSHDQeqlikEIQEHVKKTTAPYKYPR 594
Cdd:PRK12583 476 VADVQVFGVPDEKYGEEIVAWVRLHPGHAASEE-----ELREFCKARIAHFKVPR 525
|
|
| PRK06087 |
PRK06087 |
medium-chain fatty-acid--CoA ligase; |
94-599 |
4.36e-40 |
|
medium-chain fatty-acid--CoA ligase;
Pssm-ID: 180393 [Multi-domain] Cd Length: 547 Bit Score: 154.14 E-value: 4.36e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217306889 94 RWSFEELGSLSRKFANILSeACSLQRGDRVILILPRVPEWWLANVACLRTGTVLIPGTTQLTQKDILYRLQSSKANCIIt 173
Cdd:PRK06087 49 SYTYSALDHAASRLANWLL-AKGIEPGDRVAFQLPGWCEFTIIYLACLKVGAVSVPLLPSWREAELVWVLNKCQAKMFF- 126
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217306889 174 ndvlAPAVDAvaskcENLHSKLIVSenSREGWGNLKELMKVFLCHPGWSTVARSWLTATSTSLVQAIlsllsswdyrhas 253
Cdd:PRK06087 127 ----APTLFK-----QTRPVDLILP--LQNQLPQLQQIVGVDKLAPATSSLSLSQIIADYEPLTTAI------------- 182
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217306889 254 dshtcvKTKHNEIMAIFFTSGTSGYPKMTAHTHSSFGLG-LSVNGRfwLDLTPSDVMWNTSDTGWAKSAWSSVFSPWIQG 332
Cdd:PRK06087 183 ------TTHGDELAAVLFTSGTEGLPKGVMLTHNNILASeRAYCAR--LNLTWQDVFMMPAPLGHATGFLHGVTAPFLIG 254
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217306889 333 ACVFThhLPRFEPTSILQTLSKYPITVFCSA-PTVYRMLVQNDITSYKFKSLKHCVSAGEPITPDVTEK-WRNktGLDIY 410
Cdd:PRK06087 255 ARSVL--LDIFTPDACLALLEQQRCTCMLGAtPFIYDLLNLLEKQPADLSALRFFLCGGTTIPKKVAREcQQR--GIKLL 330
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217306889 411 EGYGQTETV--LICGNFKGMKIKPGSMGKPSPAFDVKIVDVNGNVLPPGQEGDiGIQVLPNrpfgLFTHYVDNPSKTAST 488
Cdd:PRK06087 331 SVYGSTESSphAVVNLDDPLSRFMHTDGYAAAGVEIKVVDEARKTLPPGCEGE-EASRGPN----VFMGYLDEPELTARA 405
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217306889 489 L--RGNFYiTGDRGYMDKDGYFWFVARADDVILSSGYRIGPFEVENALNEHPSVAESAVVSSPDPIRGEVVKAFVVLNPD 566
Cdd:PRK06087 406 LdeEGWYY-SGDLCRMDEAGYIKITGRKKDIIVRGGENISSREVEDILLQHPKIHDACVVAMPDERLGERSCAYVVLKAP 484
|
490 500 510
....*....|....*....|....*....|...
gi 2217306889 567 YKSHDQEQLIKEIQEhvkKTTAPYKYPRKVGIL 599
Cdd:PRK06087 485 HHSLTLEEVVAFFSR---KRVAKYKYPEHIVVI 514
|
|
| PRK13382 |
PRK13382 |
bile acid CoA ligase; |
269-599 |
6.62e-40 |
|
bile acid CoA ligase;
Pssm-ID: 172019 [Multi-domain] Cd Length: 537 Bit Score: 153.76 E-value: 6.62e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217306889 269 IFFTSGTSGYPKMTAHTHSSFGLGLSVngrfWLDLTPsdvmWNTSDTGWAKSAwssVFSPWIQGACVFTHHLP------- 341
Cdd:PRK13382 201 ILLTSGTTGTPKGARRSGPGGIGTLKA----ILDRTP----WRAEEPTVIVAP---MFHAWGFSQLVLAASLActivtrr 269
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217306889 342 RFEPTSILQTLSKYPITVFCSAPTVYRM---LVQNDITSYKFKSLKHCVSAGEPITPDVTEKWRNKTGLDIYEGYGQTET 418
Cdd:PRK13382 270 RFDPEATLDLIDRHRATGLAVVPVMFDRimdLPAEVRNRYSGRSLRFAAASGSRMRPDVVIAFMDQFGDVIYNNYNATEA 349
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217306889 419 VLIC-GNFKGMKIKPGSMGKPSPAFDVKIVDVNGNVLPPGQEGdiGIQVLPNRPFGLFThyvdnPSKTASTLRGnFYITG 497
Cdd:PRK13382 350 GMIAtATPADLRAAPDTAGRPAEGTEIRILDQDFREVPTGEVG--TIFVRNDTQFDGYT-----SGSTKDFHDG-FMASG 421
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217306889 498 DRGYMDKDGYFWFVARADDVILSSGYRIGPFEVENALNEHPSVAESAVVSSPDPIRGEVVKAFVVLNPdykshDQEQLIK 577
Cdd:PRK13382 422 DVGYLDENGRLFVVGRDDEMIVSGGENVYPIEVEKTLATHPDVAEAAVIGVDDEQYGQRLAAFVVLKP-----GASATPE 496
|
330 340
....*....|....*....|..
gi 2217306889 578 EIQEHVKKTTAPYKYPRKVGIL 599
Cdd:PRK13382 497 TLKQHVRDNLANYKVPRDIVVL 518
|
|
| DltA |
cd05945 |
D-alanine:D-alanyl carrier protein ligase (DltA) and similar proteins; This family includes ... |
264-595 |
8.51e-40 |
|
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: 151.63 E-value: 8.51e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217306889 264 NEIMAIFFTSGTSGYPKMTAHTHS---SFGLGLsvNGRFwlDLTPSDVMWNTSDtgwaksaWS---SVFS---PWIQGAC 334
Cdd:cd05945 97 DDNAYIIFTSGSTGRPKGVQISHDnlvSFTNWM--LSDF--PLGPGDVFLNQAP-------FSfdlSVMDlypALASGAT 165
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217306889 335 VFThhLPRFE---PTSILQTLSKYPITVFCSAPTVYRMLVQN-DITSYKFKSLKHCVSAGEPITPDVTEKWRNKT-GLDI 409
Cdd:cd05945 166 LVP--VPRDAtadPKQLFRFLAEHGITVWVSTPSFAAMCLLSpTFTPESLPSLRHFLFCGEVLPHKTARALQQRFpDARI 243
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217306889 410 YEGYGQTETVLICgnfKGMKIKPGSM--------GKPSPAFDVKIVDVNGNVLPPGQEGDI---GIQVlpnrpfglFTHY 478
Cdd:cd05945 244 YNTYGPTEATVAV---TYIEVTPEVLdgydrlpiGYAKPGAKLVILDEDGRPVPPGEKGELvisGPSV--------SKGY 312
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217306889 479 VDNPSKTASTLRGNF----YITGDRGYMDKDGYFWFVARADDVILSSGYRIGPFEVENALNEHPSVAESAVVSSPDPIRG 554
Cdd:cd05945 313 LNNPEKTAAAFFPDEgqraYRTGDLVRLEADGLLFYRGRLDFQVKLNGYRIELEEIEAALRQVPGVKEAVVVPKYKGEKV 392
|
330 340 350 360
....*....|....*....|....*....|....*....|.
gi 2217306889 555 EVVKAFVVLNPdyksHDQEQLIKEIQEHVKKTTAPYKYPRK 595
Cdd:cd05945 393 TELIAFVVPKP----GAEAGLTKAIKAELAERLPPYMIPRR 429
|
|
| PRK07787 |
PRK07787 |
acyl-CoA synthetase; Validated |
338-596 |
1.97e-39 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236096 [Multi-domain] Cd Length: 471 Bit Score: 150.91 E-value: 1.97e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217306889 338 HHLPRFEPTSILQTLSKyPITVFCSAPTVYRMLVQNDITSYKFKSLKHCVSAGEPITPDVTEKWRNKTGLDIYEGYGQTE 417
Cdd:PRK07787 199 VHTGRPTPEAYAQALSE-GGTLYFGVPTVWSRIAADPEAARALRGARLLVSGSAALPVPVFDRLAALTGHRPVERYGMTE 277
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217306889 418 TVLICGNFKGMKIKPGSMGKPSPAFDVKIVDVNGNVLPPGQEGDIGIQVlpnRPFGLFTHYVDNPSKTASTLRGN-FYIT 496
Cdd:PRK07787 278 TLITLSTRADGERRPGWVGLPLAGVETRLVDEDGGPVPHDGETVGELQV---RGPTLFDGYLNRPDATAAAFTADgWFRT 354
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217306889 497 GDRGYMDKDGYFWFVAR-ADDVILSSGYRIGPFEVENALNEHPSVAESAVVSSPDPIRGEVVKAFVVLNPDYkshDQEQL 575
Cdd:PRK07787 355 GDVAVVDPDGMHRIVGReSTDLIKSGGYRIGAGEIETALLGHPGVREAAVVGVPDDDLGQRIVAYVVGADDV---AADEL 431
|
250 260
....*....|....*....|.
gi 2217306889 576 IkeiqEHVKKTTAPYKYPRKV 596
Cdd:PRK07787 432 I----DFVAQQLSVHKRPREV 448
|
|
| FACL_like_6 |
cd05922 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
213-599 |
1.45e-38 |
|
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ATP-dependent activation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions.
Pssm-ID: 341246 [Multi-domain] Cd Length: 457 Bit Score: 148.36 E-value: 1.45e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217306889 213 KVFLCHPGWSTVARSWLTATSTSLVqaILSLLSSWDYRHASDSHTCVktkHNEIMAIFFTSGTSGYPKMTAHTHSSFGLG 292
Cdd:cd05922 71 RIVLADAGAADRLRDALPASPDPGT--VLDADGIRAARASAPAHEVS---HEDLALLLYTSGSTGSPKLVRLSHQNLLAN 145
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217306889 293 L-SVNGRfwLDLTPSDVMWNTSDTGWAkSAWSSVFSPWIQGACVFTHHLPRFePTSILQTLSKYPITVFCSAPTVYRMLV 371
Cdd:cd05922 146 ArSIAEY--LGITADDRALTVLPLSYD-YGLSVLNTHLLRGATLVLTNDGVL-DDAFWEDLREHGATGLAGVPSTYAMLT 221
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217306889 372 QNDITSYKFKSLKHCVSAGEPITPDVTEKWRNK-TGLDIYEGYGQTETvlicgnFKGMKI--------KPGSMGKPSPAF 442
Cdd:cd05922 222 RLGFDPAKLPSLRYLTQAGGRLPQETIARLRELlPGAQVYVMYGQTEA------TRRMTYlpperileKPGSIGLAIPGG 295
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217306889 443 DVKIVDVNGNVLPPGQEGDIGiqvlPNRPFGLFTHYVDNPSKTASTLRGNFYITGDRGYMDKDGYFWFVARADDVILSSG 522
Cdd:cd05922 296 EFEILDDDGTPTPPGEPGEIV----HRGPNVMKGYWNDPPYRRKEGRGGGVLHTGDLARRDEDGFLFIVGRRDRMIKLFG 371
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2217306889 523 YRIGPFEVENALNEHPSVAESAVVSSPDPIrGEVVKAFVVLNPDYKSHDqeqlikeIQEHVKKTTAPYKYPRKVGIL 599
Cdd:cd05922 372 NRISPTEIEAAARSIGLIIEAAAVGLPDPL-GEKLALFVTAPDKIDPKD-------VLRSLAERLPPYKVPATVRVV 440
|
|
| BACL_like |
cd05929 |
Bacterial Bile acid CoA ligases and similar proteins; Bile acid-Coenzyme A ligase catalyzes ... |
340-596 |
2.89e-38 |
|
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: 147.91 E-value: 2.89e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217306889 340 LPRFEPTSILQTLSKYPITVFCSAPTVY-RML-----VQNditSYKFKSLKHCVSAGEPITPDVTEKWRNKTGLDIYEGY 413
Cdd:cd05929 200 MEKFDPEEFLRLIERYRVTFAQFVPTMFvRLLklpeaVRN---AYDLSSLKRVIHAAAPCPPWVKEQWIDWGGPIIWEYY 276
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217306889 414 GQTETV-LICGNFKGMKIKPGSMGKPSPAfDVKIVDVNGNVLPPGQEGDIgiQVLPNRPFglftHYVDNPSKTA-STLRG 491
Cdd:cd05929 277 GGTEGQgLTIINGEEWLTHPGSVGRAVLG-KVHILDEDGNEVPPGEIGEV--YFANGPGF----EYTNDPEKTAaARNEG 349
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217306889 492 NFYITGDRGYMDKDGYFWFVARADDVILSSGYRIGPFEVENALNEHPSVAESAVVSSPDPIRGEVVKAfvVLNPDYKSHD 571
Cdd:cd05929 350 GWSTLGDVGYLDEDGYLYLTDRRSDMIISGGVNIYPQEIENALIAHPKVLDAAVVGVPDEELGQRVHA--VVQPAPGADA 427
|
250 260
....*....|....*....|....*
gi 2217306889 572 QEQLIKEIQEHVKKTTAPYKYPRKV 596
Cdd:cd05929 428 GTALAEELIAFLRDRLSRYKCPRSI 452
|
|
| PRK13390 |
PRK13390 |
acyl-CoA synthetase; Provisional |
78-596 |
4.35e-38 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 139538 [Multi-domain] Cd Length: 501 Bit Score: 147.85 E-value: 4.35e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217306889 78 PSNPAFWwINRNGEEMrwSFEELGSLSRKFANILSEAcSLQRGDRVILILPRVPEWWLANVACLRTGTVLIPGTTQLTQK 157
Cdd:PRK13390 11 PDRPAVI-VAETGEQV--SYRQLDDDSAALARVLYDA-GLRTGDVVALLSDNSPEALVVLWAALRSGLYITAINHHLTAP 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217306889 158 DILYRLQSSKANCIitndVLAPAVDAVASKCENLHSKLIVSENSREGWGNLKelmkvflchpgwstvarSWLTATSTSLV 237
Cdd:PRK13390 87 EADYIVGDSGARVL----VASAALDGLAAKVGADLPLRLSFGGEIDGFGSFE-----------------AALAGAGPRLT 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217306889 238 QailsllsswdyrhasdsHTCvktkhNEIMaiFFTSGTSGYPK-----MTAHTHSSFGLGLSVNGRFWLDLTPSDVMWNT 312
Cdd:PRK13390 146 E-----------------QPC-----GAVM--LYSSGTTGFPKgiqpdLPGRDVDAPGDPIVAIARAFYDISESDIYYSS 201
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217306889 313 SDTGWAKS-AWSSVFSPwIQGACVFTHhlpRFEPTSILQTLSKYPITVFCSAPTVY-RMLVQND--ITSYKFKSLKHCVS 388
Cdd:PRK13390 202 APIYHAAPlRWCSMVHA-LGGTVVLAK---RFDAQATLGHVERYRITVTQMVPTMFvRLLKLDAdvRTRYDVSSLRAVIH 277
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217306889 389 AGEPITPDVTEKWRNKTGLDIYEGYGQTE----TVLICGNFKGmkiKPGSMGKpSPAFDVKIVDVNGNVLPPGQEGDIGI 464
Cdd:PRK13390 278 AAAPCPVDVKHAMIDWLGPIVYEYYSSTEahgmTFIDSPDWLA---HPGSVGR-SVLGDLHICDDDGNELPAGRIGTVYF 353
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217306889 465 Q--VLPNRpfglfthYVDNPSKTASTLRGN--FYIT-GDRGYMDKDGYFWFVARADDVILSSGYRIGPFEVENALNEHPS 539
Cdd:PRK13390 354 ErdRLPFR-------YLNDPEKTAAAQHPAhpFWTTvGDLGSVDEDGYLYLADRKSFMIISGGVNIYPQETENALTMHPA 426
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*..
gi 2217306889 540 VAESAVVSSPDPIRGEVVKAFVVLNPDYKShdQEQLIKEIQEHVKKTTAPYKYPRKV 596
Cdd:PRK13390 427 VHDVAVIGVPDPEMGEQVKAVIQLVEGIRG--SDELARELIDYTRSRIAHYKAPRSV 481
|
|
| PRK12406 |
PRK12406 |
long-chain-fatty-acid--CoA ligase; Provisional |
341-598 |
5.98e-38 |
|
long-chain-fatty-acid--CoA ligase; Provisional
Pssm-ID: 183506 [Multi-domain] Cd Length: 509 Bit Score: 147.54 E-value: 5.98e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217306889 341 PRFEPTSILQTLSKYPITVFCSAPTVY-RML-----VQNditSYKFKSLKHCVSAGEPITPDVT----EKWrnktGLDIY 410
Cdd:PRK12406 228 PRFDPEELLQLIERHRITHMHMVPTMFiRLLklpeeVRA---KYDVSSLRHVIHAAAPCPADVKramiEWW----GPVIY 300
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217306889 411 EGYGQTET--VLICGNFKGMKiKPGSMGKPSPAFDVKIVDVNGNVLPPGQEGDIGIQVLPNrpfGLFThYVDNPSKTAST 488
Cdd:PRK12406 301 EYYGSTESgaVTFATSEDALS-HPGTVGKAAPGAELRFVDEDGRPLPQGEIGEIYSRIAGN---PDFT-YHNKPEKRAEI 375
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217306889 489 LRGNFYITGDRGYMDKDGYFWFVARADDVILSSGYRIGPFEVENALNEHPSVAESAVVSSPDPIRGEVVKAFVVLNPDyK 568
Cdd:PRK12406 376 DRGGFITSGDVGYLDADGYLFLCDRKRDMVISGGVNIYPAEIEAVLHAVPGVHDCAVFGIPDAEFGEALMAVVEPQPG-A 454
|
250 260 270
....*....|....*....|....*....|
gi 2217306889 569 SHDQEqlikEIQEHVKKTTAPYKYPRKVGI 598
Cdd:PRK12406 455 TLDEA----DIRAQLKARLAGYKVPKHIEI 480
|
|
| PRK05677 |
PRK05677 |
long-chain-fatty-acid--CoA ligase; Validated |
96-608 |
8.55e-38 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 168170 [Multi-domain] Cd Length: 562 Bit Score: 147.99 E-value: 8.55e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217306889 96 SFEELGSLSRKFANILSEACSLQRGDRVILILPRVPEWWLANVACLRTGTVLIPGTTQLTQKDILYRLQSSKANCIITND 175
Cdd:PRK05677 51 TYGELYKLSGAFAAWLQQHTDLKPGDRIAVQLPNVLQYPVAVFGAMRAGLIVVNTNPLYTAREMEHQFNDSGAKALVCLA 130
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217306889 176 VLAPAVDAVASKCENLHskLIVSEnsregWGNLKELMKVFLCHPGWSTVARswlTATSTSLVQAI--LSLLSswdyRHAS 253
Cdd:PRK05677 131 NMAHLAEKVLPKTGVKH--VIVTE-----VADMLPPLKRLLINAVVKHVKK---MVPAYHLPQAVkfNDALA----KGAG 196
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217306889 254 DSHTCVKTKHNEIMAIFFTSGTSGYPKMTAHTHSSfglgLSVNgrfWLDLTP--SDVMWNTSDTGWAKSAWSSVFSpwiq 331
Cdd:PRK05677 197 QPVTEANPQADDVAVLQYTGGTTGVAKGAMLTHRN----LVAN---MLQCRAlmGSNLNEGCEILIAPLPLYHIYA---- 265
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217306889 332 gacvFTHHL---------------PRFEPtSILQTLSKYPITVFCSAPTVYRMLVQN-DITSYKFKSLKHCVSAGEPITP 395
Cdd:PRK05677 266 ----FTFHCmammlignhnilisnPRDLP-AMVKELGKWKFSGFVGLNTLFVALCNNeAFRKLDFSALKLTLSGGMALQL 340
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217306889 396 DVTEKWRNKTGLDIYEGYGQTETV-LICGNFKGmKIKPGSMGKPSPAFDVKIVDVNGNVLPPGQEGDI---GIQVLPNrp 471
Cdd:PRK05677 341 ATAERWKEVTGCAICEGYGMTETSpVVSVNPSQ-AIQVGTIGIPVPSTLCKVIDDDGNELPLGEVGELcvkGPQVMKG-- 417
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217306889 472 fglfthYVDNPSKTASTLRGNFYI-TGDRGYMDKDGYFWFVARADDVILSSGYRIGPFEVENALNEHPSVAESAVVSSPD 550
Cdd:PRK05677 418 ------YWQRPEATDEILDSDGWLkTGDIALIQEDGYMRIVDRKKDMILVSGFNVYPNELEDVLAALPGVLQCAAIGVPD 491
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2217306889 551 PIRGEVVKAFVVLNPDykshdqEQLIKE-IQEHVKKTTAPYKYPRKV---GILIITNICSVL 608
Cdd:PRK05677 492 EKSGEAIKVFVVVKPG------ETLTKEqVMEHMRANLTGYKVPKAVefrDELPTTNVGKIL 547
|
|
| FACL_like_2 |
cd05917 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
269-596 |
1.36e-37 |
|
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: 142.80 E-value: 1.36e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217306889 269 IFFTSGTSGYPKMTAHTHSSFglgLSvNGRF---WLDLTPSDVM----------------WNTSDTGwaksawssvfspw 329
Cdd:cd05917 7 IQFTSGTTGSPKGATLTHHNI---VN-NGYFigeRLGLTEQDRLcipvplfhcfgsvlgvLACLTHG------------- 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217306889 330 iqGACVFTHhlPRFEPTSILQTLSKYPITVFCSAPTVY-RMLVQNDITSYKFKSLKHCVSAGEPITPDVTEKWRNKTGL- 407
Cdd:cd05917 70 --ATMVFPS--PSFDPLAVLEAIEKEKCTALHGVPTMFiAELEHPDFDKFDLSSLRTGIMAGAPCPPELMKRVIEVMNMk 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217306889 408 DIYEGYGQTETVLICgnFKGMKIKP-----GSMGKPSPAFDVKIVDVNGNVLPP-GQEGDIGIqvlpnRPFGLFTHYVDN 481
Cdd:cd05917 146 DVTIAYGMTETSPVS--TQTRTDDSiekrvNTVGRIMPHTEAKIVDPEGGIVPPvGVPGELCI-----RGYSVMKGYWND 218
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217306889 482 PSKTASTLRG-NFYITGDRGYMDKDGYFWFVARADDVILSSGYRIGPFEVENALNEHPSVAESAVVSSPDPIRGEVVKAF 560
Cdd:cd05917 219 PEKTAEAIDGdGWLHTGDLAVMDEDGYCRIVGRIKDMIIRGGENIYPREIEEFLHTHPKVSDVQVVGVPDERYGEEVCAW 298
|
330 340 350
....*....|....*....|....*....|....*.
gi 2217306889 561 VVLNPDYKSHDQeqlikEIQEHVKKTTAPYKYPRKV 596
Cdd:cd05917 299 IRLKEGAELTEE-----DIKAYCKGKIAHYKVPRYV 329
|
|
| PRK08751 |
PRK08751 |
long-chain fatty acid--CoA ligase; |
96-596 |
6.31e-37 |
|
long-chain fatty acid--CoA ligase;
Pssm-ID: 181546 [Multi-domain] Cd Length: 560 Bit Score: 145.40 E-value: 6.31e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217306889 96 SFEELGSLSRKFANILSEACSLQRGDRVILILPRVPEWWLANVACLRTGTVLIPGTTQLTQKDILYRLQSSKANCIITND 175
Cdd:PRK08751 52 TYREADQLVEQFAAYLLGELQLKKGDRVALMMPNCLQYPIATFGVLRAGLTVVNVNPLYTPRELKHQLIDSGASVLVVID 131
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217306889 176 VLAPAVDAVASKCEnlhskliVSENSREGWGNLKELMKVFLCHPGWSTVAR---SWLTATSTSLVQAiLSLLSswdyRHa 252
Cdd:PRK08751 132 NFGTTVQQVIADTP-------VKQVITTGLGDMLGFPKAALVNFVVKYVKKlvpEYRINGAIRFREA-LALGR----KH- 198
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217306889 253 sdSHTCVKTKHNEIMAIFFTSGTSGYPKMTAHTHSSFGLGLSVNGRfWLDLTpsdvmwNTSDTG-------------WAK 319
Cdd:PRK08751 199 --SMPTLQIEPDDIAFLQYTGGTTGVAKGAMLTHRNLVANMQQAHQ-WLAGT------GKLEEGcevvitalplyhiFAL 269
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217306889 320 SAWSSVFSPWiqGACvftHHL---PRFEPTSIlQTLSKYPITVFCSAPTVYRMLVQN-DITSYKFKSLKHCVSAGEPITP 395
Cdd:PRK08751 270 TANGLVFMKI--GGC---NHLisnPRDMPGFV-KELKKTRFTAFTGVNTLFNGLLNTpGFDQIDFSSLKMTLGGGMAVQR 343
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217306889 396 DVTEKWRNKTGLDIYEGYGQTETV-LICGNFKGMKIKPGSMGKPSPAFDVKIVDVNGNVLPPGQEGDI---GIQVLPNrp 471
Cdd:PRK08751 344 SVAERWKQVTGLTLVEAYGLTETSpAACINPLTLKEYNGSIGLPIPSTDACIKDDAGTVLAIGEIGELcikGPQVMKG-- 421
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217306889 472 fglfthYVDNPSKTASTLRGNFYI-TGDRGYMDKDGYFWFVARADDVILSSGYRIGPFEVENALNEHPSVAESAVVSSPD 550
Cdd:PRK08751 422 ------YWKRPEETAKVMDADGWLhTGDIARMDEQGFVYIVDRKKDMILVSGFNVYPNEIEDVIAMMPGVLEVAAVGVPD 495
|
490 500 510 520
....*....|....*....|....*....|....*....|....*.
gi 2217306889 551 PIRGEVVKAFVVlnpdykSHDQEQLIKEIQEHVKKTTAPYKYPRKV 596
Cdd:PRK08751 496 EKSGEIVKVVIV------KKDPALTAEDVKAHARANLTGYKQPRII 535
|
|
| PtmA |
cd17636 |
long-chain fatty acid CoA ligase (FadD); This family contains fatty acid CoA ligases, ... |
332-596 |
1.18e-36 |
|
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: 139.74 E-value: 1.18e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217306889 332 GACVFthhLPRFEPTSILQTLSKYPIT-VFCSAPTVYRMLVQNDITSYKFKSLKHCVSAGE---PITPDVTEkWRNKTGl 407
Cdd:cd17636 67 GTNVF---VRRVDAEEVLELIEAERCThAFLLPPTIDQIVELNADGLYDLSSLRSSPAAPEwndMATVDTSP-WGRKPG- 141
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217306889 408 diyeGYGQTETV-LICGNFKGMKIKpGSMGKPSPAFDVKIVDVNGNVLPPGQEGDIGIqvlpnRPFGLFTHYVDNPSKTA 486
Cdd:cd17636 142 ----GYGQTEVMgLATFAALGGGAI-GGAGRPSPLVQVRILDEDGREVPDGEVGEIVA-----RGPTVMAGYWNRPEVNA 211
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217306889 487 STLRGNFYITGDRGYMDKDGYFWFVARADDVILSSGYRIGPFEVENALNEHPSVAESAVVSSPDPIRGEVVKAFVVLNPD 566
Cdd:cd17636 212 RRTRGGWHHTNDLGRREPDGSLSFVGPKTRMIKSGAENIYPAEVERCLRQHPAVADAAVIGVPDPRWAQSVKAIVVLKPG 291
|
250 260 270
....*....|....*....|....*....|
gi 2217306889 567 yKSHDQEQLIkeiqEHVKKTTAPYKYPRKV 596
Cdd:cd17636 292 -ASVTEAELI----EHCRARIASYKKPKSV 316
|
|
| ttLC_FACS_AEE21_like |
cd12118 |
Fatty acyl-CoA synthetases similar to LC-FACS from Thermus thermophiles and Arabidopsis; This ... |
92-596 |
2.28e-36 |
|
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: 142.44 E-value: 2.28e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217306889 92 EMRWSFEELGSLSRKFANILSEAcSLQRGDRVILILPRVPEWWLANVACLRTGTVLIPGTTQLTQKDILYRLQSSKANCI 171
Cdd:cd12118 27 DRRYTWRQTYDRCRRLASALAAL-GISRGDTVAVLAPNTPAMYELHFGVPMAGAVLNALNTRLDAEEIAFILRHSEAKVL 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217306889 172 IT------NDVLApavdavaskcenlhsklivsensrEGWGNlkelmkvflchPGWSTVARSWltatstslvQAIlslls 245
Cdd:cd12118 106 FVdrefeyEDLLA------------------------EGDPD-----------FEWIPPADEW---------DPI----- 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217306889 246 swdyrhasdshtcvktkhneimAIFFTSGTSGYPKMTAHTHSSFGLGLSVNGRFWlDLTPSDV-MWNTSD---TGWAksa 321
Cdd:cd12118 137 ----------------------ALNYTSGTTGRPKGVVYHHRGAYLNALANILEW-EMKQHPVyLWTLPMfhcNGWC--- 190
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217306889 322 wssvfSPWIQGACVFTHH-LPRFEPTSILQTLSKYPITVFCSAPTVYRMLVqNDITSYKfKSLKHCVS---AGEPITPDV 397
Cdd:cd12118 191 -----FPWTVAAVGGTNVcLRKVDAKAIYDLIEKHKVTHFCGAPTVLNMLA-NAPPSDA-RPLPHRVHvmtAGAPPPAAV 263
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217306889 398 TEKWRNKtGLDIYEGYGQTET---VLICgnfkgmKIKPGSMGKPSP---------------AFDVKIVDVNGNVLPPGQE 459
Cdd:cd12118 264 LAKMEEL-GFDVTHVYGLTETygpATVC------AWKPEWDELPTEerarlkarqgvryvgLEEVDVLDPETMKPVPRDG 336
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217306889 460 GDIGIQVLpnRPFGLFTHYVDNPSKTASTLRGNFYITGDRGYMDKDGYFWFVARADDVILSSGYRIGPFEVENALNEHPS 539
Cdd:cd12118 337 KTIGEIVF--RGNIVMKGYLKNPEATAEAFRGGWFHSGDLAVIHPDGYIEIKDRSKDIIISGGENISSVEVEGVLYKHPA 414
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*..
gi 2217306889 540 VAESAVVSSPDPIRGEVVKAFVVLNPDYKSHDQeqlikEIQEHVKKTTAPYKYPRKV 596
Cdd:cd12118 415 VLEAAVVARPDEKWGEVPCAFVELKEGAKVTEE-----EIIAFCREHLAGFMVPKTV 466
|
|
| PRK07788 |
PRK07788 |
acyl-CoA synthetase; Validated |
261-596 |
6.29e-36 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236097 [Multi-domain] Cd Length: 549 Bit Score: 142.37 E-value: 6.29e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217306889 261 TKHNEImaIFFTSGTSGYPKMTAHTHSSfglGLSVNGRFwLDLTP---SDVMWNTS----DTGWAKSAWSSVFspwiqGA 333
Cdd:PRK07788 206 PKPGGI--VILTSGTTGTPKGAPRPEPS---PLAPLAGL-LSRVPfraGETTLLPApmfhATGWAHLTLAMAL-----GS 274
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217306889 334 CVFTHHlpRFEPTSILQTLSKYPITVFCSAPT-VYRML--VQNDITSYKFKSLKHCVSAGEPITPDVTEKWRNKTGLDIY 410
Cdd:PRK07788 275 TVVLRR--RFDPEATLEDIAKHKATALVVVPVmLSRILdlGPEVLAKYDTSSLKIIFVSGSALSPELATRALEAFGPVLY 352
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217306889 411 EGYGQTE----TVlicGNFKGMKIKPGSMGKPSPAFDVKIVDVNGNVLPPGQEGDIGIqvlpnRPFGLFTHYVDNPSKta 486
Cdd:PRK07788 353 NLYGSTEvafaTI---ATPEDLAEAPGTVGRPPKGVTVKILDENGNEVPRGVVGRIFV-----GNGFPFEGYTDGRDK-- 422
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217306889 487 STLRGnFYITGDRGYMDKDGYfWFVA-RADDVILSSGYRIGPFEVENALNEHPSVAESAVVSSPDPIRGEVVKAFVVLNP 565
Cdd:PRK07788 423 QIIDG-LLSSGDVGYFDEDGL-LFVDgRDDDMIVSGGENVFPAEVEDLLAGHPDVVEAAVIGVDDEEFGQRLRAFVVKAP 500
|
330 340 350
....*....|....*....|....*....|.
gi 2217306889 566 DyKSHDQEqlikEIQEHVKKTTAPYKYPRKV 596
Cdd:PRK07788 501 G-AALDED----AIKDYVRDNLARYKVPRDV 526
|
|
| ttLC_FACS_AlkK_like |
cd12119 |
Fatty acyl-CoA synthetases similar to LC-FACS from Thermus thermophiles; This family includes ... |
90-585 |
6.51e-36 |
|
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: 141.61 E-value: 6.51e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217306889 90 GEEMRWSFEELGSLSRKFANILSEAcSLQRGDRVILIL---PRVPEWWLAnVAClrTGTVLIPGTTQLTQKDILYRLQSS 166
Cdd:cd12119 21 GEVHRYTYAEVAERARRLANALRRL-GVKPGDRVATLAwntHRHLELYYA-VPG--MGAVLHTINPRLFPEQIAYIINHA 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217306889 167 KANCIITNDVLAPAVDAVASKcenlhsklivsensregwgnLKELMKVFLchpgwstvarswLTATSTSLVQAILSLLSS 246
Cdd:cd12119 97 EDRVVFVDRDFLPLLEAIAPR--------------------LPTVEHVVV------------MTDDAAMPEPAGVGVLAY 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217306889 247 WDYRHA-SDSHTCVKTKHNEIMAIFFTSGTSGYPKMTAHTHSSFGLG-LSVNGRFWLDLTPSDV------MWNTSdtgwa 318
Cdd:cd12119 145 EELLAAeSPEYDWPDFDENTAAAICYTSGTTGNPKGVVYSHRSLVLHaMAALLTDGLGLSESDVvlpvvpMFHVN----- 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217306889 319 ksAWSSVFSPWIQGAC-VFTHhlPRFEPTSILQTLSKYPITVFCSAPTVYRMLVQN-DITSYKFKSLKHCVSAGEPITPD 396
Cdd:cd12119 220 --AWGLPYAAAMVGAKlVLPG--PYLDPASLAELIEREGVTFAAGVPTVWQGLLDHlEANGRDLSSLRRVVIGGSAVPRS 295
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217306889 397 VTEKWRNKtGLDIYEGYGQTET--VLICGnfkgmKIKPG--------------SMGKPSPAFDVKIVDVNGNVLP--PGQ 458
Cdd:cd12119 296 LIEAFEER-GVRVIHAWGMTETspLGTVA-----RPPSEhsnlsedeqlalraKQGRPVPGVELRIVDDDGRELPwdGKA 369
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217306889 459 EGDIgiQVlpnR-PFgLFTHYVDNPSKTASTLRGNFYITGDRGYMDKDGYFWFVARADDVILSSGYRIGPFEVENALNEH 537
Cdd:cd12119 370 VGEL--QV---RgPW-VTKSYYKNDEESEALTEDGWLRTGDVATIDEDGYLTITDRSKDVIKSGGEWISSVELENAIMAH 443
|
490 500 510 520
....*....|....*....|....*....|....*....|....*...
gi 2217306889 538 PSVAESAVVSSPDPIRGEVVKAFVVLNPDyKSHDQEQLIKEIQEHVKK 585
Cdd:cd12119 444 PAVAEAAVIGVPHPKWGERPLAVVVLKEG-ATVTAEELLEFLADKVAK 490
|
|
| AAS_C |
cd05909 |
C-terminal domain of the acyl-acyl carrier protein synthetase (also called ... |
258-607 |
6.97e-36 |
|
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: 141.31 E-value: 6.97e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217306889 258 CVKTKHNEIMAIFFTSGTSGYPKMTAHTHSSFGLGL-SVNGRFwlDLTPSDVMWNTSDTGWAKSAWSSVFSPWIQGACVF 336
Cdd:cd05909 141 VAPVQPDDPAVILFTSGSEGLPKGVVLSHKNLLANVeQITAIF--DPNPEDVVFGALPFFHSFGLTGCLWLPLLSGIKVV 218
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217306889 337 THHLPrFEPTSILQTLSKYPITVFCSAPTVYRMLVQNdITSYKFKSLKHCVSAGEPITPDVTEKWRNKTGLDIYEGYGQT 416
Cdd:cd05909 219 FHPNP-LDYKKIPELIYDKKATILLGTPTFLRGYARA-AHPEDFSSLRLVVAGAEKLKDTLRQEFQEKFGIRILEGYGTT 296
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217306889 417 ETV-LICGNFKGMKIKPGSMGKPSPAFDVKIVDVNGNV-LPPGQEGDIGIQVlPNrpfgLFTHYVDNPSKTASTLRGNFY 494
Cdd:cd05909 297 ECSpVISVNTPQSPNKEGTVGRPLPGMEVKIVSVETHEeVPIGEGGLLLVRG-PN----VMLGYLNEPELTSFAFGDGWY 371
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217306889 495 ITGDRGYMDKDGYFWFVARaddviLSSGYRIG----PFE-VENALNEH-PSVAESAVVSSPDPIRGEVVKAFVVLnpdyk 568
Cdd:cd05909 372 DTGDIGKIDGEGFLTITGR-----LSRFAKIAgemvSLEaIEDILSEIlPEDNEVAVVSVPDGRKGEKIVLLTTT----- 441
|
330 340 350
....*....|....*....|....*....|....*....
gi 2217306889 569 sHDQEQLikEIQEHVKKTTAPykyprkvGILIITNICSV 607
Cdd:cd05909 442 -TDTDPS--SLNDILKNAGIS-------NLAKPSYIHQV 470
|
|
| FadD3 |
cd17638 |
acyl-CoA synthetase FadD3 and similar proteins; This family contains long chain fatty acid CoA ... |
265-599 |
2.82e-35 |
|
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: 136.09 E-value: 2.82e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217306889 265 EIMAIFFTSGTSGYPK--MTAHTHSsfgLGLSVNgrfWldltpSDVMWNTSDTGWA-----------KSAWSSVFspwIQ 331
Cdd:cd17638 1 DVSDIMFTSGTTGRSKgvMCAHRQT---LRAAAA---W-----ADCADLTEDDRYLiinpffhtfgyKAGIVACL---LT 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217306889 332 GACVFTHHLprFEPTSILQTLSKYPITVFCSAPTVYR-MLVQNDITSYKFKSLKHCVSAGEPITPDVTEKWRNKTGLD-I 409
Cdd:cd17638 67 GATVVPVAV--FDVDAILEAIERERITVLPGPPTLFQsLLDHPGRKKFDLSSLRAAVTGAATVPVELVRRMRSELGFEtV 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217306889 410 YEGYGQTE--TVLICGNFKGMKIKPGSMGKPSPAFDVKIVDvNGNVLPPGqegdigiqvlPNRPFGlfthYVDNPSKTAS 487
Cdd:cd17638 145 LTAYGLTEagVATMCRPGDDAETVATTCGRACPGFEVRIAD-DGEVLVRG----------YNVMQG----YLDDPEATAE 209
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217306889 488 TLRGNFYI-TGDRGYMDKDGYFWFVARADDVILSSGYRIGPFEVENALNEHPSVAESAVVSSPDPIRGEVVKAFVVLNPD 566
Cdd:cd17638 210 AIDADGWLhTGDVGELDERGYLRITDRLKDMYIVGGFNVYPAEVEGALAEHPGVAQVAVIGVPDERMGEVGKAFVVARPG 289
|
330 340 350
....*....|....*....|....*....|...
gi 2217306889 567 yKSHDQEQLIKEIQEHVkkttAPYKYPRKVGIL 599
Cdd:cd17638 290 -VTLTEEDVIAWCRERL----ANYKVPRFVRFL 317
|
|
| PRK13391 |
PRK13391 |
acyl-CoA synthetase; Provisional |
78-596 |
1.01e-34 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 184022 [Multi-domain] Cd Length: 511 Bit Score: 138.29 E-value: 1.01e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217306889 78 PSNPAFWwINRNGEEMrwSFEELGSLSRKFANILSEAcSLQRGDRVILIL---PRVPEwwlANVACLRTGTVLIPGTTQL 154
Cdd:PRK13391 11 PDKPAVI-MASTGEVV--TYRELDERSNRLAHLFRSL-GLKRGDHVAIFMennLRYLE---VCWAAERSGLYYTCVNSHL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217306889 155 TQKDILYRLQSSKANCIITNDVLAPAVDAVASKCENLHSKLIV-SENSREGWGNLKElmkvflchpgwsTVARswLTATs 233
Cdd:PRK13391 84 TPAEAAYIVDDSGARALITSAAKLDVARALLKQCPGVRHRLVLdGDGELEGFVGYAE------------AVAG--LPAT- 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217306889 234 tslvqailsllsswdyRHASDShtcvktkhnEIMAIFFTSGTSGYPK----------------MTAHTHSSFGLGlsvNG 297
Cdd:PRK13391 149 ----------------PIADES---------LGTDMLYSSGTTGRPKgikrplpeqppdtplpLTAFLQRLWGFR---SD 200
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217306889 298 RFWLDLTPsdvMWNTsdtgwAKSAWSSVfspwIQ--GACVFThhLPRFEPTSILQTLSKYPITVFCSAPTVY-RML-VQN 373
Cdd:PRK13391 201 MVYLSPAP---LYHS-----APQRAVML----VIrlGGTVIV--MEHFDAEQYLALIEEYGVTHTQLVPTMFsRMLkLPE 266
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217306889 374 DI-TSYKFKSLKHCVSAGEPITPDVTEKWRNKTGLDIYEGYGQTETVLICG-NFKGMKIKPGSMGKPSPAfDVKIVDVNG 451
Cdd:PRK13391 267 EVrDKYDLSSLEVAIHAAAPCPPQVKEQMIDWWGPIIHEYYAATEGLGFTAcDSEEWLAHPGTVGRAMFG-DLHILDDDG 345
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217306889 452 NVLPPGQEGDIGIQvlPNRPFglftHYVDNPSKTASTL--RGNFYITGDRGYMDKDGYFWFVARADDVILSSGYRIGPFE 529
Cdd:PRK13391 346 AELPPGEPGTIWFE--GGRPF----EYLNDPAKTAEARhpDGTWSTVGDIGYVDEDGYLYLTDRAAFMIISGGVNIYPQE 419
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2217306889 530 VENALNEHPSVAESAVVSSPDPIRGEVVKAFVVLNP--DYKSHDQEQLIKEIQEHVkkttAPYKYPRKV 596
Cdd:PRK13391 420 AENLLITHPKVADAAVFGVPNEDLGEEVKAVVQPVDgvDPGPALAAELIAFCRQRL----SRQKCPRSI 484
|
|
| FAA1 |
COG1022 |
Long-chain acyl-CoA synthetase (AMP-forming) [Lipid transport and metabolism]; |
74-585 |
1.26e-34 |
|
Long-chain acyl-CoA synthetase (AMP-forming) [Lipid transport and metabolism];
Pssm-ID: 440645 [Multi-domain] Cd Length: 603 Bit Score: 139.08 E-value: 1.26e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217306889 74 AGKKPSNPAFWWiNRNGEEMRWSFEELGSLSRKFANILsEACSLQRGDRVILILPRVPEWWLANVACLRTGTVLIPGTTQ 153
Cdd:COG1022 21 AARFPDRVALRE-KEDGIWQSLTWAEFAERVRALAAGL-LALGVKPGDRVAILSDNRPEWVIADLAILAAGAVTVPIYPT 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217306889 154 LTQKDILYRLQSSKANCIIT-NDVLAPAVDAVASKCENLhsKLIVSENSREGWGNLKELmkvflchpGWSTVARSWLTAT 232
Cdd:COG1022 99 SSAEEVAYILNDSGAKVLFVeDQEQLDKLLEVRDELPSL--RHIVVLDPRGLRDDPRLL--------SLDELLALGREVA 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217306889 233 STSLVQAILSllsswdyrhasdshtcvKTKHNEIMAIFFTSGTSGYPKMTAHTHSSFgLGLSVNGRFWLDLTPSDV---- 308
Cdd:COG1022 169 DPAELEARRA-----------------AVKPDDLATIIYTSGTTGRPKGVMLTHRNL-LSNARALLERLPLGPGDRtlsf 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217306889 309 --MWNTSDTGWaksawsSVFSpWIQGACVftHHLPRfePTSILQTLSKYPITVFCSAPTVYRMlVQNDITS--------- 377
Cdd:COG1022 231 lpLAHVFERTV------SYYA-LAAGATV--AFAES--PDTLAEDLREVKPTFMLAVPRVWEK-VYAGIQAkaeeagglk 298
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217306889 378 ---------------------------YKFK------------------SLKHCVSAGEPITPDVTEKWRNkTGLDIYEG 412
Cdd:COG1022 299 rklfrwalavgrryararlagkspsllLRLKhaladklvfsklrealggRLRFAVSGGAALGPELARFFRA-LGIPVLEG 377
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217306889 413 YGQTET-VLICGNFKGmKIKPGSMGKPSPAFDVKIvdvngnvlppGQEGDI---GIQVlpnrpfglFTHYVDNPSKTAST 488
Cdd:COG1022 378 YGLTETsPVITVNRPG-DNRIGTVGPPLPGVEVKI----------AEDGEIlvrGPNV--------MKGYYKNPEATAEA 438
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217306889 489 LR--GNFYiTGDRGYMDKDGYFWFVARADDVI-LSSGYRIGPFEVENALNEHPSVAESAVVsspdpirGE----VVkAFV 561
Cdd:COG1022 439 FDadGWLH-TGDIGELDEDGFLRITGRKKDLIvTSGGKNVAPQPIENALKASPLIEQAVVV-------GDgrpfLA-ALI 509
|
570 580 590 600
....*....|....*....|....*....|....*....|
gi 2217306889 562 VLNPD------------YKSHDQ----EQLIKEIQEHVKK 585
Cdd:COG1022 510 VPDFEalgewaeenglpYTSYAElaqdPEVRALIQEEVDR 549
|
|
| PRK13295 |
PRK13295 |
cyclohexanecarboxylate-CoA ligase; Reviewed |
67-599 |
2.59e-34 |
|
cyclohexanecarboxylate-CoA ligase; Reviewed
Pssm-ID: 171961 [Multi-domain] Cd Length: 547 Bit Score: 137.49 E-value: 2.59e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217306889 67 QWTDK-------EKAGKKPSNPAFWWINRNGEEM-RWSFEELGSLSRKFANILSEaCSLQRGDRVILilpRVPEWWLANV 138
Cdd:PRK13295 20 HWHDRtinddldACVASCPDKTAVTAVRLGTGAPrRFTYRELAALVDRVAVGLAR-LGVGRGDVVSC---QLPNWWEFTV 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217306889 139 ---ACLRTGTVLIPGTTQLTQKDILYRLQSSKANCIItndvlAPAV----DAVAskcenlhskliVSENSREGWGNLKEL 211
Cdd:PRK13295 96 lylACSRIGAVLNPLMPIFRERELSFMLKHAESKVLV-----VPKTfrgfDHAA-----------MARRLRPELPALRHV 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217306889 212 MKV----------FLCHPGWSTVARSwltatstslvQAILSllsswdyRHASDShtcvktkhNEIMAIFFTSGTSGYPKM 281
Cdd:PRK13295 160 VVVggdgadsfeaLLITPAWEQEPDA----------PAILA-------RLRPGP--------DDVTQLIYTSGTTGEPKG 214
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217306889 282 TAHTHSS-FGLGLSVNGRfwLDLTPSDVMWNTS----DTGWAKSAwssvFSPWIQGACVFTHHLprFEPTSILQTLSKYP 356
Cdd:PRK13295 215 VMHTANTlMANIVPYAER--LGLGADDVILMASpmahQTGFMYGL----MMPVMLGATAVLQDI--WDPARAAELIRTEG 286
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217306889 357 ITvFCSAPTVYRM-LVQN-DITSYKFKSLKHCVSAGEPITPDVTEKWRNKTGLDIYEGYGQTETVLICGnfkgmkIKPG- 433
Cdd:PRK13295 287 VT-FTMASTPFLTdLTRAvKESGRPVSSLRTFLCAGAPIPGALVERARAALGAKIVSAWGMTENGAVTL------TKLDd 359
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217306889 434 -------SMGKPSPAFDVKIVDVNGNVLPPGQEGDIgiQVlpnRPFGLFTHYVDNPSKTASTLRGnFYITGDRGYMDKDG 506
Cdd:PRK13295 360 pderastTDGCPLPGVEVRVVDADGAPLPAGQIGRL--QV---RGCSNFGGYLKRPQLNGTDADG-WFDTGDLARIDADG 433
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217306889 507 YFWFVARADDVILSSGYRIGPFEVENALNEHPSVAESAVVSSPDPIRGEVVKAFVVLNPDyKSHDQEQLIKEIQEHvkKT 586
Cdd:PRK13295 434 YIRISGRSKDVIIRGGENIPVVEIEALLYRHPAIAQVAIVAYPDERLGERACAFVVPRPG-QSLDFEEMVEFLKAQ--KV 510
|
570
....*....|...
gi 2217306889 587 TAPYkYPRKVGIL 599
Cdd:PRK13295 511 AKQY-IPERLVVR 522
|
|
| PRK12492 |
PRK12492 |
long-chain-fatty-acid--CoA ligase; Provisional |
96-596 |
7.44e-34 |
|
long-chain-fatty-acid--CoA ligase; Provisional
Pssm-ID: 171539 [Multi-domain] Cd Length: 562 Bit Score: 136.49 E-value: 7.44e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217306889 96 SFEELGSLSRKFANILSEACSLQRGDRVILILPRVPEWWLANVACLRTGTVLIPGTTQLTQKDILYRLQSSKANCIITND 175
Cdd:PRK12492 51 SYAELERHSAAFAAYLQQHTDLVPGDRIAVQMPNVLQYPIAVFGALRAGLIVVNTNPLYTAREMRHQFKDSGARALVYLN 130
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217306889 176 VLAPAVDAVASKCENLHskLIVSEnsregwgnLKELMkvflchpgwsTVARSWLTATSTSLVQAIL---SLLSSWDYRHA 252
Cdd:PRK12492 131 MFGKLVQEVLPDTGIEY--LIEAK--------MGDLL----------PAAKGWLVNTVVDKVKKMVpayHLPQAVPFKQA 190
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217306889 253 -----SDSHTCVKTKHNEIMAIFFTSGTSGYPKMTAHTHSSfglgLSVN--------GRFWLDLTPsdVMWNTSDTGWAK 319
Cdd:PRK12492 191 lrqgrGLSLKPVPVGLDDIAVLQYTGGTTGLAKGAMLTHGN----LVANmlqvraclSQLGPDGQP--LMKEGQEVMIAP 264
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217306889 320 SAWSSVFSPWIQGACVF---THHLPRFEPTSI---LQTLSKYPITVFCSAPTVYRMLVQN-DITSYKFKSLKHCVSAGEP 392
Cdd:PRK12492 265 LPLYHIYAFTANCMCMMvsgNHNVLITNPRDIpgfIKELGKWRFSALLGLNTLFVALMDHpGFKDLDFSALKLTNSGGTA 344
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217306889 393 ITPDVTEKWRNKTGLDIYEGYGQTETV-LICGNFKGMKIKPGSMGKPSPAFDVKIVDVNGNVLPPGQEGDI---GIQVLP 468
Cdd:PRK12492 345 LVKATAERWEQLTGCTIVEGYGLTETSpVASTNPYGELARLGTVGIPVPGTALKVIDDDGNELPLGERGELcikGPQVMK 424
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217306889 469 NrpfglfthYVDNPSKTASTLRGN-FYITGDRGYMDKDGYFWFVARADDVILSSGYRIGPFEVENALNEHPSVAESAVVS 547
Cdd:PRK12492 425 G--------YWQQPEATAEALDAEgWFKTGDIAVIDPDGFVRIVDRKKDLIIVSGFNVYPNEIEDVVMAHPKVANCAAIG 496
|
490 500 510 520
....*....|....*....|....*....|....*....|....*....
gi 2217306889 548 SPDPIRGEVVKAFVVlnpdykSHDQEQLIKEIQEHVKKTTAPYKYPRKV 596
Cdd:PRK12492 497 VPDERSGEAVKLFVV------ARDPGLSVEELKAYCKENFTGYKVPKHI 539
|
|
| PRK06145 |
PRK06145 |
acyl-CoA synthetase; Validated |
264-596 |
1.99e-33 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 102207 [Multi-domain] Cd Length: 497 Bit Score: 134.24 E-value: 1.99e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217306889 264 NEIMAIFFTSGTSGYPKMTAHTHSSF---------GLGLSVNGRFW----------LDLTPSDVMWntsdtgwaksawss 324
Cdd:PRK06145 149 TDLVRLMYTSGTTDRPKGVMHSYGNLhwksidhviALGLTASERLLvvgplyhvgaFDLPGIAVLW-------------- 214
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217306889 325 vfspwiQGACVFTHHlpRFEPTSILQTLSKYPITVFCSAPTVY-RMLVQNDITSYKFKSLKHCVSAGEPiTP-----DVT 398
Cdd:PRK06145 215 ------VGGTLRIHR--EFDPEAVLAAIERHRLTCAWMAPVMLsRVLTVPDRDRFDLDSLAWCIGGGEK-TPesrirDFT 285
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217306889 399 EKWRNKTGLDiyeGYGQTETvliCGNFKGMKI-----KPGSMGKPSPAFDVKIVDVNGNVLPPGQEGDIGIQVlPNRPFG 473
Cdd:PRK06145 286 RVFTRARYID---AYGLTET---CSGDTLMEAgreieKIGSTGRALAHVEIRIADGAGRWLPPNMKGEICMRG-PKVTKG 358
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217306889 474 lfthYVDNPSKTASTLRGNFYITGDRGYMDKDGYFWFVARADDVILSSGYRIGPFEVENALNEHPSVAESAVVSSPDPIR 553
Cdd:PRK06145 359 ----YWKDPEKTAEAFYGDWFRSGDVGYLDEEGFLYLTDRKKDMIISGGENIASSEVERVIYELPEVAEAAVIGVHDDRW 434
|
330 340 350 360
....*....|....*....|....*....|....*....|...
gi 2217306889 554 GEVVKAFVVLNPdykshDQEQLIKEIQEHVKKTTAPYKYPRKV 596
Cdd:PRK06145 435 GERITAVVVLNP-----GATLTLEALDRHCRQRLASFKVPRQL 472
|
|
| Firefly_Luc |
cd17642 |
insect luciferase, similar to plant 4-coumarate: CoA ligases; This family contains insect ... |
92-594 |
6.92e-33 |
|
insect luciferase, similar to plant 4-coumarate: CoA ligases; This family contains insect firefly luciferases that share significant sequence similarity to plant 4-coumarate:coenzyme A ligases, despite their functional diversity. Luciferase catalyzes the production of light in the presence of MgATP, molecular oxygen, and luciferin. In the first step, luciferin is activated by acylation of its carboxylate group with ATP, resulting in an enzyme-bound luciferyl adenylate. In the second step, luciferyl adenylate reacts with molecular oxygen, producing an enzyme-bound excited state product (Luc=O*) and releasing AMP. This excited-state product then decays to the ground state (Luc=O), emitting a quantum of visible light.
Pssm-ID: 341297 [Multi-domain] Cd Length: 532 Bit Score: 133.04 E-value: 6.92e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217306889 92 EMRWSFEELGSLSRKFANILSEAcSLQRGDRVILILPRVPEWWLANVACLRTGTVLIPGTTQLTQKDILYRLQSSKANCI 171
Cdd:cd17642 42 GVNYSYAEYLEMSVRLAEALKKY-GLKQNDRIAVCSENSLQFFLPVIAGLFIGVGVAPTNDIYNERELDHSLNISKPTIV 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217306889 172 ITNDVLAPAVDAVASKceNLHSKLIVSENSREGWGNLKELMKvFLCHPGWSTVARSWLTATSTSlvqailsllsswdyrh 251
Cdd:cd17642 121 FCSKKGLQKVLNVQKK--LKIIKTIIILDSKEDYKGYQCLYT-FITQNLPPGFNEYDFKPPSFD---------------- 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217306889 252 asdshtcvktKHNEIMAIFFTSGTSGYPKMTAHTHssfglgLSVNGRFWLDLTPSDVMWNTSDTgwaksAWSSVFsPWIQ 331
Cdd:cd17642 182 ----------RDEQVALIMNSSGSTGLPKGVQLTH------KNIVARFSHARDPIFGNQIIPDT-----AILTVI-PFHH 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217306889 332 GACVFTH-----------HLPRFEPTSILQTLSKYPITVFCSAPTVYRMLVQNDITS-YKFKSLKHCVSAGEPITPDVTE 399
Cdd:cd17642 240 GFGMFTTlgylicgfrvvLMYKFEEELFLRSLQDYKVQSALLVPTLFAFFAKSTLVDkYDLSNLHEIASGGAPLSKEVGE 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217306889 400 KWRNKTGLD-IYEGYGQTET---VLICGNfkgMKIKPGSMGKPSPAFDVKIVDVN-GNVLPPGQEGDIGIqvlpnRPFGL 474
Cdd:cd17642 320 AVAKRFKLPgIRQGYGLTETtsaILITPE---GDDKPGAVGKVVPFFYAKVVDLDtGKTLGPNERGELCV-----KGPMI 391
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217306889 475 FTHYVDNPSKTASTLRGNFYI-TGDRGYMDKDGYFWFVARADDVILSSGYRIGPFEVENALNEHPSVAESAVVSSPDPIR 553
Cdd:cd17642 392 MKGYVNNPEATKALIDKDGWLhSGDIAYYDEDGHFFIVDRLKSLIKYKGYQVPPAELESILLQHPKIFDAGVAGIPDEDA 471
|
490 500 510 520
....*....|....*....|....*....|....*....|.
gi 2217306889 554 GEVVKAFVVLnpdykSHDQEQLIKEIQEHVKKTTAPYKYPR 594
Cdd:cd17642 472 GELPAAVVVL-----EAGKTMTEKEVMDYVASQVSTAKRLR 507
|
|
| PLN02246 |
PLN02246 |
4-coumarate--CoA ligase |
72-596 |
1.06e-32 |
|
4-coumarate--CoA ligase
Pssm-ID: 215137 [Multi-domain] Cd Length: 537 Bit Score: 132.41 E-value: 1.06e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217306889 72 EKAGKKPSNPAFwwIN-RNGEEMrwSFEELGSLSRKFANILSeACSLQRGDRVILILPRVPEWWLANVACLRTGTVLIPG 150
Cdd:PLN02246 31 ERLSEFSDRPCL--IDgATGRVY--TYADVELLSRRVAAGLH-KLGIRQGDVVMLLLPNCPEFVLAFLGASRRGAVTTTA 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217306889 151 TTQLTQKDILYRLQSSKANCIITndvLAPAVDAVASKCENLHSKLIVSENSREGWGNLKELMkvflchpgwstvarswlt 230
Cdd:PLN02246 106 NPFYTPAEIAKQAKASGAKLIIT---QSCYVDKLKGLAEDDGVTVVTIDDPPEGCLHFSELT------------------ 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217306889 231 atstslvqailsllsswdyrhASDSHTC--VKTKHNEIMAIFFTSGTSGYPKMTAHTHSsfGLGLSV---------Ngrf 299
Cdd:PLN02246 165 ---------------------QADENELpeVEISPDDVVALPYSSGTTGLPKGVMLTHK--GLVTSVaqqvdgenpN--- 218
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217306889 300 wLDLTPSDVMWNTSDTGWAKSAWSSVFSPWIQGACVFThhLPRFEPTSILQTLSKYPITVFCSAPTVYRMLVQNDIT-SY 378
Cdd:PLN02246 219 -LYFHSDDVILCVLPMFHIYSLNSVLLCGLRVGAAILI--MPKFEIGALLELIQRHKVTIAPFVPPIVLAIAKSPVVeKY 295
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217306889 379 KFKSLKHCVSAGEPITPDVTEKWRNKTGLDIY-EGYGQTE--TVL-ICGNF--KGMKIKPGSMGKPSPAFDVKIVDVN-G 451
Cdd:PLN02246 296 DLSSIRMVLSGAAPLGKELEDAFRAKLPNAVLgQGYGMTEagPVLaMCLAFakEPFPVKSGSCGTVVRNAELKIVDPEtG 375
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217306889 452 NVLPPGQEGDIGIqvlpnRPFGLFTHYVDNPSKTASTL-RGNFYITGDRGYMDKDGYFWFVARADDVILSSGYRIGPFEV 530
Cdd:PLN02246 376 ASLPRNQPGEICI-----RGPQIMKGYLNDPEATANTIdKDGWLHTGDIGYIDDDDELFIVDRLKELIKYKGFQVAPAEL 450
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2217306889 531 ENALNEHPSVAESAVVSSPDPIRGEVVKAFVVLNPDYK-SHDqeqlikEIQEHVKKTTAPYKYPRKV 596
Cdd:PLN02246 451 EALLISHPSIADAAVVPMKDEVAGEVPVAFVVRSNGSEiTED------EIKQFVAKQVVFYKRIHKV 511
|
|
| FADD10 |
cd17635 |
adenylate forming domain, fatty acid CoA ligase (FadD10); This family contains long chain ... |
265-604 |
5.79e-32 |
|
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: 126.61 E-value: 5.79e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217306889 265 EIMAIFFTSGTSGYPKMTAHTHSSFGLGLSVNGRFWLDLTPSDVMWNTSDTGWAKSAWSSVFSPWIQGACVFTHHlpRFE 344
Cdd:cd17635 2 DPLAVIFTSGTTGEPKAVLLANKTFFAVPDILQKEGLNWVVGDVTYLPLPATHIGGLWWILTCLIHGGLCVTGGE--NTT 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217306889 345 PTSILQTLSKYPITVFCSAPTVYRMLVQNDITSYKFKSLKHCVSAG--EPITPDVTEKWRNKTgLDIYEGYGQTET-VLI 421
Cdd:cd17635 80 YKSLFKILTTNAVTTTCLVPTLLSKLVSELKSANATVPSLRLIGYGgsRAIAADVRFIEATGL-TNTAQVYGLSETgTAL 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217306889 422 CGNFKGMKIKPGSMGKPSPAFDVKIVDVNGNVLPPGQEGDIGIQVlPNRPFGlfthYVDNPSKTASTLRGNFYITGDRGY 501
Cdd:cd17635 159 CLPTDDDSIEINAVGRPYPGVDVYLAATDGIAGPSASFGTIWIKS-PANMLG----YWNNPERTAEVLIDGWVNTGDLGE 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217306889 502 MDKDGYFWFVARADDVILSSGYRIGPFEVENALNEHPSVAESAVVSSPDPIRGEVVKAFVVLNpdykSHDQEQLIKEIQE 581
Cdd:cd17635 234 RREDGFLFITGRSSESINCGGVKIAPDEVERIAEGVSGVQECACYEISDEEFGELVGLAVVAS----AELDENAIRALKH 309
|
330 340
....*....|....*....|...
gi 2217306889 582 HVKKTTAPYKYPRKvgILIITNI 604
Cdd:cd17635 310 TIRRELEPYARPST--IVIVTDI 330
|
|
| A_NRPS_AB3403-like |
cd17646 |
Peptide Synthetase; The adenylation (A) domain of NRPS recognizes a specific amino acid or ... |
72-593 |
3.51e-31 |
|
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: 127.39 E-value: 3.51e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217306889 72 EKAGKKPSNPAFWWinrngEEMRWSFEELGSLSRKFANILSEAcSLQRGDRVILILPRVPEWWLANVACLRTGTVLIPGT 151
Cdd:cd17646 6 EQAARTPDAPAVVD-----EGRTLTYRELDERANRLAHLLRAR-GVGPEDRVAVLLPRSADLVVALLAVLKAGAAYLPLD 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217306889 152 TQLTQKDILYRLQSSKANCIITNDVLA---PAVDAVASKCEnlhsklivsensregwgnlkelmkvflchpgwstvarsW 228
Cdd:cd17646 80 PGYPADRLAYMLADAGPAVVLTTADLAarlPAGGDVALLGD--------------------------------------E 121
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217306889 229 LTATSTSLVQAILSLLSSWDYrhasdshtcvktkhneimaIFFTSGTSGYPKMTAHTHSSFglglsVNGRFWL----DLT 304
Cdd:cd17646 122 ALAAPPATPPLVPPRPDNLAY-------------------VIYTSGSTGRPKGVMVTHAGI-----VNRLLWMqdeyPLG 177
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217306889 305 PSDVMWNTSDTGWAKSAWSsVFSPWIQGAC-VFTHHLPRFEPTSILQTLSKYPITVFCSAPTVYRMLVQnDITSYKFKSL 383
Cdd:cd17646 178 PGDRVLQKTPLSFDVSVWE-LFWPLVAGARlVVARPGGHRDPAYLAALIREHGVTTCHFVPSMLRVFLA-EPAAGSCASL 255
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217306889 384 KHCVSAGEPITPDVTEKWRNKTGLDIYEGYGQTET---VLICGNFKGMKIKPGSMGKPSPAFDVKIVDVNGNVLPPGQEG 460
Cdd:cd17646 256 RRVFCSGEALPPELAARFLALPGAELHNLYGPTEAaidVTHWPVRGPAETPSVPIGRPVPNTRLYVLDDALRPVPVGVPG 335
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217306889 461 DI---GIQV---LPNRPfGLfT--HYVDNPSKTASTLrgnfYITGDRGYMDKDGYFWFVARADDVILSSGYRIGPFEVEN 532
Cdd:cd17646 336 ELylgGVQLargYLGRP-AL-TaeRFVPDPFGPGSRM----YRTGDLARWRPDGALEFLGRSDDQVKIRGFRVEPGEIEA 409
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2217306889 533 ALNEHPSVAESAVVSSPDPIRGEVVKAFVVLNPDYKSHDQEQLikeiQEHVKKTTAPYKYP 593
Cdd:cd17646 410 ALAAHPAVTHAVVVARAAPAGAARLVGYVVPAAGAAGPDTAAL----RAHLAERLPEYMVP 466
|
|
| CBAL |
cd05923 |
4-Chlorobenzoate-CoA ligase (CBAL); CBAL catalyzes the conversion of 4-chlorobenzoate (4-CB) ... |
337-572 |
6.36e-31 |
|
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: 126.85 E-value: 6.36e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217306889 337 THHLPR-FEPTSILQTLSKYPITVFCSAPTVYRMLVQN-DITSYKFKSLKHCVSAGEPITPDVTEKWRNKTGLDIYEGYG 414
Cdd:cd05923 221 TYVVVEeFDPADALKLIEQERVTSLFATPTHLDALAAAaEFAGLKLSSLRHVTFAGATMPDAVLERVNQHLPGEKVNIYG 300
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217306889 415 QTETVlicgNFKGMK-IKPGSMGKPSPAFDVKIVDVNGNV---LPPGQEGDIGIQVLPNRPFglfTHYVDNPSKTASTLR 490
Cdd:cd05923 301 TTEAM----NSLYMRdARTGTEMRPGFFSEVRIVRIGGSPdeaLANGEEGELIVAAAADAAF---TGYLNQPEATAKKLQ 373
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217306889 491 GNFYITGDRGYMDKDGYFWFVARADDVILSSGYRIGPFEVENALNEHPSVAESAVVSSPDPIRGEVVKAFVVLNPDYKSH 570
Cdd:cd05923 374 DGWYRTGDVGYVDPSGDVRILGRVDDMIISGGENIHPSEIERVLSRHPGVTEVVVIGVADERWGQSVTACVVPREGTLSA 453
|
..
gi 2217306889 571 DQ 572
Cdd:cd05923 454 DE 455
|
|
| PLN02330 |
PLN02330 |
4-coumarate--CoA ligase-like 1 |
95-596 |
1.04e-30 |
|
4-coumarate--CoA ligase-like 1
Pssm-ID: 215189 [Multi-domain] Cd Length: 546 Bit Score: 126.63 E-value: 1.04e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217306889 95 WSFEELGSLSRKFANILSeACSLQRGDRVILILPRVPEWWLANVACLRTGTVLIPGTTQLTQKDILYRLQSSKANCIITN 174
Cdd:PLN02330 56 VTYGEVVRDTRRFAKALR-SLGLRKGQVVVVVLPNVAEYGIVALGIMAAGGVFSGANPTALESEIKKQAEAAGAKLIVTN 134
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217306889 175 DvlapavdAVASKCENLHSKLIV-SENSREGWGNLKELmkvflchpgwstvarswltatstslvqailslLSSWDyrHAS 253
Cdd:PLN02330 135 D-------TNYGKVKGLGLPVIVlGEEKIEGAVNWKEL--------------------------------LEAAD--RAG 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217306889 254 DSHTCVKTKHNEIMAIFFTSGTSGYPKMTAHTH---------SSFGLGLSVNGRF-WLDLTPSDVMWNtsdtgwaksaws 323
Cdd:PLN02330 174 DTSDNEEILQTDLCALPFSSGTTGISKGVMLTHrnlvanlcsSLFSVGPEMIGQVvTLGLIPFFHIYG------------ 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217306889 324 svfspwIQGACVFTHH-------LPRFEPTSILQTLSKYPITVFCSAPTVYRMLVQN------DITSYKFKSLkhcVSAG 390
Cdd:PLN02330 242 ------ITGICCATLRnkgkvvvMSRFELRTFLNALITQEVSFAPIVPPIILNLVKNpiveefDLSKLKLQAI---MTAA 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217306889 391 EPITPDVTEKWRNK-TGLDIYEGYGQTETVLICGNF----KGMKI-KPGSMGKPSPAFDVKIVDV-NGNVLPPGQEGDIG 463
Cdd:PLN02330 313 APLAPELLTAFEAKfPGVQVQEAYGLTEHSCITLTHgdpeKGHGIaKKNSVGFILPNLEVKFIDPdTGRSLPKNTPGELC 392
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217306889 464 IqvlpnRPFGLFTHYVDNPSKTASTLRGNFYI-TGDRGYMDKDGYFWFVARADDVILSSGYRIGPFEVENALNEHPSVAE 542
Cdd:PLN02330 393 V-----RSQCVMQGYYNNKEETDRTIDEDGWLhTGDIGYIDDDGDIFIVDRIKELIKYKGFQVAPAELEAILLTHPSVED 467
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....
gi 2217306889 543 SAVVSSPDPIRGEVVKAFVVLNPDYKSHDQeqlikEIQEHVKKTTAPYKYPRKV 596
Cdd:PLN02330 468 AAVVPLPDEEAGEIPAACVVINPKAKESEE-----DILNFVAANVAHYKKVRVV 516
|
|
| VL_LC_FACS_like |
cd05907 |
Long-chain fatty acid CoA synthetases and Bubblegum-like very long-chain fatty acid CoA ... |
95-585 |
1.42e-30 |
|
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: 125.02 E-value: 1.42e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217306889 95 WSFEELGSLSRKFANILsEACSLQRGDRVILILPRVPEWWLANVACLRTGTVLIPGTTQLTQKDILYRLQSSKAnciitn 174
Cdd:cd05907 6 ITWAEFAEEVRALAKGL-IALGVEPGDRVAILSRNRPEWTIADLAILAIGAVPVPIYPTSSAEQIAYILNDSEA------ 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217306889 175 dvlapavdavaskcenlhsKLIVSENSREgwgnlkelmkvflchpgwstvarswlTATstslvqailsllsswdyrhasd 254
Cdd:cd05907 79 -------------------KALFVEDPDD--------------------------LAT---------------------- 91
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217306889 255 shtcvktkhneimaIFFTSGTSGYPKMTAHTHSSFglglsvngrfwldltpsdvMWN--TSDTGWAKSAWSSVFS----- 327
Cdd:cd05907 92 --------------IIYTSGTTGRPKGVMLSHRNI-------------------LSNalALAERLPATEGDRHLSflpla 138
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217306889 328 -----------PWIQGACVFthHLPRFEptSILQTLSKYPITVFCSAPTVYRML----VQNDITSYK--------FKSLK 384
Cdd:cd05907 139 hvferraglyvPLLAGARIY--FASSAE--TLLDDLSEVRPTVFLAVPRVWEKVyaaiKVKAVPGLKrklfdlavGGRLR 214
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217306889 385 HCVSAGEPITPDVTEKWRnKTGLDIYEGYGQTETV-LICGNFKGmKIKPGSMGKPSPAFDVKIVDVNgnvlppgqEgdig 463
Cdd:cd05907 215 FAASGGAPLPAELLHFFR-ALGIPVYEGYGLTETSaVVTLNPPG-DNRIGTVGKPLPGVEVRIADDG--------E---- 280
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217306889 464 IQVlpnRPFGLFTHYVDNPSKTA-STLRGNFYITGDRGYMDKDGYFWFVARADDVI-LSSGYRIGPFEVENALNEHPSVA 541
Cdd:cd05907 281 ILV---RGPNVMLGYYKNPEATAeALDADGWLHTGDLGEIDEDGFLHITGRKKDLIiTSGGKNISPEPIENALKASPLIS 357
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217306889 542 ESAVVSSPDPirgeVVKAFVVLNPDY-----KSHD-----------QEQLIKEIQEHVKK 585
Cdd:cd05907 358 QAVVIGDGRP----FLVALIVPDPEAleawaEEHGiaytdvaelaaNPAVRAEIEAAVEA 413
|
|
| A_NRPS_VisG_like |
cd17651 |
similar to adenylation domain of virginiamycin S synthetase; This family of the adenylation (A) ... |
90-566 |
2.02e-30 |
|
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: 125.15 E-value: 2.02e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217306889 90 GEEMRWSFEELGSLSRKFANILsEACSLQRGDRVILILPRVPEWWLANVACLRTGTVLIPGTTQLTQKDILYRLQSSKAN 169
Cdd:cd17651 16 AEGRRLTYAELDRRANRLAHRL-RARGVGPGDLVALCARRSAELVVALLAILKAGAAYVPLDPAYPAERLAFMLADAGPV 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217306889 170 CIITNDVLAPAVDAVAskcenlhsklivsensregwgnlkelmkvflcHPGWSTVARSWLTATSTSLVQAilsllsswdy 249
Cdd:cd17651 95 LVLTHPALAGELAVEL--------------------------------VAVTLLDQPGAAAGADAEPDPA---------- 132
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217306889 250 RHASDshtcvktkhneIMAIFFTSGTSGYPKMTAHTHSSFglglsVNGRFWLD----LTPSDVMWNTSDTGWAKSAWSsV 325
Cdd:cd17651 133 LDADD-----------LAYVIYTSGSTGRPKGVVMPHRSL-----ANLVAWQArassLGPGARTLQFAGLGFDVSVQE-I 195
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217306889 326 FSPWIQGACVfthHLP----RFEPTSILQTLSKYPITVfCSAPTVY--RMLVQNDITSYKFKSLKHCVSAGEP--ITPDV 397
Cdd:cd17651 196 FSTLCAGATL---VLPpeevRTDPPALAAWLDEQRISR-VFLPTVAlrALAEHGRPLGVRLAALRYLLTGGEQlvLTEDL 271
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217306889 398 TEKWRNKTGLDIYEGYGQTE----TVLICGNFKGMKIKPGSMGKPSPAFDVKIVDVNGNVLPPGQEGDI---GIQVLP-- 468
Cdd:cd17651 272 REFCAGLPGLRLHNHYGPTEthvvTALSLPGDPAAWPAPPPIGRPIDNTRVYVLDAALRPVPPGVPGELyigGAGLARgy 351
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217306889 469 -NRPfGLfTH--YVDNPSKTASTLrgnfYITGDRGYMDKDGYFWFVARADDVILSSGYRIGPFEVENALNEHPSVAESAV 545
Cdd:cd17651 352 lNRP-EL-TAerFVPDPFVPGARM----YRTGDLARWLPDGELEFLGRADDQVKIRGFRIELGEIEAALARHPGVREAVV 425
|
490 500
....*....|....*....|.
gi 2217306889 546 VSSPDPIRGEVVKAFVVLNPD 566
Cdd:cd17651 426 LAREDRPGEKRLVAYVVGDPE 446
|
|
| A_NRPS_PvdJ-like |
cd17649 |
non-ribosomal peptide synthetase; This family of the adenylation (A) domain of nonribosomal ... |
254-593 |
7.87e-30 |
|
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: 122.86 E-value: 7.87e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217306889 254 DS-HTCVKTKHNEIMA-IFFTSGTSGYPKMTAHTHSSFGLGLSVNGRFwLDLTPSDVMWNTSDTGWaKSAWSSVFSPWIQ 331
Cdd:cd17649 82 DSgAGLLLTHHPRQLAyVIYTSGSTGTPKGVAVSHGPLAAHCQATAER-YGLTPGDRELQFASFNF-DGAHEQLLPPLIC 159
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217306889 332 GACVFTHHLPRFEPTSILQTL-SKYPITVFCSAPTVYRMLVQ--NDITSYKFKSLKHCVSAGEPITPDVTEKWRnKTGLD 408
Cdd:cd17649 160 GACVVLRPDELWASADELAEMvRELGVTVLDLPPAYLQQLAEeaDRTGDGRPPSLRLYIFGGEALSPELLRRWL-KAPVR 238
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217306889 409 IYEGYGQTETVLICGNFK---GMKIKPGSM--GKPSPAFDVKIVDVNGNVLPPGQEGD--IGIQVLP----NRPfGLfTH 477
Cdd:cd17649 239 LFNAYGPTEATVTPLVWKceaGAARAGASMpiGRPLGGRSAYILDADLNPVPVGVTGElyIGGEGLArgylGRP-EL-TA 316
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217306889 478 --YVDNPSKTAStlrGNFYITGD--RgYMDkDGYFWFVARADDVILSSGYRIGPFEVENALNEHPSVAESAVVSSPDPIR 553
Cdd:cd17649 317 erFVPDPFGAPG---SRLYRTGDlaR-WRD-DGVIEYLGRVDHQVKIRGFRIELGEIEAALLEHPGVREAAVVALDGAGG 391
|
330 340 350 360
....*....|....*....|....*....|....*....|
gi 2217306889 554 GEVVkAFVVLNPDYKshdQEQLIKEIQEHVKKTTAPYKYP 593
Cdd:cd17649 392 KQLV-AYVVLRAAAA---QPELRAQLRTALRASLPDYMVP 427
|
|
| PRK08162 |
PRK08162 |
acyl-CoA synthetase; Validated |
91-596 |
9.89e-30 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236169 [Multi-domain] Cd Length: 545 Bit Score: 123.90 E-value: 9.89e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217306889 91 EEMRWSFEELGSLSRKFANILSEAcSLQRGDRVILILPRVPEWWLANVACLRTGTVLIPGTTQLTQKDILYRLQSSKANC 170
Cdd:PRK08162 40 GDRRRTWAETYARCRRLASALARR-GIGRGDTVAVLLPNIPAMVEAHFGVPMAGAVLNTLNTRLDAASIAFMLRHGEAKV 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217306889 171 IITNDVLAPAVDAVASKCENLHSKLI-VSENSREGWGNLKEL-MKVFLCH--PG--WSTVARSWltatstslvQAIlsll 244
Cdd:PRK08162 119 LIVDTEFAEVAREALALLPGPKPLVIdVDDPEYPGGRFIGALdYEAFLASgdPDfaWTLPADEW---------DAI---- 185
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217306889 245 sswdyrhasdshtcvktkhneimAIFFTSGTSGYPKMTAHTHSSFGLGLSVNGRFWlDLTPSDV-MW-------NtsdtG 316
Cdd:PRK08162 186 -----------------------ALNYTSGTTGNPKGVVYHHRGAYLNALSNILAW-GMPKHPVyLWtlpmfhcN----G 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217306889 317 WAksawssvFsPWIQGACVFTH-HLPRFEPTSILQTLSKYPITVFCSAPTVYRMLVqNDITSYKfKSLKHCVS---AGEP 392
Cdd:PRK08162 238 WC-------F-PWTVAARAGTNvCLRKVDPKLIFDLIREHGVTHYCGAPIVLSALI-NAPAEWR-AGIDHPVHamvAGAA 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217306889 393 ITPDVTEKWRNkTGLDIYEGYGQTET---VLIC--------------GNFKGMK------------IKPGSMgKPSPAFD 443
Cdd:PRK08162 308 PPAAVIAKMEE-IGFDLTHVYGLTETygpATVCawqpewdalplderAQLKARQgvryplqegvtvLDPDTM-QPVPADG 385
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217306889 444 VKI--VDVNGNVLPPGqegdigiqvlpnrpfglfthYVDNPSKTASTLRGNFYITGDRGYMDKDGYFWFVARADDVILSS 521
Cdd:PRK08162 386 ETIgeIMFRGNIVMKG--------------------YLKNPKATEEAFAGGWFHTGDLAVLHPDGYIKIKDRSKDIIISG 445
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2217306889 522 GYRIGPFEVENALNEHPSVAESAVVSSPDPIRGEVVKAFVVLNPDyKSHDQEqlikEIQEHVKKTTAPYKYPRKV 596
Cdd:PRK08162 446 GENISSIEVEDVLYRHPAVLVAAVVAKPDPKWGEVPCAFVELKDG-ASATEE----EIIAHCREHLAGFKVPKAV 515
|
|
| PRK06060 |
PRK06060 |
p-hydroxybenzoic acid--AMP ligase FadD22; |
117-599 |
1.39e-29 |
|
p-hydroxybenzoic acid--AMP ligase FadD22;
Pssm-ID: 180374 [Multi-domain] Cd Length: 705 Bit Score: 124.37 E-value: 1.39e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217306889 117 LQRGDRVILILPRVPEWWLANVACLRTGTVLIPGTTQLTQKDILYRLQSSKANCIITNDVLapavdavaskCENLHSKLI 196
Cdd:PRK06060 52 LSSGDRVLLCLPDSPDLVQLLLACLARGVMAFLANPELHRDDHALAARNTEPALVVTSDAL----------RDRFQPSRV 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217306889 197 VSEnsregwgnlKELMkvflchpgwSTVARSwltatstslvqailsllSSWDYRHASDSHTCVKTkhneimaifFTSGTS 276
Cdd:PRK06060 122 AEA---------AELM---------SEAARV-----------------APGGYEPMGGDALAYAT---------YTSGTT 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217306889 277 GYPKMTAHTHSSFGLGLSVNGRFWLDLTPSDVMWNTSDTGWAKSAWSSVFSPWIQGACVFTHHLP-RFEPTSILQTlsKY 355
Cdd:PRK06060 158 GPPKAAIHRHADPLTFVDAMCRKALRLTPEDTGLCSARMYFAYGLGNSVWFPLATGGSAVINSAPvTPEAAAILSA--RF 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217306889 356 PITVFCSAPTVYRMLVqNDITSYKFKSLKHCVSAGEPITPDVTEKWRNK-TGLDIYEGYGQTEtvlICGNFKGMKI---K 431
Cdd:PRK06060 236 GPSVLYGVPNFFARVI-DSCSPDSFRSLRCVVSAGEALELGLAERLMEFfGGIPILDGIGSTE---VGQTFVSNRVdewR 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217306889 432 PGSMGKPSPAFDVKIVDVNGNVLPPGQEGDIGI------QVLPNRPFGLFTHyvdnpsktastlrGNFYITGDRGYMDKD 505
Cdd:PRK06060 312 LGTLGRVLPPYEIRVVAPDGTTAGPGVEGDLWVrgpaiaKGYWNRPDSPVAN-------------EGWLDTRDRVCIDSD 378
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217306889 506 GYFWFVARADDVILSSGYRIGPFEVENALNEHPSVAESAVVSSPDPIRGEVVKAFVVlnPDYKSHDQEQLIKEIQEHVKK 585
Cdd:PRK06060 379 GWVTYRCRADDTEVIGGVNVDPREVERLIIEDEAVAEAAVVAVRESTGASTLQAFLV--ATSGATIDGSVMRDLHRGLLN 456
|
490
....*....|....
gi 2217306889 586 TTAPYKYPRKVGIL 599
Cdd:PRK06060 457 RLSAFKVPHRFAVV 470
|
|
| PRK09088 |
PRK09088 |
acyl-CoA synthetase; Validated |
269-596 |
2.25e-29 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 181644 [Multi-domain] Cd Length: 488 Bit Score: 122.22 E-value: 2.25e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217306889 269 IFFTSGTSGYPK--MTA-----HTHSSFGLGLSVNGR--FWLDlTPsdvMWNTsdTGWAksawSSVFSPWIQGACVFTHh 339
Cdd:PRK09088 140 ILFTSGTSGQPKgvMLSernlqQTAHNFGVLGRVDAHssFLCD-AP---MFHI--IGLI----TSVRPVLAVGGSILVS- 208
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217306889 340 lPRFEPTSILQTLS--KYPITVFCSAPTVYRML-VQNDITSYKFKSLKHCVSAGEPITPDVTEKWRNKtGLDIYEGYGQT 416
Cdd:PRK09088 209 -NGFEPKRTLGRLGdpALGITHYFCVPQMAQAFrAQPGFDAAALRHLTALFTGGAPHAAEDILGWLDD-GIPMVDGFGMS 286
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217306889 417 E--TVLicgnfkGMKI-------KPGSMGKPSPAFDVKIVDVNGNVLPPGQEGDIGIQVlPNrpfgLFTHYVDNPSKTAS 487
Cdd:PRK09088 287 EagTVF------GMSVdcdviraKAGAAGIPTPTVQTRVVDDQGNDCPAGVPGELLLRG-PN----LSPGYWRRPQATAR 355
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217306889 488 TLRGN-FYITGDRGYMDKDGYFWFVARADDVILSSGYRIGPFEVENALNEHPSVAESAVVSSPDPIRGEVVKAFVVLNPd 566
Cdd:PRK09088 356 AFTGDgWFRTGDIARRDADGFFWVVDRKKDMFISGGENVYPAEIEAVLADHPGIRECAVVGMADAQWGEVGYLAIVPAD- 434
|
330 340 350
....*....|....*....|....*....|
gi 2217306889 567 ykshDQEQLIKEIQEHVKKTTAPYKYPRKV 596
Cdd:PRK09088 435 ----GAPLDLERIRSHLSTRLAKYKVPKHL 460
|
|
| OSB_MenE-like |
cd17630 |
O-succinylbenzoic acid-CoA ligase; This family contains O-succinylbenzoyl-CoA (OSB-CoA) ... |
269-594 |
2.54e-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: 118.59 E-value: 2.54e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217306889 269 IFFTSGTSGYPKMTAHT-----HSSFG----LGLSVNGRfWLDLTPS------DVMWNtsdtgWAKSAWSSVFSPWIQGA 333
Cdd:cd17630 5 VILTSGSTGTPKAVVHTaanllASAAGlhsrLGFGGGDS-WLLSLPLyhvgglAILVR-----SLLAGAELVLLERNQAL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217306889 334 cvfthhlprfeptsiLQTLSKYPITVFCSAPTVYRMLVQNDITSYKFKSLKHCVSAGEPITPDVTEKWRNKtGLDIYEGY 413
Cdd:cd17630 79 ---------------AEDLAPPGVTHVSLVPTQLQRLLDSGQGPAALKSLRAVLLGGAPIPPELLERAADR-GIPLYTTY 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217306889 414 GQTETV-LICGNFKGMKiKPGSMGKPSPAFDVKIVDvngnvlppgqEGDIGIqvlpnRPFGLFTHYVDNPSKTASTLRGN 492
Cdd:cd17630 143 GMTETAsQVATKRPDGF-GRGGVGVLLPGRELRIVE----------DGEIWV-----GGASLAMGYLRGQLVPEFNEDGW 206
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217306889 493 FYiTGDRGYMDKDGYFWFVARADDVILSSGYRIGPFEVENALNEHPSVAESAVVSSPDPIRGEVVKAFVVLNPdykSHDQ 572
Cdd:cd17630 207 FT-TKDLGELHADGRLTVLGRADNMIISGGENIQPEEIEAALAAHPAVRDAFVVGVPDEELGQRPVAVIVGRG---PADP 282
|
330 340
....*....|....*....|..
gi 2217306889 573 EQLIkeiqEHVKKTTAPYKYPR 594
Cdd:cd17630 283 AELR----AWLKDKLARFKLPK 300
|
|
| A_NRPS_Srf_like |
cd12117 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including Bacillus subtilis ... |
269-593 |
4.05e-28 |
|
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: 118.07 E-value: 4.05e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217306889 269 IFFTSGTSGYPKMTAHTHSSFgLGLsVNGRFWLDLTPSDVMWNTSDTGWAKSAWSsVFSPWIQGACVF---THHLPRfeP 345
Cdd:cd12117 141 VMYTSGSTGRPKGVAVTHRGV-VRL-VKNTNYVTLGPDDRVLQTSPLAFDASTFE-IWGALLNGARLVlapKGTLLD--P 215
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217306889 346 TSILQTLSKYPITV-FCSAPtVYRMLVQNDITSykFKSLKHCVSAGEPITPDVTEKWRNKT-GLDIYEGYGQTE--TVLI 421
Cdd:cd12117 216 DALGALIAEEGVTVlWLTAA-LFNQLADEDPEC--FAGLRELLTGGEVVSPPHVRRVLAACpGLRLVNGYGPTEntTFTT 292
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217306889 422 CGNFKGMKIKPGS--MGKPSPAFDVKIVDVNGNVLPPGQEGDI---GIQVLP---NRPFGLFTHYVDNPSKTASTLrgnf 493
Cdd:cd12117 293 SHVVTELDEVAGSipIGRPIANTRVYVLDEDGRPVPPGVPGELyvgGDGLALgylNRPALTAERFVADPFGPGERL---- 368
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217306889 494 YITGDRGYMDKDGYFWFVARADDVILSSGYRIGPFEVENALNEHPSVAESAV-VSSPDPIRGEVVkAFVVLNPDyKSHDq 572
Cdd:cd12117 369 YRTGDLARWLPDGRLEFLGRIDDQVKIRGFRIELGEIEAALRAHPGVREAVVvVREDAGGDKRLV-AYVVAEGA-LDAA- 445
|
330 340
....*....|....*....|.
gi 2217306889 573 eqlikEIQEHVKKTTAPYKYP 593
Cdd:cd12117 446 -----ELRAFLRERLPAYMVP 461
|
|
| PLN02574 |
PLN02574 |
4-coumarate--CoA ligase-like |
253-596 |
2.73e-27 |
|
4-coumarate--CoA ligase-like
Pssm-ID: 215312 [Multi-domain] Cd Length: 560 Bit Score: 116.48 E-value: 2.73e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217306889 253 SDSHTCVK--TKHNEIMAIFFTSGTSGYPKMTAHTHSSFGLGLSVNGRFwldltpsdvmwntSDTGWAKSAWSSVFSP-- 328
Cdd:PLN02574 185 EDFDFVPKpvIKQDDVAAIMYSSGTTGASKGVVLTHRNLIAMVELFVRF-------------EASQYEYPGSDNVYLAal 251
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217306889 329 ---WIQGACVFTHHL----------PRFEPTSILQTLSKYPITVFCSAPTVYRMLVQN--DITSYKFKSLKHCVSAGEPI 393
Cdd:PLN02574 252 pmfHIYGLSLFVVGLlslgstivvmRRFDASDMVKVIDRFKVTHFPVVPPILMALTKKakGVCGEVLKSLKQVSCGAAPL 331
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217306889 394 TPDVTEKW-RNKTGLDIYEGYGQTETVLICG---NFKGMKiKPGSMGKPSPAFDVKIVD-VNGNVLPPGQEGDIGIQvlp 468
Cdd:PLN02574 332 SGKFIQDFvQTLPHVDFIQGYGMTESTAVGTrgfNTEKLS-KYSSVGLLAPNMQAKVVDwSTGCLLPPGNCGELWIQ--- 407
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217306889 469 nRPfGLFTHYVDNPSKTASTLRGNFYI-TGDRGYMDKDGYFWFVARADDVILSSGYRIGPFEVENALNEHPSVAESAVVS 547
Cdd:PLN02574 408 -GP-GVMKGYLNNPKATQSTIDKDGWLrTGDIAYFDEDGYLYIVDRLKEIIKYKGFQIAPADLEAVLISHPEIIDAAVTA 485
|
330 340 350 360
....*....|....*....|....*....|....*....|....*....
gi 2217306889 548 SPDPIRGEVVKAFVVLNPDyKSHDQEQLIkeiqEHVKKTTAPYKYPRKV 596
Cdd:PLN02574 486 VPDKECGEIPVAFVVRRQG-STLSQEAVI----NYVAKQVAPYKKVRKV 529
|
|
| A_NRPS_Cytc1-like |
cd17643 |
similar to adenylation domain of cytotrienin synthetase CytC1; This family of the adenylation ... |
269-594 |
4.57e-27 |
|
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: 114.71 E-value: 4.57e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217306889 269 IFFTSGTSGYPKMTAHTHSSFgLGLSVNGRFWLDLTPSDVMWNTSDTGWAKSAWSsVFSPWIQGA--CVFTHHLPRfEPT 346
Cdd:cd17643 98 VIYTSGSTGRPKGVVVSHANV-LALFAATQRWFGFNEDDVWTLFHSYAFDFSVWE-IWGALLHGGrlVVVPYEVAR-SPE 174
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217306889 347 SILQTLSKYPITVFCSAPTVYRMLVQNDITSYKFK-SLKHCVSAGEPITPDVTEKWRNKTGL---DIYEGYGQTET-VLI 421
Cdd:cd17643 175 DFARLLRDEGVTVLNQTPSAFYQLVEAADRDGRDPlALRYVIFGGEALEAAMLRPWAGRFGLdrpQLVNMYGITETtVHV 254
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217306889 422 cgNFKGMK---IKPGSM---GKPSPAFDVKIVDVNGNVLPPGQEGDI---GIQVLP---NRPFGLFTHYVDNPsKTASTL 489
Cdd:cd17643 255 --TFRPLDaadLPAAAAspiGRPLPGLRVYVLDADGRPVPPGVVGELyvsGAGVARgylGRPELTAERFVANP-FGGPGS 331
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217306889 490 RGnfYITGDRGYMDKDGYFWFVARADDVILSSGYRIGPFEVENALNEHPSVAESAVVSSPDPIRGEVVKAFVVLNpdyks 569
Cdd:cd17643 332 RM--YRTGDLARRLPDGELEYLGRADEQVKIRGFRIELGEIEAALATHPSVRDAAVIVREDEPGDTRLVAYVVAD----- 404
|
330 340
....*....|....*....|....*
gi 2217306889 570 HDQEQLIKEIQEHVKKTTAPYKYPR 594
Cdd:cd17643 405 DGAAADIAELRALLKELLPDYMVPA 429
|
|
| AFD_YhfT-like |
cd17633 |
fatty acid-CoA ligase VraA; This family of acyl-CoA ligases includes Bacillus subtilis YhfT, ... |
271-596 |
4.85e-27 |
|
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: 112.11 E-value: 4.85e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217306889 271 FTSGTSGYPKMTAHTHSSfglglsvngrfWLDLTPSDVMwntsdtGWAKSAWSSVFSPwiqGACVFTHHL---------- 340
Cdd:cd17633 7 FTSGTTGLPKAYYRSERS-----------WIESFVCNED------LFNISGEDAILAP---GPLSHSLFLygaisalylg 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217306889 341 ------PRFEPTSILQTLSKYPITVFCSAPTVYRMLVQNDITSYKFKSLkhcVSAGEPITPDVTEKWRNKT-GLDIYEGY 413
Cdd:cd17633 67 gtfigqRKFNPKSWIRKINQYNATVIYLVPTMLQALARTLEPESKIKSI---FSSGQKLFESTKKKLKNIFpKANLIEFY 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217306889 414 GQTETVLICGNFKGMKIKPGSMGKPSPAFDVKIVDVNGNVlppgqegdIG-IQVLPNRpfgLFTHYVDNPSKTAstlrGN 492
Cdd:cd17633 144 GTSELSFITYNFNQESRPPNSVGRPFPNVEIEIRNADGGE--------IGkIFVKSEM---VFSGYVRGGFSNP----DG 208
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217306889 493 FYITGDRGYMDKDGYFWFVARADDVILSSGYRIGPFEVENALNEHPSVAESAVVSSPDPIRGEVVKAFVVLNpdyKSHDQ 572
Cdd:cd17633 209 WMSVGDIGYVDEEGYLYLVGRESDMIIIGGINIFPTEIESVLKAIPGIEEAIVVGIPDARFGEIAVALYSGD---KLTYK 285
|
330 340
....*....|....*....|....
gi 2217306889 573 EQLIKeiqehVKKTTAPYKYPRKV 596
Cdd:cd17633 286 QLKRF-----LKQKLSRYEIPKKI 304
|
|
| EntF |
COG1020 |
EntF, seryl-AMP synthase component of non-ribosomal peptide synthetase [Secondary metabolites ... |
271-566 |
1.33e-26 |
|
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: 116.11 E-value: 1.33e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217306889 271 FTSGTSGYPKMTAHTHSSFG-LGLSVNGRFwlDLTPSDVM-WNTS---DTgwakSAWSsVFSPWIQGACVfthHLP---- 341
Cdd:COG1020 624 YTSGSTGRPKGVMVEHRALVnLLAWMQRRY--GLGPGDRVlQFASlsfDA----SVWE-IFGALLSGATL---VLAppea 693
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217306889 342 RFEPTSILQTLSKYPITVFCSAPTVYRMLVQNDITSykFKSLKHCVSAGEPITPDVTEKWRNKT-GLDIYEGYGQTETVL 420
Cdd:COG1020 694 RRDPAALAELLARHRVTVLNLTPSLLRALLDAAPEA--LPSLRLVLVGGEALPPELVRRWRARLpGARLVNLYGPTETTV 771
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217306889 421 --ICGNFKGMKIKPGSM--GKPSPAFDVKIVDVNGNVLPPGQEGDI---GIQV----LpNRPfGL----FthyVDNPSKT 485
Cdd:COG1020 772 dsTYYEVTPPDADGGSVpiGRPIANTRVYVLDAHLQPVPVGVPGELyigGAGLargyL-NRP-ELtaerF---VADPFGF 846
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217306889 486 ASTlRgnFYITGDRGYMDKDGYFWFVARADDVILSSGYRIGPFEVENALNEHPSVAESAVVSSPDPIRGEVVKAFVVLNP 565
Cdd:COG1020 847 PGA-R--LYRTGDLARWLPDGNLEFLGRADDQVKIRGFRIELGEIEAALLQHPGVREAVVVAREDAPGDKRLVAYVVPEA 923
|
.
gi 2217306889 566 D 566
Cdd:COG1020 924 G 924
|
|
| A_NRPS_Bac |
cd17655 |
bacitracin synthetase and related proteins; This family of the adenylation (A) domain of ... |
269-593 |
1.50e-26 |
|
bacitracin synthetase and related proteins; This family of the adenylation (A) domain of nonribosomal peptide synthases (NRPS) includes bacitracin synthetases 1, 2, and 3 (BA1, also known as ATP-dependent cysteine adenylase or cysteine activase, BA2, also known as ATP-dependent lysine adenylase or lysine activase, and BA3, also known as ATP-dependent isoleucine adenylase or isoleucine activase) in Bacilli. Bacitracin is a mixture of related cyclic peptides used as a polypeptide antibiotic. This family also includes gramicidin synthetase 1 involved in synthesis of the cyclic peptide antibiotic gramicidin S via activation of phenylalanine. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.
Pssm-ID: 341310 [Multi-domain] Cd Length: 490 Bit Score: 113.58 E-value: 1.50e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217306889 269 IFFTSGTSGYPKMTAHTHSSFglglsVNGRFWLD----LTPSDVMWNTSDTGWAKSAWSsVFSPWIQGACVFTH-HLPRF 343
Cdd:cd17655 142 VIYTSGSTGKPKGVMIEHRGV-----VNLVEWANkviyQGEHLRVALFASISFDASVTE-IFASLLSGNTLYIVrKETVL 215
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217306889 344 EPTSILQTLSKYPITVFCSAPTVYRMLVQNDITSykFKSLKHCVSAGEPITPDVTEKW--RNKTGLDIYEGYGQTETVLI 421
Cdd:cd17655 216 DGQALTQYIRQNRITIIDLTPAHLKLLDAADDSE--GLSLKHLIVGGEALSTELAKKIieLFGTNPTITNAYGPTETTVD 293
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217306889 422 C--GNFKGMKIKPGS--MGKPSPAFDVKIVDVNGNVLPPGQEGDIGI------QVLPNRPFGLFTHYVDNPSKTAstlrG 491
Cdd:cd17655 294 AsiYQYEPETDQQVSvpIGKPLGNTRIYILDQYGRPQPVGVAGELYIggegvaRGYLNRPELTAEKFVDDPFVPG----E 369
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217306889 492 NFYITGDRGYMDKDGYFWFVARADDVILSSGYRIGPFEVENALNEHPSVAESAVVSSPDPIRGEVVKAFVVLNPDYKshd 571
Cdd:cd17655 370 RMYRTGDLARWLPDGNIEFLGRIDHQVKIRGYRIELGEIEARLLQHPDIKEAVVIARKDEQGQNYLCAYIVSEKELP--- 446
|
330 340
....*....|....*....|..
gi 2217306889 572 qeqlIKEIQEHVKKTTAPYKYP 593
Cdd:cd17655 447 ----VAQLREFLARELPDYMIP 464
|
|
| PLN02860 |
PLN02860 |
o-succinylbenzoate-CoA ligase |
212-594 |
2.11e-26 |
|
o-succinylbenzoate-CoA ligase
Pssm-ID: 215464 [Multi-domain] Cd Length: 563 Bit Score: 113.74 E-value: 2.11e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217306889 212 MKVFLCHPGWSTV--ARSWLTaTSTSLVQAILSllSSWDYRHASDShtcvktkhneIMAIFFTSGTSGYPKMTAHTHSSF 289
Cdd:PLN02860 131 WQVFLESPSSSVFifLNSFLT-TEMLKQRALGT--TELDYAWAPDD----------AVLICFTSGTTGRPKGVTISHSAL 197
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217306889 290 ---GLG-LSVNGrfwldLTPSDVMWNTS---DTGwaksAWSSVFSPWIQGAC-VFthhLPRFEPTSILQTLSKYPITVFC 361
Cdd:PLN02860 198 ivqSLAkIAIVG-----YGEDDVYLHTAplcHIG----GLSSALAMLMVGAChVL---LPKFDAKAALQAIKQHNVTSMI 265
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217306889 362 SAPTVYRMLV---QNDITSYKFKSLKHCVSAGEPIT----PDVTEKWRNKtglDIYEGYGQTET----------VLICGN 424
Cdd:PLN02860 266 TVPAMMADLIsltRKSMTWKVFPSVRKILNGGGSLSsrllPDAKKLFPNA---KLFSAYGMTEAcssltfmtlhDPTLES 342
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217306889 425 FK-----GMKIKPGS--------MGKPSPAFDVKIvdvngnvlppGQEGDIGIQVLPNRPFGLFTHYVDNPSKTASTLRG 491
Cdd:PLN02860 343 PKqtlqtVNQTKSSSvhqpqgvcVGKPAPHVELKI----------GLDESSRVGRILTRGPHVMLGYWGQNSETASVLSN 412
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217306889 492 NFYI-TGDRGYMDKDGYFWFVARADDVILSSGYRIGPFEVENALNEHPSVAESAVVSSPDPIRGEVVKAFVVLNPDYK-S 569
Cdd:PLN02860 413 DGWLdTGDIGWIDKAGNLWLIGRSNDRIKTGGENVYPEEVEAVLSQHPGVASVVVVGVPDSRLTEMVVACVRLRDGWIwS 492
|
410 420 430
....*....|....*....|....*....|....
gi 2217306889 570 HDQEQLIK--------EIQEHV-KKTTAPYKYPR 594
Cdd:PLN02860 493 DNEKENAKknltlsseTLRHHCrEKNLSRFKIPK 526
|
|
| PRK08315 |
PRK08315 |
AMP-binding domain protein; Validated |
94-596 |
5.12e-26 |
|
AMP-binding domain protein; Validated
Pssm-ID: 236236 [Multi-domain] Cd Length: 559 Bit Score: 112.60 E-value: 5.12e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217306889 94 RWSFEELGSLSRKFANILSeACSLQRGDRVILILPRVPEWWLANVACLRTGTVLIPGTTQLTQKDILYRLQSS--KANCI 171
Cdd:PRK08315 43 RWTYREFNEEVDALAKGLL-ALGIEKGDRVGIWAPNVPEWVLTQFATAKIGAILVTINPAYRLSELEYALNQSgcKALIA 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217306889 172 I----TNDVLApAVDAVASKCENLHSKLIVSENSREgwgnLKELmkVFLC---HPG---WSTVARSWLTATSTSLvQAIL 241
Cdd:PRK08315 122 AdgfkDSDYVA-MLYELAPELATCEPGQLQSARLPE----LRRV--IFLGdekHPGmlnFDELLALGRAVDDAEL-AARQ 193
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217306889 242 SLLSSWDyrhasdshtcvktkhneIMAIFFTSGTSGYPKMTAHTHSSFGLglsvNGRF---WLDLTPSD----------- 307
Cdd:PRK08315 194 ATLDPDD-----------------PINIQYTSGTTGFPKGATLTHRNILN----NGYFigeAMKLTEEDrlcipvplyhc 252
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217306889 308 ---VMWNTsdtgwaksawssvfspwiqgACVfTHH------LPRFEPTSILQTLSKYPITVFCSAPTVY-RMLVQNDITS 377
Cdd:PRK08315 253 fgmVLGNL--------------------ACV-THGatmvypGEGFDPLATLAAVEEERCTALYGVPTMFiAELDHPDFAR 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217306889 378 YKFKSLKHCVSAGEPITPDVTEKWRNKTGL-DIYEGYGQTETvlicgnfkgmkiKPGSM---------------GKPSPA 441
Cdd:PRK08315 312 FDLSSLRTGIMAGSPCPIEVMKRVIDKMHMsEVTIAYGMTET------------SPVSTqtrtddplekrvttvGRALPH 379
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217306889 442 FDVKIVD-VNGNVLPPGQEGDigiqvLPNRPFGLFTHYVDNPSKTASTL-RGNFYITGDRGYMDKDGYFWFVARADDVIL 519
Cdd:PRK08315 380 LEVKIVDpETGETVPRGEQGE-----LCTRGYSVMKGYWNDPEKTAEAIdADGWMHTGDLAVMDEEGYVNIVGRIKDMII 454
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2217306889 520 SSGYRIGPFEVENALNEHPSVAESAVVSSPDPIRGEVVKAFVVLNPDYKSHDQeqlikEIQEHVKKTTAPYKYPRKV 596
Cdd:PRK08315 455 RGGENIYPREIEEFLYTHPKIQDVQVVGVPDEKYGEEVCAWIILRPGATLTEE-----DVRDFCRGKIAHYKIPRYI 526
|
|
| PTZ00237 |
PTZ00237 |
acetyl-CoA synthetase; Provisional |
269-604 |
8.40e-26 |
|
acetyl-CoA synthetase; Provisional
Pssm-ID: 240325 [Multi-domain] Cd Length: 647 Bit Score: 112.53 E-value: 8.40e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217306889 269 IFFTSGTSGYPKMTAHTHSSFGLGLSVNGRFWLDLTPSDVMWNTSDTGWAKsawssvFSPWIQGACVFTHHLPRFE---- 344
Cdd:PTZ00237 259 ILYTSGTTGNSKAVVRSNGPHLVGLKYYWRSIIEKDIPTVVFSHSSIGWVS------FHGFLYGSLSLGNTFVMFEggii 332
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217306889 345 -----PTSILQTLSKYPITVFCSAPTVYRMLVQND-----ITS-YKFKSLKHCVSAGEPITPDVTEKWRNKTGLDIYEGY 413
Cdd:PTZ00237 333 knkhiEDDLWNTIEKHKVTHTLTLPKTIRYLIKTDpeatiIRSkYDLSNLKEIWCGGEVIEESIPEYIENKLKIKSSRGY 412
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217306889 414 GQTET-VLICGNFKGMKIKPGSMGKPSPAFDVKIVDVNGNVLPPGQEGDIGIQvLPNRPFGLFTHYV-DNPSKTASTLRG 491
Cdd:PTZ00237 413 GQTEIgITYLYCYGHINIPYNATGVPSIFIKPSILSEDGKELNVNEIGEVAFK-LPMPPSFATTFYKnDEKFKQLFSKFP 491
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217306889 492 NFYITGDRGYMDKDGYFWFVARADDVILSSGYRIGPFEVENALNEHPSVAESAVVSSPDPIRGEVVKAFVVLNPDYKSH- 570
Cdd:PTZ00237 492 GYYNSGDLGFKDENGYYTIVSRSDDQIKISGNKVQLNTIETSILKHPLVLECCSIGIYDPDCYNVPIGLLVLKQDQSNQs 571
|
330 340 350
....*....|....*....|....*....|....*
gi 2217306889 571 -DQEQLIKEIQEHVKKTTAPYKYPRKvgILIITNI 604
Cdd:PTZ00237 572 iDLNKLKNEINNIITQDIESLAVLRK--IIIVNQL 604
|
|
| LC_FACL_like |
cd05914 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); The members of this family are ... |
261-602 |
8.42e-26 |
|
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: 110.99 E-value: 8.42e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217306889 261 TKHNEIMAIFFTSGTSGYPKMTAHTHSSfgLGLSVNGRFWLD-LTPSDVMWNTSDTGWAKSAWSSVFSPWIQGACVftHH 339
Cdd:cd05914 86 SDEDDVALINYTSGTTGNSKGVMLTYRN--IVSNVDGVKEVVlLGKGDKILSILPLHHIYPLTFTLLLPLLNGAHV--VF 161
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217306889 340 LPRFePTSILQTLSKYPITVFCSAPTVYRM--------LVQNDITSYKFK------------------------SLKHCV 387
Cdd:cd05914 162 LDKI-PSAKIIALAFAQVTPTLGVPVPLVIekifkmdiIPKLTLKKFKFKlakkinnrkirklafkkvheafggNIKEFV 240
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217306889 388 SAGEPITPDVTEKWRnKTGLDIYEGYGQTETV-LICGNFKGmKIKPGSMGKPSPAFDVKIVDVNgnvlPPGQEGDIgiQV 466
Cdd:cd05914 241 IGGAKINPDVEEFLR-TIGFPYTIGYGMTETApIISYSPPN-RIRLGSAGKVIDGVEVRIDSPD----PATGEGEI--IV 312
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217306889 467 lpnRPFGLFTHYVDNPSKTAS--TLRGNFYiTGDRGYMDKDGYFWFVARADDVI-LSSGYRIGPFEVENALNEHPSVAES 543
Cdd:cd05914 313 ---RGPNVMKGYYKNPEATAEafDKDGWFH-TGDLGKIDAEGYLYIRGRKKEMIvLSSGKNIYPEEIEAKINNMPFVLES 388
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2217306889 544 AVVsspdpIRGEVVKAFVVLNPDY---KSHDQEQLIKEIQEHVKK---TTAPyKYPRKVGILIIT 602
Cdd:cd05914 389 LVV-----VQEKKLVALAYIDPDFldvKALKQRNIIDAIKWEVRDkvnQKVP-NYKKISKVKIVK 447
|
|
| PRK08633 |
PRK08633 |
2-acyl-glycerophospho-ethanolamine acyltransferase; Validated |
258-589 |
1.97e-25 |
|
2-acyl-glycerophospho-ethanolamine acyltransferase; Validated
Pssm-ID: 236315 [Multi-domain] Cd Length: 1146 Bit Score: 112.32 E-value: 1.97e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217306889 258 CVKTKHNE-IMAIFFTSGTSGYPK--MTAHT----------------------------HSsfgLGLSVNgrFWLdltps 306
Cdd:PRK08633 775 YGPTFKPDdTATIIFSSGSEGEPKgvMLSHHnilsnieqisdvfnlrnddvilsslpffHS---FGLTVT--LWL----- 844
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217306889 307 dvmwntsdtgwaksawssvfsPWIQGACVFTHHLPrFEPTSILQTLSKYPITVFCSAPTVYRMLVQND-ITSYKFKSLKH 385
Cdd:PRK08633 845 ---------------------PLLEGIKVVYHPDP-TDALGIAKLVAKHRATILLGTPTFLRLYLRNKkLHPLMFASLRL 902
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217306889 386 CVSAGEPITPDVTEKWRNKTGLDIYEGYGQTET----------VLICGNFKGMKIKPGSMGKPSPAFDVKIVD-VNGNVL 454
Cdd:PRK08633 903 VVAGAEKLKPEVADAFEEKFGIRILEGYGATETspvasvnlpdVLAADFKRQTGSKEGSVGMPLPGVAVRIVDpETFEEL 982
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217306889 455 PPGQEGDI---GIQVLpnrpfglfTHYVDNPSKTASTLR----GNFYITGDRGYMDKDGYFWFVARaddviLSSGYRIG- 526
Cdd:PRK08633 983 PPGEDGLIligGPQVM--------KGYLGDPEKTAEVIKdidgIGWYVTGDKGHLDEDGFLTITDR-----YSRFAKIGg 1049
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217306889 527 ---PF-EVENALNE--HPSVAESAVVSSPDPIRGEVVkafVVLnpdyksHDQEQL-IKEIQEHVKKTTAP 589
Cdd:PRK08633 1050 emvPLgAVEEELAKalGGEEVVFAVTAVPDEKKGEKL---VVL------HTCGAEdVEELKRAIKESGLP 1110
|
|
| PRK07798 |
PRK07798 |
acyl-CoA synthetase; Validated |
58-596 |
3.27e-25 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236100 [Multi-domain] Cd Length: 533 Bit Score: 109.97 E-value: 3.27e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217306889 58 FNFAkDVLDQWTDKekagkKPSNPAFWWINRngeemRWSFEELGSLSRKFANILSEAcSLQRGDRVILILPRVPEWWLAN 137
Cdd:PRK07798 3 WNIA-DLFEAVADA-----VPDRVALVCGDR-----RLTYAELEERANRLAHYLIAQ-GLGPGDHVGIYARNRIEYVEAM 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217306889 138 VACLRTGTVLIPGTTQLTQKDILYRLQSSKANCIITNDVLAPAVDAVASKCENLHSKLIVSENSREGWGnlkelmkvflc 217
Cdd:PRK07798 71 LGAFKARAVPVNVNYRYVEDELRYLLDDSDAVALVYEREFAPRVAEVLPRLPKLRTLVVVEDGSGNDLL----------- 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217306889 218 hPGwstvARSWLTATStslvqailsllsswdyrhASDSHTCVKTKHNEIMAIFFTSGTSGYPK--MTAHT---HSSFGLG 292
Cdd:PRK07798 140 -PG----AVDYEDALA------------------AGSPERDFGERSPDDLYLLYTGGTTGMPKgvMWRQEdifRVLLGGR 196
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217306889 293 LSVNGRF------------------WLDLTPsdVMWNTSDtgWAksAWSSVFSpwiqGACVFTHHLPRFEPTSILQTLSK 354
Cdd:PRK07798 197 DFATGEPiedeeelakraaagpgmrRFPAPP--LMHGAGQ--WA--AFAALFS----GQTVVLLPDVRFDADEVWRTIER 266
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217306889 355 YPITV-FCSAPTVYRMLVQ--NDITSYKFKSLKHCVSAGEPITPDVTEKWR----NKTGLDiyeGYGQTETvlicgNFKG 427
Cdd:PRK07798 267 EKVNViTIVGDAMARPLLDalEARGPYDLSSLFAIASGGALFSPSVKEALLellpNVVLTD---SIGSSET-----GFGG 338
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217306889 428 MKI-KPGSMGKPSPAF----DVKIVDVNGNVLPPGqEGDIG-IQVLPNRPFGlfthYVDNPSKTASTLR---GNFY-ITG 497
Cdd:PRK07798 339 SGTvAKGAVHTGGPRFtigpRTVVLDEDGNPVEPG-SGEIGwIARRGHIPLG----YYKDPEKTAETFPtidGVRYaIPG 413
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217306889 498 DRGYMDKDGYFWFVARADDVILSSGYRIGPFEVENALNEHPSVAESAVVSSPDPIRGEVVKAFVVLNPDyKSHDQEqlik 577
Cdd:PRK07798 414 DRARVEADGTITLLGRGSVCINTGGEKVFPEEVEEALKAHPDVADALVVGVPDERWGQEVVAVVQLREG-ARPDLA---- 488
|
570
....*....|....*....
gi 2217306889 578 EIQEHVKKTTAPYKYPRKV 596
Cdd:PRK07798 489 ELRAHCRSSLAGYKVPRAI 507
|
|
| EntE |
COG1021 |
EntE, 2,3-dihydroxybenzoate-AMP synthase component of non-ribosomal peptide synthetase ... |
63-593 |
5.66e-25 |
|
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: 109.08 E-value: 5.66e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217306889 63 DVLDQWtdkekAGKKPSNPAFwwInrnGEEMRWSFEELGSLSRKFANILSEAcSLQRGDRVILILPRVPEWWLANVACLR 142
Cdd:COG1021 29 DLLRRR-----AERHPDRIAV--V---DGERRLSYAELDRRADRLAAGLLAL-GLRPGDRVVVQLPNVAEFVIVFFALFR 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217306889 143 TGtvLIPGTT--QLTQKDILYRLQSSKANCIITNDV-----LAPAVDAVASKCENLhsKLIVSENSREGWGNLKELMKvf 215
Cdd:COG1021 98 AG--AIPVFAlpAHRRAEISHFAEQSEAVAYIIPDRhrgfdYRALARELQAEVPSL--RHVLVVGDAGEFTSLDALLA-- 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217306889 216 lcHPGWSTVARSwltatstslvqailsllsswdyrHASDshtcvktkhneiMAIFFTS-GTSGYPKMTAHTHSSFGLGLS 294
Cdd:COG1021 172 --APADLSEPRP-----------------------DPDD------------VAFFQLSgGTTGLPKLIPRTHDDYLYSVR 214
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217306889 295 VNGRFWlDLTPSDVMW-------NtsdtgwakSAWSS--VFSPWIQGACVFTHhlPRFEPTSILQTLSKYPITVFCSAPT 365
Cdd:COG1021 215 ASAEIC-GLDADTVYLaalpaahN--------FPLSSpgVLGVLYAGGTVVLA--PDPSPDTAFPLIERERVTVTALVPP 283
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217306889 366 VYRMLVQ-NDITSYKFKSLKHCVSAGEPITPDVTEKWRNKTGLDIYEGYG-------QT------ETVLicgnfkgmkik 431
Cdd:COG1021 284 LALLWLDaAERSRYDLSSLRVLQVGGAKLSPELARRVRPALGCTLQQVFGmaeglvnYTrlddpeEVIL----------- 352
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217306889 432 pGSMGKP-SPAFDVKIVDVNGNVLPPGQEGdigiqVLPNRPFGLFTHYVDNPSKTAS--TLRGnFYITGDRGYMDKDGYF 508
Cdd:COG1021 353 -TTQGRPiSPDDEVRIVDEDGNPVPPGEVG-----ELLTRGPYTIRGYYRAPEHNARafTPDG-FYRTGDLVRRTPDGYL 425
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217306889 509 WFVARADDVILSSGYRIGPFEVENALNEHPSVAESAVVSSPDPIRGEVVKAFVVLNpdykshDQEQLIKEIQEHVK-KTT 587
Cdd:COG1021 426 VVEGRAKDQINRGGEKIAAEEVENLLLAHPAVHDAAVVAMPDEYLGERSCAFVVPR------GEPLTLAELRRFLReRGL 499
|
....*.
gi 2217306889 588 APYKYP 593
Cdd:COG1021 500 AAFKLP 505
|
|
| PLN02479 |
PLN02479 |
acetate-CoA ligase |
267-596 |
2.85e-24 |
|
acetate-CoA ligase
Pssm-ID: 178097 [Multi-domain] Cd Length: 567 Bit Score: 107.24 E-value: 2.85e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217306889 267 MAIFFTSGTSGYPKmtahthssfGLGLSVNGRFWLDLTpSDVMWNTSD-------------TGWAKSaWSsvfspwIQGA 333
Cdd:PLN02479 198 IALGYTSGTTASPK---------GVVLHHRGAYLMALS-NALIWGMNEgavylwtlpmfhcNGWCFT-WT------LAAL 260
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217306889 334 CVFTHHLPRFEPTSILQTLSKYPITVFCSAPTVYRMLVqNDITSYKFKSLKHCV---SAGEPITPDVTEKWrNKTGLDIY 410
Cdd:PLN02479 261 CGTNICLRQVTAKAIYSAIANYGVTHFCAAPVVLNTIV-NAPKSETILPLPRVVhvmTAGAAPPPSVLFAM-SEKGFRVT 338
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217306889 411 EGYGQTETVlicgnfkgmkiKPGSMGKPSPAFD-----------------------VKIVDVNGNVLPPGQEGDIGIQVL 467
Cdd:PLN02479 339 HTYGLSETY-----------GPSTVCAWKPEWDslppeeqarlnarqgvryiglegLDVVDTKTMKPVPADGKTMGEIVM 407
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217306889 468 pnRPFGLFTHYVDNPSKTASTLRGNFYITGDRGYMDKDGYFWFVARADDVILSSGYRIGPFEVENALNEHPSVAESAVVS 547
Cdd:PLN02479 408 --RGNMVMKGYLKNPKANEEAFANGWFHSGDLGVKHPDGYIEIKDRSKDIIISGGENISSLEVENVVYTHPAVLEASVVA 485
|
330 340 350 360
....*....|....*....|....*....|....*....|....*....
gi 2217306889 548 SPDPIRGEVVKAFVVLNPDYKSHDQEQLIKEIQEHVKKTTAPYKYPRKV 596
Cdd:PLN02479 486 RPDERWGESPCAFVTLKPGVDKSDEAALAEDIMKFCRERLPAYWVPKSV 534
|
|
| A_NRPS_GliP_like |
cd17653 |
nonribosomal peptide synthase GliP-like; This family includes the adenylation (A) domain of ... |
233-583 |
4.46e-24 |
|
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: 105.47 E-value: 4.46e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217306889 233 STSLVQAILSLL-----------SSWDYR-----HASDSHTCVKTKH-NEIMAIFFTSGTSGYPKMTAHTHSSFgLGLSV 295
Cdd:cd17653 57 SLEMLVAILAILkagaayvpldaKLPSARiqailRTSGATLLLTTDSpDDLAYIIFTSGSTGIPKGVMVPHRGV-LNYVS 135
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217306889 296 NGRFWLDLTPSDVMWNTSDTGWAKSAWSsVFSPWIQGAcvfthHLPRFEPTSILQTLSKyPITVFCSAPTVYRMLVQNDi 375
Cdd:cd17653 136 QPPARLDVGPGSRVAQVLSIAFDACIGE-IFSTLCNGG-----TLVLADPSDPFAHVAR-TVDALMSTPSILSTLSPQD- 207
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217306889 376 tsykFKSLKHCVSAGEPITPDVTEKWRNktGLDIYEGYGQTETVLICGNFKGMKIKPGSMGKPSPAFDVKIVDVNGNVLP 455
Cdd:cd17653 208 ----FPNLKTIFLGGEAVPPSLLDRWSP--GRRLYNAYGPTECTISSTMTELLPGQPVTIGKPIPNSTCYILDADLQPVP 281
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217306889 456 PGQEGDI---GIQVLPNrpfglfthYVDNPSKTASTLRGN-------FYITGDRGYMDKDGYFWFVARADDVILSSGYRI 525
Cdd:cd17653 282 EGVVGEIcisGVQVARG--------YLGNPALTASKFVPDpfwpgsrMYRTGDYGRWTEDGGLEFLGREDNQVKVRGFRI 353
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*...
gi 2217306889 526 GPFEVENALNEHPSVAESAVVSSpdpIRGEVVkAFVVlnPDykSHDQEQLIKEIQEHV 583
Cdd:cd17653 354 NLEEIEEVVLQSQPEVTQAAAIV---VNGRLV-AFVT--PE--TVDVDGLRSELAKHL 403
|
|
| PRK09274 |
PRK09274 |
peptide synthase; Provisional |
96-582 |
6.23e-24 |
|
peptide synthase; Provisional
Pssm-ID: 236443 [Multi-domain] Cd Length: 552 Bit Score: 106.14 E-value: 6.23e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217306889 96 SFEELGSLSRKFANILSEAcSLQRGDRVILILPRVPEWWLANVACLRTG--TVLI-PGttqLTQKDILYRLQSSKANCII 172
Cdd:PRK09274 43 SFAELDARSDAIAHGLNAA-GIGRGMRAVLMVTPSLEFFALTFALFKAGavPVLVdPG---MGIKNLKQCLAEAQPDAFI 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217306889 173 TNDvLAPAVdavaskcenlhSKLIvsensreGWGnlKELMKVFLchpgwsTVARSWLTAtSTSLVQAILsllsswdyRHA 252
Cdd:PRK09274 119 GIP-KAHLA-----------RRLF-------GWG--KPSVRRLV------TVGGRLLWG-GTTLATLLR--------DGA 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217306889 253 SDSHTCVKTKHNEIMAIFFTSGTSGYPKMTAHTHSSF---------GLGLSVNGRfwlDLTPSDVMwntsdtgwaksaws 323
Cdd:PRK09274 163 AAPFPMADLAPDDMAAILFTSGSTGTPKGVVYTHGMFeaqiealreDYGIEPGEI---DLPTFPLF-------------- 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217306889 324 SVFSPWIQGACVfthhLPRFEPT--------SILQTLSKYPITVFCSAPTVYRML----VQNDItsyKFKSLKHCVSAGE 391
Cdd:PRK09274 226 ALFGPALGMTSV----IPDMDPTrpatvdpaKLFAAIERYGVTNLFGSPALLERLgrygEANGI---KLPSLRRVISAGA 298
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217306889 392 PITPDVTEKWRN--KTGLDIYEGYGQTETVLICgnfkgmKIkpGS------------------MGKPSPAFDVKIVDVNG 451
Cdd:PRK09274 299 PVPIAVIERFRAmlPPDAEILTPYGATEALPIS------SI--ESreilfatraatdngagicVGRPVDGVEVRIIAISD 370
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217306889 452 N---------VLPPGQEGDI---GIQVLPNrpfglfthYVDNPSKTA-----STLRGNFYITGDRGYMDKDGYFWFVAR- 513
Cdd:PRK09274 371 ApipewddalRLATGEIGEIvvaGPMVTRS--------YYNRPEATRlakipDGQGDVWHRMGDLGYLDAQGRLWFCGRk 442
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217306889 514 ADDVILSSGyRIGPFEVENALNEHPSVAESAVVSSPDPirGEVVKAFVV-LNPDyKSHDQEQLIKEIQEH 582
Cdd:PRK09274 443 AHRVETAGG-TLYTIPCERIFNTHPGVKRSALVGVGVP--GAQRPVLCVeLEPG-VACSKSALYQELRAL 508
|
|
| PLN03102 |
PLN03102 |
acyl-activating enzyme; Provisional |
105-596 |
9.07e-24 |
|
acyl-activating enzyme; Provisional
Pssm-ID: 215576 [Multi-domain] Cd Length: 579 Bit Score: 105.87 E-value: 9.07e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217306889 105 RKFANILSeaCSLQRGDRVILILPRVPEWWLANVACLRTGTVLIPGTTQLTQKDILYRLQSSKANCIITNDVLAPAVDAV 184
Cdd:PLN03102 51 RLAASLIS--LNITKNDVVSVLAPNTPAMYEMHFAVPMAGAVLNPINTRLDATSIAAILRHAKPKILFVDRSFEPLAREV 128
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217306889 185 ----ASKCENLHSKLI-VSENSREGWGNLKELMKVFLCHPGWSTvarswltatsTSLVQAILsllsswdyrhasdshtCV 259
Cdd:PLN03102 129 lhllSSEDSNLNLPVIfIHEIDFPKRPSSEELDYECLIQRGEPT----------PSLVARMF----------------RI 182
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217306889 260 KTKHNEImAIFFTSGTSGYPKMTAHTHSSFGL-GLSVNGRFWLDLTPSdVMWNTSD---TGWAKSaWSSVFSpwiQGACV 335
Cdd:PLN03102 183 QDEHDPI-SLNYTSGTTADPKGVVISHRGAYLsTLSAIIGWEMGTCPV-YLWTLPMfhcNGWTFT-WGTAAR---GGTSV 256
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217306889 336 FTHHLPRFEptsILQTLSKYPITVFCSAPTVYRMLVQNDITSYKFKSLK-HCVSAGEPiTPDVTEKWRNKTGLDIYEGYG 414
Cdd:PLN03102 257 CMRHVTAPE---IYKNIEMHNVTHMCCVPTVFNILLKGNSLDLSPRSGPvHVLTGGSP-PPAALVKKVQRLGFQVMHAYG 332
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217306889 415 QTET---VLIC-----------GNFKGMKIKPGSMGKPSPAFDVKIVDVNGNVLPPGQE-GDIGIqvlpnRPFGLFTHYV 479
Cdd:PLN03102 333 LTEAtgpVLFCewqdewnrlpeNQQMELKARQGVSILGLADVDVKNKETQESVPRDGKTmGEIVI-----KGSSIMKGYL 407
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217306889 480 DNPSKTASTLRGNFYITGDRGYMDKDGYFWFVARADDVILSSGYRIGPFEVENALNEHPSVAESAVVSSPDPIRGEVVKA 559
Cdd:PLN03102 408 KNPKATSEAFKHGWLNTGDVGVIHPDGHVEIKDRSKDIIISGGENISSVEVENVLYKYPKVLETAVVAMPHPTWGETPCA 487
|
490 500 510 520
....*....|....*....|....*....|....*....|..
gi 2217306889 560 FVVL--NPDYKSHDQEQLI---KEIQEHVKKTTAPYKYPRKV 596
Cdd:PLN03102 488 FVVLekGETTKEDRVDKLVtreRDLIEYCRENLPHFMCPRKV 529
|
|
| PRK07867 |
PRK07867 |
acyl-CoA synthetase; Validated |
267-566 |
1.20e-23 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236120 [Multi-domain] Cd Length: 529 Bit Score: 105.15 E-value: 1.20e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217306889 267 MAIFfTSGTSGYPKMTAHTHSSF-GLGLSVNGRFwlDLTPSDVMWntsdtgwaksawssVFSPWIQGACVFTHHLP---- 341
Cdd:PRK07867 156 MLIF-TSGTSGDPKAVRCTHRKVaSAGVMLAQRF--GLGPDDVCY--------------VSMPLFHSNAVMAGWAValaa 218
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217306889 342 --------RFEPTSILQTLSKYPITVFcsaptvyrmlvqnditSYKFKSLKHCVSA---------------GEPITPDVT 398
Cdd:PRK07867 219 gasialrrKFSASGFLPDVRRYGATYA----------------NYVGKPLSYVLATperpddadnplrivyGNEGAPGDI 282
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217306889 399 EKWRNKTGLDIYEGYGQTETvlicgnfkGMKIK------PGSMGKPSPafDVKIVDVN-GNVLPPGQEGD---------I 462
Cdd:PRK07867 283 ARFARRFGCVVVDGFGSTEG--------GVAITrtpdtpPGALGPLPP--GVAIVDPDtGTECPPAEDADgrllnadeaI 352
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217306889 463 GIQVLPNRPfGLFTHYVDNPSKTASTLRGNFYITGDRGYMDKDGYFWFVARADDVILSSGYRIGPFEVENALNEHPSVAE 542
Cdd:PRK07867 353 GELVNTAGP-GGFEGYYNDPEADAERMRGGVYWSGDLAYRDADGYAYFAGRLGDWMRVDGENLGTAPIERILLRYPDATE 431
|
330 340
....*....|....*....|....
gi 2217306889 543 SAVVSSPDPIRGEVVKAFVVLNPD 566
Cdd:PRK07867 432 VAVYAVPDPVVGDQVMAALVLAPG 455
|
|
| A_NRPS_Ta1_like |
cd12116 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including salinosporamide A ... |
91-582 |
1.82e-23 |
|
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: 103.91 E-value: 1.82e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217306889 91 EEMRWSFEELGSLSRKFANILSEAcSLQRGDRVILILPRVPEWWLANVACLRTGTVLIPGTTQLTQKDILYRLQSSKANC 170
Cdd:cd12116 9 DDRSLSYAELDERANRLAARLRAR-GVGPGDRVAVYLPRSARLVAAMLAVLKAGAAYVPLDPDYPADRLRYILEDAEPAL 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217306889 171 IITNDVLapavdavaskCENLHSKLIVSENSREGWGNlkelmkvflchpgwsTVARSWLTATSTSLVqailsllsswdYr 250
Cdd:cd12116 88 VLTDDAL----------PDRLPAGLPVLLLALAAAAA---------------APAAPRTPVSPDDLA-----------Y- 130
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217306889 251 hasdshtcvktkhneimaIFFTSGTSGYPKMTAHTHSSF-GLGLSVNGRfwLDLTPSDVMWNTSDTGWAKSAWSsVFSPW 329
Cdd:cd12116 131 ------------------VIYTSGSTGRPKGVVVSHRNLvNFLHSMRER--LGLGPGDRLLAVTTYAFDISLLE-LLLPL 189
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217306889 330 IQGACVftHHLPR---FEPTSILQTLSKYPITVFCSAPTVYRMLVQNDitsykFKSLKH----CvsAGEPITPDVTEKWR 402
Cdd:cd12116 190 LAGARV--VIAPRetqRDPEALARLIEAHSITVMQATPATWRMLLDAG-----WQGRAGltalC--GGEALPPDLAARLL 260
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217306889 403 NKTGlDIYEGYGQTETVL------ICGNFKGMKIkpgsmGKPSPAFDVKIVDVNGNVLPPGQEGDI---GIQVLP---NR 470
Cdd:cd12116 261 SRVG-SLWNLYGPTETTIwstaarVTAAAGPIPI-----GRPLANTQVYVLDAALRPVPPGVPGELyigGDGVAQgylGR 334
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217306889 471 PFGLFTHYVDNPSKTAstlRGNFYITGDRGYMDKDGYFWFVARADDVILSSGYRIGPFEVENALNEHPSVAESAVVSSPD 550
Cdd:cd12116 335 PALTAERFVPDPFAGP---GSRLYRTGDLVRRRADGRLEYLGRADGQVKIRGHRIELGEIEAALAAHPGVAQAAVVVRED 411
|
490 500 510
....*....|....*....|....*....|..
gi 2217306889 551 PIRGEVVkAFVVLnPDYKSHDQEQLIKEIQEH 582
Cdd:cd12116 412 GGDRRLV-AYVVL-KAGAAPDAAALRAHLRAT 441
|
|
| PRK05852 |
PRK05852 |
fatty acid--CoA ligase family protein; |
96-593 |
2.27e-23 |
|
fatty acid--CoA ligase family protein;
Pssm-ID: 235625 [Multi-domain] Cd Length: 534 Bit Score: 104.20 E-value: 2.27e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217306889 96 SFEELGSLSRKFANILSEAcSLQRGDRVILILPRVPEWWLANVACLRTGTVLIPGTTQLTQKDILYRLQSSKANCIITnD 175
Cdd:PRK05852 45 SYRDLARLVDDLAGQLTRS-GLLPGDRVALRMGSNAEFVVALLAASRADLVVVPLDPALPIAEQRVRSQAAGARVVLI-D 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217306889 176 VLAPAVDAVASkcenlhsklivsensregwgnlkelmkvflcHPGWSTVARswlTATSTSLVQAILSLlsswdYRHASDS 255
Cdd:PRK05852 123 ADGPHDRAEPT-------------------------------TRWWPLTVN---VGGDSGPSGGTLSV-----HLDAATE 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217306889 256 HTCVKT-----KHNEIMaIFFTSGTSGYPKMTAHTHSSfgLGLSVNGRFW-LDLTPSD----VMWNTSDTGWAKSAWSSV 325
Cdd:PRK05852 164 PTPATStpeglRPDDAM-IMFTGGTTGLPKMVPWTHAN--IASSVRAIITgYRLSPRDatvaVMPLYHGHGLIAALLATL 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217306889 326 FSpwiqGACVFTHHLPRFEPTSILQTLSKYPITVFCSAPTVYRMLVQNDITSY---KFKSLKHCVSAGEPITPDVTEKWR 402
Cdd:PRK05852 241 AS----GGAVLLPARGRFSAHTFWDDIKAVGATWYTAVPTIHQILLERAATEPsgrKPAALRFIRSCSAPLTAETAQALQ 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217306889 403 NKTGLDIYEGYGQTET--------VLICGNFKGMKIKPGSMGKpSPAFDVKIVDVNGNVLPPGQEGDIGIqvlpnRPFGL 474
Cdd:PRK05852 317 TEFAAPVVCAFGMTEAthqvtttqIEGIGQTENPVVSTGLVGR-STGAQIRIVGSDGLPLPAGAVGEVWL-----RGTTV 390
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217306889 475 FTHYVDNPSKTASTLRGNFYITGDRGYMDKDGYFWFVARADDVILSSGYRIGPFEVENALNEHPSVAESAVVSSPDPIRG 554
Cdd:PRK05852 391 VRGYLGDPTITAANFTDGWLRTGDLGSLSAAGDLSIRGRIKELINRGGEKISPERVEGVLASHPNVMEAAVFGVPDQLYG 470
|
490 500 510
....*....|....*....|....*....|....*....
gi 2217306889 555 EVVKAFVVlnPDYKSHDQEQlikEIQEHVKKTTAPYKYP 593
Cdd:PRK05852 471 EAVAAVIV--PRESAPPTAE---ELVQFCRERLAAFEIP 504
|
|
| FACL_like_5 |
cd05924 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
269-596 |
2.38e-23 |
|
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ATP-dependent activation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions.
Pssm-ID: 341248 [Multi-domain] Cd Length: 364 Bit Score: 102.08 E-value: 2.38e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217306889 269 IFFTSGTSGYPKMTAHTHSSFGLGLS-----VNGRFWLDLTPSDVMWNTSDTGW--------AKSAWSSVFSPWIQGACV 335
Cdd:cd05924 8 ILYTGGTTGMPKGVMWRQEDIFRMLMggadfGTGEFTPSEDAHKAAAAAAGTVMfpapplmhGTGSWTAFGGLLGGQTVV 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217306889 336 FthHLPRFEPTSILQTLSKYPITVFCSAPTVY-RMLVQ--NDITSYKFKSLKHCVSAGEPITPDVTEKW-RNKTGLDIYE 411
Cdd:cd05924 88 L--PDDRFDPEEVWRTIEKHKVTSMTIVGDAMaRPLIDalRDAGPYDLSSLFAISSGGALLSPEVKQGLlELVPNITLVD 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217306889 412 GYGQTET-VLICGNFKGMKIKPGSMGKPSPafDVKIVDVNGNVLPPGQEGDIGIQVLPNRPFGlfthYVDNPSKTASTLR 490
Cdd:cd05924 166 AFGSSETgFTGSGHSAGSGPETGPFTRANP--DTVVLDDDGRVVPPGSGGVGWIARRGHIPLG----YYGDEAKTAETFP 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217306889 491 ---GNFY-ITGDRGYMDKDGYFWFVARADDVILSSGYRIGPFEVENALNEHPSVAESAVVSSPDPIRGEVVKAFVVLNPD 566
Cdd:cd05924 240 evdGVRYaVPGDRATVEADGTVTLLGRGSVCINTGGEKVFPEEVEEALKSHPAVYDVLVVGRPDERWGQEVVAVVQLREG 319
|
330 340 350
....*....|....*....|....*....|
gi 2217306889 567 YKSHDQeqlikEIQEHVKKTTAPYKYPRKV 596
Cdd:cd05924 320 AGVDLE-----ELREHCRTRIARYKLPKQV 344
|
|
| 23DHB-AMP_lg |
cd05920 |
2,3-dihydroxybenzoate-AMP ligase; 2,3-dihydroxybenzoate-AMP ligase activates 2, ... |
90-565 |
2.92e-23 |
|
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: 103.56 E-value: 2.92e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217306889 90 GEEMRWSFEELGSLSRKFANILSEAcSLQRGDRVILILPRVPEWWLANVACLRTGTVLIPGTTQLTQKDILYRLQSSKAN 169
Cdd:cd05920 36 DGDRRLTYRELDRRADRLAAGLRGL-GIRPGDRVVVQLPNVAEFVVLFFALLRLGAVPVLALPSHRRSELSAFCAHAEAV 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217306889 170 CIITNDVLAPavdavaskcenlhsklivsensregwgnlkelmkvflchpgwstvarswltatstslvqailsllsswdY 249
Cdd:cd05920 115 AYIVPDRHAG---------------------------------------------------------------------F 125
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217306889 250 RHASDSHTcVKTKHNEIMAIFFTSGTSGYPKMTAHTHSSFGLGLSvngrfwldlTPSDVMWNTSDT----------GWAK 319
Cdd:cd05920 126 DHRALARE-LAESIPEVALFLLSGGTTGTPKLIPRTHNDYAYNVR---------ASAEVCGLDQDTvylavlpaahNFPL 195
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217306889 320 SAWSSVFSPWIQGACVFThhlPRFEPTSILQTLSKYPITVFCSAPTVYRMLVQNDITS-YKFKSLKHCVSAGEPITPDVT 398
Cdd:cd05920 196 ACPGVLGTLLAGGRVVLA---PDPSPDAAFPLIEREGVTVTALVPALVSLWLDAAASRrADLSSLRLLQVGGARLSPALA 272
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217306889 399 EKWRNKTGLDIYEGYGQTETVLicgNFKGM----KIKPGSMGKP-SPAFDVKIVDVNGNVLPPGQEGdigiQVLPNRPFg 473
Cdd:cd05920 273 RRVPPVLGCTLQQVFGMAEGLL---NYTRLddpdEVIIHTQGRPmSPDDEIRVVDEEGNPVPPGEEG----ELLTRGPY- 344
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217306889 474 LFTHYVDNPSKTASTLRGN-FYITGDRGYMDKDGYFWFVARADDVILSSGYRIGPFEVENALNEHPSVAESAVVSSPDPI 552
Cdd:cd05920 345 TIRGYYRAPEHNARAFTPDgFYRTGDLVRRTPDGYLVVEGRIKDQINRGGEKIAAEEVENLLLRHPAVHDAAVVAMPDEL 424
|
490
....*....|...
gi 2217306889 553 RGEVVKAFVVLNP 565
Cdd:cd05920 425 LGERSCAFVVLRD 437
|
|
| PRK06164 |
PRK06164 |
acyl-CoA synthetase; Validated |
96-599 |
3.92e-23 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 235722 [Multi-domain] Cd Length: 540 Bit Score: 103.67 E-value: 3.92e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217306889 96 SFEELGSLSRKFANILSEAcSLQRGDRVILILPRVPEWWLANVACLRTGTVLIPGTTQLTQKDILYRLQSSKANCIitnd 175
Cdd:PRK06164 37 SRAELRALVDRLAAWLAAQ-GVRRGDRVAVWLPNCIEWVVLFLACARLGATVIAVNTRYRSHEVAHILGRGRARWL---- 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217306889 176 VLAPA---VDAVAskcenlhsklIVSENSREGwgnLKELMKVFLCHPGWSTVARSWLTATSTSLVQAILSLLSSWDYRHA 252
Cdd:PRK06164 112 VVWPGfkgIDFAA----------ILAAVPPDA---LPPLRAIAVVDDAADATPAPAPGARVQLFALPDPAPPAAAGERAA 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217306889 253 SDSHTCVktkhneimaIFFTSGTSGYPKMTAHTHSSF---------GLGLSVNGRFWLDLTPSDVMwntsdtgwaksAWS 323
Cdd:PRK06164 179 DPDAGAL---------LFTTSGTTSGPKLVLHRQATLlrharaiarAYGYDPGAVLLAALPFCGVF-----------GFS 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217306889 324 SVFSPWIQGACVftHHLPRFEPTSILQTLSKYPIT-VFCSAPTVYRMLVQNDiTSYKFKSLKHC-VSAGEPITPDVTEkW 401
Cdd:PRK06164 239 TLLGALAGGAPL--VCEPVFDAARTARALRRHRVThTFGNDEMLRRILDTAG-ERADFPSARLFgFASFAPALGELAA-L 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217306889 402 RNKTGLDIYEGYGQTE--TVLICGNFK---GMKIKPGsmGKP-SPAFDVKIVDV-NGNVLPPGQEGDIGIQVlPNrpfgL 474
Cdd:PRK06164 315 ARARGVPLTGLYGSSEvqALVALQPATdpvSVRIEGG--GRPaSPEARVRARDPqDGALLPDGESGEIEIRA-PS----L 387
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217306889 475 FTHYVDNPSKTASTLRGN-FYITGDRGYMDKDGYFWFVARADDVILSSGYRIGPFEVENALNEHPSVAESAVVSSpdPIR 553
Cdd:PRK06164 388 MRGYLDNPDATARALTDDgYFRTGDLGYTRGDGQFVYQTRMGDSLRLGGFLVNPAEIEHALEALPGVAAAQVVGA--TRD 465
|
490 500 510 520
....*....|....*....|....*....|....*....|....*..
gi 2217306889 554 GE-VVKAFVVLNpDYKSHDQEQLIKeiqeHVKKTTAPYKYPRKVGIL 599
Cdd:PRK06164 466 GKtVPVAFVIPT-DGASPDEAGLMA----ACREALAGFKVPARVQVV 507
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
72-593 |
5.29e-23 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 105.04 E-value: 5.29e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217306889 72 EKAGKKPSNPAFWWinrngEEMRWSFEELGSLSRKFANILseacsLQRG----DRVILILPRVPEWWLANVACLRTGTVL 147
Cdd:PRK12316 4559 ERARMTPDAVAVVF-----DEEKLTYAELNRRANRLAHAL-----IARGvgpeVLVGIAMERSAEMMVGLLAVLKAGGAY 4628
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217306889 148 IPGTTQLTQKDILYRLQSSKANCIITNDVLA---PAVDAVASkcenlhsklivsensregwgnlkelmkvflchpgwstv 224
Cdd:PRK12316 4629 VPLDPEYPRERLAYMMEDSGAALLLTQSHLLqrlPIPDGLAS-------------------------------------- 4670
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217306889 225 arswltatstslvqaiLSLLSSWDYRHASDSHTCVKTKHNEIMAIFFTSGTSGYPKMTAHTHSSFGLGLSVNGRFWlDLT 304
Cdd:PRK12316 4671 ----------------LALDRDEDWEGFPAHDPAVRLHPDNLAYVIYTSGSTGRPKGVAVSHGSLVNHLHATGERY-ELT 4733
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217306889 305 PSDVMWNTSDTGWAKSAWSsVFSPWIQGACVFTHHLPRFEPTSILQTLSKYPITVFCSAPTVYRMLVQNDITSYKFKSLK 384
Cdd:PRK12316 4734 PDDRVLQFMSFSFDGSHEG-LYHPLINGASVVIRDDSLWDPERLYAEIHEHRVTVLVFPPVYLQQLAEHAERDGEPPSLR 4812
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217306889 385 HCVSAGEPITPD-VTEKWRNKTGLDIYEGYGQTETVLICGNFKGMK-IKPGS----MGKPSPAFDVKIVDVNGNVLPPGQ 458
Cdd:PRK12316 4813 VYCFGGEAVAQAsYDLAWRALKPVYLFNGYGPTETTVTVLLWKARDgDACGAaympIGTPLGNRSGYVLDGQLNPLPVGV 4892
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217306889 459 EGD--IGIQvlpnrpfGLFTHYVDNPSKTASTL--------RGNFYITGDRGYMDKDGYFWFVARADDVILSSGYRIGPF 528
Cdd:PRK12316 4893 AGElyLGGE-------GVARGYLERPALTAERFvpdpfgapGGRLYRTGDLARYRADGVIDYLGRVDHQVKIRGFRIELG 4965
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2217306889 529 EVENALNEHPSVAESAVVSSPDPIRGEVVKAFVVLNPDYKSHDQEQ--LIKEIQEHVKKTTAPYKYP 593
Cdd:PRK12316 4966 EIEARLREHPAVREAVVIAQEGAVGKQLVGYVVPQDPALADADEAQaeLRDELKAALRERLPEYMVP 5032
|
|
| PRK13383 |
PRK13383 |
acyl-CoA synthetase; Provisional |
332-599 |
1.13e-22 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 139531 [Multi-domain] Cd Length: 516 Bit Score: 102.00 E-value: 1.13e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217306889 332 GACVFTHHlpRFEPTSILQTLSKYPITVFCSAPTVY-RMLVQNDITSYK--FKSLKHCVSAGEPITPDVTEKWRNKTGLD 408
Cdd:PRK13383 242 GGTVLTHR--HFDAEAALAQASLHRADAFTAVPVVLaRILELPPRVRARnpLPQLRVVMSSGDRLDPTLGQRFMDTYGDI 319
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217306889 409 IYEGYGQTET-VLICGNFKGMKIKPGSMGKPSPAFDVKIVDVNGNVLPPGQEGDIGIQVLPNRpfglfTHYVDNPSKtaS 487
Cdd:PRK13383 320 LYNGYGSTEVgIGALATPADLRDAPETVGKPVAGCPVRILDRNNRPVGPRVTGRIFVGGELAG-----TRYTDGGGK--A 392
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217306889 488 TLRGnFYITGDRGYMDKDGYFWFVARADDVILSSGYRIGPFEVENALNEHPSVAESAVVSSPDPIRGEVVKAFVVLNPDy 567
Cdd:PRK13383 393 VVDG-MTSTGDMGYLDNAGRLFIVGREDDMIISGGENVYPRAVENALAAHPAVADNAVIGVPDERFGHRLAAFVVLHPG- 470
|
250 260 270
....*....|....*....|....*....|..
gi 2217306889 568 KSHDQEQlikeIQEHVKKTTAPYKYPRKVGIL 599
Cdd:PRK13383 471 SGVDAAQ----LRDYLKDRVSRFEQPRDINIV 498
|
|
| LC_FACS_bac |
cd05932 |
Bacterial long-chain fatty acid CoA synthetase (LC-FACS), including Marinobacter ... |
89-611 |
1.58e-22 |
|
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: 101.39 E-value: 1.58e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217306889 89 NGEEMRWSFEELGSLSRKFANILsEACSLQRGDRVILILPRVPEWWLANVACLRTGTVLIPGTTQLTQKDILYRLQSSKA 168
Cdd:cd05932 1 GGQVVEFTWGEVADKARRLAAAL-RALGLEPGSKIALISKNCAEWFITDLAIWMAGHISVPLYPTLNPDTIRYVLEHSES 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217306889 169 NCIIT-----NDVLAPAV-DAVASKCENLHSKLivseNSREGWGNLKElmkvflCHPgwstvarswltatstslvqails 242
Cdd:cd05932 80 KALFVgklddWKAMAPGVpEGLISISLPPPSAA----NCQYQWDDLIA------QHP----------------------- 126
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217306889 243 lLSSWDYRHASDshtcvktkhnEIMAIFFTSGTSGYPKMTAHTHSSFGLGLSvNGRFWLDLTPSDVMWntSDTGWAKSAW 322
Cdd:cd05932 127 -PLEERPTRFPE----------QLATLIYTSGTTGQPKGVMLTFGSFAWAAQ-AGIEHIGTEENDRML--SYLPLAHVTE 192
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217306889 323 SS-VFSPWIQGACV--FTHHLPRFeptsiLQTLSKYPITVFCSAP---TVYRMLVQNDITSYKFKSL----------KHC 386
Cdd:cd05932 193 RVfVEGGSLYGGVLvaFAESLDTF-----VEDVQRARPTLFFSVPrlwTKFQQGVQDKIPQQKLNLLlkipvvnslvKRK 267
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217306889 387 VSAG-------------EPITPDVTEkWRNKTGLDIYEGYGQTETVLICGNFKGMKIKPGSMGKPSPAFDVKIvdvngnv 453
Cdd:cd05932 268 VLKGlgldqcrlagcgsAPVPPALLE-WYRSLGLNILEAYGMTENFAYSHLNYPGRDKIGTVGNAGPGVEVRI------- 339
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217306889 454 lppGQEGDIGIqvlpnRPFGLFTHYVDNPSKTASTLRGN-FYITGDRGYMDKDGYFWFVARADDVILSS-GYRIGPFEVE 531
Cdd:cd05932 340 ---SEDGEILV-----RSPALMMGYYKDPEATAEAFTADgFLRTGDKGELDADGNLTITGRVKDIFKTSkGKYVAPAPIE 411
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217306889 532 NALNEHPSVAESAVVSS--PDPIRGEVVKAFVVLNPDykSHDQEQLIKEIQEHVKKTTAPY-KYPRKVGILIITNIcsvl 608
Cdd:cd05932 412 NKLAEHDRVEMVCVIGSglPAPLALVVLSEEARLRAD--AFARAELEASLRAHLARVNSTLdSHEQLAGIVVVKDP---- 485
|
...
gi 2217306889 609 WTI 611
Cdd:cd05932 486 WSI 488
|
|
| A_NRPS_CmdD_like |
cd17652 |
similar to adenylation domain of chondramide synthase cmdD; This family of the adenylation (A) ... |
257-599 |
1.86e-22 |
|
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: 100.40 E-value: 1.86e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217306889 257 TCVKTKHNEIMAIFFTSGTSGYPKMTAHTHSSFGlGLSVNGRFWLDLTPSDVMWNTSDTGWAKSAWSsVFSPWIQGACVf 336
Cdd:cd17652 86 ALLLTTPDNLAYVIYTSGSTGRPKGVVVTHRGLA-NLAAAQIAAFDVGPGSRVLQFASPSFDASVWE-LLMALLAGATL- 162
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217306889 337 thHLPRFEPTS----ILQTLSKYPITVFCSAPTVYRMLVQNDITSykfksLKHCVSAGEPITPDVTEKWrnKTGLDIYEG 412
Cdd:cd17652 163 --VLAPAEELLpgepLADLLREHRITHVTLPPAALAALPPDDLPD-----LRTLVVAGEACPAELVDRW--APGRRMINA 233
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217306889 413 YGQTETVL---ICGNFKGMKIKPgsMGKPSPAFDVKIVDVNGNVLPPGQEGDI---GIqvlpnrpfGLFTHYVDNPSKTA 486
Cdd:cd17652 234 YGPTETTVcatMAGPLPGGGVPP--IGRPVPGTRVYVLDARLRPVPPGVPGELyiaGA--------GLARGYLNRPGLTA 303
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217306889 487 --------STLRGNFYITGDRGYMDKDGYFWFVARADDVILSSGYRIGPFEVENALNEHPSVAESAVVSSPDPIRGEVVK 558
Cdd:cd17652 304 erfvadpfGAPGSRMYRTGDLARWRADGQLEFLGRADDQVKIRGFRIELGEVEAALTEHPGVAEAVVVVRDDRPGDKRLV 383
|
330 340 350 360
....*....|....*....|....*....|....*....|.
gi 2217306889 559 AFVVLNPDyKSHDQEQLikeiQEHVKKTTAPYKYPRKVGIL 599
Cdd:cd17652 384 AYVVPAPG-AAPTAAEL----RAHLAERLPGYMVPAAFVVL 419
|
|
| PRK07638 |
PRK07638 |
acyl-CoA synthetase; Validated |
271-595 |
2.06e-22 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236071 [Multi-domain] Cd Length: 487 Bit Score: 101.01 E-value: 2.06e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217306889 271 FTSGTSGYPKMTAHTHSSfglglsvngrfWL---DLTPSDV-MWNTSDTGWAKSAWSSVF-----SPWIQGACVftHHLP 341
Cdd:PRK07638 150 FTSGSTGKPKAFLRAQQS-----------WLhsfDCNVHDFhMKREDSVLIAGTLVHSLFlygaiSTLYVGQTV--HLMR 216
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217306889 342 RFEPTSILQTLSKYPITVFCSAPTVYRMLVQndITSYKFKSLKhCVSAGEPITPDVTEKWRNK-TGLDIYEGYGQTE--- 417
Cdd:PRK07638 217 KFIPNQVLDKLETENISVMYTVPTMLESLYK--ENRVIENKMK-IISSGAKWEAEAKEKIKNIfPYAKLYEFYGASElsf 293
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217306889 418 -TVLICGNFKgmkIKPGSMGKPSPAFDVKIVDVNGNVLPPGQEGDIGIqvlpNRPFgLFTHYVdNPSKTASTLRGNFYIT 496
Cdd:PRK07638 294 vTALVDEESE---RRPNSVGRPFHNVQVRICNEAGEEVQKGEIGTVYV----KSPQ-FFMGYI-IGGVLARELNADGWMT 364
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217306889 497 -GDRGYMDKDGYFWFVARADDVILSSGYRIGPFEVENALNEHPSVAESAVVSSPDPIRGEVVKAFVvlnpdykshDQEQL 575
Cdd:PRK07638 365 vRDVGYEDEEGFIYIVGREKNMILFGGINIFPEEIESVLHEHPAVDEIVVIGVPDSYWGEKPVAII---------KGSAT 435
|
330 340
....*....|....*....|
gi 2217306889 576 IKEIQEHVKKTTAPYKYPRK 595
Cdd:PRK07638 436 KQQLKSFCLQRLSSFKIPKE 455
|
|
| LC_FACS_like |
cd17640 |
Long-chain fatty acid CoA synthetase; This family includes long-chain fatty acid (C12-C20) CoA ... |
249-546 |
2.43e-22 |
|
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: 100.51 E-value: 2.43e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217306889 249 YRHASDSHTCVKTKHNEIMAIFFTSGTSGYPKMTAHTHSSF---------GLGLSVNGRFwLDLTPSdvmWNTSDtgwaK 319
Cdd:cd17640 73 LNHSESVALVVENDSDDLATIIYTSGTTGNPKGVMLTHANLlhqirslsdIVPPQPGDRF-LSILPI---WHSYE----R 144
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217306889 320 SAWSSVFSpwiQG-ACVFThhlprfEPTSILQTLSKYPITVFCSAPTVYRMLVQNDITSYKFKS---------------L 383
Cdd:cd17640 145 SAEYFIFA---CGcSQAYT------SIRTLKDDLKRVKPHYIVSVPRLWESLYSGIQKQVSKSSpikqflflfflsggiF 215
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217306889 384 KHCVSAGEPITPDVtEKWRNKTGLDIYEGYGQTET--VLICGNFKGMKIkpGSMGKPSPAFDVKIVDVNGN-VLPPGQEG 460
Cdd:cd17640 216 KFGISGGGALPPHV-DTFFEAIGIEVLNGYGLTETspVVSARRLKCNVR--GSVGRPLPGTEIKIVDPEGNvVLPPGEKG 292
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217306889 461 DI---GIQVLPNrpfglfthYVDNPSKTASTLRGN-FYITGDRGYMDKDGYFWFVARADDVI-LSSGYRIGPFEVENALN 535
Cdd:cd17640 293 IVwvrGPQVMKG--------YYKNPEATSKVLDSDgWFNTGDLGWLTCGGELVLTGRAKDTIvLSNGENVEPQPIEEALM 364
|
330
....*....|.
gi 2217306889 536 EHPSVAESAVV 546
Cdd:cd17640 365 RSPFIEQIMVV 375
|
|
| LC_FACS_bac1 |
cd17641 |
bacterial long-chain fatty acid CoA synthetase; The members of this family are bacterial ... |
95-565 |
1.28e-20 |
|
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: 95.95 E-value: 1.28e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217306889 95 WSFEELGSLSRKFANILSeACSLQRGDRVILILPRVPEWWLANVACLRTGTVLIPGTTQLTQKDILYRLQSSKANCIITN 174
Cdd:cd17641 12 FTWADYADRVRAFALGLL-ALGVGRGDVVAILGDNRPEWVWAELAAQAIGALSLGIYQDSMAEEVAYLLNYTGARVVIAE 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217306889 175 DvlAPAVDavaskcenlhsKLIvsensrEGWGNLKELMKVFLCHP-GWSTVARSWLTAtstslVQAILSLLSSWDYRHAS 253
Cdd:cd17641 91 D--EEQVD-----------KLL------EIADRIPSVRYVIYCDPrGMRKYDDPRLIS-----FEDVVALGRALDRRDPG 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217306889 254 DSHTCVKTKHNEIMAIF-FTSGTSGYPKMTAHTHSSFgLGLSVNGRFWLDLTPSDVMWNTSDTGWAKSAWSSVFSPWIQG 332
Cdd:cd17641 147 LYEREVAAGKGEDVAVLcTTSGTTGKPKLAMLSHGNF-LGHCAAYLAADPLGPGDEYVSVLPLPWIGEQMYSVGQALVCG 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217306889 333 ACVfthHLPRfEPTSILQTLSKYPITVFCSAPTVYRMLVQN------DITSYK--------------------------- 379
Cdd:cd17641 226 FIV---NFPE-EPETMMEDLREIGPTFVLLPPRVWEGIAADvrarmmDATPFKrfmfelgmklglraldrgkrgrpvslw 301
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217306889 380 ---------------------FKSLKHCVSAGEPITPDVTEKWRnKTGLDIYEGYGQTETVLICGNFKGMKIKPGSMGKP 438
Cdd:cd17641 302 lrlaswladallfrplrdrlgFSRLRSAATGGAALGPDTFRFFH-AIGVPLKQLYGQTELAGAYTVHRDGDVDPDTVGVP 380
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217306889 439 SPAFDVKIVDVnGNVLPPGQegdigiqvlpnrpfGLFTHYVDNPSKTASTL-RGNFYITGDRGYMDKDGYFWFVARADDV 517
Cdd:cd17641 381 FPGTEVRIDEV-GEILVRSP--------------GVFVGYYKNPEATAEDFdEDGWLHTGDAGYFKENGHLVVIDRAKDV 445
|
490 500 510 520
....*....|....*....|....*....|....*....|....*....
gi 2217306889 518 -ILSSGYRIGPFEVENALNEHPSVAESAVVSSPDPIrgevVKAFVVLNP 565
Cdd:cd17641 446 gTTSDGTRFSPQFIENKLKFSPYIAEAVVLGAGRPY----LTAFICIDY 490
|
|
| PRK12467 |
PRK12467 |
peptide synthase; Provisional |
269-593 |
1.75e-20 |
|
peptide synthase; Provisional
Pssm-ID: 237108 [Multi-domain] Cd Length: 3956 Bit Score: 96.77 E-value: 1.75e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217306889 269 IFFTSGTSGYPKMTAHTHSSFGLGLSVNGRfWLDLTPSDVMWNTSDTGWAKSAWSsVFSPWIQGACVftHHLPR---FEP 345
Cdd:PRK12467 661 VIYTSGSTGQPKGVAISHGALANYVCVIAE-RLQLAADDSMLMVSTFAFDLGVTE-LFGALASGATL--HLLPPdcaRDA 736
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217306889 346 TSILQTLSKYPITVFCSAPTVYRMLVQnDITSYKFKSLKHCVSAGEPITPDVTEKWRNKT-GLDIYEGYGQTETVLICGN 424
Cdd:PRK12467 737 EAFAALMADQGVTVLKIVPSHLQALLQ-ASRVALPRPQRALVCGGEALQVDLLARVRALGpGARLINHYGPTETTVGVST 815
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217306889 425 FK----GMKIKPGSMGKPSPAFDVKIVDVNGNVLPPGQEGD--IGIQVLPN----RPFGLFTHYVDNPSKTAStlrGNFY 494
Cdd:PRK12467 816 YElsdeERDFGNVPIGQPLANLGLYILDHYLNPVPVGVVGElyIGGAGLARgyhrRPALTAERFVPDPFGADG---GRLY 892
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217306889 495 ITGDRGYMDKDGYFWFVARADDVILSSGYRIGPFEVENALNEHPSVAESAVVSSPDPIRGEVVkAFVVlnPDYKSHDQEQ 574
Cdd:PRK12467 893 RTGDLARYRADGVIEYLGRMDHQVKIRGFRIELGEIEARLLAQPGVREAVVLAQPGDAGLQLV-AYLV--PAAVADGAEH 969
|
330 340
....*....|....*....|.
gi 2217306889 575 LIK--EIQEHVKKTTAPYKYP 593
Cdd:PRK12467 970 QATrdELKAQLRQVLPDYMVP 990
|
|
| PRK13388 |
PRK13388 |
acyl-CoA synthetase; Provisional |
243-566 |
1.87e-20 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 237374 [Multi-domain] Cd Length: 540 Bit Score: 95.09 E-value: 1.87e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217306889 243 LLSSWDYRHASDSHTCVkTKHNEIMA-----IFFTSGTSGYPKMTAHTHSSFG-LGLSVNGRFwlDLTPSDVMW------ 310
Cdd:PRK13388 125 DVDTPAYAELVAAAGAL-TPHREVDAmdpfmLIFTSGTTGAPKAVRCSHGRLAfAGRALTERF--GLTRDDVCYvsmplf 201
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217306889 311 --NTSDTGWAKSAwssvfspwIQGACVFTHhlPRFEPTSILQTLSKYPITVF--CSAPTVYRMLV-------QNDITsyk 379
Cdd:PRK13388 202 hsNAVMAGWAPAV--------ASGAAVALP--AKFSASGFLDDVRRYGATYFnyVGKPLAYILATperpddaDNPLR--- 268
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217306889 380 fkslkhcVSAGEPITPDVTEKWRNKTGLDIYEGYGQTETVLICGNFKGMKikPGSMGKPSPafDVKIVDV---------- 449
Cdd:PRK13388 269 -------VAFGNEASPRDIAEFSRRFGCQVEDGYGSSEGAVIVVREPGTP--PGSIGRGAP--GVAIYNPetltecavar 337
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217306889 450 ---NGNVLPPgqegDIGIQVLPNRP-FGLFTHYVDNPSKTASTLRGNFYITGDRGYMDKDGYFWFVARADDVILSSGYRI 525
Cdd:PRK13388 338 fdaHGALLNA----DEAIGELVNTAgAGFFEGYYNNPEATAERMRHGMYWSGDLAYRDADGWIYFAGRTADWMRVDGENL 413
|
330 340 350 360
....*....|....*....|....*....|....*....|.
gi 2217306889 526 GPFEVENALNEHPSVAESAVVSSPDPIRGEVVKAFVVLNPD 566
Cdd:PRK13388 414 SAAPIERILLRHPAINRVAVYAVPDERVGDQVMAALVLRDG 454
|
|
| AMP-binding_C |
pfam13193 |
AMP-binding enzyme C-terminal domain; This is a small domain that is found C terminal to ... |
529-596 |
2.24e-20 |
|
AMP-binding enzyme C-terminal domain; This is a small domain that is found C terminal to pfam00501. It has a central beta sheet core that is flanked by alpha helices.
Pssm-ID: 463804 [Multi-domain] Cd Length: 76 Bit Score: 85.29 E-value: 2.24e-20
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2217306889 529 EVENALNEHPSVAESAVVSSPDPIRGEVVKAFVVLNPDYkshdqEQLIKEIQEHVKKTTAPYKYPRKV 596
Cdd:pfam13193 1 EVESALVSHPAVAEAAVVGVPDELKGEAPVAFVVLKPGV-----ELLEEELVAHVREELGPYAVPKEV 63
|
|
| PRK05620 |
PRK05620 |
long-chain fatty-acid--CoA ligase; |
96-589 |
3.46e-20 |
|
long-chain fatty-acid--CoA ligase;
Pssm-ID: 180167 [Multi-domain] Cd Length: 576 Bit Score: 94.46 E-value: 3.46e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217306889 96 SFEELGSLSRKFANILSEACSLQRGDRVILILPRVPEWW--LANVACLrtGTVLIPGTTQLTQKDILYRLQSSKANCIIT 173
Cdd:PRK05620 40 TFAAIGARAAALAHALHDELGITGDQRVGSMMYNCAEHLevLFAVACM--GAVFNPLNKQLMNDQIVHIINHAEDEVIVA 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217306889 174 NDVLAPAVDAVASKCENLHSKLIVSENSregwgnlkelmkvflchpgwSTVARSwltatstslvqAILSLLSSWDYRHAS 253
Cdd:PRK05620 118 DPRLAEQLGEILKECPCVRAVVFIGPSD--------------------ADSAAA-----------HMPEGIKVYSYEALL 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217306889 254 DSHTCV----KTKHNEIMAIFFTSGTSGYPKMTAHTHSSFGLGLsvngrfwLDLTPSDVMWNTSDTGWAKS-------AW 322
Cdd:PRK05620 167 DGRSTVydwpELDETTAAAICYSTGTTGAPKGVVYSHRSLYLQS-------LSLRTTDSLAVTHGESFLCCvpiyhvlSW 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217306889 323 SSVFSPWIQGA-CVFTHHlpRFEPTSILQTLSKYPITVFCSAPTVY-RMLVQNDITSYKFKSLKHCVSAGEPITPDVTEK 400
Cdd:PRK05620 240 GVPLAAFMSGTpLVFPGP--DLSAPTLAKIIATAMPRVAHGVPTLWiQLMVHYLKNPPERMSLQEIYVGGSAVPPILIKA 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217306889 401 WRNKTGLDIYEGYGQTETVLIcgnfkGMKIKPG-------------SMGKPSPAFDVKIVDvNGNVLPPGQEGDIGIQVL 467
Cdd:PRK05620 318 WEERYGVDVVHVWGMTETSPV-----GTVARPPsgvsgearwayrvSQGRFPASLEYRIVN-DGQVMESTDRNEGEIQVR 391
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217306889 468 PNRpfgLFTHYVDNPSKT----ASTLRGN-------------FYITGDRGYMDKDGYFWFVARADDVILSSGYRIGPFEV 530
Cdd:PRK05620 392 GNW---VTASYYHSPTEEgggaASTFRGEdvedandrftadgWLRTGDVGSVTRDGFLTIHDRARDVIRSGGEWIYSAQL 468
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2217306889 531 ENALNEHPSVAESAVVSSPDPIRGEVVKAFVVLNPDYKSHDQ--EQLIKEIQEHVKKTTAP 589
Cdd:PRK05620 469 ENYIMAAPEVVECAVIGYPDDKWGERPLAVTVLAPGIEPTREtaERLRDQLRDRLPNWMLP 529
|
|
| A_NRPS_TubE_like |
cd05906 |
The adenylation domain (A domain) of a family of nonribosomal peptide synthetases (NRPSs) ... |
86-583 |
3.09e-19 |
|
The adenylation domain (A domain) of a family of nonribosomal peptide synthetases (NRPSs) synthesizing toxins and antitumor agents; The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino)-acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. This family includes NRPSs that synthesize toxins and antitumor agents; for example, TubE for Tubulysine, CrpA for cryptophycin, TdiA for terrequinone A, KtzG for kutzneride, and Vlm1/Vlm2 for Valinomycin. Nonribosomal peptide synthetases are large multifunctional enzymes which synthesize many therapeutically useful peptides. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and, in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.
Pssm-ID: 341232 [Multi-domain] Cd Length: 540 Bit Score: 91.57 E-value: 3.09e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217306889 86 INRNGEEMRWSFEELGSLSRKFANILSEAcSLQRGDRVILILPR----VPEWWlanvACLRTGTVLIPGTTQLTqkdilY 161
Cdd:cd05906 31 IDADGSEEFQSYQDLLEDARRLAAGLRQL-GLRPGDSVILQFDDnedfIPAFW----ACVLAGFVPAPLTVPPT-----Y 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217306889 162 RLQSSKAN------------CIITNDVLAPAVDAVASKCENLHSKLIVSENSREGWGNlkelmkvflcHPgwstvarsWL 229
Cdd:cd05906 101 DEPNARLRklrhiwqllgspVVLTDAELVAEFAGLETLSGLPGIRVLSIEELLDTAAD----------HD--------LP 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217306889 230 TATSTSLVqailsllsswdyrhasdshtcvktkhneimAIFFTSGTSGYPKMTAHTHSSF---GLGLSVNGRFwldlTPS 306
Cdd:cd05906 163 QSRPDDLA------------------------------LLMLTSGSTGFPKAVPLTHRNIlarSAGKIQHNGL----TPQ 208
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217306889 307 DVMWNtsdtgwaksawssvfspWIQ----GACVFTHHLPRF---------------EPTSILQTLSKYPITV-FcsAPT- 365
Cdd:cd05906 209 DVFLN-----------------WVPldhvGGLVELHLRAVYlgcqqvhvpteeilaDPLRWLDLIDRYRVTItW--APNf 269
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217306889 366 VYRMLVQ----NDITSYKFKSLKHCVSAGEPITPDVTEKWRN---KTGLD---IYEGYGQTET---VLICGNFKGMKIKP 432
Cdd:cd05906 270 AFALLNDlleeIEDGTWDLSSLRYLVNAGEAVVAKTIRRLLRllePYGLPpdaIRPAFGMTETcsgVIYSRSFPTYDHSQ 349
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217306889 433 G----SMGKPSPAFDVKIVDVNGNVLPPGQEGDIGIQVLPnrpfgLFTHYVDNPSKTASTLR-GNFYITGDRGYMDkDGY 507
Cdd:cd05906 350 AlefvSLGRPIPGVSMRIVDDEGQLLPEGEVGRLQVRGPV-----VTKGYYNNPEANAEAFTeDGWFRTGDLGFLD-NGN 423
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2217306889 508 FWFVARADDVILSSGYRIGPFEVENALNEHPSVAES--AVVSSPDPIRGEVVKAfVVLNPDYKSHDQ-EQLIKEIQEHV 583
Cdd:cd05906 424 LTITGRTKDTIIVNGVNYYSHEIEAAVEEVPGVEPSftAAFAVRDPGAETEELA-IFFVPEYDLQDAlSETLRAIRSVV 501
|
|
| A_NRPS_ApnA-like |
cd17644 |
similar to adenylation domain of anabaenopeptin synthetase (ApnA); This family of the ... |
261-593 |
3.86e-19 |
|
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: 90.57 E-value: 3.86e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217306889 261 TKHNEIMAIFFTSGTSGYPKMTAHTHSS---FGLGLSVNgrfwLDLTPSDVMWNTSDTGWAKSAwSSVFSPWIQGAC-VF 336
Cdd:cd17644 103 TQPENLAYVIYTSGSTGKPKGVMIEHQSlvnLSHGLIKE----YGITSSDRVLQFASIAFDVAA-EEIYVTLLSGATlVL 177
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217306889 337 THHLPRFEPTSILQTLSKYPITVFCSAPTVYRMLV----QNDITSykFKSLKHCVSAGEPITPDVTEKWRNKTGLDI--Y 410
Cdd:cd17644 178 RPEEMRSSLEDFVQYIQQWQLTVLSLPPAYWHLLVlellLSTIDL--PSSLRLVIVGGEAVQPELVRQWQKNVGNFIqlI 255
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217306889 411 EGYGQTETVL--ICGNFK---GMKIKPGSMGKPSPAFDVKIVDVNGNVLPPGQEGDIGIQVLpnrpfGLFTHYVDNPSKT 485
Cdd:cd17644 256 NVYGPTEATIaaTVCRLTqltERNITSVPIGRPIANTQVYILDENLQPVPVGVPGELHIGGV-----GLARGYLNRPELT 330
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217306889 486 ASTLRGN---------FYITGDRGYMDKDGYFWFVARADDVILSSGYRIGPFEVENALNEHPSVAESAVVSSPDPIRGEV 556
Cdd:cd17644 331 AEKFISHpfnsseserLYKTGDLARYLPDGNIEYLGRIDNQVKIRGFRIELGEIEAVLSQHNDVKTAVVIVREDQPGNKR 410
|
330 340 350
....*....|....*....|....*....|....*..
gi 2217306889 557 VKAFVVlnPDYkshDQEQLIKEIQEHVKKTTAPYKYP 593
Cdd:cd17644 411 LVAYIV--PHY---EESPSTVELRQFLKAKLPDYMIP 442
|
|
| PRK04813 |
PRK04813 |
D-alanine--poly(phosphoribitol) ligase subunit DltA; |
350-595 |
8.02e-19 |
|
D-alanine--poly(phosphoribitol) ligase subunit DltA;
Pssm-ID: 235313 [Multi-domain] Cd Length: 503 Bit Score: 89.95 E-value: 8.02e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217306889 350 QTLSKYPITVFCSAPTVYRM-LVQNDITSYKFKSLKHCVSAGEPITPDVTEKWRNK-TGLDIYEGYGQTE-TVLIcgnfK 426
Cdd:PRK04813 228 ETLPQLPINVWVSTPSFADMcLLDPSFNEEHLPNLTHFLFCGEELPHKTAKKLLERfPSATIYNTYGPTEaTVAV----T 303
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217306889 427 GMKI--------KPGSMGKPSPAFDVKIVDVNGNVLPPGQEGDIGIqVLPNRPFGlfthYVDNPSKTAS---TLRGN-FY 494
Cdd:PRK04813 304 SIEItdemldqyKRLPIGYAKPDSPLLIIDEEGTKLPDGEQGEIVI-SGPSVSKG----YLNNPEKTAEaffTFDGQpAY 378
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217306889 495 ITGDRGYMDkDGYFWFVARADDVILSSGYRIGPFEVENALNEHPSVAESAVVsspdPI-RGEVVK---AFVVLNPdyksH 570
Cdd:PRK04813 379 HTGDAGYLE-DGLLFYQGRIDFQIKLNGYRIELEEIEQNLRQSSYVESAVVV----PYnKDHKVQyliAYVVPKE----E 449
|
250 260
....*....|....*....|....*...
gi 2217306889 571 DQE---QLIKEIQEHVKKTTAPYKYPRK 595
Cdd:PRK04813 450 DFErefELTKAIKKELKERLMEYMIPRK 477
|
|
| A_NRPS_SidN3_like |
cd05918 |
The adenylation (A) domain of siderophore-synthesizing nonribosomal peptide synthetases (NRPS); ... |
262-590 |
8.10e-19 |
|
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: 89.91 E-value: 8.10e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217306889 262 KHNEIMAIFFTSGTSGYPKMTAHTHSSFGLGLSVNGRFwLDLTPS-----------DVMWNtsdtgwaksawsSVFSPWI 330
Cdd:cd05918 104 SPSDAAYVIFTSGSTGKPKGVVIEHRALSTSALAHGRA-LGLTSEsrvlqfasytfDVSIL------------EIFTTLA 170
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217306889 331 QGACVFT-------HHLPRFeptsilqtLSKYPITVFCSAPTVYRMLVQNDITSykfksLKHCVSAGEPITPDVTEKWRN 403
Cdd:cd05918 171 AGGCLCIpseedrlNDLAGF--------INRLRVTWAFLTPSVARLLDPEDVPS-----LRTLVLGGEALTQSDVDTWAD 237
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217306889 404 KTGLdiYEGYGQTE-TVLICGNFKGMKIKPGSMGKPSPAFdVKIVDVNGN--VLPPGQEGDI---GIQVLPnrpfGlfth 477
Cdd:cd05918 238 RVRL--INAYGPAEcTIAATVSPVVPSTDPRNIGRPLGAT-CWVVDPDNHdrLVPIGAVGELlieGPILAR----G---- 306
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217306889 478 YVDNPSKTA--------------STLRGNFYITGDRGYMDKDGYFWFVARADDVILSSGYRIGPFEVENALNEHPSVAES 543
Cdd:cd05918 307 YLNDPEKTAaafiedpawlkqegSGRGRRLYRTGDLVRYNPDGSLEYVGRKDTQVKIRGQRVELGEIEHHLRQSLPGAKE 386
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2217306889 544 AVVSSPDPIRGEVVK---AFVVLNPDYKSHDQEQ------------LIKEIQEHVKKTTAPY 590
Cdd:cd05918 387 VVVEVVKPKDGSSSPqlvAFVVLDGSSSGSGDGDslflepsdefraLVAELRSKLRQRLPSY 448
|
|
| A_NRPS_Sfm_like |
cd12115 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including Saframycin A gene ... |
269-599 |
1.42e-18 |
|
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: 88.91 E-value: 1.42e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217306889 269 IFFTSGTSGYPKMTAHTHSSfglglSVNGRFWLDLT-PSD----VMWNTSdTGWAKSAWSsVFSPWIQGACVFT------ 337
Cdd:cd12115 110 VIYTSGSTGRPKGVAIEHRN-----AAAFLQWAAAAfSAEelagVLASTS-ICFDLSVFE-LFGPLATGGKVVLadnvla 182
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217306889 338 -HHLPRFEPTSILQTLskypitvfcsaPTVYRMLVQNDITSykfKSLKHCVSAGEPITPD-VTEKWRNKTGLDIYEGYGQ 415
Cdd:cd12115 183 lPDLPAAAEVTLINTV-----------PSAAAELLRHDALP---ASVRVVNLAGEPLPRDlVQRLYARLQVERVVNLYGP 248
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217306889 416 TE-----TVLICGnfKGMKIKPgSMGKPSPAFDVKIVDVNGNVLPPGQEGDI---GIqvlpnrpfGLFTHYVDNPSKTAS 487
Cdd:cd12115 249 SEdttysTVAPVP--PGASGEV-SIGRPLANTQAYVLDRALQPVPLGVPGELyigGA--------GVARGYLGRPGLTAE 317
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217306889 488 TLRGN-------FYITGDRGYMDKDGYFWFVARADDVILSSGYRIGPFEVENALNEHPSVAESAVVSSPDPIRGEVVKAF 560
Cdd:cd12115 318 RFLPDpfgpgarLYRTGDLVRWRPDGLLEFLGRADNQVKVRGFRIELGEIEAALRSIPGVREAVVVAIGDAAGERRLVAY 397
|
330 340 350
....*....|....*....|....*....|....*....
gi 2217306889 561 VVLNPDYKShdqeqLIKEIQEHVKKTTAPYKYPRKVGIL 599
Cdd:cd12115 398 IVAEPGAAG-----LVEDLRRHLGTRLPAYMVPSRFVRL 431
|
|
| PRK05857 |
PRK05857 |
fatty acid--CoA ligase; |
72-604 |
1.51e-18 |
|
fatty acid--CoA ligase;
Pssm-ID: 180293 [Multi-domain] Cd Length: 540 Bit Score: 89.30 E-value: 1.51e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217306889 72 EKAGKKPSNPAfwwINRNGEEMRWSFEELGSLSRKFANILsEACSLQRGDRVILILPRVPEWWLANVACLRTGTVlipgt 151
Cdd:PRK05857 22 EQARQQPEAIA---LRRCDGTSALRYRELVAEVGGLAADL-RAQSVSRGSRVLVISDNGPETYLSVLACAKLGAI----- 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217306889 152 tqltqkdilyrlqsskanCIITNDVLAPAvdAVASKCENLH-SKLIVSENSREGWGNLKELMKVFlchPGWSTVARSWLT 230
Cdd:PRK05857 93 ------------------AVMADGNLPIA--AIERFCQITDpAAALVAPGSKMASSAVPEALHSI---PVIAVDIAAVTR 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217306889 231 ATSTSLVQAILSllsswdyrhasdshTCVKTKHNEIMAIFFTSGTSGYPKMTAHTHSSFGLG---LSVNGRFWLDltpsd 307
Cdd:PRK05857 150 ESEHSLDAASLA--------------GNADQGSEDPLAMIFTSGTTGEPKAVLLANRTFFAVpdiLQKEGLNWVT----- 210
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217306889 308 vmWNTSDTGWAKSAWSSVFSPW------IQGACVFTHHlprfEPT-SILQTLSKYPITVFCSAPTVYRMLVQN-DITSYK 379
Cdd:PRK05857 211 --WVVGETTYSPLPATHIGGLWwiltclMHGGLCVTGG----ENTtSLLEILTTNAVATTCLVPTLLSKLVSElKSANAT 284
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217306889 380 FKSLKHCVSAG-EPITPDVteKWRNKTGLDIYEGYGQTET-----VLICGNFKGMKIKPGSMGKPSPAFDVKIVDVNG-- 451
Cdd:PRK05857 285 VPSLRLVGYGGsRAIAADV--RFIEATGVRTAQVYGLSETgctalCLPTDDGSIVKIEAGAVGRPYPGVDVYLAATDGig 362
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217306889 452 -NVLPPGQEGDIGIQVL--PNRPFGlfthYVDNPSKTASTLRGNFYITGDRGYMDKDGYFWFVARADDVILSSGYRIGPF 528
Cdd:PRK05857 363 pTAPGAGPSASFGTLWIksPANMLG----YWNNPERTAEVLIDGWVNTGDLLERREDGFFYIKGRSSEMIICGGVNIAPD 438
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2217306889 529 EVENALNEHPSVAESAVVSSPDPIRGEVVKAFVVLNPDYKSHDQEQLIKEIQEHVKKTTAPYKYPRKvgILIITNI 604
Cdd:PRK05857 439 EVDRIAEGVSGVREAACYEIPDEEFGALVGLAVVASAELDESAARALKHTIAARFRRESEPMARPST--IVIVTDI 512
|
|
| PRK12467 |
PRK12467 |
peptide synthase; Provisional |
269-599 |
1.77e-18 |
|
peptide synthase; Provisional
Pssm-ID: 237108 [Multi-domain] Cd Length: 3956 Bit Score: 90.61 E-value: 1.77e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217306889 269 IFFTSGTSGYPKMTAHTHSSFGLGLSVNGRFWlDLTPSDVMWNTSDTGWAKSAWSsVFSPWIQGACVFTHHLPRFEPTSI 348
Cdd:PRK12467 3242 VIYTSGSTGKPKGVGVRHGALANHLCWIAEAY-ELDANDRVLLFMSFSFDGAQER-FLWTLICGGCLVVRDNDLWDPEEL 3319
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217306889 349 LQTLSKYPITVFCSAPTVYRMLVQN-DITSYKfkSLKHCVSAGEPITPDVTEKWRNKTG-LDIYEGYGQTETVLI----- 421
Cdd:PRK12467 3320 WQAIHAHRISIACFPPAYLQQFAEDaGGADCA--SLDIYVFGGEAVPPAAFEQVKRKLKpRGLTNGYGPTEAVVTvtlwk 3397
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217306889 422 CGNFKGMKIKPGSMGKPSPAFDVKIVDVNGNVLPPGQEGDIGIQVLpnrpfGLFTHYVDNPSKTA--------STLRGNF 493
Cdd:PRK12467 3398 CGGDAVCEAPYAPIGRPVAGRSIYVLDGQLNPVPVGVAGELYIGGV-----GLARGYHQRPSLTAerfvadpfSGSGGRL 3472
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217306889 494 YITGDRGYMDKDGYFWFVARADDVILSSGYRIGPFEVENALNEHPSVAESAVVSSpDPIRGEVVKAFVVLNPdykshDQE 573
Cdd:PRK12467 3473 YRTGDLARYRADGVIEYLGRIDHQVKIRGFRIELGEIEARLLQHPSVREAVVLAR-DGAGGKQLVAYVVPAD-----PQG 3546
|
330 340
....*....|....*....|....*.
gi 2217306889 574 QLIKEIQEHVKKTTAPYKYPRKVGIL 599
Cdd:PRK12467 3547 DWRETLRDHLAASLPDYMVPAQLLVL 3572
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
233-593 |
1.98e-18 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 90.40 E-value: 1.98e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217306889 233 STSLVQAILSLLSSWDYRHASDSHTCVKTKHNEIMAIFFTSGTSGYPKMTAHTHSSFGLGLSVNGRFwLDLTPSDVMWNT 312
Cdd:PRK12316 3165 RLPLAQGVQVLDLDRGDENYAEANPAIRTMPENLAYVIYTSGSTGKPKGVGIRHSALSNHLCWMQQA-YGLGVGDRVLQF 3243
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217306889 313 SDTGWAKSAWSsVFSPWIQGACVFTHHLPRF-EPTSILQTLSKYPITVFCSAPTVYRMLVQnDITSYKFKSLKHCVSAGE 391
Cdd:PRK12316 3244 TTFSFDVFVEE-LFWPLMSGARVVLAGPEDWrDPALLVELINSEGVDVLHAYPSMLQAFLE-EEDAHRCTSLKRIVCGGE 3321
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217306889 392 PITPDVTEKWrnKTGLDIYEGYGQTETVLICGNFKGMKIKPGS--MGKPSPAFDVKIVDVNGNVLPPGQEGD--IGIQVL 467
Cdd:PRK12316 3322 ALPADLQQQV--FAGLPLYNLYGPTEATITVTHWQCVEEGKDAvpIGRPIANRACYILDGSLEPVPVGALGElyLGGEGL 3399
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217306889 468 P----NRPFGLFTHYVDNPSKTASTLrgnfYITGDRGYMDKDGYFWFVARADDVILSSGYRIGPFEVENALNEHPSVAES 543
Cdd:PRK12316 3400 ArgyhNRPGLTAERFVPDPFVPGERL----YRTGDLARYRADGVIEYIGRVDHQVKIRGFRIELGEIEARLLEHPWVREA 3475
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|
gi 2217306889 544 AVVSspdpIRGEVVKAFVVLnpdykSHDQEQLIKEIQEHVKKTTAPYKYP 593
Cdd:PRK12316 3476 VVLA----VDGRQLVAYVVP-----EDEAGDLREALKAHLKASLPEYMVP 3516
|
|
| PRK08279 |
PRK08279 |
long-chain-acyl-CoA synthetase; Validated |
63-550 |
6.65e-18 |
|
long-chain-acyl-CoA synthetase; Validated
Pssm-ID: 236217 [Multi-domain] Cd Length: 600 Bit Score: 87.62 E-value: 6.65e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217306889 63 DVLDQWTDKekagkKPSNPAFwwinrNGEEMRWSFEELGSLSRKFANILSEAcSLQRGDRVILILPRVPEWWLANVACLR 142
Cdd:PRK08279 41 DVFEEAAAR-----HPDRPAL-----LFEDQSISYAELNARANRYAHWAAAR-GVGKGDVVALLMENRPEYLAAWLGLAK 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217306889 143 TGTV--LIpgTTQLTQKDILYRLQSSKANCIITNDVLAPAVDAVASkCENLHSKLIV----SENSREGWGNLKELMKVFl 216
Cdd:PRK08279 110 LGAVvaLL--NTQQRGAVLAHSLNLVDAKHLIVGEELVEAFEEARA-DLARPPRLWVaggdTLDDPEGYEDLAAAAAGA- 185
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217306889 217 chPGWSTVARSWLTATSTSLvqailsllsswdYrhasdshtcvktkhneimaiFFTSGTSGYPKMTAHTH-----SSFGL 291
Cdd:PRK08279 186 --PTTNPASRSGVTAKDTAF------------Y--------------------IYTSGTTGLPKAAVMSHmrwlkAMGGF 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217306889 292 GLSvngrfwLDLTPSDVMWNT----SDTGwAKSAWSSVFSPwiqGACV-----FThhLPRFEPTSIlqtlsKYPITVFCS 362
Cdd:PRK08279 232 GGL------LRLTPDDVLYCClplyHNTG-GTVAWSSVLAA---GATLalrrkFS--ASRFWDDVR-----RYRATAFQY 294
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217306889 363 APTVYRMLVQNDITSY-KFKSLKHCVSAGepITPDVTEKWRNKTGLD-IYEGYGQTE--TVLIcgNFKGmkiKPGSMGKp 438
Cdd:PRK08279 295 IGELCRYLLNQPPKPTdRDHRLRLMIGNG--LRPDIWDEFQQRFGIPrILEFYAASEgnVGFI--NVFN---FDGTVGR- 366
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217306889 439 SPAFDVK---IV-----------DVNGNVLP--PGQEGD-IGiQVLPNRPFglfTHYVDnPSKT-ASTLRGNF------Y 494
Cdd:PRK08279 367 VPLWLAHpyaIVkydvdtgepvrDADGRCIKvkPGEVGLlIG-RITDRGPF---DGYTD-PEASeKKILRDVFkkgdawF 441
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2217306889 495 ITGDRGYMDKDGYFWFVARADDVilssgYR-----IGPFEVENALNEHPSVAESAV--VSSPD 550
Cdd:PRK08279 442 NTGDLMRDDGFGHAQFVDRLGDT-----FRwkgenVATTEVENALSGFPGVEEAVVygVEVPG 499
|
|
| PRK07445 |
PRK07445 |
O-succinylbenzoic acid--CoA ligase; Reviewed |
413-595 |
6.11e-17 |
|
O-succinylbenzoic acid--CoA ligase; Reviewed
Pssm-ID: 236019 [Multi-domain] Cd Length: 452 Bit Score: 83.89 E-value: 6.11e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217306889 413 YGQTETV-LICgnfkgmKIKPG-------SMGKPSPAFDVKIVdvngnvlpPGQEGDIGIQVlPNRPFGLFTHYVDNPsk 484
Cdd:PRK07445 261 YGMTETAsQIA------TLKPDdflagnnSSGQVLPHAQITIP--------ANQTGNITIQA-QSLALGYYPQILDSQ-- 323
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217306889 485 tastlrgNFYITGDRGYMDKDGYFWFVARADDVILSSGYRIGPFEVENALNEHPSVAESAVVSSPDPIRGEVVKAFVVln 564
Cdd:PRK07445 324 -------GIFETDDLGYLDAQGYLHILGRNSQKIITGGENVYPAEVEAAILATGLVQDVCVLGLPDPHWGEVVTAIYV-- 394
|
170 180 190
....*....|....*....|....*....|.
gi 2217306889 565 PDYKSHDQEqlikEIQEHVKKTTAPYKYPRK 595
Cdd:PRK07445 395 PKDPSISLE----ELKTAIKDQLSPFKQPKH 421
|
|
| A_NRPS_LgrA-like |
cd17645 |
adenylation (A) domain of linear gramicidin synthetase (LgrA) and similar proteins; This ... |
252-593 |
7.83e-17 |
|
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: 83.37 E-value: 7.83e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217306889 252 ASDSHTCVKTKHNEIMA-IFFTSGTSGYPKMTAHTHSSFglglsVNGRFW----LDLTPSDVMWNTSDTGWAKSAWSsVF 326
Cdd:cd17645 91 LADSSAKILLTNPDDLAyVIYTSGSTGLPKGVMIEHHNL-----VNLCEWhrpyFGVTPADKSLVYASFSFDASAWE-IF 164
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217306889 327 SPWIQGACVftHHLP---RFEPTSILQTLSKYPITVFCSAPTVYRMLVQNDITSykfksLKHCVSAGepitpDVTEKWRN 403
Cdd:cd17645 165 PHLTAGAAL--HVVPserRLDLDALNDYFNQEGITISFLPTGAAEQFMQLDNQS-----LRVLLTGG-----DKLKKIER 232
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217306889 404 KtGLDIYEGYGQTETVLICGNFKGMKIKPG-SMGKPSPAFDVKIVDVNGNVLPPGQEGDIGIQvlpnrPFGLFTHYVDNP 482
Cdd:cd17645 233 K-GYKLVNNYGPTENTVVATSFEIDKPYANiPIGKPIDNTRVYILDEALQLQPIGVAGELCIA-----GEGLARGYLNRP 306
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217306889 483 SKTASTLRGN-------FYITGDRGYMDKDGYFWFVARADDVILSSGYRIGPFEVENALNEHPSVAESAVVSSPDPIRGE 555
Cdd:cd17645 307 ELTAEKFIVHpfvpgerMYRTGDLAKFLPDGNIEFLGRLDQQVKIRGYRIEPGEIEPFLMNHPLIELAAVLAKEDADGRK 386
|
330 340 350
....*....|....*....|....*....|....*...
gi 2217306889 556 VVKAFVVLnpdykshDQEQLIKEIQEHVKKTTAPYKYP 593
Cdd:cd17645 387 YLVAYVTA-------PEEIPHEELREWLKNDLPDYMIP 417
|
|
| entE |
PRK10946 |
(2,3-dihydroxybenzoyl)adenylate synthase; |
436-599 |
9.04e-17 |
|
(2,3-dihydroxybenzoyl)adenylate synthase;
Pssm-ID: 236803 [Multi-domain] Cd Length: 536 Bit Score: 83.50 E-value: 9.04e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217306889 436 GKP-SPAFDVKIVDVNGNVLPPGQEGdigiqVLPNR-PFgLFTHYVDNPSKTASTLRGN-FYITGDRGYMDKDGYFWFVA 512
Cdd:PRK10946 356 GRPmSPDDEVWVADADGNPLPQGEVG-----RLMTRgPY-TFRGYYKSPQHNASAFDANgFYCSGDLVSIDPDGYITVVG 429
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217306889 513 RADDVILSSGYRIGPFEVENALNEHPSVAESAVVSSPDPIRGEVVKAFVVLNPDYKS-----HDQEQLIkeiqehvkktt 587
Cdd:PRK10946 430 REKDQINRGGEKIAAEEIENLLLRHPAVIHAALVSMEDELMGEKSCAFLVVKEPLKAvqlrrFLREQGI----------- 498
|
170
....*....|..
gi 2217306889 588 APYKYPRKVGIL 599
Cdd:PRK10946 499 AEFKLPDRVECV 510
|
|
| PRK12467 |
PRK12467 |
peptide synthase; Provisional |
269-593 |
1.13e-16 |
|
peptide synthase; Provisional
Pssm-ID: 237108 [Multi-domain] Cd Length: 3956 Bit Score: 84.44 E-value: 1.13e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217306889 269 IFFTSGTSGYPKMTAHTHSSFgLGLSVNGRFWLDLTPSDVMWNTSDTGWAKSAWSsVFSPWIQGACV----FTHHLprfE 344
Cdd:PRK12467 1723 VIYTSGSTGRPKGAGNRHGAL-VNRLCATQEAYQLSAADVVLQFTSFAFDVSVWE-LFWPLINGARLviapPGAHR---D 1797
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217306889 345 PTSILQTLSKYPITVFCSAPTVYRMLVQNDITSYKFKSLKHCVSAGEPITPDVTEKWRNKTG-LDIYEGYGQTETVL--- 420
Cdd:PRK12467 1798 PEQLIQLIERQQVTTLHFVPSMLQQLLQMDEQVEHPLSLRRVVCGGEALEVEALRPWLERLPdTGLFNLYGPTETAVdvt 1877
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217306889 421 --IC--GNFKGMKIKPgsMGKPSPAFDVKIVDVNGNVLPPGQEGD--IGIQVLP----NRPFGLFTHYVDNPSktaSTLR 490
Cdd:PRK12467 1878 hwTCrrKDLEGRDSVP--IGQPIANLSTYILDASLNPVPIGVAGElyLGGVGLArgylNRPALTAERFVADPF---GTVG 1952
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217306889 491 GNFYITGDRGYMDKDGYFWFVARADDVILSSGYRIGPFEVENALNEHPSVAESAVVSSpDPIRGEVVKAFVV-LNPDYKS 569
Cdd:PRK12467 1953 SRLYRTGDLARYRADGVIEYLGRIDHQVKIRGFRIELGEIEARLREQGGVREAVVIAQ-DGANGKQLVAYVVpTDPGLVD 2031
|
330 340
....*....|....*....|....*.
gi 2217306889 570 HDQEQ--LIKEIQEHVKKTTAPYKYP 593
Cdd:PRK12467 2032 DDEAQvaLRAILKNHLKASLPEYMVP 2057
|
|
| A_NRPS_ACVS-like |
cd17648 |
N-(5-amino-5-carboxypentanoyl)-L-cysteinyl-D-valine synthase; This family contains ACV ... |
269-551 |
1.82e-16 |
|
N-(5-amino-5-carboxypentanoyl)-L-cysteinyl-D-valine synthase; This family contains ACV synthetase (ACVS, EC 6.3.2.26; also known as N-(5-amino-5-carboxypentanoyl)-L-cysteinyl-D-valine synthase or delta-(L-alpha-aminoadipyl)-L-cysteinyl-D-valine synthetase) is involved in medically important antibiotic biosynthesis. ACV synthetase is active in an early step in the penicillin G biosynthesis pathway which involves the formation of the tripeptide 6-(L-alpha-aminoadipyl)-L-cysteinyl-D-valine (ACV); each of the constituent amino acids of the tripeptide ACV are activated as aminoacyl-adenylates with peptide bonds formed through the participation of amino acid thioester intermediates. ACV is then cyclized by the action of isopenicillin N synthase.
Pssm-ID: 341303 [Multi-domain] Cd Length: 453 Bit Score: 82.45 E-value: 1.82e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217306889 269 IFFTSGTSGYPK--MTAHtHSSFGLGLSVNGRFWLDLTPSDVMWNTSdtgwaksawSSVFSPWIQGAC--VFTHH----L 340
Cdd:cd17648 99 AIYTSGTTGKPKgvLVEH-GSVVNLRTSLSERYFGRDNGDEAVLFFS---------NYVFDFFVEQMTlaLLNGQklvvP 168
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217306889 341 P---RFEPTSILQTLSKYPITVFCSAPTVyrmLVQNDITSykFKSLKHCVSAGEPITPDVTEKWRNKTGLDIYEGYGQTE 417
Cdd:cd17648 169 PdemRFDPDRFYAYINREKVTYLSGTPSV---LQQYDLAR--LPHLKRVDAAGEEFTAPVFEKLRSRFAGLIINAYGPTE 243
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217306889 418 TVL--ICGNFKGMKIKPGSMGKPSPAFDVKIVDVNGNVLPPGQEGDI---GIQVLP---NRPFGLFTHYVDNPSKTAS-T 488
Cdd:cd17648 244 TTVtnHKRFFPGDQRFDKSLGRPVRNTKCYVLNDAMKRVPVGAVGELylgGDGVARgylNRPELTAERFLPNPFQTEQeR 323
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2217306889 489 LRGNF---YITGDRGYMDKDGYFWFVARADDVILSSGYRIGPFEVENALNEHPSVAESAVVSSPDP 551
Cdd:cd17648 324 ARGRNarlYKTGDLVRWLPSGELEYLGRNDFQVKIRGQRIEPGEVEAALASYPGVRECAVVAKEDA 389
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
71-563 |
3.14e-16 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 83.08 E-value: 3.14e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217306889 71 KEKAGKKPSNPAFwwinRNGEEmRWSFEELGSLSRKFANILSEaCSLQRGDRVILILPRVPEWWLANVACLRTGTVLIPG 150
Cdd:PRK12316 518 EEQVERTPEAPAL----AFGEE-TLDYAELNRRANRLAHALIE-RGVGPDVLVGVAMERSIEMVVALLAILKAGGAYVPL 591
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217306889 151 TTQLTQKDILYRLQSSKANCIITNDVLAPAVDAVAskcenlhsklivsensregwgnlkELMKVFLCHPGwstvarSWLT 230
Cdd:PRK12316 592 DPEYPAERLAYMLEDSGVQLLLSQSHLGRKLPLAA------------------------GVQVLDLDRPA------AWLE 641
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217306889 231 ATST-SLVQAIlsllsswdyrhasdshtcvktkHNEIMA-IFFTSGTSGYPKMTAHTHSSFglglsVNGRFW----LDLT 304
Cdd:PRK12316 642 GYSEeNPGTEL----------------------NPENLAyVIYTSGSTGKPKGAGNRHRAL-----SNRLCWmqqaYGLG 694
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217306889 305 PSDVMWNTSDTGWAKSAWSsVFSPWIQGA-CVFTHHLPRFEPTSILQTLSKYPITVFCSAPTVYRMLVQN-DITSykFKS 382
Cdd:PRK12316 695 VGDTVLQKTPFSFDVSVWE-FFWPLMSGArLVVAAPGDHRDPAKLVELINREGVDTLHFVPSMLQAFLQDeDVAS--CTS 771
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217306889 383 LKHCVSAGEPITPDVTEK-WRNKTGLDIYEGYGQTETVLICGNFKGMKIKPGS--MGKPSPAFDVKIVDVNGNVLPPGQE 459
Cdd:PRK12316 772 LRRIVCSGEALPADAQEQvFAKLPQAGLYNLYGPTEAAIDVTHWTCVEEGGDSvpIGRPIANLACYILDANLEPVPVGVL 851
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217306889 460 GDIgiqVLPNRpfGLFTHYVDNPSKTASTLRGN-------FYITGDRGYMDKDGYFWFVARADDVILSSGYRIGPFEVEN 532
Cdd:PRK12316 852 GEL---YLAGR--GLARGYHGRPGLTAERFVPSpfvagerMYRTGDLARYRADGVIEYAGRIDHQVKLRGLRIELGEIEA 926
|
490 500 510
....*....|....*....|....*....|.
gi 2217306889 533 ALNEHPSVAESAVVSspdpIRGEVVKAFVVL 563
Cdd:PRK12316 927 RLLEHPWVREAAVLA----VDGKQLVGYVVL 953
|
|
| FACL_like_1 |
cd05910 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
261-546 |
4.03e-16 |
|
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: 81.35 E-value: 4.03e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217306889 261 TKHNEIMAIFFTSGTSGYPKMTAHTHSSFGLGLSVNgRFWLDLTPSDVMWntsdtgwAKSAWSSVFSPWIQGACV---FT 337
Cdd:cd05910 82 PKADEPAAILFTSGSTGTPKGVVYRHGTFAAQIDAL-RQLYGIRPGEVDL-------ATFPLFALFGPALGLTSVipdMD 153
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217306889 338 HHLP-RFEPTSILQTLSKYPITVFCSAPTVYRML----VQNDITsykFKSLKHCVSAGEPITPDVTEKWRN--KTGLDIY 410
Cdd:cd05910 154 PTRPaRADPQKLVGAIRQYGVSIVFGSPALLERVarycAQHGIT---LPSLRRVLSAGAPVPIALAARLRKmlSDEAEIL 230
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217306889 411 EGYGQTETVLICG-------NFKGMKIKPGS---MGKPSPAFDVKIVDVN---------GNVLPPGQEGDI---GIQVLP 468
Cdd:cd05910 231 TPYGATEALPVSSigsrellATTTAATSGGAgtcVGRPIPGVRVRIIEIDdepiaewddTLELPRGEIGEItvtGPTVTP 310
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217306889 469 NrpfglfthYVDNPSKTA----STLRGNF-YITGDRGYMDKDGYFWFVARADDVILSSGYRIGPFEVENALNEHPSVAES 543
Cdd:cd05910 311 T--------YVNRPVATAlakiDDNSEGFwHRMGDLGYLDDEGRLWFCGRKAHRVITTGGTLYTEPVERVFNTHPGVRRS 382
|
...
gi 2217306889 544 AVV 546
Cdd:cd05910 383 ALV 385
|
|
| PRK06018 |
PRK06018 |
putative acyl-CoA synthetase; Provisional |
268-575 |
4.31e-16 |
|
putative acyl-CoA synthetase; Provisional
Pssm-ID: 235673 [Multi-domain] Cd Length: 542 Bit Score: 81.72 E-value: 4.31e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217306889 268 AIFFTSGTSGYPKMTAHTHSSFGL-GLSVNGRFWLDLTPSDVMWNTSDTGWAkSAWSSVFSPWIQGACVFthhLP--RFE 344
Cdd:PRK06018 181 GMCYTSGTTGDPKGVLYSHRSNVLhALMANNGDALGTSAADTMLPVVPLFHA-NSWGIAFSAPSMGTKLV---MPgaKLD 256
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217306889 345 PTSILQTLSKYPITVFCSAPTVYRMLVQN-DITSYKFKSLKHCVSAGEPItPDVTEKWRNKTGLDIYEGYGQTETVLI-- 421
Cdd:PRK06018 257 GASVYELLDTEKVTFTAGVPTVWLMLLQYmEKEGLKLPHLKMVVCGGSAM-PRSMIKAFEDMGVEVRHAWGMTEMSPLgt 335
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217306889 422 CGNFKG----------MKIKPgSMGKPSPAFDVKIVDVNGNVLPpgQEGdigiqvlpnRPFGLFThyVDNPSKTASTLRG 491
Cdd:PRK06018 336 LAALKPpfsklpgdarLDVLQ-KQGYPPFGVEMKITDDAGKELP--WDG---------KTFGRLK--VRGPAVAAAYYRV 401
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217306889 492 N--------FYITGDRGYMDKDGYFWFVARADDVILSSGYRIGPFEVENALNEHPSVAESAVVSSPDPIRGEVVKAFVVL 563
Cdd:PRK06018 402 DgeildddgFFDTGDVATIDAYGYMRITDRSKDVIKSGGEWISSIDLENLAVGHPKVAEAAVIGVYHPKWDERPLLIVQL 481
|
330
....*....|..
gi 2217306889 564 NPDYKSHDQEQL 575
Cdd:PRK06018 482 KPGETATREEIL 493
|
|
| A_NRPS_TlmIV_like |
cd12114 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including ... |
94-575 |
4.57e-16 |
|
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: 81.16 E-value: 4.57e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217306889 94 RWSFEELGSLSRKFANILsEACSLQRGDRVILILPRVPEWWLANVACLRTGTVLIPGTTQLTQKDILYRLQSSKANCIIT 173
Cdd:cd12114 12 TLTYGELAERARRVAGAL-KAAGVRPGDLVAVTLPKGPEQVVAVLGILAAGAAYVPVDIDQPAARREAILADAGARLVLT 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217306889 174 NDVLAPAVDAVAskcenlhsklivsensregwgnlkelmkvflchpgwstvarswlTATSTSLVQAILSLLSSWDYRHAS 253
Cdd:cd12114 91 DGPDAQLDVAVF--------------------------------------------DVLILDLDALAAPAPPPPVDVAPD 126
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217306889 254 DshtcvktkhneiMA-IFFTSGTSGYPKMTAHTHSS-FGLGLSVNGRFwlDLTPSDVMWNTSDTGWAKSAWSsVFSPWIQ 331
Cdd:cd12114 127 D------------LAyVIFTSGSTGTPKGVMISHRAaLNTILDINRRF--AVGPDDRVLALSSLSFDLSVYD-IFGALSA 191
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217306889 332 GAC-VFTHHLPRFEPTSILQTLSKYPITVFCSAPTVYRMLV----QNDITSykfKSLKHCVSAGEPITPDVTEKWRNKT- 405
Cdd:cd12114 192 GATlVLPDEARRRDPAHWAELIERHGVTLWNSVPALLEMLLdvleAAQALL---PSLRLVLLSGDWIPLDLPARLRALAp 268
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217306889 406 GLDIYEGYGQTETVlICGNFkgMKIKPGSM-------GKPSPAFDVKIVDVNGNVLPPGQEGDI---GIqvlpnrpfGLF 475
Cdd:cd12114 269 DARLISLGGATEAS-IWSIY--HPIDEVPPdwrsipyGRPLANQRYRVLDPRGRDCPDWVPGELwigGR--------GVA 337
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217306889 476 THYVDNPSKTAS-----TLRGNFYITGDRGYMDKDGYFWFVARADDVILSSGYRIGPFEVENALNEHPSVAESAVVSSPD 550
Cdd:cd12114 338 LGYLGDPELTAArfvthPDGERLYRTGDLGRYRPDGTLEFLGRRDGQVKVRGYRIELGEIEAALQAHPGVARAVVVVLGD 417
|
490 500
....*....|....*....|....*
gi 2217306889 551 PiRGEVVKAFVVLNPDYKSHDQEQL 575
Cdd:cd12114 418 P-GGKRLAAFVVPDNDGTPIAPDAL 441
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
239-599 |
1.59e-15 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 80.77 E-value: 1.59e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217306889 239 AILSLLSSWDYRHASDSHTCVKTKHNEIMAIFFTSGTSGYPKMTAHTHSSFGLGLSVNGRFWlDLTPSDVMWNTSDTGWA 318
Cdd:PRK12316 2121 ARLPLDRDAEWADYPDTAPAVQLAGENLAYVIYTSGSTGLPKGVAVSHGALVAHCQAAGERY-ELSPADCELQFMSFSFD 2199
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217306889 319 KSAWSsVFSPWIQGACVFTHHLPRFEPTSILQTLSKYPITVFCSAPTVYRMLVQNDITSYKFKSLKHCVSAGEPITPDVT 398
Cdd:PRK12316 2200 GAHEQ-WFHPLLNGARVLIRDDELWDPEQLYDEMERHGVTILDFPPVYLQQLAEHAERDGRPPAVRVYCFGGEAVPAASL 2278
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217306889 399 EK-WRNKTGLDIYEGYGQTETVLICGNFKGMKIKPGS-----MGKPSPAFDVKIVDVNGNVLPPGQEGD--IGIQvlpnr 470
Cdd:PRK12316 2279 RLaWEALRPVYLFNGYGPTEAVVTPLLWKCRPQDPCGaayvpIGRALGNRRAYILDADLNLLAPGMAGElyLGGE----- 2353
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217306889 471 pfGLFTHYVDNPSKTA--------STLRGNFYITGDRGYMDKDGYFWFVARADDVILSSGYRIGPFEVENALNEHPSVAE 542
Cdd:PRK12316 2354 --GLARGYLNRPGLTAerfvpdpfSASGERLYRTGDLARYRADGVVEYLGRIDHQVKIRGFRIELGEIEARLQAHPAVRE 2431
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*..
gi 2217306889 543 SAVVSSpDPIRGEVVKAFVVlnPDyksHDQEQLIKEIQEHVKKTTAPYKYPRKVGIL 599
Cdd:PRK12316 2432 AVVVAQ-DGASGKQLVAYVV--PD---DAAEDLLAELRAWLAARLPAYMVPAHWVVL 2482
|
|
| A_NRPS_ProA |
cd17656 |
gramicidin S synthase 2, also known as ATP-dependent proline adenylase; This family of the ... |
251-595 |
2.23e-15 |
|
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: 79.06 E-value: 2.23e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217306889 251 HASDSHTCVKTKHNEIMAIFFTSGTSGYPKMTAHTHSSFGLGLSVNGRFWLDLTPSDVMWNTSDTgwAKSAWSSVFSPWI 330
Cdd:cd17656 115 QEDTSNIDYINNSDDLLYIIYTSGTTGKPKGVQLEHKNMVNLLHFEREKTNINFSDKVLQFATCS--FDVCYQEIFSTLL 192
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217306889 331 QGAcvfTHHLPRFEPTSILQTL----SKYPITVFcSAPTVYRMLVQNDITSYK--FKSLKHCVSAGEP--ITPDVTEKWR 402
Cdd:cd17656 193 SGG---TLYIIREETKRDVEQLfdlvKRHNIEVV-FLPVAFLKFIFSEREFINrfPTCVKHIITAGEQlvITNEFKEMLH 268
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217306889 403 NKtGLDIYEGYGQTETVLIcgnfKGMKIKPGS-------MGKPSPAFDVKIVDVNGNVLPPGQEGDIGIQVLpnrpfGLF 475
Cdd:cd17656 269 EH-NVHLHNHYGPSETHVV----TTYTINPEAeipelppIGKPISNTWIYILDQEQQLQPQGIVGELYISGA-----SVA 338
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217306889 476 THYVDNPSKTASTLRGN-------FYITGDRGYMDKDGYFWFVARADDVILSSGYRIGPFEVENALNEHPSVAESAVVSS 548
Cdd:cd17656 339 RGYLNRQELTAEKFFPDpfdpnerMYRTGDLARYLPDGNIEFLGRADHQVKIRGYRIELGEIEAQLLNHPGVSEAVVLDK 418
|
330 340 350 360
....*....|....*....|....*....|....*....|....*..
gi 2217306889 549 PDPIRGEVVKAFVVLnpdykshDQEQLIKEIQEHVKKTTAPYKYPRK 595
Cdd:cd17656 419 ADDKGEKYLCAYFVM-------EQELNISQLREYLAKQLPEYMIPSF 458
|
|
| LC-FACS_euk |
cd05927 |
Eukaryotic long-chain fatty acid CoA synthetase (LC-FACS); The members of this family are ... |
262-567 |
5.34e-15 |
|
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: 78.03 E-value: 5.34e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217306889 262 KHNEIMAIFFTSGTSGYPKMTAHTHSSFGLGLSVNGRFWLDLtpsdVMWNTSDTGWAKSAWSSVFSPWIQ------GACV 335
Cdd:cd05927 112 KPEDLATICYTSGTTGNPKGVMLTHGNIVSNVAGVFKILEIL----NKINPTDVYISYLPLAHIFERVVEalflyhGAKI 187
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217306889 336 -FTHHLPRfEPTSILQTLSkyPiTVFCSAPTVY-RML--VQNDI--------------TSYKFKSLKH------------ 385
Cdd:cd05927 188 gFYSGDIR-LLLDDIKALK--P-TVFPGVPRVLnRIYdkIFNKVqakgplkrklfnfaLNYKLAELRSgvvraspfwdkl 263
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217306889 386 ---------------CVSAGEPITPDVTEKWRNKTGLDIYEGYGQTETV-LICGNFKGMKIkPGSMGKPSPAFDVKIVDV 449
Cdd:cd05927 264 vfnkikqalggnvrlMLTGSAPLSPEVLEFLRVALGCPVLEGYGQTECTaGATLTLPGDTS-VGHVGGPLPCAEVKLVDV 342
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217306889 450 ---NGNVLPPGQEGDIGIqvlpnRPFGLFTHYVDNPSKTASTLRGN-FYITGDRGYMDKDGYFWFVARADDVI-LSSGYR 524
Cdd:cd05927 343 pemNYDAKDPNPRGEVCI-----RGPNVFSGYYKDPEKTAEALDEDgWLHTGDIGEWLPNGTLKIIDRKKNIFkLSQGEY 417
|
330 340 350 360
....*....|....*....|....*....|....*....|....*..
gi 2217306889 525 IGPFEVENALNEHPSVAESAVvsspdpiRGEVVKAF----VVLNPDY 567
Cdd:cd05927 418 VAPEKIENIYARSPFVAQIFV-------YGDSLKSFlvaiVVPDPDV 457
|
|
| ttLC_FACS_like |
cd05915 |
Fatty acyl-CoA synthetases similar to LC-FACS from Thermus thermophiles; This family includes ... |
267-596 |
1.32e-14 |
|
Fatty acyl-CoA synthetases similar to LC-FACS from Thermus thermophiles; This family includes fatty acyl-CoA synthetases that can activate medium-chain to long-chain fatty acids. They catalyze the ATP-dependent acylation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. Fatty acyl-CoA synthetases are responsible for fatty acid degradation as well as physiological regulation of cellular functions via the production of fatty acyl-CoA esters. The fatty acyl-CoA synthetase from Thermus thermophiles in this family has been shown to catalyze the long-chain fatty acid, myristoyl acid, while another member in this family, the AlkK protein identified in Pseudomonas oleovorans, targets medium chain fatty acids. This family also includes an uncharacterized subgroup of FACS.
Pssm-ID: 213283 [Multi-domain] Cd Length: 509 Bit Score: 76.70 E-value: 1.32e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217306889 267 MAIFFTSGTSGYPKMTAHTHSSFGLGLSVNGRF-WLDLTPSDVMWNTSDTgWAKSAWSSVFS-PWIQGACVFTHHLPRFE 344
Cdd:cd05915 156 CGMAYTTGTTGLPKGVVYSHRALVLHSLAASLVdGTALSEKDVVLPVVPM-FHVNAWCLPYAaTLVGAKQVLPGPRLDPA 234
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217306889 345 ptSILQTLSKYPITVFCSAPTVYRMLVQ-NDITSYKFKSLKHCVSAGEPiTPDVTEKWRNKTGLDIYEGYGQTETVLI-- 421
Cdd:cd05915 235 --SLVELFDGEGVTFTAGVPTVWLALADyLESTGHRLKTLRRLVVGGSA-APRSLIARFERMGVEVRQGYGLTETSPVvv 311
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217306889 422 ----------CGNFKGMKIK----------------PGSMGKPSPAFDVKIVDVNGNVLPPGqegdigiqvlpnrpfglf 475
Cdd:cd05915 312 qnfvkshlesLSEEEKLTLKaktglpiplvrlrvadEEGRPVPKDGKALGEVQLKGPWITGG------------------ 373
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217306889 476 tHYVDNPSKTASTLRGNFYITGDRGYMDKDGYFWFVARADDVILSSGYRIGPFEVENALNEHPSVAESAVVSSPDPIRGE 555
Cdd:cd05915 374 -YYGNEEATRSALTPDGFFRTGDIAVWDEEGYVEIKDRLKDLIKSGGEWISSVDLENALMGHPKVKEAAVVAIPHPKWQE 452
|
330 340 350 360
....*....|....*....|....*....|....*....|..
gi 2217306889 556 VVKAFVVLNpdykshDQEQLIKEIQEHVKKTTAPYKY-PRKV 596
Cdd:cd05915 453 RPLAVVVPR------GEKPTPEELNEHLLKAGFAKWQlPDAY 488
|
|
| entF |
PRK10252 |
enterobactin non-ribosomal peptide synthetase EntF; |
96-546 |
1.36e-14 |
|
enterobactin non-ribosomal peptide synthetase EntF;
Pssm-ID: 236668 [Multi-domain] Cd Length: 1296 Bit Score: 77.78 E-value: 1.36e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217306889 96 SFEELGSLSRKFANILSEAcSLQRGDRVILILPRVPEWWLANVACLRTGTVLIPGTTQLTQKDILYRLQSSKANCIITND 175
Cdd:PRK10252 485 SYREMREQVVALANLLRER-GVKPGDSVAVALPRSVFLTLALHAIVEAGAAWLPLDTGYPDDRLKMMLEDARPSLLITTA 563
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217306889 176 VLAPAVDAVASKcenlhsklivsensregwgnlkelmkVFLCHPGWstvarsWLTATSTSLVqaiLSLLSSWDYrhasds 255
Cdd:PRK10252 564 DQLPRFADVPDL--------------------------TSLCYNAP------LAPQGAAPLQ---LSQPHHTAY------ 602
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217306889 256 htcvktkhneimaIFFTSGTSGYPKMTAHTHSSFglglsVNGRFWLD----LTPSDVMWNTSDTGWAKSAWSsVFSPWIQ 331
Cdd:PRK10252 603 -------------IIFTSGSTGRPKGVMVGQTAI-----VNRLLWMQnhypLTADDVVLQKTPCSFDVSVWE-FFWPFIA 663
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217306889 332 GACVF-----THHlprfEPTSILQTLSKYPITV----------FCSAPTVyrmlvqnDITSYKFKSLKHCVSAGEPITPD 396
Cdd:PRK10252 664 GAKLVmaepeAHR----DPLAMQQFFAEYGVTTthfvpsmlaaFVASLTP-------EGARQSCASLRQVFCSGEALPAD 732
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217306889 397 VTEKWRNKTGLDIYEGYGQTET-VLICGNFKGMKIKPGSMGKPSP-AFDV-----KIVDVNGNVLPPGQEGDI---GIQv 466
Cdd:PRK10252 733 LCREWQQLTGAPLHNLYGPTEAaVDVSWYPAFGEELAAVRGSSVPiGYPVwntglRILDARMRPVPPGVAGDLyltGIQ- 811
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217306889 467 lpnrpfgLFTHYVDNPSKTASTLRGN-------FYITGDRGYMDKDGYFWFVARADDVILSSGYRIGPFEVENALNEHPS 539
Cdd:PRK10252 812 -------LAQGYLGRPDLTASRFIADpfapgerMYRTGDVARWLDDGAVEYLGRSDDQLKIRGQRIELGEIDRAMQALPD 884
|
....*..
gi 2217306889 540 VAESAVV 546
Cdd:PRK10252 885 VEQAVTH 891
|
|
| PRK07008 |
PRK07008 |
long-chain-fatty-acid--CoA ligase; Validated |
178-551 |
5.01e-14 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 235908 [Multi-domain] Cd Length: 539 Bit Score: 75.13 E-value: 5.01e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217306889 178 APAVDAVASKCENLhsklivsensrEGWgnlkelmkVFLCHpgwstvaRSWLTATSTSLvqailslLSSWDYRHA-SDSH 256
Cdd:PRK07008 122 LPLVDALAPQCPNV-----------KGW--------VAMTD-------AAHLPAGSTPL-------LCYETLVGAqDGDY 168
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217306889 257 TCVKTKHNEIMAIFFTSGTSGYPKMTAHTHSS-----FGLGLSVNgrfwLDLTPSDV------MWNTSdtgwaksAWSSV 325
Cdd:PRK07008 169 DWPRFDENQASSLCYTSGTTGNPKGALYSHRStvlhaYGAALPDA----MGLSARDAvlpvvpMFHVN-------AWGLP 237
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217306889 326 FSPWIQGA-CVFTHhlPRFEPTSILQTLSKYPITVFCSAPTVYRMLVQN-DITSYKFKSLKHCVSAGEPITPDVTEKWRN 403
Cdd:PRK07008 238 YSAPLTGAkLVLPG--PDLDGKSLYELIEAERVTFSAGVPTVWLGLLNHmREAGLRFSTLRRTVIGGSACPPAMIRTFED 315
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217306889 404 KTGLDIYEGYGQTETVLIcGNFKGMKIKPGSM------------GKPSPAFDVKIVDVNGNVLP-PGQE-GDIgiQVlpn 469
Cdd:PRK07008 316 EYGVEVIHAWGMTEMSPL-GTLCKLKWKHSQLpldeqrkllekqGRVIYGVDMKIVGDDGRELPwDGKAfGDL--QV--- 389
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217306889 470 RPFGLFTHYVDNpskTASTLRGNFYITGDRGYMDKDGYFWFVARADDVILSSGYRIGPFEVENALNEHPSVAESAVVSSP 549
Cdd:PRK07008 390 RGPWVIDRYFRG---DASPLVDGWFPTGDVATIDADGFMQITDRSKDVIKSGGEWISSIDIENVAVAHPAVAEAACIACA 466
|
..
gi 2217306889 550 DP 551
Cdd:PRK07008 467 HP 468
|
|
| FAAL |
cd05931 |
Fatty acyl-AMP ligase (FAAL); FAAL belongs to the class I adenylate forming enzyme family and ... |
74-583 |
8.91e-14 |
|
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: 74.20 E-value: 8.91e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217306889 74 AGKKPSNPAFWWINR-NGEEMRWSFEELGSLSRKFANILSEACslQRGDRVILILPRVPEWWLANVACLRTGTV---LIP 149
Cdd:cd05931 3 AAARPDRPAYTFLDDeGGREETLTYAELDRRARAIAARLQAVG--KPGDRVLLLAPPGLDFVAAFLGCLYAGAIavpLPP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217306889 150 GTTQLTQKDILYRLQSSKANCIITNDVLAPAVDAVASKcenlhsklivsensregwgnlkelmkvflcHPGWSTVARSWL 229
Cdd:cd05931 81 PTPGRHAERLAAILADAGPRVVLTTAAALAAVRAFAAS------------------------------RPAAGTPRLLVV 130
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217306889 230 TATSTSlvqailsllsswdyrhASDSHTCVKTKHNEIMAIFFTSGTSGYPK--MTAHT--HSSFGLGLSVngrfwLDLTP 305
Cdd:cd05931 131 DLLPDT----------------SAADWPPPSPDPDDIAYLQYTSGSTGTPKgvVVTHRnlLANVRQIRRA-----YGLDP 189
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217306889 306 SDVMWNtsdtgwaksaW----------SSVFSPWIQGA-CVFTHhlPR-F--EPTSILQTLSKYPITvFCSAPT-VYRML 370
Cdd:cd05931 190 GDVVVS----------WlplyhdmgliGGLLTPLYSGGpSVLMS--PAaFlrRPLRWLRLISRYRAT-ISAAPNfAYDLC 256
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217306889 371 VQ----NDITSYKFKSLKHCVSAGEPITPDVTEKWRNK---TGLD---IYEGYGQTE-TVLICGNFKG------------ 427
Cdd:cd05931 257 VRrvrdEDLEGLDLSSWRVALNGAEPVRPATLRRFAEAfapFGFRpeaFRPSYGLAEaTLFVSGGPPGtgpvvlrvdrda 336
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217306889 428 ------MKIKPG-------SMGKPSPAFDVKIVDVNGN-VLPPGQEGDIGIQVlPNRPFGlfthYVDNPSKTASTLR--- 490
Cdd:cd05931 337 lagravAVAADDpaarelvSCGRPLPDQEVRIVDPETGrELPDGEVGEIWVRG-PSVASG----YWGRPEATAETFGala 411
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217306889 491 ----GNFYITGDRGYMdKDGYFWFVARADDVILSSGYRIGPFEVENAL-NEHPSVAES--AVVSSPDPIRGEVVkAFVVL 563
Cdd:cd05931 412 atdeGGWLRTGDLGFL-HDGELYITGRLKDLIIVRGRNHYPQDIEATAeEAHPALRPGcvAAFSVPDDGEERLV-VVAEV 489
|
570 580
....*....|....*....|
gi 2217306889 564 NPDYKSHDQEQLIKEIQEHV 583
Cdd:cd05931 490 ERGADPADLAAIAAAIRAAV 509
|
|
| PRK08308 |
PRK08308 |
acyl-CoA synthetase; Validated |
335-593 |
1.08e-13 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236231 [Multi-domain] Cd Length: 414 Bit Score: 73.53 E-value: 1.08e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217306889 335 VFTHHLPRFeptsILQTLSKYPITVFCSAPTVYRMLVQNDITSYKFKSLkhcVSAGEPITPDVTEKWRNKTgLDIYEGYG 414
Cdd:PRK08308 173 IITNKNPKF----ALNILRNTPQHILYAVPLMLHILGRLLPGTFQFHAV---MTSGTPLPEAWFYKLRERT-TYMMQQYG 244
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217306889 415 QTET--VLICGNFKgmkiKPGSMGKPSPAFDVKIvdvngnvlppGQEgdigiqvlpnrpfglfthyVDNPSKTASTLRGN 492
Cdd:PRK08308 245 CSEAgcVSICPDMK----SHLDLGNPLPHVSVSA----------GSD-------------------ENAPEEIVVKMGDK 291
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217306889 493 FYITGDRGYMDKDGYFWFVARADDVILSSGYRIGPFEVENALNEHPSVAESAVVSSPDPIRGEVVKAFVVlnpdykSHDQ 572
Cdd:PRK08308 292 EIFTKDLGYKSERGTLHFMGRMDDVINVSGLNVYPIEVEDVMLRLPGVQEAVVYRGKDPVAGERVKAKVI------SHEE 365
|
250 260
....*....|....*....|.
gi 2217306889 573 EQLIkEIQEHVKKTTAPYKYP 593
Cdd:PRK08308 366 IDPV-QLREWCIQHLAPYQVP 385
|
|
| A_NRPS_PpsD_like |
cd17650 |
similar to adenylation domain of plipastatin synthase (PpsD); This family of the adenylation ... |
269-550 |
1.33e-13 |
|
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: 73.27 E-value: 1.33e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217306889 269 IFFTSGTSGYPKMTAHTHSSFG-LGLSVNGRFWLDLTPSDVMWNTS---DTGWAKSAWSSVFSpwiqGACVFTHHLPRFE 344
Cdd:cd17650 98 VIYTSGTTGKPKGVMVEHRNVAhAAHAWRREYELDSFPVRLLQMASfsfDVFAGDFARSLLNG----GTLVICPDEVKLD 173
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217306889 345 PTSILQTLSKYPITVFCSAPTVYRMLVQN-DITSYKFKSLKHCV--SAGEPITPDVTEKWRNKTGLDIYEGYGQTETVLI 421
Cdd:cd17650 174 PAALYDLILKSRITLMESTPALIRPVMAYvYRNGLDLSAMRLLIvgSDGCKAQDFKTLAARFGQGMRIINSYGVTEATID 253
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217306889 422 CGNFK-GMKIKPGS----MGKPSPAFDVKIVDVNGNVLPPGQEGDIGI------QVLPNRPFGLFTHYVDNPSKTAstlr 490
Cdd:cd17650 254 STYYEeGRDPLGDSanvpIGRPLPNTAMYVLDERLQPQPVGVAGELYIggagvaRGYLNRPELTAERFVENPFAPG---- 329
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217306889 491 GNFYITGDRGYMDKDGYFWFVARADDVILSSGYRIGPFEVENALNEHPSVAESAVVSSPD 550
Cdd:cd17650 330 ERMYRTGDLARWRADGNVELLGRVDHQVKIRGFRIELGEIESQLARHPAIDEAVVAVRED 389
|
|
| A_NRPS_acs4 |
cd17654 |
acyl-CoA synthetase family member 4; This family of the adenylation (A) domain of nonribosomal ... |
229-545 |
1.73e-12 |
|
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: 69.81 E-value: 1.73e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217306889 229 LTATSTSLVQAILS---LLSSWDYRHASDSHTCVKTKHNEIMAIFfTSGTSGYPKMTAHTHSSFgLGLSVNGRFWLDLTP 305
Cdd:cd17654 81 LTVMKKCHVSYLLQnkeLDNAPLSFTPEHRHFNIRTDECLAYVIH-TSGTTGTPKIVAVPHKCI-LPNIQHFRSLFNITS 158
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217306889 306 SDVMWNTSDTGWAKSAwSSVFSPWIQGAC-VFTHHLPRFEPTSILQTLSKYP-ITVFCSAPTVYRMLVQNDITSY---KF 380
Cdd:cd17654 159 EDILFLTSPLTFDPSV-VEIFLSLSSGATlLIVPTSVKVLPSKLADILFKRHrITVLQATPTLFRRFGSQSIKSTvlsAT 237
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217306889 381 KSLKHCVSAGEPITPDVTEK-WRNK-TGLDIYEGYGQTETVlICGNFKGMKIKPGSMGKPSPAFDVKI--VDVNGNVlPP 456
Cdd:cd17654 238 SSLRVLALGGEPFPSLVILSsWRGKgNRTRIFNIYGITEVS-CWALAYKVPEEDSPVQLGSPLLGTVIevRDQNGSE-GT 315
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217306889 457 GQEGDIGIqvlpNRpFGLFTHYVDNPsktastlRGNFYITGDRGYMdKDGYFWFVARADDVILSSGYRIGPFEVENALNE 536
Cdd:cd17654 316 GQVFLGGL----NR-VCILDDEVTVP-------KGTMRATGDFVTV-KDGELFFLGRKDSQIKRRGKRINLDLIQQVIES 382
|
....*....
gi 2217306889 537 HPSVAESAV 545
Cdd:cd17654 383 CLGVESCAV 391
|
|
| PRK06814 |
PRK06814 |
acyl-[ACP]--phospholipid O-acyltransferase; |
268-555 |
1.06e-11 |
|
acyl-[ACP]--phospholipid O-acyltransferase;
Pssm-ID: 235865 [Multi-domain] Cd Length: 1140 Bit Score: 68.07 E-value: 1.06e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217306889 268 AIFFTSGTSGYPKMTAHTHSSFglgLS----VNGRfwLDLTPSDVMWNTsdtgwaksawssvfspwiqgacvfthhLPRF 343
Cdd:PRK06814 797 VILFTSGSEGTPKGVVLSHRNL---LAnraqVAAR--IDFSPEDKVFNA---------------------------LPVF 844
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217306889 344 EP---TS--ILQTLSKYPITVFCSaPTVYR----MLVQNDIT-----------------SYKFKSLKHCVSAGEPITPDV 397
Cdd:PRK06814 845 HSfglTGglVLPLLSGVKVFLYPS-PLHYRiipeLIYDTNATilfgtdtflngyaryahPYDFRSLRYVFAGAEKVKEET 923
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217306889 398 TEKWRNKTGLDIYEGYGQTET--VLICGNfkGMKIKPGSMGKPSPAFDVKIVDVngnvlpPGQEGDIGIQVL-PNRPFGl 474
Cdd:PRK06814 924 RQTWMEKFGIRILEGYGVTETapVIALNT--PMHNKAGTVGRLLPGIEYRLEPV------PGIDEGGRLFVRgPNVMLG- 994
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217306889 475 fthYV--DNPSkTASTLRGNFYITGDRGYMDKDGYFWFVARADDVILSSGYRIGPFEVENALNEHPSVAESAVVSSPDPI 552
Cdd:PRK06814 995 ---YLraENPG-VLEPPADGWYDTGDIVTIDEEGFITIKGRAKRFAKIAGEMISLAAVEELAAELWPDALHAAVSIPDAR 1070
|
...
gi 2217306889 553 RGE 555
Cdd:PRK06814 1071 KGE 1073
|
|
| PRK08043 |
PRK08043 |
bifunctional acyl-ACP--phospholipid O-acyltransferase/long-chain-fatty-acid--ACP ligase; |
259-582 |
1.35e-11 |
|
bifunctional acyl-ACP--phospholipid O-acyltransferase/long-chain-fatty-acid--ACP ligase;
Pssm-ID: 181207 [Multi-domain] Cd Length: 718 Bit Score: 67.43 E-value: 1.35e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217306889 259 VKTKHNEIMAIFFTSGTSGYPKMTAHTHSSFgLGLSVNGRFWLDLTPSDVMWNTSDTGWAKSAWSSVFSPWIQGACVFTh 338
Cdd:PRK08043 360 VKQQPEDAALILFTSGSEGHPKGVVHSHKSL-LANVEQIKTIADFTPNDRFMSALPLFHSFGLTVGLFTPLLTGAEVFL- 437
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217306889 339 hlprfeptsilqtlskYPitvfcsAPTVYRM---LV--QNDI----TS------------YKFKSLKHCVSAGEPITPDV 397
Cdd:PRK08043 438 ----------------YP------SPLHYRIvpeLVydRNCTvlfgTStflgnyarfanpYDFARLRYVVAGAEKLQEST 495
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217306889 398 TEKWRNKTGLDIYEGYGQTETVLICGNFKGMKIKPGSMGKPSPAFDVKIVDVngnvlpPGQEGDIGIQVL-PNRPFGLFT 476
Cdd:PRK08043 496 KQLWQDKFGLRILEGYGVTECAPVVSINVPMAAKPGTVGRILPGMDARLLSV------PGIEQGGRLQLKgPNIMNGYLR 569
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217306889 477 hyVDNPSK----TASTLRG----NFYITGDRGYMDKDGYFWFVARADDVILSSGYRIGPFEVENALNEHPSVAESAVVSS 548
Cdd:PRK08043 570 --VEKPGVlevpTAENARGemerGWYDTGDIVRFDEQGFVQIQGRAKRFAKIAGEMVSLEMVEQLALGVSPDKQHATAIK 647
|
330 340 350
....*....|....*....|....*....|....
gi 2217306889 549 PDPIRGEvvkAFVVLNPDyKSHDQEQLIKEIQEH 582
Cdd:PRK08043 648 SDASKGE---ALVLFTTD-SELTREKLQQYAREH 677
|
|
| PRK05691 |
PRK05691 |
peptide synthase; Validated |
263-546 |
2.67e-11 |
|
peptide synthase; Validated
Pssm-ID: 235564 [Multi-domain] Cd Length: 4334 Bit Score: 67.12 E-value: 2.67e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217306889 263 HNEIMA-IFFTSGTSGYPKMTAHTHSSFGLGLSvngrfWLD----LTPSDVMWNTSDTGWAKSAWSsVFSPWIQG----- 332
Cdd:PRK05691 1271 HGDNLAyVIYTSGSTGQPKGVGNTHAALAERLQ-----WMQatyaLDDSDVLMQKAPISFDVSVWE-CFWPLITGcrlvl 1344
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217306889 333 ACVFTHHlprfEPTSILQTLSKYPITVFCSAPTVYRMLVQNDITSyKFKSLKHCVSAGEPITPDVTEKWRNK-TGLDIYE 411
Cdd:PRK05691 1345 AGPGEHR----DPQRIAELVQQYGVTTLHFVPPLLQLFIDEPLAA-ACTSLRRLFSGGEALPAELRNRVLQRlPQVQLHN 1419
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217306889 412 GYGQTETVL-----ICGNFKGMKikpGSMGKPSPAFDVKIVDVNGNVLPPGQEGDIGIQVLpnrpfGLFTHYVDNPSKTA 486
Cdd:PRK05691 1420 RYGPTETAInvthwQCQAEDGER---SPIGRPLGNVLCRVLDAELNLLPPGVAGELCIGGA-----GLARGYLGRPALTA 1491
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2217306889 487 --------STLRGNFYITGDRGYMDKDGYFWFVARADDVILSSGYRIGPFEVENALNEHPSVAESAVV 546
Cdd:PRK05691 1492 erfvpdplGEDGARLYRTGDRARWNADGALEYLGRLDQQVKLRGFRVEPEEIQARLLAQPGVAQAAVL 1559
|
|
| hsFATP2a_ACSVL_like |
cd05938 |
Fatty acid transport proteins (FATP) including hsFATP2, hsFATP5, and hsFATP6, and similar ... |
91-594 |
8.62e-11 |
|
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: 64.62 E-value: 8.62e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217306889 91 EEMRWSFEELGSLSRKFANILSEACSLQRGDRVILILPRVPEW---WLAnVACLRTGTVLIPgtTQLTQKDILYRLQSSK 167
Cdd:cd05938 2 EGETYTYRDVDRRSNQAARALLAHAGLRPGDTVALLLGNEPAFlwiWLG-LAKLGCPVAFLN--TNIRSKSLLHCFRCCG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217306889 168 ANCIITNDVLAPAVDAV--ASKCENLHSKLIVSENSREGWGNLKELMKvflchpgwstvarswltATSTSLVQAILSLLS 245
Cdd:cd05938 79 AKVLVVAPELQEAVEEVlpALRADGVSVWYLSHTSNTEGVISLLDKVD-----------------AASDEPVPASLRAHV 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217306889 246 SWdyrhasdSHTCVktkhneimaIFFTSGTSGYPKMTAHTHSSFglgLSVNGRFWL-DLTPSDVMWNTSDTgWAKSAWSS 324
Cdd:cd05938 142 TI-------KSPAL---------YIYTSGTTGLPKAARISHLRV---LQCSGFLSLcGVTADDVIYITLPL-YHSSGFLL 201
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217306889 325 VFSPWIQ-GA-CVFThhlPRFEPTSILQTLSKYPITVFCSAPTVYRMLVQndiTSYKFKSLKHCV--SAGEPITPDVTEK 400
Cdd:cd05938 202 GIGGCIElGAtCVLK---PKFSASQFWDDCRKHNVTVIQYIGELLRYLCN---QPQSPNDRDHKVrlAIGNGLRADVWRE 275
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217306889 401 WRNKTG-LDIYEGYGQTETVLICGNFKGmkiKPGSMGKPS-------P----AFDVK----IVDVNGNVLP--PGQEGDI 462
Cdd:cd05938 276 FLRRFGpIRIREFYGSTEGNIGFFNYTG---KIGAVGRVSylykllfPfeliKFDVEkeepVRDAQGFCIPvaKGEPGLL 352
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217306889 463 GIQVLPNRPFglfTHYVDNPSKTASTL------RGNFYI-TGDRGYMDKDGYFWFVARADDVILSSGYRIGPFEVENALN 535
Cdd:cd05938 353 VAKITQQSPF---LGYAGDKEQTEKKLlrdvfkKGDVYFnTGDLLVQDQQNFLYFHDRVGDTFRWKGENVATTEVADVLG 429
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2217306889 536 EHPSVAESAV--VSSPDpIRGEVVKAFVVLNPDYkSHDQEQLIkeiqEHVKKTTAPYKYPR 594
Cdd:cd05938 430 LLDFLQEVNVygVTVPG-HEGRIGMAAVKLKPGH-EFDGKKLY----QHVREYLPAYARPR 484
|
|
| PRK05691 |
PRK05691 |
peptide synthase; Validated |
271-593 |
1.13e-10 |
|
peptide synthase; Validated
Pssm-ID: 235564 [Multi-domain] Cd Length: 4334 Bit Score: 65.19 E-value: 1.13e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217306889 271 FTSGTSGYPKMTAHTHSSFGLGL-SVNGRFwlDLTPSDVMWNTSDTGWaKSAWSSVFSPWIQGACVFTHHLPRFEPTSIL 349
Cdd:PRK05691 2340 YTSGSTGKPKGVVVSHGEIAMHCqAVIERF--GMRADDCELHFYSINF-DAASERLLVPLLCGARVVLRAQGQWGAEEIC 2416
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217306889 350 QTLSKYPITVFCSAPTVYRMLVQNDITSYKFKSLKHCVSAGEPITPDVTEKWRNKTGLD-IYEGYGQTETV---LICGNF 425
Cdd:PRK05691 2417 QLIREQQVSILGFTPSYGSQLAQWLAGQGEQLPVRMCITGGEALTGEHLQRIRQAFAPQlFFNAYGPTETVvmpLACLAP 2496
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217306889 426 KGMKIKPGS--MGKPSPAFDVKIVDVNGNVLPPGQEGDIGIQVLpnrpfGLFTHYVDNPSKTA--------STLRGNFYI 495
Cdd:PRK05691 2497 EQLEEGAASvpIGRVVGARVAYILDADLALVPQGATGELYVGGA-----GLAQGYHDRPGLTAerfvadpfAADGGRLYR 2571
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217306889 496 TGDRGYMDKDGYFWFVARADDVILSSGYRIGPFEVENALNEHPSVAESAVVSSPDPIRGEVVKAFVVLNPDYKSHDQEQL 575
Cdd:PRK05691 2572 TGDLVRLRADGLVEYVGRIDHQVKIRGFRIELGEIESRLLEHPAVREAVVLALDTPSGKQLAGYLVSAVAGQDDEAQAAL 2651
|
330
....*....|....*...
gi 2217306889 576 IKEIQEHVKKTTAPYKYP 593
Cdd:PRK05691 2652 REALKAHLKQQLPDYMVP 2669
|
|
| FATP_FACS |
cd05940 |
Fatty acid transport proteins (FATP) play dual roles as fatty acid transporters and its ... |
271-550 |
1.25e-10 |
|
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: 63.91 E-value: 1.25e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217306889 271 FTSGTSGYPKMTAHTHSSFGLGLSVNGrFWLDLTPSDVMWNT----SDTGwAKSAWSSVFspwIQGACVFTHHlpRFEPT 346
Cdd:cd05940 88 YTSGTTGLPKAAIISHRRAWRGGAFFA-GSGGALPSDVLYTClplyHSTA-LIVGWSACL---ASGATLVIRK--KFSAS 160
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217306889 347 SILQTLSKYPITVFCSAPTVYRMLVQndiTSYKFKSLKHCVSA--GEPITPDVTEKWRNKTGL-DIYEGYGQTETVLICG 423
Cdd:cd05940 161 NFWDDIRKYQATIFQYIGELCRYLLN---QPPKPTERKHKVRMifGNGLRPDIWEEFKERFGVpRIAEFYAATEGNSGFI 237
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217306889 424 NFKGmkiKPGSMGKPSP----AFDVKIV-----------DVNGNV--LPPGQEGDIGIQVLPNRPFglfTHYVDNPSKTA 486
Cdd:cd05940 238 NFFG---KPGAIGRNPSllrkVAPLALVkydlesgepirDAEGRCikVPRGEPGLLISRINPLEPF---DGYTDPAATEK 311
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2217306889 487 STLRGNF------YITGDRGYMDKDGYFWFVARADDVILSSGYRIGPFEVENALNEHPSVAESAV--VSSPD 550
Cdd:cd05940 312 KILRDVFkkgdawFNTGDLMRLDGEGFWYFVDRLGDTFRWKGENVSTTEVAAVLGAFPGVEEANVygVQVPG 383
|
|
| PRK05691 |
PRK05691 |
peptide synthase; Validated |
269-593 |
2.34e-10 |
|
peptide synthase; Validated
Pssm-ID: 235564 [Multi-domain] Cd Length: 4334 Bit Score: 64.03 E-value: 2.34e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217306889 269 IFFTSGTSGYPKmtahthssfglGLSVNGRF----------WLDLTPSDVMWNTSDTGWAKSAWSSVFSPWIQGACVFTH 338
Cdd:PRK05691 3874 VIYTSGSTGLPK-----------GVMVEQRGmlnnqlskvpYLALSEADVIAQTASQSFDISVWQFLAAPLFGARVEIVP 3942
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217306889 339 HLPRFEPTSILQTLSKYPITVFCSAPT-VYRMLVQNDITsykFKSLKHCVSAGEPITPDVTEKWRNK-TGLDIYEGYGQT 416
Cdd:PRK05691 3943 NAIAHDPQGLLAHVQAQGITVLESVPSlIQGMLAEDRQA---LDGLRWMLPTGEAMPPELARQWLQRyPQIGLVNAYGPA 4019
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217306889 417 ETVLICGNFK-GMKIKPGS---MGKPSPAFDVKIVDVNGNVLPPGQEGDIGIQvlpnrPFGLFTHYVDNPSKTASTLRGN 492
Cdd:PRK05691 4020 ECSDDVAFFRvDLASTRGSylpIGSPTDNNRLYLLDEALELVPLGAVGELCVA-----GTGVGRGYVGDPLRTALAFVPH 4094
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217306889 493 --------FYITGDRGYMDKDGYFWFVARADDVILSSGYRIGPFEVENALNEHPSVAESAVVSSPDPiRGEVVKAFVVln 564
Cdd:PRK05691 4095 pfgapgerLYRTGDLARRRSDGVLEYVGRIDHQVKIRGYRIELGEIEARLHEQAEVREAAVAVQEGV-NGKHLVGYLV-- 4171
|
330 340
....*....|....*....|....*....
gi 2217306889 565 PDYKSHDQEQLIKEIQEHVKKTTAPYKYP 593
Cdd:PRK05691 4172 PHQTVLAQGALLERIKQRLRAELPDYMVP 4200
|
|
| AACS |
cd05943 |
Acetoacetyl-CoA synthetase (acetoacetate-CoA ligase, AACS); AACS is a cytosolic ligase that ... |
55-601 |
1.34e-09 |
|
Acetoacetyl-CoA synthetase (acetoacetate-CoA ligase, AACS); AACS is a cytosolic ligase that specifically activates acetoacetate to its coenzyme A ester by a two-step reaction. Acetoacetate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This is the first step of the mevalonate pathway of isoprenoid biosynthesis via isopentenyl diphosphate. Isoprenoids are a large class of compounds found in all living organisms. AACS is widely distributed in bacteria, archaea and eukaryotes. In bacteria, AACS is known to exhibit an important role in the metabolism of poly-b-hydroxybutyrate, an intracellular reserve of organic carbon and chemical energy by some microorganisms. In mammals, AACS influences the rate of ketone body utilization for the formation of physiologically important fatty acids and cholesterol.
Pssm-ID: 341265 [Multi-domain] Cd Length: 629 Bit Score: 61.13 E-value: 1.34e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217306889 55 PEYF-----NFAKDVLdqwtdkekAGKKPSNPAFWWINRNGEEMRWSFEELGSLSRKFANILsEACSLQRGDRVILILPR 129
Cdd:cd05943 62 ARWFpgarlNYAENLL--------RHADADDPAAIYAAEDGERTEVTWAELRRRVARLAAAL-RALGVKPGDRVAGYLPN 132
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217306889 130 VPEwwlANVACLRT---GTVLIPGTTQLTQKDILYRLQSSKANCIITNDV---------LAPAVDAVASKCENLHSKLIV 197
Cdd:cd05943 133 IPE---AVVAMLATasiGAIWSSCSPDFGVPGVLDRFGQIEPKVLFAVDAytyngkrhdVREKVAELVKGLPSLLAVVVV 209
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217306889 198 SENSREGWGNLKELMKvflchpgWSTVARSWLTATSTSLvqailsllsswDYRHASDSHTcvktkhneiMAIFFTSGTSG 277
Cdd:cd05943 210 PYTVAAGQPDLSKIAK-------ALTLEDFLATGAAGEL-----------EFEPLPFDHP---------LYILYSSGTTG 262
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217306889 278 YPKmtAHTHSSFGLGLSVNGRFWL--DLTPSDVM-WNTSdTGWAksAWSSVFSPWIQGACVFTHHLPRFEPTS--ILQTL 352
Cdd:cd05943 263 LPK--CIVHGAGGTLLQHLKEHILhcDLRPGDRLfYYTT-CGWM--MWNWLVSGLAVGATIVLYDGSPFYPDTnaLWDLA 337
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217306889 353 SKYPITVFCSAPTVYRMLVQNDI---TSYKFKSLKHCVSAGEPITPD----VTEKWrnKTGLDIYEGYGQTEtvlICGNF 425
Cdd:cd05943 338 DEEGITVFGTSAKYLDALEKAGLkpaETHDLSSLRTILSTGSPLKPEsfdyVYDHI--KPDVLLASISGGTD---IISCF 412
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217306889 426 KGMK----IKPGSMGKPSPAFDVKIVDVNGNVLPpGQEGDIGI-QVLPNRPfglfTHYVDNPSktASTLRGNFYIT---- 496
Cdd:cd05943 413 VGGNpllpVYRGEIQCRGLGMAVEAFDEEGKPVW-GEKGELVCtKPFPSMP----VGFWNDPD--GSRYRAAYFAKypgv 485
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217306889 497 ---GDRGYMDKDGYFWFVARADDVILSSGYRIGPFEVENALNEHPSVAESAVVSSPDPIRGEVVKAFVVLNPDykshdqE 573
Cdd:cd05943 486 wahGDWIEITPRGGVVILGRSDGTLNPGGVRIGTAEIYRVVEKIPEVEDSLVVGQEWKDGDERVILFVKLREG------V 559
|
570 580
....*....|....*....|....*...
gi 2217306889 574 QLIKEIQEHVKKTTAPYKYPRKVGILII 601
Cdd:cd05943 560 ELDDELRKRIRSTIRSALSPRHVPAKII 587
|
|
| A_NRPS_MycA_like |
cd05908 |
The adenylation domain of nonribosomal peptide synthetases (NRPS) similar to mycosubtilin ... |
264-587 |
2.45e-09 |
|
The adenylation domain of nonribosomal peptide synthetases (NRPS) similar to mycosubtilin synthase subunit A (MycA); The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as (amino)-acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms thioester to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. This family includes NRPS similar to mycosubtilin synthase subunit A (MycA). Mycosubtilin, which is characterized by a beta-amino fatty acid moiety linked to the circular heptapeptide Asn-Tyr-Asn-Gln-Pro-Ser-Asn, belongs to the iturin family of lipopeptide antibiotics. The mycosubtilin synthase subunit A (MycA) combines functional domains derived from peptide synthetases, amino transferases, and fatty acid synthases. Nonribosomal peptide synthetases are large multifunction enzymes that synthesize many therapeutically useful peptides. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and, in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.
Pssm-ID: 341234 [Multi-domain] Cd Length: 499 Bit Score: 60.19 E-value: 2.45e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217306889 264 NEIMAIFFTSGTSGYPKMTAHTHSSFGLG-LSVNGRFWLDLTPSDVMWN--TSDTGWAksawSSVFSPWIQGACVFTHHL 340
Cdd:cd05908 106 DELAFIQFSSGSTGDPKGVMLTHENLVHNmFAILNSTEWKTKDRILSWMplTHDMGLI----AFHLAPLIAGMNQYLMPT 181
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217306889 341 PRF--EPTSILQTLSKYPITVFCSAPTVYRMLVQ----NDITSYKFKSLKHCVSAGEPITPDVTE---KWRNKTGLD--- 408
Cdd:cd05908 182 RLFirRPILWLKKASEHKATIVSSPNFGYKYFLKtlkpEKANDWDLSSIRMILNGAEPIDYELCHeflDHMSKYGLKrna 261
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217306889 409 IYEGYGQTE-TVLICGNFKGMKIKPGSM-------GKPSPAFD--------------------VKIVDVNGNVLPPGQEG 460
Cdd:cd05908 262 ILPVYGLAEaSVGASLPKAQSPFKTITLgrrhvthGEPEPEVDkkdsecltfvevgkpidetdIRICDEDNKILPDGYIG 341
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217306889 461 DI---GIQVLPNrpfglfthYVDNPSKTASTLRGN-FYITGDRGYMdKDGYFWFVARADDVILSSGYRIGPFEVENALNE 536
Cdd:cd05908 342 HIqirGKNVTPG--------YYNNPEATAKVFTDDgWLKTGDLGFI-RNGRLVITGREKDIIFVNGQNVYPHDIERIAEE 412
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*
gi 2217306889 537 HPSVAESAVVS---SPDPIRGEVVKAFVVLNpdyKSHDQ-EQLIKEIQEHVKKTT 587
Cdd:cd05908 413 LEGVELGRVVAcgvNNSNTRNEEIFCFIEHR---KSEDDfYPLGKKIKKHLNKRG 464
|
|
| PLN03051 |
PLN03051 |
acyl-activating enzyme; Provisional |
268-589 |
4.40e-09 |
|
acyl-activating enzyme; Provisional
Pssm-ID: 215552 [Multi-domain] Cd Length: 499 Bit Score: 59.06 E-value: 4.40e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217306889 268 AIFFTSGTSGYPKMTAHTHSSfGLGLSVNGRFWLDLTPSDVM-WNTSdTGWAKSAWsSVFSPWIQGACVFTHHlprFEPT 346
Cdd:PLN03051 123 NILFSSGTTGEPKAIPWTHLS-PLRCASDGWAHMDIQPGDVVcWPTN-LGWMMGPW-LLYSAFLNGATLALYG---GAPL 196
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217306889 347 S--ILQTLSKYPITVFCSAPTV---YRMLVQNDITSYKFKSLKHCVSAGEPITPDvTEKWRNKT------------GLDI 409
Cdd:PLN03051 197 GrgFGKFVQDAGVTVLGLVPSIvkaWRHTGAFAMEGLDWSKLRVFASTGEASAVD-DVLWLSSVrgyykpvieycgGTEL 275
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217306889 410 YEGYGQTETVLICGnfkgmkikPGSMGKPSPAFDVKIVDVNGNVLPPGQE--GDIGI--------QVLPNRPFGLfTHYV 479
Cdd:PLN03051 276 ASGYISSTLLQPQA--------PGAFSTASLGTRFVLLNDNGVPYPDDQPcvGEVALappmlgasDRLLNADHDK-VYYK 346
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217306889 480 DNP--SKTASTLRGNfyitGDRGYMDKDGYFWFVARADDVILSSGYRIGPFEVENALNE-HPSVAESAVVSSPDPIRGE- 555
Cdd:PLN03051 347 GMPmyGSKGMPLRRH----GDIMKRTPGGYFCVQGRADDTMNLGGIKTSSVEIERACDRaVAGIAETAAVGVAPPDGGPe 422
|
330 340 350
....*....|....*....|....*....|....*..
gi 2217306889 556 ---VVKAFVVLNPDYKSHDQEQLIKEIQEHVKKTTAP 589
Cdd:PLN03051 423 llvIFLVLGEEKKGFDQARPEALQKKFQEAIQTNLNP 459
|
|
| FCS |
cd05921 |
Feruloyl-CoA synthetase (FCS); Feruloyl-CoA synthetase is an essential enzyme in the feruloyl ... |
271-566 |
5.84e-09 |
|
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: 58.98 E-value: 5.84e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217306889 271 FTSGTSGYPKMTAHTHSSFGLGLSVNGRFWLDLTPSD-VMWNtsdtgWAksAWSSVFSpwiqGACVF--------THHLP 341
Cdd:cd05921 172 FTSGSTGLPKAVINTQRMLCANQAMLEQTYPFFGEEPpVLVD-----WL--PWNHTFG----GNHNFnlvlynggTLYID 240
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217306889 342 RFEPT-----SILQTLSKYPITVFCSAPTVYRMLVQ---NDITSYK--FKSLKHCVSAGEPITPDVTEKWRN----KTGL 407
Cdd:cd05921 241 DGKPMpggfeETLRNLREISPTVYFNVPAGWEMLVAaleKDEALRRrfFKRLKLMFYAGAGLSQDVWDRLQAlavaTVGE 320
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217306889 408 DI--YEGYGQTETVLICGNFKGMKIKPGSMGKPSPAFDVKIVDVNGNVlppgqEGDI-GIQVLPNrpfglfthYVDNPSK 484
Cdd:cd05921 321 RIpmMAGLGATETAPTATFTHWPTERSGLIGLPAPGTELKLVPSGGKY-----EVRVkGPNVTPG--------YWRQPEL 387
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217306889 485 TASTL-RGNFYITGDRGYM----DKDGYFWFVAR-ADDVILSSG--YRIGPFEVEnALNEHPSVAESAVVSSPDpirGEV 556
Cdd:cd05921 388 TAQAFdEEGFYCLGDAAKLadpdDPAKGLVFDGRvAEDFKLASGtwVSVGPLRAR-AVAACAPLVHDAVVAGED---RAE 463
|
330
....*....|
gi 2217306889 557 VKAFVVLNPD 566
Cdd:cd05921 464 VGALVFPDLL 473
|
|
| PRK07768 |
PRK07768 |
long-chain-fatty-acid--CoA ligase; Validated |
345-533 |
6.36e-09 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236091 [Multi-domain] Cd Length: 545 Bit Score: 58.85 E-value: 6.36e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217306889 345 PTSILQTLSKYPITV-----FCSAPTVYRMLVQNDITSYKFKSLKHCVSAGEPITPDVTEKWRN---KTGLD---IYEGY 413
Cdd:PRK07768 235 PLLWAELISKYRGTMtaapnFAYALLARRLRRQAKPGAFDLSSLRFALNGAEPIDPADVEDLLDagaRFGLRpeaILPAY 314
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217306889 414 GQTETVLI-----CGNfkGMKI------------------KPG-----SMGKPSPAFDVKIVDVNGNVLPPGQEGDI--- 462
Cdd:PRK07768 315 GMAEATLAvsfspCGA--GLVVdevdadllaalrravpatKGNtrrlaTLGPPLPGLEVRVVDEDGQVLPPRGVGVIelr 392
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2217306889 463 GIQVLPnrpfglftHYVDNPSKTASTLRGNFYITGDRGYMDKDGYFWFVARADDVILSSGYRIGPFEVENA 533
Cdd:PRK07768 393 GESVTP--------GYLTMDGFIPAQDADGWLDTGDLGYLTEEGEVVVCGRVKDVIIMAGRNIYPTDIERA 455
|
|
| hsFATP4_like |
cd05939 |
Fatty acid transport proteins (FATP), including FATP4 and FATP1, and similar proteins; Fatty ... |
94-545 |
7.70e-09 |
|
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: 58.21 E-value: 7.70e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217306889 94 RWSFEELGSLSRKFANILSeACSLQRGDRVILILPRVPEW---WLAnVACLRTGTVLIpgTTQLTQKDILYRLQSSKANC 170
Cdd:cd05939 3 HWTFRELNEYSNKVANFFQ-AQGYRSGDVVALFMENRLEFvalWLG-LAKIGVETALI--NSNLRLESLLHCITVSKAKA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217306889 171 IITNdvlapavdavaskcenLHSKLivsensregwgnlkelmkvflchpgwstvarswLTATSTSLvqailsllsswdyr 250
Cdd:cd05939 79 LIFN----------------LLDPL---------------------------------LTQSSTEP-------------- 95
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217306889 251 hasdsHTCVKTKHNEIMAIFFTSGTSGYPKMTAHTHSSFgLGLSVNGRFWLDLTPSDVMWNTSDTGWAKSAWSSVFSPWI 330
Cdd:cd05939 96 -----PSQDDVNFRDKLFYIYTSGTTGLPKAAVIVHSRY-YRIAAGAYYAFGMRPEDVVYDCLPLYHSAGGIMGVGQALL 169
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217306889 331 QGACVFTHHlpRFEPTSILQTLSKYPITVFCSAPTVYRMLVQndiTSYKFKSLKHCV--SAGEPITPDVTEKWRNKTGL- 407
Cdd:cd05939 170 HGSTVVIRK--KFSASNFWDDCVKYNCTIVQYIGEICRYLLA---QPPSEEEQKHNVrlAVGNGLRPQIWEQFVRRFGIp 244
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217306889 408 DIYEGYGQTETVLICGNFKG------------MKIKPGSMGKPSPAFDVKIVDVNGNVLP--PGQEGDIGIQVLPNRPFG 473
Cdd:cd05939 245 QIGEFYGATEGNSSLVNIDNhvgacgfnsrilPSVYPIRLIKVDEDTGELIRDSDGLCIPcqPGEPGLLVGKIIQNDPLR 324
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2217306889 474 LFTHYVDNPSKTASTLRGNF------YITGDRGYMDKDGYFWFVARADDVILSSGYRIGPFEVENALNEHPSVAESAV 545
Cdd:cd05939 325 RFDGYVNEGATNKKIARDVFkkgdsaFLSGDVLVMDELGYLYFKDRTGDTFRWKGENVSTTEVEGILSNVLGLEDVVV 402
|
|
| PRK07824 |
PRK07824 |
o-succinylbenzoate--CoA ligase; |
494-599 |
1.61e-08 |
|
o-succinylbenzoate--CoA ligase;
Pssm-ID: 236108 [Multi-domain] Cd Length: 358 Bit Score: 56.98 E-value: 1.61e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217306889 494 YITGDRGYMDkDGYFWFVARADDVILSSGYRIGPFEVENALNEHPSVAESAVVSSPDPIRGEVVKAFVVlnpdyKSHDQE 573
Cdd:PRK07824 236 FRTDDLGALD-DGVLTVLGRADDAISTGGLTVLPQVVEAALATHPAVADCAVFGLPDDRLGQRVVAAVV-----GDGGPA 309
|
90 100
....*....|....*....|....*.
gi 2217306889 574 QLIKEIQEHVKKTTAPYKYPRKVGIL 599
Cdd:PRK07824 310 PTLEALRAHVARTLDRTAAPRELHVV 335
|
|
| PRK06334 |
PRK06334 |
long chain fatty acid--[acyl-carrier-protein] ligase; Validated |
259-537 |
3.38e-08 |
|
long chain fatty acid--[acyl-carrier-protein] ligase; Validated
Pssm-ID: 180533 [Multi-domain] Cd Length: 539 Bit Score: 56.36 E-value: 3.38e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217306889 259 VKTKHNEIMA-IFFTSGTSGYPKMTAHTHSSfglgLSVNGRFWLDL---TPSDVMWNTSDTGWAKSAWSSVFSPWIQGAC 334
Cdd:PRK06334 177 VSDKDPEDVAvILFTSGTEKLPKGVPLTHAN----LLANQRACLKFfspKEDDVMMSFLPPFHAYGFNSCTLFPLLSGVP 252
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217306889 335 VFTHHLPrFEPTSILQTLSKYPITVFCSAPTVYRMLVQndiTSYK----FKSLKHCVSAGEPITPDVTEK-WRNKTGLDI 409
Cdd:PRK06334 253 VVFAYNP-LYPKKIVEMIDEAKVTFLGSTPVFFDYILK---TAKKqescLPSLRFVVIGGDAFKDSLYQEaLKTFPHIQL 328
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217306889 410 YEGYGQTE-TVLICGNFKGMKIKPGSMGKPSPAFDVKIVDVNGNVlpPGQEGDIGIQVLpnRPFGLFTHYVDN-PSKTAS 487
Cdd:PRK06334 329 RQGYGTTEcSPVITINTVNSPKHESCVGMPIRGMDVLIVSEETKV--PVSSGETGLVLT--RGTSLFSGYLGEdFGQGFV 404
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*.
gi 2217306889 488 TLRG-NFYITGDRGYMDKDGYFWFVARaddviLSSGYRIGPFEV-----ENALNEH 537
Cdd:PRK06334 405 ELGGeTWYVTGDLGYVDRHGELFLKGR-----LSRFVKIGAEMVslealESILMEG 455
|
|
| PRK09192 |
PRK09192 |
fatty acyl-AMP ligase; |
436-584 |
5.63e-08 |
|
fatty acyl-AMP ligase;
Pssm-ID: 236403 [Multi-domain] Cd Length: 579 Bit Score: 55.78 E-value: 5.63e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217306889 436 GKPSPAFDVKIVDVNGNVLPPGQEGDIGIqvlpnRPFGLFTHYVDNPSKTASTLRGNFYITGDRGYMdKDGYFWFVARAD 515
Cdd:PRK09192 388 GKALPGHEIEIRNEAGMPLPERVVGHICV-----RGPSLMSGYFRDEESQDVLAADGWLDTGDLGYL-LDGYLYITGRAK 461
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2217306889 516 DVILSSGYRIGPFEVENALNEHPSV--AESAVVSSPDPiRGEVVKAFV---VLNPDykshDQEQLIKEIQEHVK 584
Cdd:PRK09192 462 DLIIINGRNIWPQDIEWIAEQEPELrsGDAAAFSIAQE-NGEKIVLLVqcrISDEE----RRGQLIHALAALVR 530
|
|
| ACSBG_like |
cd05933 |
Bubblegum-like very long-chain fatty acid CoA synthetase (VL-FACS); This family of very ... |
379-536 |
5.47e-07 |
|
Bubblegum-like very long-chain fatty acid CoA synthetase (VL-FACS); This family of very long-chain fatty acid CoA synthetase is named bubblegum because Drosophila melanogaster mutant bubblegum (BGM) has elevated levels of very-long-chain fatty acids (VLCFA) caused by a defective gene of this family. The human homolog (hsBG) has been characterized as a very long chain fatty acid CoA synthetase that functions specifically in the brain; hsBG may play a central role in brain VLCFA metabolism and myelinogenesis. VL-FACS is involved in the first reaction step of very long chain fatty acid degradation. It catalyzes the formation of fatty acyl-CoA in a two-step reaction: the formation of a fatty acyl-AMP molecule as an intermediate, and the formation of a fatty acyl-CoA. Free fatty acids must be "activated" to their CoA thioesters before participating in most catabolic and anabolic reactions.
Pssm-ID: 341256 [Multi-domain] Cd Length: 596 Bit Score: 52.74 E-value: 5.47e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217306889 379 KFKSLKHCV---SAGEPITPDVTEKWrnkTGLDI--YEGYGQTE-----TVLICGNFKgmkikPGSMGKPSPAFDVKIVD 448
Cdd:cd05933 315 KALGLDRCQkffTGAAPISRETLEFF---LSLNIpiMELYGMSEtsgphTISNPQAYR-----LLSCGKALPGCKTKIHN 386
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217306889 449 VNGNvlppGQeGDIGIqvlpnRPFGLFTHYVDNPSKTASTLRGNFYI-TGDRGYMDKDGYFWFVARADD-VILSSGYRIG 526
Cdd:cd05933 387 PDAD----GI-GEICF-----WGRHVFMGYLNMEDKTEEAIDEDGWLhSGDLGKLDEDGFLYITGRIKElIITAGGENVP 456
|
170
....*....|
gi 2217306889 527 PFEVENALNE 536
Cdd:cd05933 457 PVPIEDAVKK 466
|
|
| LC_FACS_euk1 |
cd17639 |
Eukaryotic long-chain fatty acid CoA synthetase (LC-FACS), including fungal proteins; The ... |
383-586 |
5.63e-07 |
|
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: 52.60 E-value: 5.63e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217306889 383 LKHCVSAGEPITPDvTEKWRNKTGLDIYEGYGQTETvliCGNfkGMKIKPGSM-----GKPSPAFDVKIVDV----NGNV 453
Cdd:cd17639 252 LRYMLSGGAPLSAD-TQEFLNIVLCPVIQGYGLTET---CAG--GTVQDPGDLetgrvGPPLPCCEIKLVDWeeggYSTD 325
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217306889 454 LPPGQeGDIGIQvlpnRPFgLFTHYVDNPSKTASTLRGN--FYiTGDRGYMDKDGYFWFVARADD-VILSSGYRIGPFEV 530
Cdd:cd17639 326 KPPPR-GEILIR----GPN-VFKGYYKNPEKTKEAFDGDgwFH-TGDIGEFHPDGTLKIIDRKKDlVKLQNGEYIALEKL 398
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 2217306889 531 ENALNEHPSVAESAVVSspDPIRGEVVkAFVVLNpdykshdQEQLIKEIQEHVKKT 586
Cdd:cd17639 399 ESIYRSNPLVNNICVYA--DPDKSYPV-AIVVPN-------EKHLTKLAEKHGVIN 444
|
|
| FATP_chFAT1_like |
cd05937 |
Uncharacterized subfamily of bifunctional fatty acid transporter/very-long-chain acyl-CoA ... |
384-546 |
6.42e-07 |
|
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: 52.05 E-value: 6.42e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217306889 384 KHCVSA--GEPITPDVTEKWRNKTGL-DIYEGYGQTETVLICGNFKGMKIKPGSMGKPSP------AFDVKIVDVNGN-- 452
Cdd:cd05937 201 DHKVRVawGNGLRPDIWERFRERFNVpEIGEFYAATEGVFALTNHNVGDFGAGAIGHHGLirrwkfENQVVLVKMDPEtd 280
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217306889 453 ------------VLPPGQEGDIgIQVLPNRPFGLFTHYVDNPSKTASTL------RGN-FYITGDRGYMDKDGYFWFVAR 513
Cdd:cd05937 281 dpirdpktgfcvRAPVGEPGEM-LGRVPFKNREAFQGYLHNEDATESKLvrdvfrKGDiYFRTGDLLRQDADGRWYFLDR 359
|
170 180 190
....*....|....*....|....*....|...
gi 2217306889 514 ADDVILSSGYRIGPFEVENALNEHPSVAESAVV 546
Cdd:cd05937 360 LGDTFRWKSENVSTTEVADVLGAHPDIAEANVY 392
|
|
| A_NRPS_alphaAR |
cd17647 |
Alpha-aminoadipate reductase; This family contains L-2-aminoadipate reductase, also known as ... |
271-593 |
5.95e-06 |
|
Alpha-aminoadipate reductase; This family contains L-2-aminoadipate reductase, also known as alpha-aminoadipate reductase (EC 1.2.1.95) or alpha-AR or L-aminoadipate-semialdehyde dehydrogenase (EC 1.2.1.31), which catalyzes the activation of alpha-aminoadipate by ATP-dependent adenylation and the reduction of activated alpha-aminoadipate by NADPH. The activated alpha-aminoadipate is bound to the phosphopantheinyl group of the enzyme itself before it is reduced to (S)-2-amino-6-oxohexanoate.
Pssm-ID: 341302 [Multi-domain] Cd Length: 520 Bit Score: 49.05 E-value: 5.95e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217306889 271 FTSGTSGYPKMTAHTHSSFGLGLS-VNGRFwlDLTPSDVMwnTSDTGWAKSAWS-SVFSPWIQGACVFthhLPRFE---- 344
Cdd:cd17647 116 FTSGSEGIPKGVLGRHFSLAYYFPwMAKRF--NLSENDKF--TMLSGIAHDPIQrDMFTPLFLGAQLL---VPTQDdigt 188
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217306889 345 PTSILQTLSKYPITVFCSAPTVYRMLVQNDITSykFKSLKHCVSAGEPITP-DVTEKWRNKTGLDIYEGYGQTETVLICG 423
Cdd:cd17647 189 PGRLAEWMAKYGATVTHLTPAMGQLLTAQATTP--FPKLHHAFFVGDILTKrDCLRLQTLAENVRIVNMYGTTETQRAVS 266
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217306889 424 NF--KGMKIKPG---SMGKPSPA----FDVKIVDVNGN----VLPPGQEGDIGIqvlpnRPFGLFTHYVDNPSKTASTLR 490
Cdd:cd17647 267 YFevPSRSSDPTflkNLKDVMPAgrgmLNVQLLVVNRNdrtqICGIGEVGEIYV-----RAGGLAEGYRGLPELNKEKFV 341
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217306889 491 GNFYITGDR-GYMDKDG-----YFWF-----------------------VARADDVILSSGYRIGPFEVENALNEHPSVA 541
Cdd:cd17647 342 NNWFVEPDHwNYLDKDNnepwrQFWLgprdrlyrtgdlgrylpngdcecCGRADDQVKIRGFRIELGEIDTHISQHPLVR 421
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2217306889 542 ES------------AVVS--SPDPIRGEVVKAFVVLNPDYKSHDQ--------EQLIKEIQEHVKKTTAPYKYP 593
Cdd:cd17647 422 ENitlvrrdkdeepTLVSyiVPRFDKPDDESFAQEDVPKEVSTDPivkgligyRKLIKDIREFLKKRLASYAIP 495
|
|
| PLN02736 |
PLN02736 |
long-chain acyl-CoA synthetase |
387-559 |
8.14e-06 |
|
long-chain acyl-CoA synthetase
Pssm-ID: 178337 [Multi-domain] Cd Length: 651 Bit Score: 48.94 E-value: 8.14e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217306889 387 VSAGEPITPDVTEKWRNKTGLDIYEGYGQTET-VLICGNFKGMKIKpGSMGKPSPAFDVKIVDVngnvlP---------P 456
Cdd:PLN02736 382 SSGASPLSPDVMEFLRICFGGRVLEGYGMTETsCVISGMDEGDNLS-GHVGSPNPACEVKLVDV-----PemnytsedqP 455
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217306889 457 GQEGDIGIqvlpnRPFGLFTHYVDNPSKTASTLRGNFYI-TGDRGYMDKDGYFWFVARADDVI-LSSGYRIGPFEVENAL 534
Cdd:PLN02736 456 YPRGEICV-----RGPIIFKGYYKDEVQTREVIDEDGWLhTGDIGLWLPGGRLKIIDRKKNIFkLAQGEYIAPEKIENVY 530
|
170 180 190
....*....|....*....|....*....|....*.
gi 2217306889 535 NEHPSVAESAV-----------VSSPDPirgEVVKA 559
Cdd:PLN02736 531 AKCKFVAQCFVygdslnsslvaVVVVDP---EVLKA 563
|
|
| PLN02430 |
PLN02430 |
long-chain-fatty-acid-CoA ligase |
387-566 |
8.91e-06 |
|
long-chain-fatty-acid-CoA ligase
Pssm-ID: 178049 [Multi-domain] Cd Length: 660 Bit Score: 48.66 E-value: 8.91e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217306889 387 VSAGEPITPDVTEKWRNKTGLDIYEGYGQTETvliCGnfkgmkikPGSMGKPSPAFDVKIVDVNG--NVLPPGQEGDIGI 464
Cdd:PLN02430 389 ISGGAPLSTEIEEFLRVTSCAFVVQGYGLTET---LG--------PTTLGFPDEMCMLGTVGAPAvyNELRLEEVPEMGY 457
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217306889 465 QVLPNRPFG--------LFTHYVDNPSKTASTLRGNFYITGDRGYMDKDGYFWFVARADDVI-LSSGYRIGPFEVENALN 535
Cdd:PLN02430 458 DPLGEPPRGeicvrgkcLFSGYYKNPELTEEVMKDGWFHTGDIGEILPNGVLKIIDRKKNLIkLSQGEYVALEYLENVYG 537
|
170 180 190
....*....|....*....|....*....|.
gi 2217306889 536 EHPSVAESAVVSspDPIRGEVVkAFVVLNPD 566
Cdd:PLN02430 538 QNPIVEDIWVYG--DSFKSMLV-AVVVPNEE 565
|
|
| PRK03584 |
PRK03584 |
acetoacetate--CoA ligase; |
59-143 |
1.40e-04 |
|
acetoacetate--CoA ligase;
Pssm-ID: 235134 [Multi-domain] Cd Length: 655 Bit Score: 44.79 E-value: 1.40e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217306889 59 NFAKDVLDQwtdkekagKKPSNPAFWWINRNGEEMRWSFEELGSLSRKFANILsEACSLQRGDRVILILPRVPEwwlANV 138
Cdd:PRK03584 87 NYAENLLRH--------RRDDRPAIIFRGEDGPRRELSWAELRRQVAALAAAL-RALGVGPGDRVAAYLPNIPE---TVV 154
|
....*
gi 2217306889 139 ACLRT 143
Cdd:PRK03584 155 AMLAT 159
|
|
| alpha_am_amid |
TIGR03443 |
L-aminoadipate-semialdehyde dehydrogenase; Members of this protein family are ... |
490-593 |
2.39e-04 |
|
L-aminoadipate-semialdehyde dehydrogenase; Members of this protein family are L-aminoadipate-semialdehyde dehydrogenase (EC 1.2.1.31), product of the LYS2 gene. It is also called alpha-aminoadipate reductase. In fungi, lysine is synthesized via aminoadipate. Currently, all members of this family are fungal.
Pssm-ID: 274582 [Multi-domain] Cd Length: 1389 Bit Score: 44.29 E-value: 2.39e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217306889 490 RGNFYITGDRGYMDKDGYFWFVARADDVILSSGYRIGPFEVENALNEHPSVAE----------------SAVVSSPDPir 553
Cdd:TIGR03443 676 RDRLYRTGDLGRYLPDGNVECCGRADDQVKIRGFRIELGEIDTHLSQHPLVREnvtlvrrdkdeeptlvSYIVPQDKS-- 753
|
90 100 110 120
....*....|....*....|....*....|....*....|....*...
gi 2217306889 554 gEVVKAFVVLNPDYKSHDQ--------EQLIKEIQEHVKKTTAPYKYP 593
Cdd:TIGR03443 754 -DELEEFKSEVDDEESSDPvvkglikyRKLIKDIREYLKKKLPSYAIP 800
|
|
| PRK05851 |
PRK05851 |
long-chain-fatty acid--ACP ligase MbtM; |
382-547 |
1.67e-03 |
|
long-chain-fatty acid--ACP ligase MbtM;
Pssm-ID: 180289 [Multi-domain] Cd Length: 525 Bit Score: 41.29 E-value: 1.67e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217306889 382 SLKHCVSAGEPITPDVTEKWRNKT---GLD---IYEGYGQTE-----TVLICGNfkGMKIKPGSM------------GKP 438
Cdd:PRK05851 273 ALRVALNGGEPVDCDGFERFATAMapfGFDagaAAPSYGLAEstcavTVPVPGI--GLRVDEVTTddgsgarrhavlGNP 350
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217306889 439 SPAFDVKIVDVNGNVLPPGQE-GDIGIqvlpnRPFGLFTHYVDNPSKTastlRGNFYITGDRGYMdKDGYFWFVARADDV 517
Cdd:PRK05851 351 IPGMEVRISPGDGAAGVAGREiGEIEI-----RGASMMSGYLGQAPID----PDDWFPTGDLGYL-VDGGLVVCGRAKEL 420
|
170 180 190
....*....|....*....|....*....|
gi 2217306889 518 ILSSGYRIGPFEVENALNEHPSVAESAVVS 547
Cdd:PRK05851 421 ITVAGRNIFPTEIERVAAQVRGVREGAVVA 450
|
|
| |
