|
Name |
Accession |
Description |
Interval |
E-value |
| PLN02479 |
PLN02479 |
acetate-CoA ligase |
3-569 |
0e+00 |
|
acetate-CoA ligase
Pssm-ID: 178097 [Multi-domain] Cd Length: 567 Bit Score: 1195.04 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228909 3 ATKWRDIDDLPKIPANYTALTPLWFLDRAAVVHPTRKSVIHGSREYTWRQTYDRCRRLASALADRSIGPGSTVAIIAPNI 82
Cdd:PLN02479 1 MAKERDIDDLPKNAANYTALTPLWFLERAAVVHPTRKSVVHGSVRYTWAQTYQRCRRLASALAKRSIGPGSTVAVIAPNI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228909 83 PAMYEAHFGVPMCGAVLNCVNIRLNAPTVAFLLSHSQSSVIMVDQEFFTLAEDSLRLMEEKAGSSFKRPLLIVIGDHTCA 162
Cdd:PLN02479 81 PAMYEAHFGVPMAGAVVNCVNIRLNAPTIAFLLEHSKSEVVMVDQEFFTLAEEALKILAEKKKSSFKPPLLIVIGDPTCD 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228909 163 PESLNRALSKGAIEYEDFLATGDPNYPWQPPADEWQSIALGYTSGTTASPKGVVLHHRGAYIMALSNPLIWGMQDGAVYL 242
Cdd:PLN02479 161 PKSLQYALGKGAIEYEKFLETGDPEFAWKPPADEWQSIALGYTSGTTASPKGVVLHHRGAYLMALSNALIWGMNEGAVYL 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228909 243 WTLPMFHCNGWCFPWSLAVLSGTSICLRQVTAKEVYSMIAKYKVTHFCAAPVVLNAIVNAPKEDTILPLPHTVHVMTAGA 322
Cdd:PLN02479 241 WTLPMFHCNGWCFTWTLAALCGTNICLRQVTAKAIYSAIANYGVTHFCAAPVVLNTIVNAPKSETILPLPRVVHVMTAGA 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228909 323 APPPSVLFSMNQKGFRVAHTYGLSETYGPSTVCAWKPEWDSLPPETQAKLNARQGVRYTGMEQLDVIDTQTGKPVPADGK 402
Cdd:PLN02479 321 APPPSVLFAMSEKGFRVTHTYGLSETYGPSTVCAWKPEWDSLPPEEQARLNARQGVRYIGLEGLDVVDTKTMKPVPADGK 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228909 403 TAGEIVFRGNMVMKGYLKNPEANKETFAGGWFHSGDIAVKHPDNYIEIKDRSKDVIISGGENISSVEVENVVYHHPAVLE 482
Cdd:PLN02479 401 TMGEIVMRGNMVMKGYLKNPKANEEAFANGWFHSGDLGVKHPDGYIEIKDRSKDIIISGGENISSLEVENVVYTHPAVLE 480
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228909 483 ASVVARPDERWQESPCAFVTLKSDYEKHDQNKLAQDIMKFCREKLPAYWVPKSVVFGPLPKTATGKIQKHILRTKAKEMG 562
Cdd:PLN02479 481 ASVVARPDERWGESPCAFVTLKPGVDKSDEAALAEDIMKFCRERLPAYWVPKSVVFGPLPKTATGKIQKHVLRAKAKEMG 560
|
....*..
gi 15228909 563 PVPRSRL 569
Cdd:PLN02479 561 PVKKSRL 567
|
|
| ttLC_FACS_AEE21_like |
cd12118 |
Fatty acyl-CoA synthetases similar to LC-FACS from Thermus thermophiles and Arabidopsis; This ... |
19-556 |
0e+00 |
|
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: 927.86 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228909 19 YTALTPLWFLDRAAVVHPTRKSVIHGSREYTWRQTYDRCRRLASALADRSIGPGSTVAIIAPNIPAMYEAHFGVPMCGAV 98
Cdd:cd12118 1 YVPLTPLSFLERAAAVYPDRTSIVYGDRRYTWRQTYDRCRRLASALAALGISRGDTVAVLAPNTPAMYELHFGVPMAGAV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228909 99 LNCVNIRLNAPTVAFLLSHSQSSVIMVDQEFftlaedslrlmeekagssfkrpllivigdhtcapeslnralskgaiEYE 178
Cdd:cd12118 81 LNALNTRLDAEEIAFILRHSEAKVLFVDREF----------------------------------------------EYE 114
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228909 179 DFLATGDPNYPWQPPADEWQSIALGYTSGTTASPKGVVLHHRGAYIMALSNPLIWGMQDGAVYLWTLPMFHCNGWCFPWS 258
Cdd:cd12118 115 DLLAEGDPDFEWIPPADEWDPIALNYTSGTTGRPKGVVYHHRGAYLNALANILEWEMKQHPVYLWTLPMFHCNGWCFPWT 194
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228909 259 LAVLSGTSICLRQVTAKEVYSMIAKYKVTHFCAAPVVLNAIVNAPKEDTiLPLPHTVHVMTAGAAPPPSVLFSMNQKGFR 338
Cdd:cd12118 195 VAAVGGTNVCLRKVDAKAIYDLIEKHKVTHFCGAPTVLNMLANAPPSDA-RPLPHRVHVMTAGAPPPAAVLAKMEELGFD 273
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228909 339 VAHTYGLSETYGPSTVCAWKPEWDSLPPETQAKLNARQGVRYTGMEQLDVIDTQTGKPVPADGKTAGEIVFRGNMVMKGY 418
Cdd:cd12118 274 VTHVYGLTETYGPATVCAWKPEWDELPTEERARLKARQGVRYVGLEEVDVLDPETMKPVPRDGKTIGEIVFRGNIVMKGY 353
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228909 419 LKNPEANKETFAGGWFHSGDIAVKHPDNYIEIKDRSKDVIISGGENISSVEVENVVYHHPAVLEASVVARPDERWQESPC 498
Cdd:cd12118 354 LKNPEATAEAFRGGWFHSGDLAVIHPDGYIEIKDRSKDIIISGGENISSVEVEGVLYKHPAVLEAAVVARPDEKWGEVPC 433
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*...
gi 15228909 499 AFVTLKSDYEkhdqnKLAQDIMKFCREKLPAYWVPKSVVFGPLPKTATGKIQKHILRT 556
Cdd:cd12118 434 AFVELKEGAK-----VTEEEIIAFCREHLAGFMVPKTVVFGELPKTSTGKIQKFVLRD 486
|
|
| PRK08162 |
PRK08162 |
acyl-CoA synthetase; Validated |
10-564 |
0e+00 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236169 [Multi-domain] Cd Length: 545 Bit Score: 891.22 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228909 10 DDLPKIPANYTALTPLWFLDRAAVVHPTRKSVIHGSREYTWRQTYDRCRRLASALADRSIGPGSTVAIIAPNIPAMYEAH 89
Cdd:PRK08162 6 QGLDRNAANYVPLTPLSFLERAAEVYPDRPAVIHGDRRRTWAETYARCRRLASALARRGIGRGDTVAVLLPNIPAMVEAH 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228909 90 FGVPMCGAVLNCVNIRLNAPTVAFLLSHSQSSVIMVDQEFFTLAEDSLRLMeekagssfKRPLLIVIGDhtcAPESLNRA 169
Cdd:PRK08162 86 FGVPMAGAVLNTLNTRLDAASIAFMLRHGEAKVLIVDTEFAEVAREALALL--------PGPKPLVIDV---DDPEYPGG 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228909 170 LSKGAIEYEDFLATGDPNYPWQPPADEWQSIALGYTSGTTASPKGVVLHHRGAYIMALSNPLIWGMQDGAVYLWTLPMFH 249
Cdd:PRK08162 155 RFIGALDYEAFLASGDPDFAWTLPADEWDAIALNYTSGTTGNPKGVVYHHRGAYLNALSNILAWGMPKHPVYLWTLPMFH 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228909 250 CNGWCFPWSLAVLSGTSICLRQVTAKEVYSMIAKYKVTHFCAAPVVLNAIVNAPKEDTIlPLPHTVHVMTAGAAPPPSVL 329
Cdd:PRK08162 235 CNGWCFPWTVAARAGTNVCLRKVDPKLIFDLIREHGVTHYCGAPIVLSALINAPAEWRA-GIDHPVHAMVAGAAPPAAVI 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228909 330 FSMNQKGFRVAHTYGLSETYGPSTVCAWKPEWDSLPPETQAKLNARQGVRYTGMEQLDVIDTQTGKPVPADGKTAGEIVF 409
Cdd:PRK08162 314 AKMEEIGFDLTHVYGLTETYGPATVCAWQPEWDALPLDERAQLKARQGVRYPLQEGVTVLDPDTMQPVPADGETIGEIMF 393
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228909 410 RGNMVMKGYLKNPEANKETFAGGWFHSGDIAVKHPDNYIEIKDRSKDVIISGGENISSVEVENVVYHHPAVLEASVVARP 489
Cdd:PRK08162 394 RGNIVMKGYLKNPKATEEAFAGGWFHTGDLAVLHPDGYIKIKDRSKDIIISGGENISSIEVEDVLYRHPAVLVAAVVAKP 473
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 15228909 490 DERWQESPCAFVTLKSdyekhDQNKLAQDIMKFCREKLPAYWVPKSVVFGPLPKTATGKIQKHILRTKAKEMGPV 564
Cdd:PRK08162 474 DPKWGEVPCAFVELKD-----GASATEEEIIAHCREHLAGFKVPKAVVFGELPKTSTGKIQKFVLREQAKSLKAI 543
|
|
| PLN03102 |
PLN03102 |
acyl-activating enzyme; Provisional |
9-561 |
0e+00 |
|
acyl-activating enzyme; Provisional
Pssm-ID: 215576 [Multi-domain] Cd Length: 579 Bit Score: 582.36 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228909 9 IDDLPKIPANYTALTPLWFLDRAAVVHPTRKSVIHGSREYTWRQTYDRCRRLASALADRSIGPGSTVAIIAPNIPAMYEA 88
Cdd:PLN03102 1 MDNLALCEANNVPLTPITFLKRASECYPNRTSIIYGKTRFTWPQTYDRCCRLAASLISLNITKNDVVSVLAPNTPAMYEM 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228909 89 HFGVPMCGAVLNCVNIRLNAPTVAFLLSHSQSSVIMVDQEFFTLAEDSLRLMEEKagSSFKRPLLIVIGDHtcapESLNR 168
Cdd:PLN03102 81 HFAVPMAGAVLNPINTRLDATSIAAILRHAKPKILFVDRSFEPLAREVLHLLSSE--DSNLNLPVIFIHEI----DFPKR 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228909 169 ALSKgAIEYEDFLATGDPNypwqpPA---------DEWQSIALGYTSGTTASPKGVVLHHRGAYIMALSNPLIWGMQDGA 239
Cdd:PLN03102 155 PSSE-ELDYECLIQRGEPT-----PSlvarmfriqDEHDPISLNYTSGTTADPKGVVISHRGAYLSTLSAIIGWEMGTCP 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228909 240 VYLWTLPMFHCNGWCFPWSLAVLSGTSICLRQVTAKEVYSMIAKYKVTHFCAAPVVLNAIVNAPKEDtILPLPHTVHVMT 319
Cdd:PLN03102 229 VYLWTLPMFHCNGWTFTWGTAARGGTSVCMRHVTAPEIYKNIEMHNVTHMCCVPTVFNILLKGNSLD-LSPRSGPVHVLT 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228909 320 AGAAPPPSVLFSMNQKGFRVAHTYGLSETYGPSTVCAWKPEWDSLPPETQAKLNARQGVRYTGMEQLDVIDTQTGKPVPA 399
Cdd:PLN03102 308 GGSPPPAALVKKVQRLGFQVMHAYGLTEATGPVLFCEWQDEWNRLPENQQMELKARQGVSILGLADVDVKNKETQESVPR 387
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228909 400 DGKTAGEIVFRGNMVMKGYLKNPEANKETFAGGWFHSGDIAVKHPDNYIEIKDRSKDVIISGGENISSVEVENVVYHHPA 479
Cdd:PLN03102 388 DGKTMGEIVIKGSSIMKGYLKNPKATSEAFKHGWLNTGDVGVIHPDGHVEIKDRSKDIIISGGENISSVEVENVLYKYPK 467
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228909 480 VLEASVVARPDERWQESPCAFVTLKSDYE--KHDQNKLA---QDIMKFCREKLPAYWVPKSVVF-GPLPKTATGKIQKHI 553
Cdd:PLN03102 468 VLETAVVAMPHPTWGETPCAFVVLEKGETtkEDRVDKLVtreRDLIEYCRENLPHFMCPRKVVFlQELPKNGNGKILKPK 547
|
....*...
gi 15228909 554 LRTKAKEM 561
Cdd:PLN03102 548 LRDIAKGL 555
|
|
| MenE/FadK |
COG0318 |
O-succinylbenzoic acid-CoA ligase MenE or related acyl-CoA synthetase (AMP-forming) [Lipid ... |
27-560 |
1.13e-146 |
|
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: 430.39 E-value: 1.13e-146
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228909 27 FLDRAAVVHPTRKSVIHGSREYTWRQTYDRCRRLASALADRSIGPGSTVAIIAPNIPAMYEAHFGVPMCGAVLNCVNIRL 106
Cdd:COG0318 4 LLRRAAARHPDRPALVFGGRRLTYAELDARARRLAAALRALGVGPGDRVALLLPNSPEFVVAFLAALRAGAVVVPLNPRL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228909 107 NAPTVAFLLSHSQSSVIMVdqefftlaedslrlmeekagssfkrpllivigdhtcapeslnralskgaieyedflatgdp 186
Cdd:COG0318 84 TAEELAYILEDSGARALVT------------------------------------------------------------- 102
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228909 187 nypwqppadewqsIALGYTSGTTASPKGVVLHHRGAYIMALSNPLIWGMQDGAVYLWTLPMFHCNGWCFPWSLAVLSG-T 265
Cdd:COG0318 103 -------------ALILYTSGTTGRPKGVMLTHRNLLANAAAIAAALGLTPGDVVLVALPLFHVFGLTVGLLAPLLAGaT 169
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228909 266 SICLRQVTAKEVYSMIAKYKVTHFCAAPVVLNAIVNAPKEDTiLPLPHTVHVMTAGAAPPPSVLFSMNQK-GFRVAHTYG 344
Cdd:COG0318 170 LVLLPRFDPERVLELIERERVTVLFGVPTMLARLLRHPEFAR-YDLSSLRLVVSGGAPLPPELLERFEERfGVRIVEGYG 248
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228909 345 LSETYGPSTVCawkpewdslPPETQAKLNARQGVRYTGMEqLDVIDtQTGKPVPADgkTAGEIVFRGNMVMKGYLKNPEA 424
Cdd:COG0318 249 LTETSPVVTVN---------PEDPGERRPGSVGRPLPGVE-VRIVD-EDGRELPPG--EVGEIVVRGPNVMKGYWNDPEA 315
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228909 425 NKETFAGGWFHSGDIAVKHPDNYIEIKDRSKDVIISGGENISSVEVENVVYHHPAVLEASVVARPDERWQESPCAFVTLK 504
Cdd:COG0318 316 TAEAFRDGWLRTGDLGRLDEDGYLYIVGRKKDMIISGGENVYPAEVEEVLAAHPGVAEAAVVGVPDEKWGERVVAFVVLR 395
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*..
gi 15228909 505 SdyekhDQNKLAQDIMKFCREKLPAYWVPKSVVF-GPLPKTATGKIQKHILRTKAKE 560
Cdd:COG0318 396 P-----GAELDAEELRAFLRERLARYKVPRRVEFvDELPRTASGKIDRRALRERYAA 447
|
|
| ttLC_FACS_like |
cd05915 |
Fatty acyl-CoA synthetases similar to LC-FACS from Thermus thermophiles; This family includes ... |
22-555 |
4.05e-145 |
|
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: 428.39 E-value: 4.05e-145
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228909 22 LTPLWFLDRAAVVHPTRKsviHGSREYTWRQTYDRCRRLASALADRSIGPGSTVAIIAPNIPAMYEAHFGVPMCGAVLNC 101
Cdd:cd05915 2 ERAAALFGRKEVVSRLHT---GEVHRTTYAEVYQRARRLMGGLRALGVGVGDRVATLGFNHFRHLEAYFAVPGMGAVLHT 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228909 102 VNIRLNAPTVAFLLSHSQSSVIMVDQEFFTLAEDSLRLMEekagssfkrpllivigDHTCAPESLNRALskgaiEYEDFL 181
Cdd:cd05915 79 ANPRLSPKEIAYILNHAEDKVLLFDPNLLPLVEAIRGELK----------------TVQHFVVMDEKAP-----EGYLAY 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228909 182 ATGDPNYPWQPPADEWQSIALGYTSGTTASPKGVVLHHRGAYIMALSNPLIWGMQDGA--VYLWTLPMFHCNGWCFPWSL 259
Cdd:cd05915 138 EEALGEEADPVRVPERAACGMAYTTGTTGLPKGVVYSHRALVLHSLAASLVDGTALSEkdVVLPVVPMFHVNAWCLPYAA 217
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228909 260 AVLSGTSICLRQVTAKEV-YSMIAKYKVTHFCAAPVVLNAIVNApKEDTILPLPHTVHVMTAGAAPPPSVLFSMNQKGFR 338
Cdd:cd05915 218 TLVGAKQVLPGPRLDPASlVELFDGEGVTFTAGVPTVWLALADY-LESTGHRLKTLRRLVVGGSAAPRSLIARFERMGVE 296
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228909 339 VAHTYGLSETYGPSTVCAWKPEWDSLPPETQAKLNARQGVRYTGmEQLDVIDTQTgKPVPADGKTAGEIVFRGNMVMKGY 418
Cdd:cd05915 297 VRQGYGLTETSPVVVQNFVKSHLESLSEEEKLTLKAKTGLPIPL-VRLRVADEEG-RPVPKDGKALGEVQLKGPWITGGY 374
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228909 419 LKNPEANK-ETFAGGWFHSGDIAVKHPDNYIEIKDRSKDVIISGGENISSVEVENVVYHHPAVLEASVVARPDERWQESP 497
Cdd:cd05915 375 YGNEEATRsALTPDGFFRTGDIAVWDEEGYVEIKDRLKDLIKSGGEWISSVDLENALMGHPKVKEAAVVAIPHPKWQERP 454
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228909 498 CAFVTLKSDYEKHdqnklaQDIMKFCREKLPAY-WVPKSVVFGP-LPKTATGKIQKHILR 555
Cdd:cd05915 455 LAVVVPRGEKPTP------EELNEHLLKAGFAKwQLPDAYVFAEeIPRTSAGKFLKRALR 508
|
|
| PRK06187 |
PRK06187 |
long-chain-fatty-acid--CoA ligase; Validated |
27-562 |
5.09e-143 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 235730 [Multi-domain] Cd Length: 521 Bit Score: 423.44 E-value: 5.09e-143
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228909 27 FLDRAAVVHPTRKSVIHGSREYTWRQTYDRCRRLASALADRSIGPGSTVAIIAPNIPAMYEAHFGVPMCGAVLNCVNIRL 106
Cdd:PRK06187 11 ILRHGARKHPDKEAVYFDGRRTTYAELDERVNRLANALRALGVKKGDRVAVFDWNSHEYLEAYFAVPKIGAVLHPINIRL 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228909 107 NAPTVAFLLSHSQSSVIMVDQEFFTLAEDSLRLMEEkagssfkRPLLIVIGDHTCAPESlnralsKGAIEYEDFLATGDP 186
Cdd:PRK06187 91 KPEEIAYILNDAEDRVVLVDSEFVPLLAAILPQLPT-------VRTVIVEGDGPAAPLA------PEVGEYEELLAAASD 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228909 187 NYPWqPPADEWQSIALGYTSGTTASPKGVVLHHRGAY--IMALSNPLIWGMQDgaVYLWTLPMFHCNGWCFPWsLAVLSG 264
Cdd:PRK06187 158 TFDF-PDIDENDAAAMLYTSGTTGHPKGVVLSHRNLFlhSLAVCAWLKLSRDD--VYLVIVPMFHVHAWGLPY-LALMAG 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228909 265 TSICL-RQVTAKEVYSMIAKYKVTHFCAAPVVLNAIVNAPkedtiLPLPH---TVHVMTAGAAP-PPSVLFSMNQK-GFR 338
Cdd:PRK06187 234 AKQVIpRRFDPENLLDLIETERVTFFFAVPTIWQMLLKAP-----RAYFVdfsSLRLVIYGGAAlPPALLREFKEKfGID 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228909 339 VAHTYGLSETYGpsTVCAWKPEWDSLPpetQAKLNARQGVRYTGMEqLDVIDTQtGKPVPADGKTAGEIVFRGNMVMKGY 418
Cdd:PRK06187 309 LVQGYGMTETSP--VVSVLPPEDQLPG---QWTKRRSAGRPLPGVE-ARIVDDD-GDELPPDGGEVGEIIVRGPWLMQGY 381
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228909 419 LKNPEANKETFAGGWFHSGDIAVKHPDNYIEIKDRSKDVIISGGENISSVEVENVVYHHPAVLEASVVARPDERWQESPC 498
Cdd:PRK06187 382 WNRPEATAETIDGGWLHTGDVGYIDEDGYLYITDRIKDVIISGGENIYPRELEDALYGHPAVAEVAVIGVPDEKWGERPV 461
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 15228909 499 AFVTLKSDyEKHDqnklAQDIMKFCREKLPAYWVPKSVVFGP-LPKTATGKIQKHILRTKAKEMG 562
Cdd:PRK06187 462 AVVVLKPG-ATLD----AKELRAFLRGRLAKFKLPKRIAFVDeLPRTSVGKILKRVLREQYAEGK 521
|
|
| ttLC_FACS_AlkK_like |
cd12119 |
Fatty acyl-CoA synthetases similar to LC-FACS from Thermus thermophiles; This family includes ... |
27-555 |
6.46e-141 |
|
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: 417.80 E-value: 6.46e-141
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228909 27 FLDRAAVVHPTRKSV----IHGSREYTWRQTYDRCRRLASALADRSIGPGSTVAIIAPNIPAMYEAHFGVPMCGAVLNCV 102
Cdd:cd12119 1 LLEHAARLHGDREIVsrthEGEVHRYTYAEVAERARRLANALRRLGVKPGDRVATLAWNTHRHLELYYAVPGMGAVLHTI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228909 103 NIRLNAPTVAFLLSHSQSSVIMVDQEFftlaedsLRLMEEKAGSSFKRPLLIVIGDHTCAPESLNralsKGAIEYEDFLA 182
Cdd:cd12119 81 NPRLFPEQIAYIINHAEDRVVFVDRDF-------LPLLEAIAPRLPTVEHVVVMTDDAAMPEPAG----VGVLAYEELLA 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228909 183 TGDPNYPWqPPADEWQSIALGYTSGTTASPKGVVLHHRGAYI--MALSNPLIWGMQDGAVYLWTLPMFHCNGWCFPWSlA 260
Cdd:cd12119 150 AESPEYDW-PDFDENTAAAICYTSGTTGNPKGVVYSHRSLVLhaMAALLTDGLGLSESDVVLPVVPMFHVNAWGLPYA-A 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228909 261 VLSGTSICL--RQVTAKEVYSMIAKYKVTHFCAAPVVLNAIVNAPkEDTILPLPHTVHVMTAGAAPPPSVLFSMNQKGFR 338
Cdd:cd12119 228 AMVGAKLVLpgPYLDPASLAELIEREGVTFAAGVPTVWQGLLDHL-EANGRDLSSLRRVVIGGSAVPRSLIEAFEERGVR 306
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228909 339 VAHTYGLSETYGPSTVCAWKPEWDSLPPETQAKLNARQGVRYTGMEqLDVIDTQtGKPVPADGKTAGEIVFRGNMVMKGY 418
Cdd:cd12119 307 VIHAWGMTETSPLGTVARPPSEHSNLSEDEQLALRAKQGRPVPGVE-LRIVDDD-GRELPWDGKAVGELQVRGPWVTKSY 384
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228909 419 LKNPEANKETFAGGWFHSGDIAVKHPDNYIEIKDRSKDVIISGGENISSVEVENVVYHHPAVLEASVVARPDERWQESPC 498
Cdd:cd12119 385 YKNDEESEALTEDGWLRTGDVATIDEDGYLTITDRSKDVIKSGGEWISSVELENAIMAHPAVAEAAVIGVPHPKWGERPL 464
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*...
gi 15228909 499 AFVTLKSdyekhDQNKLAQDIMKFCREKLPAYWVPKSVVFGP-LPKTATGKIQKHILR 555
Cdd:cd12119 465 AVVVLKE-----GATVTAEELLEFLADKVAKWWLPDDVVFVDeIPKTSTGKIDKKALR 517
|
|
| FACL_FadD13-like |
cd17631 |
fatty acyl-CoA synthetase, including FadD13; This family contains fatty acyl-CoA synthetases, ... |
28-551 |
9.52e-122 |
|
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: 365.78 E-value: 9.52e-122
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228909 28 LDRAAVVHPTRKSVIHGSREYTWRQTYDRCRRLASALADRSIGPGSTVAIIAPNIPAMYEAHFGVPMCGAVLNCVNIRLN 107
Cdd:cd17631 1 LRRRARRHPDRTALVFGGRSLTYAELDERVNRLAHALRALGVAKGDRVAVLSKNSPEFLELLFAAARLGAVFVPLNFRLT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228909 108 APTVAFLLSHSQSSVimvdqefftLAEDSLRLMeekagssfkrpllivigdhtcapeslnralskgaieyedflatgdpn 187
Cdd:cd17631 81 PPEVAYILADSGAKV---------LFDDLALLM----------------------------------------------- 104
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228909 188 ypwqppadewqsialgYTSGTTASPKGVVLHHRGAYIMALSNPLIWGMQDGAVYLWTLPMFHC---NGWCFPwsLAVLSG 264
Cdd:cd17631 105 ----------------YTSGTTGRPKGAMLTHRNLLWNAVNALAALDLGPDDVLLVVAPLFHIgglGVFTLP--TLLRGG 166
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228909 265 TSICLRQVTAKEVYSMIAKYKVTHFCAAPVVLNAIVNAPKEDTiLPLPHTVHVMTAGAAPPPSVLFSMNQKGFRVAHTYG 344
Cdd:cd17631 167 TVVILRKFDPETVLDLIERHRVTSFFLVPTMIQALLQHPRFAT-TDLSSLRAVIYGGAPMPERLLRALQARGVKFVQGYG 245
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228909 345 LSETYGPSTVcawkpewdsLPPETQAKLNARQGVRYTGMEqLDVIDtQTGKPVPADgkTAGEIVFRGNMVMKGYLKNPEA 424
Cdd:cd17631 246 MTETSPGVTF---------LSPEDHRRKLGSAGRPVFFVE-VRIVD-PDGREVPPG--EVGEIVVRGPHVMAGYWNRPEA 312
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228909 425 NKETFAGGWFHSGDIAVKHPDNYIEIKDRSKDVIISGGENISSVEVENVVYHHPAVLEASVVARPDERWQESPCAFVTLK 504
Cdd:cd17631 313 TAAAFRDGWFHTGDLGRLDEDGYLYIVDRKKDMIISGGENVYPAEVEDVLYEHPAVAEVAVIGVPDEKWGEAVVAVVVPR 392
|
490 500 510 520
....*....|....*....|....*....|....*....|....*...
gi 15228909 505 SdyekhDQNKLAQDIMKFCREKLPAYWVPKSVVFGP-LPKTATGKIQK 551
Cdd:cd17631 393 P-----GAELDEDELIAHCRERLARYKIPKSVEFVDaLPRNATGKILK 435
|
|
| PRK08316 |
PRK08316 |
acyl-CoA synthetase; Validated |
27-560 |
1.23e-96 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 181381 [Multi-domain] Cd Length: 523 Bit Score: 304.16 E-value: 1.23e-96
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228909 27 FLDRAAVVHPTRKSVIHGSREYTWRQTYDRCRRLASALADRSIGPGSTVAIIAPNIPAMYEAHFGVPMCGAVLNCVNIRL 106
Cdd:PRK08316 16 ILRRSARRYPDKTALVFGDRSWTYAELDAAVNRVAAALLDLGLKKGDRVAALGHNSDAYALLWLACARAGAVHVPVNFML 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228909 107 NAPTVAFLLSHSQSSVIMVDQEFFTLAEDSLRLMeekaGSSFKRPLLIVIGdhtcapeslnRALSKGAIEYEDFLATGDP 186
Cdd:PRK08316 96 TGEELAYILDHSGARAFLVDPALAPTAEAALALL----PVDTLILSLVLGG----------REAPGGWLDFADWAEAGSV 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228909 187 NYPWQPPADEwQSIALGYTSGTTASPKGVVLHHRGayimalsnpLIW---------GMQDGAVYLWTLPMFHCNGW-CF- 255
Cdd:PRK08316 162 AEPDVELADD-DLAQILYTSGTESLPKGAMLTHRA---------LIAeyvscivagDMSADDIPLHALPLYHCAQLdVFl 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228909 256 -PWSLavLSGTSICLRQVTAKEVYSMIAKYKVTHFCAAPVVLNAIVNAPKEDTilplphtvHVMTA------GAAP-PPS 327
Cdd:PRK08316 232 gPYLY--VGATNVILDAPDPELILRTIEAERITSFFAPPTVWISLLRHPDFDT--------RDLSSlrkgyyGASImPVE 301
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228909 328 VLFSMNQK--GFRVAHTYGLSETyGP-STVcawkpewdsLPPETQAKLNARQGVRYTGMEqLDVIDTQtGKPVPADgkTA 404
Cdd:PRK08316 302 VLKELRERlpGLRFYNCYGQTEI-APlATV---------LGPEEHLRRPGSAGRPVLNVE-TRVVDDD-GNDVAPG--EV 367
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228909 405 GEIVFRGNMVMKGYLKNPEANKETFAGGWFHSGDIAVKHPDNYIEIKDRSKDVIISGGENISSVEVENVVYHHPAVLEAS 484
Cdd:PRK08316 368 GEIVHRSPQLMLGYWDDPEKTAEAFRGGWFHSGDLGVMDEEGYITVVDRKKDMIKTGGENVASREVEEALYTHPAVAEVA 447
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 15228909 485 VVARPDERWQESPCAFVTLKSDYEkhdqnKLAQDIMKFCREKLPAYWVPKSVVFGP-LPKTATGKIQKHILRTKAKE 560
Cdd:PRK08316 448 VIGLPDPKWIEAVTAVVVPKAGAT-----VTEDELIAHCRARLAGFKVPKRVIFVDeLPRNPSGKILKRELRERYAG 519
|
|
| AMP-binding |
pfam00501 |
AMP-binding enzyme; |
28-461 |
2.00e-96 |
|
AMP-binding enzyme;
Pssm-ID: 459834 [Multi-domain] Cd Length: 417 Bit Score: 300.00 E-value: 2.00e-96
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228909 28 LDRAAVVHPTRKSVIHGS-REYTWRQTYDRCRRLASALADRSIGPGSTVAIIAPNIPAMYEAHFGVPMCGAVLNCVNIRL 106
Cdd:pfam00501 1 LERQAARTPDKTALEVGEgRRLTYRELDERANRLAAGLRALGVGKGDRVAILLPNSPEWVVAFLACLKAGAVYVPLNPRL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228909 107 NAPTVAFLLSHSQSSVIMVDQEFftLAEDSLRLMEEKagssfKRPLLIVIGDHTcapeslnralskGAIEYEDFLATGDP 186
Cdd:pfam00501 81 PAEELAYILEDSGAKVLITDDAL--KLEELLEALGKL-----EVVKLVLVLDRD------------PVLKEEPLPEEAKP 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228909 187 NYPWQ---PPADEWQSIALGYTSGTTASPKGVVLHHRGAYIMALS----NPLIWGMQDGAVYLWTLPMFHCNGWCFPWSL 259
Cdd:pfam00501 142 ADVPPpppPPPDPDDLAYIIYTSGTTGKPKGVMLTHRNLVANVLSikrvRPRGFGLGPDDRVLSTLPLFHDFGLSLGLLG 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228909 260 AVLSGTSICLRQ----VTAKEVYSMIAKYKVTHFCAAPVVLNAIVNAPKEDTILpLPHTVHVMTAGAAPPPSVLFSMNQK 335
Cdd:pfam00501 222 PLLAGATVVLPPgfpaLDPAALLELIERYKVTVLYGVPTLLNMLLEAGAPKRAL-LSSLRLVLSGGAPLPPELARRFREL 300
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228909 336 -GFRVAHTYGLSETYGPSTVCawkpewdsLPPETQAKLNARQGVRYTGMEqLDVIDTQTGKPVPaDGKTaGEIVFRGNMV 414
Cdd:pfam00501 301 fGGALVNGYGLTETTGVVTTP--------LPLDEDLRSLGSVGRPLPGTE-VKIVDDETGEPVP-PGEP-GELCVRGPGV 369
|
410 420 430 440
....*....|....*....|....*....|....*....|....*...
gi 15228909 415 MKGYLKNPEANKETF-AGGWFHSGDIAVKHPDNYIEIKDRSKDVIISG 461
Cdd:pfam00501 370 MKGYLNDPELTAEAFdEDGWYRTGDLGRRDEDGYLEIVGRKKDQIKLG 417
|
|
| AFD_class_I |
cd04433 |
Adenylate forming domain, Class I, also known as the ANL superfamily; This family is known as ... |
204-550 |
1.13e-93 |
|
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: 289.96 E-value: 1.13e-93
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228909 204 YTSGTTASPKGVVLHHRGAYIMALSNPLIWGMQDGAVYLWTLPMFHCNGWCFPWSLAVLSGTSICLRQVTAKEVYSMIAK 283
Cdd:cd04433 7 YTSGTTGKPKGVVLSHRNLLAAAAALAASGGLTEGDVFLSTLPLFHIGGLFGLLGALLAGGTVVLLPKFDPEAALELIER 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228909 284 YKVTHFCAAPVVLNAIVNAPKEDTiLPLPHTVHVMTAGAAPPPSVL--FsMNQKGFRVAHTYGLSETygPSTVCAWKPEW 361
Cdd:cd04433 87 EKVTILLGVPTLLARLLKAPESAG-YDLSSLRALVSGGAPLPPELLerF-EEAPGIKLVNGYGLTET--GGTVATGPPDD 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228909 362 DSLPPETQaklnarqGVRYTGMEqLDVIDTQTGkPVPADGktAGEIVFRGNMVMKGYLKNPEANKETFAGGWFHSGDIAV 441
Cdd:cd04433 163 DARKPGSV-------GRPVPGVE-VRIVDPDGG-ELPPGE--IGELVVRGPSVMKGYWNNPEATAAVDEDGWYRTGDLGR 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228909 442 KHPDNYIEIKDRSKDVIISGGENISSVEVENVVYHHPAVLEASVVARPDERWQESPCAFVTLksdyeKHDQNKLAQDIMK 521
Cdd:cd04433 232 LDEDGYLYIVGRLKDMIKSGGENVYPAEVEAVLLGHPGVAEAAVVGVPDPEWGERVVAVVVL-----RPGADLDAEELRA 306
|
330 340 350
....*....|....*....|....*....|
gi 15228909 522 FCREKLPAYWVPKSVVFGP-LPKTATGKIQ 550
Cdd:cd04433 307 HVRERLAPYKVPRRVVFVDaLPRTASGKID 336
|
|
| FC-FACS_FadD_like |
cd05936 |
Prokaryotic long-chain fatty acid CoA synthetases similar to Escherichia coli FadD; This ... |
25-555 |
1.98e-93 |
|
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: 294.09 E-value: 1.98e-93
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228909 25 LWFLDRAAVVHPTRKSVIHGSREYTWRQTYDRCRRLASALADRSIGPGSTVAIIAPNIPAMYEAHFGVPMCGAVLNCVNI 104
Cdd:cd05936 2 ADLLEEAARRFPDKTALIFMGRKLTYRELDALAEAFAAGLQNLGVQPGDRVALMLPNCPQFPIAYFGALKAGAVVVPLNP 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228909 105 RLNAPTVAFLLSHSQSSVIMVDQEFftlaedslrlmeekagssfkrpllivigdhtcapeslnralskgaieyEDFLATG 184
Cdd:cd05936 82 LYTPRELEHILNDSGAKALIVAVSF------------------------------------------------TDLLAAG 113
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228909 185 DPNYPWQPPADEwqSIA-LGYTSGTTASPKGVVLHHRGAY-----IMALSNPLIWGMQdgaVYLWTLPMFHCNGWCFPWS 258
Cdd:cd05936 114 APLGERVALTPE--DVAvLQYTSGTTGVPKGAMLTHRNLVanalqIKAWLEDLLEGDD---VVLAALPLFHVFGLTVALL 188
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228909 259 LAVLSG-TSICLRQVTAKEVYSMIAKYKVTHFCAAPVVLNAIVNAPKEDTILPlpHTVHVMTAGAAP-PPSVLFSMNQK- 335
Cdd:cd05936 189 LPLALGaTIVLIPRFRPIGVLKEIRKHRVTIFPGVPTMYIALLNAPEFKKRDF--SSLRLCISGGAPlPVEVAERFEELt 266
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228909 336 GFRVAHTYGLSETyGPSTVCawkpewdslppetqaklNARQGVRYTGM-------EQLDVIDTQtGKPVPaDGKTaGEIV 408
Cdd:cd05936 267 GVPIVEGYGLTET-SPVVAV-----------------NPLDGPRKPGSigiplpgTEVKIVDDD-GEELP-PGEV-GELW 325
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228909 409 FRGNMVMKGYLKNPEANKETFAGGWFHSGDIAVKHPDNYIEIKDRSKDVIISGGENISSVEVENVVYHHPAVLEASVVAR 488
Cdd:cd05936 326 VRGPQVMKGYWNRPEETAEAFVDGWLRTGDIGYMDEDGYFFIVDRKKDMIIVGGFNVYPREVEEVLYEHPAVAEAAVVGV 405
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 15228909 489 PDERWQESPCAFVTLKSdyekhDQNKLAQDIMKFCREKLPAYWVPKSVVFGP-LPKTATGKIQKHILR 555
Cdd:cd05936 406 PDPYSGEAVKAFVVLKE-----GASLTEEEIIAFCREQLAGYKVPRQVEFRDeLPKSAVGKILRRELR 468
|
|
| PRK06018 |
PRK06018 |
putative acyl-CoA synthetase; Provisional |
28-560 |
4.80e-91 |
|
putative acyl-CoA synthetase; Provisional
Pssm-ID: 235673 [Multi-domain] Cd Length: 542 Bit Score: 290.11 E-value: 4.80e-91
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228909 28 LDRAAVVHPTRKSV-------IHGSreyTWRQTYDRCRRLASALADRSIGPGSTVAIIAPNIPAMYEAHFGVPMCGAVLN 100
Cdd:PRK06018 16 IDHAARIHGNREVVtrsvegpIVRT---TYAQIHDRALKVSQALDRDGIKLGDRVATIAWNTWRHLEAWYGIMGIGAICH 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228909 101 CVNIRLNAPTVAFLLSHSQSSVIMVDQEFftlaedsLRLMEEKAGSSFKRPLLIVIGDHTCAPESLnralSKGAIEYEDF 180
Cdd:PRK06018 93 TVNPRLFPEQIAWIINHAEDRVVITDLTF-------VPILEKIADKLPSVERYVVLTDAAHMPQTT----LKNAVAYEEW 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228909 181 LATGDPNYPWQPpADEWQSIALGYTSGTTASPKGVVLHHRGAYIMAL--SNPLIWGMQDGAVYLWTLPMFHCNGWCFPWS 258
Cdd:PRK06018 162 IAEADGDFAWKT-FDENTAAGMCYTSGTTGDPKGVLYSHRSNVLHALmaNNGDALGTSAADTMLPVVPLFHANSWGIAFS 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228909 259 lAVLSGTSICL--RQVTAKEVYSMIAKYKVTHFCAAPVVLNAIVNApKEDTILPLPHTVHVMTAGAAPPPSVLFSMNQKG 336
Cdd:PRK06018 241 -APSMGTKLVMpgAKLDGASVYELLDTEKVTFTAGVPTVWLMLLQY-MEKEGLKLPHLKMVVCGGSAMPRSMIKAFEDMG 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228909 337 FRVAHTYGLSETYGPSTVCAWKPEWDSLPPETQAKLNARQGVRYTGMEqLDVIDTQtGKPVPADGKTAGEIVFRGNMVMK 416
Cdd:PRK06018 319 VEVRHAWGMTEMSPLGTLAALKPPFSKLPGDARLDVLQKQGYPPFGVE-MKITDDA-GKELPWDGKTFGRLKVRGPAVAA 396
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228909 417 GYLKnpeANKETF-AGGWFHSGDIAVKHPDNYIEIKDRSKDVIISGGENISSVEVENVVYHHPAVLEASVVARPDERWQE 495
Cdd:PRK06018 397 AYYR---VDGEILdDDGFFDTGDVATIDAYGYMRITDRSKDVIKSGGEWISSIDLENLAVGHPKVAEAAVIGVYHPKWDE 473
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 15228909 496 SPCAFVTLKSdyekhDQNKLAQDIMKFCREKLPAYWVPKSVVF-GPLPKTATGKIQKHILRTKAKE 560
Cdd:PRK06018 474 RPLLIVQLKP-----GETATREEILKYMDGKIAKWWMPDDVAFvDAIPHTATGKILKTALREQFKD 534
|
|
| PRK07008 |
PRK07008 |
long-chain-fatty-acid--CoA ligase; Validated |
48-560 |
3.49e-88 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 235908 [Multi-domain] Cd Length: 539 Bit Score: 282.75 E-value: 3.49e-88
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228909 48 YTWRQTYDRCRRLASALADRSIGPGSTVAIIAPNIPAMYEAHFGVPMCGAVLNCVNIRLNAPTVAFLLSHSQSSVIMVDQ 127
Cdd:PRK07008 40 YTYRDCERRAKQLAQALAALGVEPGDRVGTLAWNGYRHLEAYYGVSGSGAVCHTINPRLFPEQIAYIVNHAEDRYVLFDL 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228909 128 EFftlaedsLRLMEEKAGSSFKRPLLIVIGDHTCAPESLNRALSkgaieYEDFLATGDPNYPWqPPADEWQSIALGYTSG 207
Cdd:PRK07008 120 TF-------LPLVDALAPQCPNVKGWVAMTDAAHLPAGSTPLLC-----YETLVGAQDGDYDW-PRFDENQASSLCYTSG 186
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228909 208 TTASPKGVVLHHRG----AYIMALSNPLIWGMQDgaVYLWTLPMFHCNGWCFPWSLAvLSGTSICL--RQVTAKEVYSMI 281
Cdd:PRK07008 187 TTGNPKGALYSHRStvlhAYGAALPDAMGLSARD--AVLPVVPMFHVNAWGLPYSAP-LTGAKLVLpgPDLDGKSLYELI 263
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228909 282 AKYKVTHFCAAPVVLNAIVNAPKEDTIL--PLPHTVhvmTAGAAPPPSVLFSMNQK-GFRVAHTYGLSETYGPSTVCAWK 358
Cdd:PRK07008 264 EAERVTFSAGVPTVWLGLLNHMREAGLRfsTLRRTV---IGGSACPPAMIRTFEDEyGVEVIHAWGMTEMSPLGTLCKLK 340
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228909 359 PEWDSLPPETQAKLNARQGVRYTGMEqLDVIDTQtGKPVPADGKTAGEIVFRGNMVMKGYLKNPEAnkeTFAGGWFHSGD 438
Cdd:PRK07008 341 WKHSQLPLDEQRKLLEKQGRVIYGVD-MKIVGDD-GRELPWDGKAFGDLQVRGPWVIDRYFRGDAS---PLVDGWFPTGD 415
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228909 439 IAVKHPDNYIEIKDRSKDVIISGGENISSVEVENVVYHHPAVLEASVVARPDERWQESPCAFVTLKSDYEkhdqnkLAQD 518
Cdd:PRK07008 416 VATIDADGFMQITDRSKDVIKSGGEWISSIDIENVAVAHPAVAEAACIACAHPKWDERPLLVVVKRPGAE------VTRE 489
|
490 500 510 520
....*....|....*....|....*....|....*....|....
gi 15228909 519 -IMKFCREKLPAYWVPKSVVF-GPLPKTATGKIQKHILRTKAKE 560
Cdd:PRK07008 490 eLLAFYEGKVAKWWIPDDVVFvDAIPHTATGKLQKLKLREQFRD 533
|
|
| PRK07656 |
PRK07656 |
long-chain-fatty-acid--CoA ligase; Validated |
28-557 |
6.41e-87 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236072 [Multi-domain] Cd Length: 513 Bit Score: 278.33 E-value: 6.41e-87
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228909 28 LDRAAVVHPTRKSVIHGSREYTWRQTYDRCRRLASALADRSIGPGSTVAIIAPNIPAMYEAHFGVPMCGAVLNCVNIRLN 107
Cdd:PRK07656 11 LARAARRFGDKEAYVFGDQRLTYAELNARVRRAAAALAALGIGKGDRVAIWAPNSPHWVIAALGALKAGAVVVPLNTRYT 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228909 108 APTVAFLLSHSQSSVIMVDQEF---FTLAEDSLRLMEekagssfkrplLIVIgdhtCAPESlNRALSKGAIEYEDFLATG 184
Cdd:PRK07656 91 ADEAAYILARGDAKALFVLGLFlgvDYSATTRLPALE-----------HVVI----CETEE-DDPHTEKMKTFTDFLAAG 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228909 185 DPNYpwQPPADEWQSIA-LGYTSGTTASPKGVVLHHRGAYimalSNPLIW----GMQDGAVYLWTLPMFHCNGWCFPWSL 259
Cdd:PRK07656 155 DPAE--RAPEVDPDDVAdILFTSGTTGRPKGAMLTHRQLL----SNAADWaeylGLTEGDRYLAANPFFHVFGYKAGVNA 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228909 260 AVLSG-TSICLRQVTAKEVYSMIAKYKVTHFCAAPVVLNAIVNAPK-EDTILplpHTVHV-MTAGAAPPPSVLFSMNQK- 335
Cdd:PRK07656 229 PLMRGaTILPLPVFDPDEVFRLIETERITVLPGPPTMYNSLLQHPDrSAEDL---SSLRLaVTGAASMPVALLERFESEl 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228909 336 GFR-VAHTYGLSETYGPSTVCawkpewdslPPETQAKLNARQ-GVRYTGMEqLDVIDTQtGKPVPADgkTAGEIVFRGNM 413
Cdd:PRK07656 306 GVDiVLTGYGLSEASGVTTFN---------RLDDDRKTVAGTiGTAIAGVE-NKIVNEL-GEEVPVG--EVGELLVRGPN 372
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228909 414 VMKGYLKNPEANKETF-AGGWFHSGDIAVKHPDNYIEIKDRSKDVIISGGENISSVEVENVVYHHPAVLEASVVARPDER 492
Cdd:PRK07656 373 VMKGYYDDPEATAAAIdADGWLHTGDLGRLDEEGYLYIVDRKKDMFIVGGFNVYPAEVEEVLYEHPAVAEAAVIGVPDER 452
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 15228909 493 WQESPCAFVTLksdyeKHDQNKLAQDIMKFCREKLPAYWVPKSVVF-GPLPKTATGKIQKHILRTK 557
Cdd:PRK07656 453 LGEVGKAYVVL-----KPGAELTEEELIAYCREHLAKYKVPRSIEFlDELPKNATGKVLKRALREK 513
|
|
| Acs |
COG0365 |
Acyl-coenzyme A synthetase/AMP-(fatty) acid ligase [Lipid transport and metabolism]; |
27-569 |
2.16e-84 |
|
Acyl-coenzyme A synthetase/AMP-(fatty) acid ligase [Lipid transport and metabolism];
Pssm-ID: 440134 [Multi-domain] Cd Length: 565 Bit Score: 273.53 E-value: 2.16e-84
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228909 27 FLDRAAVVHPTRKSVIHGS-----REYTWRQTYDRCRRLASALADRSIGPGSTVAIIAPNIPAMYEAHFGVPMCGAVLNC 101
Cdd:COG0365 14 CLDRHAEGRGDKVALIWEGedgeeRTLTYAELRREVNRFANALRALGVKKGDRVAIYLPNIPEAVIAMLACARIGAVHSP 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228909 102 VNIRLNAPTVAFLLSHSQSSVIMVDQEFFTlAEDSLRLME--EKAGSSFKRPLLIVIGDHTCAPESLnralsKGAIEYED 179
Cdd:COG0365 94 VFPGFGAEALADRIEDAEAKVLITADGGLR-GGKVIDLKEkvDEALEELPSLEHVIVVGRTGADVPM-----EGDLDWDE 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228909 180 FLATGDPNYPWQP-PADEwqsIA-LGYTSGTTASPKGVVLHHRGAYI-MALSNPLIWGMQDGAVYLWTLP----MFHCNG 252
Cdd:COG0365 168 LLAAASAEFEPEPtDADD---PLfILYTSGTTGKPKGVVHTHGGYLVhAATTAKYVLDLKPGDVFWCTADigwaTGHSYI 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228909 253 WCFPWslavLSGTSICLRQ-----VTAKEVYSMIAKYKVTHFCAAPVVLNAIVnapKEDTILPLPHTV----HVMTAG-A 322
Cdd:COG0365 245 VYGPL----LNGATVVLYEgrpdfPDPGRLWELIEKYGVTVFFTAPTAIRALM---KAGDEPLKKYDLsslrLLGSAGeP 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228909 323 APPPSVLFSMNQKGFRVAHTYGLSETYGPstVCAWKPEWDSLPPETqaklnarqGVRYTGMEqLDVIDTQtGKPVPADgk 402
Cdd:COG0365 318 LNPEVWEWWYEAVGVPIVDGWGQTETGGI--FISNLPGLPVKPGSM--------GKPVPGYD-VAVVDED-GNPVPPG-- 383
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228909 403 TAGEIVFRGNM--VMKGYLKNPEANKETFAG---GWFHSGDIAVKHPDNYIEIKDRSKDVIISGGENISSVEVENVVYHH 477
Cdd:COG0365 384 EEGELVIKGPWpgMFRGYWNDPERYRETYFGrfpGWYRTGDGARRDEDGYFWILGRSDDVINVSGHRIGTAEIESALVSH 463
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228909 478 PAVLEASVVARPDERWQESPCAFVTLKSDYEKHDQnkLAQDIMKFCREKLPAYWVPKSVVFGP-LPKTATGKIQKHILRT 556
Cdd:COG0365 464 PAVAEAAVVGVPDEIRGQVVKAFVVLKPGVEPSDE--LAKELQAHVREELGPYAYPREIEFVDeLPKTRSGKIMRRLLRK 541
|
570
....*....|...
gi 15228909 557 KAKEMGPVPRSRL 569
Cdd:COG0365 542 IAEGRPLGDTSTL 554
|
|
| FACL_DitJ_like |
cd05934 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
46-555 |
2.98e-78 |
|
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: 252.98 E-value: 2.98e-78
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228909 46 REYTWRQTYDRCRRLASALADRSIGPGSTVAIIAPNIPAMYEAHFGVPMCGAVLNCVNIRLNAPTVAFLLSHSQSSVIMV 125
Cdd:cd05934 2 RRWTYAELLRESARIAAALAALGIRPGDRVALMLDNCPEFLFAWFALAKLGAVLVPINTALRGDELAYIIDHSGAQLVVV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228909 126 DqefftlaedslrlmeekagssfkrpllivigdhtcapeslnralskgaieyedflatgdpnypwqpPAdewqsiALGYT 205
Cdd:cd05934 82 D------------------------------------------------------------------PA------SILYT 89
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228909 206 SGTTASPKGVVLHHRGAYIMALSNPLIWGMQDGAVYLWTLPMFHCNGWCFPWSLAVLSGTSICL-RQVTAKEVYSMIAKY 284
Cdd:cd05934 90 SGTTGPPKGVVITHANLTFAGYYSARRFGLGEDDVYLTVLPLFHINAQAVSVLAALSVGATLVLlPRFSASRFWSDVRRY 169
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228909 285 KVTHFCAAPVVLNAIVNAPKEDTilPLPHTVHVmtAGAAPPPSVL---FSmNQKGFRVAHTYGLSETygpsTVCAWKPEW 361
Cdd:cd05934 170 GATVTNYLGAMLSYLLAQPPSPD--DRAHRLRA--AYGAPNPPELheeFE-ERFGVRLLEGYGMTET----IVGVIGPRD 240
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228909 362 DSLPPETQAKlnARQGVrytgmeQLDVIDTQtGKPVPADgkTAGEIVFR---GNMVMKGYLKNPEANKETFAGGWFHSGD 438
Cdd:cd05934 241 EPRRPGSIGR--PAPGY------EVRIVDDD-GQELPAG--EPGELVIRglrGWGFFKGYYNMPEATAEAMRNGWFHTGD 309
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228909 439 IAVKHPDNYIEIKDRSKDVIISGGENISSVEVENVVYHHPAVLEASVVARPDERWQESPCAFVTLksdyeKHDQNKLAQD 518
Cdd:cd05934 310 LGYRDADGFFYFVDRKKDMIRRRGENISSAEVERAILRHPAVREAAVVAVPDEVGEDEVKAVVVL-----RPGETLDPEE 384
|
490 500 510
....*....|....*....|....*....|....*...
gi 15228909 519 IMKFCREKLPAYWVPKSVVFGP-LPKTATGKIQKHILR 555
Cdd:cd05934 385 LFAFCEGQLAYFKVPRYIRFVDdLPKTPTEKVAKAQLR 422
|
|
| PRK03640 |
PRK03640 |
o-succinylbenzoate--CoA ligase; |
23-561 |
3.50e-75 |
|
o-succinylbenzoate--CoA ligase;
Pssm-ID: 235146 [Multi-domain] Cd Length: 483 Bit Score: 246.80 E-value: 3.50e-75
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228909 23 TPLWFLDRAAVVhPTRKSVIHGSREYTWRQTYDRCRRLASALADRSIGPGSTVAIIAPNIPAMYEAHFGVPMCGAVLNCV 102
Cdd:PRK03640 4 MPNWLKQRAFLT-PDRTAIEFEEKKVTFMELHEAVVSVAGKLAALGVKKGDRVALLMKNGMEMILVIHALQQLGAVAVLL 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228909 103 NIRLNAPTVAFLLSHSQSSVIMVDQEFftlaedslrLMEEKAGSSfkrpllivigdhtcapeslnralskgaIEYEDFLA 182
Cdd:PRK03640 83 NTRLSREELLWQLDDAEVKCLITDDDF---------EAKLIPGIS---------------------------VKFAELMN 126
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228909 183 TGDPNYPWQPPADEWQSIALGYTSGTTASPKGVVLHHRGAYIMALSNPLIWGMQDGAVYLWTLPMFHcngwcfpwslavL 262
Cdd:PRK03640 127 GPKEEAEIQEEFDLDEVATIMYTSGTTGKPKGVIQTYGNHWWSAVGSALNLGLTEDDCWLAAVPIFH------------I 194
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228909 263 SGTSICLRQVT------------AKEVYSMIAKYKVTHFCAAPVVLNAIVNAPKEDTilpLPHTVHVMTAGAAP-PPSVL 329
Cdd:PRK03640 195 SGLSILMRSVIygmrvvlvekfdAEKINKLLQTGGVTIISVVSTMLQRLLERLGEGT---YPSSFRCMLLGGGPaPKPLL 271
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228909 330 FSMNQKGFRVAHTYGLSETygPSTVCAWKPEwDSL-------PPETQAKLNARQgvrytgmeqldviDTQTGKPvpadgK 402
Cdd:PRK03640 272 EQCKEKGIPVYQSYGMTET--ASQIVTLSPE-DALtklgsagKPLFPCELKIEK-------------DGVVVPP-----F 330
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228909 403 TAGEIVFRGNMVMKGYLKNPEANKETFAGGWFHSGDIAVKHPDNYIEIKDRSKDVIISGGENISSVEVENVVYHHPAVLE 482
Cdd:PRK03640 331 EEGEIVVKGPNVTKGYLNREDATRETFQDGWFKTGDIGYLDEEGFLYVLDRRSDLIISGGENIYPAEIEEVLLSHPGVAE 410
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228909 483 ASVVARPDERWQESPCAFVTLKsdyEKHDQNKLAQdimkFCREKLPAYWVPKSVVF-GPLPKTATGKIQKHILRTKAKEM 561
Cdd:PRK03640 411 AGVVGVPDDKWGQVPVAFVVKS---GEVTEEELRH----FCEEKLAKYKVPKRFYFvEELPRNASGKLLRHELKQLVEEM 483
|
|
| Firefly_Luc_like |
cd05911 |
Firefly luciferase of light emitting insects and 4-Coumarate-CoA Ligase (4CL); This family ... |
45-550 |
8.06e-75 |
|
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: 245.97 E-value: 8.06e-75
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228909 45 SREYTWRQTYDRCRRLASALADRSIGPGSTVAIIAPNIPAMYEAHFGVPMCGAVLNCVNIRLNAPTVAFLLSHSQSSVIM 124
Cdd:cd05911 8 GKELTYAQLRTLSRRLAAGLRKLGLKKGDVVGIISPNSTYYPPVFLGCLFAGGIFSAANPIYTADELAHQLKISKPKVIF 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228909 125 VDQEFFtlaeDSLRLMEEKAGSSfkrPLLIVIGDHtcapesLNRALSKGAIEyEDFLATGDPNYPWQPPADEWQSIALGY 204
Cdd:cd05911 88 TDPDGL----EKVKEAAKELGPK---DKIIVLDDK------PDGVLSIEDLL-SPTLGEEDEDLPPPLKDGKDDTAAILY 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228909 205 TSGTTASPKGVVLHHRGAYIMALSNPLIWGMQDGA--VYLWTLPMFHCNG-WCFPWSLaVLSGTSICLRQVTAKEVYSMI 281
Cdd:cd05911 154 SSGTTGLPKGVCLSHRNLIANLSQVQTFLYGNDGSndVILGFLPLYHIYGlFTTLASL-LNGATVIIMPKFDSELFLDLI 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228909 282 AKYKVTHFCAAPVVLNAIVNAP---KEDtilpLPHTVHVMTAGAAPPPSVLFSMNQKGF--RVAHTYGLSETygpSTVCA 356
Cdd:cd05911 233 EKYKITFLYLVPPIAAALAKSPlldKYD----LSSLRVILSGGAPLSKELQELLAKRFPnaTIKQGYGMTET---GGILT 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228909 357 WKPEWD-------SLPPETQAKlnarqgvrytgmeqldVIDTQTGKPVPADGKtaGEIVFRGNMVMKGYLKNPEANKETF 429
Cdd:cd05911 306 VNPDGDdkpgsvgRLLPNVEAK----------------IVDDDGKDSLGPNEP--GEICVRGPQVMKGYYNNPEATKETF 367
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228909 430 -AGGWFHSGDIAVKHPDNYIEIKDRSKDVIISGGENISSVEVENVVYHHPAVLEASVVARPDERWQESPCAFVTLksdye 508
Cdd:cd05911 368 dEDGWLHTGDIGYFDEDGYLYIVDRKKELIKYKGFQVAPAELEAVLLEHPGVADAAVIGIPDEVSGELPRAYVVR----- 442
|
490 500 510 520
....*....|....*....|....*....|....*....|....
gi 15228909 509 KHDQNKLAQDIMKFCREKLPAY-WVPKSVVFGP-LPKTATGKIQ 550
Cdd:cd05911 443 KPGEKLTEKEVKDYVAKKVASYkQLRGGVVFVDeIPKSASGKIL 486
|
|
| FACL_fum10p_like |
cd05926 |
Subfamily of fatty acid CoA ligase (FACL) similar to Fum10p of Gibberella moniliformis; FACL ... |
36-555 |
1.02e-73 |
|
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: 243.37 E-value: 1.02e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228909 36 PTRKSVI--HGSREYTWRQTYDRCRRLASALADRSIGPGSTVAIIAPNIPAMYEAHFGVPMCGAVLNCVNIRLNAPTVAF 113
Cdd:cd05926 1 PDAPALVvpGSTPALTYADLAELVDDLARQLAALGIKKGDRVAIALPNGLEFVVAFLAAARAGAVVAPLNPAYKKAEFEF 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228909 114 LLSHSQSSVIMVDQEffTLAEDSlrlmeeKAGSSFKRPLLIVIGDhtcaPESLNRALSKGAIEYEDFLATGDPNYPWQPP 193
Cdd:cd05926 81 YLADLGSKLVLTPKG--ELGPAS------RAASKLGLAILELALD----VGVLIRAPSAESLSNLLADKKNAKSEGVPLP 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228909 194 ADewqsIALG-YTSGTTASPKGVVLHHRG--AYIMALSNPLIWGMQDGAVYlwTLPMFHCNGWcfpwsLAVL-----SGT 265
Cdd:cd05926 149 DD----LALIlHTSGTTGRPKGVPLTHRNlaASATNITNTYKLTPDDRTLV--VMPLFHVHGL-----VASLlstlaAGG 217
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228909 266 S-ICLRQVTAKEVYSMIAKYKVTHFCAAPVVLNAIVNAPKEDTILPLPHTVHVMTAGAAPPPSVLFSMnQKGFR--VAHT 342
Cdd:cd05926 218 SvVLPPRFSASTFWPDVRDYNATWYTAVPTIHQILLNRPEPNPESPPPKLRFIRSCSASLPPAVLEAL-EATFGapVLEA 296
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228909 343 YGLSETYGPSTVcawkpewDSLPPetqaklnarqGVRYTGmeqldvidtQTGKP-------VPADGKTA-----GEIVFR 410
Cdd:cd05926 297 YGMTEAAHQMTS-------NPLPP----------GPRKPG---------SVGKPvgvevriLDEDGEILppgvvGEICLR 350
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228909 411 GNMVMKGYLKNPEANKE-TFAGGWFHSGDIAVKHPDNYIEIKDRSKDVIISGGENISSVEVENVVYHHPAVLEASVVARP 489
Cdd:cd05926 351 GPNVTRGYLNNPEANAEaAFKDGWFRTGDLGYLDADGYLFLTGRIKELINRGGEKISPLEVDGVLLSHPAVLEAVAFGVP 430
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 15228909 490 DERWQESPCAFVTLKSDYEkhdqnKLAQDIMKFCREKLPAYWVPKSVVF-GPLPKTATGKIQKHILR 555
Cdd:cd05926 431 DEKYGEEVAAAVVLREGAS-----VTEEELRAFCRKHLAAFKVPKKVYFvDELPKTATGKIQRRKVA 492
|
|
| PRK07786 |
PRK07786 |
long-chain-fatty-acid--CoA ligase; Validated |
28-557 |
8.87e-72 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 169098 [Multi-domain] Cd Length: 542 Bit Score: 239.68 E-value: 8.87e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228909 28 LDRAAVVHPTRKSVIHGSREYTWRQTYDRCRRLASALADRSIGPGSTVAIIAPNIPAMYEAHFGVPMCGAVLNCVNIRLN 107
Cdd:PRK07786 23 LARHALMQPDAPALRFLGNTTTWRELDDRVAALAGALSRRGVGFGDRVLILMLNRTEFVESVLAANMLGAIAVPVNFRLT 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228909 108 APTVAFLLSHSQSSVIMVDQEFFTLAEdSLRLMEEKAGssfkrpLLIVIGDHTcapeslnralSKGAIEYEDFLA-TGDP 186
Cdd:PRK07786 103 PPEIAFLVSDCGAHVVVTEAALAPVAT-AVRDIVPLLS------TVVVAGGSS----------DDSVLGYEDLLAeAGPA 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228909 187 NYPWQPPADEWQSIAlgYTSGTTASPKGVVLHHRGAYIMALSNPLIWGMQDGA-VYLWTLPMFHCNGWCFPWSLAVLSGT 265
Cdd:PRK07786 166 HAPVDIPNDSPALIM--YTSGTTGRPKGAVLTHANLTGQAMTCLRTNGADINSdVGFVGVPLFHIAGIGSMLPGLLLGAP 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228909 266 SIC--LRQVTAKEVYSMIAKYKVTHFCAAPVVLNAIVNAPKEDtilPLPHTVHVMTAGAAP-PPSVLFSMNQK--GFRVA 340
Cdd:PRK07786 244 TVIypLGAFDPGQLLDVLEAEKVTGIFLVPAQWQAVCAEQQAR---PRDLALRVLSWGAAPaSDTLLRQMAATfpEAQIL 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228909 341 HTYGLSETyGPSTvCAwkpewdslppetqakLNARQGVRYTGmeqldvidtQTGKPVP--------------ADGkTAGE 406
Cdd:PRK07786 321 AAFGQTEM-SPVT-CM---------------LLGEDAIRKLG---------SVGKVIPtvaarvvdenmndvPVG-EVGE 373
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228909 407 IVFRGNMVMKGYLKNPEANKETFAGGWFHSGDIAVKHPDNYIEIKDRSKDVIISGGENISSVEVENVVYHHPAVLEASVV 486
Cdd:PRK07786 374 IVYRAPTLMSGYWNNPEATAEAFAGGWFHSGDLVRQDEEGYVWVVDRKKDMIISGGENIYCAEVENVLASHPDIVEVAVI 453
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 15228909 487 ARPDERWQESPCAFVTLKSDYEKHDQNKLAQdimkFCREKLPAYWVPKSVVFGP-LPKTATGKIQKHILRTK 557
Cdd:PRK07786 454 GRADEKWGEVPVAVAAVRNDDAALTLEDLAE----FLTDRLARYKHPKALEIVDaLPRNPAGKVLKTELRER 521
|
|
| OSB_CoA_lg |
cd05912 |
O-succinylbenzoate-CoA ligase (also known as O-succinylbenzoate-CoA synthase, OSB-CoA ... |
47-556 |
1.24e-70 |
|
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: 232.62 E-value: 1.24e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228909 47 EYTWRQTYDRCRRLASALADRSIGPGSTVAIIAPNIPAMYEAHFGVPMCGAVLNCVNIRLNAPTVAFLLSHSQSSVimvd 126
Cdd:cd05912 1 SYTFAELFEEVSRLAEHLAALGVRKGDRVALLSKNSIEMILLIHALWLLGAEAVLLNTRLTPNELAFQLKDSDVKL---- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228909 127 qefftlaEDSLRLMeekagssfkrpllivigdhtcapeslnralskgaieyedflatgdpnypwqppadewqsialgYTS 206
Cdd:cd05912 77 -------DDIATIM---------------------------------------------------------------YTS 86
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228909 207 GTTASPKGVVLHHRGAYIMALSNPLIWGMQDGAVYLWTLPMFHcngwcfpwslavLSGTSICLRQV------------TA 274
Cdd:cd05912 87 GTTGKPKGVQQTFGNHWWSAIGSALNLGLTEDDNWLCALPLFH------------ISGLSILMRSViygmtvylvdkfDA 154
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228909 275 KEVYSMIAKYKVTHFCAAPVVLNAIVnapkEDTILPLPHTVHVMTAGAAP-PPSVLFSMNQKGFRVAHTYGLSETYgpST 353
Cdd:cd05912 155 EQVLHLINSGKVTIISVVPTMLQRLL----EILGEGYPNNLRCILLGGGPaPKPLLEQCKEKGIPVYQSYGMTETC--SQ 228
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228909 354 VCAWKPEwDSLppetqAKLNArqgvryTGMEQLDV---IDTQTGKPvpadgKTAGEIVFRGNMVMKGYLKNPEANKETFA 430
Cdd:cd05912 229 IVTLSPE-DAL-----NKIGS------AGKPLFPVelkIEDDGQPP-----YEVGEILLKGPNVTKGYLNRPDATEESFE 291
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228909 431 GGWFHSGDIAVKHPDNYIEIKDRSKDVIISGGENISSVEVENVVYHHPAVLEASVVARPDERWQESPCAFVTLKSDYekh 510
Cdd:cd05912 292 NGWFKTGDIGYLDEEGFLYVLDRRSDLIISGGENIYPAEIEEVLLSHPAIKEAGVVGIPDDKWGQVPVAFVVSERPI--- 368
|
490 500 510 520
....*....|....*....|....*....|....*....|....*..
gi 15228909 511 DQNKLAQdimkFCREKLPAYWVPKSVVF-GPLPKTATGKIQKHILRT 556
Cdd:cd05912 369 SEEELIA----YCSEKLAKYKVPKKIYFvDELPRTASGKLLRHELKQ 411
|
|
| PRK06839 |
PRK06839 |
o-succinylbenzoate--CoA ligase; |
26-561 |
2.42e-69 |
|
o-succinylbenzoate--CoA ligase;
Pssm-ID: 168698 [Multi-domain] Cd Length: 496 Bit Score: 231.67 E-value: 2.42e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228909 26 WFLDRAAVVHPTRKSVIHGSREYTWRQTYDRCRRLASALADR-SIGPGSTVAIIAPNIPAMYEAHFGVPMCGAVLNCVNI 104
Cdd:PRK06839 6 YWIEKRAYLHPDRIAIITEEEEMTYKQLHEYVSKVAAYLIYElNVKKGERIAILSQNSLEYIVLLFAIAKVECIAVPLNI 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228909 105 RLNAPTVAFLLSHSQSSVIMVDQEFFTLAEdslrlmEEKAGSSFKRPLLIvigdhtcapESLNRALSKGAIEYEdflatg 184
Cdd:PRK06839 86 RLTENELIFQLKDSGTTVLFVEKTFQNMAL------SMQKVSYVQRVISI---------TSLKEIEDRKIDNFV------ 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228909 185 dpnypwqpPADEWQSIALGYTSGTTASPKGVVLHHRGAYIMALSNPLIWGMQDGAVYLWTLPMFHCNG---WCFPWSLAv 261
Cdd:PRK06839 145 --------EKNESASFIICYTSGTTGKPKGAVLTQENMFWNALNNTFAIDLTMHDRSIVLLPLFHIGGiglFAFPTLFA- 215
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228909 262 lSGTSICLRQVTAKEVYSMIAKYKVTHFCAAPVVLNAIVNAPKEDTilPLPHTVHVMTAGAAPPPSVLF-SMNQKGFRVA 340
Cdd:PRK06839 216 -GGVIIVPRKFEPTKALSMIEKHKVTVVMGVPTIHQALINCSKFET--TNLQSVRWFYNGGAPCPEELMrEFIDRGFLFG 292
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228909 341 HTYGLSETyGPSTVCAwkpewdslppetqAKLNARQGVRYTG----MEQLDVIDTQTGKpVPADGktAGEIVFRGNMVMK 416
Cdd:PRK06839 293 QGFGMTET-SPTVFML-------------SEEDARRKVGSIGkpvlFCDYELIDENKNK-VEVGE--VGELLIRGPNVMK 355
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228909 417 GYLKNPEANKETFAGGWFHSGDIAVKHPDNYIEIKDRSKDVIISGGENISSVEVENVVYHHPAVLEASVVARPDERWQES 496
Cdd:PRK06839 356 EYWNRPDATEETIQDGWLCTGDLARVDEDGFVYIVGRKKEMIISGGENIYPLEVEQVINKLSDVYEVAVVGRQHVKWGEI 435
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 15228909 497 PCAFVTLKSdyekhDQNKLAQDIMKFCREKLPAYWVPKSVVF-GPLPKTATGKIQKHILRTKAKEM 561
Cdd:PRK06839 436 PIAFIVKKS-----SSVLIEKDVIEHCRLFLAKYKIPKEIVFlKELPKNATGKIQKAQLVNQLKSR 496
|
|
| PRK13295 |
PRK13295 |
cyclohexanecarboxylate-CoA ligase; Reviewed |
2-560 |
4.26e-69 |
|
cyclohexanecarboxylate-CoA ligase; Reviewed
Pssm-ID: 171961 [Multi-domain] Cd Length: 547 Bit Score: 232.64 E-value: 4.26e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228909 2 AATKWRD---IDDLPKIPANytalTPlwflDRAAVVHPtrkSVIHGS-REYTWRQTYDRCRRLASALADRSIGPGSTVAI 77
Cdd:PRK13295 17 AAGHWHDrtiNDDLDACVAS----CP----DKTAVTAV---RLGTGApRRFTYRELAALVDRVAVGLARLGVGRGDVVSC 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228909 78 IAPN---IPAMYEAhfgvpmC---GAVLNCVNIRLNAPTVAFLLSHSQSSVIMVDQEF--FTLAEDSLRLMEEKAGSsfk 149
Cdd:PRK13295 86 QLPNwweFTVLYLA------CsriGAVLNPLMPIFRERELSFMLKHAESKVLVVPKTFrgFDHAAMARRLRPELPAL--- 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228909 150 RPLLIVIGDhtcAPESLNRALSKGAIEYE-DFLATGDPNYPwqPPADEWQSIalgYTSGTTASPKGVVlhHRGAYIMALS 228
Cdd:PRK13295 157 RHVVVVGGD---GADSFEALLITPAWEQEpDAPAILARLRP--GPDDVTQLI---YTSGTTGEPKGVM--HTANTLMANI 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228909 229 NPLIWGMQDGA--VYLWTLPMFHCNGWCFPWSLAVLSGTSICLRQV-TAKEVYSMIAKYKVTHFCAAPVVLNAIVNAPKE 305
Cdd:PRK13295 227 VPYAERLGLGAddVILMASPMAHQTGFMYGLMMPVMLGATAVLQDIwDPARAAELIRTEGVTFTMASTPFLTDLTRAVKE 306
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228909 306 DTiLPLPHTVHVMTAGAAPPPSVLFSMNQK-GFRVAHTYGLSETYGPSTVCawkpewdslPPETQAKLNARQGVRYTGME 384
Cdd:PRK13295 307 SG-RPVSSLRTFLCAGAPIPGALVERARAAlGAKIVSAWGMTENGAVTLTK---------LDDPDERASTTDGCPLPGVE 376
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228909 385 qLDVIDTqTGKPVPADgkTAGEIVFRGNMVMKGYLKNPEANKeTFAGGWFHSGDIAVKHPDNYIEIKDRSKDVIISGGEN 464
Cdd:PRK13295 377 -VRVVDA-DGAPLPAG--QIGRLQVRGCSNFGGYLKRPQLNG-TDADGWFDTGDLARIDADGYIRISGRSKDVIIRGGEN 451
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228909 465 ISSVEVENVVYHHPAVLEASVVARPDERWQESPCAFVTLKS----DYEkhdqnklaqDIMKFCREKLPA--YWVPKSVVF 538
Cdd:PRK13295 452 IPVVEIEALLYRHPAIAQVAIVAYPDERLGERACAFVVPRPgqslDFE---------EMVEFLKAQKVAkqYIPERLVVR 522
|
570 580
....*....|....*....|..
gi 15228909 539 GPLPKTATGKIQKHILRTKAKE 560
Cdd:PRK13295 523 DALPRTPSGKIQKFRLREMLRG 544
|
|
| CHC_CoA_lg |
cd05903 |
Cyclohexanecarboxylate-CoA ligase (also called cyclohex-1-ene-1-carboxylate:CoA ligase); ... |
48-556 |
2.51e-66 |
|
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: 222.26 E-value: 2.51e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228909 48 YTWRQTYDRCRRLASALADRSIGPGSTVAIIAPNIPAMYEAHFGVPMCGAVLNCVNIRLNAPTVAFLLSHSQSSVIMVDQ 127
Cdd:cd05903 2 LTYSELDTRADRLAAGLAALGVGPGDVVAFQLPNWWEFAVLYLACLRIGAVTNPILPFFREHELAFILRRAKAKVFVVPE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228909 128 EFftlaedslrlmeekagssfkrplliviGDHtcapeslnralskgaieyeDFLATGDpnypwqppadewQSIALGYTSG 207
Cdd:cd05903 82 RF---------------------------RQF-------------------DPAAMPD------------AVALLLFTSG 103
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228909 208 TTASPKGVVLHHRGayIMALSNPLI--WGMQDGAVYLWTLPMFHCNGWCFPWSLAVLSGTSICLRQV-TAKEVYSMIAKY 284
Cdd:cd05903 104 TTGEPKGVMHSHNT--LSASIRQYAerLGLGPGDVFLVASPMAHQTGFVYGFTLPLLLGAPVVLQDIwDPDKALALMREH 181
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228909 285 KVTHFCAAPVVLNAIVNAPKEDTIlPLPHTVHVMTAGAAPPPSVLFSMNQK-GFRVAHTYGLSETYGPSTVCAwkpewds 363
Cdd:cd05903 182 GVTFMMGATPFLTDLLNAVEEAGE-PLSRLRTFVCGGATVPRSLARRAAELlGAKVCSAYGSTECPGAVTSIT------- 253
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228909 364 lPPETQAKL----NARQGVRytgmeqLDVIDtQTGKPVPADgkTAGEIVFRGNMVMKGYLKNPEANKETFAGGWFHSGDI 439
Cdd:cd05903 254 -PAPEDRRLytdgRPLPGVE------IKVVD-DTGATLAPG--VEGELLSRGPSVFLGYLDRPDLTADAAPEGWFRTGDL 323
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228909 440 AVKHPDNYIEIKDRSKDVIISGGENISSVEVENVVYHHPAVLEASVVARPDERWQESPCAFVTLKS----DYEKHDQNKL 515
Cdd:cd05903 324 ARLDEDGYLRITGRSKDIIIRGGENIPVLEVEDLLLGHPGVIEAAVVALPDERLGERACAVVVTKSgallTFDELVAYLD 403
|
490 500 510 520
....*....|....*....|....*....|....*....|.
gi 15228909 516 AQDIMKFcreklpaYWVPKSVVFGPLPKTATGKIQKHILRT 556
Cdd:cd05903 404 RQGVAKQ-------YWPERLVHVDDLPRTPSGKVQKFRLRE 437
|
|
| PRK06188 |
PRK06188 |
acyl-CoA synthetase; Validated |
35-555 |
6.03e-66 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 235731 [Multi-domain] Cd Length: 524 Bit Score: 223.71 E-value: 6.03e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228909 35 HPTRKSVIHGSREYTWRQTYDRCRRLASALADRSIGPGSTVAIIAPNIPamyEAhFGVPMCGAVLNCVNIRLNAPTV--- 111
Cdd:PRK06188 25 YPDRPALVLGDTRLTYGQLADRISRYIQAFEALGLGTGDAVALLSLNRP---EV-LMAIGAAQLAGLRRTALHPLGSldd 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228909 112 -AFLLSHSQSSVIMVDQEFFtlaedslrlmEEKAGSSFKRpllivigdhtcAPeSLNRALSKGAIEY-EDFLATGDPnYP 189
Cdd:PRK06188 101 hAYVLEDAGISTLIVDPAPF----------VERALALLAR-----------VP-SLKHVLTLGPVPDgVDLLAAAAK-FG 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228909 190 WQP--PADEWQSIA-LGYTSGTTASPKGVVLHHRGAYIMALSNPLIWGMQDGAVYLWTLPMFHCNGWCFPWSLaVLSGTS 266
Cdd:PRK06188 158 PAPlvAAALPPDIAgLAYTGGTTGKPKGVMGTHRSIATMAQIQLAEWEWPADPRFLMCTPLSHAGGAFFLPTL-LRGGTV 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228909 267 ICLRQVTAKEVYSMIAKYKVTHFCAAPVVLNAIVNAPK-EDTILPlphTVHVMTAGAAP--PPSVLFSMNQKGFRVAHTY 343
Cdd:PRK06188 237 IVLAKFDPAEVLRAIEEQRITATFLVPTMIYALLDHPDlRTRDLS---SLETVYYGASPmsPVRLAEAIERFGPIFAQYY 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228909 344 GLSETygPSTVCAWKPEwDSLPpeTQAKLNARQGVRYTGMEqLDVIDTQtGKPVPADgkTAGEIVFRGNMVMKGYLKNPE 423
Cdd:PRK06188 314 GQTEA--PMVITYLRKR-DHDP--DDPKRLTSCGRPTPGLR-VALLDED-GREVAQG--EVGEICVRGPLVMDGYWNRPE 384
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228909 424 ANKETFAGGWFHSGDIAVKHPDNYIEIKDRSKDVIISGGENISSVEVENVVYHHPAVLEASVVARPDERWQESPCAFVTL 503
Cdd:PRK06188 385 ETAEAFRDGWLHTGDVAREDEDGFYYIVDRKKDMIVTGGFNVFPREVEDVLAEHPAVAQVAVIGVPDEKWGEAVTAVVVL 464
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|...
gi 15228909 504 KSDyEKHDqnklAQDIMKFCREKLPAYWVPKSVVF-GPLPKTATGKIQKHILR 555
Cdd:PRK06188 465 RPG-AAVD----AAELQAHVKERKGSVHAPKQVDFvDSLPLTALGKPDKKALR 512
|
|
| PRK08315 |
PRK08315 |
AMP-binding domain protein; Validated |
27-561 |
2.54e-64 |
|
AMP-binding domain protein; Validated
Pssm-ID: 236236 [Multi-domain] Cd Length: 559 Bit Score: 220.07 E-value: 2.54e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228909 27 FLDRAAVVHPTRKSVI--HGSREYTWRQTYDRCRRLASALADRSIGPGSTVAIIAPNIPAMYEAHFGVPMCGAVLNCVNI 104
Cdd:PRK08315 21 LLDRTAARYPDREALVyrDQGLRWTYREFNEEVDALAKGLLALGIEKGDRVGIWAPNVPEWVLTQFATAKIGAILVTINP 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228909 105 RLNAPTVAFLLSHSQSSVIMVDQEFFT------LAEDSLRLMEEKAG--SSFKRPLL---IVIGDHTCA-----PESLNR 168
Cdd:PRK08315 101 AYRLSELEYALNQSGCKALIAADGFKDsdyvamLYELAPELATCEPGqlQSARLPELrrvIFLGDEKHPgmlnfDELLAL 180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228909 169 ALSKGAIEYEDFLATGDPNYPwqppadewqsIALGYTSGTTASPKGVVLHHR-----GAYI---MALSNpliwgmQDGAV 240
Cdd:PRK08315 181 GRAVDDAELAARQATLDPDDP----------INIQYTSGTTGFPKGATLTHRnilnnGYFIgeaMKLTE------EDRLC 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228909 241 YlwTLPMFHCNGwCFPWSLAVLS-GTSIclrqVTAKEVY------SMIAKYKVTHFCAAPVVLNAIVNAPKEDT------ 307
Cdd:PRK08315 245 I--PVPLYHCFG-MVLGNLACVThGATM----VYPGEGFdplatlAAVEEERCTALYGVPTMFIAELDHPDFARfdlssl 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228909 308 ---IL---PLPhtVHVMTAgaapppsVLFSMNQKGFRVAhtYGLSETygpSTVcawkpewdSLPPETQAKLNARqgVRYT 381
Cdd:PRK08315 318 rtgIMagsPCP--IEVMKR-------VIDKMHMSEVTIA--YGMTET---SPV--------STQTRTDDPLEKR--VTTV 373
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228909 382 G--MEQLDV--IDTQTGKPVPADgkTAGEIVFRGNMVMKGYLKNPEANKETF-AGGWFHSGDIAVKHPDNYIEIKDRSKD 456
Cdd:PRK08315 374 GraLPHLEVkiVDPETGETVPRG--EQGELCTRGYSVMKGYWNDPEKTAEAIdADGWMHTGDLAVMDEEGYVNIVGRIKD 451
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228909 457 VIISGGENISSVEVENVVYHHPAVLEASVVARPDERWQESPCAFVTLKSDYEKHdqnklAQDIMKFCREKLPAYWVPKSV 536
Cdd:PRK08315 452 MIIRGGENIYPREIEEFLYTHPKIQDVQVVGVPDEKYGEEVCAWIILRPGATLT-----EEDVRDFCRGKIAHYKIPRYI 526
|
570 580
....*....|....*....|....*.
gi 15228909 537 VFGP-LPKTATGKIQKHILRTKAKEM 561
Cdd:PRK08315 527 RFVDeFPMTVTGKIQKFKMREMMIEE 552
|
|
| PRK08314 |
PRK08314 |
long-chain-fatty-acid--CoA ligase; Validated |
23-560 |
1.18e-63 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236235 [Multi-domain] Cd Length: 546 Bit Score: 217.91 E-value: 1.18e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228909 23 TPLWF-LDRAAVVHPTRKSVIHGSREYTWRQTYDRCRRLASALADR-SIGPGSTVAIIAPNIPAMYEAHFGVPMCGAVLN 100
Cdd:PRK08314 10 TSLFHnLEVSARRYPDKTAIVFYGRAISYRELLEEAERLAGYLQQEcGVRKGDRVLLYMQNSPQFVIAYYAILRANAVVV 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228909 101 CVNIRLNAPTVAFLLSHSQSSVIMVDQEfftLAEDSLRLMEEKA---------GSSFKRPLLIVIGDHTCAPESLNRALS 171
Cdd:PRK08314 90 PVNPMNREEELAHYVTDSGARVAIVGSE---LAPKVAPAVGNLRlrhvivaqySDYLPAEPEIAVPAWLRAEPPLQALAP 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228909 172 KGAIEYEDFLATGDPNYPWQPPADEwqsIA-LGYTSGTTASPKGVVLHHRGAYIMALSNPLIWGMQDGAVYLWTLPMFHC 250
Cdd:PRK08314 167 GGVVAWKEALAAGLAPPPHTAGPDD---LAvLPYTSGTTGVPKGCMHTHRTVMANAVGSVLWSNSTPESVVLAVLPLFHV 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228909 251 NGWCFPWSLAVLSGTSICL-----RQVTAKevysMIAKYKVTHFCAAP---VVLNAIVNAPKEDtilpLPHTVHVMTAGA 322
Cdd:PRK08314 244 TGMVHSMNAPIYAGATVVLmprwdREAAAR----LIERYRVTHWTNIPtmvVDFLASPGLAERD----LSSLRYIGGGGA 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228909 323 APPPSV---LFsmNQKGFRVAHTYGLSETYGPStvcawkpewDSLPPEtQAKLNArQGVRYTGMEQLdVIDTQTGKPVPa 399
Cdd:PRK08314 316 AMPEAVaerLK--ELTGLDYVEGYGLTETMAQT---------HSNPPD-RPKLQC-LGIPTFGVDAR-VIDPETLEELP- 380
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228909 400 DGKTaGEIVFRGNMVMKGYLKNPEANKETFA--GG--WFHSGDIAVKHPDNYIEIKDRSKDVIISGGENISSVEVENVVY 475
Cdd:PRK08314 381 PGEV-GEIVVHGPQVFKGYWNRPEATAEAFIeiDGkrFFRTGDLGRMDEEGYFFITDRLKRMINASGFKVWPAEVENLLY 459
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228909 476 HHPAVLEASVVARPDERWQESPCAFVTLKSDYEKHDQnklAQDIMKFCREKLPAYWVPKSVVF-GPLPKTATGKIQKHIL 554
Cdd:PRK08314 460 KHPAIQEACVIATPDPRRGETVKAVVVLRPEARGKTT---EEEIIAWAREHMAAYKYPRIVEFvDSLPKSGSGKILWRQL 536
|
....*.
gi 15228909 555 RTKAKE 560
Cdd:PRK08314 537 QEQEKA 542
|
|
| 4CL |
cd05904 |
4-Coumarate-CoA Ligase (4CL); 4-Coumarate:coenzyme A ligase is a key enzyme in the ... |
31-549 |
2.16e-62 |
|
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: 213.64 E-value: 2.16e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228909 31 AAVVHPTRKSVIHGS--REYTWRQTYDRCRRLASALADRSIGPGSTVAIIAPNIPAMYEAHFGVPMCGAVLNCVNIRLNA 108
Cdd:cd05904 14 FASAHPSRPALIDAAtgRALTYAELERRVRRLAAGLAKRGGRKGDVVLLLSPNSIEFPVAFLAVLSLGAVVTTANPLSTP 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228909 109 PTVAFLLSHSQSSVImvdqefFTLAEdslrLMEEKAGSSFKrpllIVIGDhtcapeslnRALSKGAIEYEDFLATGDPNY 188
Cdd:cd05904 94 AEIAKQVKDSGAKLA------FTTAE----LAEKLASLALP----VVLLD---------SAEFDSLSFSDLLFEADEAEP 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228909 189 PwQPPADEWQSIALGYTSGTTASPKGVVLHHRGAYIMALSNPLIWGMQD--GAVYLWTLPMFHCNGWC-FPWSLAVLSGT 265
Cdd:cd05904 151 P-VVVIKQDDVAALLYSSGTTGRSKGVMLTHRNLIAMVAQFVAGEGSNSdsEDVFLCVLPMFHIYGLSsFALGLLRLGAT 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228909 266 SICLRQVTAKEVYSMIAKYKVTHFCAAPVVLNAIVNAPKEDTiLPLPHTVHVMTaGAAPPPSVL---FSMNQKGFRVAHT 342
Cdd:cd05904 230 VVVMPRFDLEELLAAIERYKVTHLPVVPPIVLALVKSPIVDK-YDLSSLRQIMS-GAAPLGKELieaFRAKFPNVDLGQG 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228909 343 YGLSETYGPSTVCAwKPEWDSLPPETQAKLNArqgvrytGMEqLDVIDTQTGKPVPAdgKTAGEIVFRGNMVMKGYLKNP 422
Cdd:cd05904 308 YGMTESTGVVAMCF-APEKDRAKYGSVGRLVP-------NVE-AKIVDPETGESLPP--NQTGELWIRGPSIMKGYLNNP 376
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228909 423 EANKETFAG-GWFHSGDIAVKHPDNYIEIKDRSKDVIISGGENISSVEVENVVYHHPAVLEASVVARPDERWQESPCAFV 501
Cdd:cd05904 377 EATAATIDKeGWLHTGDLCYIDEDGYLFIVDRLKELIKYKGFQVAPAELEALLLSHPEILDAAVIPYPDEEAGEVPMAFV 456
|
490 500 510 520
....*....|....*....|....*....|....*....|....*....
gi 15228909 502 TLKSdyekhDQNKLAQDIMKFCREKLPAYWVPKSVVF-GPLPKTATGKI 549
Cdd:cd05904 457 VRKP-----GSSLTEDEIMDFVAKQVAPYKKVRKVAFvDAIPKSPSGKI 500
|
|
| PRK06145 |
PRK06145 |
acyl-CoA synthetase; Validated |
36-555 |
3.13e-62 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 102207 [Multi-domain] Cd Length: 497 Bit Score: 212.82 E-value: 3.13e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228909 36 PTRKSVIHGSREYTWRQTYDRCRRLASALADRSIGPGSTVAIIAPNIPAMYEAHFGVPMCGAVLNCVNIRLNAPTVAFLL 115
Cdd:PRK06145 16 PDRAALVYRDQEISYAEFHQRILQAAGMLHARGIGQGDVVALLMKNSAAFLELAFAASYLGAVFLPINYRLAADEVAYIL 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228909 116 SHSQSSVIMVDQEFftlaedslrlmEEKAGSSFKRpllIVIGDHtcAPESLNRalskgaieyedfLATGDPNYPWQPPAD 195
Cdd:PRK06145 96 GDAGAKLLLVDEEF-----------DAIVALETPK---IVIDAA--AQADSRR------------LAQGGLEIPPQAAVA 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228909 196 EWQSIALGYTSGTTASPKGVVLHHRGAYIMALSNPLIWGMQDGAVYLWTLPMFHCNGWCFPwSLAVL-SGTSICL-RQVT 273
Cdd:PRK06145 148 PTDLVRLMYTSGTTDRPKGVMHSYGNLHWKSIDHVIALGLTASERLLVVGPLYHVGAFDLP-GIAVLwVGGTLRIhREFD 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228909 274 AKEVYSMIAKYKVTHFCAAPVVLNAIVNAPKEDTiLPLPHTVHVMTAGAAPPPSVL--FSMNQKGFRVAHTYGLSETYGP 351
Cdd:PRK06145 227 PEAVLAAIERHRLTCAWMAPVMLSRVLTVPDRDR-FDLDSLAWCIGGGEKTPESRIrdFTRVFTRARYIDAYGLTETCSG 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228909 352 STVCAWKPEWDSLPPETQAKLNArqgvrytgmeQLDVIDtQTGKPVPADGKtaGEIVFRGNMVMKGYLKNPEANKETFAG 431
Cdd:PRK06145 306 DTLMEAGREIEKIGSTGRALAHV----------EIRIAD-GAGRWLPPNMK--GEICMRGPKVTKGYWKDPEKTAEAFYG 372
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228909 432 GWFHSGDIAVKHPDNYIEIKDRSKDVIISGGENISSVEVENVVYHHPAVLEASVVARPDERWQESPCAFVTLKSdyekhD 511
Cdd:PRK06145 373 DWFRSGDVGYLDEEGFLYLTDRKKDMIISGGENIASSEVERVIYELPEVAEAAVIGVHDDRWGERITAVVVLNP-----G 447
|
490 500 510 520
....*....|....*....|....*....|....*....|....*
gi 15228909 512 QNKLAQDIMKFCREKLPAYWVPKS-VVFGPLPKTATGKIQKHILR 555
Cdd:PRK06145 448 ATLTLEALDRHCRQRLASFKVPRQlKVRDELPRNPSGKVLKRVLR 492
|
|
| menE |
TIGR01923 |
O-succinylbenzoate-CoA ligase; This model represents an enzyme, O-succinylbenzoate-CoA ligase, ... |
49-551 |
3.68e-61 |
|
O-succinylbenzoate-CoA ligase; This model represents an enzyme, O-succinylbenzoate-CoA ligase, which is involved in the fourth step of the menaquinone biosynthesis pathway. O-succinylbenzoate-CoA ligase, together with menB - naphtoate synthase, take 2-succinylbenzoate and convert it into 1,4-di-hydroxy-2- naphtoate. [Biosynthesis of cofactors, prosthetic groups, and carriers, Menaquinone and ubiquinone]
Pssm-ID: 162605 [Multi-domain] Cd Length: 436 Bit Score: 208.46 E-value: 3.68e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228909 49 TWRQTYDRCRRLASALADRSIGPGSTVAIIAPNIPAMYEAHFGVPMCGAVLNCVNIRLNAPTVAFLLSHSQSSvimvdqe 128
Cdd:TIGR01923 1 TWQDLDCEAAHLAKALKAQGIRSGSRVALVGQNSIEMVLLLHACLLLGAEIAMLNTRLTENERTNQLEDLDVQ------- 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228909 129 fFTLAEDSLRlmeekagssfKRPLLIVIGDHTCAPESlnRALSKGAIEYEDFLATgdpnypwqppadewqsiaLGYTSGT 208
Cdd:TIGR01923 74 -LLLTDSLLE----------EKDFQADSLDRIEAAGR--YETSLSASFNMDQIAT------------------LMFTSGT 122
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228909 209 TASPKGVVLHHRGAYIMALSNPLIWGMQDGAVYLWTLPMFHCNGWCFPWSlAVLSGTSICLRQVTAkEVYSMIAKYKVTH 288
Cdd:TIGR01923 123 TGKPKAVPHTFRNHYASAVGSKENLGFTEDDNWLLSLPLYHISGLSILFR-WLIEGATLRIVDKFN-QLLEMIANERVTH 200
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228909 289 FCAAPVVLNAIVNAPKEDTILPLphtvhVMTAGAAPPPSVLFSMNQKGFRVAHTYGLSETYgpSTVCAWKPEWDslppet 368
Cdd:TIGR01923 201 ISLVPTQLNRLLDEGGHNENLRK-----ILLGGSAIPAPLIEEAQQYGLPIYLSYGMTETC--SQVTTATPEML------ 267
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228909 369 qaklnarqgvrytgMEQLDVidtqtGKPVP--------ADGKTAGEIVFRGNMVMKGYLKNPEANKETFAGGWFHSGDIA 440
Cdd:TIGR01923 268 --------------HARPDV-----GRPLAgreikikvDNKEGHGEIMVKGANLMKGYLYQGELTPAFEQQGWFNTGDIG 328
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228909 441 VKHPDNYIEIKDRSKDVIISGGENISSVEVENVVYHHPAVLEASVVARPDERWQESPCAFVTLKSDYekhDQNKLaqdiM 520
Cdd:TIGR01923 329 ELDGEGFLYVLGRRDDLIISGGENIYPEEIETVLYQHPGIQEAVVVPKPDAEWGQVPVAYIVSESDI---SQAKL----I 401
|
490 500 510
....*....|....*....|....*....|..
gi 15228909 521 KFCREKLPAYWVPKSVVFGP-LPKTATGKIQK 551
Cdd:TIGR01923 402 AYLTEKLAKYKVPIAFEKLDeLPYNASGKILR 433
|
|
| FACL_like_2 |
cd05917 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
198-555 |
2.37e-60 |
|
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: 203.66 E-value: 2.37e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228909 198 QSIALGYTSGTTASPKGVVLHHRGAyimaLSNPLIWGMQDGavylWT--------LPMFHCNGWCFPWSLAVLSGTSICL 269
Cdd:cd05917 3 DVINIQFTSGTTGSPKGATLTHHNI----VNNGYFIGERLG----LTeqdrlcipVPLFHCFGSVLGVLACLTHGATMVF 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228909 270 RQVT--AKEVYSMIAKYKVTHFCAAPVVLNAIVNAPkEDTILPLPHTVHVMTAGAAPPPSVLFS----MNQKGFRVAhtY 343
Cdd:cd05917 75 PSPSfdPLAVLEAIEKEKCTALHGVPTMFIAELEHP-DFDKFDLSSLRTGIMAGAPCPPELMKRvievMNMKDVTIA--Y 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228909 344 GLSETygpSTVCAWKPEWDSLP----------PETQAKlnarqgvrytgmeqldVIDtQTGKPVPADGKTaGEIVFRGNM 413
Cdd:cd05917 152 GMTET---SPVSTQTRTDDSIEkrvntvgrimPHTEAK----------------IVD-PEGGIVPPVGVP-GELCIRGYS 210
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228909 414 VMKGYLKNPEANKETFAG-GWFHSGDIAVKHPDNYIEIKDRSKDVIISGGENISSVEVENVVYHHPAVLEASVVARPDER 492
Cdd:cd05917 211 VMKGYWNDPEKTAEAIDGdGWLHTGDLAVMDEDGYCRIVGRIKDMIIRGGENIYPREIEEFLHTHPKVSDVQVVGVPDER 290
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 15228909 493 WQESPCAFVTLKSDYEKHDqnklaQDIMKFCREKLPAYWVPKSVVF-GPLPKTATGKIQKHILR 555
Cdd:cd05917 291 YGEEVCAWIRLKEGAELTE-----EDIKAYCKGKIAHYKVPRYVFFvDEFPLTVSGKIQKFKLR 349
|
|
| PRK07470 |
PRK07470 |
acyl-CoA synthetase; Validated |
27-565 |
5.44e-60 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 180988 [Multi-domain] Cd Length: 528 Bit Score: 207.59 E-value: 5.44e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228909 27 FLDRAAVVHPTRKSVIHGSREYTWRQTYDRCRRLASALADRSIGPGSTVAIIAPNIPAMYEAHFGVPMCGAVLNCVNIRL 106
Cdd:PRK07470 12 FLRQAARRFPDRIALVWGDRSWTWREIDARVDALAAALAARGVRKGDRILVHSRNCNQMFESMFAAFRLGAVWVPTNFRQ 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228909 107 NAPTVAFLLSHSQSSVIMVDQEFftlaEDSLRLMEEkAGSSFKrpLLIVIGDhtcapeslnralSKGAIEYEDFLA--TG 184
Cdd:PRK07470 92 TPDEVAYLAEASGARAMICHADF----PEHAAAVRA-ASPDLT--HVVAIGG------------ARAGLDYEALVArhLG 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228909 185 DPNYPWQPPADE--WqsiaLGYTSGTTASPKGVVL-HHRGAYIMA--LSNpLIWGMQDGAVYLWTLPMFHCNGwcFPWSL 259
Cdd:PRK07470 153 ARVANAAVDHDDpcW----FFFTSGTTGRPKAAVLtHGQMAFVITnhLAD-LMPGTTEQDASLVVAPLSHGAG--IHQLC 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228909 260 AVLSG-TSICL--RQVTAKEVYSMIAKYKVTHFCAAPVVLNAIVNAPKEDTilpLPHTV--HVMTAGAApppsvLFSMNQ 334
Cdd:PRK07470 226 QVARGaATVLLpsERFDPAEVWALVERHRVTNLFTVPTILKMLVEHPAVDR---YDHSSlrYVIYAGAP-----MYRADQ 297
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228909 335 K------GFRVAHTYGLSETYGPSTVCAwkPEWDSLPPETQAKLNArQGVRYTGMeQLDVIDTQtGKPVPAdGKTaGEIV 408
Cdd:PRK07470 298 KralaklGKVLVQYFGLGEVTGNITVLP--PALHDAEDGPDARIGT-CGFERTGM-EVQIQDDE-GRELPP-GET-GEIC 370
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228909 409 FRGNMVMKGYLKNPEANKETFAGGWFHSGDIAVKHPDNYIEIKDRSKDVIISGGENISSVEVENVVYHHPAVLEASVVAR 488
Cdd:PRK07470 371 VIGPAVFAGYYNNPEANAKAFRDGWFRTGDLGHLDARGFLYITGRASDMYISGGSNVYPREIEEKLLTHPAVSEVAVLGV 450
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 15228909 489 PDERWQESPCAFVTLKSdyekhDQNKLAQDIMKFCREKLPAYWVPKSVVFGP-LPKTATGKIQKHILRTKAKEMGPVP 565
Cdd:PRK07470 451 PDPVWGEVGVAVCVARD-----GAPVDEAELLAWLDGKVARYKLPKRFFFWDaLPKSGYGKITKKMVREELEERGLLD 523
|
|
| BCL_4HBCL |
cd05959 |
Benzoate CoA ligase (BCL) and 4-Hydroxybenzoate-Coenzyme A Ligase (4-HBA-CoA ligase); Benzoate ... |
26-555 |
1.75e-59 |
|
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: 205.68 E-value: 1.75e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228909 26 WFLDR-AAVVHPTRKSVIHGSREYTWRQTYDRCRRLASALADRSIGPGSTVAIIAPNIPAMYEAHFGVPMCGAVLNCVNI 104
Cdd:cd05959 7 TLVDLnLNEGRGDKTAFIDDAGSLTYAELEAEARRVAGALRALGVKREERVLLIMLDTVDFPTAFLGAIRAGIVPVPVNT 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228909 105 RLNAPTVAFLLSHSQSSVIMVDQEFFTLAEDSLRLMEEKagssfkRPLLIVIGDHtcAPESlnralskGAIEYEDFLATG 184
Cdd:cd05959 87 LLTPDDYAYYLEDSRARVVVVSGELAPVLAAALTKSEHT------LVVLIVSGGA--GPEA-------GALLLAELVAAE 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228909 185 DPNYPwqpPADEW-QSIALG-YTSGTTASPKGVV-LHHRGAYIMALSNPLIWGMQDGAVYLWTLPMFHC----NGWCFPW 257
Cdd:cd05959 152 AEQLK---PAATHaDDPAFWlYSSGSTGRPKGVVhLHADIYWTAELYARNVLGIREDDVCFSAAKLFFAyglgNSLTFPL 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228909 258 SLAvlsGTSICL-RQVTAKEVYSMIAKYKVTHFCAAPVVLNAIVNAP---KEDtilplPHTVHVMTAGAAPPPSVLFSMN 333
Cdd:cd05959 229 SVG---ATTVLMpERPTPAAVFKRIRRYRPTVFFGVPTLYAAMLAAPnlpSRD-----LSSLRLCVSAGEALPAEVGERW 300
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228909 334 QKGFRVAHTYGLSETYGPSTVCAWKPEwDSLPPETqaklnarqGVRYTGMEqLDVIDtQTGKPVpADGKtAGEIVFRGNM 413
Cdd:cd05959 301 KARFGLDILDGIGSTEMLHIFLSNRPG-RVRYGTT--------GKPVPGYE-VELRD-EDGGDV-ADGE-PGELYVRGPS 367
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228909 414 VMKGYLKNPEANKETFAGGWFHSGDIAVKHPDNYIEIKDRSKDVIISGGENISSVEVENVVYHHPAVLEASVVARPDERW 493
Cdd:cd05959 368 SATMYWNNRDKTRDTFQGEWTRTGDKYVRDDDGFYTYAGRADDMLKVSGIWVSPFEVESALVQHPAVLEAAVVGVEDEDG 447
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 15228909 494 QESPCAFVTLKSDYEkhDQNKLAQDIMKFCREKLPAYWVPKSVVF-GPLPKTATGKIQKHILR 555
Cdd:cd05959 448 LTKPKAFVVLRPGYE--DSEALEEELKEFVKDRLAPYKYPRWIVFvDELPKTATGKIQRFKLR 508
|
|
| LC_FACS_like |
cd05935 |
Putative long-chain fatty acid CoA ligase; The members of this family are putative long-chain ... |
47-554 |
1.30e-57 |
|
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: 198.86 E-value: 1.30e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228909 47 EYTWRQTYDRCRRLASALADRSIGPGSTVAIIAPNIPAMYEAHFGVPMCGAVLNCVNIRLNAPTVAFLLSHSQSSVIMVD 126
Cdd:cd05935 1 SLTYLELLEVVKKLASFLSNKGVRKGDRVGICLQNSPQYVIAYFAIWRANAVVVPINPMLKERELEYILNDSGAKVAVVG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228909 127 QEFFTLAedslrlmeekagssfkrpllivigdhtcapeslnralskgaieyedflatgdpnypwqppadewqsiALGYTS 206
Cdd:cd05935 81 SELDDLA-------------------------------------------------------------------LIPYTS 93
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228909 207 GTTASPKGVVLHHRGAYIMALSNPLIWGMQDGAVYLWTLPMFHCNGWCFPWSLAVLSGTSICLRQVTAKE-VYSMIAKYK 285
Cdd:cd05935 94 GTTGLPKGCMHTHFSAAANALQSAVWTGLTPSDVILACLPLFHVTGFVGSLNTAVYVGGTYVLMARWDREtALELIEKYK 173
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228909 286 VTHFCAAPVVLNAIVNAPK-EDTILPlphTVHVMTAGAAP-PPSVLFSMNQK-GFRVAHTYGLSETYGPSTVCawkpewd 362
Cdd:cd05935 174 VTFWTNIPTMLVDLLATPEfKTRDLS---SLKVLTGGGAPmPPAVAEKLLKLtGLRFVEGYGLTETMSQTHTN------- 243
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228909 363 slPPETQaKLNArQGVRYTGMEQLdVIDTQTGKPVPaDGKTaGEIVFRGNMVMKGYLKNPEANKETFA--GG--WFHSGD 438
Cdd:cd05935 244 --PPLRP-KLQC-LGIP*FGVDAR-VIDIETGRELP-PNEV-GEIVVRGPQIFKGYWNRPEETEESFIeiKGrrFFRTGD 316
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228909 439 IAVKHPDNYIEIKDRSKDVIISGGENISSVEVENVVYHHPAVLEASVVARPDERWQESPCAFVTLKSDYE-KHDqnklAQ 517
Cdd:cd05935 317 LGYMDEEGYFFFVDRVKRMINVSGFKVWPAEVEAKLYKHPAI*EVCVISVPDERVGEEVKAFIVLRPEYRgKVT----EE 392
|
490 500 510
....*....|....*....|....*....|....*...
gi 15228909 518 DIMKFCREKLPAYWVPKSVVF-GPLPKTATGKIQKHIL 554
Cdd:cd05935 393 DIIEWAREQMAAYKYPREVEFvDELPRSASGKILWRLL 430
|
|
| PRK12583 |
PRK12583 |
acyl-CoA synthetase; Provisional |
27-560 |
3.32e-57 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 237145 [Multi-domain] Cd Length: 558 Bit Score: 200.77 E-value: 3.32e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228909 27 FLDRAAVVhptrksVIHGSREYTWRQTYDRCRRLASALADRSIGPGSTVAIIAPNIPAMYEAHFGVPMCGAVLNCVNIRL 106
Cdd:PRK12583 31 FPDREALV------VRHQALRYTWRQLADAVDRLARGLLALGVQPGDRVGIWAPNCAEWLLTQFATARIGAILVNINPAY 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228909 107 NAPTVAFLLSHSQSSVIMVDQEFFTlaEDSLRLMEEKAgssfkrPLLIVIGDHTCAPE---------SLNRALSKGAIEY 177
Cdd:PRK12583 105 RASELEYALGQSGVRWVICADAFKT--SDYHAMLQELL------PGLAEGQPGALACErlpelrgvvSLAPAPPPGFLAW 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228909 178 EDFLATGDPNYPWQPPADEWQ-----SIALGYTSGTTASPKGVVLHH----RGAYIMALSnpliWGMQDGAVYLWTLPMF 248
Cdd:PRK12583 177 HELQARGETVSREALAERQASldrddPINIQYTSGTTGFPKGATLSHhnilNNGYFVAES----LGLTEHDRLCVPVPLY 252
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228909 249 HCNGWCFPWSLAVLSGTSICLRQVTAKEVYSM--IAKYKVTHFCAAPVVLNAIVNAPKEDTILPLPHTVHVMtAGAAPPP 326
Cdd:PRK12583 253 HCFGMVLANLGCMTVGACLVYPNEAFDPLATLqaVEEERCTALYGVPTMFIAELDHPQRGNFDLSSLRTGIM-AGAPCPI 331
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228909 327 S----VLFSMNQKGFRVAhtYGLSETygpSTVCAWKPEWDSLPP--ETQAKLNARQGVRytgmeqldVIDTQtGKPVPAD 400
Cdd:PRK12583 332 EvmrrVMDEMHMAEVQIA--YGMTET---SPVSLQTTAADDLERrvETVGRTQPHLEVK--------VVDPD-GATVPRG 397
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228909 401 gkTAGEIVFRGNMVMKGYLKNPEANKETF-AGGWFHSGDIAVKHPDNYIEIKDRSKDVIISGGENISSVEVENVVYHHPA 479
Cdd:PRK12583 398 --EIGELCTRGYSVMKGYWNNPEATAESIdEDGWMHTGDLATMDEQGYVRIVGRSKDMIIRGGENIYPREIEEFLFTHPA 475
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228909 480 VLEASVVARPDERWQESPCAFVTLKSdyekhDQNKLAQDIMKFCREKLPAYWVPKSVVF-GPLPKTATGKIQKHILRTKA 558
Cdd:PRK12583 476 VADVQVFGVPDEKYGEEIVAWVRLHP-----GHAASEEELREFCKARIAHFKVPRYFRFvDEFPMTVTGKVQKFRMREIS 550
|
..
gi 15228909 559 KE 560
Cdd:PRK12583 551 IE 552
|
|
| PRK05605 |
PRK05605 |
long-chain-fatty-acid--CoA ligase; Validated |
28-561 |
1.98e-56 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 235531 [Multi-domain] Cd Length: 573 Bit Score: 199.07 E-value: 1.98e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228909 28 LDRAAVVHPTRKSVIHGSREYTWRQTYDRCRRLASALADRSIGPGSTVAIIAPNIPAMYEAHFGVPMCGAVLNCVNIRLN 107
Cdd:PRK05605 38 YDNAVARFGDRPALDFFGATTTYAELGKQVRRAAAGLRALGVRPGDRVAIVLPNCPQHIVAFYAVLRLGAVVVEHNPLYT 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228909 108 APTVAFLLS-HSQSSVIMVDQEFFTLAEDSLRLMEEKagssfkrpllIVIGDHTCAPESLNR---------------ALS 171
Cdd:PRK05605 118 AHELEHPFEdHGARVAIVWDKVAPTVERLRRTTPLET----------IVSVNMIAAMPLLQRlalrlpipalrkaraALT 187
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228909 172 ---KGAIEYEDFLAT--GDPNYPWQPPADEWQSIAL-GYTSGTTASPKGVVLHHRGAYIMALSNpLIW--GMQDGA-VYL 242
Cdd:PRK05605 188 gpaPGTVPWETLVDAaiGGDGSDVSHPRPTPDDVALiLYTSGTTGKPKGAQLTHRNLFANAAQG-KAWvpGLGDGPeRVL 266
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228909 243 WTLPMFHCNGWCFPWSLAVLSGTSICL-RQVTAKEVYSMIAKYKVTHFCAAPVVLNAIVNAPKEDTIlPLpHTVHVMTAG 321
Cdd:PRK05605 267 AALPMFHAYGLTLCLTLAVSIGGELVLlPAPDIDLILDAMKKHPPTWLPGVPPLYEKIAEAAEERGV-DL-SGVRNAFSG 344
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228909 322 AA--PPPSVLFSMNQKGFRVAHTYGLSETygpSTVCAWKPEWDSlppetqaklnARQGvrYTGM----EQLDVIDTQTGK 395
Cdd:PRK05605 345 AMalPVSTVELWEKLTGGLLVEGYGLTET---SPIIVGNPMSDD----------RRPG--YVGVpfpdTEVRIVDPEDPD 409
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228909 396 PVPADGkTAGEIVFRGNMVMKGYLKNPEANKETFAGGWFHSGDIAVKHPDNYIEIKDRSKDVIISGGENISSVEVENVVY 475
Cdd:PRK05605 410 ETMPDG-EEGELLVRGPQVFKGYWNRPEETAKSFLDGWFRTGDVVVMEEDGFIRIVDRIKELIITGGFNVYPAEVEEVLR 488
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228909 476 HHPAVLEASVVARPDERWQESPCAFVTLKSDyEKHDQNKLAQdimkFCREKLPAYWVPKS-VVFGPLPKTATGKiqkhIL 554
Cdd:PRK05605 489 EHPGVEDAAVVGLPREDGSEEVVAAVVLEPG-AALDPEGLRA----YCREHLTRYKVPRRfYHVDELPRDQLGK----VR 559
|
....*..
gi 15228909 555 RTKAKEM 561
Cdd:PRK05605 560 RREVREE 566
|
|
| PRK13391 |
PRK13391 |
acyl-CoA synthetase; Provisional |
16-557 |
2.21e-55 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 184022 [Multi-domain] Cd Length: 511 Bit Score: 194.91 E-value: 2.21e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228909 16 PANYTALTPlwflDRAAVVHP-TRKSVihgsreyTWRQTYDRCRRLASALADRSIGPGSTVAIIAPNIPAMYEAHFGVPM 94
Cdd:PRK13391 3 PGIHAQTTP----DKPAVIMAsTGEVV-------TYRELDERSNRLAHLFRSLGLKRGDHVAIFMENNLRYLEVCWAAER 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228909 95 CGAVLNCVNIRLNAPTVAFLLSHSQSSVIMVDQEFFTLAEdslRLMEEKAGSsfkRPLLIVIGDHTcapeslnralSKGA 174
Cdd:PRK13391 72 SGLYYTCVNSHLTPAEAAYIVDDSGARALITSAAKLDVAR---ALLKQCPGV---RHRLVLDGDGE----------LEGF 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228909 175 IEYEDFLAtgdpNYPWQPPADEWQSIALGYTSGTTASPKGVV--LHHRGAY----IMALSNPLiWGMQDGAVYLWTLPMF 248
Cdd:PRK13391 136 VGYAEAVA----GLPATPIADESLGTDMLYSSGTTGRPKGIKrpLPEQPPDtplpLTAFLQRL-WGFRSDMVYLSPAPLY 210
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228909 249 HCNGWCFPWSLAVLSGTSICLRQVTAKEVYSMIAKYKVTHFCAAPVVLNAIVNAPKEDTILPLPHTVHVMTAGAAP-PPS 327
Cdd:PRK13391 211 HSAPQRAVMLVIRLGGTVIVMEHFDAEQYLALIEEYGVTHTQLVPTMFSRMLKLPEEVRDKYDLSSLEVAIHAAAPcPPQ 290
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228909 328 VLFSMNQKGFRVAHT-YGLSETYGpSTVCAwKPEWdslppetqakLNARQGVRYTGMEQLDVIDtQTGKPVPAdgKTAGE 406
Cdd:PRK13391 291 VKEQMIDWWGPIIHEyYAATEGLG-FTACD-SEEW----------LAHPGTVGRAMFGDLHILD-DDGAELPP--GEPGT 355
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228909 407 IVFRGNMVMKgYLKNPEANKETFA--GGWFHSGDIAVKHPDNYIEIKDRSKDVIISGGENISSVEVENVVYHHPAVLEAS 484
Cdd:PRK13391 356 IWFEGGRPFE-YLNDPAKTAEARHpdGTWSTVGDIGYVDEDGYLYLTDRAAFMIISGGVNIYPQEAENLLITHPKVADAA 434
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 15228909 485 VVARPDERWQESPCAFVTLKSDYEKHDQnkLAQDIMKFCREKLPAYWVPKSVVFGP-LPKTATGKIQKHILRTK 557
Cdd:PRK13391 435 VFGVPNEDLGEEVKAVVQPVDGVDPGPA--LAAELIAFCRQRLSRQKCPRSIDFEDeLPRLPTGKLYKRLLRDR 506
|
|
| PRK05620 |
PRK05620 |
long-chain fatty-acid--CoA ligase; |
56-555 |
4.06e-55 |
|
long-chain fatty-acid--CoA ligase;
Pssm-ID: 180167 [Multi-domain] Cd Length: 576 Bit Score: 195.77 E-value: 4.06e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228909 56 RCRRLASALADR-SIGPGSTVAIIAPNIPAMYEAHFGVPMCGAVLNCVNIRLNAPTVAFLLSHSQSSVIMVDQEfftLAE 134
Cdd:PRK05620 47 RAAALAHALHDElGITGDQRVGSMMYNCAEHLEVLFAVACMGAVFNPLNKQLMNDQIVHIINHAEDEVIVADPR---LAE 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228909 135 DSLRLMEEKAGSSfkrpLLIVIGDHTCAPESLNRALSKGAIEYEDFLATGDPNYPWqPPADEWQSIALGYTSGTTASPKG 214
Cdd:PRK05620 124 QLGEILKECPCVR----AVVFIGPSDADSAAAHMPEGIKVYSYEALLDGRSTVYDW-PELDETTAAAICYSTGTTGAPKG 198
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228909 215 VVLHHRGAYI--MALSNPLIWGMQDGAVYLWTLPMFHCNGWCFPWSlAVLSGTSICL--RQVTAKEVYSMIAKY--KVTH 288
Cdd:PRK05620 199 VVYSHRSLYLqsLSLRTTDSLAVTHGESFLCCVPIYHVLSWGVPLA-AFMSGTPLVFpgPDLSAPTLAKIIATAmpRVAH 277
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228909 289 fcAAPVVLNAIV-----NAPKEDTIlplpHTVHVmtAGAAPPPSVLFSMNQK-GFRVAHTYGLSETYGPSTVcawkpewd 362
Cdd:PRK05620 278 --GVPTLWIQLMvhylkNPPERMSL----QEIYV--GGSAVPPILIKAWEERyGVDVVHVWGMTETSPVGTV-------- 341
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228909 363 SLPP-----ETQAKLNARQGVRYTGMEQLDVIDtqtGKPVPADGKTAGEIVFRGNMVMKGYLKNP--------------- 422
Cdd:PRK05620 342 ARPPsgvsgEARWAYRVSQGRFPASLEYRIVND---GQVMESTDRNEGEIQVRGNWVTASYYHSPteegggaastfrged 418
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228909 423 --EANKETFAGGWFHSGDIAVKHPDNYIEIKDRSKDVIISGGENISSVEVENVVYHHPAVLEASVVARPDERWQESPCAF 500
Cdd:PRK05620 419 veDANDRFTADGWLRTGDVGSVTRDGFLTIHDRARDVIRSGGEWIYSAQLENYIMAAPEVVECAVIGYPDDKWGERPLAV 498
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*.
gi 15228909 501 VTLKSDYEKHDQNklAQDIMKFCREKLPAYWVPKSVVF-GPLPKTATGKIQKHILR 555
Cdd:PRK05620 499 TVLAPGIEPTRET--AERLRDQLRDRLPNWMLPEYWTFvDEIDKTSVGKFDKKDLR 552
|
|
| EntE |
COG1021 |
EntE, 2,3-dihydroxybenzoate-AMP synthase component of non-ribosomal peptide synthetase ... |
27-560 |
1.10e-54 |
|
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: 193.44 E-value: 1.10e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228909 27 FLDRAAVVHPTRKSVIHGSREYTWRQTYDRCRRLASALADRSIGPGSTVAIIAPNIPAMYEAHFGVPMCGAVlncvnirl 106
Cdd:COG1021 30 LLRRRAERHPDRIAVVDGERRLSYAELDRRADRLAAGLLALGLRPGDRVVVQLPNVAEFVIVFFALFRAGAI-------- 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228909 107 naPtVAFLLSHSQSSVimvdQEFFTLAE-------------DSLRLMEEKAGSSFKRPLLIVIGDhtcapeslnralSKG 173
Cdd:COG1021 102 --P-VFALPAHRRAEI----SHFAEQSEavayiipdrhrgfDYRALARELQAEVPSLRHVLVVGD------------AGE 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228909 174 AIEYEDFLATGDPNYPWQPPADEwqsIALGYTS-GTTASPKGVV-LHHRGAYIMALSNPlIWGMQDGAVYLWTLPMFHcN 251
Cdd:COG1021 163 FTSLDALLAAPADLSEPRPDPDD---VAFFQLSgGTTGLPKLIPrTHDDYLYSVRASAE-ICGLDADTVYLAALPAAH-N 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228909 252 gwcFPWS----LAVLS--GTSICLRQVTAKEVYSMIAKYKVTHFCAAPVVLNAIVNAPKEDTilPLPHTVHVMTAGAA-- 323
Cdd:COG1021 238 ---FPLSspgvLGVLYagGTVVLAPDPSPDTAFPLIERERVTVTALVPPLALLWLDAAERSR--YDLSSLRVLQVGGAkl 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228909 324 PP------PSVLfsmnqkGFRVAHTYGLSEtyGPstVCAWKPEwDslPPETQAklnARQG--------VRytgmeqldVI 389
Cdd:COG1021 313 SPelarrvRPAL------GCTLQQVFGMAE--GL--VNYTRLD-D--PEEVIL---TTQGrpispddeVR--------IV 368
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228909 390 DTQtGKPVPaDGkTAGEIVFRGNMVMKGYLKNPEANKETF-AGGWFHSGDIAVKHPDNYIEIKDRSKDVIISGGENISSV 468
Cdd:COG1021 369 DED-GNPVP-PG-EVGELLTRGPYTIRGYYRAPEHNARAFtPDGFYRTGDLVRRTPDGYLVVEGRAKDQINRGGEKIAAE 445
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228909 469 EVENVVYHHPAVLEASVVARPDERWQESPCAFVTLKsdyekhDQNKLAQDIMKFCREK-LPAYWVPKSVVFGP-LPKTAT 546
Cdd:COG1021 446 EVENLLLAHPAVHDAAVVAMPDEYLGERSCAFVVPR------GEPLTLAELRRFLRERgLAAFKLPDRLEFVDaLPLTAV 519
|
570
....*....|....
gi 15228909 547 GKIQKHILRTKAKE 560
Cdd:COG1021 520 GKIDKKALRAALAA 533
|
|
| PRK08276 |
PRK08276 |
long-chain-fatty-acid--CoA ligase; Validated |
30-555 |
1.59e-52 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236215 [Multi-domain] Cd Length: 502 Bit Score: 187.03 E-value: 1.59e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228909 30 RAAVVHPTrksvihgSREYTWRQTYDRCRRLASALADRSIGPGSTVAIIAPNIPAMYEAHFGVPMCGAVLNCVNIRLNAP 109
Cdd:PRK08276 1 PAVIMAPS-------GEVVTYGELEARSNRLAHGLRALGLREGDVVAILLENNPEFFEVYWAARRSGLYYTPINWHLTAA 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228909 110 TVAFLLSHSQSSVIMVDQEFFTLAEDSLRLMEEKAgssfkRPLLIVIGDHTcapeslnralskGAIEYEDFLAtGDPNYP 189
Cdd:PRK08276 74 EIAYIVDDSGAKVLIVSAALADTAAELAAELPAGV-----PLLLVVAGPVP------------GFRSYEEALA-AQPDTP 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228909 190 wqpPADEWQSIALGYTSGTTASPKGVVLHHRGAYIMALSNPLIWGM------QDGAVYLWTLPMFHC--NGWCFpWSLAv 261
Cdd:PRK08276 136 ---IADETAGADMLYSSGTTGRPKGIKRPLPGLDPDEAPGMMLALLgfgmygGPDSVYLSPAPLYHTapLRFGM-SALA- 210
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228909 262 LSGTSICLRQVTAKEVYSMIAKYKVTHFCAAPVVLNaivnapkedTILPLPHTV----------HVMTAGAAPPPSVLFS 331
Cdd:PRK08276 211 LGGTVVVMEKFDAEEALALIERYRVTHSQLVPTMFV---------RMLKLPEEVrarydvsslrVAIHAAAPCPVEVKRA 281
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228909 332 M-NQKGFRVAHTYGLSETYGpSTVCawkpewdslppetqaklNARQGVRYTG------MEQLDVIDTQtGKPVPAdgKTA 404
Cdd:PRK08276 282 MiDWWGPIIHEYYASSEGGG-VTVI-----------------TSEDWLAHPGsvgkavLGEVRILDED-GNELPP--GEI 340
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228909 405 GEIVFRGNMVMKGYLKNPEANKETFAG-GWFHSGDIAVKHPDNYIEIKDRSKDVIISGGENISSVEVENVVYHHPAVLEA 483
Cdd:PRK08276 341 GTVYFEMDGYPFEYHNDPEKTAAARNPhGWVTVGDVGYLDEDGYLYLTDRKSDMIISGGVNIYPQEIENLLVTHPKVADV 420
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 15228909 484 SVVARPDERWQESPCAFVTLKSDYEKHDQnkLAQDIMKFCREKLPAYWVPKSVVFGP-LPKTATGKIQKHILR 555
Cdd:PRK08276 421 AVFGVPDEEMGERVKAVVQPADGADAGDA--LAAELIAWLRGRLAHYKCPRSIDFEDeLPRTPTGKLYKRRLR 491
|
|
| PRK06710 |
PRK06710 |
long-chain-fatty-acid--CoA ligase; Validated |
27-554 |
2.67e-52 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 180666 [Multi-domain] Cd Length: 563 Bit Score: 187.55 E-value: 2.67e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228909 27 FLDRAAVVHPTRKSVIHGSREYTWRQTYDRCRRLASALADRSIGPGSTVAIIAPNIPAMYEAHFGVPMCGAVLNCVNIRL 106
Cdd:PRK06710 29 YVEQMASRYPEKKALHFLGKDITFSVFHDKVKRFANYLQKLGVEKGDRVAIMLPNCPQAVIGYYGTLLAGGIVVQTNPLY 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228909 107 NAPTVAFLLSHSQSSVIMVDQEFFTlaedslRLMEEKAGSSFKRPLLIVIGDHTCAPESL-----NRALSKGAIEYEDF- 180
Cdd:PRK06710 109 TERELEYQLHDSGAKVILCLDLVFP------RVTNVQSATKIEHVIVTRIADFLPFPKNLlypfvQKKQSNLVVKVSESe 182
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228909 181 ------LATGDPNYPWQPPADEWQSIAL-GYTSGTTASPKGVVLHHRGAyimaLSNPL-----IWGMQDGA-VYLWTLPM 247
Cdd:PRK06710 183 tihlwnSVEKEVNTGVEVPCDPENDLALlQYTGGTTGFPKGVMLTHKNL----VSNTLmgvqwLYNCKEGEeVVLGVLPF 258
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228909 248 FHCNGWCFPWSLAVLSGTSICL-RQVTAKEVYSMIAKYKVTHFCAAPVVLNAIVNAP--KEDTIlplpHTVHVMTAGAAP 324
Cdd:PRK06710 259 FHVYGMTAVMNLSIMQGYKMVLiPKFDMKMVFEAIKKHKVTLFPGAPTIYIALLNSPllKEYDI----SSIRACISGSAP 334
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228909 325 PPSVLFSMNQK--GFRVAHTYGLSETygpSTVCAWKPEWDSLPPetqaklnARQGVRYTGMEQLdVIDTQTGKPVPADgk 402
Cdd:PRK06710 335 LPVEVQEKFETvtGGKLVEGYGLTES---SPVTHSNFLWEKRVP-------GSIGVPWPDTEAM-IMSLETGEALPPG-- 401
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228909 403 TAGEIVFRGNMVMKGYLKNPEANKETFAGGWFHSGDIAVKHPDNYIEIKDRSKDVIISGGENISSVEVENVVYHHPAVLE 482
Cdd:PRK06710 402 EIGEIVVKGPQIMKGYWNKPEETAAVLQDGWLHTGDVGYMDEDGFFYVKDRKKDMIVASGFNVYPREVEEVLYEHEKVQE 481
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 15228909 483 ASVVARPDERWQESPCAFVTLKSDYEKHDqnklaQDIMKFCREKLPAYWVPKSVVF-GPLPKTATGKIQKHIL 554
Cdd:PRK06710 482 VVTIGVPDPYRGETVKAFVVLKEGTECSE-----EELNQFARKYLAAYKVPKVYEFrDELPKTTVGKILRRVL 549
|
|
| MACS_like |
cd05972 |
Medium-chain acyl-CoA synthetase (MACS or ACSM); MACS catalyzes the two-step activation of ... |
48-555 |
6.61e-51 |
|
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: 180.61 E-value: 6.61e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228909 48 YTWRQTYDRCRRLASALADRSIGPGSTVAIIAPNIPAMYEAHFGVPMCGAVLNCVNIRLNAPTVAFLLSHSQSSVIMVDQ 127
Cdd:cd05972 1 WSFRELKRESAKAANVLAKLGLRKGDRVAVLLPRVPELWAVILAVIKLGAVYVPLTTLLGPKDIEYRLEAAGAKAIVTDA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228909 128 EfftlaedslrlmeekagssfkrpllivigdhtcapeslnralskgaieyedflatgDPnypwqppadewqsIALGYTSG 207
Cdd:cd05972 81 E--------------------------------------------------------DP-------------ALIYFTSG 91
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228909 208 TTASPKGVVLHHRGAY--IMALSNPLiwGMQDGAVYlWTL--PMFHCNGWC---FPWSLAVlSGTSICLRQVTAKEVYSM 280
Cdd:cd05972 92 TTGLPKGVLHTHSYPLghIPTAAYWL--GLRPDDIH-WNIadPGWAKGAWSsffGPWLLGA-TVFVYEGPRFDAERILEL 167
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228909 281 IAKYKVTHFCAAPVVLNAIVnapKEDTI-LPLPHTVHVMTAGAAPPPSVLFSMNQK-GFRVAHTYGLSETYGPSTVCAWK 358
Cdd:cd05972 168 LERYGVTSFCGPPTAYRMLI---KQDLSsYKFSHLRLVVSAGEPLNPEVIEWWRAAtGLPIRDGYGQTETGLTVGNFPDM 244
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228909 359 PewdsLPPETQAKlnARQGVRytgmeqLDVIDtQTGKPVPADgkTAGEIVFRGNMV--MKGYLKNPEANKETFAGGWFHS 436
Cdd:cd05972 245 P----VKPGSMGR--PTPGYD------VAIID-DDGRELPPG--EEGDIAIKLPPPglFLGYVGDPEKTEASIRGDYYLT 309
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228909 437 GDIAVKHPDNYIEIKDRSKDVIISGGENISSVEVENVVYHHPAVLEASVVARPDERWQESPCAFVTLKSDYEkhDQNKLA 516
Cdd:cd05972 310 GDRAYRDEDGYFWFVGRADDIIKSSGYRIGPFEVESALLEHPAVAEAAVVGSPDPVRGEVVKAFVVLTSGYE--PSEELA 387
|
490 500 510 520
....*....|....*....|....*....|....*....|
gi 15228909 517 QDIMKFCREKLPAYWVPKSVVFGP-LPKTATGKIQKHILR 555
Cdd:cd05972 388 EELQGHVKKVLAPYKYPREIEFVEeLPKTISGKIRRVELR 427
|
|
| PRK09088 |
PRK09088 |
acyl-CoA synthetase; Validated |
44-555 |
8.57e-51 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 181644 [Multi-domain] Cd Length: 488 Bit Score: 181.93 E-value: 8.57e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228909 44 GSREYTWRQTYDRCRRLASALADRSIGPGSTVAIIAPNIPAMYEAHFGVPMCGAVLNCVNIRLNAPTVAFLLSHSQSSVI 123
Cdd:PRK09088 19 LGRRWTYAELDALVGRLAAVLRRRGCVDGERLAVLARNSVWLVALHFACARVGAIYVPLNWRLSASELDALLQDAEPRLL 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228909 124 MVDQEfftlaedslrlmeekagssfkrpllivIGDHTCAPESLNRALSKGAIEYEDFLATGDPNYPwqppadewqSIALg 203
Cdd:PRK09088 99 LGDDA---------------------------VAAGRTDVEDLAAFIASADALEPADTPSIPPERV---------SLIL- 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228909 204 YTSGTTASPKGVVLHHRGAYIMALSNPLIWGMQDGAVYLWTLPMFHCNGWCFPWSLAVLSGTSIclrQVT----AKEVYS 279
Cdd:PRK09088 142 FTSGTSGQPKGVMLSERNLQQTAHNFGVLGRVDAHSSFLCDAPMFHIIGLITSVRPVLAVGGSI---LVSngfePKRTLG 218
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228909 280 MIA--KYKVTHFCAAPVVLNAIVNAPKEDTIlPLPHTVHVMTAGAAPPPSVLFSMNQKGFRVAHTYGLSET---YGPSTV 354
Cdd:PRK09088 219 RLGdpALGITHYFCVPQMAQAFRAQPGFDAA-ALRHLTALFTGGAPHAAEDILGWLDDGIPMVDGFGMSEAgtvFGMSVD 297
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228909 355 CAwkpewdslppETQAKLNArQGVRYTGMeQLDVIDTQtGKPVPADgkTAGEIVFRGNMVMKGYLKNPEANKETFAG-GW 433
Cdd:PRK09088 298 CD----------VIRAKAGA-AGIPTPTV-QTRVVDDQ-GNDCPAG--VPGELLLRGPNLSPGYWRRPQATARAFTGdGW 362
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228909 434 FHSGDIAVKHPDNYIEIKDRSKDVIISGGENISSVEVENVVYHHPAVLEASVVARPDERWQESPCAFVTLKSdyekhDQN 513
Cdd:PRK09088 363 FRTGDIARRDADGFFWVVDRKKDMFISGGENVYPAEIEAVLADHPGIRECAVVGMADAQWGEVGYLAIVPAD-----GAP 437
|
490 500 510 520
....*....|....*....|....*....|....*....|...
gi 15228909 514 KLAQDIMKFCREKLPAYWVPKSV-VFGPLPKTATGKIQKHILR 555
Cdd:PRK09088 438 LDLERIRSHLSTRLAKYKVPKHLrLVDALPRTASGKLQKARLR 480
|
|
| PRK07529 |
PRK07529 |
AMP-binding domain protein; Validated |
27-558 |
3.15e-50 |
|
AMP-binding domain protein; Validated
Pssm-ID: 236043 [Multi-domain] Cd Length: 632 Bit Score: 183.23 E-value: 3.15e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228909 27 FLDRAAVVHPTRK--SVIHGSREY------TWRQTYDRCRRLASALADRSIGPGSTVAIIAPNIPAMYEAHFGVPMCGAV 98
Cdd:PRK07529 30 LLSRAAARHPDAPalSFLLDADPLdrpetwTYAELLADVTRTANLLHSLGVGPGDVVAFLLPNLPETHFALWGGEAAGIA 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228909 99 lNCVNIRLNAPTVAFLLSHSQSSVIMV-----DQEFFTLAEDSLRLMEEKagssfkRPLLIV-IGDHTCAPESLNRALS- 171
Cdd:PRK07529 110 -NPINPLLEPEQIAELLRAAGAKVLVTlgpfpGTDIWQKVAEVLAALPEL------RTVVEVdLARYLPGPKRLAVPLIr 182
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228909 172 -KGAIEYEDFLATGDPNY------PWQPPADEwqSIALGYTSGTTASPKGVVLHHRGAYIMALSNPLIWGMQDGAVYLWT 244
Cdd:PRK07529 183 rKAHARILDFDAELARQPgdrlfsGRPIGPDD--VAAYFHTGGTTGMPKLAQHTHGNEVANAWLGALLLGLGPGDTVFCG 260
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228909 245 LPMFHCNGwCFPWSLAVLS-------GTSICLRQVTA-KEVYSMIAKYKVTHFCAAPVVLNAIVNAPKEDTILPlphTVH 316
Cdd:PRK07529 261 LPLFHVNA-LLVTGLAPLArgahvvlATPQGYRGPGViANFWKIVERYRINFLSGVPTVYAALLQVPVDGHDIS---SLR 336
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228909 317 VMTAGAAPPPSVLFS--MNQKGFRVAHTYGLSETYGPSTVCawkpewdslPPETQAKLNArQGVR--YTGMEQLdVIDTQ 392
Cdd:PRK07529 337 YALCGAAPLPVEVFRrfEAATGVRIVEGYGLTEATCVSSVN---------PPDGERRIGS-VGLRlpYQRVRVV-ILDDA 405
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228909 393 TGKPVPADGKTAGEIVFRGNMVMKGYLkNPEANKETFA-GGWFHSGDIAVKHPDNYIEIKDRSKDVIISGGENISSVEVE 471
Cdd:PRK07529 406 GRYLRDCAVDEVGVLCIAGPNVFSGYL-EAAHNKGLWLeDGWLNTGDLGRIDADGYFWLTGRAKDLIIRGGHNIDPAAIE 484
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228909 472 NVVYHHPAVLEASVVARPDERWQESPCAFVTLKSDYEKHdqnklAQDIMKFCREKLP---AywVPKSVVF-GPLPKTATG 547
Cdd:PRK07529 485 EALLRHPAVALAAAVGRPDAHAGELPVAYVQLKPGASAT-----EAELLAFARDHIAeraA--VPKHVRIlDALPKTAVG 557
|
570
....*....|.
gi 15228909 548 KIQKHILRTKA 558
Cdd:PRK07529 558 KIFKPALRRDA 568
|
|
| 23DHB-AMP_lg |
cd05920 |
2,3-dihydroxybenzoate-AMP ligase; 2,3-dihydroxybenzoate-AMP ligase activates 2, ... |
28-551 |
6.68e-50 |
|
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: 179.45 E-value: 6.68e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228909 28 LDRAAVVHPTRKSVIHGSREYTWRQTYDRCRRLASALADRSIGPGSTVAIIAPNIPAMYEAHFGVpmcgavlncvnIRLN 107
Cdd:cd05920 21 LARSAARHPDRIAVVDGDRRLTYRELDRRADRLAAGLRGLGIRPGDRVVVQLPNVAEFVVLFFAL-----------LRLG 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228909 108 APTVAFLLSHsqssvimvdqefftlaedslRLMEEKAGSSFKRPLLIVIGDhtcapeslnralskgaiEYEDFlatgDPN 187
Cdd:cd05920 90 AVPVLALPSH--------------------RRSELSAFCAHAEAVAYIVPD-----------------RHAGF----DHR 128
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228909 188 YPWQPPADEWQSIALGYTS-GTTASPKGVVLHHRGAYIMALSNPLIWGMQDGAVYLWTLPMFHCNGWCFPWSLAVL--SG 264
Cdd:cd05920 129 ALARELAESIPEVALFLLSgGTTGTPKLIPRTHNDYAYNVRASAEVCGLDQDTVYLAVLPAAHNFPLACPGVLGTLlaGG 208
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228909 265 TSICLRQVTAKEVYSMIAKYKVTHFCAAPVVLNAIVNAPKEDTilPLPHTVHVMTAGAAP-PPSVLFSMNQK-GFRVAHT 342
Cdd:cd05920 209 RVVLAPDPSPDAAFPLIEREGVTVTALVPALVSLWLDAAASRR--ADLSSLRLLQVGGARlSPALARRVPPVlGCTLQQV 286
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228909 343 YGLSEtygpSTVCAWKPEwDslPPETQAklnARQGVRYTGMEQLDVIDTQtGKPVPaDGKTaGEIVFRGNMVMKGYLKNP 422
Cdd:cd05920 287 FGMAE----GLLNYTRLD-D--PDEVII---HTQGRPMSPDDEIRVVDEE-GNPVP-PGEE-GELLTRGPYTIRGYYRAP 353
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228909 423 EANKETF-AGGWFHSGDIAVKHPDNYIEIKDRSKDVIISGGENISSVEVENVVYHHPAVLEASVVARPDERWQESPCAFV 501
Cdd:cd05920 354 EHNARAFtPDGFYRTGDLVRRTPDGYLVVEGRIKDQINRGGEKIAAEEVENLLLRHPAVHDAAVVAMPDELLGERSCAFV 433
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|..
gi 15228909 502 TLKsdyekhDQNKLAQDIMKFCREK-LPAYWVPKSVVFGP-LPKTATGKIQK 551
Cdd:cd05920 434 VLR------DPPPSAAQLRRFLRERgLAAYKLPDRIEFVDsLPLTAVGKIDK 479
|
|
| PRK06155 |
PRK06155 |
crotonobetaine/carnitine-CoA ligase; Provisional |
28-555 |
7.85e-50 |
|
crotonobetaine/carnitine-CoA ligase; Provisional
Pssm-ID: 235719 [Multi-domain] Cd Length: 542 Bit Score: 180.34 E-value: 7.85e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228909 28 LDRAAVVHPTRKSVIHGSREYTWRQTYDRCRRLASALADRSIGPGSTVAIIAPNIPAMYEAHFGVPMCGAVLNCVNIRLN 107
Cdd:PRK06155 27 LARQAERYPDRPLLVFGGTRWTYAEAARAAAAAAHALAAAGVKRGDRVALMCGNRIEFLDVFLGCAWLGAIAVPINTALR 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228909 108 APTVAFLLSHSQSSVIMVDQEFFtlaeDSLRLMEEKAGSsfkRPLLIVIGdhtcAPESLNRALSKGAIEYEDFLATGDPN 187
Cdd:PRK06155 107 GPQLEHILRNSGARLLVVEAALL----AALEAADPGDLP---LPAVWLLD----APASVSVPAGWSTAPLPPLDAPAPAA 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228909 188 YPwqPPADewqSIALGYTSGTTASPKGVVLHHRGAYIMALSNPLIWGMQDGAVYLWTLPMFHCNGWCfPWSLAVLSGTSI 267
Cdd:PRK06155 176 AV--QPGD---TAAILYTSGTTGPSKGVCCPHAQFYWWGRNSAEDLEIGADDVLYTTLPLFHTNALN-AFFQALLAGATY 249
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228909 268 CL-RQVTAKEVYSMIAKykvtHFCAAPVVLNAIVN------APKEDTilplPHTVHVMTAGAAPPPSVLFSMNQKGFRVA 340
Cdd:PRK06155 250 VLePRFSASGFWPAVRR----HGATVTYLLGAMVSillsqpARESDR----AHRVRVALGPGVPAALHAAFRERFGVDLL 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228909 341 HTYGLSETygpSTVCAwkPEWDSLPPETQAKLnaRQGVrytgmeQLDVIDtQTGKPVPADgkTAGEIVFRGN---MVMKG 417
Cdd:PRK06155 322 DGYGSTET---NFVIA--VTHGSQRPGSMGRL--APGF------EARVVD-EHDQELPDG--EPGELLLRADepfAFATG 385
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228909 418 YLKNPEANKETFAGGWFHSGDIAVKHPDNYIEIKDRSKDVIISGGENISSVEVENVVYHHPAVLEASVVARPDERWQESP 497
Cdd:PRK06155 386 YFGMPEKTVEAWRNLWFHTGDRVVRDADGWFRFVDRIKDAIRRRGENISSFEVEQVLLSHPAVAAAAVFPVPSELGEDEV 465
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228909 498 CAFVTLKsdyekhDQNKL-AQDIMKFCREKLPAYWVPKSVVF-GPLPKTATGKIQKHILR 555
Cdd:PRK06155 466 MAAVVLR------DGTALePVALVRHCEPRLAYFAVPRYVEFvAALPKTENGKVQKFVLR 519
|
|
| MCS |
cd05941 |
Malonyl-CoA synthetase (MCS); MCS catalyzes the formation of malonyl-CoA in a two-step ... |
29-555 |
1.19e-49 |
|
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: 177.48 E-value: 1.19e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228909 29 DRAAVVHPTRKsvihgsreYTWRQTYDRCRRLASAL-ADRSIGPGSTVAIIAPNIPAMYEAHFGVPMCGAVLNCVNIRLN 107
Cdd:cd05941 1 DRIAIVDDGDS--------ITYADLVARAARLANRLlALGKDLRGDRVAFLAPPSAEYVVAQLAIWRAGGVAVPLNPSYP 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228909 108 APTVAFLLSHSQSSVIMvdqefftlaedslrlmeekagssfkRPLLIVigdhtcapeslnralskgaieyedflatgdpn 187
Cdd:cd05941 73 LAELEYVITDSEPSLVL-------------------------DPALIL-------------------------------- 95
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228909 188 ypwqppadewqsialgYTSGTTASPKGVVLHHRGayIMALSNPLI--WGMQDGAVYLWTLPMFHCNGWCFPWSLAVLSGT 265
Cdd:cd05941 96 ----------------YTSGTTGRPKGVVLTHAN--LAANVRALVdaWRWTEDDVLLHVLPLHHVHGLVNALLCPLFAGA 157
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228909 266 S-ICLRQVTAKEVYSMIAKYKVTHFCAAPVVLNAIVNAPKEDTILP------LPHTVHVMTAGAAP-PPSVLFSMNQK-G 336
Cdd:cd05941 158 SvEFLPKFDPKEVAISRLMPSITVFMGVPTIYTRLLQYYEAHFTDPqfaraaAAERLRLMVSGSAAlPVPTLEEWEAItG 237
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228909 337 FRVAHTYGLSETyGPSTVCAWKPEwdslppetqaklnARQGvrYTGME----QLDVIDTQTGKPVPADgkTAGEIVFRGN 412
Cdd:cd05941 238 HTLLERYGMTEI-GMALSNPLDGE-------------RRPG--TVGMPlpgvQARIVDEETGEPLPRG--EVGEIQVRGP 299
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228909 413 MVMKGYLKNPEANKETF-AGGWFHSGDIAVKHPDNYIEIKDRSKDVII-SGGENISSVEVENVVYHHPAVLEASVVARPD 490
Cdd:cd05941 300 SVFKEYWNKPEATKEEFtDDGWFKTGDLGVVDEDGYYWILGRSSVDIIkSGGYKVSALEIERVLLAHPGVSECAVIGVPD 379
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 15228909 491 ERWQESPCAFVTLKSDyekhDQNKLAQDIMKFCREKLPAYWVPKSVVFGP-LPKTATGKIQKHILR 555
Cdd:cd05941 380 PDWGERVVAVVVLRAG----AAALSLEELKEWAKQRLAPYKRPRRLILVDeLPRNAMGKVNKKELR 441
|
|
| FAA1 |
COG1022 |
Long-chain acyl-CoA synthetase (AMP-forming) [Lipid transport and metabolism]; |
27-508 |
1.45e-49 |
|
Long-chain acyl-CoA synthetase (AMP-forming) [Lipid transport and metabolism];
Pssm-ID: 440645 [Multi-domain] Cd Length: 603 Bit Score: 180.68 E-value: 1.45e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228909 27 FLDRAAVvHPTRKSVIH----GSREYTWRQTYDRCRRLASALADRSIGPGSTVAIIAPNIPAMYEAHFGVPMCGAVLNCV 102
Cdd:COG1022 17 LRRRAAR-FPDRVALREkedgIWQSLTWAEFAERVRALAAGLLALGVKPGDRVAILSDNRPEWVIADLAILAAGAVTVPI 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228909 103 NIRLNAPTVAFLLSHSQSSVIMV-DQE----FFTLAED--SLR---LMEEKAGSSFKRPL----LIVIGDHTCAPESLNR 168
Cdd:COG1022 96 YPTSSAEEVAYILNDSGAKVLFVeDQEqldkLLEVRDElpSLRhivVLDPRGLRDDPRLLsldeLLALGREVADPAELEA 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228909 169 ALSkgAIEYEDfLATgdpnypwqppadewqsiaLGYTSGTTASPKGVVLHHRGAYIMALSNPLIWGMQDGAVYLWTLPMF 248
Cdd:COG1022 176 RRA--AVKPDD-LAT------------------IIYTSGTTGRPKGVMLTHRNLLSNARALLERLPLGPGDRTLSFLPLA 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228909 249 HCNGWCfpWSLAVLS-GTSIC----LRQVTAkevysMIAKYKVTHFCAAPVVLNAIVN---------------------- 301
Cdd:COG1022 235 HVFERT--VSYYALAaGATVAfaesPDTLAE-----DLREVKPTFMLAVPRVWEKVYAgiqakaeeagglkrklfrwala 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228909 302 -----APKEDT------ILPLPHTV------------------HVMTAGAAPPPSVL-F--SMnqkGFRVAHTYGLSETY 349
Cdd:COG1022 308 vgrryARARLAgkspslLLRLKHALadklvfsklrealggrlrFAVSGGAALGPELArFfrAL---GIPVLEGYGLTETS 384
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228909 350 GPSTVcawkpewdslppetqaklNARQGVRytgmeqldvIDTqTGKPVP------ADgktAGEIVFRGNMVMKGYLKNPE 423
Cdd:COG1022 385 PVITV------------------NRPGDNR---------IGT-VGPPLPgvevkiAE---DGEILVRGPNVMKGYYKNPE 433
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228909 424 ANKETF-AGGWFHSGDIAVKHPDNYIEIKDRSKDVII-SGGENISSVEVENVVYHHPAVLEASVVArpDERwqESPCAFV 501
Cdd:COG1022 434 ATAEAFdADGWLHTGDIGELDEDGFLRITGRKKDLIVtSGGKNVAPQPIENALKASPLIEQAVVVG--DGR--PFLAALI 509
|
....*..
gi 15228909 502 TLksDYE 508
Cdd:COG1022 510 VP--DFE 514
|
|
| PRK06178 |
PRK06178 |
acyl-CoA synthetase; Validated |
27-560 |
1.97e-49 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 235724 [Multi-domain] Cd Length: 567 Bit Score: 179.85 E-value: 1.97e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228909 27 FLDRAAVVHPTRKSVIHGSREYTWRQTYDRCRRLASALADRSIGPGSTVAIIAPNIPAMYEAHFGVPMCGAVLNCVNIRL 106
Cdd:PRK06178 38 YLRAWARERPQRPAIIFYGHVITYAELDELSDRFAALLRQRGVGAGDRVAVFLPNCPQFHIVFFGILKLGAVHVPVSPLF 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228909 107 NAPTVAFLLSHSQSSVIMVDQEFFTLAEDSL--RLMEEKAGSSF-----KRPLLIVigdhtcaPESLN--RALSKGAIey 177
Cdd:PRK06178 118 REHELSYELNDAGAEVLLALDQLAPVVEQVRaeTSLRHVIVTSLadvlpAEPTLPL-------PDSLRapRLAAAGAI-- 188
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228909 178 eDFLAT--GDPNYPWQPPADEWQSIALGYTSGTTASPKGVVLHHRG-AYIMALSNPLIWGMQDGAVYLWTLPMFHCNGWC 254
Cdd:PRK06178 189 -DLLPAlrACTAPVPLPPPALDALAALNYTGGTTGMPKGCEHTQRDmVYTAAAAYAVAVVGGEDSVFLSFLPEFWIAGEN 267
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228909 255 FPWSLAVLSG-TSICLRQVTAKEVYSMIAKYKVTHfcAAPVVLNAivnapkeDTILPLPHTV--------HVMTAG---- 321
Cdd:PRK06178 268 FGLLFPLFSGaTLVLLARWDAVAFMAAVERYRVTR--TVMLVDNA-------VELMDHPRFAeydlsslrQVRVVSfvkk 338
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228909 322 ---------AAPPPSVLFSMnqkgfrvahTYGLSETYGPSTVCA----------WKPEWDSLP-PETQAKlnarqgvryt 381
Cdd:PRK06178 339 lnpdyrqrwRALTGSVLAEA---------AWGMTETHTCDTFTAgfqdddfdllSQPVFVGLPvPGTEFK---------- 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228909 382 gmeqldVIDTQTGKPVPADGKtaGEIVFRGNMVMKGYLKNPEANKETFAGGWFHSGDIAVKHPDNYIEIKDRSKDVIISG 461
Cdd:PRK06178 400 ------ICDFETGELLPLGAE--GEIVVRTPSLLKGYWNKPEATAEALRDGWLHTGDIGKIDEQGFLHYLGRRKEMLKVN 471
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228909 462 GENISSVEVENVVYHHPAVLEASVVARPDERWQESPCAFVTLKSDyekHDQNklAQDIMKFCREKLPAYWVPKSVVFGPL 541
Cdd:PRK06178 472 GMSVFPSEVEALLGQHPAVLGSAVVGRPDPDKGQVPVAFVQLKPG---ADLT--AAALQAWCRENMAVYKVPEIRIVDAL 546
|
570
....*....|....*....
gi 15228909 542 PKTATGKIQKHILRTKAKE 560
Cdd:PRK06178 547 PMTATGKVRKQDLQALAEE 565
|
|
| CBAL |
cd05923 |
4-Chlorobenzoate-CoA ligase (CBAL); CBAL catalyzes the conversion of 4-chlorobenzoate (4-CB) ... |
29-554 |
1.99e-49 |
|
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: 178.47 E-value: 1.99e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228909 29 DRAAVVHPTRksvihgSREYTWRQTYDRCRRLASALADRSIGPGSTVAIIAPNIPAMYEAHFGVPMCGAVLNCVNIRLNA 108
Cdd:cd05923 16 DACAIADPAR------GLRLTYSELRARIEAVAARLHARGLRPGQRVAVVLPNSVEAVIALLALHRLGAVPALINPRLKA 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228909 109 PTVAFLLSHSQ--SSVIMVDQEfftlaedslrLMEEKAGSsFKRPLLIVIGDHTCAPESLNRALSkgaieyedflatgDP 186
Cdd:cd05923 90 AELAELIERGEmtAAVIAVDAQ----------VMDAIFQS-GVRVLALSDLVGLGEPESAGPLIE-------------DP 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228909 187 nyPWQPPADEWqsiaLGYTSGTTASPKGVVLHHRGA----YIMALSNPLIWGmqDGAVYLWTLPMFHCNGW--CFPWSLA 260
Cdd:cd05923 146 --PREPEQPAF----VFYTSGTTGLPKGAVIPQRAAesrvLFMSTQAGLRHG--RHNVVLGLMPLYHVIGFfaVLVAALA 217
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228909 261 vLSGTSICLRQVTAKEVYSMIAKYKVTHFCAAPVVLNAIVNApKEDTILPLPHTVHVMTAGAAPPPSVLFSMNQ--KGFR 338
Cdd:cd05923 218 -LDGTYVVVEEFDPADALKLIEQERVTSLFATPTHLDALAAA-AEFAGLKLSSLRHVTFAGATMPDAVLERVNQhlPGEK 295
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228909 339 VAHtYGLSETYGPSTVCAWKPEwdslpPETQAKLNAR-QGVRYTGMEQLDVIDTQTGKPVPAdgkTAGEIVFRGnmvmkg 417
Cdd:cd05923 296 VNI-YGTTEAMNSLYMRDARTG-----TEMRPGFFSEvRIVRIGGSPDEALANGEEGELIVA---AAADAAFTG------ 360
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228909 418 YLKNPEANKETFAGGWFHSGDIAVKHPDNYIEIKDRSKDVIISGGENISSVEVENVVYHHPAVLEASVVARPDERWQESP 497
Cdd:cd05923 361 YLNQPEATAKKLQDGWYRTGDVGYVDPSGDVRILGRVDDMIISGGENIHPSEIERVLSRHPGVTEVVVIGVADERWGQSV 440
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*....
gi 15228909 498 CAFVTLksdyekHDQNKLAQDIMKFCRE-KLPAYWVPKSVVF-GPLPKTATGKIQKHIL 554
Cdd:cd05923 441 TACVVP------REGTLSADELDQFCRAsELADFKRPRRYFFlDELPKNAMNKVLRRQL 493
|
|
| BCL_like |
cd05919 |
Benzoate CoA ligase (BCL) and similar adenylate forming enzymes; This family contains benzoate ... |
38-555 |
1.18e-48 |
|
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: 174.96 E-value: 1.18e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228909 38 RKSVIHGSREYTWRQTYDRCRRLASALADRSIGPGSTVAIIAPNIPAMYEAHFGVPMCGAVLNCVNIRLNAPTVAFLLSH 117
Cdd:cd05919 1 KTAFYAADRSVTYGQLHDGANRLGSALRNLGVSSGDRVLLLMLDSPELVQLFLGCLARGAIAVVINPLLHPDDYAYIARD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228909 118 SQSSVIMVDQEfftlaedslrlmeekagssfkrpllivigdhtcapeslnralskgAIEYedflatgdpnypwqppadeW 197
Cdd:cd05919 81 CEARLVVTSAD---------------------------------------------DIAY-------------------L 96
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228909 198 QsialgYTSGTTASPKGVVLHHRGAYIMA--LSNPLIwGMQDGAVYLWTLPMFHC----NGWCFPWSlavlSGTSICLRQ 271
Cdd:cd05919 97 L-----YSSGTTGPPKGVMHAHRDPLLFAdaMAREAL-GLTPGDRVFSSAKMFFGyglgNSLWFPLA----VGASAVLNP 166
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228909 272 --VTAKEVYSMIAKYKVTHFCAAPVVLNAIVNAPKEDTILpLPHTVHVMTAGAAPPPSVL-FSMNQKGFRVAHTYGLSET 348
Cdd:cd05919 167 gwPTAERVLATLARFRPTVLYGVPTFYANLLDSCAGSPDA-LRSLRLCVSAGEALPRGLGeRWMEHFGGPILDGIGATEV 245
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228909 349 yGPSTVCAWKPEW--DSLppetqaklnarqGVRYTGMEqLDVIDtQTGKPVPADgkTAGEIVFRGNMVMKGYLKNPEANK 426
Cdd:cd05919 246 -GHIFLSNRPGAWrlGST------------GRPVPGYE-IRLVD-EEGHTIPPG--EEGDLLVRGPSAAVGYWNNPEKSR 308
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228909 427 ETFAGGWFHSGDIAVKHPDNYIEIKDRSKDVIISGGENISSVEVENVVYHHPAVLEASVVARPDERWQESPCAFVTLKSd 506
Cdd:cd05919 309 ATFNGGWYRTGDKFCRDADGWYTHAGRADDMLKVGGQWVSPVEVESLIIQHPAVAEAAVVAVPESTGLSRLTAFVVLKS- 387
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|
gi 15228909 507 yEKHDQNKLAQDIMKFCREKLPAYWVPKSVVFGP-LPKTATGKIQKHILR 555
Cdd:cd05919 388 -PAAPQESLARDIHRHLLERLSAHKVPRRIAFVDeLPRTATGKLQRFKLR 436
|
|
| PRK06087 |
PRK06087 |
medium-chain fatty-acid--CoA ligase; |
30-555 |
2.40e-48 |
|
medium-chain fatty-acid--CoA ligase;
Pssm-ID: 180393 [Multi-domain] Cd Length: 547 Bit Score: 176.48 E-value: 2.40e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228909 30 RAAVVHPTRKSVI--HGSReYTWRQTYDRCRRLASALADRSIGPGSTVAIIAPNIPAMYEAHFGVPMCGAVLNCVNIRLN 107
Cdd:PRK06087 31 QTARAMPDKIAVVdnHGAS-YTYSALDHAASRLANWLLAKGIEPGDRVAFQLPGWCEFTIIYLACLKVGAVSVPLLPSWR 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228909 108 APTVAFLLSHSQSSVIMVDQEFFTLAEDSLRLMEEKAGSSFKRPLLIvigdHTCAPESLNRALSKgaieyedFLATGDP- 186
Cdd:PRK06087 110 EAELVWVLNKCQAKMFFAPTLFKQTRPVDLILPLQNQLPQLQQIVGV----DKLAPATSSLSLSQ-------IIADYEPl 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228909 187 NYPwqPPADEWQSIALGYTSGTTASPKGVVLHHRG------AYIMALSnpLIWgmQDgaVYLWTLPMFHCNGWCFPWSLA 260
Cdd:PRK06087 179 TTA--ITTHGDELAAVLFTSGTEGLPKGVMLTHNNilaserAYCARLN--LTW--QD--VFMMPAPLGHATGFLHGVTAP 250
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228909 261 VLSGTSICLRQV-TAKEVYSMIAKYKVThfC---AAPVVLNAIVNAPKEDTILPlphTVHVMTAGAAPPPS-VLFSMNQK 335
Cdd:PRK06087 251 FLIGARSVLLDIfTPDACLALLEQQRCT--CmlgATPFIYDLLNLLEKQPADLS---ALRFFLCGGTTIPKkVARECQQR 325
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228909 336 GFRVAHTYGLSETyGPSTVcawkpewdsLPPETQAKLN-ARQGVRYTGMEqLDVIDTQTgKPVPADGKtaGEIVFRGNMV 414
Cdd:PRK06087 326 GIKLLSVYGSTES-SPHAV---------VNLDDPLSRFmHTDGYAAAGVE-IKVVDEAR-KTLPPGCE--GEEASRGPNV 391
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228909 415 MKGYLKNPEA-NKETFAGGWFHSGDIAVKHPDNYIEIKDRSKDVIISGGENISSVEVENVVYHHPAVLEASVVARPDERW 493
Cdd:PRK06087 392 FMGYLDEPELtARALDEEGWYYSGDLCRMDEAGYIKITGRKKDIIVRGGENISSREVEDILLQHPKIHDACVVAMPDERL 471
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 15228909 494 QESPCAFVTLKsdyEKHDQNKLAQDIMKFCREKLPAY-WVPKSVVFGPLPKTATGKIQKHILR 555
Cdd:PRK06087 472 GERSCAYVVLK---APHHSLTLEEVVAFFSRKRVAKYkYPEHIVVIDKLPRTASGKIQKFLLR 531
|
|
| PLN02860 |
PLN02860 |
o-succinylbenzoate-CoA ligase |
28-569 |
4.46e-48 |
|
o-succinylbenzoate-CoA ligase
Pssm-ID: 215464 [Multi-domain] Cd Length: 563 Bit Score: 176.14 E-value: 4.46e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228909 28 LDRAAVVHPTRKSVIHGSREYTWRQTYDRCRRLASALADRSIGPGSTVAIIAPNIPAMYEAHFGVPMCGAVLNCVNIRLN 107
Cdd:PLN02860 13 LTRLATLRGNAVVTISGNRRRTGHEFVDGVLSLAAGLLRLGLRNGDVVAIAALNSDLYLEWLLAVACAGGIVAPLNYRWS 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228909 108 aptvaflLSHSQSSVIMVDQEFFTLAEDSLRLMEEKAGSSFKRPLLIVIGDHTCAPES--LNRALSKGAIeYEDFLATGD 185
Cdd:PLN02860 93 -------FEEAKSAMLLVRPVMLVTDETCSSWYEELQNDRLPSLMWQVFLESPSSSVFifLNSFLTTEML-KQRALGTTE 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228909 186 PNYPWQPpadewQSIAL-GYTSGTTASPKGVVLHHRGAYIMALSNPLIWGMQDGAVYLWTLPMFHCNGWCFPWSLAVLSG 264
Cdd:PLN02860 165 LDYAWAP-----DDAVLiCFTSGTTGRPKGVTISHSALIVQSLAKIAIVGYGEDDVYLHTAPLCHIGGLSSALAMLMVGA 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228909 265 TSICLRQVTAKEVYSMIAKYKVTHFCAAPVVLNAIVNAPKEDTILPLPHTVHVMTAGAAPPPSVLFSMNQKGF---RVAH 341
Cdd:PLN02860 240 CHVLLPKFDAKAALQAIKQHNVTSMITVPAMMADLISLTRKSMTWKVFPSVRKILNGGGSLSSRLLPDAKKLFpnaKLFS 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228909 342 TYGLSETYGPSTVCAWkpewDSLPPETQAKLNARQGVRYTGMEQLDViDTQTGKPVP--------ADGKTAGEIVFRGNM 413
Cdd:PLN02860 320 AYGMTEACSSLTFMTL----HDPTLESPKQTLQTVNQTKSSSVHQPQ-GVCVGKPAPhvelkiglDESSRVGRILTRGPH 394
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228909 414 VMKGYL-KNPEANKETFAGGWFHSGDIAVKHPDNYIEIKDRSKDVIISGGENISSVEVENVVYHHPAVLEASVVARPDER 492
Cdd:PLN02860 395 VMLGYWgQNSETASVLSNDGWLDTGDIGWIDKAGNLWLIGRSNDRIKTGGENVYPEEVEAVLSQHPGVASVVVVGVPDSR 474
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228909 493 WQESPCAFVTLK-----SDYEKHDQNK---LAQDIMK-FCREK-LPAYWVPKSVVF--GPLPKTATGKIQKHILRTKAKE 560
Cdd:PLN02860 475 LTEMVVACVRLRdgwiwSDNEKENAKKnltLSSETLRhHCREKnLSRFKIPKLFVQwrKPFPLTTTGKIRRDEVRREVLS 554
|
....*....
gi 15228909 561 MGPVPRSRL 569
Cdd:PLN02860 555 HLQSLPSNL 563
|
|
| PRK07798 |
PRK07798 |
acyl-CoA synthetase; Validated |
28-548 |
1.56e-47 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236100 [Multi-domain] Cd Length: 533 Bit Score: 173.92 E-value: 1.56e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228909 28 LDRAAVVHPTRKSVIHGSREYTWRQTYDRCRRLASALADRSIGPGSTVAIIAPNIPAMYEAHFGVPMCGAVLNCVNIRLN 107
Cdd:PRK07798 9 FEAVADAVPDRVALVCGDRRLTYAELEERANRLAHYLIAQGLGPGDHVGIYARNRIEYVEAMLGAFKARAVPVNVNYRYV 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228909 108 APTVAFLLSHSQSSVIMVDQEFftlAEDSLRLMEEKAGSSfkrpLLIVIGDHTCAPeslnraLSKGAIEYEDFLATGDPN 187
Cdd:PRK07798 89 EDELRYLLDDSDAVALVYEREF---APRVAEVLPRLPKLR----TLVVVEDGSGND------LLPGAVDYEDALAAGSPE 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228909 188 YPWQPP-ADEwqsIALGYTSGTTASPKGVVLHH--------------RGAYIMALsnpliWGMQDGA------VYLWTLP 246
Cdd:PRK07798 156 RDFGERsPDD---LYLLYTGGTTGMPKGVMWRQedifrvllggrdfaTGEPIEDE-----EELAKRAaagpgmRRFPAPP 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228909 247 MFHCNGwcfPWSL--AVLSGTSICLRQVT---AKEVYSMIAKYKVThfcAAPVVLNAIVnAPKEDTILP-----LPHTVH 316
Cdd:PRK07798 228 LMHGAG---QWAAfaALFSGQTVVLLPDVrfdADEVWRTIEREKVN---VITIVGDAMA-RPLLDALEArgpydLSSLFA 300
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228909 317 VMTAGAAPPPSVlfsmnQKGFR-------VAHTYGLSET-YGPSTVCAWKPewdslPPETQAKLNARQGVRytgmeqldV 388
Cdd:PRK07798 301 IASGGALFSPSV-----KEALLellpnvvLTDSIGSSETgFGGSGTVAKGA-----VHTGGPRFTIGPRTV--------V 362
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228909 389 IDTQtGKPVPADGKTAGEIVFRGNMVMkGYLKNPEANKETF--AGG--WFHSGDIAVKHPDNYIEIKDRSKDVIISGGEN 464
Cdd:PRK07798 363 LDED-GNPVEPGSGEIGWIARRGHIPL-GYYKDPEKTAETFptIDGvrYAIPGDRARVEADGTITLLGRGSVCINTGGEK 440
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228909 465 ISSVEVENVVYHHPAVLEASVVARPDERWQESPCAFVTLKSDYEkHDqnklAQDIMKFCREKLPAYWVPKSVVFGP-LPK 543
Cdd:PRK07798 441 VFPEEVEEALKAHPDVADALVVGVPDERWGQEVVAVVQLREGAR-PD----LAELRAHCRSSLAGYKVPRAIWFVDeVQR 515
|
....*
gi 15228909 544 TATGK 548
Cdd:PRK07798 516 SPAGK 520
|
|
| FadD3 |
cd17638 |
acyl-CoA synthetase FadD3 and similar proteins; This family contains long chain fatty acid CoA ... |
204-551 |
2.36e-47 |
|
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: 168.45 E-value: 2.36e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228909 204 YTSGTTASPKGVVLHHRGAYIMALSNPLIWGMQDGAVYLWTLPMFHCNGWCFPWSLAVLSGTSICLRQV-TAKEVYSMIA 282
Cdd:cd17638 7 FTSGTTGRSKGVMCAHRQTLRAAAAWADCADLTEDDRYLIINPFFHTFGYKAGIVACLLTGATVVPVAVfDVDAILEAIE 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228909 283 KYKVTHFCAAPVVLNAIVNAPKEDTiLPLPHTVHVMTAGAAPPPSVLFSMNQK-GFR-VAHTYGLSETyGPSTVCawKPE 360
Cdd:cd17638 87 RERITVLPGPPTLFQSLLDHPGRKK-FDLSSLRAAVTGAATVPVELVRRMRSElGFEtVLTAYGLTEA-GVATMC--RPG 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228909 361 wDslPPETQAklnarqgvrytgmeqldvidTQTGKPVP------ADgktAGEIVFRGNMVMKGYLKNPEANKETF-AGGW 433
Cdd:cd17638 163 -D--DAETVA--------------------TTCGRACPgfevriAD---DGEVLVRGYNVMQGYLDDPEATAEAIdADGW 216
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228909 434 FHSGDIAVKHPDNYIEIKDRSKDVIISGGENISSVEVENVVYHHPAVLEASVVARPDERWQESPCAFVTLKSdyekhDQN 513
Cdd:cd17638 217 LHTGDVGELDERGYLRITDRLKDMYIVGGFNVYPAEVEGALAEHPGVAQVAVIGVPDERMGEVGKAFVVARP-----GVT 291
|
330 340 350
....*....|....*....|....*....|....*....
gi 15228909 514 KLAQDIMKFCREKLPAYWVPKSVVF-GPLPKTATGKIQK 551
Cdd:cd17638 292 LTEEDVIAWCRERLANYKVPRFVRFlDELPRNASGKVMK 330
|
|
| MACS_like_4 |
cd05969 |
Uncharacterized subfamily of Acetyl-CoA synthetase like family (ACS); This family is most ... |
48-558 |
2.97e-46 |
|
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: 168.45 E-value: 2.97e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228909 48 YTWRQTYDRCRRLASALADRSIGPGSTVAIIAPNIPAMYEAHFGVPMCGAVLncvnirlnAPTvafllshsqssvimvdq 127
Cdd:cd05969 1 YTFAQLKVLSARFANVLKSLGVGKGDRVFVLSPRSPELYFSMLGIGKIGAVI--------CPL----------------- 55
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228909 128 eFFTLAEDSLRlmeekagssfkrpllivigdhtcapESLNRALSKGAIEYEDFLATGDPNYPwqppadewqsIALGYTSG 207
Cdd:cd05969 56 -FSAFGPEAIR-------------------------DRLENSEAKVLITTEELYERTDPEDP----------TLLHYTSG 99
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228909 208 TTASPKGVVLHHRGAYIMALSNPLIWGMQDGAVYL------WTLPMFHcnGWCFPWslavLSGTSICLRQ--VTAKEVYS 279
Cdd:cd05969 100 TTGTPKGVLHVHDAMIFYYFTGKYVLDLHPDDIYWctadpgWVTGTVY--GIWAPW----LNGVTNVVYEgrFDAESWYG 173
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228909 280 MIAKYKVTHFCAAPvvlNAIVNAPKEDTILP----LPHTVHVMTAGAAPPPSVL-FSMNQKGFRVAHTYGLSETyGPSTV 354
Cdd:cd05969 174 IIERVKVTVWYTAP---TAIRMLMKEGDELArkydLSSLRFIHSVGEPLNPEAIrWGMEVFGVPIHDTWWQTET-GSIMI 249
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228909 355 CAWkpewdslpPETQAKLNArQGVRYTGMEQLdVIDTQtGKPVPADgkTAGEIVFRGNM--VMKGYLKNPEANKETFAGG 432
Cdd:cd05969 250 ANY--------PCMPIKPGS-MGKPLPGVKAA-VVDEN-GNELPPG--TKGILALKPGWpsMFRGIWNDEERYKNSFIDG 316
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228909 433 WFHSGDIAVKHPDNYIEIKDRSKDVIISGGENISSVEVENVVYHHPAVLEASVVARPDERWQESPCAFVTLKSDYEKHDq 512
Cdd:cd05969 317 WYLTGDLAYRDEDGYFWFVGRADDIIKTSGHRVGPFEVESALMEHPAVAEAGVIGKPDPLRGEIIKAFISLKEGFEPSD- 395
|
490 500 510 520
....*....|....*....|....*....|....*....|....*..
gi 15228909 513 nKLAQDIMKFCREKLPAYWVPKSVVF-GPLPKTATGKIQKHILRTKA 558
Cdd:cd05969 396 -ELKEEIINFVRQKLGAHVAPREIEFvDNLPKTRSGKIMRRVLKAKE 441
|
|
| VL_LC_FACS_like |
cd05907 |
Long-chain fatty acid CoA synthetases and Bubblegum-like very long-chain fatty acid CoA ... |
46-487 |
8.64e-46 |
|
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: 167.39 E-value: 8.64e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228909 46 REYTWRQTYDRCRRLASALADRSIGPGSTVAIIAPNIPAMYEAHFGVPMCGAVLNCVNIRLNAPTVAFLLSHSQSSVIMV 125
Cdd:cd05907 4 QPITWAEFAEEVRALAKGLIALGVEPGDRVAILSRNRPEWTIADLAILAIGAVPVPIYPTSSAEQIAYILNDSEAKALFV 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228909 126 DqefftlaedslrlmeekagssfkrpllivigdhtcAPeslnralskgaieyeDFLATgdpnypwqppadewqsiaLGYT 205
Cdd:cd05907 84 E-----------------------------------DP---------------DDLAT------------------IIYT 95
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228909 206 SGTTASPKGVVLHHRGayIMALSNPLI--WGMQDGAVYLWTLPMFHCNGWCFPWSLAVLSGTSICLRQvTAKEVYSMIAK 283
Cdd:cd05907 96 SGTTGRPKGVMLSHRN--ILSNALALAerLPATEGDRHLSFLPLAHVFERRAGLYVPLLAGARIYFAS-SAETLLDDLSE 172
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228909 284 YKVTHFCAAPVVLNAIVNAPKEDTI----------LPLPHTVHVMTAGAAPPPSVLFSMNQKGFRVAHTYGLSETYGPST 353
Cdd:cd05907 173 VRPTVFLAVPRVWEKVYAAIKVKAVpglkrklfdlAVGGRLRFAASGGAPLPAELLHFFRALGIPVYEGYGLTETSAVVT 252
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228909 354 VCawkpewdslPPETQaklnarqgvrytgmeqldVIDTqTGKPVP------ADgktAGEIVFRGNMVMKGYLKNPEANKE 427
Cdd:cd05907 253 LN---------PPGDN------------------RIGT-VGKPLPgvevriAD---DGEILVRGPNVMLGYYKNPEATAE 301
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 15228909 428 TF-AGGWFHSGDIAVKHPDNYIEIKDRSKDVII-SGGENISSVEVENVVYHHPAVLEASVVA 487
Cdd:cd05907 302 ALdADGWLHTGDLGEIDEDGFLHITGRKKDLIItSGGKNISPEPIENALKASPLISQAVVIG 363
|
|
| caiC |
PRK08008 |
putative crotonobetaine/carnitine-CoA ligase; Validated |
10-555 |
1.71e-45 |
|
putative crotonobetaine/carnitine-CoA ligase; Validated
Pssm-ID: 181195 [Multi-domain] Cd Length: 517 Bit Score: 167.94 E-value: 1.71e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228909 10 DDLPKIPANYTALTplwFLDRAAVVhptrksvihgsREYTWRQTYDRCRRLASALADRSIGPGSTVAIIAPNIPAMYEAH 89
Cdd:PRK08008 14 DDLADVYGHKTALI---FESSGGVV-----------RRYSYLELNEEINRTANLFYSLGIRKGDKVALHLDNCPEFIFCW 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228909 90 FGVPMCGAVLNCVNIRLNAPTVAFLLSHSQSSVIMVDQEFFTLaedsLRLMEEKAGSSFKRPLLIVIGDHTcapeslnra 169
Cdd:PRK08008 80 FGLAKIGAIMVPINARLLREESAWILQNSQASLLVTSAQFYPM----YRQIQQEDATPLRHICLTRVALPA--------- 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228909 170 lSKGAIEYEDFLATGDPNYPWQPP--ADEWQSIAlgYTSGTTASPKGVVLHHR----GAYIMAlsnpliW--GMQDGAVY 241
Cdd:PRK08008 147 -DDGVSSFTQLKAQQPATLCYAPPlsTDDTAEIL--FTSGTTSRPKGVVITHYnlrfAGYYSA------WqcALRDDDVY 217
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228909 242 LWTLPMFHCNGWCFPwSLAVLS--GTSICLRQVTAKEVYSMIAKYKVTHFCAAPVVLNAIVNAPkedtilPLP----HTV 315
Cdd:PRK08008 218 LTVMPAFHIDCQCTA-AMAAFSagATFVLLEKYSARAFWGQVCKYRATITECIPMMIRTLMVQP------PSAndrqHCL 290
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228909 316 HvmtagaapppSVLFSMN----QK-------GFRVAHTYGLSETYG------PSTvcawKPEWDSLppetqaklnARQGV 378
Cdd:PRK08008 291 R----------EVMFYLNlsdqEKdafeerfGVRLLTSYGMTETIVgiigdrPGD----KRRWPSI---------GRPGF 347
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228909 379 RYtgmeQLDVIDTQtGKPVPADgkTAGEIVFRG---NMVMKGYLKNPEANKETF-AGGWFHSGDIAVKHPDNYIEIKDRS 454
Cdd:PRK08008 348 CY----EAEIRDDH-NRPLPAG--EIGEICIKGvpgKTIFKEYYLDPKATAKVLeADGWLHTGDTGYVDEEGFFYFVDRR 420
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228909 455 KDVIISGGENISSVEVENVVYHHPAVLEASVVARPDERWQESPCAFVTLKSDYEkhdqnkLAQD-IMKFCREKLPAYWVP 533
Cdd:PRK08008 421 CNMIKRGGENVSCVELENIIATHPKIQDIVVVGIKDSIRDEAIKAFVVLNEGET------LSEEeFFAFCEQNMAKFKVP 494
|
570 580
....*....|....*....|...
gi 15228909 534 KSVVF-GPLPKTATGKIQKHILR 555
Cdd:PRK08008 495 SYLEIrKDLPRNCSGKIIKKNLK 517
|
|
| PtmA |
cd17636 |
long-chain fatty acid CoA ligase (FadD); This family contains fatty acid CoA ligases, ... |
204-547 |
1.49e-44 |
|
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: 160.93 E-value: 1.49e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228909 204 YTSGTTASPKGVVLHHRGAYIMALSNPLIWGMQDGAVYLWTLPMFHCNGWCFPWSLAVLSGTSICLRQVTAKEVYSMIAK 283
Cdd:cd17636 7 YTAAFSGRPNGALLSHQALLAQALVLAVLQAIDEGTVFLNSGPLFHIGTLMFTLATFHAGGTNVFVRRVDAEEVLELIEA 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228909 284 YKVTHFCAAPVVLNAIVNAPKEDT--------ILPLPHTVHVMTAGAAPPPSVLFSmnqkgfrvahtYGLSETYGPSTVC 355
Cdd:cd17636 87 ERCTHAFLLPPTIDQIVELNADGLydlsslrsSPAAPEWNDMATVDTSPWGRKPGG-----------YGQTEVMGLATFA 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228909 356 AWkpewdslppetqaklnARQGV----RYTGMEQLDVIDTQtGKPVPaDGKTaGEIVFRGNMVMKGYLKNPEANKETFAG 431
Cdd:cd17636 156 AL----------------GGGAIggagRPSPLVQVRILDED-GREVP-DGEV-GEIVARGPTVMAGYWNRPEVNARRTRG 216
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228909 432 GWFHSGDIAVKHPD---NYIEIKDRskdVIISGGENISSVEVENVVYHHPAVLEASVVARPDERWQESPCAFVTLKSdye 508
Cdd:cd17636 217 GWHHTNDLGRREPDgslSFVGPKTR---MIKSGAENIYPAEVERCLRQHPAVADAAVIGVPDPRWAQSVKAIVVLKP--- 290
|
330 340 350 360
....*....|....*....|....*....|....*....|
gi 15228909 509 khDQNKLAQDIMKFCREKLPAYWVPKSVVF-GPLPKTATG 547
Cdd:cd17636 291 --GASVTEAELIEHCRARIASYKKPKSVEFaDALPRTAGG 328
|
|
| MACS_like_3 |
cd05971 |
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the ... |
43-555 |
8.30e-43 |
|
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: 158.75 E-value: 8.30e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228909 43 HGSREYTWRQTYDRCRRLASALADRSIGPGSTVAIIAPNIPAMYEAHFGVPMCGAVLNCVNIRLNAPTVAFLLSHSQSSV 122
Cdd:cd05971 2 GTPEKVTFKELKTASNRFANVLKEIGLEKGDRVGVFLSQGPECAIAHIAILRSGAIAVPLFALFGPEALEYRLSNSGASA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228909 123 IMVDqefftLAEDslrlmeekagssfkrPLLIVigdhtcapeslnralskgaieyedflatgdpnypwqppadewqsial 202
Cdd:cd05971 82 LVTD-----GSDD---------------PALII----------------------------------------------- 94
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228909 203 gYTSGTTASPKG------VVLHHRGAYIMALSN-----PLIWGMQD----GAVYLWTLPMFHcngwcfpWSLAVLSGTSi 267
Cdd:cd05971 95 -YTSGTTGPPKGalhahrVLLGHLPGVQFPFNLfprdgDLYWTPADwawiGGLLDVLLPSLY-------FGVPVLAHRM- 165
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228909 268 clRQVTAKEVYSMIAKYKVTHFCAAPVVLNAI--VNAPKEDTILPLphtVHVMTAGAAP-PPSVLFSMNQKGFRVAHTYG 344
Cdd:cd05971 166 --TKFDPKAALDLMSRYGVTTAFLPPTALKMMrqQGEQLKHAQVKL---RAIATGGESLgEELLGWAREQFGVEVNEFYG 240
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228909 345 LSETYGPSTVCAwkpewDSLPPEtqaklNARQGVRYTGmEQLDVIDTQtGKPVPADgkTAGEI-VFRGNMV-MKGYLKNP 422
Cdd:cd05971 241 QTECNLVIGNCS-----ALFPIK-----PGSMGKPIPG-HRVAIVDDN-GTPLPPG--EVGEIaVELPDPVaFLGYWNNP 306
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228909 423 EANKETFAGGWFHSGDIAVKHPDNYIEIKDRSKDVIISGGENISSVEVENVVYHHPAVLEASVVARPDERWQESPCAFVT 502
Cdd:cd05971 307 SATEKKMAGDWLLTGDLGRKDSDGYFWYVGRDDDVITSSGYRIGPAEIEECLLKHPAVLMAAVVGIPDPIRGEIVKAFVV 386
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....
gi 15228909 503 LKSDYEKHDQnkLAQDIMKFCREKLPAYWVPKSVVFGP-LPKTATGKIQKHILR 555
Cdd:cd05971 387 LNPGETPSDA--LAREIQELVKTRLAAHEYPREIEFVNeLPRTATGKIRRRELR 438
|
|
| ACLS-CaiC |
cd17637 |
acyl-CoA synthetase (AMP-forming)/AMP-acid ligase II; This family contains fatty acid CoA ... |
204-549 |
8.83e-43 |
|
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: 155.89 E-value: 8.83e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228909 204 YTSGTTASPKGVVLHHRGAYIMALSNPLIWGMQDGAVYLWTLPMFHCNGWCFpwSLAVL--SGTSICLRQVTAKEVYSMI 281
Cdd:cd17637 7 HTAAVAGRPRGAVLSHGNLIAANLQLIHAMGLTEADVYLNMLPLFHIAGLNL--ALATFhaGGANVVMEKFDPAEALELI 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228909 282 AKYKVTHFCAAPVVLNAIVNAPKEDTI----------LPLPHTV---HVMTagaappPSVLFSMnqkgfrvahtYGLSET 348
Cdd:cd17637 85 EEEKVTLMGSFPPILSNLLDAAEKSGVdlsslrhvlgLDAPETIqrfEETT------GATFWSL----------YGQTET 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228909 349 YGPSTVcawkpewdslppetqAKLNARQGV--RYTGMEQLDVIDtQTGKPVPADgkTAGEIVFRGNMVMKGYLKNPEANK 426
Cdd:cd17637 149 SGLVTL---------------SPYRERPGSagRPGPLVRVRIVD-DNDRPVPAG--ETGEIVVRGPLVFQGYWNLPELTA 210
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228909 427 ETFAGGWFHSGDIAVKHPDNYIEIKDRS--KDVIISGGENISSVEVENVVYHHPAVLEASVVARPDERWQESPCAFVTLK 504
Cdd:cd17637 211 YTFRNGWHHTGDLGRFDEDGYLWYAGRKpeKELIKPGGENVYPAEVEKVILEHPAIAEVCVIGVPDPKWGEGIKAVCVLK 290
|
330 340 350 360
....*....|....*....|....*....|....*....|....*.
gi 15228909 505 SdyekhDQNKLAQDIMKFCREKLPAYWVPKSVVF-GPLPKTATGKI 549
Cdd:cd17637 291 P-----GATLTADELIEFVGSRIARYKKPRYVVFvEALPKTADGSI 331
|
|
| DHB_AMP_lig |
TIGR02275 |
2,3-dihydroxybenzoate-AMP ligase; Proteins in this family belong to the AMP-binding enzyme ... |
27-555 |
1.20e-41 |
|
2,3-dihydroxybenzoate-AMP ligase; Proteins in this family belong to the AMP-binding enzyme family (pfam00501). Members activate 2,3-dihydroxybenzoate (DHB) by ligation of AMP from ATP with the release of pyrophosphate; many are involved in synthesis of siderophores such as enterobactin, vibriobactin, vulnibactin, etc. The most closely related proteine believed to differ in function activates salicylate rather than DHB. [Transport and binding proteins, Cations and iron carrying compounds]
Pssm-ID: 274063 [Multi-domain] Cd Length: 526 Bit Score: 157.26 E-value: 1.20e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228909 27 FLDRAAVVHPTRKSVIHGSREYTWRQTYDRCRRLASALADRSIGPGSTVAIIAPNIPAMYEAHFGVpmcgavlncvnIRL 106
Cdd:TIGR02275 28 ILRDQAARYPDAIAIICGNRQWSYRELDQRADNLAAGLTKLGIKQGDTAVVQLPNIAEFYIVFFAL-----------LKL 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228909 107 NAPTVAFLLSHSQSSVimvdQEFFTLAEDSLRLMEEK----AGSSFKRPLLivigdhTCAPESLNRALSKGAIEYEDFLA 182
Cdd:TIGR02275 97 GVAPVLALFSHRKSEL----TAYASQIEPALYIIDRAhslfDYDDFARQLQ------SKLPTLRNIIVAGQTGEAELFLW 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228909 183 TGDPNYPWQ-PPADEWQSIALGYTSGTTASPKGVV-LHHRGAYIMALSNPLIWGMQDgAVYLWTLPMFHCNGWCFPWSLA 260
Cdd:TIGR02275 167 LESPAEPVKfPPTKSDEVAFFQLSGGSTGTPKLIPrTHNDYYYSVRRSVEICWLTQQ-TRYLCALPAAHNYPLSSPGALG 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228909 261 VL--SGTSICLRQVTAKEVYSMIAKYKVTHFC-AAPVVLNAIVNAPKEDTILPLPHTVHV-----MTAGAAPPPSVLfsm 332
Cdd:TIGR02275 246 VFyaGGCVVLAPDPSPTDCFPLIERHKVTVTAlVPPAVALWMQAASKSRADLSSLKLLQVggakfSAAAARRVPAVF--- 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228909 333 nqkGFRVAHTYGLSEtygpSTVCAWKPEwdslppETQAKLNARQGVRYTGMEQLDVIDTQtGKPVpADGKTaGEIVFRGN 412
Cdd:TIGR02275 323 ---GCQLQQVFGMAE----GLVNYTRLD------DPAEIIFTTQGRPMSPDDEVRVVDDH-GNPV-APGET-GMLLTRGP 386
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228909 413 MVMKGYLKNPEANKETF-AGGWFHSGDIAVKHPDNYIEIKDRSKDVIISGGENISSVEVENVVYHHPAVLEASVVARPDE 491
Cdd:TIGR02275 387 YTFRGYYKAPEHNAAAFdAEGFYYTGDLVRLTPEGYIVVVGRAKDQINRGGEKIAAEEIENLLLAHPAVHDAALVSMPDE 466
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 15228909 492 RWQESPCAFVTLKsdyekhDQNKLAQDIMKFCREK-LPAYWVPKSVVF-GPLPKTATGKIQKHILR 555
Cdd:TIGR02275 467 LLGEKSCAFIVVR------DPALKAAQLRRFLRERgLAEYKLPDRVEFvDSLPLTAVGKVDKKALR 526
|
|
| PRK07788 |
PRK07788 |
acyl-CoA synthetase; Validated |
31-555 |
1.46e-41 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236097 [Multi-domain] Cd Length: 549 Bit Score: 157.40 E-value: 1.46e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228909 31 AAVVHPTRKSVI--HGSReyTWRQTYDRCRRLASALADRSIGPGSTVAIIAPNIPAMYEAHFGVPMCGAVLNCVNIRLNA 108
Cdd:PRK07788 58 AARRAPDRAALIdeRGTL--TYAELDEQSNALARGLLALGVRAGDGVAVLARNHRGFVLALYAAGKVGARIILLNTGFSG 135
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228909 109 PTVAFLLSHSQSSVIMVDQEFFTLAEDslrLMEEkagssfkRPLLIVIGDHTCAPESLNRalskGAIEYEDFLATGDPNy 188
Cdd:PRK07788 136 PQLAEVAAREGVKALVYDDEFTDLLSA---LPPD-------LGRLRAWGGNPDDDEPSGS----TDETLDDLIAGSSTA- 200
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228909 189 PWQPPADEWQSIALgyTSGTTASPKGVVlhhRG-----AYIMALSNPLIWGMqdGAVYLWTLPMFHCNGW-CFPWSLAvL 262
Cdd:PRK07788 201 PLPKPPKPGGIVIL--TSGTTGTPKGAP---RPepsplAPLAGLLSRVPFRA--GETTLLPAPMFHATGWaHLTLAMA-L 272
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228909 263 SGTSICLRQVTAKEVYSMIAKYKVTHFCAAPVVLNAIVNAPKEdtILPLPHTVH---VMTAGAAPPPSVlfsmnqkGFRV 339
Cdd:PRK07788 273 GSTVVLRRRFDPEATLEDIAKHKATALVVVPVMLSRILDLGPE--VLAKYDTSSlkiIFVSGSALSPEL-------ATRA 343
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228909 340 AHTYG--LSETYGpSTVCAW----KPEWDSLPPETQAKlnARQGVRytgMEQLDvidtQTGKPVPadGKTAGEIVFRGNM 413
Cdd:PRK07788 344 LEAFGpvLYNLYG-STEVAFatiaTPEDLAEAPGTVGR--PPKGVT---VKILD----ENGNEVP--RGVVGRIFVGNGF 411
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228909 414 VMKGYLKNPeaNKETfAGGWFHSGDIAVKHPDNYIEIKDRSKDVIISGGENISSVEVENVVYHHPAVLEASVVARPDERW 493
Cdd:PRK07788 412 PFEGYTDGR--DKQI-IDGLLSSGDVGYFDEDGLLFVDGRDDDMIVSGGENVFPAEVEDLLAGHPDVVEAAVIGVDDEEF 488
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 15228909 494 QESPCAFVTLksdyeKHDQNKLAQDIMKFCREKLPAYWVPKSVVFGP-LPKTATGKIQKHILR 555
Cdd:PRK07788 489 GQRLRAFVVK-----APGAALDEDAIKDYVRDNLARYKVPRDVVFLDeLPRNPTGKVLKRELR 546
|
|
| A_NRPS |
cd05930 |
The adenylation domain of nonribosomal peptide synthetases (NRPS); The adenylation (A) domain ... |
36-549 |
3.57e-41 |
|
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: 154.22 E-value: 3.57e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228909 36 PTRKSVIHGSREYTWRQTYDRCRRLASALADRSIGPGSTVAIIAPNIPAMYEAHFGVPMCGAVlnCVNIRLNAPT--VAF 113
Cdd:cd05930 1 PDAVAVVDGDQSLTYAELDARANRLARYLRERGVGPGDLVAVLLERSLEMVVAILAVLKAGAA--YVPLDPSYPAerLAY 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228909 114 LLSHSQSSVIMVDQEffTLAedslrlmeekagssfkrpllIVIgdhtcapeslnralskgaieyedflatgdpnypwqpp 193
Cdd:cd05930 79 ILEDSGAKLVLTDPD--DLA--------------------YVI------------------------------------- 99
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228909 194 adewqsialgYTSGTTASPKGVVLHHRGAYIMALSNPLIWGMQDGAVYL-WTLPMFHCNGWCFPWSLavLSG-TSICLRQ 271
Cdd:cd05930 100 ----------YTSGSTGKPKGVMVEHRGLVNLLLWMQEAYPLTPGDRVLqFTSFSFDVSVWEIFGAL--LAGaTLVVLPE 167
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228909 272 VTAK---EVYSMIAKYKVTHFCAAPVVLNAIVNAPKEDTILPLphtVHVMTAGAAPPPSVLFSMNQKGF--RVAHTYGLS 346
Cdd:cd05930 168 EVRKdpeALADLLAEEGITVLHLTPSLLRLLLQELELAALPSL---RLVLVGGEALPPDLVRRWRELLPgaRLVNLYGPT 244
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228909 347 ETYGPST--VCAWKPEWDSLPPETQAKLNarqgvryTGMEQLDvidtQTGKPVPaDGKTaGEIVFRGNMVMKGYLKNPEA 424
Cdd:cd05930 245 EATVDATyyRVPPDDEEDGRVPIGRPIPN-------TRVYVLD----ENLRPVP-PGVP-GELYIGGAGLARGYLNRPEL 311
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228909 425 NKETF------AGGWFH-SGDIAVKHPDNYIEIKDRSKD-VIISG-----GEnissveVENVVYHHPAVLEASVVARPDE 491
Cdd:cd05930 312 TAERFvpnpfgPGERMYrTGDLVRWLPDGNLEFLGRIDDqVKIRGyrielGE------IEAALLAHPGVREAAVVAREDG 385
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*....
gi 15228909 492 RWQESPCAFVTLKSDYEKHdqnklAQDIMKFCREKLPAYWVPKSVVFGP-LPKTATGKI 549
Cdd:cd05930 386 DGEKRLVAYVVPDEGGELD-----EEELRAHLAERLPDYMVPSAFVVLDaLPLTPNGKV 439
|
|
| benz_CoA_lig |
TIGR02262 |
benzoate-CoA ligase family; Characterized members of this protein family include benzoate-CoA ... |
26-555 |
5.62e-41 |
|
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: 155.00 E-value: 5.62e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228909 26 WFLDRAAVVHPTRKSV-IHGSREYTWRQTYDRCRRLASALADRSIGPGSTVAIIAPNIPAMYEAHFGVPMCGAVLNCVNI 104
Cdd:TIGR02262 8 DLLDRNVVEGRGGKTAfIDDISSLSYGELEAQVRRLAAALRRLGVKREERVLLLMLDGVDFPIAFLGAIRAGIVPVALNT 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228909 105 RLNAPTVAFLLSHSQSSVIMVDQEFftlaedsLRLMEEKAGSSFKRPLLIVIGDhtcaPESlnralskGAIEYEDFLATG 184
Cdd:TIGR02262 88 LLTADDYAYMLEDSRARVVFVSGAL-------LPVIKAALGKSPHLEHRVVVGR----PEA-------GEVQLAELLATE 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228909 185 DPNY-PWQPPADE---WQsialgYTSGTTASPKGVVLHHRGAYIMA-LSNPLIWGMQDGAVYLWTLPMFHC----NGWCF 255
Cdd:TIGR02262 150 SEQFkPAATQADDpafWL-----YSSGSTGMPKGVVHTHSNPYWTAeLYARNTLGIREDDVCFSAAKLFFAyglgNALTF 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228909 256 PwsLAVLSGTSICLRQVTAKEVYSMIAKYKVTHFCAAPVVLNAIVNAPKEDTILPLPHTVHVmTAGAAPPPSVlfsmnqk 335
Cdd:TIGR02262 225 P--MSVGATTVLMGERPTPDAVFDRLRRHQPTIFYGVPTLYAAMLADPNLPSEDQVRLRLCT-SAGEALPAEV------- 294
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228909 336 GFRVAHTYGLsetygpstvcawkpewDSLppetqaklnarQGVRYTGMEQL-------DVIDTQTGKPVP---------- 398
Cdd:TIGR02262 295 GQRWQARFGV----------------DIV-----------DGIGSTEMLHIflsnlpgDVRYGTSGKPVPgyrlrlvgdg 347
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228909 399 ----ADGKtAGEIVFRGNMVMKGYLKNPEANKETFAGGWFHSGDIAVKHPDNYIEIKDRSKDVIISGGENISSVEVENVV 474
Cdd:TIGR02262 348 gqdvADGE-PGELLISGPSSATMYWNNRAKSRDTFQGEWTRSGDKYVRNDDGSYTYAGRTDDMLKVSGIYVSPFEIESAL 426
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228909 475 YHHPAVLEASVVARPDERWQESPCAFVTLKSDYEKhdqnkLAQDIMKFCREKLPAYWVPKSVVF-GPLPKTATGKIQKHI 553
Cdd:TIGR02262 427 IQHPAVLEAAVVGVADEDGLIKPKAFVVLRPGQTA-----LETELKEHVKDRLAPYKYPRWIVFvDDLPKTATGKIQRFK 501
|
..
gi 15228909 554 LR 555
Cdd:TIGR02262 502 LR 503
|
|
| PLN02574 |
PLN02574 |
4-coumarate--CoA ligase-like |
163-555 |
1.81e-40 |
|
4-coumarate--CoA ligase-like
Pssm-ID: 215312 [Multi-domain] Cd Length: 560 Bit Score: 154.61 E-value: 1.81e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228909 163 PESLNraLSKGAIEYEDF--LATGDPNYPWQPPADEWQSIALGYTSGTTASPKGVVLHHRGAYIMALSNPLIWGMQDGA- 239
Cdd:PLN02574 164 PENYD--FDSKRIEFPKFyeLIKEDFDFVPKPVIKQDDVAAIMYSSGTTGASKGVVLTHRNLIAMVELFVRFEASQYEYp 241
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228909 240 ----VYLWTLPMFHCNGWC-FPWSLAVLSGTSICLRQVTAKEVYSMIAKYKVTHFCAAPVVLNAIVNAPKEDTILPLPHT 314
Cdd:PLN02574 242 gsdnVYLAALPMFHIYGLSlFVVGLLSLGSTIVVMRRFDASDMVKVIDRFKVTHFPVVPPILMALTKKAKGVCGEVLKSL 321
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228909 315 VHVMTaGAAPppsvLFSMNQKGF--RVAHT-----YGLSETYGPSTvcawkpewdslppetqAKLNARQGVRYTGMEQL- 386
Cdd:PLN02574 322 KQVSC-GAAP----LSGKFIQDFvqTLPHVdfiqgYGMTESTAVGT----------------RGFNTEKLSKYSSVGLLa 380
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228909 387 -----DVIDTQTGKPVPADGktAGEIVFRGNMVMKGYLKNPEANKETF-AGGWFHSGDIAVKHPDNYIEIKDRSKDVIIS 460
Cdd:PLN02574 381 pnmqaKVVDWSTGCLLPPGN--CGELWIQGPGVMKGYLNNPKATQSTIdKDGWLRTGDIAYFDEDGYLYIVDRLKEIIKY 458
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228909 461 GGENISSVEVENVVYHHPAVLEASVVARPDERWQESPCAFVTLKSDyekhdqNKLAQ-DIMKFCREKLPAYWVPKSVVF- 538
Cdd:PLN02574 459 KGFQIAPADLEAVLISHPEIIDAAVTAVPDKECGEIPVAFVVRRQG------STLSQeAVINYVAKQVAPYKKVRKVVFv 532
|
410
....*....|....*..
gi 15228909 539 GPLPKTATGKIQKHILR 555
Cdd:PLN02574 533 QSIPKSPAGKILRRELK 549
|
|
| FACL_like_4 |
cd05944 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
204-560 |
6.18e-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: 148.78 E-value: 6.18e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228909 204 YTSGTTASPKGVVLHHRGAYIMALSNPLIWGMQDGAVYLWTLPMFHCNGWCFPWSLAVLSGTSICL------RQVTA-KE 276
Cdd:cd05944 9 HTGGTTGTPKLAQHTHSNEVYNAWMLALNSLFDPDDVLLCGLPLFHVNGSVVTLLTPLASGAHVVLagpagyRNPGLfDN 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228909 277 VYSMIAKYKVTHFCAAPVVLNAIVNAPKEDTILPLPHTVhvmtAGAAPPPSVLFSMNQK--GFRVAHTYGLSETYGPSTV 354
Cdd:cd05944 89 FWKLVERYRITSLSTVPTVYAALLQVPVNADISSLRFAM----SGAAPLPVELRARFEDatGLPVVEGYGLTEATCLVAV 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228909 355 CawkpewdslPPETQAKLNA-RQGVRYTGMeQLDVIDTQTGKPVPADGKTAGEIVFRGNMVMKGYLkNPEANKETFA-GG 432
Cdd:cd05944 165 N---------PPDGPKRPGSvGLRLPYARV-RIKVLDGVGRLLRDCAPDEVGEICVAGPGVFGGYL-YTEGNKNAFVaDG 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228909 433 WFHSGDIAVKHPDNYIEIKDRSKDVIISGGENISSVEVENVVYHHPAVLEASVVARPDERWQESPCAFVTLKSDYEKHDQ 512
Cdd:cd05944 234 WLNTGDLGRLDADGYLFITGRAKDLIIRGGHNIDPALIEEALLRHPAVAFAGAVGQPDAHAGELPVAYVQLKPGAVVEEE 313
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|
gi 15228909 513 NKLAqdimkFCREKLPAY-WVPKSV-VFGPLPKTATGKIQKHILRTKAKE 560
Cdd:cd05944 314 ELLA-----WARDHVPERaAVPKHIeVLEELPVTAVGKVFKPALRADAIH 358
|
|
| PRK12406 |
PRK12406 |
long-chain-fatty-acid--CoA ligase; Provisional |
41-555 |
7.40e-40 |
|
long-chain-fatty-acid--CoA ligase; Provisional
Pssm-ID: 183506 [Multi-domain] Cd Length: 509 Bit Score: 152.16 E-value: 7.40e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228909 41 VIHGSREYTWRQTYDRCRRLASALADRSIGPGSTVAIIAPNIPAMYEAHFGVPMCGAVLNCVNIRLNAPTVAFLLSHSQS 120
Cdd:PRK12406 5 IISGDRRRSFDELAQRAARAAGGLAALGVRPGDCVALLMRNDFAFFEAAYAAMRLGAYAVPVNWHFKPEEIAYILEDSGA 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228909 121 SVIMVDQEFFTLAEDslRLMEEKAGSSFKRPLLIV----IGDHTCAPESlnralskGAIEYEDFLATGDPnypWQPPADE 196
Cdd:PRK12406 85 RVLIAHADLLHGLAS--ALPAGVTVLSVPTPPEIAaayrISPALLTPPA-------GAIDWEGWLAQQEP---YDGPPVP 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228909 197 wQSIALGYTSGTTASPKGV-----VLHHRGAYIMALSnpLIWGMQDGAVYLWTLPMFHCNGWCFPWSLAVLSGTSICLRQ 271
Cdd:PRK12406 153 -QPQSMIYTSGTTGHPKGVrraapTPEQAAAAEQMRA--LIYGLKPGIRALLTGPLYHSAPNAYGLRAGRLGGVLVLQPR 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228909 272 VTAKEVYSMIAKYKVTHFCAAPVVLNAIVNAPKE-----DTIlPLPHTVHvmtaGAAP-PPSVLFSM-NQKGFRVAHTYG 344
Cdd:PRK12406 230 FDPEELLQLIERHRITHMHMVPTMFIRLLKLPEEvrakyDVS-SLRHVIH----AAAPcPADVKRAMiEWWGPVIYEYYG 304
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228909 345 LSETyGPSTVCAwkPEwDSLP-PETQAKlnARQGVrytgmeQLDVIDtQTGKPVPADgkTAGEIVFR-GNMVMKGYLKNP 422
Cdd:PRK12406 305 STES-GAVTFAT--SE-DALShPGTVGK--AAPGA------ELRFVD-EDGRPLPQG--EIGEIYSRiAGNPDFTYHNKP 369
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228909 423 EANKETFAGGWFHSGDIAVKHPDNYIEIKDRSKDVIISGGENISSVEVENVVYHHPAVLEASVVARPDERWQESPCAFVt 502
Cdd:PRK12406 370 EKRAEIDRGGFITSGDVGYLDADGYLFLCDRKRDMVISGGVNIYPAEIEAVLHAVPGVHDCAVFGIPDAEFGEALMAVV- 448
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*
gi 15228909 503 lksdyEKHDQNKL-AQDIMKFCREKLPAYWVPKSVVFGP-LPKTATGKIQKHILR 555
Cdd:PRK12406 449 -----EPQPGATLdEADIRAQLKARLAGYKVPKHIEIMAeLPREDSGKIFKRRLR 498
|
|
| PRK04319 |
PRK04319 |
acetyl-CoA synthetase; Provisional |
46-562 |
9.87e-40 |
|
acetyl-CoA synthetase; Provisional
Pssm-ID: 235279 [Multi-domain] Cd Length: 570 Bit Score: 152.74 E-value: 9.87e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228909 46 REYTWRQTYDRCRRLASALADRSIGPGSTVAIIAPNIPAMYEAHFGVPMCGAVLncvnirlnAPTV-AFL-------LSH 117
Cdd:PRK04319 72 EKYTYKELKELSNKFANVLKELGVEKGDRVFIFMPRIPELYFALLGALKNGAIV--------GPLFeAFMeeavrdrLED 143
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228909 118 SQSSVIMVDQEFFTlaedslRLMEEKAgssfkrPLL---IVIGDHTCAPEslnralskGAIEYEDFLATGDPNYPwQPPA 194
Cdd:PRK04319 144 SEAKVLITTPALLE------RKPADDL------PSLkhvLLVGEDVEEGP--------GTLDFNALMEQASDEFD-IEWT 202
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228909 195 DEWQSIALGYTSGTTASPKGVVLHHR--------GAYIMALsnpliwgmQDGAVYlWtlpmfhCN---GWCF-------- 255
Cdd:PRK04319 203 DREDGAILHYTSGSTGKPKGVLHVHNamlqhyqtGKYVLDL--------HEDDVY-W------CTadpGWVTgtsygifa 267
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228909 256 PWslavLSGTSICLRQV--TAKEVYSMIAKYKVTHFCAAPVVLNAIVNAPKE-----DtilpLPHTVHVMTAGAaP--PP 326
Cdd:PRK04319 268 PW----LNGATNVIDGGrfSPERWYRILEDYKVTVWYTAPTAIRMLMGAGDDlvkkyD----LSSLRHILSVGE-PlnPE 338
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228909 327 SVLFSMNQKGFRVAHTYGLSETyGPSTVCawkpewdslppetqaklnarqgvRYTGMeqlDVIDTQTGKPVP-------- 398
Cdd:PRK04319 339 VVRWGMKVFGLPIHDNWWMTET-GGIMIA-----------------------NYPAM---DIKPGSMGKPLPgieaaivd 391
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228909 399 --ADGKTAGEIvfrGNMV--------MKGYLKNPEANKETFAGGWFHSGDIAVKHPDNYIEIKDRSKDVIISGGENISSV 468
Cdd:PRK04319 392 dqGNELPPNRM---GNLAikkgwpsmMRGIWNNPEKYESYFAGDWYVSGDSAYMDEDGYFWFQGRVDDVIKTSGERVGPF 468
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228909 469 EVENVVYHHPAVLEASVVARPDERWQESPCAFVTLKSDYEKHDQnkLAQDIMKFCREKLPAYWVPKSVVFGP-LPKTATG 547
Cdd:PRK04319 469 EVESKLMEHPAVAEAGVIGKPDPVRGEIIKAFVALRPGYEPSEE--LKEEIRGFVKKGLGAHAAPREIEFKDkLPKTRSG 546
|
570
....*....|....*
gi 15228909 548 KIQKHILrtKAKEMG 562
Cdd:PRK04319 547 KIMRRVL--KAWELG 559
|
|
| PLN02246 |
PLN02246 |
4-coumarate--CoA ligase |
12-557 |
1.13e-39 |
|
4-coumarate--CoA ligase
Pssm-ID: 215137 [Multi-domain] Cd Length: 537 Bit Score: 152.06 E-value: 1.13e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228909 12 LPKIP-ANYTALTPLWFlDRAAVVhPTRKSVIHGS--REYTWRQTYDRCRRLASALADRSIGPGSTVAIIAPNIPAMYEA 88
Cdd:PLN02246 14 LPDIYiPNHLPLHDYCF-ERLSEF-SDRPCLIDGAtgRVYTYADVELLSRRVAAGLHKLGIRQGDVVMLLLPNCPEFVLA 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228909 89 HFGVPMCGAVLNCVNIRLNAPTVAFLLSHSQSSVImvdqefFTLAEDSLRLMEEKAGSSFKrplLIVIGDHT--CAPESL 166
Cdd:PLN02246 92 FLGASRRGAVTTTANPFYTPAEIAKQAKASGAKLI------ITQSCYVDKLKGLAEDDGVT---VVTIDDPPegCLHFSE 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228909 167 NRALSKGAIEYEDFlatgDPNYPwqppadewqsIALGYTSGTTASPKGVVLHHRG-----AYIMALSNP-LIWGMQDgaV 240
Cdd:PLN02246 163 LTQADENELPEVEI----SPDDV----------VALPYSSGTTGLPKGVMLTHKGlvtsvAQQVDGENPnLYFHSDD--V 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228909 241 YLWTLPMFHCngwcfpWSL-AVL-----SGTSICL-RQVTAKEVYSMIAKYKVTHFCAAPVVLNAIVNAP---KEDTilp 310
Cdd:PLN02246 227 ILCVLPMFHI------YSLnSVLlcglrVGAAILImPKFEIGALLELIQRHKVTIAPFVPPIVLAIAKSPvveKYDL--- 297
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228909 311 lpHTVHVMTAGAAPPPSVLfsmnQKGFR-------VAHTYGLSETyGPstVCAWKPEWDSLPPETQAklnarqG-----V 378
Cdd:PLN02246 298 --SSIRMVLSGAAPLGKEL----EDAFRaklpnavLGQGYGMTEA-GP--VLAMCLAFAKEPFPVKS------GscgtvV 362
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228909 379 RYTgmeQLDVIDTQTGKPVPADgkTAGEIVFRGNMVMKGYLKNPEANKETF-AGGWFHSGDIAVKHPDNYIEIKDRSKDV 457
Cdd:PLN02246 363 RNA---ELKIVDPETGASLPRN--QPGEICIRGPQIMKGYLNDPEATANTIdKDGWLHTGDIGYIDDDDELFIVDRLKEL 437
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228909 458 IISGGENISSVEVENVVYHHPAVLEASVVARPDERWQESPCAFVTLKSDYEKHDqnklaQDIMKFCREKLPAYWVPKSVV 537
Cdd:PLN02246 438 IKYKGFQVAPAELEALLISHPSIADAAVVPMKDEVAGEVPVAFVVRSNGSEITE-----DEIKQFVAKQVVFYKRIHKVF 512
|
570 580
....*....|....*....|.
gi 15228909 538 FGP-LPKTATGKIQKHILRTK 557
Cdd:PLN02246 513 FVDsIPKAPSGKILRKDLRAK 533
|
|
| PRK07787 |
PRK07787 |
acyl-CoA synthetase; Validated |
182-556 |
4.32e-39 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236096 [Multi-domain] Cd Length: 471 Bit Score: 148.98 E-value: 4.32e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228909 182 ATGDPNYPwQPPADewqSIAL-GYTSGTTASPKGVVLHHRG--AYIMALSNPLIWGMQDGAVYlwTLPMFHCNGWCfpws 258
Cdd:PRK07787 116 ARSWHRYP-EPDPD---APALiVYTSGTTGPPKGVVLSRRAiaADLDALAEAWQWTADDVLVH--GLPLFHVHGLV---- 185
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228909 259 LAVLSGTSICLRQV-TAK---EVYSMIAKYKVTHFCAAPVVLNAIVNAPKEDTIL-----------PLPHTVHVMTAGAA 323
Cdd:PRK07787 186 LGVLGPLRIGNRFVhTGRptpEAYAQALSEGGTLYFGVPTVWSRIAADPEAARALrgarllvsgsaALPVPVFDRLAALT 265
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228909 324 pppsvlfsmnqkGFRVAHTYGLSETYGPSTVCA---WKPEWDSLPpetqaklnaRQGVrytgmeQLDVIDtQTGKPVPAD 400
Cdd:PRK07787 266 ------------GHRPVERYGMTETLITLSTRAdgeRRPGWVGLP---------LAGV------ETRLVD-EDGGPVPHD 317
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228909 401 GKTAGEIVFRGNMVMKGYLKNPEANKETF-AGGWFHSGDIAVKHPDNYIEIKDR-SKDVIISGGENISSVEVENVVYHHP 478
Cdd:PRK07787 318 GETVGELQVRGPTLFDGYLNRPDATAAAFtADGWFRTGDVAVVDPDGMHRIVGReSTDLIKSGGYRIGAGEIETALLGHP 397
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 15228909 479 AVLEASVVARPDERWQESPCAFVTLKSDYEkhdqnklAQDIMKFCREKLPAYWVPKSVVFGP-LPKTATGKIQKHILRT 556
Cdd:PRK07787 398 GVREAAVVGVPDDDLGQRIVAYVVGADDVA-------ADELIDFVAQQLSVHKRPREVRFVDaLPRNAMGKVLKKQLLS 469
|
|
| OSB_MenE-like |
cd17630 |
O-succinylbenzoic acid-CoA ligase; This family contains O-succinylbenzoyl-CoA (OSB-CoA) ... |
205-558 |
7.05e-39 |
|
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: 145.17 E-value: 7.05e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228909 205 TSGTTASPKGVVLHHRG--AYIMALSNPLiwGMQDGAVYLWTLPMFHCNGWcFPWSLAVLSGTSICLRQVTAkEVYSMIA 282
Cdd:cd17630 8 TSGSTGTPKAVVHTAANllASAAGLHSRL--GFGGGDSWLLSLPLYHVGGL-AILVRSLLAGAELVLLERNQ-ALAEDLA 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228909 283 KYKVTHFCAAPVVLNAIVNAPKedTILPLPHTVHVMTAGAAPPPSVLFSMNQKGFRVAHTYGLSETygPSTVCAWKPewd 362
Cdd:cd17630 84 PPGVTHVSLVPTQLQRLLDSGQ--GPAALKSLRAVLLGGAPIPPELLERAADRGIPLYTTYGMTET--ASQVATKRP--- 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228909 363 slpPETQAklnARQGVRYTGMEqLDVIDTqtgkpvpadgktaGEIVFRGNMVMKGYLKNPEANkETFAGGWFHSGDIAVK 442
Cdd:cd17630 157 ---DGFGR---GGVGVLLPGRE-LRIVED-------------GEIWVGGASLAMGYLRGQLVP-EFNEDGWFTTKDLGEL 215
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228909 443 HPDNYIEIKDRSKDVIISGGENISSVEVENVVYHHPAVLEASVVARPDERWQESPCAFVTLksdyekhDQNKLAQDIMKF 522
Cdd:cd17630 216 HADGRLTVLGRADNMIISGGENIQPEEIEAALAAHPAVRDAFVVGVPDEELGQRPVAVIVG-------RGPADPAELRAW 288
|
330 340 350
....*....|....*....|....*....|....*..
gi 15228909 523 CREKLPAYWVPKSVVFGP-LPKTATGKIQKHILRTKA 558
Cdd:cd17630 289 LKDKLARFKLPKRIYPVPeLPRTGGGKVDRRALRAWL 325
|
|
| MACS_AAE_MA_like |
cd05970 |
Medium-chain acyl-CoA synthetase (MACS) of AAE_MA like; MACS catalyzes the two-step activation ... |
28-557 |
8.40e-39 |
|
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: 149.57 E-value: 8.40e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228909 28 LDRAAVVHPTRKSVIH-----GSREYTWRQTYDRCRRLASALADRSIGPGSTVAIIapnIPAMYEAHFGVP---MCGAVL 99
Cdd:cd05970 23 VDAMAKEYPDKLALVWcddagEERIFTFAELADYSDKTANFFKAMGIGKGDTVMLT---LKRRYEFWYSLLalhKLGAIA 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228909 100 NCVNIRLNAPTVAFLLSHSQSSVIMVDQEfftlaEDSLRLMEEKAGSSFKRPLLIVIGDhtcapeslnrALSKGAIEYED 179
Cdd:cd05970 100 IPATHQLTAKDIVYRIESADIKMIVAIAE-----DNIPEEIEKAAPECPSKPKLVWVGD----------PVPEGWIDFRK 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228909 180 FLATGDPNYPwqPPADEWQS----IALGY-TSGTTASPKGVvlHHRGAYIMA-LSNPLIW-GMQDGAVYLWTLPMfhcng 252
Cdd:cd05970 165 LIKNASPDFE--RPTANSYPcgedILLVYfSSGTTGMPKMV--EHDFTYPLGhIVTAKYWqNVREGGLHLTVADT----- 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228909 253 wcfPWSLAV---LSGTSIC--------LRQVTAKEVYSMIAKYKVTHFCAAPVVLNAIVnapKED-TILPLPHTVHVMTA 320
Cdd:cd05970 236 ---GWGKAVwgkIYGQWIAgaavfvydYDKFDPKALLEKLSKYGVTTFCAPPTIYRFLI---REDlSRYDLSSLRYCTTA 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228909 321 GAAPPPSVLFSMNQK-GFRVAHTYGLSETygpsTVCAWKPEWDSLPPETQAKLNARQGVrytgmeqlDVIDTQtGKPVPA 399
Cdd:cd05970 310 GEALNPEVFNTFKEKtGIKLMEGFGQTET----TLTIATFPWMEPKPGSMGKPAPGYEI--------DLIDRE-GRSCEA 376
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228909 400 DgkTAGEIVFRGNM-----VMKGYLKNPEANKETFAGGWFHSGDIAVKHPDNYIEIKDRSKDVIISGGENISSVEVENVV 474
Cdd:cd05970 377 G--EEGEIVIRTSKgkpvgLFGGYYKDAEKTAEVWHDGYYHTGDAAWMDEDGYLWFVGRTDDLIKSSGYRIGPFEVESAL 454
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228909 475 YHHPAVLEASVVARPDERWQESPCAFVTLKSDYEKHDQnkLAQDIMKFCREKLPAYWVPKSVVFGP-LPKTATGKIQKHI 553
Cdd:cd05970 455 IQHPAVLECAVTGVPDPIRGQVVKATIVLAKGYEPSEE--LKKELQDHVKKVTAPYKYPRIVEFVDeLPKTISGKIRRVE 532
|
....
gi 15228909 554 LRTK 557
Cdd:cd05970 533 IRER 536
|
|
| PRK07059 |
PRK07059 |
Long-chain-fatty-acid--CoA ligase; Validated |
8-559 |
1.24e-38 |
|
Long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 235923 [Multi-domain] Cd Length: 557 Bit Score: 149.40 E-value: 1.24e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228909 8 DIDdlpkiPANYTALTPLwfLDRAAVVHPTRKSVIHGSREYTWRQTYDRCRRLASALADRSIGPGSTVAIIAPNIPAMYE 87
Cdd:PRK07059 16 EID-----ASQYPSLADL--LEESFRQYADRPAFICMGKAITYGELDELSRALAAWLQSRGLAKGARVAIMMPNVLQYPV 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228909 88 AHFGVPMCGAVLNCVNIRLNAPTVAFLLSHSQSSVIMVDQEFFTLAEDSLrlmeekAGSSFKRPLLIVIGDHTCAPESL- 166
Cdd:PRK07059 89 AIAAVLRAGYVVVNVNPLYTPRELEHQLKDSGAEAIVVLENFATTVQQVL------AKTAVKHVVVASMGDLLGFKGHIv 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228909 167 N---RALSK--------GAIEYEDFLATGDpNYPWQPPADEWQSIA-LGYTSGTTASPKGVVLHHRGAyimaLSNPL--- 231
Cdd:PRK07059 163 NfvvRRVKKmvpawslpGHVRFNDALAEGA-RQTFKPVKLGPDDVAfLQYTGGTTGVSKGATLLHRNI----VANVLqme 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228909 232 IWgMQ---------DGAVYLWTLPMFHCngwcfpWSLAV-------LSGTSICL---RQVTA--KEvysmIAKYKVTHFC 290
Cdd:PRK07059 238 AW-LQpafekkprpDQLNFVCALPLYHI------FALTVcgllgmrTGGRNILIpnpRDIPGfiKE----LKKYQVHIFP 306
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228909 291 AAPVVLNAIVNAPKEDTiLPLPHTVHVMTAGAAPPPSVLFSMNQK-GFRVAHTYGLSETyGPSTVCawkpewdslppetq 369
Cdd:PRK07059 307 AVNTLYNALLNNPDFDK-LDFSKLIVANGGGMAVQRPVAERWLEMtGCPITEGYGLSET-SPVATC-------------- 370
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228909 370 aklNARQGVRYTG-----MEQLDV-IDTQTGKPVPADgkTAGEIVFRGNMVMKGYLKNP-EANKETFAGGWFHSGDIAVK 442
Cdd:PRK07059 371 ---NPVDATEFSGtiglpLPSTEVsIRDDDGNDLPLG--EPGEICIRGPQVMAGYWNRPdETAKVMTADGFFRTGDVGVM 445
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228909 443 HPDNYIEIKDRSKDVIISGGENISSVEVENVVYHHPAVLEASVVARPDERWQESPCAFVTlksdyeKHDQNKLAQDIMKF 522
Cdd:PRK07059 446 DERGYTKIVDRKKDMILVSGFNVYPNEIEEVVASHPGVLEVAAVGVPDEHSGEAVKLFVV------KKDPALTEEDVKAF 519
|
570 580 590
....*....|....*....|....*....|....*...
gi 15228909 523 CREKLPAYWVPKSVVF-GPLPKTATGKIQKHILRTKAK 559
Cdd:PRK07059 520 CKERLTNYKRPKFVEFrTELPKTNVGKILRRELRDGKA 557
|
|
| ABCL |
cd05958 |
2-aminobenzoate-CoA ligase (ABCL); ABCL catalyzes the initial step in the 2-aminobenzoate ... |
38-555 |
2.19e-38 |
|
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: 146.47 E-value: 2.19e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228909 38 RKSVIHGSREYTWRQTYDRCRRLASALADR-SIGPGSTVAIIAPNIPAMYEAHFGVPMCGAVLNCVNIRLNAPTVAFLLS 116
Cdd:cd05958 1 RTCLRSPEREWTYRDLLALANRIANVLVGElGIVPGNRVLLRGSNSPELVACWFGIQKAGAIAVATMPLLRPKELAYILD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228909 117 HSQSSVIMVDQEFfTLAEDslrlmeekagssfkrpllivigdhTCApeslnralskgaieyedflatgdpnypwqppade 196
Cdd:cd05958 81 KARITVALCAHAL-TASDD------------------------ICI---------------------------------- 101
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228909 197 wqsiaLGYTSGTTASPKGVVLHHRGAYIMA-LSNPLIWGMQDGAVYLWTLPMFHCNGW----CFPWSLavlsGTS-ICLR 270
Cdd:cd05958 102 -----LAFTSGTTGAPKATMHFHRDPLASAdRYAVNVLRLREDDRFVGSPPLAFTFGLggvlLFPFGV----GASgVLLE 172
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228909 271 QVTAKEVYSMIAKYKVTHFCAAPVVLNAIVNAPKEDT--ILPLPHTVhvmTAGAAPPPSVLFSMNQK-GFRVAHTYGLSE 347
Cdd:cd05958 173 EATPDLLLSAIARYKPTVLFTAPTAYRAMLAHPDAAGpdLSSLRKCV---SAGEALPAALHRAWKEAtGIPIIDGIGSTE 249
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228909 348 TYgpstvcawkpewdslppetQAKLNARQGVRYTGmeqldvidtQTGKPVP--------ADGKT--AGEIvfrGNMVMKG 417
Cdd:cd05958 250 MF-------------------HIFISARPGDARPG---------ATGKPVPgyeakvvdDEGNPvpDGTI---GRLAVRG 298
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228909 418 -----YLKNPEANKeTFAGGWFHSGDIAVKHPDNYIEIKDRSKDVIISGGENISSVEVENVVYHHPAVLEASVVARPDER 492
Cdd:cd05958 299 ptgcrYLADKRQRT-YVQGGWNITGDTYSRDPDGYFRHQGRSDDMIVSGGYNIAPPEVEDVLLQHPAVAECAVVGHPDES 377
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 15228909 493 WQESPCAFVTLKSDYEKHDQnkLAQDIMKFCREKLPAYWVPKSVVF-GPLPKTATGKIQKHILR 555
Cdd:cd05958 378 RGVVVKAFVVLRPGVIPGPV--LARELQDHAKAHIAPYKYPRAIEFvTELPRTATGKLQRFALR 439
|
|
| ligase_PEP_1 |
TIGR03098 |
acyl-CoA ligase (AMP-forming), exosortase A-associated; This group of proteins contains an ... |
28-554 |
2.51e-38 |
|
acyl-CoA ligase (AMP-forming), exosortase A-associated; This group of proteins contains an AMP-binding domain (pfam00501) associated with acyl CoA-ligases. These proteins are generally found in genomes containing the exosortase/PEP-CTERM protein expoert system, specifically the type 1 variant of this system described by the Genome Property GenProp0652. When found in this context they are invariably present next to a decarboxylase enzyme. A number of sequences from Burkholderia species also hit this model, but the genomic context is obviously different. The hypothesis of a constant substrate for this family is only strong where the exosortase context is present.
Pssm-ID: 211788 [Multi-domain] Cd Length: 517 Bit Score: 148.01 E-value: 2.51e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228909 28 LDRAAVVHPTRKSVIHGSREYTWRQTYDRCRRLASALADRSIGPGSTVAIIAPNIPAMYEAHFGVPMCGAVLNCVNIRLN 107
Cdd:TIGR03098 6 LEDAAARLPDATALVHHDRTLTYAALSERVLALASGLRGLGLARGERVAIYLDKRLETVTAMFGAALAGGVFVPINPLLK 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228909 108 APTVAFLLSHSQSSVIMVDQEFFTLAEDSLrlmeekAGSSFKRPLLIViGDHTCAPESLNRALSkgaIEYEDFLATGDPn 187
Cdd:TIGR03098 86 AEQVAHILADCNVRLLVTSSERLDLLHPAL------PGCHDLRTLIIV-GDPAHASEGHPGEEP---ASWPKLLALGDA- 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228909 188 ypwQPPADEWQS--IALGYTSGTTASPKGVVLHHRGayimalsnpLIWGMQDGAVYL---------WTLPMfhcngwCFP 256
Cdd:TIGR03098 155 ---DPPHPVIDSdmAAILYTSGSTGRPKGVVLSHRN---------LVAGAQSVATYLenrpddrllAVLPL------SFD 216
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228909 257 WSL-----AVLSGTSICLRQ-VTAKEVYSMIAKYKVTHFCAAPVVLNAIVNA--PKEDTilplPHTVHVMTAGAAPPPSV 328
Cdd:TIGR03098 217 YGFnqlttAFYVGATVVLHDyLLPRDVLKALEKHGITGLAAVPPLWAQLAQLdwPESAA----PSLRYLTNSGGAMPRAT 292
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228909 329 LFSMNQK--GFRVAHTYGLSETYGPSTvcawkpewdsLPPetqaklnarqgvrytgmEQLDVIDTQTGKPVP-------- 398
Cdd:TIGR03098 293 LSRLRSFlpNARLFLMYGLTEAFRSTY----------LPP-----------------EEVDRRPDSIGKAIPnaevlvlr 345
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228909 399 ADGKTA-----GEIVFRGNMVMKGYLKNPEANKETF------------AGGWFHSGDIAVKHPDNYIEIKDRSKDVIISG 461
Cdd:TIGR03098 346 EDGSECapgeeGELVHRGALVAMGYWNDPEKTAERFrplppfpgelhlPELAVWSGDTVRRDEEGFLYFVGRRDEMIKTS 425
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228909 462 GENISSVEVENVVYHHPAVLEASVVARPDERWQESPCAFVTLKSDYEKHdqnklAQDIMKFCREKLPAYWVPKSVVF-GP 540
Cdd:TIGR03098 426 GYRVSPTEVEEVAYATGLVAEAVAFGVPDPTLGQAIVLVVTPPGGEELD-----RAALLAECRARLPNYMVPALIHVrQA 500
|
570
....*....|....
gi 15228909 541 LPKTATGKIQKHIL 554
Cdd:TIGR03098 501 LPRNANGKIDRKAL 514
|
|
| LC_FACL_like |
cd05914 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); The members of this family are ... |
41-554 |
2.61e-38 |
|
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: 146.82 E-value: 2.61e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228909 41 VIHGSREYTWRQTYDRCRRLASALADRSIGPGSTVAIIAPNIPAMYEAHFGVPMCGAVLNCVNIRLNAPTVAFLLSHSQS 120
Cdd:cd05914 1 LYYGGEPLTYKDLADNIAKFALLLKINGVGTGDRVALMGENRPEWGIAFFAIWTYGAIAVPILAEFTADEVHHILNHSEA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228909 121 SVImvdqefFTLAEDSLRLmeekagssfkrpllivigdhtcapeslnralskgaieyedflatgdpnypwqppadewqsi 200
Cdd:cd05914 81 KAI------FVSDEDDVAL------------------------------------------------------------- 93
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228909 201 aLGYTSGTTASPKGVVLHHRG--AYIMALSNPLIWGMQDgaVYLWTLPMFHCNGWCFPWSLAVLSGTSICLRQVTAKEVY 278
Cdd:cd05914 94 -INYTSGTTGNSKGVMLTYRNivSNVDGVKEVVLLGKGD--KILSILPLHHIYPLTFTLLLPLLNGAHVVFLDKIPSAKI 170
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228909 279 SMIAKYKVTHFCAAPVVL-------NAIVNA-------------PKEDTILPLP----------HTVHVMTAGAAPPPSV 328
Cdd:cd05914 171 IALAFAQVTPTLGVPVPLviekifkMDIIPKltlkkfkfklakkINNRKIRKLAfkkvheafggNIKEFVIGGAKINPDV 250
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228909 329 LFSMNQKGFRVAHTYGLSETyGPsTVCawkpewdSLPPETQaKLNArqgvryTGmEQLDVIDTQTGKPVPADGktAGEIV 408
Cdd:cd05914 251 EEFLRTIGFPYTIGYGMTET-AP-IIS-------YSPPNRI-RLGS------AG-KVIDGVEVRIDSPDPATG--EGEII 311
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228909 409 FRGNMVMKGYLKNPEANKETF-AGGWFHSGDIAVKHPDNYIEIKDRSKDVIISG-GENISSVEVENVVYHHPAVLEASVV 486
Cdd:cd05914 312 VRGPNVMKGYYKNPEATAEAFdKDGWFHTGDLGKIDAEGYLYIRGRKKEMIVLSsGKNIYPEEIEAKINNMPFVLESLVV 391
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 15228909 487 ARPDERwqespCAFVTLKSDYEKHDQNKLAQDIMKFCRE-------KLPAY--WVPKSVVFGPLPKTATGKIQKHIL 554
Cdd:cd05914 392 VQEKKL-----VALAYIDPDFLDVKALKQRNIIDAIKWEvrdkvnqKVPNYkkISKVKIVKEEFEKTPKGKIKRFLY 463
|
|
| PRK06164 |
PRK06164 |
acyl-CoA synthetase; Validated |
28-561 |
1.39e-37 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 235722 [Multi-domain] Cd Length: 540 Bit Score: 146.04 E-value: 1.39e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228909 28 LDRAAVVHPTRKSVIHGSREYTWRQTYDRCRRLASALADRSIGPGSTVAIIAPNIPAMYEAHFGVPMCGAVLNCVNIRLN 107
Cdd:PRK06164 16 LDAHARARPDAVALIDEDRPLSRAELRALVDRLAAWLAAQGVRRGDRVAVWLPNCIEWVVLFLACARLGATVIAVNTRYR 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228909 108 APTVAFLLSHSQSSVIMVDQEFFTLaeDSLRLMEEKAGSSFKR-PLLIVIGDhtcAPESLNRALSKGAIEYEDFLATGDP 186
Cdd:PRK06164 96 SHEVAHILGRGRARWLVVWPGFKGI--DFAAILAAVPPDALPPlRAIAVVDD---AADATPAPAPGARVQLFALPDPAPP 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228909 187 NYPWQPPADEWQSIALGYTSGTTASPKGV------VLHHRGAYIMALsnpliwGMQDGAVYLWTLPMfhCNGWCFPWSLA 260
Cdd:PRK06164 171 AAAGERAADPDAGALLFTTSGTTSGPKLVlhrqatLLRHARAIARAY------GYDPGAVLLAALPF--CGVFGFSTLLG 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228909 261 VLSG--TSICLRQVTAKEVYSMIAKYKVTHFCAAPVVLNAIVNAPKEDTilPLPHTVHVMTAGAAPPPSVLFSMNQKgfR 338
Cdd:PRK06164 243 ALAGgaPLVCEPVFDAARTARALRRHRVTHTFGNDEMLRRILDTAGERA--DFPSARLFGFASFAPALGELAALARA--R 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228909 339 VAHTYGLsetYGPSTVCAWKPEWDSLPPEtQAKLNArQGVRYTGMEQLDVIDTQTGKPVPaDGKTaGEIVFRGNMVMKGY 418
Cdd:PRK06164 319 GVPLTGL---YGSSEVQALVALQPATDPV-SVRIEG-GGRPASPEARVRARDPQDGALLP-DGES-GEIEIRAPSLMRGY 391
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228909 419 LKNPEANKETF-AGGWFHSGDIAVKHPDNYIEIKDRSKDVIISGGENISSVEVENVVYHHPAVLEASVVArPDERWQESP 497
Cdd:PRK06164 392 LDNPDATARALtDDGYFRTGDLGYTRGDGQFVYQTRMGDSLRLGGFLVNPAEIEHALEALPGVAAAQVVG-ATRDGKTVP 470
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 15228909 498 CAFVTLkSDYEKHDQnklaQDIMKFCREKLPAYWVPKSVVF-GPLPKTATG---KIQKHILRTKAKEM 561
Cdd:PRK06164 471 VAFVIP-TDGASPDE----AGLMAACREALAGFKVPARVQVvEAFPVTESAngaKIQKHRLREMAQAR 533
|
|
| FADD10 |
cd17635 |
adenylate forming domain, fatty acid CoA ligase (FadD10); This family contains long chain ... |
204-551 |
5.37e-37 |
|
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: 140.47 E-value: 5.37e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228909 204 YTSGTTASPKGVVLHHRGAYiMALSNPLIWGMQ--DGAVYLWTLPMFHCNGwcFPWSLAVLSGTSICL---RQVTAKEVY 278
Cdd:cd17635 8 FTSGTTGEPKAVLLANKTFF-AVPDILQKEGLNwvVGDVTYLPLPATHIGG--LWWILTCLIHGGLCVtggENTTYKSLF 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228909 279 SMIAKYKVTHFCAAPVVLNAIVNAPKeDTILPLPHTVHVMTAGAAP-PPSVLFSMNQKGFRVAHTYGLSETygpSTVCAW 357
Cdd:cd17635 85 KILTTNAVTTTCLVPTLLSKLVSELK-SANATVPSLRLIGYGGSRAiAADVRFIEATGLTNTAQVYGLSET---GTALCL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228909 358 KPEWDSLppetqaKLNArQGVRYTGMEqLDVIDTQtGKPVPADGKtaGEIVFRGNMVMKGYLKNPEANKETFAGGWFHSG 437
Cdd:cd17635 161 PTDDDSI------EINA-VGRPYPGVD-VYLAATD-GIAGPSASF--GTIWIKSPANMLGYWNNPERTAEVLIDGWVNTG 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228909 438 DIAVKHPDNYIEIKDRSKDVIISGGENISSVEVENVVYHHPAVLEASVVARPDERWQESPCAFVTLKsdyEKHDQNKLAQ 517
Cdd:cd17635 230 DLGERREDGFLFITGRSSESINCGGVKIAPDEVERIAEGVSGVQECACYEISDEEFGELVGLAVVAS---AELDENAIRA 306
|
330 340 350
....*....|....*....|....*....|....*
gi 15228909 518 DIMKFCREkLPAYWVPKSVVF-GPLPKTATGKIQK 551
Cdd:cd17635 307 LKHTIRRE-LEPYARPSTIVIvTDIPRTQSGKVKR 340
|
|
| PRK13390 |
PRK13390 |
acyl-CoA synthetase; Provisional |
16-555 |
1.15e-36 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 139538 [Multi-domain] Cd Length: 501 Bit Score: 142.84 E-value: 1.15e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228909 16 PANYTALTPlwflDRAAVVhptrksVIHGSREYTWRQTYDRCRRLASALADRSIGPGSTVAIIAPNIPAMYEAHFGVPMC 95
Cdd:PRK13390 3 PGTHAQIAP----DRPAVI------VAETGEQVSYRQLDDDSAALARVLYDAGLRTGDVVALLSDNSPEALVVLWAALRS 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228909 96 GAVLNCVNIRLNAPTVAFLLSHSQSSVImvdqefftLAEDSLRLMEEKAGSSFkrPLLIVIGDHTcapeslnralsKGAI 175
Cdd:PRK13390 73 GLYITAINHHLTAPEADYIVGDSGARVL--------VASAALDGLAAKVGADL--PLRLSFGGEI-----------DGFG 131
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228909 176 EYEDFLATGDPNYPWQPPAdewqSIALgYTSGTTASPKGVVLHHRGAYIMALSNPLI------WGMQDGAVYLWTLPMFH 249
Cdd:PRK13390 132 SFEAALAGAGPRLTEQPCG----AVML-YSSGTTGFPKGIQPDLPGRDVDAPGDPIVaiarafYDISESDIYYSSAPIYH 206
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228909 250 CNG--WCfpWSLAVLSGTSICLRQVTAKEVYSMIAKYKVTHFCAAPVVLNAIVNAPKE-DTILPLPHTVHVMTAGAAPPP 326
Cdd:PRK13390 207 AAPlrWC--SMVHALGGTVVLAKRFDAQATLGHVERYRITVTQMVPTMFVRLLKLDADvRTRYDVSSLRAVIHAAAPCPV 284
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228909 327 SVLFSM-NQKGFRVAHTYGLSETYGPSTVCAwkPEWDSLPpetqaklnarQGVRYTGMEQLDVIDTQtGKPVPAdGKTaG 405
Cdd:PRK13390 285 DVKHAMiDWLGPIVYEYYSSTEAHGMTFIDS--PDWLAHP----------GSVGRSVLGDLHICDDD-GNELPA-GRI-G 349
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228909 406 EIVFRGNMVMKGYLKNPEANKETFAGG---WFHSGDIAVKHPDNYIEIKDRSKDVIISGGENISSVEVENVVYHHPAVLE 482
Cdd:PRK13390 350 TVYFERDRLPFRYLNDPEKTAAAQHPAhpfWTTVGDLGSVDEDGYLYLADRKSFMIISGGVNIYPQETENALTMHPAVHD 429
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 15228909 483 ASVVARPDERWQESPCAFVTLKSDYEKHDQnkLAQDIMKFCREKLPAYWVPKSVVF-GPLPKTATGKIQKHILR 555
Cdd:PRK13390 430 VAVIGVPDPEMGEQVKAVIQLVEGIRGSDE--LARELIDYTRSRIAHYKAPRSVEFvDELPRTPTGKLVKGLLR 501
|
|
| PRK13382 |
PRK13382 |
bile acid CoA ligase; |
31-557 |
1.28e-36 |
|
bile acid CoA ligase;
Pssm-ID: 172019 [Multi-domain] Cd Length: 537 Bit Score: 143.36 E-value: 1.28e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228909 31 AAVVHPTRKSVIHGSREYTWRQTYDRCRRLASALADRSIGPGSTVAIIAPNIPAMYEAHFGVPMCGAVLNCVNIRLNAPT 110
Cdd:PRK13382 52 AAQRCPDRPGLIDELGTLTWRELDERSDALAAALQALPIGEPRVVGIMCRNHRGFVEALLAANRIGADILLLNTSFAGPA 131
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228909 111 VAFLLSHSQSSVIMVDQEFFTLAEDSLRlmeekagssfKRPLLIVIGDHTCAPESLN-RALSKGAIEYedflatgdpnyp 189
Cdd:PRK13382 132 LAEVVTREGVDTVIYDEEFSATVDRALA----------DCPQATRIVAWTDEDHDLTvEVLIAAHAGQ------------ 189
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228909 190 wQPPADEWQSIALGYTSGTTASPKGVVLHHRGAYiMALSNPL---IWGMQDGAVYlwTLPMFHcnGWCFPWSL--AVLSG 264
Cdd:PRK13382 190 -RPEPTGRKGRVILLTSGTTGTPKGARRSGPGGI-GTLKAILdrtPWRAEEPTVI--VAPMFH--AWGFSQLVlaASLAC 263
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228909 265 TSICLRQVTAKEVYSMIAKYKVTHFCAAPVVLNAIVNAPKEDTILPLPHTVHVMTA-GAAPPPSVLFS-MNQKGFRVAHT 342
Cdd:PRK13382 264 TIVTRRRFDPEATLDLIDRHRATGLAVVPVMFDRIMDLPAEVRNRYSGRSLRFAAAsGSRMRPDVVIAfMDQFGDVIYNN 343
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228909 343 YGLSETYGPSTvcawkpewdSLPPETQAKLNArQGVRYTGMEqLDVIDtQTGKPVPaDGKTaGEIVFRGNMVMKGYlkNP 422
Cdd:PRK13382 344 YNATEAGMIAT---------ATPADLRAAPDT-AGRPAEGTE-IRILD-QDFREVP-TGEV-GTIFVRNDTQFDGY--TS 407
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228909 423 EANKEtFAGGWFHSGDIAVKHPDNYIEIKDRSKDVIISGGENISSVEVENVVYHHPAVLEASVVARPDERWQESPCAFVT 502
Cdd:PRK13382 408 GSTKD-FHDGFMASGDVGYLDENGRLFVVGRDDEMIVSGGENVYPIEVEKTLATHPDVAEAAVIGVDDEQYGQRLAAFVV 486
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*.
gi 15228909 503 LKSdyekhDQNKLAQDIMKFCREKLPAYWVPKS-VVFGPLPKTATGKIQKHILRTK 557
Cdd:PRK13382 487 LKP-----GASATPETLKQHVRDNLANYKVPRDiVVLDELPRGATGKILRRELQAR 537
|
|
| FACL_like_6 |
cd05922 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
59-549 |
1.52e-36 |
|
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: 141.81 E-value: 1.52e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228909 59 RLASALADRSIGPGSTVAIIAPNIPAMYEAHFGVPMCGAVLNCVNIRLNAPTVAFLLSHsqssvIMvdqeffTLAEDSLR 138
Cdd:cd05922 5 AAASALLEAGGVRGERVVLILPNRFTYIELSFAVAYAGGRLGLVFVPLNPTLKESVLRY-----LV------ADAGGRIV 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228909 139 LMEEKAGSSFkRPLLIVIGDHTCApeslnralskgaIEYEDFLATGDPNyPWQPPADEwQSIALGYTSGTTASPKGVVLH 218
Cdd:cd05922 74 LADAGAADRL-RDALPASPDPGTV------------LDADGIRAARASA-PAHEVSHE-DLALLLYTSGSTGSPKLVRLS 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228909 219 HRGayimalsnpLIWGMQDGAVYL---------WTLPMfhcnGWCFPWSL---AVLSGTSICL--RQVTAKEVYSMIAKY 284
Cdd:cd05922 139 HQN---------LLANARSIAEYLgitaddralTVLPL----SYDYGLSVlntHLLRGATLVLtnDGVLDDAFWEDLREH 205
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228909 285 KVTHFCAAPVvLNAIVNAPKEDTIlPLPHTVHVMTAGAAPPPSVLFSMNQK--GFRVAHTYGLSETYGPSTVcawkpewd 362
Cdd:cd05922 206 GATGLAGVPS-TYAMLTRLGFDPA-KLPSLRYLTQAGGRLPQETIARLRELlpGAQVYVMYGQTEATRRMTY-------- 275
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228909 363 sLPPETQAKLNARQGVRYTGMEQldVIDTQTGKPVPAdgKTAGEIVFRGNMVMKGYLKNP-EANKETFAGGWFHSGDIAV 441
Cdd:cd05922 276 -LPPERILEKPGSIGLAIPGGEF--EILDDDGTPTPP--GEPGEIVHRGPNVMKGYWNDPpYRRKEGRGGGVLHTGDLAR 350
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228909 442 KHPDNYIEIKDRSKDVIISGGENISSVEVENVVYHHPAVLEASVVARPDERwQESPCAFVTLKSDYEKHdqnklaqDIMK 521
Cdd:cd05922 351 RDEDGFLFIVGRRDRMIKLFGNRISPTEIEAAARSIGLIIEAAAVGLPDPL-GEKLALFVTAPDKIDPK-------DVLR 422
|
490 500
....*....|....*....|....*....
gi 15228909 522 FCREKLPAYWVPKSVVF-GPLPKTATGKI 549
Cdd:cd05922 423 SLAERLPPYKVPATVRVvDELPLTASGKV 451
|
|
| PrpE |
cd05967 |
Propionyl-CoA synthetase (PrpE); EC 6.2.1.17: propanoate:CoA ligase (AMP-forming) or ... |
29-555 |
2.25e-36 |
|
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: 143.61 E-value: 2.25e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228909 29 DRAAVVHPTrkSVIHGSREYTWRQTYDRCRRLASALADRSIGPGSTVAIIAPNIPamyEAHFGVPMC---GAVLNCVNIR 105
Cdd:cd05967 66 DQIALIYDS--PVTGTERTYTYAELLDEVSRLAGVLRKLGVVKGDRVIIYMPMIP---EAAIAMLACariGAIHSVVFGG 140
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228909 106 LNAPTVAFLLSHSQSSVIMVDQ---------EFFTLAEDSLRLmeekAGSSFKRPLLIVIGDHTCAPESLNRALskgaiE 176
Cdd:cd05967 141 FAAKELASRIDDAKPKLIVTAScgiepgkvvPYKPLLDKALEL----SGHKPHHVLVLNRPQVPADLTKPGRDL-----D 211
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228909 177 YEDFLATGDPNYPWQPPADEWQSIAlgYTSGTTASPKGVVlHHRGAYIMALSNPL--IWGMQDGAVYLWTLPMfhcnGWC 254
Cdd:cd05967 212 WSELLAKAEPVDCVPVAATDPLYIL--YTSGTTGKPKGVV-RDNGGHAVALNWSMrnIYGIKPGDVWWAASDV----GWV 284
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228909 255 FPWSLAV----LSG-TSIC-----LRQVTAKEVYSMIAKYKVTHFCAAPVVLNAIVNAPKEDTIL---PLPHTVHVMTAG 321
Cdd:cd05967 285 VGHSYIVygplLHGaTTVLyegkpVGTPDPGAFWRVIEKYQVNALFTAPTAIRAIRKEDPDGKYIkkyDLSSLRTLFLAG 364
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228909 322 A-APPPSVLFSMNQKGFRVAHTYGLSETYGPstVCAWKPEWDSLPPETQAKLNARQGvrYtgmeQLDVIDtQTGKPVPAD 400
Cdd:cd05967 365 ErLDPPTLEWAENTLGVPVIDHWWQTETGWP--ITANPVGLEPLPIKAGSPGKPVPG--Y----QVQVLD-EDGEPVGPN 435
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228909 401 gkTAGEIVFRGNM---VMKGYLKNPEANKETFAG---GWFHSGDIAVKHPDNYIEIKDRSKDVIISGGENISSVEVENVV 474
Cdd:cd05967 436 --ELGNIVIKLPLppgCLLTLWKNDERFKKLYLSkfpGYYDTGDAGYKDEDGYLFIMGRTDDVINVAGHRLSTGEMEESV 513
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228909 475 YHHPAVLEASVVARPDERWQESPCAFVTLKSDYEKhDQNKLAQDIMKFCREKLPAYWVPKSVVF-GPLPKTATGKIQKHI 553
Cdd:cd05967 514 LSHPAVAECAVVGVRDELKGQVPLGLVVLKEGVKI-TAEELEKELVALVREQIGPVAAFRLVIFvKRLPKTRSGKILRRT 592
|
..
gi 15228909 554 LR 555
Cdd:cd05967 593 LR 594
|
|
| MACS_euk |
cd05928 |
Eukaryotic Medium-chain acyl-CoA synthetase (MACS or ACSM); MACS catalyzes the two-step ... |
48-557 |
3.74e-36 |
|
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: 141.83 E-value: 3.74e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228909 48 YTWRQTYDRCRRLASALADR-SIGPGSTVAIIAPNIPAMYEAHFGVPMCGAVLNCVNIRLNAPTVAFLLSHSQSSVIMVD 126
Cdd:cd05928 42 WSFRELGSLSRKAANVLSGAcGLQRGDRVAVILPRVPEWWLVNVACIRTGLVFIPGTIQLTAKDILYRLQASKAKCIVTS 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228909 127 QEFFTlAEDSLRLMEEkagsSFKRPLLIviGDHTCaPESLN-RALSKGAIEYEDFLATGDpnypwQPPadewqsIALGYT 205
Cdd:cd05928 122 DELAP-EVDSVASECP----SLKTKLLV--SEKSR-DGWLNfKELLNEASTEHHCVETGS-----QEP------MAIYFT 182
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228909 206 SGTTASPK---------GVVLHHRGAYIMAL-SNPLIWGMQDGAvylWTLpmfhcNGWCF---PWslavLSGTSIC---L 269
Cdd:cd05928 183 SGTTGSPKmaehshsslGLGLKVNGRYWLDLtASDIMWNTSDTG---WIK-----SAWSSlfePW----IQGACVFvhhL 250
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228909 270 RQVTAKEVYSMIAKYKVTHFCAAPVVLNAIVNapKEDTILPLPHTVHVMTAGAAPPPSVLFS-MNQKGFRVAHTYGLSET 348
Cdd:cd05928 251 PRFDPLVILKTLSSYPITTFCGAPTVYRMLVQ--QDLSSYKFPSLQHCVTGGEPLNPEVLEKwKAQTGLDIYEGYGQTET 328
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228909 349 ygpSTVCAwkpewdslppeTQAKLNARQGVRYTGMEQLDV-IDTQTGKPVPADgkTAGEIVFRGNMV-----MKGYLKNP 422
Cdd:cd05928 329 ---GLICA-----------NFKGMKIKPGSMGKASPPYDVqIIDDNGNVLPPG--TEGDIGIRVKPIrpfglFSGYVDNP 392
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228909 423 EANKETFAGGWFHSGDIAVKHPDNYIEIKDRSKDVIISGGENISSVEVENVVYHHPAVLEASVVARPDERWQESPCAFVT 502
Cdd:cd05928 393 EKTAATIRGDFYLTGDRGIMDEDGYFWFMGRADDVINSSGYRIGPFEVESALIEHPAVVESAVVSSPDPIRGEVVKAFVV 472
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*.
gi 15228909 503 LKSDYEKHDQNKLAQDIMKFCREKLPAYWVPKSVVF-GPLPKTATGKIQKHILRTK 557
Cdd:cd05928 473 LAPQFLSHDPEQLTKELQQHVKSVTAPYKYPRKVEFvQELPKTVTGKIQRNELRDK 528
|
|
| DltA |
cd05945 |
D-alanine:D-alanyl carrier protein ligase (DltA) and similar proteins; This family includes ... |
35-549 |
1.16e-35 |
|
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: 138.92 E-value: 1.16e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228909 35 HPTRKSVIHGSREYTWRQTYDRCRRLASALADRSIGPGSTVAIIAPNIPAMYEAHFGVPMCGAVlncvnirlnaptvafl 114
Cdd:cd05945 4 NPDRPAVVEGGRTLTYRELKERADALAAALASLGLDAGDPVVVYGHKSPDAIAAFLAALKAGHA---------------- 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228909 115 lshsqssVIMVDqefftlaedslrlmeekAGSSFKRPLLIVIgdhTCAPESLnralskgaieyedfLATGDPNYpwqppa 194
Cdd:cd05945 68 -------YVPLD-----------------ASSPAERIREILD---AAKPALL--------------IADGDDNA------ 100
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228909 195 dewqsiALGYTSGTTASPKGVVLHHRGayIMALSNpliW-----GMQDGAVYLWTLPmFHCNGWCFPWSLAVLSG-TSIC 268
Cdd:cd05945 101 ------YIIFTSGSTGRPKGVQISHDN--LVSFTN---WmlsdfPLGPGDVFLNQAP-FSFDLSVMDLYPALASGaTLVP 168
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228909 269 L-RQVTA--KEVYSMIAKYKVTHFCAAPVVLNAivnAPKEDTILP--LPHTVHVMTAGAAPPPSVLFSMNQK--GFRVAH 341
Cdd:cd05945 169 VpRDATAdpKQLFRFLAEHGITVWVSTPSFAAM---CLLSPTFTPesLPSLRHFLFCGEVLPHKTARALQQRfpDARIYN 245
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228909 342 TYGLSETYGPSTVCAWKPE----WDSLPpetqaklnarQGVRYTGMEqLDVIDTQtGKPVPADGKtaGEIVFRGNMVMKG 417
Cdd:cd05945 246 TYGPTEATVAVTYIEVTPEvldgYDRLP----------IGYAKPGAK-LVILDED-GRPVPPGEK--GELVISGPSVSKG 311
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228909 418 YLKNPEANKETF----AGGWFHSGDIAVKHPDNYIEIKDRSKDVIISGGENISSVEVENVVYHHPAVLEASVVARPDERW 493
Cdd:cd05945 312 YLNNPEKTAAAFfpdeGQRAYRTGDLVRLEADGLLFYRGRLDFQVKLNGYRIELEEIEAALRQVPGVKEAVVVPKYKGEK 391
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*..
gi 15228909 494 QESPCAFVTLKsdyeKHDQNKLAQDIMKFCREKLPAYWVPKSVVFGP-LPKTATGKI 549
Cdd:cd05945 392 VTELIAFVVPK----PGAEAGLTKAIKAELAERLPPYMIPRRFVYLDeLPLNANGKI 444
|
|
| PLN02330 |
PLN02330 |
4-coumarate--CoA ligase-like 1 |
46-557 |
2.12e-35 |
|
4-coumarate--CoA ligase-like 1
Pssm-ID: 215189 [Multi-domain] Cd Length: 546 Bit Score: 139.73 E-value: 2.12e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228909 46 REYTWRQTYDRCRRLASALadRSIG--PGSTVAIIAPNIPAMYEAHFGVPMCGAVLNCVNirlnaPTVafLLSHSQSSVI 123
Cdd:PLN02330 54 KAVTYGEVVRDTRRFAKAL--RSLGlrKGQVVVVVLPNVAEYGIVALGIMAAGGVFSGAN-----PTA--LESEIKKQAE 124
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228909 124 MVDQEFftLAEDSLRLMEEKagsSFKRPLlIVIGDHTCApeslnralskGAIEYEDFLATGDPNYPWQPPADEWQS--IA 201
Cdd:PLN02330 125 AAGAKL--IVTNDTNYGKVK---GLGLPV-IVLGEEKIE----------GAVNWKELLEAADRAGDTSDNEEILQTdlCA 188
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228909 202 LGYTSGTTASPKGVVLHHRGAYIMALSNPLIWG--MQDGAVYLWTLPMFHCNGWcfpwslavlsgTSICLRQVTAKEVYS 279
Cdd:PLN02330 189 LPFSSGTTGISKGVMLTHRNLVANLCSSLFSVGpeMIGQVVTLGLIPFFHIYGI-----------TGICCATLRNKGKVV 257
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228909 280 MIAKYKVTHFCAA-------------PVVLNAIVNAPKEDTILPLPHTVHVMTAGAAPPPSVLFSMNQK--GFRVAHTYG 344
Cdd:PLN02330 258 VMSRFELRTFLNAlitqevsfapivpPIILNLVKNPIVEEFDLSKLKLQAIMTAAAPLAPELLTAFEAKfpGVQVQEAYG 337
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228909 345 LSETygpstVCAWKPEWDslpPETQAKLNARQGVRYTgMEQLDV--IDTQTGKPVPADgkTAGEIVFRGNMVMKGYLKNP 422
Cdd:PLN02330 338 LTEH-----SCITLTHGD---PEKGHGIAKKNSVGFI-LPNLEVkfIDPDTGRSLPKN--TPGELCVRSQCVMQGYYNNK 406
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228909 423 EANKETF-AGGWFHSGDIAVKHPDNYIEIKDRSKDVIISGGENISSVEVENVVYHHPAVLEASVVARPDERWQESPCAFV 501
Cdd:PLN02330 407 EETDRTIdEDGWLHTGDIGYIDDDGDIFIVDRIKELIKYKGFQVAPAELEAILLTHPSVEDAAVVPLPDEEAGEIPAACV 486
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*..
gi 15228909 502 TLKSDYEKHDqnklaQDIMKFCREKLPAYWVPKSVVF-GPLPKTATGKIQKHILRTK 557
Cdd:PLN02330 487 VINPKAKESE-----EDILNFVAANVAHYKKVRVVQFvDSIPKSLSGKIMRRLLKEK 538
|
|
| PRK05677 |
PRK05677 |
long-chain-fatty-acid--CoA ligase; Validated |
166-555 |
1.65e-34 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 168170 [Multi-domain] Cd Length: 562 Bit Score: 137.59 E-value: 1.65e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228909 166 LNRALSKGAieyedflatGDPNYPWQPPADEwqsIA-LGYTSGTTASPKGVVLHHRGAYI-MALSNPLIWG-MQDGAVYL 242
Cdd:PRK05677 187 FNDALAKGA---------GQPVTEANPQADD---VAvLQYTGGTTGVAKGAMLTHRNLVAnMLQCRALMGSnLNEGCEIL 254
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228909 243 WT-LPMFHCNGWCFPWSLAVLSGTSICLRQvTAKEVYSMI---AKYKVTHFCAAPVVLNAIVNapkEDTILPLPHTVHVM 318
Cdd:PRK05677 255 IApLPLYHIYAFTFHCMAMMLIGNHNILIS-NPRDLPAMVkelGKWKFSGFVGLNTLFVALCN---NEAFRKLDFSALKL 330
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228909 319 TA--GAAPPPSVLFSMNQ-KGFRVAHTYGLSETygpSTVcawkpewdslppetqAKLNARQGVrytgmeQLDVIdtqtGK 395
Cdd:PRK05677 331 TLsgGMALQLATAERWKEvTGCAICEGYGMTET---SPV---------------VSVNPSQAI------QVGTI----GI 382
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228909 396 PVPA--------DGK-----TAGEIVFRGNMVMKGYLKNPEANKETF-AGGWFHSGDIAVKHPDNYIEIKDRSKDVIISG 461
Cdd:PRK05677 383 PVPStlckviddDGNelplgEVGELCVKGPQVMKGYWQRPEATDEILdSDGWLKTGDIALIQEDGYMRIVDRKKDMILVS 462
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228909 462 GENISSVEVENVVYHHPAVLEASVVARPDERWQESPCAFVTLKSdyekhDQNKLAQDIMKFCREKLPAYWVPKSVVF-GP 540
Cdd:PRK05677 463 GFNVYPNELEDVLAALPGVLQCAAIGVPDEKSGEAIKVFVVVKP-----GETLTKEQVMEHMRANLTGYKVPKAVEFrDE 537
|
410
....*....|....*
gi 15228909 541 LPKTATGKIQKHILR 555
Cdd:PRK05677 538 LPTTNVGKILRRELR 552
|
|
| Firefly_Luc |
cd17642 |
insect luciferase, similar to plant 4-coumarate: CoA ligases; This family contains insect ... |
43-555 |
2.39e-34 |
|
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: 136.50 E-value: 2.39e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228909 43 HGSREYTWRQTYDRCRRLASALADRSIGPGSTVAIIAPNipamyEAHFGVPMC-----GAVLNCVNIRLNAPTVAFLLSH 117
Cdd:cd17642 40 HTGVNYSYAEYLEMSVRLAEALKKYGLKQNDRIAVCSEN-----SLQFFLPVIaglfiGVGVAPTNDIYNERELDHSLNI 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228909 118 SQSSVIMVdqefftlaedSLRLMEEKAGSSFKRPLL--IVIGDhtcapeslNRALSKGAIEYEDFLATGDP----NYPWQ 191
Cdd:cd17642 115 SKPTIVFC----------SKKGLQKVLNVQKKLKIIktIIILD--------SKEDYKGYQCLYTFITQNLPpgfnEYDFK 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228909 192 PPA-DEWQSIAL-GYTSGTTASPKGVVLHHRGAyIMALSNPL--IWGMQ--DGAVYLWTLPMFHCNGwCFpwslaVLSGT 265
Cdd:cd17642 177 PPSfDRDEQVALiMNSSGSTGLPKGVQLTHKNI-VARFSHARdpIFGNQiiPDTAILTVIPFHHGFG-MF-----TTLGY 249
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228909 266 SIC------LRQVTAKEVYSMIAKYKVTHFCAAPVVLNAIVNAPKEDTiLPLPHtVHVMTAGAAPPPSVLFSMNQKGFR- 338
Cdd:cd17642 250 LICgfrvvlMYKFEEELFLRSLQDYKVQSALLVPTLFAFFAKSTLVDK-YDLSN-LHEIASGGAPLSKEVGEAVAKRFKl 327
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228909 339 --VAHTYGLSETYGPSTVcawKPEWDSLPPETqaklnarqGVRYTGMEqLDVIDTQTGKPVPADGKtaGEIVFRGNMVMK 416
Cdd:cd17642 328 pgIRQGYGLTETTSAILI---TPEGDDKPGAV--------GKVVPFFY-AKVVDLDTGKTLGPNER--GELCVKGPMIMK 393
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228909 417 GYLKNPEANKETF-AGGWFHSGDIAVKHPDNYIEIKDRSKDVIISGGENISSVEVENVVYHHPAVLEASVVARPDERWQE 495
Cdd:cd17642 394 GYVNNPEATKALIdKDGWLHSGDIAYYDEDGHFFIVDRLKSLIKYKGYQVPPAELESILLQHPKIFDAGVAGIPDEDAGE 473
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 15228909 496 SPCAFVTLksdyeKHDQNKLAQDIMKFCREKL-PAYWVPKSVVF-GPLPKTATGKIQKHILR 555
Cdd:cd17642 474 LPAAVVVL-----EAGKTMTEKEVMDYVASQVsTAKRLRGGVKFvDEVPKGLTGKIDRRKIR 530
|
|
| BACL_like |
cd05929 |
Bacterial Bile acid CoA ligases and similar proteins; Bile acid-Coenzyme A ligase catalyzes ... |
189-555 |
2.76e-34 |
|
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: 135.58 E-value: 2.76e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228909 189 PWQPPADEWQSIALGYTSGTTASPKGVVLHHRGAYIMAL---SNPLIWGMQDGAVYLWTLPMFHCNGWCFPWSLAVLSGT 265
Cdd:cd05929 117 PETPIEDEAAGWKMLYSGGTTGRPKGIKRGLPGGPPDNDtlmAAALGFGPGADSVYLSPAPLYHAAPFRWSMTALFMGGT 196
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228909 266 SICLRQVTAKEVYSMIAKYKVTHFCAAPVVLNaivnapkedTILPLPHTVH----------VMTAGAAPPPSVLFSM-NQ 334
Cdd:cd05929 197 LVLMEKFDPEEFLRLIERYRVTFAQFVPTMFV---------RLLKLPEAVRnaydlsslkrVIHAAAPCPPWVKEQWiDW 267
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228909 335 KGFRVAHTYGLSETYGpSTVCAwKPEWdslppetqakLNARQGVRYTGMEQLDVIDtQTGKPVPAdgKTAGEIVFRGN-- 412
Cdd:cd05929 268 GGPIIWEYYGGTEGQG-LTIIN-GEEW----------LTHPGSVGRAVLGKVHILD-EDGNEVPP--GEIGEVYFANGpg 332
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228909 413 -MVMKGYLKNPEANKEtfaGGWFHSGDIAVKHPDNYIEIKDRSKDVIISGGENISSVEVENVVYHHPAVLEASVVARPDE 491
Cdd:cd05929 333 fEYTNDPEKTAAARNE---GGWSTLGDVGYLDEDGYLYLTDRRSDMIISGGVNIYPQEIENALIAHPKVLDAAVVGVPDE 409
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 15228909 492 RWQESPCAFVtlKSDYEKHDQNKLAQDIMKFCREKLPAYWVPKSVVFGP-LPKTATGKIQKHILR 555
Cdd:cd05929 410 ELGQRVHAVV--QPAPGADAGTALAEELIAFLRDRLSRYKCPRSIEFVAeLPRDDTGKLYRRLLR 472
|
|
| MACS_like_2 |
cd05973 |
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the ... |
48-555 |
3.88e-34 |
|
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: 134.57 E-value: 3.88e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228909 48 YTWRQTYDRCRRLASALADRSIGPGSTVAIIAPNIPAMYEAHFGVPMCGAVLNCVNIRLNAPTVAFLLSHSQSSVIMVD- 126
Cdd:cd05973 1 LTFGELRALSARFANALQELGVGPGDVVAGLLPRTPELVVTILGIWRLGAVYQPLFTAFGPKAIEHRLRTSGARLVVTDa 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228909 127 QEFFTLAEDSLRLMeekagssfkrpllivigdhtcapeslnralskgaieyedflatgdpnypwqppadewqsialgYTS 206
Cdd:cd05973 81 ANRHKLDSDPFVMM---------------------------------------------------------------FTS 97
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228909 207 GTTASPKGVVLHHRgaYIMALSNPLIW--GMQDGAVYlWTL--PmfhcnGWCFPWSLAVLS----GTSICLRQ--VTAKE 276
Cdd:cd05973 98 GTTGLPKGVPVPLR--ALAAFGAYLRDavDLRPEDSF-WNAadP-----GWAYGLYYAITGplalGHPTILLEggFSVES 169
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228909 277 VYSMIAKYKVTHFCAAPVVLNAIVNAPKEDTILPLPHTVHVMTAGAAPPPSVL-FSMNQKGFRVAHTYGLSEtYGPSTVC 355
Cdd:cd05973 170 TWRVIERLGVTNLAGSPTAYRLLMAAGAEVPARPKGRLRRVSSAGEPLTPEVIrWFDAALGVPIHDHYGQTE-LGMVLAN 248
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228909 356 AWKPEWdslPPETQAKLNARQGVRYTgmeqldVIDTQTGKPVPAD-GKTAGEIVFRGNMVMKGYLKNPEAnkeTFAGGWF 434
Cdd:cd05973 249 HHALEH---PVHAGSAGRAMPGWRVA------VLDDDGDELGPGEpGRLAIDIANSPLMWFRGYQLPDTP---AIDGGYY 316
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228909 435 HSGDIAVKHPDNYIEIKDRSKDVIISGGENISSVEVENVVYHHPAVLEASVVARPDERWQESPCAFVTLKSDYEKHDQnk 514
Cdd:cd05973 317 LTGDTVEFDPDGSFSFIGRADDVITMSGYRIGPFDVESALIEHPAVAEAAVIGVPDPERTEVVKAFVVLRGGHEGTPA-- 394
|
490 500 510 520
....*....|....*....|....*....|....*....|..
gi 15228909 515 LAQDIMKFCREKLPAYWVPKSVVF-GPLPKTATGKIQKHILR 555
Cdd:cd05973 395 LADELQLHVKKRLSAHAYPRTIHFvDELPKTPSGKIQRFLLR 436
|
|
| ACS-like |
cd17634 |
acetate-CoA ligase; This family includes acyl- and aryl-CoA ligases, as well as the ... |
29-549 |
2.11e-33 |
|
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: 134.63 E-value: 2.11e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228909 29 DRAAVVHPTRKSVihGSREYTWRQTYDRCRRLASALADRSIGPGSTVAIIAPNIPAMYEAHFGVPMCGAVLNCVNIRLNA 108
Cdd:cd17634 68 DRTAIIYEGDDTS--QSRTISYRELHREVCRFAGTLLDLGVKKGDRVAIYMPMIPEAAVAMLACARIGAVHSVIFGGFAP 145
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228909 109 PTVAFLLSHSQSSVIMVDQEFFTLAE--DSLRLMEEKAGSSFKRPLLIVIGDHTCAPESLNRALSkgaIEYEDFLATGDP 186
Cdd:cd17634 146 EAVAGRIIDSSSRLLITADGGVRAGRsvPLKKNVDDALNPNVTSVEHVIVLKRTGSDIDWQEGRD---LWWRDLIAKASP 222
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228909 187 NYPWQPPADEwQSIALGYTSGTTASPKGVVlHHRGAYIMALSNPL--IWGMQDGAVYLWTLPMfhcnGWCF--PWSL--- 259
Cdd:cd17634 223 EHQPEAMNAE-DPLFILYTSGTTGKPKGVL-HTTGGYLVYAATTMkyVFDYGPGDIYWCTADV----GWVTghSYLLygp 296
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228909 260 AVLSGTSICLRQV----TAKEVYSMIAKYKVTHFCAAPVVLNAIvnAPKEDTILPLPHTVHVMTAGAA-----PPPSVLF 330
Cdd:cd17634 297 LACGATTLLYEGVpnwpTPARMWQVVDKHGVNILYTAPTAIRAL--MAAGDDAIEGTDRSSLRILGSVgepinPEAYEWY 374
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228909 331 SMNQKGFR--VAHTYGLSETYGpsTVCAWKPewDSLPPETQAKLNARQGVRYTgmeqldVIDTQtGKPVPadGKTAGEIV 408
Cdd:cd17634 375 WKKIGKEKcpVVDTWWQTETGG--FMITPLP--GAIELKAGSATRPVFGVQPA------VVDNE-GHPQP--GGTEGNLV 441
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228909 409 FRGNM--VMKGYLKNPEANKET----FAGGWFHsGDIAVKHPDNYIEIKDRSKDVIISGGENISSVEVENVVYHHPAVLE 482
Cdd:cd17634 442 ITDPWpgQTRTLFGDHERFEQTyfstFKGMYFS-GDGARRDEDGYYWITGRSDDVINVAGHRLGTAEIESVLVAHPKVAE 520
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 15228909 483 ASVVARPDERWQESPCAFVTLKSDYEkhDQNKLAQDIMKFCREKLPAYWVPKSVVF-GPLPKTATGKI 549
Cdd:cd17634 521 AAVVGIPHAIKGQAPYAYVVLNHGVE--PSPELYAELRNWVRKEIGPLATPDVVHWvDSLPKTRSGKI 586
|
|
| A_NRPS_Srf_like |
cd12117 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including Bacillus subtilis ... |
26-551 |
6.55e-33 |
|
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: 131.55 E-value: 6.55e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228909 26 WFLDRAAVvHPTRKSVIHGSREYTWRQTYDRCRRLASALADRSIGPGSTVAIIAPNIPAMYEAHFGVPMCGAVLNCVNIR 105
Cdd:cd12117 2 LFEEQAAR-TPDAVAVVYGDRSLTYAELNERANRLARRLRAAGVGPGDVVGVLAERSPELVVALLAVLKAGAAYVPLDPE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228909 106 LNAPTVAFLLSHSQSSVIMVDQEFFTLAEDSLRlmeekagssfkrPLLIVIGDHTCAPESLNRALSKGAIEYedflatgd 185
Cdd:cd12117 81 LPAERLAFMLADAGAKVLLTDRSLAGRAGGLEV------------AVVIDEALDAGPAGNPAVPVSPDDLAY-------- 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228909 186 pnypwqppadewqsiaLGYTSGTTASPKGVVLHHRG--------AYI-------MALSNPLIWgmqDGAVY-LWTlpmfh 249
Cdd:cd12117 141 ----------------VMYTSGSTGRPKGVAVTHRGvvrlvkntNYVtlgpddrVLQTSPLAF---DASTFeIWG----- 196
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228909 250 cngwcfpwslAVLSGTSICL----RQVTAKEVYSMIAKYKVT-HFCAAPVvLNAIVnapkeDTILPLPHTV-HVMTAG-A 322
Cdd:cd12117 197 ----------ALLNGARLVLapkgTLLDPDALGALIAEEGVTvLWLTAAL-FNQLA-----DEDPECFAGLrELLTGGeV 260
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228909 323 APPPSVLFSMNQK-GFRVAHTYGLSETYGPSTVCAWKPEW---DSLP-----PETQAKLnarqgvrytgmeqLDvidtQT 393
Cdd:cd12117 261 VSPPHVRRVLAACpGLRLVNGYGPTENTTFTTSHVVTELDevaGSIPigrpiANTRVYV-------------LD----ED 323
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228909 394 GKPVPADgkTAGEIVFRGNMVMKGYLKNPEANKETFA------GG-WFHSGDIAVKHPDNYIEIKDRSKDVIISGGENIS 466
Cdd:cd12117 324 GRPVPPG--VPGELYVGGDGLALGYLNRPALTAERFVadpfgpGErLYRTGDLARWLPDGRLEFLGRIDDQVKIRGFRIE 401
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228909 467 SVEVENVVYHHPAVLEASVVARPDERWQESPCAFVTLksdyekhDQNKLAQDIMKFCREKLPAYWVPKSVVF-GPLPKTA 545
Cdd:cd12117 402 LGEIEAALRAHPGVREAVVVVREDAGGDKRLVAYVVA-------EGALDAAELRAFLRERLPAYMVPAAFVVlDELPLTA 474
|
....*.
gi 15228909 546 TGKIQK 551
Cdd:cd12117 475 NGKVDR 480
|
|
| PRK08751 |
PRK08751 |
long-chain fatty acid--CoA ligase; |
49-559 |
7.03e-33 |
|
long-chain fatty acid--CoA ligase;
Pssm-ID: 181546 [Multi-domain] Cd Length: 560 Bit Score: 132.69 E-value: 7.03e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228909 49 TWRQTYDRCRRLAS-ALADRSIGPGSTVAIIAPNIPAMYEAHFGVPMCGAVLNCVNIRLNAPTVAFLLSHSQSSVIMVDQ 127
Cdd:PRK08751 52 TYREADQLVEQFAAyLLGELQLKKGDRVALMMPNCLQYPIATFGVLRAGLTVVNVNPLYTPRELKHQLIDSGASVLVVID 131
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228909 128 EFFTLAEDSLrlmeekAGSSFKRPLLIVIGDHTCAPES--LNRALS-----------KGAIEYEDFLATGDPNYpwQPPA 194
Cdd:PRK08751 132 NFGTTVQQVI------ADTPVKQVITTGLGDMLGFPKAalVNFVVKyvkklvpeyriNGAIRFREALALGRKHS--MPTL 203
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228909 195 D-EWQSIA-LGYTSGTTASPKGVVLHHR--------GAYIMALSNPLIWGMQdgaVYLWTLPMFH-----CNGWCFpwsL 259
Cdd:PRK08751 204 QiEPDDIAfLQYTGGTTGVAKGAMLTHRnlvanmqqAHQWLAGTGKLEEGCE---VVITALPLYHifaltANGLVF---M 277
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228909 260 AVLSGTSICLRQVTAKEVYSMIAKYKVTHFCAAPVVLNAIVNAPKEDTIlPLPHTVHVMTAGAAPPPSVLFSMNQ-KGFR 338
Cdd:PRK08751 278 KIGGCNHLISNPRDMPGFVKELKKTRFTAFTGVNTLFNGLLNTPGFDQI-DFSSLKMTLGGGMAVQRSVAERWKQvTGLT 356
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228909 339 VAHTYGLSETyGPSTvCawkpewdsLPPETQAKLNARQGVRytgMEQLDV-IDTQTGKPVPADgkTAGEIVFRGNMVMKG 417
Cdd:PRK08751 357 LVEAYGLTET-SPAA-C--------INPLTLKEYNGSIGLP---IPSTDAcIKDDAGTVLAIG--EIGELCIKGPQVMKG 421
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228909 418 YLKNPEANKETF-AGGWFHSGDIAVKHPDNYIEIKDRSKDVIISGGENISSVEVENVVYHHPAVLEASVVARPDERWQEs 496
Cdd:PRK08751 422 YWKRPEETAKVMdADGWLHTGDIARMDEQGFVYIVDRKKDMILVSGFNVYPNEIEDVIAMMPGVLEVAAVGVPDEKSGE- 500
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 15228909 497 pcafvTLKSDYEKHDQNKLAQDIMKFCREKLPAYWVPKSVVF-GPLPKTATGKIQKHILRTKAK 559
Cdd:PRK08751 501 -----IVKVVIVKKDPALTAEDVKAHARANLTGYKQPRIIEFrKELPKTNVGKILRRELRDAAK 559
|
|
| entE |
PRK10946 |
(2,3-dihydroxybenzoyl)adenylate synthase; |
36-560 |
2.24e-32 |
|
(2,3-dihydroxybenzoyl)adenylate synthase;
Pssm-ID: 236803 [Multi-domain] Cd Length: 536 Bit Score: 130.88 E-value: 2.24e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228909 36 PTRKSVIHGSREYTWRQTYDRCRRLASALADRSIGPGSTVAIIAPNIPAMYEAHFGVPMCGAVlncvniRLNAptvafLL 115
Cdd:PRK10946 37 SDAIAVICGERQFSYRELNQASDNLACSLRRQGIKPGDTALVQLGNVAEFYITFFALLKLGVA------PVNA-----LF 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228909 116 SHSQS-----------SVIMVDQEFFTLAEDSlRLMEEKAGSSfkRPLLIVIGDHTcapeslnralskGAIEYEDFLATG 184
Cdd:PRK10946 106 SHQRSelnayasqiepALLIADRQHALFSDDD-FLNTLVAEHS--SLRVVLLLNDD------------GEHSLDDAINHP 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228909 185 DPNYPWQP-PADEWQSIALgyTSGTTASPKGVVLHHRGAY--IMAlSNPlIWGMQDGAVYLWTLPMFHCNGWCFPWSLAV 261
Cdd:PRK10946 171 AEDFTATPsPADEVAFFQL--SGGSTGTPKLIPRTHNDYYysVRR-SVE-ICGFTPQTRYLCALPAAHNYPMSSPGALGV 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228909 262 L--SGTSICLRQVTAKEVYSMIAKYKVThfcAAPVVLNAI------VNAPKEDTILplpHTVHVMTAGAAPppsvlfsmn 333
Cdd:PRK10946 247 FlaGGTVVLAPDPSATLCFPLIEKHQVN---VTALVPPAVslwlqaIAEGGSRAQL---ASLKLLQVGGAR--------- 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228909 334 qkgfrvahtygLSETYGpstvcawkpewDSLPPETQAKLN-----ARQGVRYTGMEQLD--VIDTQ-------------- 392
Cdd:PRK10946 312 -----------LSETLA-----------RRIPAELGCQLQqvfgmAEGLVNYTRLDDSDerIFTTQgrpmspddevwvad 369
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228909 393 -TGKPVPaDGkTAGEIVFRGNMVMKGYLKNPEANKETF-AGGWFHSGDIAVKHPDNYIEIKDRSKDVIISGGENISSVEV 470
Cdd:PRK10946 370 aDGNPLP-QG-EVGRLMTRGPYTFRGYYKSPQHNASAFdANGFYCSGDLVSIDPDGYITVVGREKDQINRGGEKIAAEEI 447
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228909 471 ENVVYHHPAVLEASVVARPDERWQESPCAFVTLKSDYEkhdqnklAQDIMKFCREKLPA-YWVPKSVVFGP-LPKTATGK 548
Cdd:PRK10946 448 ENLLLRHPAVIHAALVSMEDELMGEKSCAFLVVKEPLK-------AVQLRRFLREQGIAeFKLPDRVECVDsLPLTAVGK 520
|
570
....*....|..
gi 15228909 549 IQKHILRTKAKE 560
Cdd:PRK10946 521 VDKKQLRQWLAS 532
|
|
| MACS_like_1 |
cd05974 |
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the ... |
202-558 |
2.55e-32 |
|
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: 129.22 E-value: 2.55e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228909 202 LGYTSGTTASPKgVVLHHRGAYIMALSNPLIW-GMQDGAVYL-WTLPMFHCNGW-CF--PWSlavlSGTSICLRQVT--- 273
Cdd:cd05974 90 LYFTSGTTSKPK-LVEHTHRSYPVGHLSTMYWiGLKPGDVHWnISSPGWAKHAWsCFfaPWN----AGATVFLFNYArfd 164
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228909 274 AKEVYSMIAKYKVTHFCAAPVVLNAIVNAPKEDTILPLPHTVhvmtaGAAPP--PSVLFSMNQK-GFRVAHTYGLSETyg 350
Cdd:cd05974 165 AKRVLAALVRYGVTTLCAPPTVWRMLIQQDLASFDVKLREVV-----GAGEPlnPEVIEQVRRAwGLTIRDGYGQTET-- 237
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228909 351 pstvcawkpewdslppETQAKLNARQGVRYTGMeqldvidtqtGKPVP--------ADGKTA--GEIVF-----RGNMVM 415
Cdd:cd05974 238 ----------------TALVGNSPGQPVKAGSM----------GRPLPgyrvalldPDGAPAteGEVALdlgdtRPVGLM 291
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228909 416 KGYLKNPEANKETFAGGWFHSGDIAVKHPDNYIEIKDRSKDVIISGGENISSVEVENVVYHHPAVLEASVVARPDERWQE 495
Cdd:cd05974 292 KGYAGDPDKTAHAMRGGYYRTGDIAMRDEDGYLTYVGRADDVFKSSDYRISPFELESVLIEHPAVAEAAVVPSPDPVRLS 371
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 15228909 496 SPCAFVTLKSDYEKhdQNKLAQDIMKFCREKLPAYWVPKSVVFGPLPKTATGKIQKHILRTKA 558
Cdd:cd05974 372 VPKAFIVLRAGYEP--SPETALEIFRFSRERLAPYKRIRRLEFAELPKTISGKIRRVELRRRE 432
|
|
| PRK07867 |
PRK07867 |
acyl-CoA synthetase; Validated |
22-558 |
5.15e-32 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236120 [Multi-domain] Cd Length: 529 Bit Score: 129.80 E-value: 5.15e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228909 22 LTPLWFLDRAAVVHptrksvihGSREYTWRQTYDRCRRLASALADRsIGPGST--VAIIAPNIPAMYEAHFGVPMCGAVL 99
Cdd:PRK07867 11 LLPLAEDDDRGLYF--------EDSFTSWREHIRGSAARAAALRAR-LDPTRPphVGVLLDNTPEFSLLLGAAALSGIVP 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228909 100 NCVNIRLNAPTVAFLLSHSQSSVIMVDQEFFTLAEDSlrlmeekagssfkrpllivigdhtcapESLNRALSKGAIEYED 179
Cdd:PRK07867 82 VGLNPTRRGAALARDIAHADCQLVLTESAHAELLDGL---------------------------DPGVRVINVDSPAWAD 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228909 180 FLAT--GDPNYPWQPPADEwqSIALGYTSGTTASPKGVVLHHRGAYIMALSNPLIWGMQDGAVYLWTLPMFHCNGWCFPW 257
Cdd:PRK07867 135 ELAAhrDAEPPFRVADPDD--LFMLIFTSGTSGDPKAVRCTHRKVASAGVMLAQRFGLGPDDVCYVSMPLFHSNAVMAGW 212
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228909 258 SLAVLSGTSICLRQ-VTAKEVYSMIAKYKVTHFCAAPVVLNAIVNAPkedtilPLP----HTVHVMTAGAAPPPSVLFSM 332
Cdd:PRK07867 213 AVALAAGASIALRRkFSASGFLPDVRRYGATYANYVGKPLSYVLATP------ERPddadNPLRIVYGNEGAPGDIARFA 286
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228909 333 NQKGFRVAHTYGLSETyGPSTvcAWKPewdSLPPETQAKLnarqgvrytgMEQLDVIDTQTGKPVP-----ADGKTA--- 404
Cdd:PRK07867 287 RRFGCVVVDGFGSTEG-GVAI--TRTP---DTPPGALGPL----------PPGVAIVDPDTGTECPpaedaDGRLLNade 350
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228909 405 --GEIV-FRGNMVMKGYLKNPEANKETFAGGWFHSGDIAVKHPDNYIEIKDRSKDVIISGGENISSVEVENVVYHHPAVL 481
Cdd:PRK07867 351 aiGELVnTAGPGGFEGYYNDPEADAERMRGGVYWSGDLAYRDADGYAYFAGRLGDWMRVDGENLGTAPIERILLRYPDAT 430
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228909 482 EASVVARPDERWQESPCAFVTLKSDYEkHDQNKLAQdimkFCREK--LPAYWVPKSV-VFGPLPKTATGKIQKHILRTKA 558
Cdd:PRK07867 431 EVAVYAVPDPVVGDQVMAALVLAPGAK-FDPDAFAE----FLAAQpdLGPKQWPSYVrVCAELPRTATFKVLKRQLSAEG 505
|
|
| A_NRPS_AB3403-like |
cd17646 |
Peptide Synthetase; The adenylation (A) domain of NRPS recognizes a specific amino acid or ... |
28-549 |
6.29e-32 |
|
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: 128.93 E-value: 6.29e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228909 28 LDRAAVVHPTRKSVIHGSREYTWRQTYDRCRRLASALADRSIGPGSTVAIIAPNIPAMYEAHFGVPMCGAVLNCVNIRLN 107
Cdd:cd17646 4 VAEQAARTPDAPAVVDEGRTLTYRELDERANRLAHLLRARGVGPEDRVAVLLPRSADLVVALLAVLKAGAAYLPLDPGYP 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228909 108 APTVAFLLSHSQSSVimvdqeFFTLAEDSLRLMEEkagssfkrplliviGDHTCAPESLnralskgaieyedfLATGDPN 187
Cdd:cd17646 84 ADRLAYMLADAGPAV------VLTTADLAARLPAG--------------GDVALLGDEA--------------LAAPPAT 129
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228909 188 YPWQPPADEwQSIALGYTSGTTASPKGVVLHHRGayimaLSNPLIWgMQDG-------AVYLWTLPMFHCNGWCFPWSLA 260
Cdd:cd17646 130 PPLVPPRPD-NLAYVIYTSGSTGRPKGVMVTHAG-----IVNRLLW-MQDEyplgpgdRVLQKTPLSFDVSVWELFWPLV 202
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228909 261 VlSGTSICLRQVTAKEV---YSMIAKYKVT--HFcaAPVVLNAIVNAPKEDTILPLPHtvhVMTAGAAPPPSV--LFsMN 333
Cdd:cd17646 203 A-GARLVVARPGGHRDPaylAALIREHGVTtcHF--VPSMLRVFLAEPAAGSCASLRR---VFCSGEALPPELaaRF-LA 275
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228909 334 QKGFRVAHTYGLSETYGPSTVCAWKPEWDSLP-PETQAKLNARqgvrytgmeqLDVIDtQTGKPVPADgkTAGEIVFRGN 412
Cdd:cd17646 276 LPGAELHNLYGPTEAAIDVTHWPVRGPAETPSvPIGRPVPNTR----------LYVLD-DALRPVPVG--VPGELYLGGV 342
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228909 413 MVMKGYLKNPEANKETFAGGWF-------HSGDIAVKHPDNYIEIKDRSKDVIISGGENISSVEVENVVYHHPAVLEASV 485
Cdd:cd17646 343 QLARGYLGRPALTAERFVPDPFgpgsrmyRTGDLARWRPDGALEFLGRSDDQVKIRGFRVEPGEIEAALAAHPAVTHAVV 422
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 15228909 486 VARPDERWQESPCAFVTLKSDYEKHDQNKLAQdimkFCREKLPAYWVPKSVVFGP-LPKTATGKI 549
Cdd:cd17646 423 VARAAPAGAARLVGYVVPAAGAAGPDTAALRA----HLAERLPEYMVPAAFVVLDaLPLTANGKL 483
|
|
| PRK05857 |
PRK05857 |
fatty acid--CoA ligase; |
44-558 |
8.71e-32 |
|
fatty acid--CoA ligase;
Pssm-ID: 180293 [Multi-domain] Cd Length: 540 Bit Score: 129.36 E-value: 8.71e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228909 44 GSREYTWRQTYDRCRRLASALADRSIGPGSTVAIIAPNIPAMYEAHFGVPMCGAVLNCVNIRLNAPTVAFLLSHSQSSVI 123
Cdd:PRK05857 38 GTSALRYRELVAEVGGLAADLRAQSVSRGSRVLVISDNGPETYLSVLACAKLGAIAVMADGNLPIAAIERFCQITDPAAA 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228909 124 MVDQEfftlaedslrlmeEKAGSSFKRPLLIVIGDHTCAPESlnralskgaiEYEDFLATGDPNYPWQPP---ADEwqSI 200
Cdd:PRK05857 118 LVAPG-------------SKMASSAVPEALHSIPVIAVDIAA----------VTRESEHSLDAASLAGNAdqgSED--PL 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228909 201 ALGYTSGTTASPKGVVLHHRGAYIMA--LSNP-LIW-GMQDGAVYLWTLPMFHCNG-WcfpWSLAVLSGTSIClrqVTAK 275
Cdd:PRK05857 173 AMIFTSGTTGEPKAVLLANRTFFAVPdiLQKEgLNWvTWVVGETTYSPLPATHIGGlW---WILTCLMHGGLC---VTGG 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228909 276 E----VYSMIAKYKVTHFCAAPVVLNAIVNAPK-EDTILPlPHTVHVMTAGAAPPPSVLFsMNQKGFRVAHTYGLSETyG 350
Cdd:PRK05857 247 EnttsLLEILTTNAVATTCLVPTLLSKLVSELKsANATVP-SLRLVGYGGSRAIAADVRF-IEATGVRTAQVYGLSET-G 323
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228909 351 PSTVCawkpewdsLPPETQAKLNARQGV---RYTGMEQLdVIDTQTGKPVPADGKTA---GEIVFRGNMVMKGYLKNPEA 424
Cdd:PRK05857 324 CTALC--------LPTDDGSIVKIEAGAvgrPYPGVDVY-LAATDGIGPTAPGAGPSasfGTLWIKSPANMLGYWNNPER 394
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228909 425 NKETFAGGWFHSGDIAVKHPDNYIEIKDRSKDVIISGGENISSVEVENVVYHHPAVLEASVVARPDERWQESPCAFVTLK 504
Cdd:PRK05857 395 TAEVLIDGWVNTGDLLERREDGFFYIKGRSSEMIICGGVNIAPDEVDRIAEGVSGVREAACYEIPDEEFGALVGLAVVAS 474
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*
gi 15228909 505 SDYEKHDQNKLAQDIMKFCREKLPAYWVPKSVVF-GPLPKTATGKIQKHILRTKA 558
Cdd:PRK05857 475 AELDESAARALKHTIAARFRRESEPMARPSTIVIvTDIPRTQSGKVMRASLAAAA 529
|
|
| PRK08974 |
PRK08974 |
long-chain-fatty-acid--CoA ligase FadD; |
202-559 |
4.53e-31 |
|
long-chain-fatty-acid--CoA ligase FadD;
Pssm-ID: 236359 [Multi-domain] Cd Length: 560 Bit Score: 127.48 E-value: 4.53e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228909 202 LGYTSGTTASPKGVVLHHR----------GAYImalsnPLIwgmQDGAVYLWT-LPMFHCngwcfpWSLAV-------LS 263
Cdd:PRK08974 211 LQYTGGTTGVAKGAMLTHRnmlanleqakAAYG-----PLL---HPGKELVVTaLPLYHI------FALTVncllfieLG 276
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228909 264 GTSICL---RQVTA--KEvysmIAKYKVTHFCAAPVVLNAIVNAPkEDTILPLPhTVHVMTAGAAPPPSVLFSMNQK--G 336
Cdd:PRK08974 277 GQNLLItnpRDIPGfvKE----LKKYPFTAITGVNTLFNALLNNE-EFQELDFS-SLKLSVGGGMAVQQAVAERWVKltG 350
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228909 337 FRVAHTYGLSETYGPSTVCawkpewdslpPETQAKLNARQGVRYTGMEqLDVIDTQtGKPVPADgkTAGEIVFRGNMVMK 416
Cdd:PRK08974 351 QYLLEGYGLTECSPLVSVN----------PYDLDYYSGSIGLPVPSTE-IKLVDDD-GNEVPPG--EPGELWVKGPQVML 416
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228909 417 GYLKNPEANKETFAGGWFHSGDIAVKHPDNYIEIKDRSKDVIISGGENISSVEVENVVYHHPAVLEASVVARPDERWQES 496
Cdd:PRK08974 417 GYWQRPEATDEVIKDGWLATGDIAVMDEEGFLRIVDRKKDMILVSGFNVYPNEIEDVVMLHPKVLEVAAVGVPSEVSGEA 496
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 15228909 497 PCAFVTlksdyeKHDQNKLAQDIMKFCREKLPAYWVPKSVVF-GPLPKTATGKIQKHILRTKAK 559
Cdd:PRK08974 497 VKIFVV------KKDPSLTEEELITHCRRHLTGYKVPKLVEFrDELPKSNVGKILRRELRDEAR 554
|
|
| PRK08279 |
PRK08279 |
long-chain-acyl-CoA synthetase; Validated |
26-555 |
6.01e-31 |
|
long-chain-acyl-CoA synthetase; Validated
Pssm-ID: 236217 [Multi-domain] Cd Length: 600 Bit Score: 127.30 E-value: 6.01e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228909 26 WFLDRAAVVHPTRKSVIHGSREYTWRQTYDRCRRLASALADRSIGPGSTVAIIAPNIPAMYEAHFGVPMCGAVLNCVNIR 105
Cdd:PRK08279 41 DVFEEAAARHPDRPALLFEDQSISYAELNARANRYAHWAAARGVGKGDVVALLMENRPEYLAAWLGLAKLGAVVALLNTQ 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228909 106 LNAPTVAFLLSHSQSSVIMVDQEFFTLAEDSlrlmeeKAGSSFKRPLLIVIGDHTCAPEslnralskGAIEYEDFLATgd 185
Cdd:PRK08279 121 QRGAVLAHSLNLVDAKHLIVGEELVEAFEEA------RADLARPPRLWVAGGDTLDDPE--------GYEDLAAAAAG-- 184
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228909 186 pnYPWQPPADEwQSIALG------YTSGTTASPKGVVLHHRGAYIMALSNPLIWGM-QDGAVYLwTLPMFHCNGWCFPWS 258
Cdd:PRK08279 185 --APTTNPASR-SGVTAKdtafyiYTSGTTGLPKAAVMSHMRWLKAMGGFGGLLRLtPDDVLYC-CLPLYHNTGGTVAWS 260
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228909 259 LAVLSGTSICL-RQVTAKEVYSMIAKYKVTHFCAAPVVLNAIVNAPKEDTIlpLPHTVHVMTaGAAPPPSVLFSMNQKgF 337
Cdd:PRK08279 261 SVLAAGATLALrRKFSASRFWDDVRRYRATAFQYIGELCRYLLNQPPKPTD--RDHRLRLMI-GNGLRPDIWDEFQQR-F 336
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228909 338 ---RVAHTYGLSET-------YGPSTVCAWKPEWDSLPpetqAKLnarqgVRYtgmeqldviDTQTGKPV-PADG---KT 403
Cdd:PRK08279 337 gipRILEFYAASEGnvgfinvFNFDGTVGRVPLWLAHP----YAI-----VKY---------DVDTGEPVrDADGrciKV 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228909 404 A--------GEIVFRGNmvMKGYLkNPEANK-----ETFAGG--WFHSGDIAVKHPDNYIEIKDRSKDVIISGGENISSV 468
Cdd:PRK08279 399 KpgevglliGRITDRGP--FDGYT-DPEASEkkilrDVFKKGdaWFNTGDLMRDDGFGHAQFVDRLGDTFRWKGENVATT 475
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228909 469 EVENVVYHHPAVLEASV--VARPDerwQESPC--AFVTLKSDYEkHDQNKLAQdimkFCREKLPAYWVPksvVF----GP 540
Cdd:PRK08279 476 EVENALSGFPGVEEAVVygVEVPG---TDGRAgmAAIVLADGAE-FDLAALAA----HLYERLPAYAVP---LFvrlvPE 544
|
570
....*....|....*
gi 15228909 541 LPKTATGKIQKHILR 555
Cdd:PRK08279 545 LETTGTFKYRKVDLR 559
|
|
| PRK07514 |
PRK07514 |
malonyl-CoA synthase; Validated |
30-555 |
8.86e-31 |
|
malonyl-CoA synthase; Validated
Pssm-ID: 181011 [Multi-domain] Cd Length: 504 Bit Score: 125.76 E-value: 8.86e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228909 30 RAAVVHPTRKSV-IHGSREYTWRQTYDRCRRLASALADRSIGPGSTVAIIAPNIPAMYEAHFGVPMCGAVLNCVNIRLNA 108
Cdd:PRK07514 10 RAAFADRDAPFIeTPDGLRYTYGDLDAASARLANLLVALGVKPGDRVAVQVEKSPEALALYLATLRAGAVFLPLNTAYTL 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228909 109 PTVAFLLSHSQSSVIMVDQEfftlAEDSLRLMEEKAGSsfkrPLLIVIGDHtcAPESLNRALSKGAIEYEDfLATGdpny 188
Cdd:PRK07514 90 AELDYFIGDAEPALVVCDPA----NFAWLSKIAAAAGA----PHVETLDAD--GTGSLLEAAAAAPDDFET-VPRG---- 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228909 189 pwqppADEWQSIAlgYTSGTTASPKGVVLHHRGAyimaLSNPL----IWGMQDGAVYLWTLPMFHCNGWCFPWSLAVLSG 264
Cdd:PRK07514 155 -----ADDLAAIL--YTSGTTGRSKGAMLSHGNL----LSNALtlvdYWRFTPDDVLIHALPIFHTHGLFVATNVALLAG 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228909 265 TS-ICLRQVTAKEVYSMIAKykVTHFCAAPVVLNAIVNAPKEDtilplPHTVHVM---TAGAAPppsvLFSMNQKGF--R 338
Cdd:PRK07514 224 ASmIFLPKFDPDAVLALMPR--ATVMMGVPTFYTRLLQEPRLT-----REAAAHMrlfISGSAP----LLAETHREFqeR 292
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228909 339 VAHT----YGLSET-------YG----PSTVcaWKPewdsLPpetqaklnarqGVrytgmeQLDVIDTQTGKPVPADGkt 403
Cdd:PRK07514 293 TGHAilerYGMTETnmntsnpYDgerrAGTV--GFP----LP-----------GV------SLRVTDPETGAELPPGE-- 347
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228909 404 AGEIVFRGNMVMKGYLKNPEANKETF-AGGWFHSGDIAVKHPDNYIEIKDRSKDVIISGGENISSVEVENVVYHHPAVLE 482
Cdd:PRK07514 348 IGMIEVKGPNVFKGYWRMPEKTAEEFrADGFFITGDLGKIDERGYVHIVGRGKDLIISGGYNVYPKEVEGEIDELPGVVE 427
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 15228909 483 ASVVARPDERWQESPCAFVTLKSdyekhDQNKLAQDIMKFCREKLPAYWVPKSVVFGP-LPKTATGKIQKHILR 555
Cdd:PRK07514 428 SAVIGVPHPDFGEGVTAVVVPKP-----GAALDEAAILAALKGRLARFKQPKRVFFVDeLPRNTMGKVQKNLLR 496
|
|
| PRK12492 |
PRK12492 |
long-chain-fatty-acid--CoA ligase; Provisional |
336-558 |
1.51e-30 |
|
long-chain-fatty-acid--CoA ligase; Provisional
Pssm-ID: 171539 [Multi-domain] Cd Length: 562 Bit Score: 125.70 E-value: 1.51e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228909 336 GFRVAHTYGLSETygpstvcawKPEWDSLPPETQAKLNArQGVRYTGMeQLDVIDTQtGKPVPADGKtaGEIVFRGNMVM 415
Cdd:PRK12492 358 GCTIVEGYGLTET---------SPVASTNPYGELARLGT-VGIPVPGT-ALKVIDDD-GNELPLGER--GELCIKGPQVM 423
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228909 416 KGYLKNPEANKETF-AGGWFHSGDIAVKHPDNYIEIKDRSKDVIISGGENISSVEVENVVYHHPAVLEASVVARPDERWQ 494
Cdd:PRK12492 424 KGYWQQPEATAEALdAEGWFKTGDIAVIDPDGFVRIVDRKKDLIIVSGFNVYPNEIEDVVMAHPKVANCAAIGVPDERSG 503
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 15228909 495 ESPCAFVTLKsdyekhDQNKLAQDIMKFCREKLPAYWVPKSVVF-GPLPKTATGKIQKHILRTKA 558
Cdd:PRK12492 504 EAVKLFVVAR------DPGLSVEELKAYCKENFTGYKVPKHIVLrDSLPMTPVGKILRRELRDIA 562
|
|
| FAAL |
cd05931 |
Fatty acyl-AMP ligase (FAAL); FAAL belongs to the class I adenylate forming enzyme family and ... |
30-550 |
1.53e-30 |
|
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: 125.43 E-value: 1.53e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228909 30 RAAVVHPTRKSVIH------GSREYTWRQTYDRCRRLASALADRSiGPGSTVAIIAPNIPAMYEAHFGVPMCGAVLncV- 102
Cdd:cd05931 1 RRAAARPDRPAYTFlddeggREETLTYAELDRRARAIAARLQAVG-KPGDRVLLLAPPGLDFVAAFLGCLYAGAIA--Vp 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228909 103 ----NIRLNAPTVAFLLSHSQSSVIMVDQEFftlaEDSLRLMEEKAGSSFKRPLLIVigdhtcapeslnralskgaieye 178
Cdd:cd05931 78 lpppTPGRHAERLAAILADAGPRVVLTTAAA----LAAVRAFAASRPAAGTPRLLVV----------------------- 130
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228909 179 DFLATGDPNyPWQPPADEWQSIA-LGYTSGTTASPKGVVLHHRGAyimaLSNPLI----WGMQDGAVYL-WtLPMFH--- 249
Cdd:cd05931 131 DLLPDTSAA-DWPPPSPDPDDIAyLQYTSGSTGTPKGVVVTHRNL----LANVRQirraYGLDPGDVVVsW-LPLYHdmg 204
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228909 250 -CNGWCFPW----------SLAVLSGTSICLRqvtakevysMIAKYKVTHfCAAP-----VVLNAIVNAPKEDTILplpH 313
Cdd:cd05931 205 lIGGLLTPLysggpsvlmsPAAFLRRPLRWLR---------LISRYRATI-SAAPnfaydLCVRRVRDEDLEGLDL---S 271
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228909 314 TVHVMTAGAAP-PPSVLFSMNQK----GFRV-AHT--YGLSE-TYGPSTVCAWKP----EWDSLPPETQAKLNARQGVRY 380
Cdd:cd05931 272 SWRVALNGAEPvRPATLRRFAEAfapfGFRPeAFRpsYGLAEaTLFVSGGPPGTGpvvlRVDRDALAGRAVAVAADDPAA 351
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228909 381 T-----GMEQLD----VIDTQTGKPVPADgkTAGEIVFRGNMVMKGYLKNPEANKETF-------AGGWFHSGDIAVKHp 444
Cdd:cd05931 352 RelvscGRPLPDqevrIVDPETGRELPDG--EVGEIWVRGPSVASGYWGRPEATAETFgalaatdEGGWLRTGDLGFLH- 428
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228909 445 DNYIEIKDRSKDVIISGGENISSVEVENVVYH-HPAVLEASVVARPDERWQESPCAFVT-LKSDYEKHDQNKLAQDIM-K 521
Cdd:cd05931 429 DGELYITGRLKDLIIVRGRNHYPQDIEATAEEaHPALRPGCVAAFSVPDDGEERLVVVAeVERGADPADLAAIAAAIRaA 508
|
570 580 590
....*....|....*....|....*....|...
gi 15228909 522 FCRE-KLPaywvPKSVVF---GPLPKTATGKIQ 550
Cdd:cd05931 509 VAREhGVA----PADVVLvrpGSIPRTSSGKIQ 537
|
|
| A_NRPS_Bac |
cd17655 |
bacitracin synthetase and related proteins; This family of the adenylation (A) domain of ... |
36-554 |
1.56e-30 |
|
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: 124.75 E-value: 1.56e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228909 36 PTRKSVIHGSREYTWRQTYDRCRRLASALADRSIGPGSTVAIIAPNIPAMYEAHFGVPMCGAVLNCVNIRLNAPTVAFLL 115
Cdd:cd17655 11 PDHTAVVFEDQTLTYRELNERANQLARTLREKGVGPDTIVGIMAERSLEMIVGILGILKAGGAYLPIDPDYPEERIQYIL 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228909 116 SHSQSSVIMVDQEFF--TLAEDSLRLMEEKAGSSFKRpllivigdhtcapESLNRALSKGAIEYedflatgdpnypwqpp 193
Cdd:cd17655 91 EDSGADILLTQSHLQppIAFIGLIDLLDEDTIYHEES-------------ENLEPVSKSDDLAY---------------- 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228909 194 adewqsiaLGYTSGTTASPKGVVLHHRGayimaLSNpLIWGM-----QDGAVYLWTLPMFHCNGWCFPWSLAVLSGTSIC 268
Cdd:cd17655 142 --------VIYTSGSTGKPKGVMIEHRG-----VVN-LVEWAnkviyQGEHLRVALFASISFDASVTEIFASLLSGNTLY 207
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228909 269 L-RQVTAKEVYSM---IAKYKVTHFCAAPVVLNAIvnapKEDTILPLPHTVHVMTAGAAPPPSV---LFSMNQKGFRVAH 341
Cdd:cd17655 208 IvRKETVLDGQALtqyIRQNRITIIDLTPAHLKLL----DAADDSEGLSLKHLIVGGEALSTELakkIIELFGTNPTITN 283
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228909 342 TYGLSETygpsTVCA----WKPEWDSL--PPETQAKLNArqgvrytgmeQLDVIDtQTGKPVPADgkTAGEIVFRGNMVM 415
Cdd:cd17655 284 AYGPTET----TVDAsiyqYEPETDQQvsVPIGKPLGNT----------RIYILD-QYGRPQPVG--VAGELYIGGEGVA 346
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228909 416 KGYLKNPEANKETF------AGG-WFHSGDIAVKHPDNYIEIKDRSKDVIISGGENISSVEVENVVYHHPAVLEASVVAR 488
Cdd:cd17655 347 RGYLNRPELTAEKFvddpfvPGErMYRTGDLARWLPDGNIEFLGRIDHQVKIRGYRIELGEIEARLLQHPDIKEAVVIAR 426
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 15228909 489 PDERWQESPCAFVTLKSDYEkhdqnklAQDIMKFCREKLPAYWVPKSVV-FGPLPKTATGKIQKHIL 554
Cdd:cd17655 427 KDEQGQNYLCAYIVSEKELP-------VAQLREFLARELPDYMIPSYFIkLDEIPLTPNGKVDRKAL 486
|
|
| FATP_FACS |
cd05940 |
Fatty acid transport proteins (FATP) play dual roles as fatty acid transporters and its ... |
46-558 |
9.77e-30 |
|
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: 122.08 E-value: 9.77e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228909 46 REYTWRQTYDRCRRLASALADRSIGPGSTVAIIAPNIPAMYEAHFGVPMCGAVLNCVNIRLNAPTVAFLLSHSQSSVIMV 125
Cdd:cd05940 2 EALTYAELDAMANRYARWLKSLGLKPGDVVALFMENRPEYVLLWLGLVKIGAVAALINYNLRGESLAHCLNVSSAKHLVV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228909 126 DqefftlaedslrlmeekagssfkRPLLIvigdhtcapeslnralskgaieyedflatgdpnypwqppadewqsialgYT 205
Cdd:cd05940 82 D-----------------------AALYI-------------------------------------------------YT 89
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228909 206 SGTTASPK-GVVLHHRGAYIMALSNPLIWGMQDGAVYLwTLPMFHCNGWCFPWSLAVLSGTSICLR-QVTAKEVYSMIAK 283
Cdd:cd05940 90 SGTTGLPKaAIISHRRAWRGGAFFAGSGGALPSDVLYT-CLPLYHSTALIVGWSACLASGATLVIRkKFSASNFWDDIRK 168
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228909 284 YKVTHFCAAPVVLNAIVNAPKEDTilPLPHTVHVMTaGAAPPPSVLFSMnQKGF---RVAHTYGLSETYGPSTVCAWKPE 360
Cdd:cd05940 169 YQATIFQYIGELCRYLLNQPPKPT--ERKHKVRMIF-GNGLRPDIWEEF-KERFgvpRIAEFYAATEGNSGFINFFGKPG 244
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228909 361 WDSLPPETQAKLNARQGVRYtgmeqldviDTQTGKPV-PADGKT-------AGEIVFRGNMV--MKGYLKNPEANK---- 426
Cdd:cd05940 245 AIGRNPSLLRKVAPLALVKY---------DLESGEPIrDAEGRCikvprgePGLLISRINPLepFDGYTDPAATEKkilr 315
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228909 427 ETFAGG--WFHSGDIAVKHPDNYIEIKDRSKDVIISGGENISSVEVENVVYHHPAVLEASV----VARPDERwqeSPCAF 500
Cdd:cd05940 316 DVFKKGdaWFNTGDLMRLDGEGFWYFVDRLGDTFRWKGENVSTTEVAAVLGAFPGVEEANVygvqVPGTDGR---AGMAA 392
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*....
gi 15228909 501 VTLKSDYEkHDQNKLAQDIMKfcreKLPAYWVPKSVVFGP-LPKTATGKIQKHILRTKA 558
Cdd:cd05940 393 IVLQPNEE-FDLSALAAHLEK----NLPGYARPLFLRLQPeMEITGTFKQQKVDLRNEG 446
|
|
| AA-adenyl-dom |
TIGR01733 |
amino acid adenylation domain; This model represents a domain responsible for the specific ... |
49-485 |
3.22e-29 |
|
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: 119.68 E-value: 3.22e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228909 49 TWRQTYDRCRRLASALADR-SIGPGSTVAIIAPNIPAMYEAHFGVPMCGAVlnCVNIRLNAPT--VAFLLSHSQSSVIMV 125
Cdd:TIGR01733 1 TYRELDERANRLARHLRAAgGVGPGDRVAVLLERSAELVVAILAVLKAGAA--YVPLDPAYPAerLAFILEDAGARLLLT 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228909 126 DQEFFTLAEDslrlmeekagssfkRPLLIVIGDhtcapeslnralskgaieyEDFLATGDPNYPWQPPADEWQSIALGY- 204
Cdd:TIGR01733 79 DSALASRLAG--------------LVLPVILLD-------------------PLELAALDDAPAPPPPDAPSGPDDLAYv 125
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228909 205 --TSGTTASPKGVVLHHRGAYIMALSNPLIWGMQDGAVYLWTLPmFHCNGWCFPWSLAVLSGTSICL-----RQVTAKEV 277
Cdd:TIGR01733 126 iyTSGSTGRPKGVVVTHRSLVNLLAWLARRYGLDPDDRVLQFAS-LSFDASVEEIFGALLAGATLVVppedeERDDAALL 204
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228909 278 YSMIAKYKVTHFCAAPVVLNAIVNAPKEDtilpLPHTVHVMTAGAAPPPSVLFSMNQK--GFRVAHTYGLSETygpSTVC 355
Cdd:TIGR01733 205 AALIAEHPVTVLNLTPSLLALLAAALPPA----LASLRLVILGGEALTPALVDRWRARgpGARLINLYGPTET---TVWS 277
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228909 356 AWKPEWDSLPPETQAkLNArqGVRYTGMeQLDVIDtQTGKPVPADGktAGEIVFRGNMVMKGYLKNPEANKETFA----- 430
Cdd:TIGR01733 278 TATLVDPDDAPRESP-VPI--GRPLANT-RLYVLD-DDLRPVPVGV--VGELYIGGPGVARGYLNRPELTAERFVpdpfa 350
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 15228909 431 ----GGWFHSGDIAVKHPDNYIEIKDRSKD-VIISG-----GenissvEVENVVYHHPAVLEASV 485
Cdd:TIGR01733 351 ggdgARLYRTGDLVRYLPDGNLEFLGRIDDqVKIRGyrielG------EIEAALLRHPGVREAVV 409
|
|
| A_NRPS_VisG_like |
cd17651 |
similar to adenylation domain of virginiamycin S synthetase; This family of the adenylation (A) ... |
30-549 |
4.97e-29 |
|
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: 120.53 E-value: 4.97e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228909 30 RAAVVHPTRKSVIHGSREYTWRQTYDRCRRLASALADRSIGPGSTVAIIAPNIPAMYEAHFGVPMCGAVLNCVNIRLNAP 109
Cdd:cd17651 3 RQAARTPDAPALVAEGRRLTYAELDRRANRLAHRLRARGVGPGDLVALCARRSAELVVALLAILKAGAAYVPLDPAYPAE 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228909 110 TVAFLLSHSQSSVIMVDQEFFTLAEDslrlmEEKAGSsfkrpLLIVIGDHTCAPESLNRALSKGAIEYedflatgdpnyp 189
Cdd:cd17651 83 RLAFMLADAGPVLVLTHPALAGELAV-----ELVAVT-----LLDQPGAAAGADAEPDPALDADDLAY------------ 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228909 190 wqppadewqsiaLGYTSGTTASPKGVVLHHRGayimaLSNPLIW------GMQDGAVYLWTLPMFHCNGW-CFPwslAVL 262
Cdd:cd17651 141 ------------VIYTSGSTGRPKGVVMPHRS-----LANLVAWqarassLGPGARTLQFAGLGFDVSVQeIFS---TLC 200
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228909 263 SGTSICLR----QVTAKEVYSMIAKYKVTHFCAAPVVLNAIVNAPKEDTILPlPHTVHVMTAGAAPPPSVL---FSMNQK 335
Cdd:cd17651 201 AGATLVLPpeevRTDPPALAAWLDEQRISRVFLPTVALRALAEHGRPLGVRL-AALRYLLTGGEQLVLTEDlreFCAGLP 279
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228909 336 GFRVAHTYGLSETYGPS--TVCAWKPEWDSLPPETQAKLNARqgvrytgmeqLDVIDTQtGKPVPaDGKTaGEIVFRGNM 413
Cdd:cd17651 280 GLRLHNHYGPTETHVVTalSLPGDPAAWPAPPPIGRPIDNTR----------VYVLDAA-LRPVP-PGVP-GELYIGGAG 346
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228909 414 VMKGYLKNPEANKETFAGGWF-------HSGDIAVKHPDNYIEIKDRSKDVIISGGENISSVEVENVVYHHPAVLEASVV 486
Cdd:cd17651 347 LARGYLNRPELTAERFVPDPFvpgarmyRTGDLARWLPDGELEFLGRADDQVKIRGFRIELGEIEAALARHPGVREAVVL 426
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 15228909 487 ARPDERWQESPCAFVTLKSDYEkhdqnKLAQDIMKFCREKLPAYWVPKSVV-FGPLPKTATGKI 549
Cdd:cd17651 427 AREDRPGEKRLVAYVVGDPEAP-----VDAAELRAALATHLPEYMVPSAFVlLDALPLTPNGKL 485
|
|
| LC_FACS_like |
cd17640 |
Long-chain fatty acid CoA synthetase; This family includes long-chain fatty acid (C12-C20) CoA ... |
48-492 |
1.52e-28 |
|
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: 118.62 E-value: 1.52e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228909 48 YTWRQTYDRCRRLASALADRSIGPGSTVAIIAPNIPAMYEAHFGVPMCGavlnCVNI-RLNAPTV---AFLLSHSQSSVI 123
Cdd:cd17640 6 ITYKDLYQEILDFAAGLRSLGVKAGEKVALFADNSPRWLIADQGIMALG----AVDVvRGSDSSVeelLYILNHSESVAL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228909 124 MVDqefftlaedslrlmeekagssfkrpllivigdhtcapeslNRalskgaieyEDFLATgdpnypwqppadewqsiaLG 203
Cdd:cd17640 82 VVE----------------------------------------ND---------SDDLAT------------------II 94
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228909 204 YTSGTTASPKGVVLHHRGayimalsnpLIWGM---------QDGAVYLWTLPMFH-----CNGWCFPWSLAVLSgTSIcl 269
Cdd:cd17640 95 YTSGTTGNPKGVMLTHAN---------LLHQIrslsdivppQPGDRFLSILPIWHsyersAEYFIFACGCSQAY-TSI-- 162
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228909 270 rqvtaKEVYSMIAKYKVTHFCAAPVVLNAIVNAPKED-------------TILPLPHTVHVMTAGAAPPPSVLFSMNQKG 336
Cdd:cd17640 163 -----RTLKDDLKRVKPHYIVSVPRLWESLYSGIQKQvsksspikqflflFFLSGGIFKFGISGGGALPPHVDTFFEAIG 237
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228909 337 FRVAHTYGLSETYGPSTV-CAWKPEWDSL--P-PETQAKlnarqgvrytgmeqldVIDTQTGKPVPADGKtaGEIVFRGN 412
Cdd:cd17640 238 IEVLNGYGLTETSPVVSArRLKCNVRGSVgrPlPGTEIK----------------IVDPEGNVVLPPGEK--GIVWVRGP 299
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228909 413 MVMKGYLKNPEANKETF-AGGWFHSGDIAVKHPDNYIEIKDRSKDVII-SGGENISSVEVENVVYHHPAVLEASVVARpD 490
Cdd:cd17640 300 QVMKGYYKNPEATSKVLdSDGWFNTGDLGWLTCGGELVLTGRAKDTIVlSNGENVEPQPIEEALMRSPFIEQIMVVGQ-D 378
|
..
gi 15228909 491 ER 492
Cdd:cd17640 379 QK 380
|
|
| PRK13388 |
PRK13388 |
acyl-CoA synthetase; Provisional |
28-558 |
3.59e-28 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 237374 [Multi-domain] Cd Length: 540 Bit Score: 118.59 E-value: 3.59e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228909 28 LDRAAVVHPtrkSVIHGSREYTWRQTYDRCRRLASALADRSIGPGST-VAIIAPNIPAMYEAHFGVPMCGAVLNCVNIRL 106
Cdd:PRK13388 10 RDRAGDDTI---AVRYGDRTWTWREVLAEAAARAAALIALADPDRPLhVGVLLGNTPEMLFWLAAAALGGYVLVGLNTTR 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228909 107 NAPTVAFLLSHSQSSVIMVDQEFFTLAeDSLRLMEEkagssfkrPLLIVIGDhtcapeslnralskgaiEYEDFLATGDP 186
Cdd:PRK13388 87 RGAALAADIRRADCQLLVTDAEHRPLL-DGLDLPGV--------RVLDVDTP-----------------AYAELVAAAGA 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228909 187 NYPwQPPADEWQSIALGYTSGTTASPKGVVLHHRGAYIMALSNPLIWGMQDGAVYLWTLPMFHCNGWCFPWSLAVLSGTS 266
Cdd:PRK13388 141 LTP-HREVDAMDPFMLIFTSGTTGAPKAVRCSHGRLAFAGRALTERFGLTRDDVCYVSMPLFHSNAVMAGWAPAVASGAA 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228909 267 ICLR-QVTAKEVYSMIAKYKVTHFCAAPVVLNAIVNAPK--EDTILPLphtVHVMTAGAAPPPSVLFSmNQKGFRVAHTY 343
Cdd:PRK13388 220 VALPaKFSASGFLDDVRRYGATYFNYVGKPLAYILATPErpDDADNPL---RVAFGNEASPRDIAEFS-RRFGCQVEDGY 295
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228909 344 GLSETYGPSTvcawkpewdsLPPetqaklNARQGVRYTGMEQLDVIDTQTGKPVP-----ADGKTA------GEIVFR-G 411
Cdd:PRK13388 296 GSSEGAVIVV----------REP------GTPPGSIGRGAPGVAIYNPETLTECAvarfdAHGALLnadeaiGELVNTaG 359
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228909 412 NMVMKGYLKNPEANKETFAGGWFHSGDIAVKHPDNYIEIKDRSKDVIISGGENISSVEVENVVYHHPAVLEASVVARPDE 491
Cdd:PRK13388 360 AGFFEGYYNNPEATAERMRHGMYWSGDLAYRDADGWIYFAGRTADWMRVDGENLSAAPIERILLRHPAINRVAVYAVPDE 439
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228909 492 RWQESPCAFVTLkSDYEKHDQNKLAQdimkF--CREKLPAYWVPKSV-VFGPLPKTATGKIQKHILRTKA 558
Cdd:PRK13388 440 RVGDQVMAALVL-RDGATFDPDAFAA----FlaAQPDLGTKAWPRYVrIAADLPSTATNKVLKRELIAQG 504
|
|
| AACS_like |
cd05968 |
Uncharacterized acyl-CoA synthetase subfamily similar to Acetoacetyl-CoA synthetase; This ... |
28-555 |
9.56e-28 |
|
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: 117.59 E-value: 9.56e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228909 28 LDRAAVVHPTRKSVIH-----GSREYTWRQTYDRCRRLASALADRSIGPGSTVAIIAPNIPAMYEAHFGVPMCGAVLNCV 102
Cdd:cd05968 67 LDKWLADTRTRPALRWegedgTSRTLTYGELLYEVKRLANGLRALGVGKGDRVGIYLPMIPEIVPAFLAVARIGGIVVPI 146
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228909 103 NIRLNAPTVAFLLSHSQSSVIMVdQEFFTLAEDSLRLMEEKAGSSFKRPLL--IVIGDHTCAPESLNRAlskGAIEYEDF 180
Cdd:cd05968 147 FSGFGKEAAATRLQDAEAKALIT-ADGFTRRGREVNLKEEADKACAQCPTVekVVVVRHLGNDFTPAKG---RDLSYDEE 222
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228909 181 LATGDPNYPWQPPADEWQSIalgYTSGTTASPKGVVLHHRGAYI-MALSNPLIWGMQDGAVYLWTLPMfhcnGWCF-PWS 258
Cdd:cd05968 223 KETAGDGAERTESEDPLMII---YTSGTTGKPKGTVHVHAGFPLkAAQDMYFQFDLKPGDLLTWFTDL----GWMMgPWL 295
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228909 259 L--AVLSGTSICLRQ-----VTAKEVYSMIAKYKVTHFCAAPVVLNAIVNAPKEDTILPLPHTVHVMTAGAAP----PPS 327
Cdd:cd05968 296 IfgGLILGATMVLYDgapdhPKADRLWRMVEDHEITHLGLSPTLIRALKPRGDAPVNAHDLSSLRVLGSTGEPwnpePWN 375
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228909 328 VLFSMNQKGFRVAHTY-GLSETYGPSTVCAWkpewdsLPPETQAKLNARqgvrYTGMEQlDVIDTQtGKPVPadgKTAGE 406
Cdd:cd05968 376 WLFETVGKGRNPIINYsGGTEISGGILGNVL------IKPIKPSSFNGP----VPGMKA-DVLDES-GKPAR---PEVGE 440
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228909 407 IVFRGNMV--MKGYLKNPEANKET----FAGGWFHsGDIAVKHPDNYIEIKDRSKDVIISGGENISSVEVENVVYHHPAV 480
Cdd:cd05968 441 LVLLAPWPgmTRGFWRDEDRYLETywsrFDNVWVH-GDFAYYDEEGYFYILGRSDDTINVAGKRVGPAEIESVLNAHPAV 519
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 15228909 481 LEASVVARPDERWQESPCAFVTLKSDYEKHDQnkLAQDIMKFCREKLPAYWVPKSVVFGP-LPKTATGKIQKHILR 555
Cdd:cd05968 520 LESAAIGVPHPVKGEAIVCFVVLKPGVTPTEA--LAEELMERVADELGKPLSPERILFVKdLPKTRNAKVMRRVIR 593
|
|
| PRK05852 |
PRK05852 |
fatty acid--CoA ligase family protein; |
204-551 |
1.02e-27 |
|
fatty acid--CoA ligase family protein;
Pssm-ID: 235625 [Multi-domain] Cd Length: 534 Bit Score: 116.91 E-value: 1.02e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228909 204 YTSGTTASPKGVVLHHrgAYIMALSNPLI--WGMQDGAVYLWTLPMFHCNGWCFPWSLAVLSGTSICLR---QVTAKEVY 278
Cdd:PRK05852 183 FTGGTTGLPKMVPWTH--ANIASSVRAIItgYRLSPRDATVAVMPLYHGHGLIAALLATLASGGAVLLPargRFSAHTFW 260
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228909 279 SMIAKYKVTHFCAAPVVLNAIVNAPKEDTILPLPHTVHVMTAGAAP--PPSVLFSMNQKGFRVAHTYGLSE-TYGPSTVC 355
Cdd:PRK05852 261 DDIKAVGATWYTAVPTIHQILLERAATEPSGRKPAALRFIRSCSAPltAETAQALQTEFAAPVVCAFGMTEaTHQVTTTQ 340
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228909 356 AWKPEWDSLPPETQAKLNARQGVRYTgmeqldvIDTQTGKPVPADgkTAGEIVFRGNMVMKGYLKNPEANKETFAGGWFH 435
Cdd:PRK05852 341 IEGIGQTENPVVSTGLVGRSTGAQIR-------IVGSDGLPLPAG--AVGEVWLRGTTVVRGYLGDPTITAANFTDGWLR 411
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228909 436 SGDIAVKHPDNYIEIKDRSKDVIISGGENISSVEVENVVYHHPAVLEASVVARPDERWQESPCAFVTlksdyEKHDQNKL 515
Cdd:PRK05852 412 TGDLGSLSAAGDLSIRGRIKELINRGGEKISPERVEGVLASHPNVMEAAVFGVPDQLYGEAVAAVIV-----PRESAPPT 486
|
330 340 350
....*....|....*....|....*....|....*..
gi 15228909 516 AQDIMKFCREKLPAYWVPKSV-VFGPLPKTATGKIQK 551
Cdd:PRK05852 487 AEELVQFCRERLAAFEIPASFqEASGLPHTAKGSLDR 523
|
|
| FACL_like_5 |
cd05924 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
204-548 |
1.53e-27 |
|
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: 114.02 E-value: 1.53e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228909 204 YTSGTTASPKGVVLHHRGAYIMALSNPLI---------WGMQ-----DGAVYLWTLPMFHCNGWcFPWSLAVLSGTSICL 269
Cdd:cd05924 10 YTGGTTGMPKGVMWRQEDIFRMLMGGADFgtgeftpseDAHKaaaaaAGTVMFPAPPLMHGTGS-WTAFGGLLGGQTVVL 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228909 270 RQV--TAKEVYSMIAKYKVThfcAAPVVLNA----IVNAPKEDTILPLPHTVHVMTAGAAPPPSVlfsmnQKGFrVAHT- 342
Cdd:cd05924 89 PDDrfDPEEVWRTIEKHKVT---SMTIVGDAmarpLIDALRDAGPYDLSSLFAISSGGALLSPEV-----KQGL-LELVp 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228909 343 -------YGLSETYGPSTVCAwkpewDSLPPETQAKLNARQGVRytgmeqldVIDtQTGKPVPADGKTAGEIVFRGNMVM 415
Cdd:cd05924 160 nitlvdaFGSSETGFTGSGHS-----AGSGPETGPFTRANPDTV--------VLD-DDGRVVPPGSGGVGWIARRGHIPL 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228909 416 kGYLKNPEANKETF--AGG--WFHSGDIAVKHPDNYIEIKDRSKDVIISGGENISSVEVENVVYHHPAVLEASVVARPDE 491
Cdd:cd05924 226 -GYYGDEAKTAETFpeVDGvrYAVPGDRATVEADGTVTLLGRGSVCINTGGEKVFPEEVEEALKSHPAVYDVLVVGRPDE 304
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*...
gi 15228909 492 RWQESPCAFVTLKSDYEKHDqnklaQDIMKFCREKLPAYWVPKSVVFGP-LPKTATGK 548
Cdd:cd05924 305 RWGQEVVAVVQLREGAGVDL-----EELREHCRTRIARYKLPKQVVFVDeIERSPAGK 357
|
|
| LC_FACS_bac1 |
cd17641 |
bacterial long-chain fatty acid CoA synthetase; The members of this family are bacterial ... |
46-488 |
3.26e-27 |
|
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: 115.98 E-value: 3.26e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228909 46 REYTWRQTYDRCRRLASALADRSIGPGSTVAIIAPNIPAMYEAHFGVPMCGAVLNCVNIRLNAPTVAFLLSHSQSSVIMV 125
Cdd:cd17641 10 QEFTWADYADRVRAFALGLLALGVGRGDVVAILGDNRPEWVWAELAAQAIGALSLGIYQDSMAEEVAYLLNYTGARVVIA 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228909 126 -DQE----FFTLAED--SLR--LMEEKAG-SSFKRPLLIVIGDHTCAPESLNRALSKgaiEYEDFLATGDPnypwqppad 195
Cdd:cd17641 90 eDEEqvdkLLEIADRipSVRyvIYCDPRGmRKYDDPRLISFEDVVALGRALDRRDPG---LYEREVAAGKG--------- 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228909 196 ewQSIA-LGYTSGTTASPKGVVLHHRGAYIMALSNPLIWGMQDGAVYLWTLPMfhcngwcfPW--------SLAVLSGTS 266
Cdd:cd17641 158 --EDVAvLCTTSGTTGKPKLAMLSHGNFLGHCAAYLAADPLGPGDEYVSVLPL--------PWigeqmysvGQALVCGFI 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228909 267 ICL--RQVTAKEVYSMIAKykvTHFCAAPVVLNAI---VNAPKEDTIlPLPHTV--HVMTAG--AAP------PPS---- 327
Cdd:cd17641 228 VNFpeEPETMMEDLREIGP---TFVLLPPRVWEGIaadVRARMMDAT-PFKRFMfeLGMKLGlrALDrgkrgrPVSlwlr 303
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228909 328 --------VLFSM--NQKGF---RVAHT-----------------------YGLSETYGPSTVcawKPEWDsLPPETqak 371
Cdd:cd17641 304 laswladaLLFRPlrDRLGFsrlRSAATggaalgpdtfrffhaigvplkqlYGQTELAGAYTV---HRDGD-VDPDT--- 376
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228909 372 lnarqgvrytgmeqldvidtqTGKPVP-ADGKTA--GEIVFRGNMVMKGYLKNPEANKETF-AGGWFHSGDIAVKHPDNY 447
Cdd:cd17641 377 ---------------------VGVPFPgTEVRIDevGEILVRSPGVFVGYYKNPEATAEDFdEDGWLHTGDAGYFKENGH 435
|
490 500 510 520
....*....|....*....|....*....|....*....|..
gi 15228909 448 IEIKDRSKDV-IISGGENISSVEVENVVYHHPAVLEASVVAR 488
Cdd:cd17641 436 LVVIDRAKDVgTTSDGTRFSPQFIENKLKFSPYIAEAVVLGA 477
|
|
| AFD_YhfT-like |
cd17633 |
fatty acid-CoA ligase VraA; This family of acyl-CoA ligases includes Bacillus subtilis YhfT, ... |
203-549 |
4.04e-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: 111.73 E-value: 4.04e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228909 203 GYTSGTTASPKGVVLHHR--------GAYIMALSNP---LIWGMQDGAVYLWTLpmfhcngwcfpwsLAVLS--GTSICL 269
Cdd:cd17633 6 GFTSGTTGLPKAYYRSERswiesfvcNEDLFNISGEdaiLAPGPLSHSLFLYGA-------------ISALYlgGTFIGQ 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228909 270 RQVTAKEVYSMIAKYKVTHFCAAPVVLNAIVNapkedTILPLPHTVHVMTAGAAPPPSvLFSMNQKGFRVAHTYglsETY 349
Cdd:cd17633 73 RKFNPKSWIRKINQYNATVIYLVPTMLQALAR-----TLEPESKIKSIFSSGQKLFES-TKKKLKNIFPKANLI---EFY 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228909 350 GPS--TVCAWKPEWDSLPPETqaklnarqgvrytgmeqldvidtqTGKPVP--------ADGKTAGEIVFRGNMVMKGYL 419
Cdd:cd17633 144 GTSelSFITYNFNQESRPPNS------------------------VGRPFPnveieirnADGGEIGKIFVKSEMVFSGYV 199
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228909 420 KNPEANKetfaGGWFHSGDIAVKHPDNYIEIKDRSKDVIISGGENISSVEVENVVYHHPAVLEASVVARPDERWQESPCA 499
Cdd:cd17633 200 RGGFSNP----DGWMSVGDIGYVDEEGYLYLVGRESDMIIIGGINIFPTEIESVLKAIPGIEEAIVVGIPDARFGEIAVA 275
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|.
gi 15228909 500 FVTLKsdyekhdqNKLAQDIMKFCREKLPAYWVPKSVVF-GPLPKTATGKI 549
Cdd:cd17633 276 LYSGD--------KLTYKQLKRFLKQKLSRYEIPKKIIFvDSLPYTSSGKI 318
|
|
| ACS |
cd05966 |
Acetyl-CoA synthetase (also known as acetate-CoA ligase and acetyl-activating enzyme); ... |
45-555 |
4.48e-27 |
|
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: 115.74 E-value: 4.48e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228909 45 SREYTWRQTYDRCRRLASALADRSIGPGSTVAIIAPNIPamyEAHFgvpmcgAVLNCVniRLNAP-TVAFL--------- 114
Cdd:cd05966 82 SRTITYRELLREVCRFANVLKSLGVKKGDRVAIYMPMIP---ELVI------AMLACA--RIGAVhSVVFAgfsaeslad 150
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228909 115 -LSHSQSSVIMVDQEFF---------TLAEDSLrlmeEKAGSSfkRPLLIVigDHTCAPESLNRALSkgaIEYEDFLATG 184
Cdd:cd05966 151 rINDAQCKLVITADGGYrggkviplkEIVDEAL----EKCPSV--EKVLVV--KRTGGEVPMTEGRD---LWWHDLMAKQ 219
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228909 185 DPNYPWQPPADEWQSIALgYTSGTTASPKGVVlHHRGAYIM--ALSNPLIWGMQDGAVYlWtlpmfhCN---GWCFPWSL 259
Cdd:cd05966 220 SPECEPEWMDSEDPLFIL-YTSGSTGKPKGVV-HTTGGYLLyaATTFKYVFDYHPDDIY-W------CTadiGWITGHSY 290
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228909 260 AV----LSGTSICLRQVTAkeVY-------SMIAKYKVTHFCAAPVVLNAIvnapkedtilplphtvhvMTAGAAPPPSv 328
Cdd:cd05966 291 IVygplANGATTVMFEGTP--TYpdpgrywDIVEKHKVTIFYTAPTAIRAL------------------MKFGDEWVKK- 349
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228909 329 lfsMNQKGFRVAHTYGlsETYGPStvcAWKpeWDSlppetqaklnarqgvRYTGMEQLDVIDT----QTG---------- 394
Cdd:cd05966 350 ---HDLSSLRVLGSVG--EPINPE---AWM--WYY---------------EVIGKERCPIVDTwwqtETGgimitplpga 404
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228909 395 ---KP----------VPA-----DGKTAGEIvfRGNMV--------MKGYLKNPEANKETFAG---GWFHSGDIAVKHPD 445
Cdd:cd05966 405 tplKPgsatrpffgiEPAildeeGNEVEGEV--EGYLVikrpwpgmARTIYGDHERYEDTYFSkfpGYYFTGDGARRDED 482
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228909 446 NYIEIKDRSKDVIISGGENISSVEVENVVYHHPAVLEASVVARPDERWQESPCAFVTLKSDYEKHDqnKLAQDIMKFCRE 525
Cdd:cd05966 483 GYYWITGRVDDVINVSGHRLGTAEVESALVAHPAVAEAAVVGRPHDIKGEAIYAFVTLKDGEEPSD--ELRKELRKHVRK 560
|
570 580 590
....*....|....*....|....*....|.
gi 15228909 526 KLPAYWVPKSVVFGP-LPKTATGKIQKHILR 555
Cdd:cd05966 561 EIGPIATPDKIQFVPgLPKTRSGKIMRRILR 591
|
|
| A_NRPS_Sfm_like |
cd12115 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including Saframycin A gene ... |
27-549 |
1.34e-26 |
|
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: 112.80 E-value: 1.34e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228909 27 FLDRAAVVHPTRKSVIHGSREYTWRQTYDRCRRLASALADRSIGPGSTVAIIAPNIPAMYEAHFGVPMCGAVLncVNIRL 106
Cdd:cd12115 4 LVEAQAARTPDAIALVCGDESLTYAELNRRANRLAARLRAAGVGPESRVGVCLERTPDLVVALLAVLKAGAAY--VPLDP 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228909 107 NAPT--VAFLLSHSQSSVIMVDQEfftlaedslrlmeekagssfkrpllivigdhtcapeslnralskgaieyedflatg 184
Cdd:cd12115 82 AYPPerLRFILEDAQARLVLTDPD-------------------------------------------------------- 105
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228909 185 DPNYpwqppadewqsiaLGYTSGTTASPKGVVLHHRGAyimalSNPLIWGMQDGAVYLWTlpmfhcngwcfpwslAVLSG 264
Cdd:cd12115 106 DLAY-------------VIYTSGSTGRPKGVAIEHRNA-----AAFLQWAAAAFSAEELA---------------GVLAS 152
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228909 265 TSICLRQvtakEVYSMIakykVTHFCAAPVVL--NAIV----NAPKEDTIL--------------PLPHTVHVMT-AGAA 323
Cdd:cd12115 153 TSICFDL----SVFELF----GPLATGGKVVLadNVLAlpdlPAAAEVTLIntvpsaaaellrhdALPASVRVVNlAGEP 224
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228909 324 PPPSVLFSMNQK--GFRVAHTYGLSETYGPSTVCAwkpewdsLPPETQAKLNARQGVRYTgmeQLDVIDtQTGKPVPADg 401
Cdd:cd12115 225 LPRDLVQRLYARlqVERVVNLYGPSEDTTYSTVAP-------VPPGASGEVSIGRPLANT---QAYVLD-RALQPVPLG- 292
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228909 402 kTAGEIVFRGNMVMKGYLKNPEANKETFAGGWFHS-------GDIAVKHPDNYIEIKDRSKDVIISGGENISSVEVENVV 474
Cdd:cd12115 293 -VPGELYIGGAGVARGYLGRPGLTAERFLPDPFGPgarlyrtGDLVRWRPDGLLEFLGRADNQVKVRGFRIELGEIEAAL 371
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 15228909 475 YHHPAVLEASVVARPDERWQESPCAFVTLKSDYEkhdqnKLAQDIMKFCREKLPAYWVPKSVVFGP-LPKTATGKI 549
Cdd:cd12115 372 RSIPGVREAVVVAIGDAAGERRLVAYIVAEPGAA-----GLVEDLRRHLGTRLPAYMVPSRFVRLDaLPLTPNGKI 442
|
|
| AAS_C |
cd05909 |
C-terminal domain of the acyl-acyl carrier protein synthetase (also called ... |
204-549 |
2.49e-26 |
|
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: 112.42 E-value: 2.49e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228909 204 YTSGTTASPKGVVLHHRGAY--IMALSNPLIWGMQDgaVYLWTLPMFHCNGWCFPWSLAVLSGTSICL--RQVTAKEVYS 279
Cdd:cd05909 154 FTSGSEGLPKGVVLSHKNLLanVEQITAIFDPNPED--VVFGALPFFHSFGLTGCLWLPLLSGIKVVFhpNPLDYKKIPE 231
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228909 280 MIAKYKVTHFCAAPVVLNAIVNAPKEDTIlplpHTVHVMTAGAAPPPSVLFSMNQKGF--RVAHTYGLSETygpSTVCAW 357
Cdd:cd05909 232 LIYDKKATILLGTPTFLRGYARAAHPEDF----SSLRLVVAGAEKLKDTLRQEFQEKFgiRILEGYGTTEC---SPVISV 304
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228909 358 -KPEWDSlPPETQAKLnarqgvrYTGMEQLdVIDTQTGKPVPAdGKTaGEIVFRGNMVMKGYLKNPEANKETFAGGWFHS 436
Cdd:cd05909 305 nTPQSPN-KEGTVGRP-------LPGMEVK-IVSVETHEEVPI-GEG-GLLLVRGPNVMLGYLNEPELTSFAFGDGWYDT 373
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228909 437 GDIAVKHPDNYIEIKDRSKDVIISGGENISSVEVENVVYHH-PAVLEASVVARPDERWQESPCAFVTLkSDYEKHDQNKL 515
Cdd:cd05909 374 GDIGKIDGEGFLTITGRLSRFAKIAGEMVSLEAIEDILSEIlPEDNEVAVVSVPDGRKGEKIVLLTTT-TDTDPSSLNDI 452
|
330 340 350
....*....|....*....|....*....|....*
gi 15228909 516 AQDImkfcreKLPAYWVPKSV-VFGPLPKTATGKI 549
Cdd:cd05909 453 LKNA------GISNLAKPSYIhQVEEIPLLGTGKP 481
|
|
| LC-FACS_euk |
cd05927 |
Eukaryotic long-chain fatty acid CoA synthetase (LC-FACS); The members of this family are ... |
47-555 |
4.35e-26 |
|
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: 112.31 E-value: 4.35e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228909 47 EYTW---RQTYDRCRRLASALadRSIG----PGSTVAIIAPNIP----AMYEAH-FGvpmcgavLNCVNI--RLNAPTVA 112
Cdd:cd05927 2 PYEWisyKEVAERADNIGSAL--RSLGgkpaPASFVGIYSINRPewiiSELACYaYS-------LVTVPLydTLGPEAIE 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228909 113 FLLSHSQSSVIMVDQ--EFFTLaedslrlmeekagssfkrpllivigdhtcapeslnralskgaieyEDFLATGDPN-YP 189
Cdd:cd05927 73 YILNHAEISIVFCDAgvKVYSL---------------------------------------------EEFEKLGKKNkVP 107
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228909 190 WQPPADEwqSIA-LGYTSGTTASPKGVVLHHRGayIMALSNPLIWGMQDGA------VYLWTLPMFHCNGWCFPWsLAVL 262
Cdd:cd05927 108 PPPPKPE--DLAtICYTSGTTGNPKGVMLTHGN--IVSNVAGVFKILEILNkinptdVYISYLPLAHIFERVVEA-LFLY 182
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228909 263 SGTSICLRQVTAKEVYSMIAKYKVTHFCAAPVVLN----AIVNAPKEDTIL--------------------PLPHT---- 314
Cdd:cd05927 183 HGAKIGFYSGDIRLLLDDIKALKPTVFPGVPRVLNriydKIFNKVQAKGPLkrklfnfalnyklaelrsgvVRASPfwdk 262
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228909 315 -------------VHVMTAGAAP-PPSVLfsmnqKGFRVA------HTYGLSETYGPSTVcawkpewdSLPPETQAklna 374
Cdd:cd05927 263 lvfnkikqalggnVRLMLTGSAPlSPEVL-----EFLRVAlgcpvlEGYGQTECTAGATL--------TLPGDTSV---- 325
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228909 375 rqgvrytgmeqldvidTQTGKPVP----------------ADGKTAGEIVFRGNMVMKGYLKNPEANKETFA-GGWFHSG 437
Cdd:cd05927 326 ----------------GHVGGPLPcaevklvdvpemnydaKDPNPRGEVCIRGPNVFSGYYKDPEKTAEALDeDGWLHTG 389
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228909 438 DIAVKHPDNYIEIKDRSKDVI-ISGGENISSVEVENVVYHHPAV---------LEASVVA--RPDE----RWQESPCAFv 501
Cdd:cd05927 390 DIGEWLPNGTLKIIDRKKNIFkLSQGEYVAPEKIENIYARSPFVaqifvygdsLKSFLVAivVPDPdvlkEWAASKGGG- 468
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 15228909 502 tlKSDYE---KHDQNKLA--QDIMKFCRE-KLPAYWVPKSVVFGPLP-------KTATGKIQKHILR 555
Cdd:cd05927 469 --TGSFEelcKNPEVKKAilEDLVRLGKEnGLKGFEQVKAIHLEPEPfsvenglLTPTFKLKRPQLK 533
|
|
| PRK13383 |
PRK13383 |
acyl-CoA synthetase; Provisional |
31-549 |
4.49e-26 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 139531 [Multi-domain] Cd Length: 516 Bit Score: 112.01 E-value: 4.49e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228909 31 AAVVHPTRKSVIHGSREYTWRQTYDRCRRLASALADRSIGPGSTVAIIAPNIPAMYEAHFGVPMCGAVLNCVNIRLNAPT 110
Cdd:PRK13383 44 TAARWPGRTAIIDDDGALSYRELQRATESLARRLTRDGVAPGRAVGVMCRNGRGFVTAVFAVGLLGADVVPISTEFRSDA 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228909 111 VAFLLSHSQSSVIMVDQEFftlaedslrlMEEKAGSSfkrPLLIVIGDHTCAPESlnralskgaieyedflATGDPNYpw 190
Cdd:PRK13383 124 LAAALRAHHISTVVADNEF----------AERIAGAD---DAVAVIDPATAGAEE----------------SGGRPAV-- 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228909 191 QPPAdewqSIALgYTSGTTASPKGV-----VLHHRGAYIMALSNPLiwgMQDGAVYLWTLPMFHCNGWCFPWSLAVLSGT 265
Cdd:PRK13383 173 AAPG----RIVL-LTSGTTGKPKGVprapqLRSAVGVWVTILDRTR---LRTGSRISVAMPMFHGLGLGMLMLTIALGGT 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228909 266 SICLRQVTAKEVYSMIAKYKVTHFCAAPVVLNAIVNAPKEDTIL-PLPHTVHVMTAGAAPPPSVlfsmnqkGFRVAHTYG 344
Cdd:PRK13383 245 VLTHRHFDAEAALAQASLHRADAFTAVPVVLARILELPPRVRARnPLPQLRVVMSSGDRLDPTL-------GQRFMDTYG 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228909 345 --LSETYGPSTV---CAWKPEWDSLPPETQAKLNARQGVRytgmeqldvIDTQTGKPVPAdgKTAGEIVFRGNMVMKGYl 419
Cdd:PRK13383 318 diLYNGYGSTEVgigALATPADLRDAPETVGKPVAGCPVR---------ILDRNNRPVGP--RVTGRIFVGGELAGTRY- 385
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228909 420 knPEANKETFAGGWFHSGDIAVKHPDNYIEIKDRSKDVIISGGENISSVEVENVVYHHPAVLEASVVARPDERWQESPCA 499
Cdd:PRK13383 386 --TDGGGKAVVDGMTSTGDMGYLDNAGRLFIVGREDDMIISGGENVYPRAVENALAAHPAVADNAVIGVPDERFGHRLAA 463
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|...
gi 15228909 500 FVTLK--SDYEkhdqnklAQDIMKFCREKLPAYWVPKSV-VFGPLPKTATGKI 549
Cdd:PRK13383 464 FVVLHpgSGVD-------AAQLRDYLKDRVSRFEQPRDInIVSSIPRNPTGKV 509
|
|
| A_NRPS_PvdJ-like |
cd17649 |
non-ribosomal peptide synthetase; This family of the adenylation (A) domain of nonribosomal ... |
36-555 |
1.03e-25 |
|
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: 110.15 E-value: 1.03e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228909 36 PTRKSVIHGSREYTWRQTYDRCRRLASALADRSIGPGSTVAIIAPNIPAMYEAHFGVPMCGAVlnCVNIRLNAPTvafll 115
Cdd:cd17649 1 PDAVALVFGDQSLSYAELDARANRLAHRLRALGVGPEVRVGIALERSLEMVVALLAILKAGGA--YVPLDPEYPA----- 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228909 116 shsqssvimvdqefftlaeDSLRLMEEKAGSSfkrpllIVIGDHtcaPESLnralskgaiEYedflatgdpnypwqppad 195
Cdd:cd17649 74 -------------------ERLRYMLEDSGAG------LLLTHH---PRQL---------AY------------------ 98
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228909 196 ewqsiaLGYTSGTTASPKGVVLHHrGAYIMALSNPL-IWGMQDGAVYLWTLPM----FHcNGWCFPWslavLSGTSICLR 270
Cdd:cd17649 99 ------VIYTSGSTGTPKGVAVSH-GPLAAHCQATAeRYGLTPGDRELQFASFnfdgAH-EQLLPPL----ICGACVVLR 166
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228909 271 Q----VTAKEVYSMIAKYKVTHFCAAPVVLNAIVnAPKEDTILPLPHTVHVMTAGA-APPPSVLFSMNQKGFRVAHTYGL 345
Cdd:cd17649 167 PdelwASADELAEMVRELGVTVLDLPPAYLQQLA-EEADRTGDGRPPSLRLYIFGGeALSPELLRRWLKAPVRLFNAYGP 245
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228909 346 SETYGPSTVcaWKPEWDslppetqaklNARQGV-----RYTGMEQLDVIDTQTGkPVPADGktAGEIVFRGNMVMKGYLK 420
Cdd:cd17649 246 TEATVTPLV--WKCEAG----------AARAGAsmpigRPLGGRSAYILDADLN-PVPVGV--TGELYIGGEGLARGYLG 310
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228909 421 NPEANKETF-------AGG-WFHSGDIAVKHPDNYIEIKDRSKDVIISGGENISSVEVENVVYHHPAVLEASVVARPDER 492
Cdd:cd17649 311 RPELTAERFvpdpfgaPGSrLYRTGDLARWRDDGVIEYLGRVDHQVKIRGFRIELGEIEAALLEHPGVREAAVVALDGAG 390
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 15228909 493 wQESPCAFVTLKSDYEkhdQNKLAQDIMKFCREKLPAYWVPKSVVFGP-LPKTATGKIQKHILR 555
Cdd:cd17649 391 -GKQLVAYVVLRAAAA---QPELRAQLRTALRASLPDYMVPAHLVFLArLPLTPNGKLDRKALP 450
|
|
| A_NRPS_Cytc1-like |
cd17643 |
similar to adenylation domain of cytotrienin synthetase CytC1; This family of the adenylation ... |
36-551 |
1.50e-25 |
|
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: 109.70 E-value: 1.50e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228909 36 PTRKSVIHGSREYTWRQTYDRCRRLASALADRSIGPGSTVAIIAPNIPAMYEAHFGVPMCGAVLncVNIRLNAPT--VAF 113
Cdd:cd17643 1 PEAVAVVDEDRRLTYGELDARANRLARTLRAEGVGPGDRVALALPRSAELIVALLAILKAGGAY--VPIDPAYPVerIAF 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228909 114 LLSHSQSSVIMVDqefftlAEDslrlmeekagssfkrpLLIVIgdhtcapeslnralskgaieyedflatgdpnypwqpp 193
Cdd:cd17643 79 ILADSGPSLLLTD------PDD----------------LAYVI------------------------------------- 99
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228909 194 adewqsialgYTSGTTASPKGVVLHHRGAyiMALSNPLIWGMQDGAVYLWTlpMFHCNGWCFP-WSL--AVLSGTsiclR 270
Cdd:cd17643 100 ----------YTSGSTGRPKGVVVSHANV--LALFAATQRWFGFNEDDVWT--LFHSYAFDFSvWEIwgALLHGG----R 161
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228909 271 QV--------TAKEVYSMIAKYKVTHFCAAPVVLNAIVNAPKEDTILPLPHTVhVMTAGAAPPPSVLFSMNQK----GFR 338
Cdd:cd17643 162 LVvvpyevarSPEDFARLLRDEGVTVLNQTPSAFYQLVEAADRDGRDPLALRY-VIFGGEALEAAMLRPWAGRfgldRPQ 240
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228909 339 VAHTYGLSETygpsTV-CAWKPewdSLPPETQAKLNARQGVRYTGMeQLDVIDtQTGKPVPADGktAGEIVFRGNMVMKG 417
Cdd:cd17643 241 LVNMYGITET----TVhVTFRP---LDAADLPAAAASPIGRPLPGL-RVYVLD-ADGRPVPPGV--VGELYVSGAGVARG 309
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228909 418 YLKNPEANKETF----AGG----WFHSGDIAVKHPDNYIEIKDRSKDVIISGGENISSVEVENVVYHHPAVLEASVVARP 489
Cdd:cd17643 310 YLGRPELTAERFvanpFGGpgsrMYRTGDLARRLPDGELEYLGRADEQVKIRGFRIELGEIEAALATHPSVRDAAVIVRE 389
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 15228909 490 DERWQESPCAFVTLKSdyekhDQNKLAQDIMKFCREKLPAYWVPKSVVFGP-LPKTATGKIQK 551
Cdd:cd17643 390 DEPGDTRLVAYVVADD-----GAAADIAELRALLKELLPDYMVPARYVPLDaLPLTVNGKLDR 447
|
|
| A_NRPS_PpsD_like |
cd17650 |
similar to adenylation domain of plipastatin synthase (PpsD); This family of the adenylation ... |
36-554 |
1.82e-25 |
|
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: 109.48 E-value: 1.82e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228909 36 PTRKSVIHGSREYTWRQTYDRCRRLASALADRSIGPGSTVAIIAPNIPAMYEAHFGVPMCGAVLNCVNIRLNAPTVAFLL 115
Cdd:cd17650 1 PDAIAVSDATRQLTYRELNERANQLARTLRGLGVAPGSVVGVCADRSLDAIVGLLAVLKAGGAYVPIDPDYPAERLQYML 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228909 116 SHSQSSVIMVDQEfftlaedslrlmeekagssfkrpllivigdhtcapeslnralskgaieyedflatgDPNYpwqppad 195
Cdd:cd17650 81 EDSGAKLLLTQPE--------------------------------------------------------DLAY------- 97
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228909 196 ewqsiaLGYTSGTTASPKGVVLHHRGAYIMALSNPLIWGMQDGAVYLWTLPMFHCNGWCFPWSLAVLSGTS--ICLRQVT 273
Cdd:cd17650 98 ------VIYTSGTTGKPKGVMVEHRNVAHAAHAWRREYELDSFPVRLLQMASFSFDVFAGDFARSLLNGGTlvICPDEVK 171
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228909 274 AK--EVYSMIAKYKVTHFCAAPVVLNAIVNAPKEDTILPLPHTVHVMTAGAAPP--PSVLFSMNQKGFRVAHTYGLSETY 349
Cdd:cd17650 172 LDpaALYDLILKSRITLMESTPALIRPVMAYVYRNGLDLSAMRLLIVGSDGCKAqdFKTLAARFGQGMRIINSYGVTEAT 251
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228909 350 GPSTVCawkpEWDSLPPETQAKLNARQGVRYTGMEQLDvidtQTGKPVPADgkTAGEIVFRGNMVMKGYLKNPEANKETF 429
Cdd:cd17650 252 IDSTYY----EEGRDPLGDSANVPIGRPLPNTAMYVLD----ERLQPQPVG--VAGELYIGGAGVARGYLNRPELTAERF 321
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228909 430 ------AGG-WFHSGDIAVKHPDNYIEIKDRSKDVIISGGENISSVEVENVVYHHPAVLEASVVARPDERWQESPCAFVT 502
Cdd:cd17650 322 venpfaPGErMYRTGDLARWRADGNVELLGRVDHQVKIRGFRIELGEIESQLARHPAIDEAVVAVREDKGGEARLCAYVV 401
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|...
gi 15228909 503 LKsdyEKHDQNKLAQdimkFCREKLPAYWVPKS-VVFGPLPKTATGKIQKHIL 554
Cdd:cd17650 402 AA---ATLNTAELRA----FLAKELPSYMIPSYyVQLDALPLTPNGKVDRRAL 447
|
|
| LC_FACS_bac |
cd05932 |
Bacterial long-chain fatty acid CoA synthetase (LC-FACS), including Marinobacter ... |
47-486 |
5.65e-25 |
|
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: 108.71 E-value: 5.65e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228909 47 EYTWRQTYDRCRRLASALADRSIGPGSTVAIIAPNIPAMYEAHFGVPMCGAVLNCVNIRLNAPTVAFLLSHSQSSVIMVD 126
Cdd:cd05932 6 EFTWGEVADKARRLAAALRALGLEPGSKIALISKNCAEWFITDLAIWMAGHISVPLYPTLNPDTIRYVLEHSESKALFVG 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228909 127 QEfftlaeDSLRLMEEKAGssfKRPLLIVIGDHTCAPESLnralskgaiEYEDFLATGDPNYPWQPPADEwQSIALGYTS 206
Cdd:cd05932 86 KL------DDWKAMAPGVP---EGLISISLPPPSAANCQY---------QWDDLIAQHPPLEERPTRFPE-QLATLIYTS 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228909 207 GTTASPKGVvLHHRGAYIMALSNPL-IWGMQDGAVYLWTLPMFHCNGWCFPWSLAVLSGTSIC----------------- 268
Cdd:cd05932 147 GTTGQPKGV-MLTFGSFAWAAQAGIeHIGTEENDRMLSYLPLAHVTERVFVEGGSLYGGVLVAfaesldtfvedvqrarp 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228909 269 --------LRQVTAKEVYSMIAKYKVTHFCAAPVVlNAIVNApKEDTILPLPHtVHVMTAGAAP-PPSVLFSMNQKGFRV 339
Cdd:cd05932 226 tlffsvprLWTKFQQGVQDKIPQQKLNLLLKIPVV-NSLVKR-KVLKGLGLDQ-CRLAGCGSAPvPPALLEWYRSLGLNI 302
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228909 340 AHTYGLSETYGPSTVCawkpewdslppetqaklnaRQGVRYTGMeqldvidtqTGKPVPA-DGKTA--GEIVFRGNMVMK 416
Cdd:cd05932 303 LEAYGMTENFAYSHLN-------------------YPGRDKIGT---------VGNAGPGvEVRISedGEILVRSPALMM 354
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 15228909 417 GYLKNPEANKETF-AGGWFHSGDIAVKHPDNYIEIKDRSKDVI-ISGGENISSVEVENVVYHHPAVlEASVV 486
Cdd:cd05932 355 GYYKDPEATAEAFtADGFLRTGDKGELDADGNLTITGRVKDIFkTSKGKYVAPAPIENKLAEHDRV-EMVCV 425
|
|
| A_NRPS_CmdD_like |
cd17652 |
similar to adenylation domain of chondramide synthase cmdD; This family of the adenylation (A) ... |
36-549 |
8.42e-25 |
|
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: 107.34 E-value: 8.42e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228909 36 PTRKSVIHGSREYTWRQTYDRCRRLASALADRSIGPGSTVAIIAPNIPAMYEAHFGVPMCGAVLNCVNIRLNAPTVAFLL 115
Cdd:cd17652 1 PDAPAVVFGDETLTYAELNARANRLARLLAARGVGPERLVALALPRSAELVVAILAVLKAGAAYLPLDPAYPAERIAYML 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228909 116 SHSQSSVIMvdqeffTLAEDslrlmeekagssfkrpLLIVIgdhtcapeslnralskgaieyedflatgdpnypwqppad 195
Cdd:cd17652 81 ADARPALLL------TTPDN----------------LAYVI--------------------------------------- 99
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228909 196 ewqsialgYTSGTTASPKGVVLHHRGayIMALSNPLIWGMQ---DGAVYLWTLPMFHCNGWcfPWSLAVLSGTSICL--- 269
Cdd:cd17652 100 --------YTSGSTGRPKGVVVTHRG--LANLAAAQIAAFDvgpGSRVLQFASPSFDASVW--ELLMALLAGATLVLapa 167
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228909 270 -RQVTAKEVYSMIAKYKVTHFCAAPVVLNAIvnaPKEDtilpLPHTVHVMTAGAAPPPSvLFSMNQKGFRVAHTYGLSET 348
Cdd:cd17652 168 eELLPGEPLADLLREHRITHVTLPPAALAAL---PPDD----LPDLRTLVVAGEACPAE-LVDRWAPGRRMINAYGPTET 239
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228909 349 ygpsTVCAwkPEWDSLPPETQAKLnarqGVRYTGMeQLDVIDTQTgKPVPADgkTAGEIVFRGNMVMKGYLKNPEANKET 428
Cdd:cd17652 240 ----TVCA--TMAGPLPGGGVPPI----GRPVPGT-RVYVLDARL-RPVPPG--VPGELYIAGAGLARGYLNRPGLTAER 305
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228909 429 FAGGWF--------HSGDIAVKHPDNYIEIKDRSKDVIISGGENISSVEVENVVYHHPAVLEASVVARPDERWQESPCAF 500
Cdd:cd17652 306 FVADPFgapgsrmyRTGDLARWRADGQLEFLGRADDQVKIRGFRIELGEVEAALTEHPGVAEAVVVVRDDRPGDKRLVAY 385
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|
gi 15228909 501 VTlksdyEKHDQNKLAQDIMKFCREKLPAYWVPKSVVFGP-LPKTATGKI 549
Cdd:cd17652 386 VV-----PAPGAAPTAAELRAHLAERLPGYMVPAAFVVLDaLPLTPNGKL 430
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
27-554 |
1.28e-24 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 109.66 E-value: 1.28e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228909 27 FLDRAAVvHPTRKSVIHGSREYTWRQTYDRCRRLASALADRSIGPGSTVAIIAPNIPAMYEAHFGVPMCGAVLNCVNIRL 106
Cdd:PRK12316 4557 VAERARM-TPDAVAVVFDEEKLTYAELNRRANRLAHALIARGVGPEVLVGIAMERSAEMMVGLLAVLKAGGAYVPLDPEY 4635
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228909 107 NAPTVAFLLSHSQSSVIMVDQefftlaedslRLMEEkagssfkrpLLIVIGDHTCApesLNRALskgaiEYEDFLATgDP 186
Cdd:PRK12316 4636 PRERLAYMMEDSGAALLLTQS----------HLLQR---------LPIPDGLASLA---LDRDE-----DWEGFPAH-DP 4687
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228909 187 NYPWQPpadewQSIA-LGYTSGTTASPKGVVLHHRgayimALSNPLIWGMQ------------------DGAVYLWTLPM 247
Cdd:PRK12316 4688 AVRLHP-----DNLAyVIYTSGSTGRPKGVAVSHG-----SLVNHLHATGEryeltpddrvlqfmsfsfDGSHEGLYHPL 4757
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228909 248 fhCNGWCFpwslaVLSGTSICLRQVTakevYSMIAKYKVTHFCAAPVVLNAIVNAPKEDTilPLPHTVHVMTAGAAPPPS 327
Cdd:PRK12316 4758 --INGASV-----VIRDDSLWDPERL----YAEIHEHRVTVLVFPPVYLQQLAEHAERDG--EPPSLRVYCFGGEAVAQA 4824
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228909 328 VLfsmnQKGFRVAHTYGLSETYGPSTVCAWKPEWDSLPPETQAKLNARQGvRYTGMEQLDVIDTQtGKPVPADGktAGEI 407
Cdd:PRK12316 4825 SY----DLAWRALKPVYLFNGYGPTETTVTVLLWKARDGDACGAAYMPIG-TPLGNRSGYVLDGQ-LNPLPVGV--AGEL 4896
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228909 408 VFRGNMVMKGYLKNPEANKETF--------AGGWFHSGDIAVKHPDNYIEIKDRSKDVIISGGENISSVEVENVVYHHPA 479
Cdd:PRK12316 4897 YLGGEGVARGYLERPALTAERFvpdpfgapGGRLYRTGDLARYRADGVIDYLGRVDHQVKIRGFRIELGEIEARLREHPA 4976
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228909 480 VLEASVVARPDERWQESpCAFVT-----LKSDYEKhdQNKLAQDIMKFCREKLPAYWVPKSVVF-GPLPKTATGKIQKHI 553
Cdd:PRK12316 4977 VREAVVIAQEGAVGKQL-VGYVVpqdpaLADADEA--QAELRDELKAALRERLPEYMVPAHLVFlARMPLTPNGKLDRKA 5053
|
.
gi 15228909 554 L 554
Cdd:PRK12316 5054 L 5054
|
|
| PRK07638 |
PRK07638 |
acyl-CoA synthetase; Validated |
36-561 |
2.15e-24 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236071 [Multi-domain] Cd Length: 487 Bit Score: 106.40 E-value: 2.15e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228909 36 PTRKSVIHGSREYTWRQTYDRCRRLASALADRSIGPgSTVAIIAPNIPAMYEAHFGVPMCGAVLNCVNIRLNAPTVAFLL 115
Cdd:PRK07638 15 PNKIAIKENDRVLTYKDWFESVCKVANWLNEKESKN-KTIAILLENRIEFLQLFAGAAMAGWTCVPLDIKWKQDELKERL 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228909 116 SHSQSSVIMVDQEFFTlaedslRLMEEKAgssfkRPLLIvigdhtcapESLNRALSKGAIEY---EDflATGDPNYpwqp 192
Cdd:PRK07638 94 AISNADMIVTERYKLN------DLPDEEG-----RVIEI---------DEWKRMIEKYLPTYapiEN--VQNAPFY---- 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228909 193 padewqsiaLGYTSGTTASPKGVVLHHRgAYIMALS-NPLIWGMQDGAVYLWTLPMFHCNGWCFPWSLAVLSGTSICLRQ 271
Cdd:PRK07638 148 ---------MGFTSGSTGKPKAFLRAQQ-SWLHSFDcNVHDFHMKREDSVLIAGTLVHSLFLYGAISTLYVGQTVHLMRK 217
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228909 272 VTAKEVYSMIAKYKVTHFCAAPVVLNAIVnapKEDTILPlpHTVHVMTAGAA-PPPSVLFSMNQkgFRVAHTYglsETYG 350
Cdd:PRK07638 218 FIPNQVLDKLETENISVMYTVPTMLESLY---KENRVIE--NKMKIISSGAKwEAEAKEKIKNI--FPYAKLY---EFYG 287
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228909 351 PST---VCAWKPEWDSLPPETQAK--LNARQGVRYTGMEQLdvidtQTGKpvpadgktAGEIVFRGNMVMKGYLKNPEAN 425
Cdd:PRK07638 288 ASElsfVTALVDEESERRPNSVGRpfHNVQVRICNEAGEEV-----QKGE--------IGTVYVKSPQFFMGYIIGGVLA 354
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228909 426 KETFAGGWFHSGDIAVKHPDNYIEIKDRSKDVIISGGENISSVEVENVVYHHPAVLEASVVARPDERWQESPCAFVtlks 505
Cdd:PRK07638 355 RELNADGWMTVRDVGYEDEEGFIYIVGREKNMILFGGINIFPEEIESVLHEHPAVDEIVVIGVPDSYWGEKPVAII---- 430
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*..
gi 15228909 506 dyekhDQNKLAQDIMKFCREKLPAYWVPKSVVF-GPLPKTATGKIQKHILRTKAKEM 561
Cdd:PRK07638 431 -----KGSATKQQLKSFCLQRLSSFKIPKEWHFvDEIPYTNSGKIARMEAKSWIENQ 482
|
|
| PLN02614 |
PLN02614 |
long-chain acyl-CoA synthetase |
38-542 |
2.30e-24 |
|
long-chain acyl-CoA synthetase
Pssm-ID: 166255 [Multi-domain] Cd Length: 666 Bit Score: 107.41 E-value: 2.30e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228909 38 RKSVIHGSR-EYTWR---QTYDRCRRLASALADRSIGPGSTVAIIAPNIPamyEAHFGVPMCGAV-LNCVNI--RLNAPT 110
Cdd:PLN02614 66 RREIVDGKPgKYVWQtyqEVYDIVIKLGNSLRSVGVKDEAKCGIYGANSP---EWIISMEACNAHgLYCVPLydTLGAGA 142
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228909 111 VAFLLSHSQSSVIMVDQ----EFFTLAEDSLRLMEekagssfkrpllIVIGDHTCAPESLNRALSKGAIEY--EDFLATG 184
Cdd:PLN02614 143 VEFIISHSEVSIVFVEEkkisELFKTCPNSTEYMK------------TVVSFGGVSREQKEEAETFGLVIYawDEFLKLG 210
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228909 185 DP---NYPWQPPADewqSIALGYTSGTTASPKGVVLHHRG-----AYIMALSNPLIWGMQDGAVYLWTLPMFHCNGW--- 253
Cdd:PLN02614 211 EGkqyDLPIKKKSD---ICTIMYTSGTTGDPKGVMISNESivtliAGVIRLLKSANAALTVKDVYLSYLPLAHIFDRvie 287
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228909 254 -CFpwslaVLSGTSICLRQVTAKEVYSMIAKYKVTHFCAAPVVLNAIVN------------------------------- 301
Cdd:PLN02614 288 eCF-----IQHGAAIGFWRGDVKLLIEDLGELKPTIFCAVPRVLDRVYSglqkklsdggflkkfvfdsafsykfgnmkkg 362
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228909 302 ------APKEDTIL------PLPHTVHVMTAGAAPppsvLFSMNQKGFRVAHTYGLSETYGPSTVCAwkPEWDSLPPEtq 369
Cdd:PLN02614 363 qshveaSPLCDKLVfnkvkqGLGGNVRIILSGAAP----LASHVESFLRVVACCHVLQGYGLTESCA--GTFVSLPDE-- 434
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228909 370 aklnarqgvrytgmeqLDVIDTqTGKPVP---------------ADGKTA-GEIVFRGNMVMKGYLKNPEANKETFAGGW 433
Cdd:PLN02614 435 ----------------LDMLGT-VGPPVPnvdirlesvpemeydALASTPrGEICIRGKTLFSGYYKREDLTKEVLIDGW 497
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228909 434 FHSGDIAVKHPDNYIEIKDRSKDVI-ISGGENISSVEVENvVYHHPAVLEA------------SVVARPDERWQESPCAF 500
Cdd:PLN02614 498 LHTGDVGEWQPNGSMKIIDRKKNIFkLSQGEYVAVENIEN-IYGEVQAVDSvwvygnsfesflVAIANPNQQILERWAAE 576
|
570 580 590 600
....*....|....*....|....*....|....*....|....*...
gi 15228909 501 VTLKSDYEKHDQNKLAQ-----DIMKFCRE-KLPAYWVPKSVVFGPLP 542
Cdd:PLN02614 577 NGVSGDYNALCQNEKAKefilgELVKMAKEkKMKGFEIIKAIHLDPVP 624
|
|
| A_NRPS_TlmIV_like |
cd12114 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including ... |
36-549 |
4.19e-24 |
|
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: 105.43 E-value: 4.19e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228909 36 PTRKSVIHGSREYTWRQTYDRCRRLASALADRSIGPGSTVAIIAPNIPAMYEAHFGVPMCGAVLNCVNIRLNAPTVAFLL 115
Cdd:cd12114 1 PDATAVICGDGTLTYGELAERARRVAGALKAAGVRPGDLVAVTLPKGPEQVVAVLGILAAGAAYVPVDIDQPAARREAIL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228909 116 SHSQSSVIMVDqefftlaedslrlmeekagssfkrplliviGDHTCAPESLNRALskgaIEYEDFLATGDPnypwqPPAD 195
Cdd:cd12114 81 ADAGARLVLTD------------------------------GPDAQLDVAVFDVL----ILDLDALAAPAP-----PPPV 121
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228909 196 EWQSIALGY---TSGTTASPKGVVLHHRGAY-----------------IMALSnPLIWgmqDGAVYlwtlPMFhcngwcf 255
Cdd:cd12114 122 DVAPDDLAYvifTSGSTGTPKGVMISHRAALntildinrrfavgpddrVLALS-SLSF---DLSVY----DIF------- 186
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228909 256 pwslAVLS-GTSICL-RQVTAKEVYSM---IAKYKVTHFCAAPVVLNAIVNAPKEDTILP----------------LPHT 314
Cdd:cd12114 187 ----GALSaGATLVLpDEARRRDPAHWaelIERHGVTLWNSVPALLEMLLDVLEAAQALLpslrlvllsgdwipldLPAR 262
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228909 315 VHVMTAGAApppsvLFSMNqkgfrvahtyGLSETYGPSTVC---AWKPEWDSLPpetqaklnarQGVRYTGMeQLDVIDT 391
Cdd:cd12114 263 LRALAPDAR-----LISLG----------GATEASIWSIYHpidEVPPDWRSIP----------YGRPLANQ-RYRVLDP 316
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228909 392 QtGKPVPaDGkTAGEIVFRGNMVMKGYLKNPEANKETF-----AGGWFHSGDIAVKHPDNYIEIKDRSKDVIISGGENIS 466
Cdd:cd12114 317 R-GRDCP-DW-VPGELWIGGRGVALGYLGDPELTAARFvthpdGERLYRTGDLGRYRPDGTLEFLGRRDGQVKVRGYRIE 393
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228909 467 SVEVENVVYHHPAVLEASVVARpDERWQESPCAFVTLKSDYEKHDQNKLAQdimkFCREKLPAYWVPKSVVFGP-LPKTA 545
Cdd:cd12114 394 LGEIEAALQAHPGVARAVVVVL-GDPGGKRLAAFVVPDNDGTPIAPDALRA----FLAQTLPAYMIPSRVIALEaLPLTA 468
|
....
gi 15228909 546 TGKI 549
Cdd:cd12114 469 NGKV 472
|
|
| LC_FACS_euk1 |
cd17639 |
Eukaryotic long-chain fatty acid CoA synthetase (LC-FACS), including fungal proteins; The ... |
204-501 |
4.42e-24 |
|
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: 105.76 E-value: 4.42e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228909 204 YTSGTTASPKGVVLHHRG--AYIMALSNPLIWGMQDGAVYLWTLPMFH-----CNGWCFPWSLAVLSGTSICLRQVTAKE 276
Cdd:cd17639 95 YTSGSTGNPKGVMLTHGNlvAGIAGLGDRVPELLGPDDRYLAYLPLAHifelaAENVCLYRGGTIGYGSPRTLTDKSKRG 174
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228909 277 VYSMIAKYKVTHFCAAPVVLNAI-------VNAP--------------KEDTILPLPHT------------------VHV 317
Cdd:cd17639 175 CKGDLTEFKPTLMVGVPAIWDTIrkgvlakLNPMgglkrtlfwtayqsKLKALKEGPGTplldelvfkkvraalggrLRY 254
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228909 318 MTAGAAP--PPSVLFsMNQKGFRVAHTYGLSETYGPSTVCAWkPEWDS-----LPPETQAKLnarqgvrytgmeqLDVID 390
Cdd:cd17639 255 MLSGGAPlsADTQEF-LNIVLCPVIQGYGLTETCAGGTVQDP-GDLETgrvgpPLPCCEIKL-------------VDWEE 319
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228909 391 --TQTGKPVPAdgktaGEIVFRGNMVMKGYLKNPEANKETFAG-GWFHSGDIAVKHPDNYIEIKDRSKD-VIISGGENIS 466
Cdd:cd17639 320 ggYSTDKPPPR-----GEILIRGPNVFKGYYKNPEKTKEAFDGdGWFHTGDIGEFHPDGTLKIIDRKKDlVKLQNGEYIA 394
|
330 340 350
....*....|....*....|....*....|....*
gi 15228909 467 SVEVENVVYHHPAVLEASVVARPDerwQESPCAFV 501
Cdd:cd17639 395 LEKLESIYRSNPLVNNICVYADPD---KSYPVAIV 426
|
|
| ACSBG_like |
cd05933 |
Bubblegum-like very long-chain fatty acid CoA synthetase (VL-FACS); This family of very ... |
49-524 |
7.56e-24 |
|
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: 105.52 E-value: 7.56e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228909 49 TWRQTYDRCRRLASALADRSIGPGSTVAIIAPNIPAMYEAHFGVPMCGAVlnCVNI-RLNAP-TVAFLLSHSQSSVIMVD 126
Cdd:cd05933 10 TYKEYYEACRQAAKAFLKLGLERFHGVGILGFNSPEWFIAAVGAIFAGGI--AVGIyTTNSPeACQYVAETSEANILVVE 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228909 127 QEfftlaedslRLMEEKAGSSFKRPLLivigdhtcapeslnralsKGAIEYEDFLATGDPN-YPWQP--------PADEW 197
Cdd:cd05933 88 NQ---------KQLQKILQIQDKLPHL------------------KAIIQYKEPLKEKEPNlYSWDEfmelgrsiPDEQL 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228909 198 QSI----------ALGYTSGTTASPKGVVLHH-------RGAYIMALSNPLIWGMQDGAVYL------------WTlPMF 248
Cdd:cd05933 141 DAIissqkpnqccTLIYTSGTTGMPKGVMLSHdnitwtaKAASQHMDLRPATVGQESVVSYLplshiaaqildiWL-PIK 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228909 249 HCNGWCFPwSLAVLSGTSI-CLRQVT-------------------AKEVYSMIAKYKVTHFcAAPVVLNAIVNAPKEDTI 308
Cdd:cd05933 220 VGGQVYFA-QPDALKGTLVkTLREVRptafmgvprvwekiqekmkAVGAKSGTLKRKIASW-AKGVGLETNLKLMGGESP 297
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228909 309 LPLPHTV------------------HVMTAGAAPPPS----VLFSMNqkgFRVAHTYGLSETYGPSTVCAwkpewdslpP 366
Cdd:cd05933 298 SPLFYRLakklvfkkvrkalgldrcQKFFTGAAPISRetleFFLSLN---IPIMELYGMSETSGPHTISN---------P 365
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228909 367 ETQAKLNArqGVRYTGME-QLDVIDtqtgkpvpADGKtaGEIVFRGNMVMKGYLKNPEANKETF-AGGWFHSGDIAVKHP 444
Cdd:cd05933 366 QAYRLLSC--GKALPGCKtKIHNPD--------ADGI--GEICFWGRHVFMGYLNMEDKTEEAIdEDGWLHSGDLGKLDE 433
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228909 445 DNYIEIKDRSKDVII-SGGENISSVEVENVVYHH-PAVLEASVVArpDERwqESPCAFVTLKS--DYEKHDQ-NKLAQDI 519
Cdd:cd05933 434 DGFLYITGRIKELIItAGGENVPPVPIEDAVKKElPIISNAMLIG--DKR--KFLSMLLTLKCevNPETGEPlDELTEEA 509
|
....*
gi 15228909 520 MKFCR 524
Cdd:cd05933 510 IEFCR 514
|
|
| EntF |
COG1020 |
EntF, seryl-AMP synthase component of non-ribosomal peptide synthetase [Secondary metabolites ... |
26-568 |
1.10e-23 |
|
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: 106.09 E-value: 1.10e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228909 26 WFLDRAAVvHPTRKSVIHGSREYTWRQTYDRCRRLASALADRSIGPGSTVAIIAPNIPAMYEAHFGVPMCGAVlnCVNIR 105
Cdd:COG1020 481 LFEAQAAR-TPDAVAVVFGDQSLTYAELNARANRLAHHLRALGVGPGDLVGVCLERSLEMVVALLAVLKAGAA--YVPLD 557
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228909 106 LNAPT--VAFLLSHSQSSVIMVDQEFFT-LAEDSLRLM----EEKAGSSFKRPLLIVIGDHtcapeslnralskgaieye 178
Cdd:COG1020 558 PAYPAerLAYMLEDAGARLVLTQSALAArLPELGVPVLaldaLALAAEPATNPPVPVTPDD------------------- 618
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228909 179 dfLAtgdpnYpwqppadewqsiaLGYTSGTTASPKGVVLHHRGayimaLSNpLIWGMQ-------------------DGA 239
Cdd:COG1020 619 --LA-----Y-------------VIYTSGSTGRPKGVMVEHRA-----LVN-LLAWMQrryglgpgdrvlqfaslsfDAS 672
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228909 240 VY--LWTLpmfhCNGwcfpwslavlsGTSICLRQVTAKEVYSM---IAKYKVTHFCAAPVVLNAIVNAPKEDtilpLPHT 314
Cdd:COG1020 673 VWeiFGAL----LSG-----------ATLVLAPPEARRDPAALaelLARHRVTVLNLTPSLLRALLDAAPEA----LPSL 733
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228909 315 VHVMTAGAAPPPSVL--FSMNQKGFRVAHTYGLSETygpsTVCA--WK-----PEWDSLP-----PETQAklnarqgvrY 380
Cdd:COG1020 734 RLVLVGGEALPPELVrrWRARLPGARLVNLYGPTET----TVDStyYEvtppdADGGSVPigrpiANTRV---------Y 800
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228909 381 tgmeqldVIDTQtGKPVPaDGkTAGEIVFRGNMVMKGYLKNPE-------ANKETFAGG-WFHSGDIAVKHPDNYIEIKD 452
Cdd:COG1020 801 -------VLDAH-LQPVP-VG-VPGELYIGGAGLARGYLNRPEltaerfvADPFGFPGArLYRTGDLARWLPDGNLEFLG 870
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228909 453 RSKD-VIISG-----GEnissveVENVVYHHPAVLEASVVARPDERWQESPCAFVTLKSDYEKHDQNKLAQDimkfcREK 526
Cdd:COG1020 871 RADDqVKIRGfrielGE------IEAALLQHPGVREAVVVAREDAPGDKRLVAYVVPEAGAAAAAALLRLAL-----ALL 939
|
570 580 590 600
....*....|....*....|....*....|....*....|..
gi 15228909 527 LPAYWVPkSVVFGPLPKTATGKIQKHILRTKAKEMGPVPRSR 568
Cdd:COG1020 940 LPPYMVP-AAVVLLLPLPLTGNGKLDRLALPAPAAAAAAAAA 980
|
|
| PRK00174 |
PRK00174 |
acetyl-CoA synthetase; Provisional |
204-559 |
2.07e-23 |
|
acetyl-CoA synthetase; Provisional
Pssm-ID: 234677 [Multi-domain] Cd Length: 637 Bit Score: 104.45 E-value: 2.07e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228909 204 YTSGTTASPKGVvLHHRGAYIM--ALSNPLIWGMQDGAVYlWtlpmfhCN---GWCFPWSLAV---LS--GTSICLRQV- 272
Cdd:PRK00174 252 YTSGSTGKPKGV-LHTTGGYLVyaAMTMKYVFDYKDGDVY-W------CTadvGWVTGHSYIVygpLAngATTLMFEGVp 323
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228909 273 ---TAKEVYSMIAKYKVTHFCAAPVVLNAIvnapkedtilplphtvhvMTAGAAPPpsvlfsmnqKGF-----RVAHTYG 344
Cdd:PRK00174 324 nypDPGRFWEVIDKHKVTIFYTAPTAIRAL------------------MKEGDEHP---------KKYdlsslRLLGSVG 376
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228909 345 lsETYGPStvcAWkpEW-------------DS-------------LPPETQAKLNARQ----GVrytgmeQLDVIDTqTG 394
Cdd:PRK00174 377 --EPINPE---AW--EWyykvvggercpivDTwwqtetggimitpLPGATPLKPGSATrplpGI------QPAVVDE-EG 442
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228909 395 KPVPADGktageivfRGNMV--------MKGYLKNPEANKET----FAGGWFhSGDIAVKHPDNYIEIKDRSKDVIISGG 462
Cdd:PRK00174 443 NPLEGGE--------GGNLVikdpwpgmMRTIYGDHERFVKTyfstFKGMYF-TGDGARRDEDGYYWITGRVDDVLNVSG 513
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228909 463 ENISSVEVENVVYHHPAVLEASVVARPDERWQESPCAFVTLKSDYEKHDQnkLAQDIMKFCREKLPAYWVPKSVVFGP-L 541
Cdd:PRK00174 514 HRLGTAEIESALVAHPKVAEAAVVGRPDDIKGQGIYAFVTLKGGEEPSDE--LRKELRNWVRKEIGPIAKPDVIQFAPgL 591
|
410
....*....|....*...
gi 15228909 542 PKTATGKIQKHILRTKAK 559
Cdd:PRK00174 592 PKTRSGKIMRRILRKIAE 609
|
|
| A_NRPS_TubE_like |
cd05906 |
The adenylation domain (A domain) of a family of nonribosomal peptide synthetases (NRPSs) ... |
175-556 |
2.10e-23 |
|
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: 103.90 E-value: 2.10e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228909 175 IEYEDFLATGdPNYPWqPPADEWQSIALGYTSGTTASPKGVVLHHRGAYIMALSNPLIWGMQDGAVYLWTLPMFHCNGWC 254
Cdd:cd05906 147 LSIEELLDTA-ADHDL-PQSRPDDLALLMLTSGSTGFPKAVPLTHRNILARSAGKIQHNGLTPQDVFLNWVPLDHVGGLV 224
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228909 255 FPWSLAVLSGtsiCLR-QVTAKEVYS-------MIAKYKVTHFCAAPVVLNAIVNAPKEDTILP--LPHTVHVMTAGAAp 324
Cdd:cd05906 225 ELHLRAVYLG---CQQvHVPTEEILAdplrwldLIDRYRVTITWAPNFAFALLNDLLEEIEDGTwdLSSLRYLVNAGEA- 300
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228909 325 ppsVLFSMNQKGFRVAHTYGLSET-----YGPSTVCA---WKPEwDSLPPETQAKLNARQGVRYTGMEqLDVIDtQTGKP 396
Cdd:cd05906 301 ---VVAKTIRRLLRLLEPYGLPPDairpaFGMTETCSgviYSRS-FPTYDHSQALEFVSLGRPIPGVS-MRIVD-DEGQL 374
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228909 397 VPADgkTAGEIVFRGNMVMKGYLKNPEANKETF-AGGWFHSGDIAVKHpDNYIEIKDRSKDVIISGGENISSVEVENVVY 475
Cdd:cd05906 375 LPEG--EVGRLQVRGPVVTKGYYNNPEANAEAFtEDGWFRTGDLGFLD-NGNLTITGRTKDTIIVNGVNYYSHEIEAAVE 451
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228909 476 HHPAVLEASVVA---RPDERWQESPCafVTLKSDYEKHDQ-NKLAQDIMKFCREKL---PAYWVPksVVFGPLPKTATGK 548
Cdd:cd05906 452 EVPGVEPSFTAAfavRDPGAETEELA--IFFVPEYDLQDAlSETLRAIRSVVSREVgvsPAYLIP--LPKEEIPKTSLGK 527
|
....*...
gi 15228909 549 IQKHILRT 556
Cdd:cd05906 528 IQRSKLKA 535
|
|
| AMP-binding_C |
pfam13193 |
AMP-binding enzyme C-terminal domain; This is a small domain that is found C terminal to ... |
469-548 |
2.78e-23 |
|
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: 93.38 E-value: 2.78e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228909 469 EVENVVYHHPAVLEASVVARPDERWQESPCAFVTLKSDYEkhdqnKLAQDIMKFCREKLPAYWVPKSVVFGP-LPKTATG 547
Cdd:pfam13193 1 EVESALVSHPAVAEAAVVGVPDELKGEAPVAFVVLKPGVE-----LLEEELVAHVREELGPYAVPKEVVFVDeLPKTRSG 75
|
.
gi 15228909 548 K 548
Cdd:pfam13193 76 K 76
|
|
| PRK08633 |
PRK08633 |
2-acyl-glycerophospho-ethanolamine acyltransferase; Validated |
204-549 |
9.52e-23 |
|
2-acyl-glycerophospho-ethanolamine acyltransferase; Validated
Pssm-ID: 236315 [Multi-domain] Cd Length: 1146 Bit Score: 103.08 E-value: 9.52e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228909 204 YTSGTTASPKGVVLHHR--GAYIMALSNplIWGMQDGAVYLWTLPMFHCNGWCFPWSLAVLSG-TSICLRQVT-AKEVYS 279
Cdd:PRK08633 789 FSSGSEGEPKGVMLSHHniLSNIEQISD--VFNLRNDDVILSSLPFFHSFGLTVTLWLPLLEGiKVVYHPDPTdALGIAK 866
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228909 280 MIAKYKVTHFCAAPVVLNAIVNAPKedtILPLP-HTVHVMTAGAAP-PPSVLFSMNQK-GFRVAHTYGLSETYGPSTVCA 356
Cdd:PRK08633 867 LVAKHRATILLGTPTFLRLYLRNKK---LHPLMfASLRLVVAGAEKlKPEVADAFEEKfGIRILEGYGATETSPVASVNL 943
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228909 357 wkPewDSLPPETQAKLNARQGVryTGME----QLDVIDTQTGKPVPAdgKTAGEIVFRGNMVMKGYLKNP----EANKET 428
Cdd:PRK08633 944 --P--DVLAADFKRQTGSKEGS--VGMPlpgvAVRIVDPETFEELPP--GEDGLILIGGPQVMKGYLGDPektaEVIKDI 1015
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228909 429 FAGGWFHSGDIAVKHPDNYIEIKDR----SKdvIisGGENISSVEVENVVYhhpAVLEAS-----VVARPDERWQESPCA 499
Cdd:PRK08633 1016 DGIGWYVTGDKGHLDEDGFLTITDRysrfAK--I--GGEMVPLGAVEEELA---KALGGEevvfaVTAVPDEKKGEKLVV 1088
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|.
gi 15228909 500 FVTLKSDYEKHDQNKLAQdimkfcrEKLPAYWVPKSVVFG-PLPKTATGKI 549
Cdd:PRK08633 1089 LHTCGAEDVEELKRAIKE-------SGLPNLWKPSRYFKVeALPLLGSGKL 1132
|
|
| PLN02430 |
PLN02430 |
long-chain-fatty-acid-CoA ligase |
49-480 |
4.85e-22 |
|
long-chain-fatty-acid-CoA ligase
Pssm-ID: 178049 [Multi-domain] Cd Length: 660 Bit Score: 100.27 E-value: 4.85e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228909 49 TWRQTYDRCRRLASALADRSIGPGSTVAIIAPNIPAMYEAhfgVPMCGA-VLNCVNI--RLNAPTVAFLLSHSQSSVIMV 125
Cdd:PLN02430 78 TYKEVYEEVLQIGSALRASGAEPGSRVGIYGSNCPQWIVA---MEACAAhSLICVPLydTLGPGAVDYIVDHAEIDFVFV 154
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228909 126 -DQEFFTLAEDSLRlmeekagsSFKRpLLIVIGDHTCAPESLNRALSKGAIEY--EDFLATGDPNyPWQPPADEWQSI-A 201
Cdd:PLN02430 155 qDKKIKELLEPDCK--------SAKR-LKAIVSFTSVTEEESDKASQIGVKTYswIDFLHMGKEN-PSETNPPKPLDIcT 224
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228909 202 LGYTSGTTASPKGVVLHHRGAYIMALSNPLIW-----GMQDGAVYLWTLPMFHC-----NGWCF---------------- 255
Cdd:PLN02430 225 IMYTSGTSGDPKGVVLTHEAVATFVRGVDLFMeqfedKMTHDDVYLSFLPLAHIldrmiEEYFFrkgasvgyyhgdlnal 304
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228909 256 --------PWSLA--------VLSGTSICLRQVTA--KEVYSMIAKYKV-------THFCAAPVVLNAIVNAPKEDtilp 310
Cdd:PLN02430 305 rddlmelkPTLLAgvprvferIHEGIQKALQELNPrrRLIFNALYKYKLawmnrgySHKKASPMADFLAFRKVKAK---- 380
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228909 311 LPHTVHVMTAGAAPppsvLFSMNQKGFRVA------HTYGLSETYGPSTVCAwkpewdslpPETQAKLNARQGVR-YTGM 383
Cdd:PLN02430 381 LGGRLRLLISGGAP----LSTEIEEFLRVTscafvvQGYGLTETLGPTTLGF---------PDEMCMLGTVGAPAvYNEL 447
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228909 384 EQLDVIDTQTGkpvPADGKTAGEIVFRGNMVMKGYLKNPEANKETFAGGWFHSGDIAVKHPDNYIEIKDRSKDVI-ISGG 462
Cdd:PLN02430 448 RLEEVPEMGYD---PLGEPPRGEICVRGKCLFSGYYKNPELTEEVMKDGWFHTGDIGEILPNGVLKIIDRKKNLIkLSQG 524
|
490
....*....|....*...
gi 15228909 463 ENISSVEVENVVYHHPAV 480
Cdd:PLN02430 525 EYVALEYLENVYGQNPIV 542
|
|
| A_NRPS_Ta1_like |
cd12116 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including salinosporamide A ... |
36-549 |
1.59e-21 |
|
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: 97.75 E-value: 1.59e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228909 36 PTRKSVIHGSREYTWRQTYDRCRRLASALADRSIGPGSTVAIIAPNIPAMYEAHFGVpmcgavlncvnIRLNAPTVAfll 115
Cdd:cd12116 1 PDATAVRDDDRSLSYAELDERANRLAARLRARGVGPGDRVAVYLPRSARLVAAMLAV-----------LKAGAAYVP--- 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228909 116 shsqssvimVDQEFftlAEDSLRLMEEKAGssfkrPLLIVIGDHTCAPESLNRALSKGAIEYedflATGDPNYPWQPPAD 195
Cdd:cd12116 67 ---------LDPDY---PADRLRYILEDAE-----PALVLTDDALPDRLPAGLPVLLLALAA----AAAAPAAPRTPVSP 125
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228909 196 EwQSIALGYTSGTTASPKGVVLHHRG--AYIMALSNPLIWGMQDGAVYLWTLpmfhcngwCFPWS-----LAVLSGTS-- 266
Cdd:cd12116 126 D-DLAYVIYTSGSTGRPKGVVVSHRNlvNFLHSMRERLGLGPGDRLLAVTTY--------AFDISllellLPLLAGARvv 196
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228909 267 ICLRQVT--AKEVYSMIAKYKVTHFCAAPVVLNAIVNAPKEDtilplPHTVHVMTAGAAPPPSVLFSMNQKGFRVAHTYG 344
Cdd:cd12116 197 IAPRETQrdPEALARLIEAHSITVMQATPATWRMLLDAGWQG-----RAGLTALCGGEALPPDLAARLLSRVGSLWNLYG 271
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228909 345 LSETYGPSTVCAWKPEWDSLP-----PETQaklnarqgvrytgmeqLDVIDTQtGKPVPADgkTAGEIVFRGNMVMKGYL 419
Cdd:cd12116 272 PTETTIWSTAARVTAAAGPIPigrplANTQ----------------VYVLDAA-LRPVPPG--VPGELYIGGDGVAQGYL 332
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228909 420 KNPEANKETF-------AGG-WFHSGDIAVKHPDNYIEIKDRSKDVIISGGENISSVEVENVVYHHPAVLEASVVARPDE 491
Cdd:cd12116 333 GRPALTAERFvpdpfagPGSrLYRTGDLVRRRADGRLEYLGRADGQVKIRGHRIELGEIEAALAAHPGVAQAAVVVREDG 412
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*....
gi 15228909 492 RWQESpCAFVTLksdyeKHDQNKLAQDIMKFCREKLPAYWVPKSVVFGP-LPKTATGKI 549
Cdd:cd12116 413 GDRRL-VAYVVL-----KAGAAPDAAALRAHLRATLPAYMVPSAFVRLDaLPLTANGKL 465
|
|
| FATP_chFAT1_like |
cd05937 |
Uncharacterized subfamily of bifunctional fatty acid transporter/very-long-chain acyl-CoA ... |
44-557 |
1.83e-21 |
|
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: 97.50 E-value: 1.83e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228909 44 GSREYTWRQTYDRCRRLASALAD-RSIGPGSTVAIIAPNIPAMYEAHFGVPMCGAVLNCVNIRLNAPTvaflLSHSqssv 122
Cdd:cd05937 2 EGKTWTYSETYDLVLRYAHWLHDdLGVQAGDFVAIDLTNSPEFVFLWLGLWSIGAAPAFINYNLSGDP----LIHC---- 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228909 123 imvdqefftlaedsLRLMEEKagssfkrpLLIVigdhtcapeslnralskgaieyedflatgDPNYPwqppadewqsIAL 202
Cdd:cd05937 74 --------------LKLSGSR--------FVIV-----------------------------DPDDP----------AIL 92
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228909 203 GYTSGTTASPKGVVLHHRGAYIMALSNPLIWGMQDGAVYLWTLPMFHCNGWCFPWSLAVLSGTSICL-RQVTAKEVYSMI 281
Cdd:cd05937 93 IYTSGTTGLPKAAAISWRRTLVTSNLLSHDLNLKNGDRTYTCMPLYHGTAAFLGACNCLMSGGTLALsRKFSASQFWKDV 172
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228909 282 AKYKVTHFCAAPVVLNAIVNAPKEdtILPLPHTVHVMTAGAAPPPsvLFSMNQKGFRV-------AHTYGLSETY----G 350
Cdd:cd05937 173 RDSGATIIQYVGELCRYLLSTPPS--PYDRDHKVRVAWGNGLRPD--IWERFRERFNVpeigefyAATEGVFALTnhnvG 248
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228909 351 PSTVCA---------WKPEWDSLPpetqaklnarqgVRYTGMEQLDVIDTQTGKPVPADGKTAGEIVFRGNMVMK----G 417
Cdd:cd05937 249 DFGAGAighhglirrWKFENQVVL------------VKMDPETDDPIRDPKTGFCVRAPVGEPGEMLGRVPFKNReafqG 316
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228909 418 YLKNPEANK-----ETFAGG--WFHSGDIAVKHPDNYIEIKDRSKDVIISGGENISSVEVENVVYHHPAVLEASV----V 486
Cdd:cd05937 317 YLHNEDATEsklvrDVFRKGdiYFRTGDLLRQDADGRWYFLDRLGDTFRWKSENVSTTEVADVLGAHPDIAEANVygvkV 396
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 15228909 487 ARPDERwqeSPCAFVTLK-SDYEKHDQNKLAQDimKFCREKLPAYWVPKSVVFGP-LPKTATGKIQKHILRTK 557
Cdd:cd05937 397 PGHDGR---AGCAAITLEeSSAVPTEFTKSLLA--SLARKNLPSYAVPLFLRLTEeVATTDNHKQQKGVLRDE 464
|
|
| PLN02861 |
PLN02861 |
long-chain-fatty-acid-CoA ligase |
10-480 |
3.06e-21 |
|
long-chain-fatty-acid-CoA ligase
Pssm-ID: 178452 [Multi-domain] Cd Length: 660 Bit Score: 97.99 E-value: 3.06e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228909 10 DDLPKIPANYtaLTPLWFLDRAAVVHPT-----RKSVIHGSR-EYTW---RQTYDRCRRLASALADRSIGPGSTVAIIAP 80
Cdd:PLN02861 33 DGLLDLPADI--DSPWQFFSDAVKKYPNnqmlgRRQVTDSKVgPYVWltyKEVYDAAIRIGSAIRSRGVNPGDRCGIYGS 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228909 81 NIPAMYEAHFGVPMCGAVLNCVNIRLNAPTVAFLLSHSQSSVIMVDQEFFTlaedSLRLMEEKAGSSFKRplLIVIGDHT 160
Cdd:PLN02861 111 NCPEWIIAMEACNSQGITYVPLYDTLGANAVEFIINHAEVSIAFVQESKIS----SILSCLPKCSSNLKT--IVSFGDVS 184
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228909 161 CAPESLNRALSKGAIEYEDFLATGDPNYPWqPPADEWQSIALGYTSGTTASPKGVVLHHRGAYIMALSNPLIWGMQDGAV 240
Cdd:PLN02861 185 SEQKEEAEELGVSCFSWEEFSLMGSLDCEL-PPKQKTDICTIMYTSGTTGEPKGVILTNRAIIAEVLSTDHLLKVTDRVA 263
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228909 241 -----YLWTLPMFHC-----NGWCfpwslaVLSGTSICLRQVTAKEVYSMIAKYKVTHFCAAPVVLNAIVN--------- 301
Cdd:PLN02861 264 teedsYFSYLPLAHVydqviETYC------ISKGASIGFWQGDIRYLMEDVQALKPTIFCGVPRVYDRIYTgimqkissg 337
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228909 302 ----------------------------APKEDTIL------PLPHTVHVMTAGAAPPPSVLfsmnQKGFRVAHTYGLSE 347
Cdd:PLN02861 338 gmlrkklfdfaynyklgnlrkglkqeeaSPRLDRLVfdkikeGLGGRVRLLLSGAAPLPRHV----EEFLRVTSCSVLSQ 413
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228909 348 TYGPSTVCAwkPEWDSLPPETQakLNARQGVRYTGME-QLDvidtqtgkPVPADGKTA------GEIVFRGNMVMKGYLK 420
Cdd:PLN02861 414 GYGLTESCG--GCFTSIANVFS--MVGTVGVPMTTIEaRLE--------SVPEMGYDAlsdvprGEICLRGNTLFSGYHK 481
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 15228909 421 NPEANKETFAGGWFHSGDIAVKHPDNYIEIKDRSKDVI-ISGGENISSVEVENVVYHHPAV 480
Cdd:PLN02861 482 RQDLTEEVLIDGWFHTGDIGEWQPNGAMKIIDRKKNIFkLSQGEYVAVENLENTYSRCPLI 542
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
36-554 |
1.38e-20 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 96.95 E-value: 1.38e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228909 36 PTRKSVIHGSREYTWRQTYDRCRRLASALADRSIGPGSTVAIIAPNIPAMYEAHFGVPMCGAVLNCVNIRLNAPTVAFLL 115
Cdd:PRK12316 2017 PEAIAVVFGDQHLSYAELDSRANRLAHRLRARGVGPEVRVAIAAERSFELVVALLAVLKAGGAYVPLDPNYPAERLAYML 2096
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228909 116 SHSQSSVIMVDQeffTLAEDslrlmeekagssfkrpLLIvigdhtcaPESLNRALSKGAIEYEDFlATGDPnypwQPPAD 195
Cdd:PRK12316 2097 EDSGAALLLTQR---HLLER----------------LPL--------PAGVARLPLDRDAEWADY-PDTAP----AVQLA 2144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228909 196 EWQSIALGYTSGTTASPKGVVLHHrgayiMALSNPLIW-----GMQDGAVYLWTLPmFHCNGWCFPWSLAVLSGTSICLR 270
Cdd:PRK12316 2145 GENLAYVIYTSGSTGLPKGVAVSH-----GALVAHCQAageryELSPADCELQFMS-FSFDGAHEQWFHPLLNGARVLIR 2218
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228909 271 ---QVTAKEVYSMIAKYKVTHFCAAPVVLNAIVNAPKEDTILPLPHTVHVmtAGAAPPpsvlfsmnQKGFRVAH----TY 343
Cdd:PRK12316 2219 ddeLWDPEQLYDEMERHGVTILDFPPVYLQQLAEHAERDGRPPAVRVYCF--GGEAVP--------AASLRLAWealrPV 2288
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228909 344 GLSETYGPS----TVCAWKPEWDSLPPETQAKLNARQGVRytgmeQLDVIDTQTgKPVPADGktAGEIVFRGNMVMKGYL 419
Cdd:PRK12316 2289 YLFNGYGPTeavvTPLLWKCRPQDPCGAAYVPIGRALGNR-----RAYILDADL-NLLAPGM--AGELYLGGEGLARGYL 2360
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228909 420 KNPEANKETF--------AGGWFHSGDIAVKHPDNYIEIKDRSKDVIISGGENISSVEVENVVYHHPAVLEASVVArpde 491
Cdd:PRK12316 2361 NRPGLTAERFvpdpfsasGERLYRTGDLARYRADGVVEYLGRIDHQVKIRGFRIELGEIEARLQAHPAVREAVVVA---- 2436
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 15228909 492 rwQESP-----CAFVTLKSdyekhDQNKLAQDIMKFCREKLPAYWVPKSVVF-GPLPKTATGKIQKHIL 554
Cdd:PRK12316 2437 --QDGAsgkqlVAYVVPDD-----AAEDLLAELRAWLAARLPAYMVPAHWVVlERLPLNPNGKLDRKAL 2498
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
36-554 |
3.82e-20 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 95.41 E-value: 3.82e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228909 36 PTRKSVIHGSREYTWRQTYDRCRRLASALADRSIGPGSTVAIIAPNIPAMYEAHFGVPMCGAVLNCVNIRLNAPTVAFLL 115
Cdd:PRK12316 525 PEAPALAFGEETLDYAELNRRANRLAHALIERGVGPDVLVGVAMERSIEMVVALLAILKAGGAYVPLDPEYPAERLAYML 604
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228909 116 SHSQSSVIMVDQefftlaedslRLMEekagssfKRPLlivigdhtcAPESLNRALSKGAIEYEdflatgdpNYPWQPPAD 195
Cdd:PRK12316 605 EDSGVQLLLSQS----------HLGR-------KLPL---------AAGVQVLDLDRPAAWLE--------GYSEENPGT 650
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228909 196 EWQSIALGY---TSGTTASPKGVVLHHRgayimALSNPLIW-----GMQDGAVYLWTLPM-FHCNGWCFPWSLAvlSGTS 266
Cdd:PRK12316 651 ELNPENLAYviyTSGSTGKPKGAGNRHR-----ALSNRLCWmqqayGLGVGDTVLQKTPFsFDVSVWEFFWPLM--SGAR 723
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228909 267 ICL----RQVTAKEVYSMIAKYKVTHFCAAPVVLNAIVNAPKEDTILPLPHTVhvmTAGAAPPPSVLFSMNQKgFRVAHT 342
Cdd:PRK12316 724 LVVaapgDHRDPAKLVELINREGVDTLHFVPSMLQAFLQDEDVASCTSLRRIV---CSGEALPADAQEQVFAK-LPQAGL 799
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228909 343 YGLsetYGPS------TVCAWKPEWDSLPPETQAKLNarqgvryTGMEQLDVidtqTGKPVPAdgKTAGEIVFRGNMVMK 416
Cdd:PRK12316 800 YNL---YGPTeaaidvTHWTCVEEGGDSVPIGRPIAN-------LACYILDA----NLEPVPV--GVLGELYLAGRGLAR 863
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228909 417 GYLKNPEANKETFAGGWF-------HSGDIAVKHPDNYIEIKDRSKDVIISGGENISSVEVENVVYHHPAVLEASVVARp 489
Cdd:PRK12316 864 GYHGRPGLTAERFVPSPFvagermyRTGDLARYRADGVIEYAGRIDHQVKLRGLRIELGEIEARLLEHPWVREAAVLAV- 942
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 15228909 490 dERWQesPCAFVTLKSdyekhDQNKLAQDIMKFCREKLPAYWVPKSVVF-GPLPKTATGKIQKHIL 554
Cdd:PRK12316 943 -DGKQ--LVGYVVLES-----EGGDWREALKAHLAASLPEYMVPAQWLAlERLPLTPNGKLDRKAL 1000
|
|
| A_NRPS_ApnA-like |
cd17644 |
similar to adenylation domain of anabaenopeptin synthetase (ApnA); This family of the ... |
204-554 |
1.77e-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: 91.34 E-value: 1.77e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228909 204 YTSGTTASPKGVVLHHRgayimALSNpLIWGMQdgAVYLWTLPMFHCNGWCFPWSLAV-------LSGTSICLR--QV-- 272
Cdd:cd17644 113 YTSGSTGKPKGVMIEHQ-----SLVN-LSHGLI--KEYGITSSDRVLQFASIAFDVAAeeiyvtlLSGATLVLRpeEMrs 184
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228909 273 TAKEVYSMIAKYKVTHFCAAPVVLNAIVNAPKEDTIlPLPHTVH-VMTAGAAPPPS---VLFSMNQKGFRVAHTYGLSET 348
Cdd:cd17644 185 SLEDFVQYIQQWQLTVLSLPPAYWHLLVLELLLSTI-DLPSSLRlVIVGGEAVQPElvrQWQKNVGNFIQLINVYGPTEA 263
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228909 349 YGPSTVCawkpewDSLPPETQAKLNARQGvRYTGMEQLDVIDtQTGKPVPADgkTAGEIVFRGNMVMKGYLKNPEANKET 428
Cdd:cd17644 264 TIAATVC------RLTQLTERNITSVPIG-RPIANTQVYILD-ENLQPVPVG--VPGELHIGGVGLARGYLNRPELTAEK 333
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228909 429 FAGGWFHS---------GDIAVKHPDNYIEIKDRSKDVIISGGENISSVEVENVVYHHPAVLEASVVARPDERWQESPCA 499
Cdd:cd17644 334 FISHPFNSseserlyktGDLARYLPDGNIEYLGRIDNQVKIRGFRIELGEIEAVLSQHNDVKTAVVIVREDQPGNKRLVA 413
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*.
gi 15228909 500 FVTLKSDyEKHDQNKLAQdimkFCREKLPAYWVPKS-VVFGPLPKTATGKIQKHIL 554
Cdd:cd17644 414 YIVPHYE-ESPSTVELRQ----FLKAKLPDYMIPSAfVVLEELPLTPNGKIDRRAL 464
|
|
| PRK12467 |
PRK12467 |
peptide synthase; Provisional |
7-554 |
2.44e-19 |
|
peptide synthase; Provisional
Pssm-ID: 237108 [Multi-domain] Cd Length: 3956 Bit Score: 92.92 E-value: 2.44e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228909 7 RDIDDLPKIPANYTALTPLWFLDRAAVVHPTRKSVIHGSREYTWRQTYDRCRRLASALADRSIGPGSTVAIIAPNIPAMY 86
Cdd:PRK12467 497 RELVRWNAPATEYAPDCVHQLIEAQARQHPERPALVFGEQVLSYAELNRQANRLAHVLIAAGVGPDVLVGIAVERSIEMV 576
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228909 87 EAHFGVPMCGAvlncvnirlnaptvAFLlshsqssviMVDQEFftlAEDSLRLMEEKAGSSFkrplliVIGDhtcaPESL 166
Cdd:PRK12467 577 VGLLAVLKAGG--------------AYV---------PLDPEY---PQDRLAYMLDDSGVRL------LLTQ----SHLL 620
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228909 167 NRALSKGAIEYedfLATGDPNYPWQPPADEWQSIALG--------YTSGTTASPKGVVLHHRgayimALSNPLIWGMQ-- 236
Cdd:PRK12467 621 AQLPVPAGLRS---LCLDEPADLLCGYSGHNPEVALDpdnlayviYTSGSTGQPKGVAISHG-----ALANYVCVIAErl 692
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228909 237 ----DGAVYLWTLPMFHCNGWCFPWSLAvlSGTSICL--RQVT--AKEVYSMIAKYKVTHFCAAPVVLNAIVNAPKEDTI 308
Cdd:PRK12467 693 qlaaDDSMLMVSTFAFDLGVTELFGALA--SGATLHLlpPDCArdAEAFAALMADQGVTVLKIVPSHLQALLQASRVALP 770
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228909 309 LPLpHTVHVmtAGAAPPPSVLfsmnQKGFRVAHTYGLSETYGPSTVCAWKPEWDsLPPETQAKLNARQGVRYTGMeQLDV 388
Cdd:PRK12467 771 RPQ-RALVC--GGEALQVDLL----ARVRALGPGARLINHYGPTETTVGVSTYE-LSDEERDFGNVPIGQPLANL-GLYI 841
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228909 389 IDTQTgKPVPadGKTAGEIVFRGNMVMKGYLKNPEANKETF-------AGG-WFHSGDIAVKHPDNYIEIKDRSKDVIIS 460
Cdd:PRK12467 842 LDHYL-NPVP--VGVVGELYIGGAGLARGYHRRPALTAERFvpdpfgaDGGrLYRTGDLARYRADGVIEYLGRMDHQVKI 918
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228909 461 GGENISSVEVENVVYHHPAVLEASVVARPDERWQESpCAFVTLKSDYEKHDQNKLAQDIMKFCREKLPAYWVPKSVVF-G 539
Cdd:PRK12467 919 RGFRIELGEIEARLLAQPGVREAVVLAQPGDAGLQL-VAYLVPAAVADGAEHQATRDELKAQLRQVLPDYMVPAHLLLlD 997
|
570
....*....|....*
gi 15228909 540 PLPKTATGKIQKHIL 554
Cdd:PRK12467 998 SLPLTPNGKLDRKAL 1012
|
|
| PRK09029 |
PRK09029 |
O-succinylbenzoic acid--CoA ligase; Provisional |
32-544 |
2.65e-19 |
|
O-succinylbenzoic acid--CoA ligase; Provisional
Pssm-ID: 236363 [Multi-domain] Cd Length: 458 Bit Score: 90.70 E-value: 2.65e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228909 32 AVVHPTRKSVIHGSREYTWRQTYDRCRRLASALADRSIGPGSTVAIIAPNIPAMYEAHFGVPMCGAVLNCVNIRLNAPTV 111
Cdd:PRK09029 13 AQVRPQAIALRLNDEVLTWQQLCARIDQLAAGFAQQGVVEGSGVALRGKNSPETLLAYLALLQCGARVLPLNPQLPQPLL 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228909 112 AFLLSHSQSSVIMVDQEFFTLAEDSLRLMEEKAGSsfkrpllivigdhtcapeslnralskgaieyedflatgdPNYPWQ 191
Cdd:PRK09029 93 EELLPSLTLDFALVLEGENTFSALTSLHLQLVEGA---------------------------------------HAVAWQ 133
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228909 192 PpadewQSIA-LGYTSGTTASPKGVVLHHRGAYIMA--LSNPLIWGMQDGavYLWTLPMFHCNG----WcfPWslaVLSG 264
Cdd:PRK09029 134 P-----QRLAtMTLTSGSTGLPKAAVHTAQAHLASAegVLSLMPFTAQDS--WLLSLPLFHVSGqgivW--RW---LYAG 201
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228909 265 TSICLRqvTAKEVYSMIAKykVTHFCAAPVVLNAIVNAPKEDTILPlphtvHVMTAGAAPPPSVLFSMNQKGFRVAHTYG 344
Cdd:PRK09029 202 ATLVVR--DKQPLEQALAG--CTHASLVPTQLWRLLDNRSEPLSLK-----AVLLGGAAIPVELTEQAEQQGIRCWCGYG 272
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228909 345 LSETygPSTVCAwKpEWDSLPpetqaklnarqGVrytgmeqldvidtqtGKPVPadGK----TAGEIVFRGNMVMKGYLK 420
Cdd:PRK09029 273 LTEM--ASTVCA-K-RADGLA-----------GV---------------GSPLP--GRevklVDGEIWLRGASLALGYWR 320
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228909 421 N----PEANKEtfagGWFHSGDIAVKHpDNYIEIKDRSKDVIISGGENISSVEVENVVYHHPAVLEASVVARPDERWQES 496
Cdd:PRK09029 321 QgqlvPLVNDE----GWFATRDRGEWQ-NGELTILGRLDNLFFSGGEGIQPEEIERVINQHPLVQQVFVVPVADAEFGQR 395
|
490 500 510 520
....*....|....*....|....*....|....*....|....*...
gi 15228909 497 PCAFVTLKSdyeKHDQNKLAQdimkFCREKLPAYWVPksVVFGPLPKT 544
Cdd:PRK09029 396 PVAVVESDS---EAAVVNLAE----WLQDKLARFQQP--VAYYLLPPE 434
|
|
| PRK07768 |
PRK07768 |
long-chain-fatty-acid--CoA ligase; Validated |
43-561 |
8.25e-19 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236091 [Multi-domain] Cd Length: 545 Bit Score: 89.67 E-value: 8.25e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228909 43 HGSREYTWRQTYDRCRRLASALADRSIGPGSTVAIIAPNIPAMYEAHFGVPMCGAVLNCvnirLNAPTvafllshSQSSV 122
Cdd:PRK07768 25 DAPVRHTWGEVHERARRIAGGLAAAGVGPGDAVAVLAGAPVEIAPTAQGLWMRGASLTM----LHQPT-------PRTDL 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228909 123 ImvdqeffTLAEDSLR---LMEEKAgssfkrpllIVIGDhtcaP-ESLNRALSKGAIEYE--DFLATGDPNYPwqPPADE 196
Cdd:PRK07768 94 A-------VWAEDTLRvigMIGAKA---------VVVGE----PfLAAAPVLEEKGIRVLtvADLLAADPIDP--VETGE 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228909 197 wQSIAL-GYTSGTTASPKGVVLHHRGAY-----------------IMALSNPLIWGMqdGAVYLWTLPMFHCNGWCFPWS 258
Cdd:PRK07768 152 -DDLALmQLTSGSTGSPKAVQITHGNLYanaeamfvaaefdvetdVMVSWLPLFHDM--GMVGFLTVPMYFGAELVKVTP 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228909 259 LAVLSGTSICLRqvtakevysMIAKYKVThFCAAP----VVLNAIVNAPKEDTILPLPhTVHVMTAGAAP-PPSVLFSMN 333
Cdd:PRK07768 229 MDFLRDPLLWAE---------LISKYRGT-MTAAPnfayALLARRLRRQAKPGAFDLS-SLRFALNGAEPiDPADVEDLL 297
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228909 334 QKGFR-------VAHTYGLSET-----YGP-------STVCAwkpewDSLPPETQA----KLNARQGVRY----TGMEqL 386
Cdd:PRK07768 298 DAGARfglrpeaILPAYGMAEAtlavsFSPcgaglvvDEVDA-----DLLAALRRAvpatKGNTRRLATLgpplPGLE-V 371
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228909 387 DVIDtQTGKPVPADGktAGEIVFRGNMVMKGYLK--NPEANKEtfAGGWFHSGDIAVKHPDNYIEIKDRSKDVIISGGEN 464
Cdd:PRK07768 372 RVVD-EDGQVLPPRG--VGVIELRGESVTPGYLTmdGFIPAQD--ADGWLDTGDLGYLTEEGEVVVCGRVKDVIIMAGRN 446
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228909 465 ISSVEVENVVYHHPAVLEASVVA----RPDERwqESPCAFVTLKSDYEKHDQNKLAQDIMKFCREKLPAYwvPKSVVF-- 538
Cdd:PRK07768 447 IYPTDIERAAARVEGVRPGNAVAvrldAGHSR--EGFAVAVESNAFEDPAEVRRIRHQVAHEVVAEVGVR--PRNVVVlg 522
|
570 580
....*....|....*....|....
gi 15228909 539 -GPLPKTATGKIQkhilRTKAKEM 561
Cdd:PRK07768 523 pGSIPKTPSGKLR----RANAAEL 542
|
|
| AACS |
cd05943 |
Acetoacetyl-CoA synthetase (acetoacetate-CoA ligase, AACS); AACS is a cytosolic ligase that ... |
29-550 |
7.19e-18 |
|
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: 86.94 E-value: 7.19e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228909 29 DRAAVVHPTRKSVihgsREYTWRQTYDRCRRLASALADRSIGPGSTVAIIAPNIPAMYEAHFGVPMCGAVLNCVNIRLNA 108
Cdd:cd05943 84 DPAAIYAAEDGER----TEVTWAELRRRVARLAAALRALGVKPGDRVAGYLPNIPEAVVAMLATASIGAIWSSCSPDFGV 159
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228909 109 PTVAFLLSHSQSSVIMVDQEFF----------TLAE--DSLRLMEEkagssfkrpllIVIGDHTCAPESLNRALSKGAIE 176
Cdd:cd05943 160 PGVLDRFGQIEPKVLFAVDAYTyngkrhdvreKVAElvKGLPSLLA-----------VVVVPYTVAAGQPDLSKIAKALT 228
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228909 177 YEDFLATGD--PNYPWQPPADewQSIALGYTSGTTASPKGVVLHHRGAYIMALSNPLI-WGMQDGAVYLWtlpmFHCNGW 253
Cdd:cd05943 229 LEDFLATGAagELEFEPLPFD--HPLYILYSSGTTGLPKCIVHGAGGTLLQHLKEHILhCDLRPGDRLFY----YTTCGW 302
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228909 254 CFpWSL---AVLSGTSICLRQ-----VTAKEVYSMIAKYKVTHFCAAPVVLNAIVNAPKEdtilplPHTVH-------VM 318
Cdd:cd05943 303 MM-WNWlvsGLAVGATIVLYDgspfyPDTNALWDLADEEGITVFGTSAKYLDALEKAGLK------PAETHdlsslrtIL 375
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228909 319 TAGAAPPPSvlfsmnqkGFRVAHTYG-----LSETYGPSTVCAW-------KPEWdslPPETQAklnarqgvRYTGMEQl 386
Cdd:cd05943 376 STGSPLKPE--------SFDYVYDHIkpdvlLASISGGTDIISCfvggnplLPVY---RGEIQC--------RGLGMAV- 435
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228909 387 DVIDTQtGKPVPADgktAGEIVFRGNM-VMKGYLKNPEANK-------ETFAGGWFHsGDIAVKHPDNYIEIKDRSKDVI 458
Cdd:cd05943 436 EAFDEE-GKPVWGE---KGELVCTKPFpSMPVGFWNDPDGSryraayfAKYPGVWAH-GDWIEITPRGGVVILGRSDGTL 510
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228909 459 ISGGENISSVEVENVVYHHPAVLEASVVARPDERWQESPCAFVTLKSDYEKHDQnkLAQDIMKFCREKLPAYWVPKSVVF 538
Cdd:cd05943 511 NPGGVRIGTAEIYRVVEKIPEVEDSLVVGQEWKDGDERVILFVKLREGVELDDE--LRKRIRSTIRSALSPRHVPAKIIA 588
|
570
....*....|...
gi 15228909 539 GP-LPKTATGKIQ 550
Cdd:cd05943 589 VPdIPRTLSGKKV 601
|
|
| PRK12467 |
PRK12467 |
peptide synthase; Provisional |
204-554 |
9.95e-18 |
|
peptide synthase; Provisional
Pssm-ID: 237108 [Multi-domain] Cd Length: 3956 Bit Score: 87.52 E-value: 9.95e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228909 204 YTSGTTASPKGVVLHHRgayimALSNPLIWGMQ------DGAVYLWTLPMFHCNGWCFPWSLavLSGTSICLR---QVTA 274
Cdd:PRK12467 3244 YTSGSTGKPKGVGVRHG-----ALANHLCWIAEayeldaNDRVLLFMSFSFDGAQERFLWTL--ICGGCLVVRdndLWDP 3316
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228909 275 KEVYSMIAKYKVTHFCAAPVVLNAIVNAPKEDTILPLPHTVhvmTAGAAPPPSVLfsmnQKGFRVAHTYGLSETYGPS-- 352
Cdd:PRK12467 3317 EELWQAIHAHRISIACFPPAYLQQFAEDAGGADCASLDIYV---FGGEAVPPAAF----EQVKRKLKPRGLTNGYGPTea 3389
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228909 353 --TVCAWKPEWDSLPPETQAKLNARQGVRytgmeQLDVIDTQtGKPVPADgkTAGEIVFRGNMVMKGYLKNPEANKETF- 429
Cdd:PRK12467 3390 vvTVTLWKCGGDAVCEAPYAPIGRPVAGR-----SIYVLDGQ-LNPVPVG--VAGELYIGGVGLARGYHQRPSLTAERFv 3461
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228909 430 ------AGG-WFHSGDIAVKHPDNYIEIKDRSKDVIISGGENISSVEVENVVYHHPAVLEASVVARPDERWQESpCAFVT 502
Cdd:PRK12467 3462 adpfsgSGGrLYRTGDLARYRADGVIEYLGRIDHQVKIRGFRIELGEIEARLLQHPSVREAVVLARDGAGGKQL-VAYVV 3540
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|...
gi 15228909 503 LKSdyekhDQNKLAQDIMKFCREKLPAYWVPKSVVFGP-LPKTATGKIQKHIL 554
Cdd:PRK12467 3541 PAD-----PQGDWRETLRDHLAASLPDYMVPAQLLVLAaMPLGPNGKVDRKAL 3588
|
|
| PRK07445 |
PRK07445 |
O-succinylbenzoic acid--CoA ligase; Reviewed |
317-558 |
1.27e-17 |
|
O-succinylbenzoic acid--CoA ligase; Reviewed
Pssm-ID: 236019 [Multi-domain] Cd Length: 452 Bit Score: 85.43 E-value: 1.27e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228909 317 VMTAGAAPPPSVLFSMNQKGFRVAHTYGLSETygPSTVCAWKPEwDSLppetqaklnarQGVRYTGM----EQLDVIDTQ 392
Cdd:PRK07445 235 ILLGGAPAWPSLLEQARQLQLRLAPTYGMTET--ASQIATLKPD-DFL-----------AGNNSSGQvlphAQITIPANQ 300
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228909 393 TGKpvpadgktageIVFRGNMVMKGYLKNPEANKetfagGWFHSGDIAVKHPDNYIEIKDRSKDVIISGGENISSVEVEN 472
Cdd:PRK07445 301 TGN-----------ITIQAQSLALGYYPQILDSQ-----GIFETDDLGYLDAQGYLHILGRNSQKIITGGENVYPAEVEA 364
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228909 473 VVYHHPAVLEASVVARPDERWQESPCAFVTLK--SDYEKHDQNKLAQDIMKFcreKLPAYWVPKSvvfgPLPKTATGKIQ 550
Cdd:PRK07445 365 AILATGLVQDVCVLGLPDPHWGEVVTAIYVPKdpSISLEELKTAIKDQLSPF---KQPKHWIPVP----QLPRNPQGKIN 437
|
....*...
gi 15228909 551 KHILRTKA 558
Cdd:PRK07445 438 RQQLQQIA 445
|
|
| A_NRPS_GliP_like |
cd17653 |
nonribosomal peptide synthase GliP-like; This family includes the adenylation (A) domain of ... |
204-555 |
1.47e-17 |
|
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: 85.05 E-value: 1.47e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228909 204 YTSGTTASPKGVVLHHRGayimaLSNpLIWGMQDGavyLWTLP------MFHCNGWCFPWSL--AVLSGTSICLRqvTAK 275
Cdd:cd17653 112 FTSGSTGIPKGVMVPHRG-----VLN-YVSQPPAR---LDVGPgsrvaqVLSIAFDACIGEIfsTLCNGGTLVLA--DPS 180
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228909 276 EVYSMIAKyKVTHFCAAPVVLNAIvnapkEDTILPlphTVHVMTAGAAPPPSVLFSMNQKGFRVAHTYGLSETygpsTVC 355
Cdd:cd17653 181 DPFAHVAR-TVDALMSTPSILSTL-----SPQDFP---NLKTIFLGGEAVPPSLLDRWSPGRRLYNAYGPTEC----TIS 247
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228909 356 AWKPEwdsLPPETQAKLnaRQGVRYTGMEQLDViDTQtgkPVPADGKtaGEIVFRGNMVMKGYLKNPEANKETFAGGWFH 435
Cdd:cd17653 248 STMTE---LLPGQPVTI--GKPIPNSTCYILDA-DLQ---PVPEGVV--GEICISGVQVARGYLGNPALTASKFVPDPFW 316
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228909 436 -------SGDIAVKHPDNYIEIKDRSKDVIISGGENISSVEVENVVYHHPAVLE---ASVVarpderwQESPCAFVT-LK 504
Cdd:cd17653 317 pgsrmyrTGDYGRWTEDGGLEFLGREDNQVKVRGFRINLEEIEEVVLQSQPEVTqaaAIVV-------NGRLVAFVTpET 389
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|..
gi 15228909 505 SDYEkhdqnklaqDIMKFCREKLPAYWVPKSVV-FGPLPKTATGKIQKHILR 555
Cdd:cd17653 390 VDVD---------GLRSELAKHLPSYAVPDRIIaLDSFPLTANGKVDRKALR 432
|
|
| A_NRPS_ProA |
cd17656 |
gramicidin S synthase 2, also known as ATP-dependent proline adenylase; This family of the ... |
36-554 |
3.83e-17 |
|
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: 84.45 E-value: 3.83e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228909 36 PTRKSVIHGSREYTWRQTYDRCRRLASALADRSIGPGSTVAIIAPNIPAMYEAHFGVPMCGAVLNCVNIRLNAPTVAFLL 115
Cdd:cd17656 2 PDAVAVVFENQKLTYRELNERSNQLARFLREKGVKKDSIVAIMMERSAEMIVGILGILKAGGAFVPIDPEYPEERRIYIM 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228909 116 SHSQSSVIMvdqefftlaedslrlmeekagssfkrpllivigdhTCA--PESLNRALSKGAIEYEDFLATGDPNYPWQPP 193
Cdd:cd17656 82 LDSGVRVVL-----------------------------------TQRhlKSKLSFNKSTILLEDPSISQEDTSNIDYINN 126
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228909 194 ADEWQSIAlgYTSGTTASPKGVVLHHRG-AYIMALSNPLIWGMQDGAVYLWTLPMFHC------NGWCFPWSLAVLSGTS 266
Cdd:cd17656 127 SDDLLYII--YTSGTTGKPKGVQLEHKNmVNLLHFEREKTNINFSDKVLQFATCSFDVcyqeifSTLLSGGTLYIIREET 204
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228909 267 iclrQVTAKEVYSMIAKYKvTHFCAAPVVLNAIVNAPKEdTILPLPHTV-HVMTAGAAPPPSVLFS--MNQKGFRVAHTY 343
Cdd:cd17656 205 ----KRDVEQLFDLVKRHN-IEVVFLPVAFLKFIFSERE-FINRFPTCVkHIITAGEQLVITNEFKemLHEHNVHLHNHY 278
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228909 344 GLSETYGPSTvCAWKPE--WDSLPPETQAKLNarqgvryTGMEQLDvidtQTGKPVPADgkTAGEIVFRGNMVMKGYLKN 421
Cdd:cd17656 279 GPSETHVVTT-YTINPEaeIPELPPIGKPISN-------TWIYILD----QEQQLQPQG--IVGELYISGASVARGYLNR 344
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228909 422 PEANKETFAGGWFHS-------GDIAVKHPDNYIEIKDRSKDVIISGGENISSVEVENVVYHHPAVLEASVVARPDERWQ 494
Cdd:cd17656 345 QELTAEKFFPDPFDPnermyrtGDLARYLPDGNIEFLGRADHQVKIRGYRIELGEIEAQLLNHPGVSEAVVLDKADDKGE 424
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 15228909 495 ESPCA-FVTLKSDYEKHDQNKLAQDIMKFcreKLPAYWVPksvvFGPLPKTATGKIQKHIL 554
Cdd:cd17656 425 KYLCAyFVMEQELNISQLREYLAKQLPEY---MIPSFFVP----LDQLPLTPNGKVDRKAL 478
|
|
| PLN02736 |
PLN02736 |
long-chain acyl-CoA synthetase |
47-473 |
9.71e-17 |
|
long-chain acyl-CoA synthetase
Pssm-ID: 178337 [Multi-domain] Cd Length: 651 Bit Score: 83.61 E-value: 9.71e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228909 47 EYTWrQTYDRC--RRLA--SALADRSIGPGSTVAIIAPNIP---------AMYeAHFGVPMCGAvlncvnirLNAPTVAF 113
Cdd:PLN02736 75 EYKW-MTYGEAgtARTAigSGLVQHGIPKGACVGLYFINRPewlivdhacSAY-SYVSVPLYDT--------LGPDAVKF 144
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228909 114 LLSHSQ-SSVIMVDQEFFTLaedsLRLMEEKAGSSfkrpLLIVIGDHTCAPESLNRALSKGAIEYEDFLATGDPN-YPWQ 191
Cdd:PLN02736 145 IVNHAEvAAIFCVPQTLNTL----LSCLSEIPSVR----LIVVVGGADEPLPSLPSGTGVEIVTYSKLLAQGRSSpQPFR 216
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228909 192 PPADEwqSIA-LGYTSGTTASPKGVVLHHRGAYIMALSNPLIWGMQDGAVYLWTLPMFH----CNgwcfpWSLAVLSGTS 266
Cdd:PLN02736 217 PPKPE--DVAtICYTSGTTGTPKGVVLTHGNLIANVAGSSLSTKFYPSDVHISYLPLAHiyerVN-----QIVMLHYGVA 289
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228909 267 ICLRQVTAKEVYSMIAKYKVTHFCAAPVVLN----AIVNAPKEDTIL---------------------PLPH-------- 313
Cdd:PLN02736 290 VGFYQGDNLKLMDDLAALRPTIFCSVPRLYNriydGITNAVKESGGLkerlfnaaynakkqalengknPSPMwdrlvfnk 369
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228909 314 -------TVHVMTAGAAP-PPSVL-FSMNQKGFRVAHTYGLSETygpSTVCAWKPEWDSL------P-PETQAKLNARQG 377
Cdd:PLN02736 370 ikaklggRVRFMSSGASPlSPDVMeFLRICFGGRVLEGYGMTET---SCVISGMDEGDNLsghvgsPnPACEVKLVDVPE 446
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228909 378 VRYTGMEQldvidtqtgkPVPAdgktaGEIVFRGNMVMKGYLKNPEANKETF-AGGWFHSGDIAVKHPDNYIEIKDRSKD 456
Cdd:PLN02736 447 MNYTSEDQ----------PYPR-----GEICVRGPIIFKGYYKDEVQTREVIdEDGWLHTGDIGLWLPGGRLKIIDRKKN 511
|
490
....*....|....*...
gi 15228909 457 VI-ISGGENISSVEVENV 473
Cdd:PLN02736 512 IFkLAQGEYIAPEKIENV 529
|
|
| A_NRPS_ACVS-like |
cd17648 |
N-(5-amino-5-carboxypentanoyl)-L-cysteinyl-D-valine synthase; This family contains ACV ... |
204-549 |
1.03e-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: 82.83 E-value: 1.03e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228909 204 YTSGTTASPKGVVLHHRGayIMALSNPLI--WGMQ---DGAVylwtlpMFHCNgWCFPWS-----LAVLSGTSICL---- 269
Cdd:cd17648 101 YTSGTTGKPKGVLVEHGS--VVNLRTSLSerYFGRdngDEAV------LFFSN-YVFDFFveqmtLALLNGQKLVVppde 171
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228909 270 RQVTAKEVYSMIAKYKVTHFCAAPVVLNAIVNAPkedtilpLPHTVHVMTAGAAPPPSVLFSMNQkGF--RVAHTYGLSE 347
Cdd:cd17648 172 MRFDPDRFYAYINREKVTYLSGTPSVLQQYDLAR-------LPHLKRVDAAGEEFTAPVFEKLRS-RFagLIINAYGPTE 243
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228909 348 TygpsTVCAWKPEWdslPPETQAKLNARQGVRYTGMEQLDvidtQTGKPVPADGktAGEIVFRGNMVMKGYLKNPEANKE 427
Cdd:cd17648 244 T----TVTNHKRFF---PGDQRFDKSLGRPVRNTKCYVLN----DAMKRVPVGA--VGELYLGGDGVARGYLNRPELTAE 310
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228909 428 TFAGGWFHS---------------GDIAVKHPDNYIEIKDRSKDVIISGGENISSVEVENVVYHHPAVLEASVVARPDER 492
Cdd:cd17648 311 RFLPNPFQTeqerargrnarlyktGDLVRWLPSGELEYLGRNDFQVKIRGQRIEPGEVEAALASYPGVRECAVVAKEDAS 390
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 15228909 493 WQESP------CAFVTlksdyekhDQNKL-AQDIMKFCREKLPAYWVPKSVV-FGPLPKTATGKI 549
Cdd:cd17648 391 QAQSRiqkylvGYYLP--------EPGHVpESDLLSFLRAKLPRYMVPARLVrLEGIPVTINGKL 447
|
|
| PLN02654 |
PLN02654 |
acetate-CoA ligase |
49-558 |
1.78e-16 |
|
acetate-CoA ligase
Pssm-ID: 215353 [Multi-domain] Cd Length: 666 Bit Score: 82.64 E-value: 1.78e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228909 49 TWRQTYDRCRRLASALADRSIGPGSTVAIIAPNIPAMYEAHFGVPMCGAVLNCVNIRLNAPTVAFLLSHSQSSVIMvdqe 128
Cdd:PLN02654 122 TYSELLDRVCQLANYLKDVGVKKGDAVVIYLPMLMELPIAMLACARIGAVHSVVFAGFSAESLAQRIVDCKPKVVI---- 197
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228909 129 fftlaedslrlmeekAGSSFKR-PLLIVIGDHTCAP--ESLNRALSKGA-IEYEDFLATGDPNYPWQPPADEW------- 197
Cdd:PLN02654 198 ---------------TCNAVKRgPKTINLKDIVDAAldESAKNGVSVGIcLTYENQLAMKREDTKWQEGRDVWwqdvvpn 262
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228909 198 -------------QSIALGYTSGTTASPKGVvLHHRGAYIM--ALSNPLIWGMQDGAVYLWTLPMFHCNGWCFPWSLAVL 262
Cdd:PLN02654 263 yptkcevewvdaeDPLFLLYTSGSTGKPKGV-LHTTGGYMVytATTFKYAFDYKPTDVYWCTADCGWITGHSYVTYGPML 341
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228909 263 SGTSICLRQVT-----AKEVYSMIAKYKVTHFCAAPVVLNAIVNAPKEDTILPLPHTVHVMTAGAAP--PPSVLFSMNQK 335
Cdd:PLN02654 342 NGATVLVFEGApnypdSGRCWDIVDKYKVTIFYTAPTLVRSLMRDGDEYVTRHSRKSLRVLGSVGEPinPSAWRWFFNVV 421
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228909 336 GFR---VAHTYGLSETYG------PStvcAW--KPEWDSLPpetqaklnarqgvrYTGMEQldVIDTQTGKPVpaDGKTA 404
Cdd:PLN02654 422 GDSrcpISDTWWQTETGGfmitplPG---AWpqKPGSATFP--------------FFGVQP--VIVDEKGKEI--EGECS 480
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228909 405 GEIVFRGNMvmKGYLKNPEANKE--------TFAGGWFhSGDIAVKHPDNYIEIKDRSKDVIISGGENISSVEVENVVYH 476
Cdd:PLN02654 481 GYLCVKKSW--PGAFRTLYGDHEryettyfkPFAGYYF-SGDGCSRDKDGYYWLTGRVDDVINVSGHRIGTAEVESALVS 557
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228909 477 HPAVLEASVVARPDERWQESPCAFVTLKSDYEKHDQnkLAQDIMKFCREKLPAYWVPKSVVFGP-LPKTATGKIQKHILR 555
Cdd:PLN02654 558 HPQCAEAAVVGIEHEVKGQGIYAFVTLVEGVPYSEE--LRKSLILTVRNQIGAFAAPDKIHWAPgLPKTRSGKIMRRILR 635
|
...
gi 15228909 556 TKA 558
Cdd:PLN02654 636 KIA 638
|
|
| hsFATP2a_ACSVL_like |
cd05938 |
Fatty acid transport proteins (FATP) including hsFATP2, hsFATP5, and hsFATP6, and similar ... |
48-554 |
2.00e-16 |
|
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: 82.34 E-value: 2.00e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228909 48 YTWRQTYDRCRRLASALAD-RSIGPGSTVAIIAPNIPAMYEAHFGVPMCGAVLNCVNIRLNAPTVAFLLSHSQSSVIMVD 126
Cdd:cd05938 6 YTYRDVDRRSNQAARALLAhAGLRPGDTVALLLGNEPAFLWIWLGLAKLGCPVAFLNTNIRSKSLLHCFRCCGAKVLVVA 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228909 127 QEFFTLAEDSLRLMEEKAGSSFkrplLIVIGDHTCAPESLNRALSKgaieyedflATGDPnypwqPPAD-----EWQSIA 201
Cdd:cd05938 86 PELQEAVEEVLPALRADGVSVW----YLSHTSNTEGVISLLDKVDA---------ASDEP-----VPASlrahvTIKSPA 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228909 202 LG-YTSGTTASPKGVVLHHRGAYIMALSNPLIWGMQDGAVYLwTLPMFHCNGWCFPWSLAVLSGTSICLR-QVTAKEVYS 279
Cdd:cd05938 148 LYiYTSGTTGLPKAARISHLRVLQCSGFLSLCGVTADDVIYI-TLPLYHSSGFLLGIGGCIELGATCVLKpKFSASQFWD 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228909 280 MIAKYKVTHFCAAPVVLNAIVNAPK--EDTIlplpHTVHvMTAGAAPPPSVlFSMNQKGF---RVAHTYGLSETygpstv 354
Cdd:cd05938 227 DCRKHNVTVIQYIGELLRYLCNQPQspNDRD----HKVR-LAIGNGLRADV-WREFLRRFgpiRIREFYGSTEG------ 294
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228909 355 cawkpewdslppeTQAKLNarqgvrYTG--------------MEQLDVI--DTQTGKPV-PADG---KTA-GEIvfrGNM 413
Cdd:cd05938 295 -------------NIGFFN------YTGkigavgrvsylyklLFPFELIkfDVEKEEPVrDAQGfciPVAkGEP---GLL 352
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228909 414 VMK--------GYLKNPEAN-----KETFAGG--WFHSGDIAVKHPDNYIEIKDRSKDVIISGGENISSVEVENVVYHHP 478
Cdd:cd05938 353 VAKitqqspflGYAGDKEQTekkllRDVFKKGdvYFNTGDLLVQDQQNFLYFHDRVGDTFRWKGENVATTEVADVLGLLD 432
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 15228909 479 AVLEASV--VARPDERWQESPCAfVTLKSDYEkHDQNKLAQDIMKFcrekLPAYWVPKSV-VFGPLPKTATGKIQKHIL 554
Cdd:cd05938 433 FLQEVNVygVTVPGHEGRIGMAA-VKLKPGHE-FDGKKLYQHVREY----LPAYARPRFLrIQDSLEITGTFKQQKVRL 505
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
36-554 |
2.01e-15 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 80.39 E-value: 2.01e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228909 36 PTRKSVIHGSREYTWRQTYDRCRRLASALADRSIGPGSTVAIIAPNIPAMYEAHFGVPMCGAVLNCVNIRLNAPTVAFLL 115
Cdd:PRK12316 3071 PDAVALAFGEQRLSYAELNRRANRLAHRLIERGVGPDVLVGVAVERSLEMVVGLLAILKAGGAYVPLDPEYPEERLAYML 3150
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228909 116 SHSQSSVImvdqefftLAEDSLRLmeekAGSSFKRPLLIVIGDHTCAPESLNRALSKGAIEYedflatgdpnypwqppad 195
Cdd:PRK12316 3151 EDSGAQLL--------LSQSHLRL----PLAQGVQVLDLDRGDENYAEANPAIRTMPENLAY------------------ 3200
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228909 196 ewqsiaLGYTSGTTASPKGVVLHHRgayimALSNPLIWGMQ------DGAVYLWTLPMFHCNGWCFPWSLAVlsGTSICL 269
Cdd:PRK12316 3201 ------VIYTSGSTGKPKGVGIRHS-----ALSNHLCWMQQayglgvGDRVLQFTTFSFDVFVEELFWPLMS--GARVVL 3267
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228909 270 RqvtAKEVYSMIAKYKVTHFCAAPVVLNAIVNAPKEDTILPLPHTV----HVMTAGAAPPPSVLFSMNQKGfrvahtyGL 345
Cdd:PRK12316 3268 A---GPEDWRDPALLVELINSEGVDVLHAYPSMLQAFLEEEDAHRCtslkRIVCGGEALPADLQQQVFAGL-------PL 3337
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228909 346 SETYGPSTVCAWKPEWDsLPPETQAKLNARQGVRYTGMEQLDVidtqTGKPVPADgkTAGEIVFRGNMVMKGYLKNPEAN 425
Cdd:PRK12316 3338 YNLYGPTEATITVTHWQ-CVEEGKDAVPIGRPIANRACYILDG----SLEPVPVG--ALGELYLGGEGLARGYHNRPGLT 3410
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228909 426 KETFAGGWF-------HSGDIAVKHPDNYIEIKDRSKDVIISGGENISSVEVENVVYHHPAVLEASVVARPDERWqespC 498
Cdd:PRK12316 3411 AERFVPDPFvpgerlyRTGDLARYRADGVIEYIGRVDHQVKIRGFRIELGEIEARLLEHPWVREAVVLAVDGRQL----V 3486
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*..
gi 15228909 499 AFVTLKSdyekhDQNKLAQDIMKFCREKLPAYWVPKSVVFGP-LPKTATGKIQKHIL 554
Cdd:PRK12316 3487 AYVVPED-----EAGDLREALKAHLKASLPEYMVPAHLLFLErMPLTPNGKLDRKAL 3538
|
|
| PTZ00237 |
PTZ00237 |
acetyl-CoA synthetase; Provisional |
193-554 |
4.19e-15 |
|
acetyl-CoA synthetase; Provisional
Pssm-ID: 240325 [Multi-domain] Cd Length: 647 Bit Score: 78.24 E-value: 4.19e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228909 193 PADEWQSIALGYTSGTTASPKGVVlHHRGAYIMAL--SNPLIWGMQDGAVYLWTlpmfHCNGWC-----FPWSLA----- 260
Cdd:PTZ00237 250 PVESSHPLYILYTSGTTGNSKAVV-RSNGPHLVGLkyYWRSIIEKDIPTVVFSH----SSIGWVsfhgfLYGSLSlgntf 324
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228909 261 VLSGTSICLRQVTAKEVYSMIAKYKVTHFcaapvvlnaivnapkedtiLPLPHTVHVmtagaapppsvLFSMNQKGFRVA 340
Cdd:PTZ00237 325 VMFEGGIIKNKHIEDDLWNTIEKHKVTHT-------------------LTLPKTIRY-----------LIKTDPEATIIR 374
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228909 341 HTYGLSETygPSTVCAWKPEWDSLPPETQAKLNARQGVRY----TGMEQL---DVIDTQ---TGKPVP--------ADGK 402
Cdd:PTZ00237 375 SKYDLSNL--KEIWCGGEVIEESIPEYIENKLKIKSSRGYgqteIGITYLycyGHINIPynaTGVPSIfikpsilsEDGK 452
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228909 403 T-----AGEIVFRGNM---VMKGYLKNPEANKETFAG--GWFHSGDIAVKHPDNYIEIKDRSKDVIISGGENISSVEVEN 472
Cdd:PTZ00237 453 ElnvneIGEVAFKLPMppsFATTFYKNDEKFKQLFSKfpGYYNSGDLGFKDENGYYTIVSRSDDQIKISGNKVQLNTIET 532
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228909 473 VVYHHPAVLEASVVARPDERWQESPCAFVTLKSDYEKH--DQNKLAQDIMKFCREKLPAYWVPKSVVFGP-LPKTATGKI 549
Cdd:PTZ00237 533 SILKHPLVLECCSIGIYDPDCYNVPIGLLVLKQDQSNQsiDLNKLKNEINNIITQDIESLAVLRKIIIVNqLPKTKTGKI 612
|
....*
gi 15228909 550 QKHIL 554
Cdd:PTZ00237 613 PRQII 617
|
|
| PTZ00216 |
PTZ00216 |
acyl-CoA synthetase; Provisional |
49-481 |
4.40e-15 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 240316 [Multi-domain] Cd Length: 700 Bit Score: 78.48 E-value: 4.40e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228909 49 TWRQTYDRCRRLASALADRSIGPGSTVAIiapnipamYE--------AHFGVPMCGAVLNCVNIRLNAPTVAFLLSHSQS 120
Cdd:PTZ00216 123 TYAELWERIVNFGRGLAELGLTKGSNVAI--------YEetrwewlaSIYGIWSQSMVAATVYANLGEDALAYALRETEC 194
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228909 121 SVIMVDQEfftLAEDSLRLMEEKAgssFKRPLLIVIGDhtcAPESLNralSKG--AIEYEDFLATGDP---NYPWQPPAD 195
Cdd:PTZ00216 195 KAIVCNGK---NVPNLLRLMKSGG---MPNTTIIYLDS---LPASVD---TEGcrLVAWTDVVAKGHSagsHHPLNIPEN 262
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228909 196 EWQSIALGYTSGTTASPKGVVLHHRGAY--IMALS---NPLIWGMQDGAVYLWTLPMFHCngwcfpWSLAVLS-----GT 265
Cdd:PTZ00216 263 NDDLALIMYTSGTTGDPKGVMHTHGSLTagILALEdrlNDLIGPPEEDETYCSYLPLAHI------MEFGVTNiflarGA 336
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228909 266 SIC------LRQVTAKEvYSMIAKYKVTHFCAAPVVLNAIVNAPKEDtiLPLPHT------------------------- 314
Cdd:PTZ00216 337 LIGfgsprtLTDTFARP-HGDLTEFRPVFLIGVPRIFDTIKKAVEAK--LPPVGSlkrrvfdhayqsrlralkegkdtpy 413
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228909 315 ----------------VHVMTAGAAP--PP-----SVLFSMnqkgfrVAHTYGLSETYGpstvCAWKPEWDSLPPEtqak 371
Cdd:PTZ00216 414 wnekvfsapravlggrVRAMLSGGGPlsAAtqefvNVVFGM------VIQGWGLTETVC----CGGIQRTGDLEPN---- 479
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228909 372 lNARQGVRYTGMEQLDVID-TQTGKPVPAdgktaGEIVFRGNMVMKGYLKNPEANKETF-AGGWFHSGDIAVKHPDNYIE 449
Cdd:PTZ00216 480 -AVGQLLKGVEMKLLDTEEyKHTDTPEPR-----GEILLRGPFLFKGYYKQEELTREVLdEDGWFHTGDVGSIAANGTLR 553
|
490 500 510
....*....|....*....|....*....|....*.
gi 15228909 450 IKDR----SKDVIisgGENISSVEVENVVYHHPAVL 481
Cdd:PTZ00216 554 IIGRvkalAKNCL---GEYIALEALEALYGQNELVV 586
|
|
| PRK12467 |
PRK12467 |
peptide synthase; Provisional |
16-554 |
1.14e-14 |
|
peptide synthase; Provisional
Pssm-ID: 237108 [Multi-domain] Cd Length: 3956 Bit Score: 77.89 E-value: 1.14e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228909 16 PANYTA--LTPLWFLDRAAVVhPTRKSVIHGSREYTWRQTYDRCRRLASALADRSIGPGSTVAIIAPNIPAMYEAHFGVP 93
Cdd:PRK12467 1567 HTGYPLarLVHQLIEDQAAAT-PEAVALVFGEQELTYGELNRRANRLAHRLIALGVGPEVLVGIAVERSLEMVVGLLAIL 1645
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228909 94 MCGAVLncvnirlnaptvafllshsqssvIMVDQEFftlAEDSLRLMEEKAGSSfkrplLIVIGDHTCA----PESLnRA 169
Cdd:PRK12467 1646 KAGGAY-----------------------VPLDPEY---PRERLAYMIEDSGIE-----LLLTQSHLQArlplPDGL-RS 1693
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228909 170 LSKGAIEyeDFLATGDPNYPWQPPADewQSIA-LGYTSGTTASPKGVVLHHRgayimALSNPLIWgMQ-------DGAVY 241
Cdd:PRK12467 1694 LVLDQED--DWLEGYSDSNPAVNLAP--QNLAyVIYTSGSTGRPKGAGNRHG-----ALVNRLCA-TQeayqlsaADVVL 1763
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228909 242 LWTLPMFHCNGWCFPWSLavLSGTSICLRQVTA----KEVYSMIAKYKVTHFCAAPVVLNAIVNAPKEDTiLPLPHTVHV 317
Cdd:PRK12467 1764 QFTSFAFDVSVWELFWPL--INGARLVIAPPGAhrdpEQLIQLIERQQVTTLHFVPSMLQQLLQMDEQVE-HPLSLRRVV 1840
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228909 318 MTAGAAPPPSVlfsmnQKGFRVAHTYGLSETYGPS----TVCAWKpeWDSLPPETQAKLNARQGVRYTGMEQLDvidtQT 393
Cdd:PRK12467 1841 CGGEALEVEAL-----RPWLERLPDTGLFNLYGPTetavDVTHWT--CRRKDLEGRDSVPIGQPIANLSTYILD----AS 1909
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228909 394 GKPVPAdgKTAGEIVFRGNMVMKGYLKNPEANKETF--------AGGWFHSGDIAVKHPDNYIEIKDRSKDVIISGGENI 465
Cdd:PRK12467 1910 LNPVPI--GVAGELYLGGVGLARGYLNRPALTAERFvadpfgtvGSRLYRTGDLARYRADGVIEYLGRIDHQVKIRGFRI 1987
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228909 466 SSVEVENVVYHHPAVLEASVVARpDERWQESPCAFVTLKSD---YEKHDQNKLAQDIMKFCREKLPAYWVPKSVVF-GPL 541
Cdd:PRK12467 1988 ELGEIEARLREQGGVREAVVIAQ-DGANGKQLVAYVVPTDPglvDDDEAQVALRAILKNHLKASLPEYMVPAHLVFlARM 2066
|
570
....*....|...
gi 15228909 542 PKTATGKIQKHIL 554
Cdd:PRK12467 2067 PLTPNGKLDRKAL 2079
|
|
| PRK06060 |
PRK06060 |
p-hydroxybenzoic acid--AMP ligase FadD22; |
26-558 |
4.29e-14 |
|
p-hydroxybenzoic acid--AMP ligase FadD22;
Pssm-ID: 180374 [Multi-domain] Cd Length: 705 Bit Score: 75.45 E-value: 4.29e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228909 26 WFlDRAAVVHPtrKSVIHGsreytwrQTYDRCRRLASALADRSIGPGSTVAIIAPNIPAMYEAHFGVPMCGAVLNCVNIR 105
Cdd:PRK06060 19 WY-DRPAFYAA--DVVTHG-------QIHDGAARLGEVLRNRGLSSGDRVLLCLPDSPDLVQLLLACLARGVMAFLANPE 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228909 106 LNAPTVAFLLSHSQSSVIMVDQEfftlaedslrLMEEKAGSSFKRPllivigdhtcaPESLNRALSKGAIEYEdfLATGD 185
Cdd:PRK06060 89 LHRDDHALAARNTEPALVVTSDA----------LRDRFQPSRVAEA-----------AELMSEAARVAPGGYE--PMGGD 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228909 186 pnypwqppADEWQSialgYTSGTTASPKGVVLHHRG--AYIMAL-SNPLIWGMQDgaVYLWTLPMFHCNG-----WcFPw 257
Cdd:PRK06060 146 --------ALAYAT----YTSGTTGPPKAAIHRHADplTFVDAMcRKALRLTPED--TGLCSARMYFAYGlgnsvW-FP- 209
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228909 258 sLAVLSGTSICLRQVTAKEVYSMIAKYKVTHFCAAPVVLNAIVNAPKEDTILPLPHtvhVMTAGAAPPPSVLFSMNQ--K 335
Cdd:PRK06060 210 -LATGGSAVINSAPVTPEAAAILSARFGPSVLYGVPNFFARVIDSCSPDSFRSLRC---VVSAGEALELGLAERLMEffG 285
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228909 336 GFRVAHTYGLSE---TYGPSTVCAWKPE--WDSLPPEtqaklnarqgvrytgmeQLDVidtqtgkpVPADGKTAG----- 405
Cdd:PRK06060 286 GIPILDGIGSTEvgqTFVSNRVDEWRLGtlGRVLPPY-----------------EIRV--------VAPDGTTAGpgveg 340
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228909 406 EIVFRGNMVMKGYLKNPEANKETfaGGWFHSGDIAVKHPDNYIEIKDRSKDVIISGGENISSVEVENVVYHHPAVLEASV 485
Cdd:PRK06060 341 DLWVRGPAIAKGYWNRPDSPVAN--EGWLDTRDRVCIDSDGWVTYRCRADDTEVIGGVNVDPREVERLIIEDEAVAEAAV 418
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 15228909 486 VARPDERWQESPCAFVTLKSDyEKHDQNkLAQDIMKFCREKLPAYWVP-KSVVFGPLPKTATGKIQKHILRTKA 558
Cdd:PRK06060 419 VAVRESTGASTLQAFLVATSG-ATIDGS-VMRDLHRGLLNRLSAFKVPhRFAVVDRLPRTPNGKLVRGALRKQS 490
|
|
| prpE |
PRK10524 |
propionyl-CoA synthetase; Provisional |
46-549 |
5.42e-14 |
|
propionyl-CoA synthetase; Provisional
Pssm-ID: 182517 [Multi-domain] Cd Length: 629 Bit Score: 74.99 E-value: 5.42e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228909 46 REYTWRQTYDRCRRLASALADRSIGPGSTVAIIAPNIPamyEAHFgvpmcgAVLNCVniRLNA-PTVAF--LLSHSQSS- 121
Cdd:PRK10524 83 RTYTFRQLHDEVNRMAAMLRSLGVQRGDRVLIYMPMIA---EAAF------AMLACA--RIGAiHSVVFggFASHSLAAr 151
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228909 122 --------VIMVDQ--------EFFTLAEDSLRLMEEKagssfkrPLLIVIGDHTCAPESLN----------RALSKGAI 175
Cdd:PRK10524 152 iddakpvlIVSADAgsrggkvvPYKPLLDEAIALAQHK-------PRHVLLVDRGLAPMARVagrdvdyatlRAQHLGAR 224
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228909 176 EYEDFLATGDPNYpwqppadewqsiaLGYTSGTTASPKGVvlhHR--GAYIMAL--SNPLIWGMQDGAVYLWTLPMfhcn 251
Cdd:PRK10524 225 VPVEWLESNEPSY-------------ILYTSGTTGKPKGV---QRdtGGYAVALatSMDTIFGGKAGETFFCASDI---- 284
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228909 252 GWCFPWSLAV----LSG-TSIclrqvtakeVY-------------SMIAKYKVTHFCAAPVvlnAIVNAPKEDTILPLPH 313
Cdd:PRK10524 285 GWVVGHSYIVyaplLAGmATI---------MYeglptrpdagiwwRIVEKYKVNRMFSAPT---AIRVLKKQDPALLRKH 352
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228909 314 TV----HVMTAGAapP---PSVLFSMNQKGFRVAHTYGLSETYGPstVCAWKPEWDSLPPetqaKLNArQGVRYTGMeQL 386
Cdd:PRK10524 353 DLsslrALFLAGE--PldePTASWISEALGVPVIDNYWQTETGWP--ILAIARGVEDRPT----RLGS-PGVPMYGY-NV 422
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228909 387 DVIDTQTGKPVPADGKtaGEIVFRGNMVmKGYLKNPEANKETFAGGWFHS--------GDIAVKHPDNYIEIKDRSKDVI 458
Cdd:PRK10524 423 KLLNEVTGEPCGPNEK--GVLVIEGPLP-PGCMQTVWGDDDRFVKTYWSLfgrqvystFDWGIRDADGYYFILGRTDDVI 499
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228909 459 ISGGENISSVEVENVVYHHPAVLEASVVARPDERWQESPCAFVTLKSDYEKHDQN---KLAQDIMKFCREKLPAYWVPKS 535
Cdd:PRK10524 500 NVAGHRLGTREIEESISSHPAVAEVAVVGVKDALKGQVAVAFVVPKDSDSLADREarlALEKEIMALVDSQLGAVARPAR 579
|
570
....*....|....*
gi 15228909 536 VVF-GPLPKTATGKI 549
Cdd:PRK10524 580 VWFvSALPKTRSGKL 594
|
|
| entF |
PRK10252 |
enterobactin non-ribosomal peptide synthetase EntF; |
20-554 |
1.39e-13 |
|
enterobactin non-ribosomal peptide synthetase EntF;
Pssm-ID: 236668 [Multi-domain] Cd Length: 1296 Bit Score: 73.93 E-value: 1.39e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228909 20 TALTPLwfLDRAAVVHPTRKSVIHGSREYTWRQTYDRCRRLASALADRSIGPGSTVAIIAPNIPAMYEAHFGVPMCGAvl 99
Cdd:PRK10252 458 TTLSAL--VAQQAAKTPDAPALADARYQFSYREMREQVVALANLLRERGVKPGDSVAVALPRSVFLTLALHAIVEAGA-- 533
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228909 100 ncvnirlnaptvAFLlshsqssviMVDQEFftlAEDSLRLMEEKAgssfkRPLLIVigdhtcAPESLNRALSKGaieyeD 179
Cdd:PRK10252 534 ------------AWL---------PLDTGY---PDDRLKMMLEDA-----RPSLLI------TTADQLPRFADV-----P 573
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228909 180 FLATGDPNYPWQPPADEWQSIALG-------YTSGTTASPKGVVLHHRgayimALSNPLIWgMQD------GAVYLWTLP 246
Cdd:PRK10252 574 DLTSLCYNAPLAPQGAAPLQLSQPhhtayiiFTSGSTGRPKGVMVGQT-----AIVNRLLW-MQNhypltaDDVVLQKTP 647
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228909 247 M-FHCNGWCFPWSLavLSGTsiCLrqVTAK--------EVYSMIAKYKVT--HFcaAPVVLNAIVNAPK-EDTILPLPHT 314
Cdd:PRK10252 648 CsFDVSVWEFFWPF--IAGA--KL--VMAEpeahrdplAMQQFFAEYGVTttHF--VPSMLAAFVASLTpEGARQSCASL 719
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228909 315 VHVMTAGAAPPPSVlfsmnqkgfrVAHTYGLSET-----YGPST----VCAWKPEWDSLPPETQAKLNARQGVRYTGMEQ 385
Cdd:PRK10252 720 RQVFCSGEALPADL----------CREWQQLTGAplhnlYGPTEaavdVSWYPAFGEELAAVRGSSVPIGYPVWNTGLRI 789
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228909 386 LDvidtQTGKPVPADgkTAGEIVFRGNMVMKGYLKNPEANKETFAGGWF-------HSGDIAVKHPDNYIEIKDRSKDVI 458
Cdd:PRK10252 790 LD----ARMRPVPPG--VAGDLYLTGIQLAQGYLGRPDLTASRFIADPFapgermyRTGDVARWLDDGAVEYLGRSDDQL 863
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228909 459 ISGGENISSVEVENVVYHHPAVLEASVVARPDERWQESP------CAFVTLKSDyEKHDQNKLAQDImkfcREKLPAYWV 532
Cdd:PRK10252 864 KIRGQRIELGEIDRAMQALPDVEQAVTHACVINQAAATGgdarqlVGYLVSQSG-LPLDTSALQAQL----RERLPPHMV 938
|
570 580
....*....|....*....|...
gi 15228909 533 PKSVV-FGPLPKTATGKIQKHIL 554
Cdd:PRK10252 939 PVVLLqLDQLPLSANGKLDRKAL 961
|
|
| hsFATP4_like |
cd05939 |
Fatty acid transport proteins (FATP), including FATP4 and FATP1, and similar proteins; Fatty ... |
204-555 |
1.84e-13 |
|
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: 72.84 E-value: 1.84e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228909 204 YTSGTTASPKGVVLHHRGAYIMALSNPLIWGMQDGAVYLWTLPMFHCNGWCFPWSLAVLSGTSICLRQ-VTAKEVYSMIA 282
Cdd:cd05939 111 YTSGTTGLPKAAVIVHSRYYRIAAGAYYAFGMRPEDVVYDCLPLYHSAGGIMGVGQALLHGSTVVIRKkFSASNFWDDCV 190
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228909 283 KYKVTHFCAAPVVLNAIVNAPKEDTilPLPHTVHVMTaGAAPPPSVLFSMNQKgFRVAHT---YGLSEtyGPSTV----- 354
Cdd:cd05939 191 KYNCTIVQYIGEICRYLLAQPPSEE--EQKHNVRLAV-GNGLRPQIWEQFVRR-FGIPQIgefYGATE--GNSSLvnidn 264
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228909 355 ----CAWKPEW-DSLPPETQAKLNarqgvRYTGmeqlDVIDTQTGKPVPADGKTAGEIVFR---GNMVMK--GYLKNPEA 424
Cdd:cd05939 265 hvgaCGFNSRIlPSVYPIRLIKVD-----EDTG----ELIRDSDGLCIPCQPGEPGLLVGKiiqNDPLRRfdGYVNEGAT 335
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228909 425 NK----ETFAGG--WFHSGDIAVKHPDNYIEIKDRSKDVIISGGENISSVEVENVVyHHPAVLEASVVARPDERWQESPC 498
Cdd:cd05939 336 NKkiarDVFKKGdsAFLSGDVLVMDELGYLYFKDRTGDTFRWKGENVSTTEVEGIL-SNVLGLEDVVVYGVEVPGVEGRA 414
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*...
gi 15228909 499 AFVTLKSDYEKHDQNKLAQDIMKfcreKLPAYWVPKSVVFGP-LPKTATGKIQKHILR 555
Cdd:cd05939 415 GMAAIVDPERKVDLDRFSAVLAK----SLPPYARPQFIRLLPeVDKTGTFKLQKTDLQ 468
|
|
| PRK09192 |
PRK09192 |
fatty acyl-AMP ligase; |
382-561 |
2.94e-13 |
|
fatty acyl-AMP ligase;
Pssm-ID: 236403 [Multi-domain] Cd Length: 579 Bit Score: 72.35 E-value: 2.94e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228909 382 GMEqLDVIDtQTGKPVPAdgKTAGEIVFRGNMVMKGYLKNPEANKETFAGGWFHSGDIAVKHpDNYIEIKDRSKDVIISG 461
Cdd:PRK09192 393 GHE-IEIRN-EAGMPLPE--RVVGHICVRGPSLMSGYFRDEESQDVLAADGWLDTGDLGYLL-DGYLYITGRAKDLIIIN 467
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228909 462 GENISSVEVENVVYHHPAVL--EASVVARPDERwQESPCAFVTLK-SDYEkhDQNKLAQDIMKFCREklpAYWVPKSVVF 538
Cdd:PRK09192 468 GRNIWPQDIEWIAEQEPELRsgDAAAFSIAQEN-GEKIVLLVQCRiSDEE--RRGQLIHALAALVRS---EFGVEAAVEL 541
|
170 180
....*....|....*....|....*.
gi 15228909 539 GP---LPKTATGKIQkhilRTKAKEM 561
Cdd:PRK09192 542 VPphsLPRTSSGKLS----RAKAKKR 563
|
|
| A_NRPS_SidN3_like |
cd05918 |
The adenylation (A) domain of siderophore-synthesizing nonribosomal peptide synthetases (NRPS); ... |
204-549 |
3.48e-13 |
|
The adenylation (A) domain of siderophore-synthesizing nonribosomal peptide synthetases (NRPS); The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. This family of siderophore-synthesizing NRPS includes the third adenylation domain of SidN from the endophytic fungus Neotyphodium lolii, ferrichrome siderophore synthetase, HC-toxin synthetase, and enniatin synthase. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.
Pssm-ID: 341242 [Multi-domain] Cd Length: 481 Bit Score: 71.80 E-value: 3.48e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228909 204 YTSGTTASPKGVVLHHRGAYIMALSNPLIWGMQDG------AVYLWTLPMFHCngwcfpwsLAVL-SGTSIClrqVTAKE 276
Cdd:cd05918 113 FTSGSTGKPKGVVIEHRALSTSALAHGRALGLTSEsrvlqfASYTFDVSILEI--------FTTLaAGGCLC---IPSEE 181
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228909 277 -----VYSMIAKYKVTHFCAAPVVLNAIvnAPKEdtilpLPHTVHVMTAGAAPPPSVLFSMNQKGfRVAHTYGLSETygp 351
Cdd:cd05918 182 drlndLAGFINRLRVTWAFLTPSVARLL--DPED-----VPSLRTLVLGGEALTQSDVDTWADRV-RLINAYGPAEC--- 250
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228909 352 sTVCAwkpewdslppeTQAKLNARQGVRYTGmEQLD----VIDTQT-GKPVPADGktAGEIVFRGNMVMKGYLKNPEANK 426
Cdd:cd05918 251 -TIAA-----------TVSPVVPSTDPRNIG-RPLGatcwVVDPDNhDRLVPIGA--VGELLIEGPILARGYLNDPEKTA 315
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228909 427 ETF---------AGGWFHS-----GDIAVKHPDNYIEIKDRsKD--VIISG-----GenissvEVENVVYHHPAVLE--- 482
Cdd:cd05918 316 AAFiedpawlkqEGSGRGRrlyrtGDLVRYNPDGSLEYVGR-KDtqVKIRGqrvelG------EIEHHLRQSLPGAKevv 388
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228909 483 ASVVARPDERWQESPCAFVTLKSDYEKHDQ------------NKLAQDIMKFCREKLPAYWVPKSVVFGP-LPKTATGKI 549
Cdd:cd05918 389 VEVVKPKDGSSSPQLVAFVVLDGSSSGSGDgdslflepsdefRALVAELRSKLRQRLPSYMVPSVFLPLShLPLTASGKI 468
|
|
| PRK07824 |
PRK07824 |
o-succinylbenzoate--CoA ligase; |
205-549 |
4.22e-13 |
|
o-succinylbenzoate--CoA ligase;
Pssm-ID: 236108 [Multi-domain] Cd Length: 358 Bit Score: 70.84 E-value: 4.22e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228909 205 TSGTTASPKGVVL------------HHRgayimaLSNPLIWgmqdgavyLWTLPMFHCNGwcfpwsLAVLsgtsicLRQV 272
Cdd:PRK07824 43 TSGTTGTPKGAMLtaaaltasadatHDR------LGGPGQW--------LLALPAHHIAG------LQVL------VRSV 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228909 273 TAKE---VYSMIAKYKVTHFCAA--------------PVVLNAIVNAPKEDTILPLPHTVHVmtAGAAPPPSVLFSMNQK 335
Cdd:PRK07824 97 IAGSepvELDVSAGFDPTALPRAvaelgggrrytslvPMQLAKALDDPAATAALAELDAVLV--GGGPAPAPVLDAAAAA 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228909 336 GFRVAHTYGLSETYGpstvcawkpewdslppetqaklnarqGVRYTGmeqldvidtqtgkpVPADGKTA----GEIVFRG 411
Cdd:PRK07824 175 GINVVRTYGMSETSG--------------------------GCVYDG--------------VPLDGVRVrvedGRIALGG 214
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228909 412 NMVMKGYlKNPEANKETFAGGWFHSGDIAVKHpDNYIEIKDRSKDVIISGGENISSVEVENVVYHHPAVLEASVVARPDE 491
Cdd:PRK07824 215 PTLAKGY-RNPVDPDPFAEPGWFRTDDLGALD-DGVLTVLGRADDAISTGGLTVLPQVVEAALATHPAVADCAVFGLPDD 292
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 15228909 492 RWQE--------SPCAFVTLkSDYEKHDQnklaqdimkfcrEKLPAYWVPKSV-VFGPLPKTATGKI 549
Cdd:PRK07824 293 RLGQrvvaavvgDGGPAPTL-EALRAHVA------------RTLDRTAAPRELhVVDELPRRGIGKV 346
|
|
| PRK08308 |
PRK08308 |
acyl-CoA synthetase; Validated |
202-565 |
1.57e-12 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236231 [Multi-domain] Cd Length: 414 Bit Score: 69.68 E-value: 1.57e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228909 202 LGYTSGTTASPKGV------VLHHRGAYIMALSNPliwgmqDGAVYLWTLPMFHcngwcfpwSLAVLSGTSICLRQ---- 271
Cdd:PRK08308 106 LQYSSGTTGEPKLIrrswteIDREIEAYNEALNCE------QDETPIVACPVTH--------SYGLICGVLAALTRgskp 171
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228909 272 --VTAKEVYSMIAKYKVTH---FCAAPVVLNAIVNAPKEDtilplpHTVH-VMTAGAAPPPSVLFSMNQKGFRVAHTYGL 345
Cdd:PRK08308 172 viITNKNPKFALNILRNTPqhiLYAVPLMLHILGRLLPGT------FQFHaVMTSGTPLPEAWFYKLRERTTYMMQQYGC 245
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228909 346 SETyGPSTVCawkpewdslPPETQAklnarqgvrytgmeqldvidTQTGKPVPADGKTAGEivfrgNMvmkgylKNPEAN 425
Cdd:PRK08308 246 SEA-GCVSIC---------PDMKSH--------------------LDLGNPLPHVSVSAGS-----DE------NAPEEI 284
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228909 426 KETFAGGWFHSGDIAVKHPDNYIEIKDRSKDVIISGGENISSVEVENVVYHHPAVLEASVVARPDERWQESPCAFVTLKS 505
Cdd:PRK08308 285 VVKMGDKEIFTKDLGYKSERGTLHFMGRMDDVINVSGLNVYPIEVEDVMLRLPGVQEAVVYRGKDPVAGERVKAKVISHE 364
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 15228909 506 DYEkhdqnklAQDIMKFCREKLPAYWVPKSVVFGP-LPKTATGKIQKhilrtKAKEMGPVP 565
Cdd:PRK08308 365 EID-------PVQLREWCIQHLAPYQVPHEIESVTeIPKNANGKVSR-----KLLELGEVT 413
|
|
| PLN02387 |
PLN02387 |
long-chain-fatty-acid-CoA ligase family protein |
393-560 |
2.70e-12 |
|
long-chain-fatty-acid-CoA ligase family protein
Pssm-ID: 215217 [Multi-domain] Cd Length: 696 Bit Score: 69.38 E-value: 2.70e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228909 393 TGKPVPAdgktaGEIVFRGNMVMKGYLKNPEANKETF-----AGGWFHSGDIAVKHPDNYIEIKDRSKDVI-ISGGENIS 466
Cdd:PLN02387 496 SDKPMPR-----GEIVIGGPSVTLGYFKNQEKTDEVYkvderGMRWFYTGDIGQFHPDGCLEIIDRKKDIVkLQHGEYVS 570
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228909 467 --SVE--------VENVVYH----HPAVLEASVVARPD-ERW-QESPCAFVTL-----KSDYEKHDQNKLAQDIMKFCRE 525
Cdd:PLN02387 571 lgKVEaalsvspyVDNIMVHadpfHSYCVALVVPSQQAlEKWaKKAGIDYSNFaelceKEEAVKEVQQSLSKAAKAARLE 650
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 15228909 526 K---------LPAYWVPKSVVFgplpkTATGKIQKHILRTKAKE 560
Cdd:PLN02387 651 KfeipakiklLPEPWTPESGLV-----TAALKLKREQIRKKFKD 689
|
|
| PRK09274 |
PRK09274 |
peptide synthase; Provisional |
29-427 |
5.35e-12 |
|
peptide synthase; Provisional
Pssm-ID: 236443 [Multi-domain] Cd Length: 552 Bit Score: 68.39 E-value: 5.35e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228909 29 DRAAVVHPTRKSViHGSREY---TWRQTYDRCRRLASALADRSIGPGS-TVAIIAPNIP--AMYEAHFGVpmcGAV---- 98
Cdd:PRK09274 21 DQLAVAVPGGRGA-DGKLAYdelSFAELDARSDAIAHGLNAAGIGRGMrAVLMVTPSLEffALTFALFKA---GAVpvlv 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228909 99 ---------LNCvnirlnaptvaflLSHSQSSVimvdqeFFTLAEDSL-RLMEEKAGSSFKRplLIVIGdhtcapeslnR 168
Cdd:PRK09274 97 dpgmgiknlKQC-------------LAEAQPDA------FIGIPKAHLaRRLFGWGKPSVRR--LVTVG----------G 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228909 169 ALSKGAIEYEDFLAtGDPNYPWQP---PADEWQSIAlgYTSGTTASPKGVVLHHRG--AYIMALSNplIWGMQDGAVYLW 243
Cdd:PRK09274 146 RLLWGGTTLATLLR-DGAAAPFPMadlAPDDMAAIL--FTSGSTGTPKGVVYTHGMfeAQIEALRE--DYGIEPGEIDLP 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228909 244 TLPMFhcngwcfpwSL--AVLSGTSI-------CLRQVTAKEVYSMIAKYKVTHFCAAPVVLNAIVNAPKEDTIlPLPHT 314
Cdd:PRK09274 221 TFPLF---------ALfgPALGMTSVipdmdptRPATVDPAKLFAAIERYGVTNLFGSPALLERLGRYGEANGI-KLPSL 290
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228909 315 VHVMTAGAAPPPSVL--FS-MNQKGFRVAHTYGLSETYGPSTVcawkpEWDSLPPETQAKLNARQGV----RYTGMEqLD 387
Cdd:PRK09274 291 RRVISAGAPVPIAVIerFRaMLPPDAEILTPYGATEALPISSI-----ESREILFATRAATDNGAGIcvgrPVDGVE-VR 364
|
410 420 430 440
....*....|....*....|....*....|....*....|....*...
gi 15228909 388 VIDTqTGKPVP--------ADGKTaGEIVFRGNMVMKGYLKNPEANKE 427
Cdd:PRK09274 365 IIAI-SDAPIPewddalrlATGEI-GEIVVAGPMVTRSYYNRPEATRL 410
|
|
| PRK08180 |
PRK08180 |
feruloyl-CoA synthase; Reviewed |
27-442 |
6.11e-12 |
|
feruloyl-CoA synthase; Reviewed
Pssm-ID: 236175 [Multi-domain] Cd Length: 614 Bit Score: 68.37 E-value: 6.11e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228909 27 FLDRAAVVHPTR-----KSVIHGSREYTWRQTYDRCRRLASALADRSIGPGSTVAIIAPNIPA----MYEA-HFGVPMCg 96
Cdd:PRK08180 44 RLVHWAQEAPDRvflaeRGADGGWRRLTYAEALERVRAIAQALLDRGLSAERPLMILSGNSIEhallALAAmYAGVPYA- 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228909 97 AVlncvnirlnAPTVAfLLSHSQS---SVIMVDQEFFTLAEDslrlmeekaGSSFKRPLLIVIGDHTCAPESLNRALSKG 173
Cdd:PRK08180 123 PV---------SPAYS-LVSQDFGklrHVLELLTPGLVFADD---------GAAFARALAAVVPADVEVVAVRGAVPGRA 183
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228909 174 AIEYEDFLATGDPnypwqPPADEW------QSIA-LGYTSGTTASPKGVVLHHRgayiMALSNpliwgmQdgAVYLWTLP 246
Cdd:PRK08180 184 ATPFAALLATPPT-----AAVDAAhaavgpDTIAkFLFTSGSTGLPKAVINTHR----MLCAN------Q--QMLAQTFP 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228909 247 MFHCNG-----WcFPWSLAVlsGTSICLRQVTA----------KEVYSMIAK-------YKVTHFCAAPVVLNAIVNAPK 304
Cdd:PRK08180 247 FLAEEPpvlvdW-LPWNHTF--GGNHNLGIVLYnggtlyiddgKPTPGGFDEtlrnlreISPTVYFNVPKGWEMLVPALE 323
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228909 305 EDTIL--PLPHTVHVMT-AGAAPPPSVL-----FSMNQKGFRVAHT--YGLSETYGPSTVCAWkpewdslpPETQAKLna 374
Cdd:PRK08180 324 RDAALrrRFFSRLKLLFyAGAALSQDVWdrldrVAEATCGERIRMMtgLGMTETAPSATFTTG--------PLSRAGN-- 393
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 15228909 375 rQGVRYTGMEQldvidtqtgKPVPADGKTagEIVFRGNMVMKGYLKNPEANKETF-AGGWFHSGDiAVK 442
Cdd:PRK08180 394 -IGLPAPGCEV---------KLVPVGGKL--EVRVKGPNVTPGYWRAPELTAEAFdEEGYYRSGD-AVR 449
|
|
| A_NRPS_LgrA-like |
cd17645 |
adenylation (A) domain of linear gramicidin synthetase (LgrA) and similar proteins; This ... |
35-554 |
9.30e-12 |
|
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: 67.19 E-value: 9.30e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228909 35 HPTRKSVIHGSREYTWRQTYDRCRRLASALADRSIGPGSTVAIIAPNIPAMYEAHFGVPMCGAVLNCVNIRLNAPTVAFL 114
Cdd:cd17645 11 TPDHVAVVDRGQSLTYKQLNEKANQLARHLRGKGVKPDDQVGIMLDKSLDMIAAILGVLKAGGAYVPIDPDYPGERIAYM 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228909 115 LSHSQSSVIMVDqefftlAEDslrlmeekagssfkrpLLIVIgdhtcapeslnralskgaieyedflatgdpnypwqppa 194
Cdd:cd17645 91 LADSSAKILLTN------PDD----------------LAYVI-------------------------------------- 110
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228909 195 dewqsialgYTSGTTASPKGVVLHHRgayimALSNPLIW-------GMQDGAVYLWTLPmFHCNGW-CFPWSLAvlsGTS 266
Cdd:cd17645 111 ---------YTSGSTGLPKGVMIEHH-----NLVNLCEWhrpyfgvTPADKSLVYASFS-FDASAWeIFPHLTA---GAA 172
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228909 267 IclrQVTAKEVYSMIAKykVTHFCAAPVVLNAIVNAPKEDTILPLP-HTVHVMTAGAapppSVLFSMNQKGFRVAHTYGL 345
Cdd:cd17645 173 L---HVVPSERRLDLDA--LNDYFNQEGITISFLPTGAAEQFMQLDnQSLRVLLTGG----DKLKKIERKGYKLVNNYGP 243
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228909 346 SETYGPSTVCAWKPEWDSLPPetqAKLNARQGVrYTGMEQLDVidtqtgKPVPAdgktAGEIVFRGNMVMKGYLKNPEAN 425
Cdd:cd17645 244 TENTVVATSFEIDKPYANIPI---GKPIDNTRV-YILDEALQL------QPIGV----AGELCIAGEGLARGYLNRPELT 309
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228909 426 KETFAGGWF-------HSGDIAVKHPDNYIEIKDRSKDVIISGGENISSVEVENVVYHHPAVLEASVVARPDERWQESPC 498
Cdd:cd17645 310 AEKFIVHPFvpgermyRTGDLAKFLPDGNIEFLGRLDQQVKIRGYRIEPGEIEPFLMNHPLIELAAVLAKEDADGRKYLV 389
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*..
gi 15228909 499 AFVTLKSDYEkhdqnklAQDIMKFCREKLPAYWVPKSVV-FGPLPKTATGKIQKHIL 554
Cdd:cd17645 390 AYVTAPEEIP-------HEELREWLKNDLPDYMIPTYFVhLKALPLTANGKVDRKAL 439
|
|
| FCS |
cd05921 |
Feruloyl-CoA synthetase (FCS); Feruloyl-CoA synthetase is an essential enzyme in the feruloyl ... |
43-445 |
1.08e-11 |
|
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: 67.46 E-value: 1.08e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228909 43 HGSREYTWRQTYDRCRRLASALADRSIGPGSTVAIIAPN--------IPAMyeaHFGVPMCgAVlncvnirlnAPTVAfL 114
Cdd:cd05921 21 GGWRRVTYAEALRQVRAIAQGLLDLGLSAERPLLILSGNsiehalmaLAAM---YAGVPAA-PV---------SPAYS-L 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228909 115 LSHSQSSVimvdQEFFTLAEDSLRLMEekAGSSFKRPLLIVIGDHTCAPESLNRALSKGAIEYEDFLAT-----GDPNYP 189
Cdd:cd05921 87 MSQDLAKL----KHLFELLKPGLVFAQ--DAAPFARALAAIFPLGTPLVVSRNAVAGRGAISFAELAATpptaaVDAAFA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228909 190 WQPPADewqsIA-LGYTSGTTASPKGVVLHHRgayIMALSNPLI---WGMQDG--AVYLWTLPMFHCNGWCFPWSLAVLS 263
Cdd:cd05921 161 AVGPDT----VAkFLFTSGSTGLPKAVINTQR---MLCANQAMLeqtYPFFGEepPVLVDWLPWNHTFGGNHNFNLVLYN 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228909 264 GTSICLRQvtAKEVYSMIAK-----YKV--THFCAAPVVLNAIVNAPKEDTIL--PLPHTVHVMT-AGAAPPPSVL---- 329
Cdd:cd05921 234 GGTLYIDD--GKPMPGGFEEtlrnlREIspTVYFNVPAGWEMLVAALEKDEALrrRFFKRLKLMFyAGAGLSQDVWdrlq 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228909 330 -FSMNQKGFRVAHT--YGLSETYGPSTVCAW---KPEWDSLP-PETQAKLnarqgvrytgmeqldvidtqtgkpVPADGK 402
Cdd:cd05921 312 aLAVATVGERIPMMagLGATETAPTATFTHWpteRSGLIGLPaPGTELKL------------------------VPSGGK 367
|
410 420 430 440
....*....|....*....|....*....|....*....|....
gi 15228909 403 TagEIVFRGNMVMKGYLKNPEANKETF-AGGWFHSGDiAVKHPD 445
Cdd:cd05921 368 Y--EVRVKGPNVTPGYWRQPELTAQAFdEEGFYCLGD-AAKLAD 408
|
|
| PRK06334 |
PRK06334 |
long chain fatty acid--[acyl-carrier-protein] ligase; Validated |
204-521 |
1.59e-11 |
|
long chain fatty acid--[acyl-carrier-protein] ligase; Validated
Pssm-ID: 180533 [Multi-domain] Cd Length: 539 Bit Score: 66.76 E-value: 1.59e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228909 204 YTSGTTASPKGVVLHHrgAYIMA-------LSNPLiwgMQDgaVYLWTLPMFHCNGW--C--FPwslaVLSGTSICL--R 270
Cdd:PRK06334 190 FTSGTEKLPKGVPLTH--ANLLAnqraclkFFSPK---EDD--VMMSFLPPFHAYGFnsCtlFP----LLSGVPVVFayN 258
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228909 271 QVTAKEVYSMIAKYKVTHFCAAPVVLNAIVN-APKEDTILPlphTVHVMTAGAAPPPSVLFSMNQKGFrvAHTyGLSETY 349
Cdd:PRK06334 259 PLYPKKIVEMIDEAKVTFLGSTPVFFDYILKtAKKQESCLP---SLRFVVIGGDAFKDSLYQEALKTF--PHI-QLRQGY 332
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228909 350 GpSTVCAwkPEWdSLPPETQAKLNARQGVRYTGMEQLdVIDTQTGKPVPAdGKTaGEIVFRGNMVMKGYLKNPEANKETF 429
Cdd:PRK06334 333 G-TTECS--PVI-TINTVNSPKHESCVGMPIRGMDVL-IVSEETKVPVSS-GET-GLVLTRGTSLFSGYLGEDFGQGFVE 405
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228909 430 AGG--WFHSGDIAVKHPDNYIEIKDRSKDVIISGGENISSVEVENVVYHHPAVLEAS------VVARPDERwqESPCAFV 501
Cdd:PRK06334 406 LGGetWYVTGDLGYVDRHGELFLKGRLSRFVKIGAEMVSLEALESILMEGFGQNAADhagplvVCGLPGEK--VRLCLFT 483
|
330 340
....*....|....*....|...
gi 15228909 502 TLKSD-YEKHD--QNKLAQDIMK 521
Cdd:PRK06334 484 TFPTSiSEVNDilKNSKTSSILK 506
|
|
| PRK07769 |
PRK07769 |
long-chain-fatty-acid--CoA ligase; Validated |
46-485 |
1.15e-10 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 181109 [Multi-domain] Cd Length: 631 Bit Score: 64.37 E-value: 1.15e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228909 46 REYTWRQTYDRCRRLASALaDRSIGPGSTVAIIAPN--------IPAMYEAHFGVPMCGAVLNCVNIRLNAptvafLLSH 117
Cdd:PRK07769 54 RDLTWSQFGARNRAVGARL-QQVTKPGDRVAILAPQnldyliafFGALYAGRIAVPLFDPAEPGHVGRLHA-----VLDD 127
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228909 118 SQSSVIMVDQEFFTLAEDSLRLMEEKagssfKRPLLIVIgdhTCAPESLNralskgaieyedflATgdpnypWQPPADEW 197
Cdd:PRK07769 128 CTPSAILTTTDSAEGVRKFFRARPAK-----ERPRVIAV---DAVPDEVG--------------AT------WVPPEANE 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228909 198 QSIA-LGYTSGTTASPKGVVLHHRGAYIMALSNPLIWGMQDGAVYLWTLPMFHCNGwCFPWSLAVLSGTSICL------- 269
Cdd:PRK07769 180 DTIAyLQYTSGSTRIPAGVQITHLNLPTNVLQVIDALEGQEGDRGVSWLPFFHDMG-LITVLLPALLGHYITFmspaafv 258
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228909 270 -------RQVTAKEvysmiaKYKVTHFCAAP---VVLNAIVNAPKEDTiLPLP-HTVHVMTAGAAPppsVLFSMNQKGFR 338
Cdd:PRK07769 259 rrpgrwiRELARKP------GGTGGTFSAAPnfaFEHAAARGLPKDGE-PPLDlSNVKGLLNGSEP---VSPASMRKFNE 328
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228909 339 VAHTYGLSETygpstvcAWKPEW---------DSLPPETQAK--------LNARQGVR---------------YTGMEQL 386
Cdd:PRK07769 329 AFAPYGLPPT-------AIKPSYgmaeatlfvSTTPMDEEPTviyvdrdeLNAGRFVEvpadapnavaqvsagKVGVSEW 401
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228909 387 DVI-DTQTGKPVPaDGKTaGEIVFRGNMVMKGYLKNPEANKETF------------AGG------WFHSGDIAVKHpDNY 447
Cdd:PRK07769 402 AVIvDPETASELP-DGQI-GEIWLHGNNIGTGYWGKPEETAATFqnilksrlseshAEGapddalWVRTGDYGVYF-DGE 478
|
490 500 510
....*....|....*....|....*....|....*...
gi 15228909 448 IEIKDRSKDVIISGGENissvevenvvyHHPAVLEASV 485
Cdd:PRK07769 479 LYITGRVKDLVIIDGRN-----------HYPQDLEYTA 505
|
|
| PRK04813 |
PRK04813 |
D-alanine--poly(phosphoribitol) ligase subunit DltA; |
204-549 |
2.75e-10 |
|
D-alanine--poly(phosphoribitol) ligase subunit DltA;
Pssm-ID: 235313 [Multi-domain] Cd Length: 503 Bit Score: 62.61 E-value: 2.75e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228909 204 YTSGTTASPKGVVLHHrgAYIMALSNpliWGMQD-----GAVYLWTLPmfhcngwcFPWSLAVLS--------GTSICL- 269
Cdd:PRK04813 150 FTSGTTGKPKGVQISH--DNLVSFTN---WMLEDfalpeGPQFLNQAP--------YSFDLSVMDlyptlasgGTLVALp 216
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228909 270 RQVTA--KEVYSMIAKYKVTHFCAAP-----VVLNAIVNAPKedtilpLPHTVHVMTAGAAPPPSVLFSMNQKgFRVAHT 342
Cdd:PRK04813 217 KDMTAnfKQLFETLPQLPINVWVSTPsfadmCLLDPSFNEEH------LPNLTHFLFCGEELPHKTAKKLLER-FPSATI 289
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228909 343 YglsETYGPS--TV-----------CAwkpEWDSLPpetqaklnarqgVRYTGMEQLDVIDTQTGKPVPADGKtaGEIVF 409
Cdd:PRK04813 290 Y---NTYGPTeaTVavtsieitdemLD---QYKRLP------------IGYAKPDSPLLIIDEEGTKLPDGEQ--GEIVI 349
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228909 410 RGNMVMKGYLKNPEANKE---TFAGGW-FHSGDIAVKhPDNYIEIKDRSKDVIISGGENISSVEVENVVYHHPAVLEASV 485
Cdd:PRK04813 350 SGPSVSKGYLNNPEKTAEaffTFDGQPaYHTGDAGYL-EDGLLFYQGRIDFQIKLNGYRIELEEIEQNLRQSSYVESAVV 428
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 15228909 486 VA-RPDERWQESPCAFVTLKSDYEKhdQNKLAQDIMKFCREKLPAYWVPKSVVF-GPLPKTATGKI 549
Cdd:PRK04813 429 VPyNKDHKVQYLIAYVVPKEEDFER--EFELTKAIKKELKERLMEYMIPRKFIYrDSLPLTPNGKI 492
|
|
| PRK05851 |
PRK05851 |
long-chain-fatty acid--ACP ligase MbtM; |
173-551 |
6.89e-10 |
|
long-chain-fatty acid--ACP ligase MbtM;
Pssm-ID: 180289 [Multi-domain] Cd Length: 525 Bit Score: 61.71 E-value: 6.89e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228909 173 GAIEYEDFLATGDPNY--PWQPPADEWQSIALGyTSGTTASPKGVVLHhRGAY---IMALSNPLIWGMQDGAVYLWtLPM 247
Cdd:PRK05851 127 SSVTVHDLATAAHTNRsaSLTPPDSGGPAVLQG-TAGSTGTPRTAILS-PGAVlsnLRGLNARVGLDAATDVGCSW-LPL 203
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228909 248 FHCNGWCFPWSlAVLSGTSICLRQVTA-----------------------KEVYSMIAKY--KVTHfcaapVVLNAivna 302
Cdd:PRK05851 204 YHDMGLAFLLT-AALAGAPLWLAPTTAfsaspfrwlswlsdsratltaapNFAYNLIGKYarRVSD-----VDLGA---- 273
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228909 303 pkedtilplphtVHVMTAGAAPPPSVLF-----SMNQKGFR---VAHTYGLSETYGPSTV----CAWKPEWDSLPPETQA 370
Cdd:PRK05851 274 ------------LRVALNGGEPVDCDGFerfatAMAPFGFDagaAAPSYGLAESTCAVTVpvpgIGLRVDEVTTDDGSGA 341
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228909 371 KLNARQGVRYTGMEqldVIDTQTGKPVPADGKTAGEIVFRGNMVMKGYLKNPEANketfAGGWFHSGDIAVkHPDNYIEI 450
Cdd:PRK05851 342 RRHAVLGNPIPGME---VRISPGDGAAGVAGREIGEIEIRGASMMSGYLGQAPID----PDDWFPTGDLGY-LVDGGLVV 413
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228909 451 KDRSKDVIISGGENISSVEVENVVYHHPAVLEASVVA-RPDERwqeSPCAFVTLKSDYEKHDQ----NKLAQDIMKFCRE 525
Cdd:PRK05851 414 CGRAKELITVAGRNIFPTEIERVAAQVRGVREGAVVAvGTGEG---SARPGLVIAAEFRGPDEagarSEVVQRVASECGV 490
|
410 420
....*....|....*....|....*....
gi 15228909 526 klpaywVPKSVVF---GPLPKTATGKIQK 551
Cdd:PRK05851 491 ------VPSDVVFvapGSLPRTSSGKLRR 513
|
|
| FACL_like_1 |
cd05910 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
192-486 |
2.18e-09 |
|
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ATP-dependent activation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions.
Pssm-ID: 341236 [Multi-domain] Cd Length: 457 Bit Score: 59.78 E-value: 2.18e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228909 192 PPADEwqSIALGYTSGTTASPKGVVLHHR--GAYIMALSNplIWGMQDGAVYLWTLPMFHCNGwcfpwslAVLSGTSI-- 267
Cdd:cd05910 82 PKADE--PAAILFTSGSTGTPKGVVYRHGtfAAQIDALRQ--LYGIRPGEVDLATFPLFALFG-------PALGLTSVip 150
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228909 268 -----CLRQVTAKEVYSMIAKYKVTHFCAAPVVLnAIVNAPKEDTILPLPHTVHVMTAGAAPPPSV---LFSMNQKGFRV 339
Cdd:cd05910 151 dmdptRPARADPQKLVGAIRQYGVSIVFGSPALL-ERVARYCAQHGITLPSLRRVLSAGAPVPIALaarLRKMLSDEAEI 229
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228909 340 AHTYGLSETYGPSTVcawkpEWDSLPPETQAKLNARQGV----RYTGMeQLDVIDTqTGKPVPADGKTA-------GEIV 408
Cdd:cd05910 230 LTPYGATEALPVSSI-----GSRELLATTTAATSGGAGTcvgrPIPGV-RVRIIEI-DDEPIAEWDDTLelprgeiGEIT 302
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228909 409 FRGNMVMKGYLKNPEANK----ETFAGGWFH-SGDIAvkhpdnYIEIKD------RSKDVIISGGENISSVEVENVVYHH 477
Cdd:cd05910 303 VTGPTVTPTYVNRPVATAlakiDDNSEGFWHrMGDLG------YLDDEGrlwfcgRKAHRVITTGGTLYTEPVERVFNTH 376
|
....*....
gi 15228909 478 PAVLEASVV 486
Cdd:cd05910 377 PGVRRSALV 385
|
|
| PRK06814 |
PRK06814 |
acyl-[ACP]--phospholipid O-acyltransferase; |
204-560 |
5.44e-09 |
|
acyl-[ACP]--phospholipid O-acyltransferase;
Pssm-ID: 235865 [Multi-domain] Cd Length: 1140 Bit Score: 59.21 E-value: 5.44e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228909 204 YTSGTTASPKGVVLHHRG--AYIMALSNPLIWGMQDgaVYLWTLPMFHCNGwcfpwslavlsgtsiclrqVTAKEVYSMI 281
Cdd:PRK06814 800 FTSGSEGTPKGVVLSHRNllANRAQVAARIDFSPED--KVFNALPVFHSFG-------------------LTGGLVLPLL 858
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228909 282 AKYKV------THFCAAPVVLNAiVNAP---KEDTILP----LPH-----TVHVMTAGAAP--PPSVLFSMNQKGFRVAH 341
Cdd:PRK06814 859 SGVKVflypspLHYRIIPELIYD-TNATilfGTDTFLNgyarYAHpydfrSLRYVFAGAEKvkEETRQTWMEKFGIRILE 937
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228909 342 TYGLSETyGPSTVCawkpewdSLP----PETQAKLnarqgvrYTGME-QLDvidtqtgkPVPA--DGktaGEIVFRGNMV 414
Cdd:PRK06814 938 GYGVTET-APVIAL-------NTPmhnkAGTVGRL-------LPGIEyRLE--------PVPGidEG---GRLFVRGPNV 991
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228909 415 MKGYLK--NPEANKETfAGGWFHSGDIAVKHPDNYIEIKDRSKDVIISGGENISSVEVENVVYH-HPAVLEAsVVARPDE 491
Cdd:PRK06814 992 MLGYLRaeNPGVLEPP-ADGWYDTGDIVTIDEEGFITIKGRAKRFAKIAGEMISLAAVEELAAElWPDALHA-AVSIPDA 1069
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 15228909 492 RWQESPCAFVTLK----SDYEKHDQNKLAQDIMkfcreklpaywVPKSV-VFGPLPKTATGKIQKHILRTKAKE 560
Cdd:PRK06814 1070 RKGERIILLTTASdatrAAFLAHAKAAGASELM-----------VPAEIiTIDEIPLLGTGKIDYVAVTKLAEE 1132
|
|
| PRK12582 |
PRK12582 |
acyl-CoA synthetase; Provisional |
27-461 |
5.51e-09 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 237144 [Multi-domain] Cd Length: 624 Bit Score: 58.90 E-value: 5.51e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228909 27 FLDRAAVVHPTR-----KSVIHGS-REYTWRQTYDRCRRLASALADRSIGPGSTVAIIAPN-----IPAMYEAHFGVPMc 95
Cdd:PRK12582 54 LLAKWAAEAPDRpwlaqREPGHGQwRKVTYGEAKRAVDALAQALLDLGLDPGRPVMILSGNsiehaLMTLAAMQAGVPA- 132
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228909 96 gavlncvnirlnAP-TVAF-LLSHSQSSVimvdQEFFTLAEDSLRLMEEkaGSSFKRPLLIV-IGDHTCApESLNRALSK 172
Cdd:PRK12582 133 ------------APvSPAYsLMSHDHAKL----KHLFDLVKPRVVFAQS--GAPFARALAALdLLDVTVV-HVTGPGEGI 193
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228909 173 GAIEYEDFLATgdpnypwqPPADEW-QSIA-LG--------YTSGTTASPKGVVLHHRgayiMALSNplIWGM------- 235
Cdd:PRK12582 194 ASIAFADLAAT--------PPTAAVaAAIAaITpdtvakylFTSGSTGMPKAVINTQR----MMCAN--IAMQeqlrpre 259
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228909 236 QDG--AVYLWTLPMFHCNGWCFPWSLAVLSGTSICLRQvtAKEVYSMIAK-----YKV--THFCAAPVVLNAIVNAPKED 306
Cdd:PRK12582 260 PDPppPVSLDWMPWNHTMGGNANFNGLLWGGGTLYIDD--GKPLPGMFEEtirnlREIspTVYGNVPAGYAMLAEAMEKD 337
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228909 307 TIL--PLPHTVHVMTAGAAPPPSVLFSMNQK------GFRVAHT--YGLSETYGPSTVCAWKPEWDS---LP-PETQAKL 372
Cdd:PRK12582 338 DALrrSFFKNLRLMAYGGATLSDDLYERMQAlavrttGHRIPFYtgYGATETAPTTTGTHWDTERVGligLPlPGVELKL 417
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228909 373 narqgvrytgmeqldvidtqtgkpVPADGKTagEIVFRGNMVMKGYLKNPEANKETF-AGGWFHSGDIAVkhpdnYIEIK 451
Cdd:PRK12582 418 ------------------------APVGDKY--EVRVKGPNVTPGYHKDPELTAAAFdEEGFYRLGDAAR-----FVDPD 466
|
490
....*....|
gi 15228909 452 DRSKDVIISG 461
Cdd:PRK12582 467 DPEKGLIFDG 476
|
|
| A_NRPS_MycA_like |
cd05908 |
The adenylation domain of nonribosomal peptide synthetases (NRPS) similar to mycosubtilin ... |
204-555 |
9.23e-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: 57.88 E-value: 9.23e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228909 204 YTSGTTASPKGVVL-HHRGAY-IMALSNPLIWGMQDGavYLWTLPMFHCNGWCFPWSLAVLSG-------TSICLRQVTA 274
Cdd:cd05908 113 FSSGSTGDPKGVMLtHENLVHnMFAILNSTEWKTKDR--ILSWMPLTHDMGLIAFHLAPLIAGmnqylmpTRLFIRRPIL 190
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228909 275 keVYSMIAKYKVTHFCAAPVVLNAIVNAPKEDTILPLPHTVHVMTAGAAPPPSV------LFSMNQKGFR---VAHTYGL 345
Cdd:cd05908 191 --WLKKASEHKATIVSSPNFGYKYFLKTLKPEKANDWDLSSIRMILNGAEPIDYelchefLDHMSKYGLKrnaILPVYGL 268
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228909 346 SEtygpSTVCAWKPEWDSlpPETQAKLNARQGVRYTGMEQLDVIDTQ------TGKPVP-------------ADGKTAGE 406
Cdd:cd05908 269 AE----ASVGASLPKAQS--PFKTITLGRRHVTHGEPEPEVDKKDSEcltfveVGKPIDetdiricdednkiLPDGYIGH 342
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228909 407 IVFRGNMVMKGYLKNPEANKETF-AGGWFHSGDIAVKHpDNYIEIKDRSKDVIISGGENISSVEVENVVYHHPAVLEASV 485
Cdd:cd05908 343 IQIRGKNVTPGYYNNPEATAKVFtDDGWLKTGDLGFIR-NGRLVITGREKDIIFVNGQNVYPHDIERIAEELEGVELGRV 421
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 15228909 486 VA---RPDERWQESPCAFVTLKSDYEkhDQNKLAQDIMKFCREKlpAYWVPKSVV-FGPLPKTATGKIQKHILR 555
Cdd:cd05908 422 VAcgvNNSNTRNEEIFCFIEHRKSED--DFYPLGKKIKKHLNKR--GGWQINEVLpIRRIPKTTSGKVKRYELA 491
|
|
| alpha_am_amid |
TIGR03443 |
L-aminoadipate-semialdehyde dehydrogenase; Members of this protein family are ... |
405-551 |
9.94e-08 |
|
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: 55.07 E-value: 9.94e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228909 405 GEIVFRGNMVMKGYLKNPEANKETFAGGWF-----------------------------HSGDIAVKHPDNYIEIKDRSK 455
Cdd:TIGR03443 622 GEIYVRAGGLAEGYLGLPELNAEKFVNNWFvdpshwidldkennkperefwlgprdrlyRTGDLGRYLPDGNVECCGRAD 701
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228909 456 DVIISGGENISSVEVENVVYHHPAVLEASVVARPDErwQESPC---------------AFVTLKSDYEKHDQ-------- 512
Cdd:TIGR03443 702 DQVKIRGFRIELGEIDTHLSQHPLVRENVTLVRRDK--DEEPTlvsyivpqdksdeleEFKSEVDDEESSDPvvkgliky 779
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 15228909 513 NKLAQDIMKFCREKLPAYWVPKSVVfgPLPK---TATGKIQK 551
Cdd:TIGR03443 780 RKLIKDIREYLKKKLPSYAIPTVIV--PLKKlplNPNGKVDK 819
|
|
| PLN03051 |
PLN03051 |
acyl-activating enzyme; Provisional |
89-569 |
1.18e-07 |
|
acyl-activating enzyme; Provisional
Pssm-ID: 215552 [Multi-domain] Cd Length: 499 Bit Score: 54.44 E-value: 1.18e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228909 89 HFGVPMCGAVLNCVNIRLNAPTVAFLLSHSQSSVIMVdQEFFTLAEDSLRLMEEKAGSSFKRPLLI-VIGDHTCAPesln 167
Cdd:PLN03051 11 YLAIVLAGCVVVSVADSFSAKEIATRLDISGAKGVFT-QDVVLRGGRALPLYSKVVEAAPAKAIVLpAAGEPVAVP---- 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228909 168 raLSKGAIEYEDFLATG------DPNYPWQPPADEWQSIALGYTSGTTASPKGVVLHHRGAYIMALSNPLIWGMQDGAVY 241
Cdd:PLN03051 86 --LREQDLSWCDFLGVAaaqgsvGGNEYSPVYAPVESVTNILFSSGTTGEPKAIPWTHLSPLRCASDGWAHMDIQPGDVV 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228909 242 LWTLPMfhcnGWCF-PWSL--AVLSGTSICLRQ--VTAKEVYSMIAKYKVTHFCAAPVVLNAIVNAPKEDTILP-LPHT- 314
Cdd:PLN03051 164 CWPTNL----GWMMgPWLLysAFLNGATLALYGgaPLGRGFGKFVQDAGVTVLGLVPSIVKAWRHTGAFAMEGLdWSKLr 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228909 315 VHVMTAGAAPPPSVLFSMNQKGFR--VAHTYG---LSETYGPSTVCawkpewdsLPPETQAKLNARQGVRYtgmeqldVI 389
Cdd:PLN03051 240 VFASTGEASAVDDVLWLSSVRGYYkpVIEYCGgteLASGYISSTLL--------QPQAPGAFSTASLGTRF-------VL 304
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228909 390 DTQTGKPVPADGKTAGEIVFRgnMVMKGY---LKNPEANKETFAGGWFHS---------GDIAVKHPDNYIEIKDRSKDV 457
Cdd:PLN03051 305 LNDNGVPYPDDQPCVGEVALA--PPMLGAsdrLLNADHDKVYYKGMPMYGskgmplrrhGDIMKRTPGGYFCVQGRADDT 382
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228909 458 IISGGENISSVEVENVVYH-HPAVLEASVVAR------PDERWqespcAFVTLKSDYEKHDQNKLAQDIMKF---CREKL 527
Cdd:PLN03051 383 MNLGGIKTSSVEIERACDRaVAGIAETAAVGVappdggPELLV-----IFLVLGEEKKGFDQARPEALQKKFqeaIQTNL 457
|
490 500 510 520
....*....|....*....|....*....|....*....|...
gi 15228909 528 -PAYWVPKSVVFGPLPKTATGKIQKHILRTKAKEMGPvPRSRL 569
Cdd:PLN03051 458 nPLFKVSRVKIVPELPRNASNKLLRRVLRDQLKKELS-GRSKL 499
|
|
| AFD_CAR-like |
cd17632 |
adenylation domain of carboxylic acid reductase (CAR); This family contains the adenylation ... |
49-252 |
6.10e-07 |
|
adenylation domain of carboxylic acid reductase (CAR); This family contains the adenylation domain of carboxylic acid reductase enzymes (CARs), and performs an equivalent function to that of the ANL superfamily of adenylating enzymes. It takes a carboxylic acid substrate and ATP, and produces an AMP-acyl phosphoester intermediate, releasing pyrophosphate. Kinetic analysis using various substrates shows that this enzyme has a broad but similar substrate specificity, preferring electron-rich acids. This suggests that attack by the carboxylate on the alpha-phosphate of adenosine triphosphate (ATP) is the step that determines the substrate specificity and reaction kinetics. CAR is an important enzyme for use as a biocatalyst providing regiospecific route to aldehydes from their respective carboxylic acids.
Pssm-ID: 341287 [Multi-domain] Cd Length: 588 Bit Score: 52.46 E-value: 6.10e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228909 49 TWRQTYDRCRRLASAL-ADRSIGPGSTVAIIAPNIPAMyeahfgvpmcgAVLNCVNIRLNAPTV-----------AFLLS 116
Cdd:cd17632 69 TYAELWERVGAVAAAHdPEQPVRPGDFVAVLGFTSPDY-----------ATVDLALTRLGAVSVplqagasaaqlAPILA 137
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228909 117 HSQSSVIMVDQEFFTLAEdslrlmeEKAGSSFKRPLLIV------IGDHTCAPESLNRALSKGAIEYEDFLATGD----- 185
Cdd:cd17632 138 ETEPRLLAVSAEHLDLAV-------EAVLEGGTPPRLVVfdhrpeVDAHRAALESARERLAAVGIPVTTLTLIAVrgrdl 210
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 15228909 186 PNYPWQPPADEWQSIA-LGYTSGTTASPKGVVLHHRGAYIMAL-SNPLIWGMQDGAVYLWTLPMFHCNG 252
Cdd:cd17632 211 PPAPLFRPEPDDDPLAlLIYTSGSTGTPKGAMYTERLVATFWLkVSSIQDIRPPASITLNFMPMSHIAG 279
|
|
| A_NRPS_alphaAR |
cd17647 |
Alpha-aminoadipate reductase; This family contains L-2-aminoadipate reductase, also known as ... |
405-554 |
6.10e-07 |
|
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: 52.13 E-value: 6.10e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228909 405 GEIVFRGNMVMKGYLKNPEANKETFAGGWF-----------------------------HSGDIAVKHPDNYIEIKDRSK 455
Cdd:cd17647 316 GEIYVRAGGLAEGYRGLPELNKEKFVNNWFvepdhwnyldkdnnepwrqfwlgprdrlyRTGDLGRYLPNGDCECCGRAD 395
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228909 456 DVIISGGENISSVEVENVVYHHPAVLEASVVARPDERWQ-----------ESPCAFVTLKSDYEKHDQN----------- 513
Cdd:cd17647 396 DQVKIRGFRIELGEIDTHISQHPLVRENITLVRRDKDEEptlvsyivprfDKPDDESFAQEDVPKEVSTdpivkgligyr 475
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 15228909 514 KLAQDIMKFCREKLPAYWVPKS-VVFGPLPKTATGKIQKHIL 554
Cdd:cd17647 476 KLIKDIREFLKKRLASYAIPSLiVVLDKLPLNPNGKVDKPKL 517
|
|
| PLN03052 |
PLN03052 |
acetate--CoA ligase; Provisional |
388-569 |
6.91e-07 |
|
acetate--CoA ligase; Provisional
Pssm-ID: 215553 [Multi-domain] Cd Length: 728 Bit Score: 52.39 E-value: 6.91e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228909 388 VIDTQTGKPVPADGKTAGEIVFRGNMVMKGY-LKNPEANKETFAGGWFHSGDIAVKHPD-------NYIEIKDRSKDVII 459
Cdd:PLN03052 537 FILDDSGNPYPDDAPCTGELALFPLMFGASStLLNADHYKVYFKGMPVFNGKILRRHGDifertsgGYYRAHGRADDTMN 616
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228909 460 SGGENISSVEVENVVYH-HPAVLE-ASVVARPDERWQESPCAFVTLKSDYEKHDQNKLAQdiMKFCRE---KL-PAYWVP 533
Cdd:PLN03052 617 LGGIKVSSVEIERVCNAaDESVLEtAAIGVPPPGGGPEQLVIAAVLKDPPGSNPDLNELK--KIFNSAiqkKLnPLFKVS 694
|
170 180 190
....*....|....*....|....*....|....*.
gi 15228909 534 KSVVFGPLPKTATGKIQKHILRTKAKEMgpVPRSRL 569
Cdd:PLN03052 695 AVVIVPSFPRTASNKVMRRVLRQQLAQE--LSRSKL 728
|
|
| PRK05691 |
PRK05691 |
peptide synthase; Validated |
202-554 |
1.12e-06 |
|
peptide synthase; Validated
Pssm-ID: 235564 [Multi-domain] Cd Length: 4334 Bit Score: 52.09 E-value: 1.12e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228909 202 LGYTSGTTASPKGVVLHHrGAYIMALSNPL-IWGMQDGAVYLwtlpmfHCNGWCFPWS-----LAVLSGTSICLR---QV 272
Cdd:PRK05691 2338 LIYTSGSTGKPKGVVVSH-GEIAMHCQAVIeRFGMRADDCEL------HFYSINFDAAserllVPLLCGARVVLRaqgQW 2410
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228909 273 TAKEVYSMIAKYKVTHFCAAPVVLNAIVN-APKEDTILPLPHtvhVMTAGAAPPPSVLFSMNQkGFRVAHTYglsETYGP 351
Cdd:PRK05691 2411 GAEEICQLIREQQVSILGFTPSYGSQLAQwLAGQGEQLPVRM---CITGGEALTGEHLQRIRQ-AFAPQLFF---NAYGP 2483
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228909 352 S-TVCAwkpEWDSLPPETQAKLNARQGV-RYTGMEQLDVIDTQTGkPVPADGktAGEIVFRGNMVMKGYLKNPEANKETF 429
Cdd:PRK05691 2484 TeTVVM---PLACLAPEQLEEGAASVPIgRVVGARVAYILDADLA-LVPQGA--TGELYVGGAGLAQGYHDRPGLTAERF 2557
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228909 430 --------AGGWFHSGDIAVKHPDNYIEIKDRSKDVIISGGENISSVEVENVVYHHPAVLEASVVARPDERWQESPCAFV 501
Cdd:PRK05691 2558 vadpfaadGGRLYRTGDLVRLRADGLVEYVGRIDHQVKIRGFRIELGEIESRLLEHPAVREAVVLALDTPSGKQLAGYLV 2637
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....
gi 15228909 502 TLKSDYEKHDQNKLAQDIMKFCREKLPAYWVPKS-VVFGPLPKTATGKIQKHIL 554
Cdd:PRK05691 2638 SAVAGQDDEAQAALREALKAHLKQQLPDYMVPAHlILLDSLPLTANGKLDRRAL 2691
|
|
| PRK12476 |
PRK12476 |
putative fatty-acid--CoA ligase; Provisional |
47-485 |
1.39e-06 |
|
putative fatty-acid--CoA ligase; Provisional
Pssm-ID: 171527 [Multi-domain] Cd Length: 612 Bit Score: 51.28 E-value: 1.39e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228909 47 EYTWRQTYDRCRRLASALaDRSIGPGSTVAIIAPN----IPAMYEA----HFGVPMCGAVLNCVNIRLNAptvafLLSHS 118
Cdd:PRK12476 68 ELTWTQLGVRLRAVGARL-QQVAGPGDRVAILAPQgidyVAGFFAAikagTIAVPLFAPELPGHAERLDT-----ALRDA 141
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228909 119 QSSVIMVDQEFFTLAEDSLRLMeekagSSFKRPLLIVIGDhtcAPESLNralskgaieyEDF----LATGDPNYpwqppa 194
Cdd:PRK12476 142 EPTVVLTTTAAAEAVEGFLRNL-----PRLRRPRVIAIDA---IPDSAG----------ESFvpveLDTDDVSH------ 197
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228909 195 dewqsiaLGYTSGTTASPKGVVLHHRGAYI----MALS-NPLIWGMQDGAvylWtLPMFHCNGWC---FPW----SLAVL 262
Cdd:PRK12476 198 -------LQYTSGSTRPPVGVEITHRAVGTnlvqMILSiDLLDRNTHGVS---W-LPLYHDMGLSmigFPAvyggHSTLM 266
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228909 263 SGTSICLRQVTAKEVYSMIAKYKVThFCAAP---VVLNAIVNAPKEDTILPLPHTVhvMTAGAAPppsvlFSMNQ-KGFR 338
Cdd:PRK12476 267 SPTAFVRRPQRWIKALSEGSRTGRV-VTAAPnfaYEWAAQRGLPAEGDDIDLSNVV--LIIGSEP-----VSIDAvTTFN 338
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228909 339 VAHT-YGLsetygPSTvcAWKPEW---------DSLPPETQA--------KLNARQGVRYTG---------------MEQ 385
Cdd:PRK12476 339 KAFApYGL-----PRT--AFKPSYgiaeatlfvATIAPDAEPsvvyldreQLGAGRAVRVAAdapnavahvscgqvaRSQ 411
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228909 386 LDVI-DTQTGKPVPaDGkTAGEIVFRGNMVMKGYLKNPEANKETF-------------AGG------WFHSGDIAVkHPD 445
Cdd:PRK12476 412 WAVIvDPDTGAELP-DG-EVGEIWLHGDNIGRGYWGRPEETERTFgaklqsrlaegshADGaaddgtWLRTGDLGV-YLD 488
|
490 500 510 520
....*....|....*....|....*....|....*....|
gi 15228909 446 NYIEIKDRSKDVIISGGENissvevenvvyHHPAVLEASV 485
Cdd:PRK12476 489 GELYITGRIADLIVIDGRN-----------HYPQDIEATV 517
|
|
| PRK05691 |
PRK05691 |
peptide synthase; Validated |
44-557 |
1.85e-06 |
|
peptide synthase; Validated
Pssm-ID: 235564 [Multi-domain] Cd Length: 4334 Bit Score: 51.32 E-value: 1.85e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228909 44 GSREYTWRQTYDRCRRLASALADRSiGPGSTVAIIAPNIPAMYEAHFGVPMCGAvlncvnIRLNAPTVAFLLSHSQSSV- 122
Cdd:PRK05691 37 EGVVLSYRDLDLRARTIAAALQARA-SFGDRAVLLFPSGPDYVAAFFGCLYAGV------IAVPAYPPESARRHHQERLl 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228909 123 -IMVDQE---FFTLAE--DSLRLMEEKAGSSFKrPLLIVigdhtcapESLNRALSKGaieyedflatgdpnypWQPPADE 196
Cdd:PRK05691 110 sIIADAEprlLLTVADlrDSLLQMEELAAANAP-ELLCV--------DTLDPALAEA----------------WQEPALQ 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228909 197 WQSIA-LGYTSGTTASPKGVVLHH-----------RGAYIMAlsNPliwgmqDGAVYLWtLPMFHCNGWCFPWSLAVLSG 264
Cdd:PRK05691 165 PDDIAfLQYTSGSTALPKGVQVSHgnlvaneqlirHGFGIDL--NP------DDVIVSW-LPLYHDMGLIGGLLQPIFSG 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228909 265 TSICLrqvtakevysMIAKYkvthFCAAPVV-LNAIvnAPKEDTILPLPHTVHVMTAgAAPPPSVLFSMNQKGFRVAhtY 343
Cdd:PRK05691 236 VPCVL----------MSPAY----FLERPLRwLEAI--SEYGGTISGGPDFAYRLCS-ERVSESALERLDLSRWRVA--Y 296
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228909 344 GLSETYGPSTV---------CAWKPewDSLPPE---TQAKLNARQGVRYTGMEQLDViDTQT---GKPVPADGKT----- 403
Cdd:PRK05691 297 SGSEPIRQDSLerfaekfaaCGFDP--DSFFASyglAEATLFVSGGRRGQGIPALEL-DAEAlarNRAEPGTGSVlmscg 373
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228909 404 -----------------------AGEIVFRGNMVMKGYLKNPEANKETF---AG-GWFHSGDIAVKHpDNYIEIKDRSKD 456
Cdd:PRK05691 374 rsqpghavlivdpqslevlgdnrVGEIWASGPSIAHGYWRNPEASAKTFvehDGrTWLRTGDLGFLR-DGELFVTGRLKD 452
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228909 457 VIISGGENISSVEVENVVYHHPAVLEASVVA--RPDERWQESpcafVTLKSDYEKHDQNKL-AQDIMKFCREKLP-AYW- 531
Cdd:PRK05691 453 MLIVRGHNLYPQDIEKTVEREVEVVRKGRVAafAVNHQGEEG----IGIAAEISRSVQKILpPQALIKSIRQAVAeACQe 528
|
570 580
....*....|....*....|....*....
gi 15228909 532 VPKSVVF---GPLPKTATGKIQKHILRTK 557
Cdd:PRK05691 529 APSVVLLlnpGALPKTSSGKLQRSACRLR 557
|
|
| PRK05850 |
PRK05850 |
acyl-CoA synthetase; Validated |
192-549 |
7.65e-06 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 235624 [Multi-domain] Cd Length: 578 Bit Score: 48.79 E-value: 7.65e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228909 192 PPADEWQSIA-LGYTSGTTASPKGVVLHHRGAY-----IMA--LSNPLIWGMQDGAVYLWtLPMFH----CNGWCFPwsl 259
Cdd:PRK05850 154 ARPRDLPSTAyLQYTSGSTRTPAGVMVSHRNVIanfeqLMSdyFGDTGGVPPPDTTVVSW-LPFYHdmglVLGVCAP--- 229
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228909 260 aVLSG-----TS-ICLRQVTAKEVySMIAKYKVThFCAAPvvlN-----AIVNAPKEDTI-LPLPHTVHVMTAGAAPPPS 327
Cdd:PRK05850 230 -ILGGcpavlTSpVAFLQRPARWM-QLLASNPHA-FSAAP---NfafelAVRKTSDDDMAgLDLGGVLGIISGSERVHPA 303
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228909 328 VLFSMNQkgfRVAH----------TYGLSEtygpSTVCAWKPEWDSlPPET-----------QAKLNARQG----VRYtG 382
Cdd:PRK05850 304 TLKRFAD---RFAPfnlretairpSYGLAE----ATVYVATREPGQ-PPESvrfdyeklsagHAKRCETGGgtplVSY-G 374
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228909 383 MEQ---LDVIDTQTGKPVPADgkTAGEIVFRGNMVMKGYLKNPEANKETF------------AGGWFHSGDIAVKHPDNY 447
Cdd:PRK05850 375 SPRsptVRIVDPDTCIECPAG--TVGEIWVHGDNVAAGYWQKPEETERTFgatlvdpspgtpEGPWLRTGDLGFISEGEL 452
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228909 448 IeIKDRSKDVIISGGENissvevenvvyHHPAVLEASV----------VARPDERwQESPCAFVTLKsdyEKHDQNKLAQ 517
Cdd:PRK05850 453 F-IVGRIKDLLIVDGRN-----------HYPDDIEATIqeitggrvaaISVPDDG-TEKLVAIIELK---KRGDSDEEAM 516
|
410 420 430 440
....*....|....*....|....*....|....*....|..
gi 15228909 518 DIMKFCREKLPAYwVPKS-------VVF---GPLPKTATGKI 549
Cdd:PRK05850 517 DRLRTVKREVTSA-ISKShglsvadLVLvapGSIPITTSGKI 557
|
|
| PRK03584 |
PRK03584 |
acetoacetate--CoA ligase; |
29-550 |
9.63e-05 |
|
acetoacetate--CoA ligase;
Pssm-ID: 235134 [Multi-domain] Cd Length: 655 Bit Score: 45.17 E-value: 9.63e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228909 29 DRAAVVHptrKSVIHGSREYTWRQTYDRCRRLASALADRSIGPGSTVAIIAPNIP----AMYEA------------HFGV 92
Cdd:PRK03584 99 DRPAIIF---RGEDGPRRELSWAELRRQVAALAAALRALGVGPGDRVAAYLPNIPetvvAMLATaslgaiwsscspDFGV 175
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228909 93 PmcgAVLNcvniRLN--APTVafllshsqssVIMVDQEFF---------TLAE-----DSLRlmeekagssfkrpLLIVI 156
Cdd:PRK03584 176 Q---GVLD----RFGqiEPKV----------LIAVDGYRYggkafdrraKVAElraalPSLE-------------HVVVV 225
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228909 157 GDHTCAPESlnrALSKGAIEYEDFLATGDPnypwQPPADEWqsiaLG--------YTSGTTASPKGVVLHHRGAYIMAL- 227
Cdd:PRK03584 226 PYLGPAAAA---AALPGALLWEDFLAPAEA----AELEFEP----VPfdhplwilYSSGTTGLPKCIVHGHGGILLEHLk 294
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228909 228 SNPLIWGMQDGAVYLWtlpmFHCNGWCFpWSLAV---LSGTSICLrqvtakevY-------------SMIAKYKVTHFCA 291
Cdd:PRK03584 295 ELGLHCDLGPGDRFFW----YTTCGWMM-WNWLVsglLVGATLVL--------YdgspfypdpnvlwDLAAEEGVTVFGT 361
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228909 292 APVVLNAIVNA---PKEDtiLPLPHTVHVMTAGAAPPPSvlfsmnqkGFR-----VAHTYGLSETYGPSTVCA------- 356
Cdd:PRK03584 362 SAKYLDACEKAglvPGET--HDLSALRTIGSTGSPLPPE--------GFDwvyehVKADVWLASISGGTDICScfvggnp 431
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228909 357 WKPEWdslPPETQAklnarqgvRYTGMEqLDVIDTQtGKPVpADGKtaGEIVFRGNM-VMKGYLKNPEANK-------ET 428
Cdd:PRK03584 432 LLPVY---RGEIQC--------RGLGMA-VEAWDED-GRPV-VGEV--GELVCTKPFpSMPLGFWNDPDGSryrdayfDT 495
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228909 429 FAGGWFHsGDiavkhpdnYIEIKD--------RSKDVIISGGENISSVEVENVVYHHPAVLEASVVARPDERWQESPCAF 500
Cdd:PRK03584 496 FPGVWRH-GD--------WIEITEhggvviygRSDATLNRGGVRIGTAEIYRQVEALPEVLDSLVIGQEWPDGDVRMPLF 566
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|.
gi 15228909 501 VTLKSDYEKHDQnkLAQDIMKFCREKLPAYWVPKSVVFGP-LPKTATGKIQ 550
Cdd:PRK03584 567 VVLAEGVTLDDA--LRARIRTTIRTNLSPRHVPDKIIAVPdIPRTLSGKKV 615
|
|
| PRK08043 |
PRK08043 |
bifunctional acyl-ACP--phospholipid O-acyltransferase/long-chain-fatty-acid--ACP ligase; |
396-560 |
1.13e-03 |
|
bifunctional acyl-ACP--phospholipid O-acyltransferase/long-chain-fatty-acid--ACP ligase;
Pssm-ID: 181207 [Multi-domain] Cd Length: 718 Bit Score: 42.00 E-value: 1.13e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228909 396 PVP--ADGktaGEIVFRGNMVMKGYLK-------------NPEANKETfagGWFHSGDIAVKHPDNYIEIKDRSKDVIIS 460
Cdd:PRK08043 546 SVPgiEQG---GRLQLKGPNIMNGYLRvekpgvlevptaeNARGEMER---GWYDTGDIVRFDEQGFVQIQGRAKRFAKI 619
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228909 461 GGENISSVEVENVVYHHPAVLEASVVARPDERWQESPCAFVTlksdyekhdQNKLAQD-IMKFCREK-LPAYWVPKSV-V 537
Cdd:PRK08043 620 AGEMVSLEMVEQLALGVSPDKQHATAIKSDASKGEALVLFTT---------DSELTREkLQQYAREHgVPELAVPRDIrY 690
|
170 180
....*....|....*....|...
gi 15228909 538 FGPLPKTATGKIQKHILRTKAKE 560
Cdd:PRK08043 691 LKQLPLLGSGKPDFVTLKSMVDE 713
|
|
| |
