|
Name |
Accession |
Description |
Interval |
E-value |
| Firefly_Luc |
cd17642 |
insect luciferase, similar to plant 4-coumarate: CoA ligases; This family contains insect ... |
8-539 |
0e+00 |
|
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: 1060.60 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1216630836 8 IKKGPAPFYPLEDGTAGEQLHKAMKRYALVPGTIAFTDAHIEVDITYAEYFEMSVRLAEAMKRYGLNTNHRIVVCSENSL 87
Cdd:cd17642 1 IIVGPGPFYPLEDGTAGEQLHKAMKRYASVPGTIAFTDAHTGVNYSYAEYLEMSVRLAEALKKYGLKQNDRIAVCSENSL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1216630836 88 QFFMPVLGALFIGVAVAPANDIYNERELLNSMGISQPTVVFVSKKGLQKILNVQKKLPIIQKIIIMDSKTDYQGFQSMYT 167
Cdd:cd17642 81 QFFLPVIAGLFIGVGVAPTNDIYNERELDHSLNISKPTIVFCSKKGLQKVLNVQKKLKIIKTIIILDSKEDYKGYQCLYT 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1216630836 168 FVTSHLPPGFNEYDFVPESFDRDKTIALIMNSSGSTGLPKGVALPHRTACVRFSHARDPIFGNQIIPDTAILSVVPFHHG 247
Cdd:cd17642 161 FITQNLPPGFNEYDFKPPSFDRDEQVALIMNSSGSTGLPKGVQLTHKNIVARFSHARDPIFGNQIIPDTAILTVIPFHHG 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1216630836 248 FGMFTTLGYLICGFRVVLMYRFEEELFLRSLQDYKIQSALLVPTLFSFFAKSTLIDKYDLSNLHEIASGGAPLSKEVGEA 327
Cdd:cd17642 241 FGMFTTLGYLICGFRVVLMYKFEEELFLRSLQDYKVQSALLVPTLFAFFAKSTLVDKYDLSNLHEIASGGAPLSKEVGEA 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1216630836 328 VAKRFHLPGIRQGYGLTETTSAILITPEGDDKPGAVGKVVPFFEAKVVDLDTGKTLGVNQRGELCVRGPMIMSGYVNNPE 407
Cdd:cd17642 321 VAKRFKLPGIRQGYGLTETTSAILITPEGDDKPGAVGKVVPFFYAKVVDLDTGKTLGPNERGELCVKGPMIMKGYVNNPE 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1216630836 408 ATNALIDKDGWLHSGDIAYWDEDEHFFIVDRLKSLIKYKGYQVAPAELESILLQHPNIFDAGVAGLPDDDAGELPAAVVV 487
Cdd:cd17642 401 ATKALIDKDGWLHSGDIAYYDEDGHFFIVDRLKSLIKYKGYQVPPAELESILLQHPKIFDAGVAGIPDEDAGELPAAVVV 480
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|..
gi 1216630836 488 LEHGKTMTEKEIVDYVASQVTTAKKLRGGVVFVDEVPKGLTGKLDARKIREI 539
Cdd:cd17642 481 LEAGKTMTEKEVMDYVASQVSTAKRLRGGVKFVDEVPKGLTGKIDRRKIREI 532
|
|
| Firefly_Luc_like |
cd05911 |
Firefly luciferase of light emitting insects and 4-Coumarate-CoA Ligase (4CL); This family ... |
42-531 |
0e+00 |
|
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: 641.96 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1216630836 42 AFTDAHIEVDITYAEYFEMSVRLAEAMKRYGLNTNHRIVVCSENSLQFFMPVLGALFIGVAVAPANDIYNERELLNSMGI 121
Cdd:cd05911 1 AQIDADTGKELTYAQLRTLSRRLAAGLRKLGLKKGDVVGIISPNSTYYPPVFLGCLFAGGIFSAANPIYTADELAHQLKI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1216630836 122 SQPTVVFVSKKGLQKILNVQKKLPIIQKIIIMDSKTDYQGFQSMYTFVTShlppGFNEYDFVPESFDRDKTIALIMNSSG 201
Cdd:cd05911 81 SKPKVIFTDPDGLEKVKEAAKELGPKDKIIVLDDKPDGVLSIEDLLSPTL----GEEDEDLPPPLKDGKDDTAAILYSSG 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1216630836 202 STGLPKGVALPHRTACVRFSHARDPIFGNqIIPDTAILSVVPFHHGFGMFTTLGYLICGFRVVLMYRFEEELFLRSLQDY 281
Cdd:cd05911 157 TTGLPKGVCLSHRNLIANLSQVQTFLYGN-DGSNDVILGFLPLYHIYGLFTTLASLLNGATVIIMPKFDSELFLDLIEKY 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1216630836 282 KIQSALLVPTLFSFFAKSTLIDKYDLSNLHEIASGGAPLSKEVGEAVAKRFHLPGIRQGYGLTETTSAILITPEGDDKPG 361
Cdd:cd05911 236 KITFLYLVPPIAAALAKSPLLDKYDLSSLRVILSGGAPLSKELQELLAKRFPNATIKQGYGMTETGGILTVNPDGDDKPG 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1216630836 362 AVGKVVPFFEAKVVDLDTGKTLGVNQRGELCVRGPMIMSGYVNNPEATNALIDKDGWLHSGDIAYWDEDEHFFIVDRLKS 441
Cdd:cd05911 316 SVGRLLPNVEAKIVDDDGKDSLGPNEPGEICVRGPQVMKGYYNNPEATKETFDEDGWLHTGDIGYFDEDGYLYIVDRKKE 395
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1216630836 442 LIKYKGYQVAPAELESILLQHPNIFDAGVAGLPDDDAGELPAAVVVLEHGKTMTEKEIVDYVASQVTTAKKLRGGVVFVD 521
Cdd:cd05911 396 LIKYKGFQVAPAELEAVLLEHPGVADAAVIGIPDEVSGELPRAYVVRKPGEKLTEKEVKDYVAKKVASYKQLRGGVVFVD 475
|
490
....*....|
gi 1216630836 522 EVPKGLTGKL 531
Cdd:cd05911 476 EIPKSASGKI 485
|
|
| 4CL |
cd05904 |
4-Coumarate-CoA Ligase (4CL); 4-Coumarate:coenzyme A ligase is a key enzyme in the ... |
38-530 |
2.06e-154 |
|
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: 451.30 E-value: 2.06e-154
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1216630836 38 PGTIAFTDAHIEVDITYAEYFEMSVRLAEAMKRYGLNTNHRIVVCSENSLQFFMPVLGALFIGVAVAPANDIYNERELLN 117
Cdd:cd05904 19 PSRPALIDAATGRALTYAELERRVRRLAAGLAKRGGRKGDVVLLLSPNSIEFPVAFLAVLSLGAVVTTANPLSTPAEIAK 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1216630836 118 SMGISQPTVVFVSKKGLQKILnvqkklPIIQKIIIMDSKTDYQGFQSMYTFVTSHLPPgfneydfvPESFDRDKTIALIM 197
Cdd:cd05904 99 QVKDSGAKLAFTTAELAEKLA------SLALPVVLLDSAEFDSLSFSDLLFEADEAEP--------PVVVIKQDDVAALL 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1216630836 198 NSSGSTGLPKGVALPHR--TACVRFSHARdpiFGNQIIPDTAILSVVPFHH--GFGMFTtLGYLICGFRVVLMYRFEEEL 273
Cdd:cd05904 165 YSSGTTGRSKGVMLTHRnlIAMVAQFVAG---EGSNSDSEDVFLCVLPMFHiyGLSSFA-LGLLRLGATVVVMPRFDLEE 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1216630836 274 FLRSLQDYKIQSALLVPTLFSFFAKSTLIDKYDLSNLHEIASGGAPLSKEVGEAVAKRFHLPGIRQGYGLTETTSAILIT 353
Cdd:cd05904 241 LLAAIERYKVTHLPVVPPIVLALVKSPIVDKYDLSSLRQIMSGAAPLGKELIEAFRAKFPNVDLGQGYGMTESTGVVAMC 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1216630836 354 P---EGDDKPGAVGKVVPFFEAKVVDLDTGKTLGVNQRGELCVRGPMIMSGYVNNPEATNALIDKDGWLHSGDIAYWDED 430
Cdd:cd05904 321 FapeKDRAKYGSVGRLVPNVEAKIVDPETGESLPPNQTGELWIRGPSIMKGYLNNPEATAATIDKEGWLHTGDLCYIDED 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1216630836 431 EHFFIVDRLKSLIKYKGYQVAPAELESILLQHPNIFDAGVAGLPDDDAGELPAAVVVLEHGKTMTEKEIVDYVASQVTTA 510
Cdd:cd05904 401 GYLFIVDRLKELIKYKGFQVAPAELEALLLSHPEILDAAVIPYPDEEAGEVPMAFVVRKPGSSLTEDEIMDFVAKQVAPY 480
|
490 500
....*....|....*....|
gi 1216630836 511 KKLRgGVVFVDEVPKGLTGK 530
Cdd:cd05904 481 KKVR-KVAFVDAIPKSPSGK 499
|
|
| MenE/FadK |
COG0318 |
O-succinylbenzoic acid-CoA ligase MenE or related acyl-CoA synthetase (AMP-forming) [Lipid ... |
24-543 |
3.54e-127 |
|
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: 379.54 E-value: 3.54e-127
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1216630836 24 GEQLHKAMKRYalvPGTIAFTDAhiEVDITYAEYFEMSVRLAEAMKRYGLNTNHRIVVCSENSLQFFMPVLGALFIGVAV 103
Cdd:COG0318 2 ADLLRRAAARH---PDRPALVFG--GRRLTYAELDARARRLAAALRALGVGPGDRVALLLPNSPEFVVAFLAALRAGAVV 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1216630836 104 APANDIYNERELLNSMGISQPTVVFVskkglqkilnvqkklpiiqkiiimdsktdyqgfqsmytfvtshlppgfneydfv 183
Cdd:COG0318 77 VPLNPRLTAEELAYILEDSGARALVT------------------------------------------------------ 102
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1216630836 184 pesfdrdktiALIMNSSGSTGLPKGVALPHRTACvrfSHARDPIFGNQIIPDTAILSVVPFHHGFGM-FTTLGYLICGFR 262
Cdd:COG0318 103 ----------ALILYTSGTTGRPKGVMLTHRNLL---ANAAAIAAALGLTPGDVVLVALPLFHVFGLtVGLLAPLLAGAT 169
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1216630836 263 VVLMYRFEEELFLRSLQDYKIQSALLVPTLFSFFAKSTLIDKYDLSNLHEIASGGAPLSKEVGEAVAKRFHLPgIRQGYG 342
Cdd:COG0318 170 LVLLPRFDPERVLELIERERVTVLFGVPTMLARLLRHPEFARYDLSSLRLVVSGGAPLPPELLERFEERFGVR-IVEGYG 248
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1216630836 343 LTETTSAILITPE--GDDKPGAVGKVVPFFEAKVVDlDTGKTLGVNQRGELCVRGPMIMSGYVNNPEATNALIdKDGWLH 420
Cdd:COG0318 249 LTETSPVVTVNPEdpGERRPGSVGRPLPGVEVRIVD-EDGRELPPGEVGEIVVRGPNVMKGYWNDPEATAEAF-RDGWLR 326
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1216630836 421 SGDIAYWDEDEHFFIVDRLKSLIKYKGYQVAPAELESILLQHPNIFDAGVAGLPDDDAGELPAAVVVLEHGKTMTEKEIV 500
Cdd:COG0318 327 TGDLGRLDEDGYLYIVGRKKDMIISGGENVYPAEVEEVLAAHPGVAEAAVVGVPDEKWGERVVAFVVLRPGAELDAEELR 406
|
490 500 510 520
....*....|....*....|....*....|....*....|...
gi 1216630836 501 DYVASQVTTAKKLRgGVVFVDEVPKGLTGKLDARKIREILIKA 543
Cdd:COG0318 407 AFLRERLARYKVPR-RVEFVDELPRTASGKIDRRALRERYAAG 448
|
|
| PLN02246 |
PLN02246 |
4-coumarate--CoA ligase |
53-540 |
2.11e-119 |
|
4-coumarate--CoA ligase
Pssm-ID: 215137 [Multi-domain] Cd Length: 537 Bit Score: 362.76 E-value: 2.11e-119
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1216630836 53 TYAEYFEMSVRLAEAMKRYGLNTNHRIVVCSENSLQFFMPVLGALFIGVAVAPANDIYNERELLNSMGISQPTVVFVSKK 132
Cdd:PLN02246 52 TYADVELLSRRVAAGLHKLGIRQGDVVMLLLPNCPEFVLAFLGASRRGAVTTTANPFYTPAEIAKQAKASGAKLIITQSC 131
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1216630836 133 GLQKILNVQKKLPIiqKIIIMDSKTDyqGFQSMYTFVTShlppgfNEYDFVPESFDRDKTIALIMnSSGSTGLPKGVALP 212
Cdd:PLN02246 132 YVDKLKGLAEDDGV--TVVTIDDPPE--GCLHFSELTQA------DENELPEVEISPDDVVALPY-SSGTTGLPKGVMLT 200
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1216630836 213 HRTACVRFSHARD---PIFGnqIIPDTAILSVVPFHHGFGMFTTLgylICGFRV----VLMYRFEEELFLRSLQDYKIQS 285
Cdd:PLN02246 201 HKGLVTSVAQQVDgenPNLY--FHSDDVILCVLPMFHIYSLNSVL---LCGLRVgaaiLIMPKFEIGALLELIQRHKVTI 275
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1216630836 286 ALLVPTLFSFFAKSTLIDKYDLSNLHEIASGGAPLSKEVGEAVAKRFHLPGIRQGYGLTETTSAILI------TPEgDDK 359
Cdd:PLN02246 276 APFVPPIVLAIAKSPVVEKYDLSSIRMVLSGAAPLGKELEDAFRAKLPNAVLGQGYGMTEAGPVLAMclafakEPF-PVK 354
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1216630836 360 PGAVGKVVPFFEAKVVDLDTGKTLGVNQRGELCVRGPMIMSGYVNNPEATNALIDKDGWLHSGDIAYWDEDEHFFIVDRL 439
Cdd:PLN02246 355 SGSCGTVVRNAELKIVDPETGASLPRNQPGEICIRGPQIMKGYLNDPEATANTIDKDGWLHTGDIGYIDDDDELFIVDRL 434
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1216630836 440 KSLIKYKGYQVAPAELESILLQHPNIFDAGVAGLPDDDAGELPAAVVVLEHGKTMTEKEIVDYVASQVTTAKKLRgGVVF 519
Cdd:PLN02246 435 KELIKYKGFQVAPAELEALLISHPSIADAAVVPMKDEVAGEVPVAFVVRSNGSEITEDEIKQFVAKQVVFYKRIH-KVFF 513
|
490 500
....*....|....*....|.
gi 1216630836 520 VDEVPKGLTGKLDARKIREIL 540
Cdd:PLN02246 514 VDSIPKAPSGKILRKDLRAKL 534
|
|
| AFD_class_I |
cd04433 |
Adenylate forming domain, Class I, also known as the ANL superfamily; This family is known as ... |
192-532 |
1.54e-115 |
|
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: 345.81 E-value: 1.54e-115
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1216630836 192 TIALIMNSSGSTGLPKGVALPHRTACVRFSHARDPIFGNqiiPDTAILSVVPFHHGFGMFTTLGYLICGFRVVLMYRFEE 271
Cdd:cd04433 1 DPALILYTSGTTGKPKGVVLSHRNLLAAAAALAASGGLT---EGDVFLSTLPLFHIGGLFGLLGALLAGGTVVLLPKFDP 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1216630836 272 ELFLRSLQDYKIQSALLVPTLFSFFAKSTLIDKYDLSNLHEIASGGAPLSKEVGEAVAKRFHLPgIRQGYGLTETTSAIL 351
Cdd:cd04433 78 EAALELIEREKVTILLGVPTLLARLLKAPESAGYDLSSLRALVSGGAPLPPELLERFEEAPGIK-LVNGYGLTETGGTVA 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1216630836 352 ITP--EGDDKPGAVGKVVPFFEAKVVDLDTGkTLGVNQRGELCVRGPMIMSGYVNNPEATnALIDKDGWLHSGDIAYWDE 429
Cdd:cd04433 157 TGPpdDDARKPGSVGRPVPGVEVRIVDPDGG-ELPPGEIGELVVRGPSVMKGYWNNPEAT-AAVDEDGWYRTGDLGRLDE 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1216630836 430 DEHFFIVDRLKSLIKYKGYQVAPAELESILLQHPNIFDAGVAGLPDDDAGELPAAVVVLEHGKTMTEKEIVDYVASQVTT 509
Cdd:cd04433 235 DGYLYIVGRLKDMIKSGGENVYPAEVEAVLLGHPGVAEAAVVGVPDPEWGERVVAVVVLRPGADLDAEELRAHVRERLAP 314
|
330 340
....*....|....*....|...
gi 1216630836 510 AKKLRgGVVFVDEVPKGLTGKLD 532
Cdd:cd04433 315 YKVPR-RVVFVDALPRTASGKID 336
|
|
| FC-FACS_FadD_like |
cd05936 |
Prokaryotic long-chain fatty acid CoA synthetases similar to Escherichia coli FadD; This ... |
52-537 |
1.46e-99 |
|
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: 309.11 E-value: 1.46e-99
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1216630836 52 ITYAEYFEMSVRLAEAMKRYGLNTNHRIVVCSENSLQFFMPVLGALFIGVAVAPANDIYNERELLNSMGISQPTVVFVsk 131
Cdd:cd05936 25 LTYRELDALAEAFAAGLQNLGVQPGDRVALMLPNCPQFPIAYFGALKAGAVVVPLNPLYTPRELEHILNDSGAKALIV-- 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1216630836 132 kglqkilnvqkklpiiqkiiimdsktdyqgfqsMYTFVTSHLPPGFNEYDFVPESFDrdktIALIMNSSGSTGLPKGVAL 211
Cdd:cd05936 103 ---------------------------------AVSFTDLLAAGAPLGERVALTPED----VAVLQYTSGTTGVPKGAML 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1216630836 212 PHR------TACVRfshardpIFGNQIIPDTAILSVVPFHHGFGMFTTLGY-LICGFRVVLMYRFEEELFLRSLQDYKIQ 284
Cdd:cd05936 146 THRnlvanaLQIKA-------WLEDLLEGDDVVLAALPLFHVFGLTVALLLpLALGATIVLIPRFRPIGVLKEIRKHRVT 218
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1216630836 285 SALLVPTLFSFFAKSTLIDKYDLSNLHEIASGGAPLSKEVGEAVAKRFHLPgIRQGYGLTETTSAILITP-EGDDKPGAV 363
Cdd:cd05936 219 IFPGVPTMYIALLNAPEFKKRDFSSLRLCISGGAPLPVEVAERFEELTGVP-IVEGYGLTETSPVVAVNPlDGPRKPGSI 297
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1216630836 364 GKVVPFFEAKVVDLDtGKTLGVNQRGELCVRGPMIMSGYVNNPEATNALIdKDGWLHSGDIAYWDEDEHFFIVDRLKSLI 443
Cdd:cd05936 298 GIPLPGTEVKIVDDD-GEELPPGEVGELWVRGPQVMKGYWNRPEETAEAF-VDGWLRTGDIGYMDEDGYFFIVDRKKDMI 375
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1216630836 444 KYKGYQVAPAELESILLQHPNIFDAGVAGLPDDDAGELPAAVVVLEHGKTMTEKEIVDYVASQVTTAKKLRgGVVFVDEV 523
Cdd:cd05936 376 IVGGFNVYPREVEEVLYEHPAVAEAAVVGVPDPYSGEAVKAFVVLKEGASLTEEEIIAFCREQLAGYKVPR-QVEFRDEL 454
|
490
....*....|....
gi 1216630836 524 PKGLTGKLDARKIR 537
Cdd:cd05936 455 PKSAVGKILRRELR 468
|
|
| PRK06187 |
PRK06187 |
long-chain-fatty-acid--CoA ligase; Validated |
52-538 |
1.62e-96 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 235730 [Multi-domain] Cd Length: 521 Bit Score: 303.26 E-value: 1.62e-96
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1216630836 52 ITYAEYFEMSVRLAEAMKRYGLNTNHRIVVCSENSLQFFMPVLGALFIGVAVAPANDIYNERELLNSMGISQPTVVFVSK 131
Cdd:PRK06187 32 TTYAELDERVNRLANALRALGVKKGDRVAVFDWNSHEYLEAYFAVPKIGAVLHPINIRLKPEEIAYILNDAEDRVVLVDS 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1216630836 132 KGLQKILNVQKKLPIIQKIIIMDSKTDYQGFQSMYTFVT--SHLPPgfnEYDFVPesFDRDkTIALIMNSSGSTGLPKGV 209
Cdd:PRK06187 112 EFVPLLAAILPQLPTVRTVIVEGDGPAAPLAPEVGEYEEllAAASD---TFDFPD--IDEN-DAAAMLYTSGTTGHPKGV 185
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1216630836 210 ALPHRTAcvrFSHARDPIFGNQIIPDTAILSVVP-FH-HGFGmfttLGY--LICGFRVVLMYRFEEELFLRSLQDYKIQS 285
Cdd:PRK06187 186 VLSHRNL---FLHSLAVCAWLKLSRDDVYLVIVPmFHvHAWG----LPYlaLMAGAKQVIPRRFDPENLLDLIETERVTF 258
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1216630836 286 ALLVPTLFSFFAKSTLIDKYDLSNLHEIASGGAPLSKEVGEAVAKRFHLpGIRQGYGLTETTSAILITPEGDD------K 359
Cdd:PRK06187 259 FFAVPTIWQMLLKAPRAYFVDFSSLRLVIYGGAALPPALLREFKEKFGI-DLVQGYGMTETSPVVSVLPPEDQlpgqwtK 337
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1216630836 360 PGAVGKVVPFFEAKVVDLDtGKTLGVNQR--GELCVRGPMIMSGYVNNPEATNALIDkDGWLHSGDIAYWDEDEHFFIVD 437
Cdd:PRK06187 338 RRSAGRPLPGVEARIVDDD-GDELPPDGGevGEIIVRGPWLMQGYWNRPEATAETID-GGWLHTGDVGYIDEDGYLYITD 415
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1216630836 438 RLKSLIKYKGYQVAPAELESILLQHPNIFDAGVAGLPDDDAGELPAAVVVLEHGKTMTEKEIVDYVASQVttAK-KLRGG 516
Cdd:PRK06187 416 RIKDVIISGGENIYPRELEDALYGHPAVAEVAVIGVPDEKWGERPVAVVVLKPGATLDAKELRAFLRGRL--AKfKLPKR 493
|
490 500
....*....|....*....|..
gi 1216630836 517 VVFVDEVPKGLTGKLDARKIRE 538
Cdd:PRK06187 494 IAFVDELPRTSVGKILKRVLRE 515
|
|
| PLN02330 |
PLN02330 |
4-coumarate--CoA ligase-like 1 |
3-545 |
4.78e-95 |
|
4-coumarate--CoA ligase-like 1
Pssm-ID: 215189 [Multi-domain] Cd Length: 546 Bit Score: 299.97 E-value: 4.78e-95
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1216630836 3 EDAKNIKKGPAPFYPL-EDGTAGEQLHKAMKRYAlvpGTIAFTDAHIEVDITYAEYFEMSVRLAEAMKRYGLNTNHRIVV 81
Cdd:PLN02330 9 EDNEHIFRSRYPSVPVpDKLTLPDFVLQDAELYA---DKVAFVEAVTGKAVTYGEVVRDTRRFAKALRSLGLRKGQVVVV 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1216630836 82 CSENSLQFFMPVLGALFIGVAVAPANDIYNERELLNSMGISQPTVVFVSKKGLQKILNVQkkLPIIqkiiimdsktdYQG 161
Cdd:PLN02330 86 VLPNVAEYGIVALGIMAAGGVFSGANPTALESEIKKQAEAAGAKLIVTNDTNYGKVKGLG--LPVI-----------VLG 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1216630836 162 FQSMYTFV--TSHLPPGFNEYD-FVPESFDRDKTIALIMnSSGSTGLPKGVALPHRTACVRFSHARDPIfGNQIIPDTAI 238
Cdd:PLN02330 153 EEKIEGAVnwKELLEAADRAGDtSDNEEILQTDLCALPF-SSGTTGISKGVMLTHRNLVANLCSSLFSV-GPEMIGQVVT 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1216630836 239 LSVVPFHHGFGM----FTTL---GylicgfRVVLMYRFEEELFLRSLQDYKIQSALLVPTLFSFFAKSTLIDKYDLSNL- 310
Cdd:PLN02330 231 LGLIPFFHIYGItgicCATLrnkG------KVVVMSRFELRTFLNALITQEVSFAPIVPPIILNLVKNPIVEEFDLSKLk 304
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1216630836 311 -HEIASGGAPLSKEVGEAVAKRFHLPGIRQGYGLTETtSAILIT---PE---GDDKPGAVGKVVPFFEAKVVDLDTGKTL 383
Cdd:PLN02330 305 lQAIMTAAAPLAPELLTAFEAKFPGVQVQEAYGLTEH-SCITLThgdPEkghGIAKKNSVGFILPNLEVKFIDPDTGRSL 383
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1216630836 384 GVNQRGELCVRGPMIMSGYVNNPEATNALIDKDGWLHSGDIAYWDEDEHFFIVDRLKSLIKYKGYQVAPAELESILLQHP 463
Cdd:PLN02330 384 PKNTPGELCVRSQCVMQGYYNNKEETDRTIDEDGWLHTGDIGYIDDDGDIFIVDRIKELIKYKGFQVAPAELEAILLTHP 463
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1216630836 464 NIFDAGVAGLPDDDAGELPAAVVVLEHGKTMTEKEIVDYVASQVTTAKKLRgGVVFVDEVPKGLTGKLDARKIREILIKA 543
Cdd:PLN02330 464 SVEDAAVVPLPDEEAGEIPAACVVINPKAKESEEDILNFVAANVAHYKKVR-VVQFVDSIPKSLSGKIMRRLLKEKMLSI 542
|
..
gi 1216630836 544 KK 545
Cdd:PLN02330 543 NK 544
|
|
| FACL_FadD13-like |
cd17631 |
fatty acyl-CoA synthetase, including FadD13; This family contains fatty acyl-CoA synthetases, ... |
27-532 |
1.16e-93 |
|
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: 292.98 E-value: 1.16e-93
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1216630836 27 LHKAMKRYalvPGTIAFTDAHIEvdITYAEYFEMSVRLAEAMKRYGLNTNHRIVVCSENSLQFFMPVLGALFIGVAVAPA 106
Cdd:cd17631 1 LRRRARRH---PDRTALVFGGRS--LTYAELDERVNRLAHALRALGVAKGDRVAVLSKNSPEFLELLFAAARLGAVFVPL 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1216630836 107 NDIYNERELLNSMGISQPTVVFvskkglqkilnvqkklpiiqkiiiMDsktdyqgfqsmytfvtshlppgfneydfvpes 186
Cdd:cd17631 76 NFRLTPPEVAYILADSGAKVLF------------------------DD-------------------------------- 99
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1216630836 187 fdrdktIALIMNSSGSTGLPKGVALPHRTacvRFSHARDPIFGNQIIPDTAILSVVPFHHGFGM-FTTLGYLICGFRVVL 265
Cdd:cd17631 100 ------LALLMYTSGTTGRPKGAMLTHRN---LLWNAVNALAALDLGPDDVLLVVAPLFHIGGLgVFTLPTLLRGGTVVI 170
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1216630836 266 MYRFEEELFLRSLQDYKIQSALLVPTLFSFFAKSTLIDKYDLSNLHEIASGGAPLSKEVGEAVAKRFhlPGIRQGYGLTE 345
Cdd:cd17631 171 LRKFDPETVLDLIERHRVTSFFLVPTMIQALLQHPRFATTDLSSLRAVIYGGAPMPERLLRALQARG--VKFVQGYGMTE 248
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1216630836 346 TTSAILITPEGD--DKPGAVGKVVPFFEAKVVDLDtGKTLGVNQRGELCVRGPMIMSGYVNNPEATNALIdKDGWLHSGD 423
Cdd:cd17631 249 TSPGVTFLSPEDhrRKLGSAGRPVFFVEVRIVDPD-GREVPPGEVGEIVVRGPHVMAGYWNRPEATAAAF-RDGWFHTGD 326
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1216630836 424 IAYWDEDEHFFIVDRLKSLIKYKGYQVAPAELESILLQHPNIFDAGVAGLPDDDAGELPAAVVVLEHGKTMTEKEIVDYV 503
Cdd:cd17631 327 LGRLDEDGYLYIVDRKKDMIISGGENVYPAEVEDVLYEHPAVAEVAVIGVPDEKWGEAVVAVVVPRPGAELDEDELIAHC 406
|
490 500
....*....|....*....|....*....
gi 1216630836 504 ASQVTTAKKLRgGVVFVDEVPKGLTGKLD 532
Cdd:cd17631 407 RERLARYKIPK-SVEFVDALPRNATGKIL 434
|
|
| AMP-binding |
pfam00501 |
AMP-binding enzyme; |
38-446 |
1.23e-93 |
|
AMP-binding enzyme;
Pssm-ID: 459834 [Multi-domain] Cd Length: 417 Bit Score: 292.29 E-value: 1.23e-93
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1216630836 38 PGTIAFTDAHIEvDITYAEYFEMSVRLAEAMKRYGLNTNHRIVVCSENSLQFFMPVLGALFIGVAVAPANDIYNERELLN 117
Cdd:pfam00501 9 PDKTALEVGEGR-RLTYRELDERANRLAAGLRALGVGKGDRVAILLPNSPEWVVAFLACLKAGAVYVPLNPRLPAEELAY 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1216630836 118 SMGISQPTVVFV-SKKGLQKILNVQKKLPIIQKIIIMDSKTDYQGFQSMYTFVTSHLPPgfneydFVPESFDRDkTIALI 196
Cdd:pfam00501 88 ILEDSGAKVLITdDALKLEELLEALGKLEVVKLVLVLDRDPVLKEEPLPEEAKPADVPP------PPPPPPDPD-DLAYI 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1216630836 197 MNSSGSTGLPKGVALPHR------TACVRFSHARDPIFgnqiiPDTAILSVVPFHHGFGM-FTTLGYLICGFRVVLM--- 266
Cdd:pfam00501 161 IYTSGTTGKPKGVMLTHRnlvanvLSIKRVRPRGFGLG-----PDDRVLSTLPLFHDFGLsLGLLGPLLAGATVVLPpgf 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1216630836 267 YRFEEELFLRSLQDYKIQSALLVPTLFSFFAKSTLIDKYDLSNLHEIASGGAPLSKEVGEAVAKRFHlPGIRQGYGLTET 346
Cdd:pfam00501 236 PALDPAALLELIERYKVTVLYGVPTLLNMLLEAGAPKRALLSSLRLVLSGGAPLPPELARRFRELFG-GALVNGYGLTET 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1216630836 347 TSAILITPEGDDK---PGAVGKVVPFFEAKVVDLDTGKTLGVNQRGELCVRGPMIMSGYVNNPEATNALIDKDGWLHSGD 423
Cdd:pfam00501 315 TGVVTTPLPLDEDlrsLGSVGRPLPGTEVKIVDDETGEPVPPGEPGELCVRGPGVMKGYLNDPELTAEAFDEDGWYRTGD 394
|
410 420
....*....|....*....|...
gi 1216630836 424 IAYWDEDEHFFIVDRLKSLIKYK 446
Cdd:pfam00501 395 LGRRDEDGYLEIVGRKKDQIKLG 417
|
|
| PLN02574 |
PLN02574 |
4-coumarate--CoA ligase-like |
38-540 |
3.56e-86 |
|
4-coumarate--CoA ligase-like
Pssm-ID: 215312 [Multi-domain] Cd Length: 560 Bit Score: 277.49 E-value: 3.56e-86
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1216630836 38 PGTIAFTDAHIEVDITYAEYFEMSVRLAEAMKRY-GLNTNHRIVVCSENSLQFFMPVLGALFIGVAVAPANDIYNERELL 116
Cdd:PLN02574 53 NGDTALIDSSTGFSISYSELQPLVKSMAAGLYHVmGVRQGDVVLLLLPNSVYFPVIFLAVLSLGGIVTTMNPSSSLGEIK 132
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1216630836 117 NSMGISQPTVVFVSKKGLQKILNVQKKLPIIQKIIIMDSKT-DYQGFQSMYTFvtshlppgfnEYDFVPESFDRDKTIAL 195
Cdd:PLN02574 133 KRVVDCSVGLAFTSPENVEKLSPLGVPVIGVPENYDFDSKRiEFPKFYELIKE----------DFDFVPKPVIKQDDVAA 202
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1216630836 196 IMNSSGSTGLPKGVALPHRTAC------VRFSHARDPIFGNqiipDTAILSVVPFHH--GFGMFTTlGYLICGFRVVLMY 267
Cdd:PLN02574 203 IMYSSGTTGASKGVVLTHRNLIamvelfVRFEASQYEYPGS----DNVYLAALPMFHiyGLSLFVV-GLLSLGSTIVVMR 277
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1216630836 268 RFEEELFLRSLQDYKIQSALLVPTLFSFFAKSTL-IDKYDLSNLHEIASGGAPLSKEVGEAVAKRFHLPGIRQGYGLTET 346
Cdd:PLN02574 278 RFDASDMVKVIDRFKVTHFPVVPPILMALTKKAKgVCGEVLKSLKQVSCGAAPLSGKFIQDFVQTLPHVDFIQGYGMTES 357
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1216630836 347 TSAIL--ITPEGDDKPGAVGKVVPFFEAKVVDLDTGKTLGVNQRGELCVRGPMIMSGYVNNPEATNALIDKDGWLHSGDI 424
Cdd:PLN02574 358 TAVGTrgFNTEKLSKYSSVGLLAPNMQAKVVDWSTGCLLPPGNCGELWIQGPGVMKGYLNNPKATQSTIDKDGWLRTGDI 437
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1216630836 425 AYWDEDEHFFIVDRLKSLIKYKGYQVAPAELESILLQHPNIFDAGVAGLPDDDAGELPAAVVVLEHGKTMTEKEIVDYVA 504
Cdd:PLN02574 438 AYFDEDGYLYIVDRLKEIIKYKGFQIAPADLEAVLISHPEIIDAAVTAVPDKECGEIPVAFVVRRQGSTLSQEAVINYVA 517
|
490 500 510
....*....|....*....|....*....|....*.
gi 1216630836 505 SQVTTAKKLRgGVVFVDEVPKGLTGKLDARKIREIL 540
Cdd:PLN02574 518 KQVAPYKKVR-KVVFVQSIPKSPAGKILRRELKRSL 552
|
|
| FACL_fum10p_like |
cd05926 |
Subfamily of fatty acid CoA ligase (FACL) similar to Fum10p of Gibberella moniliformis; FACL ... |
50-538 |
7.19e-82 |
|
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: 264.17 E-value: 7.19e-82
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1216630836 50 VDITYAEYFEMSVRLAEAMKRYGLNTNHRIVVCSENSLQFFMPVLGALFIGVAVAPANDIYNERELLNSMGISQPTVVFV 129
Cdd:cd05926 13 PALTYADLAELVDDLARQLAALGIKKGDRVAIALPNGLEFVVAFLAAARAGAVVAPLNPAYKKAEFEFYLADLGSKLVLT 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1216630836 130 SKKGLQKILNVQKKLPIIQKIIIMDSKTDYQGFQSmytfvtSHLPPGFNEYDFV-PESFDRDKTIALIMNSSGSTGLPKG 208
Cdd:cd05926 93 PKGELGPASRAASKLGLAILELALDVGVLIRAPSA------ESLSNLLADKKNAkSEGVPLPDDLALILHTSGTTGRPKG 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1216630836 209 VALPHRTACvrfSHARDPIFGNQIIPDTAILSVVPFHHGFGMFTT-LGYLICGFRVVLMYRFEEELFLRSLQDYKIQ--S 285
Cdd:cd05926 167 VPLTHRNLA---ASATNITNTYKLTPDDRTLVVMPLFHVHGLVASlLSTLAAGGSVVLPPRFSASTFWPDVRDYNATwyT 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1216630836 286 AllVPTLFSFFAKSTLIDKYD-LSNLHEIASGGAPLSKEVGEAVAKRFHLPGIrQGYGLTETTSAILITP--EGDDKPGA 362
Cdd:cd05926 244 A--VPTIHQILLNRPEPNPESpPPKLRFIRSCSASLPPAVLEALEATFGAPVL-EAYGMTEAAHQMTSNPlpPGPRKPGS 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1216630836 363 VGKvvPF-FEAKVVDlDTGKTLGVNQRGELCVRGPMIMSGYVNNPEATNALIDKDGWLHSGDIAYWDEDEHFFIVDRLKS 441
Cdd:cd05926 321 VGK--PVgVEVRILD-EDGEILPPGVVGEICLRGPNVTRGYLNNPEANAEAAFKDGWFRTGDLGYLDADGYLFLTGRIKE 397
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1216630836 442 LIKYKGYQVAPAELESILLQHPNIFDAGVAGLPDDDAGELPAAVVVLEHGKTMTEKEIVDYVASQVtTAKKLRGGVVFVD 521
Cdd:cd05926 398 LINRGGEKISPLEVDGVLLSHPAVLEAVAFGVPDEKYGEEVAAAVVLREGASVTEEELRAFCRKHL-AAFKVPKKVYFVD 476
|
490
....*....|....*..
gi 1216630836 522 EVPKGLTGKLDARKIRE 538
Cdd:cd05926 477 ELPKTATGKIQRRKVAE 493
|
|
| PRK07656 |
PRK07656 |
long-chain-fatty-acid--CoA ligase; Validated |
25-538 |
4.46e-81 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236072 [Multi-domain] Cd Length: 513 Bit Score: 262.53 E-value: 4.46e-81
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1216630836 25 EQLHKAMKRYalvPGTIAFTDAhiEVDITYAEYFEMSVRLAEAMKRYGLNTNHRIVVCSENSLQFFMPVLGALFIGVAVA 104
Cdd:PRK07656 9 ELLARAARRF---GDKEAYVFG--DQRLTYAELNARVRRAAAALAALGIGKGDRVAIWAPNSPHWVIAALGALKAGAVVV 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1216630836 105 PANDIYNERELLNSMGISQPTVVFVSKKGLQKILNVQKKLPIIQKIIIMDSKTDYQGFQSMYTFvTSHLPPGFNEYDFVP 184
Cdd:PRK07656 84 PLNTRYTADEAAYILARGDAKALFVLGLFLGVDYSATTRLPALEHVVICETEEDDPHTEKMKTF-TDFLAAGDPAERAPE 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1216630836 185 ESFDrdkTIALIMNSSGSTGLPKGVALPHRTAcvrFSHARDpiFGN--QIIPDTAILSVVPFHHGFGMftTLGYLIC--- 259
Cdd:PRK07656 163 VDPD---DVADILFTSGTTGRPKGAMLTHRQL---LSNAAD--WAEylGLTEGDRYLAANPFFHVFGY--KAGVNAPlmr 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1216630836 260 GFRVVLMYRFEEELFLRSLQDYKIQSALLVPTLFSFFAKSTLIDKYDLSNLHEIASGGAPLSKEVGEAVAKRFHLPGIRQ 339
Cdd:PRK07656 233 GATILPLPVFDPDEVFRLIETERITVLPGPPTMYNSLLQHPDRSAEDLSSLRLAVTGAASMPVALLERFESELGVDIVLT 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1216630836 340 GYGLTETTSAILITPEGDDK---PGAVGKVVPFFEAKVVDlDTGKTLGVNQRGELCVRGPMIMSGYVNNPEATNALIDKD 416
Cdd:PRK07656 313 GYGLSEASGVTTFNRLDDDRktvAGTIGTAIAGVENKIVN-ELGEEVPVGEVGELLVRGPNVMKGYYDDPEATAAAIDAD 391
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1216630836 417 GWLHSGDIAYWDEDEHFFIVDRLKSLIKYKGYQVAPAELESILLQHPNIFDAGVAGLPDDDAGELPAAVVVLEHGKTMTE 496
Cdd:PRK07656 392 GWLHTGDLGRLDEEGYLYIVDRKKDMFIVGGFNVYPAEVEEVLYEHPAVAEAAVIGVPDERLGEVGKAYVVLKPGAELTE 471
|
490 500 510 520
....*....|....*....|....*....|....*....|...
gi 1216630836 497 KEIVDYVASQVttAK-KLRGGVVFVDEVPKGLTGKLDARKIRE 538
Cdd:PRK07656 472 EELIAYCREHL--AKyKVPRSIEFLDELPKNATGKVLKRALRE 512
|
|
| PRK08314 |
PRK08314 |
long-chain-fatty-acid--CoA ligase; Validated |
52-538 |
4.59e-81 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236235 [Multi-domain] Cd Length: 546 Bit Score: 263.74 E-value: 4.59e-81
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1216630836 52 ITYAEYFEMSVRLAEAMKR-YGLNTNHRIVVCSENSLQFFMPVLGALFIGVAVAPANDIYNERELLNSMGISQPTVVFVS 130
Cdd:PRK08314 36 ISYRELLEEAERLAGYLQQeCGVRKGDRVLLYMQNSPQFVIAYYAILRANAVVVPVNPMNREEELAHYVTDSGARVAIVG 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1216630836 131 KKGLQKILNVQKKLPIiqKIIIMDSKTDYQGFQSMYTF----VTSHLPPGFNEYDFV-------------PESFDRDkTI 193
Cdd:PRK08314 116 SELAPKVAPAVGNLRL--RHVIVAQYSDYLPAEPEIAVpawlRAEPPLQALAPGGVVawkealaaglappPHTAGPD-DL 192
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1216630836 194 ALIMNSSGSTGLPKGVALPHRTacVRFShardpIFGNQI----IPDTAILSVVPFHHGFGMFTTL-GYLICGFRVVLMYR 268
Cdd:PRK08314 193 AVLPYTSGTTGVPKGCMHTHRT--VMAN-----AVGSVLwsnsTPESVVLAVLPLFHVTGMVHSMnAPIYAGATVVLMPR 265
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1216630836 269 FEEELFLRSLQDYKIQSALLVPT-LFSFFAkSTLIDKYDLSNLHEIASGGAPLSkevgEAVAKRFH-LPGIR--QGYGLT 344
Cdd:PRK08314 266 WDREAAARLIERYRVTHWTNIPTmVVDFLA-SPGLAERDLSSLRYIGGGGAAMP----EAVAERLKeLTGLDyvEGYGLT 340
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1216630836 345 ETTSAILITPEGDDKPGAVGkvVPFF--EAKVVDLDTGKTLGVNQRGELCVRGPMIMSGYVNNPEAT-NALIDKDG--WL 419
Cdd:PRK08314 341 ETMAQTHSNPPDRPKLQCLG--IPTFgvDARVIDPETLEELPPGEVGEIVVHGPQVFKGYWNRPEATaEAFIEIDGkrFF 418
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1216630836 420 HSGDIAYWDEDEHFFIVDRLKSLIKYKGYQVAPAELESILLQHPNIFDAGVAGLPDDDAGELPAAVVVL--EHGKTMTEK 497
Cdd:PRK08314 419 RTGDLGRMDEEGYFFITDRLKRMINASGFKVWPAEVENLLYKHPAIQEACVIATPDPRRGETVKAVVVLrpEARGKTTEE 498
|
490 500 510 520
....*....|....*....|....*....|....*....|.
gi 1216630836 498 EIVDYVASQVTTAKKLRgGVVFVDEVPKGLTGKLDARKIRE 538
Cdd:PRK08314 499 EIIAWAREHMAAYKYPR-IVEFVDSLPKSGSGKILWRQLQE 538
|
|
| LC_FACS_like |
cd05935 |
Putative long-chain fatty acid CoA ligase; The members of this family are putative long-chain ... |
52-534 |
1.30e-80 |
|
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: 258.95 E-value: 1.30e-80
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1216630836 52 ITYAEYFEMSVRLAEAMKRYGLNTNHRIVVCSENSLQFFMPVLGALFIGVAVAPANDIYNEREL---LNSMGIsqptvvf 128
Cdd:cd05935 2 LTYLELLEVVKKLASFLSNKGVRKGDRVGICLQNSPQYVIAYFAIWRANAVVVPINPMLKERELeyiLNDSGA------- 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1216630836 129 vskkglqkilnvqkklpiiqKIIIMDSKTDyqgfqsmytfvtshlppgfneydfvpesfdrdkTIALIMNSSGSTGLPKG 208
Cdd:cd05935 75 --------------------KVAVVGSELD---------------------------------DLALIPYTSGTTGLPKG 101
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1216630836 209 VALPHRTAcvrFSHARDPIFGNQIIPDTAILSVVPFHHGFGMFTTLGYLI-CGFRVVLMYRFEEELFLRSLQDYKIQSAL 287
Cdd:cd05935 102 CMHTHFSA---AANALQSAVWTGLTPSDVILACLPLFHVTGFVGSLNTAVyVGGTYVLMARWDRETALELIEKYKVTFWT 178
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1216630836 288 LVPTLFSFFAKSTLIDKYDLSNLHEIASGGAPLSKEVGEAVAKRFhlpGIR--QGYGLTETTSAILITPEGDDKPGAVGk 365
Cdd:cd05935 179 NIPTMLVDLLATPEFKTRDLSSLKVLTGGGAPMPPAVAEKLLKLT---GLRfvEGYGLTETMSQTHTNPPLRPKLQCLG- 254
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1216630836 366 vVPFF--EAKVVDLDTGKTLGVNQRGELCVRGPMIMSGYVNNPEAT-NALIDKDG--WLHSGDIAYWDEDEHFFIVDRLK 440
Cdd:cd05935 255 -IP*FgvDARVIDIETGRELPPNEVGEIVVRGPQIFKGYWNRPEETeESFIEIKGrrFFRTGDLGYMDEEGYFFFVDRVK 333
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1216630836 441 SLIKYKGYQVAPAELESILLQHPNIFDAGVAGLPDDDAGELPAAVVVL--EHGKTMTEKEIVDYVASQVTTAKKLRgGVV 518
Cdd:cd05935 334 RMINVSGFKVWPAEVEAKLYKHPAI*EVCVISVPDERVGEEVKAFIVLrpEYRGKVTEEDIIEWAREQMAAYKYPR-EVE 412
|
490
....*....|....*.
gi 1216630836 519 FVDEVPKGLTGKLDAR 534
Cdd:cd05935 413 FVDELPRSASGKILWR 428
|
|
| Acs |
COG0365 |
Acyl-coenzyme A synthetase/AMP-(fatty) acid ligase [Lipid transport and metabolism]; |
49-540 |
6.81e-76 |
|
Acyl-coenzyme A synthetase/AMP-(fatty) acid ligase [Lipid transport and metabolism];
Pssm-ID: 440134 [Multi-domain] Cd Length: 565 Bit Score: 250.41 E-value: 6.81e-76
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1216630836 49 EVDITYAEYFEMSVRLAEAMKRYGLNTNHRIVVCSENSLQFFMPVLGALFIGVAVAPANDIYNERELLNSMGISQPTVVF 128
Cdd:COG0365 37 ERTLTYAELRREVNRFANALRALGVKKGDRVAIYLPNIPEAVIAMLACARIGAVHSPVFPGFGAEALADRIEDAEAKVLI 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1216630836 129 VSKKGL---------QKILNVQKKLPIIQKIII---MDSKTDYQGFQSMYTFVTSHLPpgfneyDFVPESFDRDkTIALI 196
Cdd:COG0365 117 TADGGLrggkvidlkEKVDEALEELPSLEHVIVvgrTGADVPMEGDLDWDELLAAASA------EFEPEPTDAD-DPLFI 189
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1216630836 197 MNSSGSTGLPKGVALPHR--TACVRFSHARdpIFGnqIIPDTAILSVVP----FHHGFGMFttlGYLICGFRVVLmyrFE 270
Cdd:COG0365 190 LYTSGTTGKPKGVVHTHGgyLVHAATTAKY--VLD--LKPGDVFWCTADigwaTGHSYIVY---GPLLNGATVVL---YE 259
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1216630836 271 E-------ELFLRSLQDYKIQSALLVPTLFSFFAKS--TLIDKYDLSNLHEIASGGAPLSKEVGEAVAKRFHLPgIRQGY 341
Cdd:COG0365 260 GrpdfpdpGRLWELIEKYGVTVFFTAPTAIRALMKAgdEPLKKYDLSSLRLLGSAGEPLNPEVWEWWYEAVGVP-IVDGW 338
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1216630836 342 GLTETTSAILITPEGDD-KPGAVGKVVPFFEAKVVDlDTGKTLGVNQRGELCVRGPM--IMSGYVNNPEAT-NALIDK-D 416
Cdd:COG0365 339 GQTETGGIFISNLPGLPvKPGSMGKPVPGYDVAVVD-EDGNPVPPGEEGELVIKGPWpgMFRGYWNDPERYrETYFGRfP 417
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1216630836 417 GWLHSGDIAYWDEDEHFFIVDRLKSLIKYKGYQVAPAELESILLQHPNIFDAGVAGLPDDDAGELPAAVVVLEHGKTMTE 496
Cdd:COG0365 418 GWYRTGDGARRDEDGYFWILGRSDDVINVSGHRIGTAEIESALVSHPAVAEAAVVGVPDEIRGQVVKAFVVLKPGVEPSD 497
|
490 500 510 520
....*....|....*....|....*....|....*....|....*..
gi 1216630836 497 ---KEIVDYVASQVTTAKKLRgGVVFVDEVPKGLTGKLDARKIREIL 540
Cdd:COG0365 498 elaKELQAHVREELGPYAYPR-EIEFVDELPKTRSGKIMRRLLRKIA 543
|
|
| PRK12583 |
PRK12583 |
acyl-CoA synthetase; Provisional |
11-541 |
2.48e-73 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 237145 [Multi-domain] Cd Length: 558 Bit Score: 243.53 E-value: 2.48e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1216630836 11 GPAPFY-------PLEDGTAGEQLHKAMKRYalvPGTIAFTDAHIEVDITYAEYFEMSVRLAEAMKRYGLNTNHRIVVCS 83
Cdd:PRK12583 1 MPQPSYyqgggdkPLLTQTIGDAFDATVARF---PDREALVVRHQALRYTWRQLADAVDRLARGLLALGVQPGDRVGIWA 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1216630836 84 ENSLQFFMPVLGALFIGVAVAPANDIYNERELLNSMGISQPTVVFVSK--KG------LQKILN----------VQKKLP 145
Cdd:PRK12583 78 PNCAEWLLTQFATARIGAILVNINPAYRASELEYALGQSGVRWVICADafKTsdyhamLQELLPglaegqpgalACERLP 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1216630836 146 IIQKIIIMDSK-----TDYQGFQSMYTFVTSHlppgfnEYDFVPESFDRDKTIAlIMNSSGSTGLPKGVALPHRTacvrf 220
Cdd:PRK12583 158 ELRGVVSLAPApppgfLAWHELQARGETVSRE------ALAERQASLDRDDPIN-IQYTSGTTGFPKGATLSHHN----- 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1216630836 221 shardpIFGNQII-------PDTAILSV-VPFHHGFGM-FTTLGYLICGFRVVL-MYRFEEELFLRSLQDYKIQSALLVP 290
Cdd:PRK12583 226 ------ILNNGYFvaeslglTEHDRLCVpVPLYHCFGMvLANLGCMTVGACLVYpNEAFDPLATLQAVEEERCTALYGVP 299
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1216630836 291 TLFSFFAKSTLIDKYDLSNLHEIASGGAPLSKEVGEAVAKRFHLPGIRQGYGLTETTSAILITPEGDDKP---GAVGKVV 367
Cdd:PRK12583 300 TMFIAELDHPQRGNFDLSSLRTGIMAGAPCPIEVMRRVMDEMHMAEVQIAYGMTETSPVSLQTTAADDLErrvETVGRTQ 379
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1216630836 368 PFFEAKVVDLDtGKTLGVNQRGELCVRGPMIMSGYVNNPEATNALIDKDGWLHSGDIAYWDEDEHFFIVDRLKSLIKYKG 447
Cdd:PRK12583 380 PHLEVKVVDPD-GATVPRGEIGELCTRGYSVMKGYWNNPEATAESIDEDGWMHTGDLATMDEQGYVRIVGRSKDMIIRGG 458
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1216630836 448 YQVAPAELESILLQHPNIFDAGVAGLPDDDAGELPAAVVVLEHGKTMTEKEIVDYVASQVTTAKKLRgGVVFVDEVPKGL 527
Cdd:PRK12583 459 ENIYPREIEEFLFTHPAVADVQVFGVPDEKYGEEIVAWVRLHPGHAASEEELREFCKARIAHFKVPR-YFRFVDEFPMTV 537
|
570
....*....|....
gi 1216630836 528 TGKLDARKIREILI 541
Cdd:PRK12583 538 TGKVQKFRMREISI 551
|
|
| FACL_like_2 |
cd05917 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
200-537 |
7.30e-70 |
|
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: 228.32 E-value: 7.30e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1216630836 200 SGSTGLPKGVALPHRTacvrfshardpIFGNQII--------PDTAILSVVPFHHGFGMftTLGYLIC---GFRVVlmyr 268
Cdd:cd05917 11 SGTTGSPKGATLTHHN-----------IVNNGYFigerlgltEQDRLCIPVPLFHCFGS--VLGVLAClthGATMV---- 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1216630836 269 FEEELF-----LRSLQDYKIQSALLVPTLFSFFAKSTLIDKYDLSNLHEIASGGAPLSKEVGEAVAKRFHLPGIRQGYGL 343
Cdd:cd05917 74 FPSPSFdplavLEAIEKEKCTALHGVPTMFIAELEHPDFDKFDLSSLRTGIMAGAPCPPELMKRVIEVMNMKDVTIAYGM 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1216630836 344 TETTSAILITPEGDD---KPGAVGKVVPFFEAKVVDLDTGKTLGVNQRGELCVRGPMIMSGYVNNPEATNALIDKDGWLH 420
Cdd:cd05917 154 TETSPVSTQTRTDDSiekRVNTVGRIMPHTEAKIVDPEGGIVPPVGVPGELCIRGYSVMKGYWNDPEKTAEAIDGDGWLH 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1216630836 421 SGDIAYWDEDEHFFIVDRLKSLIKYKGYQVAPAELESILLQHPNIFDAGVAGLPDDDAGELPAAVVVLEHGKTMTEKEIV 500
Cdd:cd05917 234 TGDLAVMDEDGYCRIVGRIKDMIIRGGENIYPREIEEFLHTHPKVSDVQVVGVPDERYGEEVCAWIRLKEGAELTEEDIK 313
|
330 340 350
....*....|....*....|....*....|....*..
gi 1216630836 501 DYVASQVTTAKKLRgGVVFVDEVPKGLTGKLDARKIR 537
Cdd:cd05917 314 AYCKGKIAHYKVPR-YVFFVDEFPLTVSGKIQKFKLR 349
|
|
| PRK08315 |
PRK08315 |
AMP-binding domain protein; Validated |
17-542 |
5.87e-68 |
|
AMP-binding domain protein; Validated
Pssm-ID: 236236 [Multi-domain] Cd Length: 559 Bit Score: 229.31 E-value: 5.87e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1216630836 17 PLEDGTAGEQLHKAMKRYalvPGTIAFTDAHIEVDITYAEYFEMSVRLAEAMKRYGLNTNHRIVVCSENS-----LQFFM 91
Cdd:PRK08315 12 PLLEQTIGQLLDRTAARY---PDREALVYRDQGLRWTYREFNEEVDALAKGLLALGIEKGDRVGIWAPNVpewvlTQFAT 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1216630836 92 PVLGAlfIGVAVAPAndiYNEREL---LNSMGISqpTVVFVSK-----------------KGLQKILNVQKKLPIIQKII 151
Cdd:PRK08315 89 AKIGA--ILVTINPA---YRLSELeyaLNQSGCK--ALIAADGfkdsdyvamlyelapelATCEPGQLQSARLPELRRVI 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1216630836 152 IMDSKTdyqgFQSMYTF-----VTSHLPPGfnEYDFVPESFDRDKTIAlIMNSSGSTGLPKGVALPHR---------TAC 217
Cdd:PRK08315 162 FLGDEK----HPGMLNFdellaLGRAVDDA--ELAARQATLDPDDPIN-IQYTSGTTGFPKGATLTHRnilnngyfiGEA 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1216630836 218 VRFSHArDPIfgnqIIPdtailsvVPFHHGFGMftTLGYLIC---GFRVVLMY-RFEEELFLRSLQDYKIQSALLVPTLF 293
Cdd:PRK08315 235 MKLTEE-DRL----CIP-------VPLYHCFGM--VLGNLACvthGATMVYPGeGFDPLATLAAVEEERCTALYGVPTMF 300
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1216630836 294 -------SFfakstliDKYDLSNLHEIASGGAPLSKEVGEAVAKRFHLPGIRQGYGLTETTSAILITPEGDD---KPGAV 363
Cdd:PRK08315 301 iaeldhpDF-------ARFDLSSLRTGIMAGSPCPIEVMKRVIDKMHMSEVTIAYGMTETSPVSTQTRTDDPlekRVTTV 373
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1216630836 364 GKVVPFFEAKVVDLDTGKTLGVNQRGELCVRGPMIMSGYVNNPEATNALIDKDGWLHSGDIAYWDEDEHFFIVDRLKSLI 443
Cdd:PRK08315 374 GRALPHLEVKIVDPETGETVPRGEQGELCTRGYSVMKGYWNDPEKTAEAIDADGWMHTGDLAVMDEEGYVNIVGRIKDMI 453
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1216630836 444 KYKGYQVAPAELESILLQHPNIFDAGVAGLPDDDAGELPAAVVVLEHGKTMTEKEIVDYVASQVTTAKKLRgGVVFVDEV 523
Cdd:PRK08315 454 IRGGENIYPREIEEFLYTHPKIQDVQVVGVPDEKYGEEVCAWIILRPGATLTEEDVRDFCRGKIAHYKIPR-YIRFVDEF 532
|
570
....*....|....*....
gi 1216630836 524 PKGLTGKLDARKIREILIK 542
Cdd:PRK08315 533 PMTVTGKIQKFKMREMMIE 551
|
|
| PRK06839 |
PRK06839 |
o-succinylbenzoate--CoA ligase; |
32-540 |
7.62e-68 |
|
o-succinylbenzoate--CoA ligase;
Pssm-ID: 168698 [Multi-domain] Cd Length: 496 Bit Score: 227.44 E-value: 7.62e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1216630836 32 KRYALVPGTIAFTDAhiEVDITYAEYFEMSVRLAEAMK-RYGLNTNHRIVVCSENSLQFFMPVLGALFIGVAVAPANDIY 110
Cdd:PRK06839 10 KRAYLHPDRIAIITE--EEEMTYKQLHEYVSKVAAYLIyELNVKKGERIAILSQNSLEYIVLLFAIAKVECIAVPLNIRL 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1216630836 111 NERELLNSMGISQPTVVFVSKKGLQKILNVQKKLPIIQKIIIMDSKTDYQGFQSmytfvtshlppgfneyDFVPESFDRD 190
Cdd:PRK06839 88 TENELIFQLKDSGTTVLFVEKTFQNMALSMQKVSYVQRVISITSLKEIEDRKID----------------NFVEKNESAS 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1216630836 191 ktiALIMNSSGSTGLPKGVALphrTACVRFSHARDPIFGNQIIPDTAILSVVPFHH--GFGMFTtLGYLICGFRVVLMYR 268
Cdd:PRK06839 152 ---FIICYTSGTTGKPKGAVL---TQENMFWNALNNTFAIDLTMHDRSIVLLPLFHigGIGLFA-FPTLFAGGVIIVPRK 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1216630836 269 FEEELFLRSLQDYKIQSALLVPTLFSFFAKSTLIDKYDLSNLHEIASGGAPLSKEVGEAVAKRFHLPGirQGYGLTETTS 348
Cdd:PRK06839 225 FEPTKALSMIEKHKVTVVMGVPTIHQALINCSKFETTNLQSVRWFYNGGAPCPEELMREFIDRGFLFG--QGFGMTETSP 302
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1216630836 349 AILITPEGD--DKPGAVGKVVPFFEAKVVDLDTGKtLGVNQRGELCVRGPMIMSGYVNNPEATNALIdKDGWLHSGDIAY 426
Cdd:PRK06839 303 TVFMLSEEDarRKVGSIGKPVLFCDYELIDENKNK-VEVGEVGELLIRGPNVMKEYWNRPDATEETI-QDGWLCTGDLAR 380
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1216630836 427 WDEDEHFFIVDRLKSLIKYKGYQVAPAELESILLQHPNIFDAGVAGLPDDDAGELPAAVVVLEHGKTMTEKEIVDYVASQ 506
Cdd:PRK06839 381 VDEDGFVYIVGRKKEMIISGGENIYPLEVEQVINKLSDVYEVAVVGRQHVKWGEIPIAFIVKKSSSVLIEKDVIEHCRLF 460
|
490 500 510
....*....|....*....|....*....|....
gi 1216630836 507 VTTAKKLRgGVVFVDEVPKGLTGKLDARKIREIL 540
Cdd:PRK06839 461 LAKYKIPK-EIVFLKELPKNATGKIQKAQLVNQL 493
|
|
| OSB_CoA_lg |
cd05912 |
O-succinylbenzoate-CoA ligase (also known as O-succinylbenzoate-CoA synthase, OSB-CoA ... |
51-538 |
1.20e-67 |
|
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: 224.53 E-value: 1.20e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1216630836 51 DITYAEYFEMSVRLAEAMKRYGLNTNHRIVVCSENSLQFFMPVLGALFIGVAVAPANDIYNERELLNSMGISQPtvvfvs 130
Cdd:cd05912 1 SYTFAELFEEVSRLAEHLAALGVRKGDRVALLSKNSIEMILLIHALWLLGAEAVLLNTRLTPNELAFQLKDSDV------ 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1216630836 131 kkglqkilnvqkklpiiqkiiimdsktdyqgfqsmytfvtshlppgfneydfvpeSFDRdktIALIMNSSGSTGLPKGVA 210
Cdd:cd05912 75 -------------------------------------------------------KLDD---IATIMYTSGTTGKPKGVQ 96
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1216630836 211 LphrTACVRFSHARDPIFGNQIIPDTAILSVVPFHHGFGMFTTLGYLICGFRVVLMYRFEEELFLRSLQDYKIQSALLVP 290
Cdd:cd05912 97 Q---TFGNHWWSAIGSALNLGLTEDDNWLCALPLFHISGLSILMRSVIYGMTVYLVDKFDAEQVLHLINSGKVTIISVVP 173
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1216630836 291 TLFSffaksTLIDKYDL---SNLHEIASGGAPLSKEVGEaVAKRFHLPgIRQGYGLTETTSAIL-ITPE-GDDKPGAVGK 365
Cdd:cd05912 174 TMLQ-----RLLEILGEgypNNLRCILLGGGPAPKPLLE-QCKEKGIP-VYQSYGMTETCSQIVtLSPEdALNKIGSAGK 246
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1216630836 366 VVPFFEAKVVDLDTGKtlgvNQRGELCVRGPMIMSGYVNNPEATNALIdKDGWLHSGDIAYWDEDEHFFIVDRLKSLIKY 445
Cdd:cd05912 247 PLFPVELKIEDDGQPP----YEVGEILLKGPNVTKGYLNRPDATEESF-ENGWFKTGDIGYLDEEGFLYVLDRRSDLIIS 321
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1216630836 446 KGYQVAPAELESILLQHPNIFDAGVAGLPDDDAGELPAAVVVLEhgKTMTEKEIVDYVASQVttAK-KLRGGVVFVDEVP 524
Cdd:cd05912 322 GGENIYPAEIEEVLLSHPAIKEAGVVGIPDDKWGQVPVAFVVSE--RPISEEELIAYCSEKL--AKyKVPKKIYFVDELP 397
|
490
....*....|....
gi 1216630836 525 KGLTGKLDARKIRE 538
Cdd:cd05912 398 RTASGKLLRHELKQ 411
|
|
| ttLC_FACS_AlkK_like |
cd12119 |
Fatty acyl-CoA synthetases similar to LC-FACS from Thermus thermophiles; This family includes ... |
53-538 |
1.97e-67 |
|
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: 226.74 E-value: 1.97e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1216630836 53 TYAEYFEMSVRLAEAMKRYGLNTNHRIVVCSENSLQFFMPVLGALFIGVAVAPANDIYNERELLNSMGISQPTVVFVSKK 132
Cdd:cd12119 27 TYAEVAERARRLANALRRLGVKPGDRVATLAWNTHRHLELYYAVPGMGAVLHTINPRLFPEQIAYIINHAEDRVVFVDRD 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1216630836 133 GLQKILNVQKKLPIIQKIIIMDSKTDYQ-----GFQSMYTFVTSHlPPGFNEYDFvpesfdRDKTIALIMNSSGSTGLPK 207
Cdd:cd12119 107 FLPLLEAIAPRLPTVEHVVVMTDDAAMPepagvGVLAYEELLAAE-SPEYDWPDF------DENTAAAICYTSGTTGNPK 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1216630836 208 GVALPHRTAcvrFSHA---RDPIFGNQIIPDTaILSVVP-FH-HGFGM-FTTLgylICGFRVVLMYRFEE-ELFLRSLQD 280
Cdd:cd12119 180 GVVYSHRSL---VLHAmaaLLTDGLGLSESDV-VLPVVPmFHvNAWGLpYAAA---MVGAKLVLPGPYLDpASLAELIER 252
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1216630836 281 YKIQSALLVPTLFSFFAKSTLIDKYDLSNLHEIASGGAPLSkevgEAVAKRFHLPGIR--QGYGLTET----TSAILITP 354
Cdd:cd12119 253 EGVTFAAGVPTVWQGLLDHLEANGRDLSSLRRVVIGGSAVP----RSLIEAFEERGVRviHAWGMTETsplgTVARPPSE 328
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1216630836 355 EGDDKPGAV-------GKVVPFFEAKVVDLDT------GKTlgvnqRGELCVRGPMIMSGYVNNPEATNALiDKDGWLHS 421
Cdd:cd12119 329 HSNLSEDEQlalrakqGRPVPGVELRIVDDDGrelpwdGKA-----VGELQVRGPWVTKSYYKNDEESEAL-TEDGWLRT 402
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1216630836 422 GDIAYWDEDEHFFIVDRLKSLIKYKGYQVAPAELESILLQHPNIFDAGVAGLPDDDAGELPAAVVVLEHGKTMTEKEIVD 501
Cdd:cd12119 403 GDVATIDEDGYLTITDRSKDVIKSGGEWISSVELENAIMAHPAVAEAAVIGVPHPKWGERPLAVVVLKEGATVTAEELLE 482
|
490 500 510
....*....|....*....|....*....|....*...
gi 1216630836 502 YVASQVttAK-KLRGGVVFVDEVPKGLTGKLDARKIRE 538
Cdd:cd12119 483 FLADKV--AKwWLPDDVVFVDEIPKTSTGKIDKKALRE 518
|
|
| FAA1 |
COG1022 |
Long-chain acyl-CoA synthetase (AMP-forming) [Lipid transport and metabolism]; |
19-465 |
6.63e-67 |
|
Long-chain acyl-CoA synthetase (AMP-forming) [Lipid transport and metabolism];
Pssm-ID: 440645 [Multi-domain] Cd Length: 603 Bit Score: 227.68 E-value: 6.63e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1216630836 19 EDGTAGEQLHKAMKRYalvPGTIAFT--DAHIEVDITYAEYFEMSVRLAEAMKRYGLNTNHRIVVCSENSLQFFMPVLGA 96
Cdd:COG1022 9 PADTLPDLLRRRAARF---PDRVALRekEDGIWQSLTWAEFAERVRALAAGLLALGVKPGDRVAILSDNRPEWVIADLAI 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1216630836 97 LFIGVAVAPandIY---NERELLNSMGISQPTVVFVSKKG-LQKILNVQKKLPIIQKIIIMDSKTDYQG-----FQSMYT 167
Cdd:COG1022 86 LAAGAVTVP---IYptsSAEEVAYILNDSGAKVLFVEDQEqLDKLLEVRDELPSLRHIVVLDPRGLRDDprllsLDELLA 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1216630836 168 FVTSHLPPGfnEYDFVPESFDRDkTIALIMNSSGSTGLPKGVALPHR--TACVRFSHARDPIFgnqiiPDTAILSVVPFH 245
Cdd:COG1022 163 LGREVADPA--ELEARRAAVKPD-DLATIIYTSGTTGRPKGVMLTHRnlLSNARALLERLPLG-----PGDRTLSFLPLA 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1216630836 246 HGFGMFTTLGYLICGFRVVlmyrFEE--ELFLRSLQDYKIQSALLVP----------------------TLFSFF----- 296
Cdd:COG1022 235 HVFERTVSYYALAAGATVA----FAEspDTLAEDLREVKPTFMLAVPrvwekvyagiqakaeeagglkrKLFRWAlavgr 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1216630836 297 -----------------AKSTLIDKYDLSNLHE--------IASGGAPLSKEVGEAvakrFH---LPgIRQGYGLTETTS 348
Cdd:COG1022 311 ryararlagkspslllrLKHALADKLVFSKLREalggrlrfAVSGGAALGPELARF----FRalgIP-VLEGYGLTETSP 385
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1216630836 349 AILITPEGDDKPGAVGKVVPFFEAKVVDldtgktlgvnqRGELCVRGPMIMSGYVNNPEATNALIDKDGWLHSGDIAYWD 428
Cdd:COG1022 386 VITVNRPGDNRIGTVGPPLPGVEVKIAE-----------DGEILVRGPNVMKGYYKNPEATAEAFDADGWLHTGDIGELD 454
|
490 500 510 520
....*....|....*....|....*....|....*....|..
gi 1216630836 429 EDEHFFIVDRLKSLI-----KYkgyqVAPAELESILLQHPNI 465
Cdd:COG1022 455 EDGFLRITGRKKDLIvtsggKN----VAPQPIENALKASPLI 492
|
|
| PRK06710 |
PRK06710 |
long-chain-fatty-acid--CoA ligase; Validated |
51-545 |
7.50e-67 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 180666 [Multi-domain] Cd Length: 563 Bit Score: 226.45 E-value: 7.50e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1216630836 51 DITYAEYFEMSVRLAEAMKRYGLNTNHRIVVCSENSLQFFMPVLGALFIGVAVAPANDIYNERELLNSMGISQPTVVFVS 130
Cdd:PRK06710 49 DITFSVFHDKVKRFANYLQKLGVEKGDRVAIMLPNCPQAVIGYYGTLLAGGIVVQTNPLYTERELEYQLHDSGAKVILCL 128
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1216630836 131 KKGLQKILNVQKKLPIiqKIIIMDSKTDYQGFQS--MYTFVT------------SHLPPGFNEYD-----FVPESFDRDK 191
Cdd:PRK06710 129 DLVFPRVTNVQSATKI--EHVIVTRIADFLPFPKnlLYPFVQkkqsnlvvkvseSETIHLWNSVEkevntGVEVPCDPEN 206
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1216630836 192 TIALIMNSSGSTGLPKGVALPHRTACVRFSHARDPIFgNQIIPDTAILSVVPFHHGFGMFTTLGYLIC-GFRVVLMYRFE 270
Cdd:PRK06710 207 DLALLQYTGGTTGFPKGVMLTHKNLVSNTLMGVQWLY-NCKEGEEVVLGVLPFFHVYGMTAVMNLSIMqGYKMVLIPKFD 285
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1216630836 271 EELFLRSLQDYKIQSALLVPTLFSFFAKSTLIDKYDLSNLHEIASGGAPLSKEVGEAVaKRFHLPGIRQGYGLTETTSAI 350
Cdd:PRK06710 286 MKMVFEAIKKHKVTLFPGAPTIYIALLNSPLLKEYDISSIRACISGSAPLPVEVQEKF-ETVTGGKLVEGYGLTESSPVT 364
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1216630836 351 LITPEGDDK-PGAVGKVVPFFEAKVVDLDTGKTLGVNQRGELCVRGPMIMSGYVNNPEATNALIdKDGWLHSGDIAYWDE 429
Cdd:PRK06710 365 HSNFLWEKRvPGSIGVPWPDTEAMIMSLETGEALPPGEIGEIVVKGPQIMKGYWNKPEETAAVL-QDGWLHTGDVGYMDE 443
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1216630836 430 DEHFFIVDRLKSLIKYKGYQVAPAELESILLQHPNIFDAGVAGLPDDDAGELPAAVVVLEHGKTMTEKEIvDYVASQVTT 509
Cdd:PRK06710 444 DGFFYVKDRKKDMIVASGFNVYPREVEEVLYEHEKVQEVVTIGVPDPYRGETVKAFVVLKEGTECSEEEL-NQFARKYLA 522
|
490 500 510
....*....|....*....|....*....|....*.
gi 1216630836 510 AKKLRGGVVFVDEVPKGLTGKLdarkIREILIKAKK 545
Cdd:PRK06710 523 AYKVPKVYEFRDELPKTTVGKI----LRRVLIEEEK 554
|
|
| PRK05605 |
PRK05605 |
long-chain-fatty-acid--CoA ligase; Validated |
52-545 |
6.46e-66 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 235531 [Multi-domain] Cd Length: 573 Bit Score: 224.11 E-value: 6.46e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1216630836 52 ITYAEYFEMSVRLAEAMKRYGLNTNHRIVVCSENSLQFFMPVLGALFIGVAVAPANDIYNERELLNSMGISQPTVVFVSK 131
Cdd:PRK05605 58 TTYAELGKQVRRAAAGLRALGVRPGDRVAIVLPNCPQHIVAFYAVLRLGAVVVEHNPLYTAHELEHPFEDHGARVAIVWD 137
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1216630836 132 K------------GLQKIL--NVQKKLPIIQKI-------IIMDSKTDYQG-------FQSMytfvTSHLPPGFNEYDFV 183
Cdd:PRK05605 138 KvaptverlrrttPLETIVsvNMIAAMPLLQRLalrlpipALRKARAALTGpapgtvpWETL----VDAAIGGDGSDVSH 213
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1216630836 184 PESfdRDKTIALIMNSSGSTGLPKGVALPHRT--ACVRFSHARDPIFGNQiipDTAILSVVPFHHGFG--MFTTLGYLIc 259
Cdd:PRK05605 214 PRP--TPDDVALILYTSGTTGKPKGAQLTHRNlfANAAQGKAWVPGLGDG---PERVLAALPMFHAYGltLCLTLAVSI- 287
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1216630836 260 GFRVVLMYRFEEELFLRSLQDYKIQSALLVPTLFSFFAKSTLIDKYDLSNLHEIASGGAPLSKEVgeaVAKRFHLPG--I 337
Cdd:PRK05605 288 GGELVLLPAPDIDLILDAMKKHPPTWLPGVPPLYEKIAEAAEERGVDLSGVRNAFSGAMALPVST---VELWEKLTGglL 364
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1216630836 338 RQGYGLTETTSAILITPEGDD-KPGAVGkvVPF--FEAKVVDLDT-GKTLGVNQRGELCVRGPMIMSGYVNNPEATNALI 413
Cdd:PRK05605 365 VEGYGLTETSPIIVGNPMSDDrRPGYVG--VPFpdTEVRIVDPEDpDETMPDGEEGELLVRGPQVFKGYWNRPEETAKSF 442
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1216630836 414 dKDGWLHSGDIAYWDEDEHFFIVDRLKSLIKYKGYQVAPAELESILLQHPNIFDAGVAGLPDDDAGELPAAVVVLEHGKT 493
Cdd:PRK05605 443 -LDGWFRTGDVVVMEEDGFIRIVDRIKELIITGGFNVYPAEVEEVLREHPGVEDAAVVGLPREDGSEEVVAAVVLEPGAA 521
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|..
gi 1216630836 494 MTEKEIVDYVASQVTTAKKLRgGVVFVDEVPKGLTGKLDARKIREILIKAKK 545
Cdd:PRK05605 522 LDPEGLRAYCREHLTRYKVPR-RFYHVDELPRDQLGKVRRREVREELLEKLG 572
|
|
| FACL_DitJ_like |
cd05934 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
52-537 |
1.29e-65 |
|
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: 219.47 E-value: 1.29e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1216630836 52 ITYAEYFEMSVRLAEAMKRYGLNTNHRIVVCSENSLQFFMPVLGALFIGVAVAPANDIYNERELLNSMGISQPTVVFVSk 131
Cdd:cd05934 4 WTYAELLRESARIAAALAALGIRPGDRVALMLDNCPEFLFAWFALAKLGAVLVPINTALRGDELAYIIDHSGAQLVVVD- 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1216630836 132 kgLQKILnvqkklpiiqkiiimdsktdyqgfqsmYTfvtshlppgfneydfvpesfdrdktialimnsSGSTGLPKGVAL 211
Cdd:cd05934 83 --PASIL---------------------------YT--------------------------------SGTTGPPKGVVI 101
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1216630836 212 PHR---TACVRFSHARDpifgnqIIPDTAILSVVPFHHGFGMFTT-LGYLICGFRVVLMYRFEEELFLRSLQDYKIQSAL 287
Cdd:cd05934 102 THAnltFAGYYSARRFG------LGEDDVYLTVLPLFHINAQAVSvLAALSVGATLVLLPRFSASRFWSDVRRYGATVTN 175
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1216630836 288 LVPTLFSFFAKsTLIDKYDLSN-LHEIASGGAPlsKEVGEAVAKRFHLPgIRQGYGLTETTSAILITPEGDDKPGAVGKV 366
Cdd:cd05934 176 YLGAMLSYLLA-QPPSPDDRAHrLRAAYGAPNP--PELHEEFEERFGVR-LLEGYGMTETIVGVIGPRDEPRRPGSIGRP 251
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1216630836 367 VPFFEAKVVDlDTGKTLGVNQRGELCVR---GPMIMSGYVNNPEATNALIdKDGWLHSGDIAYWDEDEHFFIVDRLKSLI 443
Cdd:cd05934 252 APGYEVRIVD-DDGQELPAGEPGELVIRglrGWGFFKGYYNMPEATAEAM-RNGWFHTGDLGYRDADGFFYFVDRKKDMI 329
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1216630836 444 KYKGYQVAPAELESILLQHPNIFDAGVAGLPDDDAGELPAAVVVLEHGKTMTEKEIVDYVASQVTTaKKLRGGVVFVDEV 523
Cdd:cd05934 330 RRRGENISSAEVERAILRHPAVREAAVVAVPDEVGEDEVKAVVVLRPGETLDPEELFAFCEGQLAY-FKVPRYIRFVDDL 408
|
490
....*....|....
gi 1216630836 524 PKGLTGKLDARKIR 537
Cdd:cd05934 409 PKTPTEKVAKAQLR 422
|
|
| PRK08316 |
PRK08316 |
acyl-CoA synthetase; Validated |
22-543 |
7.13e-64 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 181381 [Multi-domain] Cd Length: 523 Bit Score: 217.49 E-value: 7.13e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1216630836 22 TAGEQLHKAMKRYalvPGTIAFTDAhiEVDITYAEYFEMSVRLAEAMKRYGLNTNHRIVVCSENSLQFFMPVLGALFIGV 101
Cdd:PRK08316 12 TIGDILRRSARRY---PDKTALVFG--DRSWTYAELDAAVNRVAAALLDLGLKKGDRVAALGHNSDAYALLWLACARAGA 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1216630836 102 AVAPANDIYNERELLNSMGISQPTVVFVSKKGLQKILNVQKKLPIIQKI-IIMDSKTDYQG----FQSMYTfvtshlppg 176
Cdd:PRK08316 87 VHVPVNFMLTGEELAYILDHSGARAFLVDPALAPTAEAALALLPVDTLIlSLVLGGREAPGgwldFADWAE--------- 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1216630836 177 fNEYDFVPESFDRDKTIALIMNSSGSTGLPKGVALPHR------TACvrfshardpIFGNQIIPDTAILSVVPFHHGFGM 250
Cdd:PRK08316 158 -AGSVAEPDVELADDDLAQILYTSGTESLPKGAMLTHRaliaeyVSC---------IVAGDMSADDIPLHALPLYHCAQL 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1216630836 251 FTTLG-YLICGFRVVLMYRFEEELFLRSLQDYKIQSALLVPTLFSFFAKSTLIDKYDLSNLHEIASGGAPLSKEVGEAVA 329
Cdd:PRK08316 228 DVFLGpYLYVGATNVILDAPDPELILRTIEAERITSFFAPPTVWISLLRHPDFDTRDLSSLRKGYYGASIMPVEVLKELR 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1216630836 330 KRfhLPGIR--QGYGLTET--TSAILITPEGDDKPGAVGKVVPFFEAKVVDlDTGKTLGVNQRGELCVRGPMIMSGYVNN 405
Cdd:PRK08316 308 ER--LPGLRfyNCYGQTEIapLATVLGPEEHLRRPGSAGRPVLNVETRVVD-DDGNDVAPGEVGEIVHRSPQLMLGYWDD 384
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1216630836 406 PEATNALIdKDGWLHSGDIAYWDEDEHFFIVDRLKSLIKYKGYQVAPAELESILLQHPNIFDAGVAGLPDDDAGELPAAV 485
Cdd:PRK08316 385 PEKTAEAF-RGGWFHSGDLGVMDEEGYITVVDRKKDMIKTGGENVASREVEEALYTHPAVAEVAVIGLPDPKWIEAVTAV 463
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*...
gi 1216630836 486 VVLEHGKTMTEKEIVDYVASQVtTAKKLRGGVVFVDEVPKGLTGKLDARKIREILIKA 543
Cdd:PRK08316 464 VVPKAGATVTEDELIAHCRARL-AGFKVPKRVIFVDELPRNPSGKILKRELRERYAGA 520
|
|
| MACS_like |
cd05972 |
Medium-chain acyl-CoA synthetase (MACS or ACSM); MACS catalyzes the two-step activation of ... |
53-537 |
2.27e-63 |
|
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: 213.74 E-value: 2.27e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1216630836 53 TYAEYFEMSVRLAEAMKRYGLNTNHRIVVCSENSLQFFMPVLGALFIGVAVAPANDIYNERELLNSMGISQPtvvfvskk 132
Cdd:cd05972 2 SFRELKRESAKAANVLAKLGLRKGDRVAVLLPRVPELWAVILAVIKLGAVYVPLTTLLGPKDIEYRLEAAGA-------- 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1216630836 133 glqkilnvqkklpiiqKIIIMDSKTdyqgfqsmytfvtshlppgfneydfvpesfdrdktIALIMNSSGSTGLPKGVALP 212
Cdd:cd05972 74 ----------------KAIVTDAED-----------------------------------PALIYFTSGTTGLPKGVLHT 102
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1216630836 213 HRTACVRFSHARDPIfgnQIIPDTAILSVV-PFHHGFGMFTTLGYLICGFRVVL--MYRFEEELFLRSLQDYKIQSALLV 289
Cdd:cd05972 103 HSYPLGHIPTAAYWL---GLRPDDIHWNIAdPGWAKGAWSSFFGPWLLGATVFVyeGPRFDAERILELLERYGVTSFCGP 179
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1216630836 290 PTLFSFFAKStLIDKYDLSNLHEIASGGAPLSKEVGEAVAKRFHLPgIRQGYGLTETTSAILITPEGDDKPGAVGKVVPF 369
Cdd:cd05972 180 PTAYRMLIKQ-DLSSYKFSHLRLVVSAGEPLNPEVIEWWRAATGLP-IRDGYGQTETGLTVGNFPDMPVKPGSMGRPTPG 257
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1216630836 370 FEAKVVDlDTGKTLGVNQRGELCVR--GPMIMSGYVNNPEATNALIdKDGWLHSGDIAYWDEDEHFFIVDRLKSLIKYKG 447
Cdd:cd05972 258 YDVAIID-DDGRELPPGEEGDIAIKlpPPGLFLGYVGDPEKTEASI-RGDYYLTGDRAYRDEDGYFWFVGRADDIIKSSG 335
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1216630836 448 YQVAPAELESILLQHPNIFDAGVAGLPDDDAGELPAAVVVLEHGKTMTEK---EIVDYVASQVTTAKKLRgGVVFVDEVP 524
Cdd:cd05972 336 YRIGPFEVESALLEHPAVAEAAVVGSPDPVRGEVVKAFVVLTSGYEPSEElaeELQGHVKKVLAPYKYPR-EIEFVEELP 414
|
490
....*....|...
gi 1216630836 525 KGLTGKLDARKIR 537
Cdd:cd05972 415 KTISGKIRRVELR 427
|
|
| PRK03640 |
PRK03640 |
o-succinylbenzoate--CoA ligase; |
31-540 |
1.14e-62 |
|
o-succinylbenzoate--CoA ligase;
Pssm-ID: 235146 [Multi-domain] Cd Length: 483 Bit Score: 213.29 E-value: 1.14e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1216630836 31 MKRYALVPGTIAFTDAHIEvdITYAEYFEMSVRLAEAMKRYGLNTNHRIVVCSENSLQFFMPVLGALFIGVAVAPANDIY 110
Cdd:PRK03640 9 KQRAFLTPDRTAIEFEEKK--VTFMELHEAVVSVAGKLAALGVKKGDRVALLMKNGMEMILVIHALQQLGAVAVLLNTRL 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1216630836 111 NERELLNSMGISQPTVVFVSKkglqkilNVQKKLPIIQKIIImdsktdyqgfqsmytfvtSHLPPGFNEYDFVPESFDRD 190
Cdd:PRK03640 87 SREELLWQLDDAEVKCLITDD-------DFEAKLIPGISVKF------------------AELMNGPKEEAEIQEEFDLD 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1216630836 191 KTiALIMNSSGSTGLPKGVALphrTACVRFSHARDPIFGNQIIPDTAILSVVPFHHGFGMFTTLGYLICGFRVVLMYRFE 270
Cdd:PRK03640 142 EV-ATIMYTSGTTGKPKGVIQ---TYGNHWWSAVGSALNLGLTEDDCWLAAVPIFHISGLSILMRSVIYGMRVVLVEKFD 217
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1216630836 271 EELFLRSLQDYKIQSALLVPTLFSffaksTLIDKYDLSNLHE----IASGGAPLSKEVGEaVAKRFHLPGIrQGYGLTET 346
Cdd:PRK03640 218 AEKINKLLQTGGVTIISVVSTMLQ-----RLLERLGEGTYPSsfrcMLLGGGPAPKPLLE-QCKEKGIPVY-QSYGMTET 290
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1216630836 347 TSAILITPEGD--DKPGAVGKvvPFFEAKVVDLDTGKTLGVNQRGELCVRGPMIMSGYVNNPEATNALIdKDGWLHSGDI 424
Cdd:PRK03640 291 ASQIVTLSPEDalTKLGSAGK--PLFPCELKIEKDGVVVPPFEEGEIVVKGPNVTKGYLNREDATRETF-QDGWFKTGDI 367
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1216630836 425 AYWDEDEHFFIVDRLKSLIKYKGYQVAPAELESILLQHPNIFDAGVAGLPDDDAGELPAAVVVleHGKTMTEKEIVDYVA 504
Cdd:PRK03640 368 GYLDEEGFLYVLDRRSDLIISGGENIYPAEIEEVLLSHPGVAEAGVVGVPDDKWGQVPVAFVV--KSGEVTEEELRHFCE 445
|
490 500 510
....*....|....*....|....*....|....*..
gi 1216630836 505 SQVttAK-KLRGGVVFVDEVPKGLTGKLDARKIREIL 540
Cdd:PRK03640 446 EKL--AKyKVPKRFYFVEELPRNASGKLLRHELKQLV 480
|
|
| BCL_4HBCL |
cd05959 |
Benzoate CoA ligase (BCL) and 4-Hydroxybenzoate-Coenzyme A Ligase (4-HBA-CoA ligase); Benzoate ... |
38-537 |
6.79e-62 |
|
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: 211.84 E-value: 6.79e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1216630836 38 PGTIAFTDAHIEvdITYAEYFEMSVRLAEAMKRYGLNTNHRIVVCSENSLQFFMPVLGALFIGVAVAPANDIYNERELLN 117
Cdd:cd05959 18 GDKTAFIDDAGS--LTYAELEAEARRVAGALRALGVKREERVLLIMLDTVDFPTAFLGAIRAGIVPVPVNTLLTPDDYAY 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1216630836 118 SMGISQPTVVFVSKKGLQKILN-VQKKLPIIQKIIIMDSKTDYQGFQSMYTFVTSHLPpgfneyDFVPESFDRDKtIALI 196
Cdd:cd05959 96 YLEDSRARVVVVSGELAPVLAAaLTKSEHTLVVLIVSGGAGPEAGALLLAELVAAEAE------QLKPAATHADD-PAFW 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1216630836 197 MNSSGSTGLPKGVALPHRTACVRFSHARDPIFGnqIIPDTAILSVVP--FHHGFG--MFTTLGYlicGFRVVLM-YRFEE 271
Cdd:cd05959 169 LYSSGSTGRPKGVVHLHADIYWTAELYARNVLG--IREDDVCFSAAKlfFAYGLGnsLTFPLSV---GATTVLMpERPTP 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1216630836 272 ELFLRSLQDYKIQSALLVPTLFSFFAKSTLIDKYDLSNLHEIASGGAPLSKEVGEAVAKRFHLPgIRQGYGLTETTSAIL 351
Cdd:cd05959 244 AAVFKRIRRYRPTVFFGVPTLYAAMLAAPNLPSRDLSSLRLCVSAGEALPAEVGERWKARFGLD-ILDGIGSTEMLHIFL 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1216630836 352 ITPEGDDKPGAVGKVVPFFEAKVVDlDTGKTLGVNQRGELCVRGPMIMSGYVNNPEATNALIdKDGWLHSGDIAYWDEDE 431
Cdd:cd05959 323 SNRPGRVRYGTTGKPVPGYEVELRD-EDGGDVADGEPGELYVRGPSSATMYWNNRDKTRDTF-QGEWTRTGDKYVRDDDG 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1216630836 432 HFFIVDRLKSLIKYKGYQVAPAELESILLQHPNIFDAGVAGLPDDDAGELPAAVVVLEHGKTMTEK---EIVDYVASQVT 508
Cdd:cd05959 401 FYTYAGRADDMLKVSGIWVSPFEVESALVQHPAVLEAAVVGVEDEDGLTKPKAFVVLRPGYEDSEAleeELKEFVKDRLA 480
|
490 500
....*....|....*....|....*....
gi 1216630836 509 TAKKLRgGVVFVDEVPKGLTGKLDARKIR 537
Cdd:cd05959 481 PYKYPR-WIVFVDELPKTATGKIQRFKLR 508
|
|
| PRK06188 |
PRK06188 |
acyl-CoA synthetase; Validated |
19-538 |
3.68e-60 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 235731 [Multi-domain] Cd Length: 524 Bit Score: 207.53 E-value: 3.68e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1216630836 19 EDGTAGEQLHKAMKRYalvPGTIAFTDAhiEVDITYAEYFEMSVRLAEAMKRYGLNTNHRIVVCSENSLQFFMPVLGALF 98
Cdd:PRK06188 10 SGATYGHLLVSALKRY---PDRPALVLG--DTRLTYGQLADRISRYIQAFEALGLGTGDAVALLSLNRPEVLMAIGAAQL 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1216630836 99 IG---VAVAPANDIYNERELLNSMGISqpTVVFVSKKGLQKILNVQKKLPIIQKIIIMDSKTDYQGFQSmytfvtshlpp 175
Cdd:PRK06188 85 AGlrrTALHPLGSLDDHAYVLEDAGIS--TLIVDPAPFVERALALLARVPSLKHVLTLGPVPDGVDLLA----------- 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1216630836 176 GFNEYDFVP-ESFDRDKTIALIMNSSGSTGLPKGVALPHRTACVRfshardpifgNQII-------PDTAILSVVPFHHG 247
Cdd:PRK06188 152 AAAKFGPAPlVAAALPPDIAGLAYTGGTTGKPKGVMGTHRSIATM----------AQIQlaewewpADPRFLMCTPLSHA 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1216630836 248 FGMFTTLGyLICGFRVVLMYRFEEELFLRSLQDYKIQSALLVPTLFSffaksTLID-----KYDLSNLHEIASGGAPLSK 322
Cdd:PRK06188 222 GGAFFLPT-LLRGGTVIVLAKFDPAEVLRAIEEQRITATFLVPTMIY-----ALLDhpdlrTRDLSSLETVYYGASPMSP 295
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1216630836 323 -EVGEAVaKRFHlPGIRQGYGLTETTSAILITPEGDDKP------GAVGKVVPFFEAKVVDlDTGKTLGVNQRGELCVRG 395
Cdd:PRK06188 296 vRLAEAI-ERFG-PIFAQYYGQTEAPMVITYLRKRDHDPddpkrlTSCGRPTPGLRVALLD-EDGREVAQGEVGEICVRG 372
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1216630836 396 PMIMSGYVNNPEATnALIDKDGWLHSGDIAYWDEDEHFFIVDRLKSLIKYKGYQVAPAELESILLQHPNIFDAGVAGLPD 475
Cdd:PRK06188 373 PLVMDGYWNRPEET-AEAFRDGWLHTGDVAREDEDGFYYIVDRKKDMIVTGGFNVFPREVEDVLAEHPAVAQVAVIGVPD 451
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1216630836 476 DDAGELPAAVVVLEHGKTMTEKEIVDYVASQ---VTTAKKlrggVVFVDEVPKGLTGKLDARKIRE 538
Cdd:PRK06188 452 EKWGEAVTAVVVLRPGAAVDAAELQAHVKERkgsVHAPKQ----VDFVDSLPLTALGKPDKKALRA 513
|
|
| VL_LC_FACS_like |
cd05907 |
Long-chain fatty acid CoA synthetases and Bubblegum-like very long-chain fatty acid CoA ... |
48-489 |
4.34e-60 |
|
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: 205.52 E-value: 4.34e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1216630836 48 IEVDITYAEYFEMSVRLAEAMKRYGLNTNHRIVVCSENSLQFFMPVLGALFIGVAVAPandIY------NERELLNSmgi 121
Cdd:cd05907 2 VWQPITWAEFAEEVRALAKGLIALGVEPGDRVAILSRNRPEWTIADLAILAIGAVPVP---IYptssaeQIAYILND--- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1216630836 122 SQPTVVFVSKK-GLQKIlnvqkklpiiqkiiimdsktdyqgfqsMYTfvtshlppgfneydfvpesfdrdktialimnsS 200
Cdd:cd05907 76 SEAKALFVEDPdDLATI---------------------------IYT--------------------------------S 96
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1216630836 201 GSTGLPKGVALPHRTACvrfSHARDpifGNQIIPDTA---ILSVVPFHHGFGMFTTLgYLICGFRVVLMYRFEEELFLRS 277
Cdd:cd05907 97 GTTGRPKGVMLSHRNIL---SNALA---LAERLPATEgdrHLSFLPLAHVFERRAGL-YVPLLAGARIYFASSAETLLDD 169
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1216630836 278 LQDYKIQSALLVPTLF-SFFA----------KSTLIDKYDLSNLHEIASGGAPLSKEVGEavakRFHLPGI--RQGYGLT 344
Cdd:cd05907 170 LSEVRPTVFLAVPRVWeKVYAaikvkavpglKRKLFDLAVGGRLRFAASGGAPLPAELLH----FFRALGIpvYEGYGLT 245
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1216630836 345 ETTSAILITPEGDDKPGAVGKVVPFFEAKVVDldtgktlgvnqRGELCVRGPMIMSGYVNNPEATNALIDKDGWLHSGDI 424
Cdd:cd05907 246 ETSAVVTLNPPGDNRIGTVGKPLPGVEVRIAD-----------DGEILVRGPNVMLGYYKNPEATAEALDADGWLHTGDL 314
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1216630836 425 AYWDEDEHFFIVDRLKSLIKY-KGYQVAPAELESILLQHPNIFDAGVAGlpddDAGELPAAVVVLE 489
Cdd:cd05907 315 GEIDEDGFLHITGRKKDLIITsGGKNISPEPIENALKASPLISQAVVIG----DGRPFLVALIVPD 376
|
|
| MACS_AAE_MA_like |
cd05970 |
Medium-chain acyl-CoA synthetase (MACS) of AAE_MA like; MACS catalyzes the two-step activation ... |
45-538 |
4.88e-59 |
|
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: 205.04 E-value: 4.88e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1216630836 45 DAHIEVDITYAEYFEMSVRLAEAMKRYGLNTNHRIVVCSENSLQFFMPVLGALFIGVAVAPANDIYNEREL---LNSMGI 121
Cdd:cd05970 41 DAGEERIFTFAELADYSDKTANFFKAMGIGKGDTVMLTLKRRYEFWYSLLALHKLGAIAIPATHQLTAKDIvyrIESADI 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1216630836 122 SQptVVFVSKKGL-QKILNVQKKLPIIQKIIIMdSKTDYQGFQSMYTFVtSHLPPgfneyDFVP---ESFDRDKTIALIM 197
Cdd:cd05970 121 KM--IVAIAEDNIpEEIEKAAPECPSKPKLVWV-GDPVPEGWIDFRKLI-KNASP-----DFERptaNSYPCGEDILLVY 191
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1216630836 198 NSSGSTGLPKGVALPHRTAcvrFSHARDPIFGNQIIPDTAILSVVPFHHGFGMFTTL-GYLICGFRVVL--MYRFEEELF 274
Cdd:cd05970 192 FSSGTTGMPKMVEHDFTYP---LGHIVTAKYWQNVREGGLHLTVADTGWGKAVWGKIyGQWIAGAAVFVydYDKFDPKAL 268
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1216630836 275 LRSLQDYKIQSALLVPTLFSFFAKSTLiDKYDLSNLHEIASGGAPLSKEVGEAVAKRFHLPgIRQGYGLTETTSAILITP 354
Cdd:cd05970 269 LEKLSKYGVTTFCAPPTIYRFLIREDL-SRYDLSSLRYCTTAGEALNPEVFNTFKEKTGIK-LMEGFGQTETTLTIATFP 346
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1216630836 355 EGDDKPGAVGKVVPFFEAKVVDLDtGKTLGVNQRGELCVR----GPM-IMSGYVNNPEATnALIDKDGWLHSGDIAYWDE 429
Cdd:cd05970 347 WMEPKPGSMGKPAPGYEIDLIDRE-GRSCEAGEEGEIVIRtskgKPVgLFGGYYKDAEKT-AEVWHDGYYHTGDAAWMDE 424
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1216630836 430 DEHFFIVDRLKSLIKYKGYQVAPAELESILLQHPNIFDAGVAGLPDDDAGELPAAVVVLEHGKTMTE---KEIVDYVaSQ 506
Cdd:cd05970 425 DGYLWFVGRTDDLIKSSGYRIGPFEVESALIQHPAVLECAVTGVPDPIRGQVVKATIVLAKGYEPSEelkKELQDHV-KK 503
|
490 500 510
....*....|....*....|....*....|..
gi 1216630836 507 VTTAKKLRGGVVFVDEVPKGLTGKLDARKIRE 538
Cdd:cd05970 504 VTAPYKYPRIVEFVDELPKTISGKIRRVEIRE 535
|
|
| MCS |
cd05941 |
Malonyl-CoA synthetase (MCS); MCS catalyzes the formation of malonyl-CoA in a two-step ... |
52-538 |
5.57e-58 |
|
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: 199.82 E-value: 5.57e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1216630836 52 ITYAEYFEMSVRLAEAM-KRYGLNTNHRIVVCSENSLQFFMPVLGALFIGVAVAPANDIYNERELLNSMGISQPTvvfvs 130
Cdd:cd05941 12 ITYADLVARAARLANRLlALGKDLRGDRVAFLAPPSAEYVVAQLAIWRAGGVAVPLNPSYPLAELEYVITDSEPS----- 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1216630836 131 kkglqkilnvqkklpiiqkiIIMDsktdyqgfqsmytfvtshlppgfneydfvpesfdrdktIALIMNSSGSTGLPKGVA 210
Cdd:cd05941 87 --------------------LVLD--------------------------------------PALILYTSGTTGRPKGVV 108
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1216630836 211 LPHR--TACVR-FSHARdpifgnQIIPDTAILSVVPFHHGFGMFTTL-GYLICGFRVVLMYRFEEELFLRSLQDYKIQSA 286
Cdd:cd05941 109 LTHAnlAANVRaLVDAW------RWTEDDVLLHVLPLHHVHGLVNALlCPLFAGASVEFLPKFDPKEVAISRLMPSITVF 182
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1216630836 287 LLVPTLFS--------FFAKSTLIDKYDLSNLHEIASGGAPLSKEVGEAVAKRFHLPgIRQGYGLTETTSAiLITP-EGD 357
Cdd:cd05941 183 MGVPTIYTrllqyyeaHFTDPQFARAAAAERLRLMVSGSAALPVPTLEEWEAITGHT-LLERYGMTEIGMA-LSNPlDGE 260
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1216630836 358 DKPGAVGKVVPFFEAKVVDLDTGKTLGVNQRGELCVRGPMIMSGYVNNPEATNALIDKDGWLHSGDIAYWDEDEHFFIVD 437
Cdd:cd05941 261 RRPGTVGMPLPGVQARIVDEETGEPLPRGEVGEIQVRGPSVFKEYWNKPEATKEEFTDDGWFKTGDLGVVDEDGYYWILG 340
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1216630836 438 RLKS-LIKYKGYQVAPAELESILLQHPNIFDAGVAGLPDDDAGELPAAVVVLEHGK-TMTEKEIVDyVASQVTTAKKLRG 515
Cdd:cd05941 341 RSSVdIIKSGGYKVSALEIERVLLAHPGVSECAVIGVPDPDWGERVVAVVVLRAGAaALSLEELKE-WAKQRLAPYKRPR 419
|
490 500
....*....|....*....|...
gi 1216630836 516 GVVFVDEVPKGLTGKLDARKIRE 538
Cdd:cd05941 420 RLILVDELPRNAMGKVNKKELRK 442
|
|
| menE |
TIGR01923 |
O-succinylbenzoate-CoA ligase; This model represents an enzyme, O-succinylbenzoate-CoA ligase, ... |
53-536 |
8.16e-58 |
|
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: 199.21 E-value: 8.16e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1216630836 53 TYAEYFEMSVRLAEAMKRYGLNTNHRIVVCSENSLQFFMPVLGALFIGVAVAPANDIYNERELLNSMGISQPTVVFVskk 132
Cdd:TIGR01923 1 TWQDLDCEAAHLAKALKAQGIRSGSRVALVGQNSIEMVLLLHACLLLGAEIAMLNTRLTENERTNQLEDLDVQLLLT--- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1216630836 133 glqkilnvqkklpiiqkiiimDSKTDYQGFQSmytfVTSHLPPGFNEYDFVPESFDRDKTIALIMNSSGSTGLPKGVALP 212
Cdd:TIGR01923 78 ---------------------DSLLEEKDFQA----DSLDRIEAAGRYETSLSASFNMDQIATLMFTSGTTGKPKAVPHT 132
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1216630836 213 HRTacvRFSHARDPIFGNQIIPDTAILSVVPFHHGFGMFTTLGYLICGFRVVLMYRFEEelFLRSLQDYKIQSALLVPTL 292
Cdd:TIGR01923 133 FRN---HYASAVGSKENLGFTEDDNWLLSLPLYHISGLSILFRWLIEGATLRIVDKFNQ--LLEMIANERVTHISLVPTQ 207
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1216630836 293 FSFFAKSTLIDkydlSNLHEIASGGAPLSKEVGEAVAKRfHLPgIRQGYGLTETTSAIL-ITPEGDDKPGAVGKVVPFFE 371
Cdd:TIGR01923 208 LNRLLDEGGHN----ENLRKILLGGSAIPAPLIEEAQQY-GLP-IYLSYGMTETCSQVTtATPEMLHARPDVGRPLAGRE 281
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1216630836 372 AKV-VDLDTGktlgvnqRGELCVRGPMIMSGYVNNPEATNAlIDKDGWLHSGDIAYWDEDEHFFIVDRLKSLIKYKGYQV 450
Cdd:TIGR01923 282 IKIkVDNKEG-------HGEIMVKGANLMKGYLYQGELTPA-FEQQGWFNTGDIGELDGEGFLYVLGRRDDLIISGGENI 353
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1216630836 451 APAELESILLQHPNIFDAGVAGLPDDDAGELPAAVVVLEhgKTMTEKEIVDYVASQVttAK-KLRGGVVFVDEVPKGLTG 529
Cdd:TIGR01923 354 YPEEIETVLYQHPGIQEAVVVPKPDAEWGQVPVAYIVSE--SDISQAKLIAYLTEKL--AKyKVPIAFEKLDELPYNASG 429
|
....*..
gi 1216630836 530 KLDARKI 536
Cdd:TIGR01923 430 KILRNQL 436
|
|
| PRK05677 |
PRK05677 |
long-chain-fatty-acid--CoA ligase; Validated |
27-548 |
1.65e-56 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 168170 [Multi-domain] Cd Length: 562 Bit Score: 198.83 E-value: 1.65e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1216630836 27 LHKAMKRYALVPgtiAFTDahIEVDITYAEYFEMSVRLAEAMKRY-GLNTNHRIVVCSENSLQFFMPVLGALFIGVAVAP 105
Cdd:PRK05677 30 LKQSCQRFADKP---AFSN--LGKTLTYGELYKLSGAFAAWLQQHtDLKPGDRIAVQLPNVLQYPVAVFGAMRAGLIVVN 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1216630836 106 ANDIYNERELLNSMGISQPTVVF------------VSKKGLQKIL--NVQKKLPIIQKIIIMDSKTDYQGFQSMYtfvts 171
Cdd:PRK05677 105 TNPLYTAREMEHQFNDSGAKALVclanmahlaekvLPKTGVKHVIvtEVADMLPPLKRLLINAVVKHVKKMVPAY----- 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1216630836 172 HLPP--GFNE-------YDFVPESFDRDKtIALIMNSSGSTGLPKGVALPHRTACVRFSHARDPIFGNQIIPDTAILSVV 242
Cdd:PRK05677 180 HLPQavKFNDalakgagQPVTEANPQADD-VAVLQYTGGTTGVAKGAMLTHRNLVANMLQCRALMGSNLNEGCEILIAPL 258
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1216630836 243 PFHHGFGM-FTTLGYLICGFRVVLMYRFEE-ELFLRSLQDYKIQSALLVPTLFSFFAKSTLIDKYDLSNLHEIASGGAPL 320
Cdd:PRK05677 259 PLYHIYAFtFHCMAMMLIGNHNILISNPRDlPAMVKELGKWKFSGFVGLNTLFVALCNNEAFRKLDFSALKLTLSGGMAL 338
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1216630836 321 SKevgeAVAKRF-HLPG--IRQGYGLTETTSAILITPEGDDKPGAVGKVVPFFEAKVVDlDTGKTLGVNQRGELCVRGPM 397
Cdd:PRK05677 339 QL----ATAERWkEVTGcaICEGYGMTETSPVVSVNPSQAIQVGTIGIPVPSTLCKVID-DDGNELPLGEVGELCVKGPQ 413
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1216630836 398 IMSGYVNNPEATNALIDKDGWLHSGDIAYWDEDEHFFIVDRLKSLIKYKGYQVAPAELESILLQHPNIFDAGVAGLPDDD 477
Cdd:PRK05677 414 VMKGYWQRPEATDEILDSDGWLKTGDIALIQEDGYMRIVDRKKDMILVSGFNVYPNELEDVLAALPGVLQCAAIGVPDEK 493
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1216630836 478 AGELPAAVVVLEHGKTMTEKEIVDYVASQVTTAKKLRgGVVFVDEVPKGLTGKLDARKIREILIKaKKGGK 548
Cdd:PRK05677 494 SGEAIKVFVVVKPGETLTKEQVMEHMRANLTGYKVPK-AVEFRDELPTTNVGKILRRELRDEELK-KAGLK 562
|
|
| PRK07788 |
PRK07788 |
acyl-CoA synthetase; Validated |
21-539 |
2.33e-56 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236097 [Multi-domain] Cd Length: 549 Bit Score: 197.84 E-value: 2.33e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1216630836 21 GTAGEQLHKAMKRYalvPGTIAFTDAHIEvdITYAEYFEMSVRLAEAMKRYGLNTNHRIVVCSENSLQFFMPVLGALFIG 100
Cdd:PRK07788 49 GPFAGLVAHAARRA---PDRAALIDERGT--LTYAELDEQSNALARGLLALGVRAGDGVAVLARNHRGFVLALYAAGKVG 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1216630836 101 VAVApandiynereLLNSmGISQPTVVFVSKKglQKIlnvqkklpiiqKIIIMDSKtdyqgfqsmYTFVTSHLPPGFNEY 180
Cdd:PRK07788 124 ARII----------LLNT-GFSGPQLAEVAAR--EGV-----------KALVYDDE---------FTDLLSALPPDLGRL 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1216630836 181 -------DFVPESFDRDKTIA-------------------LIMNSSGSTGLPKGVALPHRTACVrfshardpifgnqiiP 234
Cdd:PRK07788 171 rawggnpDDDEPSGSTDETLDdliagsstaplpkppkpggIVILTSGTTGTPKGAPRPEPSPLA---------------P 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1216630836 235 DTAILSVVPFHHGF------GMFTTLGY----LICGFR--VVLMYRFEEELFLRSLQDYKIQSALLVPTLFSFF--AKST 300
Cdd:PRK07788 236 LAGLLSRVPFRAGEttllpaPMFHATGWahltLAMALGstVVLRRRFDPEATLEDIAKHKATALVVVPVMLSRIldLGPE 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1216630836 301 LIDKYDLSNLHEIASGGAPLSKEVGEAVAKRFHlPGIRQGYGLTETTSAILITPEGDDK-PGAVGKVVPFFEAKVVDlDT 379
Cdd:PRK07788 316 VLAKYDTSSLKIIFVSGSALSPELATRALEAFG-PVLYNLYGSTEVAFATIATPEDLAEaPGTVGRPPKGVTVKILD-EN 393
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1216630836 380 GKTLGVNQRGELCVRGPMIMSGYVN--NPEAtnalidKDGWLHSGDIAYWDEDEHFFIVDRLKSLIKYKGYQVAPAELES 457
Cdd:PRK07788 394 GNEVPRGVVGRIFVGNGFPFEGYTDgrDKQI------IDGLLSSGDVGYFDEDGLLFVDGRDDDMIVSGGENVFPAEVED 467
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1216630836 458 ILLQHPNIFDAGVAGLPDDDAGELPAAVVVLEHGKTMTEKEIVDYVASQVTTAKKLRgGVVFVDEVPKGLTGKLDARKIR 537
Cdd:PRK07788 468 LLAGHPDVVEAAVIGVDDEEFGQRLRAFVVKAPGAALDEDAIKDYVRDNLARYKVPR-DVVFLDELPRNPTGKVLKRELR 546
|
..
gi 1216630836 538 EI 539
Cdd:PRK07788 547 EM 548
|
|
| PRK06178 |
PRK06178 |
acyl-CoA synthetase; Validated |
13-532 |
3.98e-56 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 235724 [Multi-domain] Cd Length: 567 Bit Score: 197.57 E-value: 3.98e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1216630836 13 APFYPLEDGTAGEQLHKAMKRYALVPGTIAFtdAHievDITYAEYFEMSVRLAEAMKRYGLNTNHRIVVCSENSLQFFMP 92
Cdd:PRK06178 25 EPEYPHGERPLTEYLRAWARERPQRPAIIFY--GH---VITYAELDELSDRFAALLRQRGVGAGDRVAVFLPNCPQFHIV 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1216630836 93 VLGALFIGVAVAPANDIYNERELLNSMGISQPTVVFVSKKGLQKILNVQKKLPIiqKIIIMDSKTDyqgfqsmytFVTSH 172
Cdd:PRK06178 100 FFGILKLGAVHVPVSPLFREHELSYELNDAGAEVLLALDQLAPVVEQVRAETSL--RHVIVTSLAD---------VLPAE 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1216630836 173 ----LPPGFNE--------YDFVP-----------ESFDRDKTIALimN-SSGSTGLPKGVALPHR-------TAC-VRF 220
Cdd:PRK06178 169 ptlpLPDSLRAprlaaagaIDLLPalractapvplPPPALDALAAL--NyTGGTTGMPKGCEHTQRdmvytaaAAYaVAV 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1216630836 221 SHARDPIFgnqiipdtaiLSVVPFH----HGFGMfttLGYLICGFRVVLMYRFEEELFLRSLQDYKIQS-ALLVPTLFSF 295
Cdd:PRK06178 247 VGGEDSVF----------LSFLPEFwiagENFGL---LFPLFSGATLVLLARWDAVAFMAAVERYRVTRtVMLVDNAVEL 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1216630836 296 FAKSTLIDkYDLSNLHEIasGGAPLSKEVGEAVAKRFH-LPG--IRQG-YGLTETTSAILITP--EGDD-----KPGAVG 364
Cdd:PRK06178 314 MDHPRFAE-YDLSSLRQV--RVVSFVKKLNPDYRQRWRaLTGsvLAEAaWGMTETHTCDTFTAgfQDDDfdllsQPVFVG 390
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1216630836 365 KVVPFFEAKVVDLDTGKTLGVNQRGELCVRGPMIMSGYVNNPEATNALIdKDGWLHSGDIAYWDEDEHFFIVDRLKSLIK 444
Cdd:PRK06178 391 LPVPGTEFKICDFETGELLPLGAEGEIVVRTPSLLKGYWNKPEATAEAL-RDGWLHTGDIGKIDEQGFLHYLGRRKEMLK 469
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1216630836 445 YKGYQVAPAELESILLQHPNIFDAGVAGLPDDDAGELPAAVVVLEHGKTMTEKEIVDYVASQVTTAK--KLRggvvFVDE 522
Cdd:PRK06178 470 VNGMSVFPSEVEALLGQHPAVLGSAVVGRPDPDKGQVPVAFVQLKPGADLTAAALQAWCRENMAVYKvpEIR----IVDA 545
|
570
....*....|
gi 1216630836 523 VPKGLTGKLD 532
Cdd:PRK06178 546 LPMTATGKVR 555
|
|
| FACL_like_6 |
cd05922 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
194-537 |
4.07e-54 |
|
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: 189.57 E-value: 4.07e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1216630836 194 ALIMNSSGSTGLPKGVALPHRTAcvrfshardpIFGNQII-------PDTAILSVVPFHHGFGMFTTLGYLICGFRVVLM 266
Cdd:cd05922 120 ALLLYTSGSTGSPKLVRLSHQNL----------LANARSIaeylgitADDRALTVLPLSYDYGLSVLNTHLLRGATLVLT 189
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1216630836 267 YRFE-EELFLRSLQDYKIQSALLVPTLFSFFAKSTlIDKYDLSNLHEIASGGAPLSKEVGEAVAKRFHLPGIRQGYGLTE 345
Cdd:cd05922 190 NDGVlDDAFWEDLREHGATGLAGVPSTYAMLTRLG-FDPAKLPSLRYLTQAGGRLPQETIARLRELLPGAQVYVMYGQTE 268
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1216630836 346 TTSAILITP--EGDDKPGAVGKVVPFFEAKVVDLDtGKTLGVNQRGELCVRGPMIMSGYVNNPEATNALIDKDGWLHSGD 423
Cdd:cd05922 269 ATRRMTYLPpeRILEKPGSIGLAIPGGEFEILDDD-GTPTPPGEPGEIVHRGPNVMKGYWNDPPYRRKEGRGGGVLHTGD 347
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1216630836 424 IAYWDEDEHFFIVDRLKSLIKYKGYQVAPAELESILLQHPNIFDAGVAGLPdDDAGELPAAVVVLEHGktMTEKEIVDYV 503
Cdd:cd05922 348 LARRDEDGFLFIVGRRDRMIKLFGNRISPTEIEAAARSIGLIIEAAAVGLP-DPLGEKLALFVTAPDK--IDPKDVLRSL 424
|
330 340 350
....*....|....*....|....*....|....
gi 1216630836 504 ASQVTTAkKLRGGVVFVDEVPKGLTGKLDARKIR 537
Cdd:cd05922 425 AERLPPY-KVPATVRVVDELPLTASGKVDYAALR 457
|
|
| FadD3 |
cd17638 |
acyl-CoA synthetase FadD3 and similar proteins; This family contains long chain fatty acid CoA ... |
193-531 |
2.26e-53 |
|
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: 184.24 E-value: 2.26e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1216630836 193 IALIMNSSGSTGLPKGVALPHRTACVRFSHARDPIfgnQIIPDTAILSVVPFHHGFGMftTLGYLIC---GFRVVLMYRF 269
Cdd:cd17638 2 VSDIMFTSGTTGRSKGVMCAHRQTLRAAAAWADCA---DLTEDDRYLIINPFFHTFGY--KAGIVAClltGATVVPVAVF 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1216630836 270 EEELFLRSLQDYKIQSALLVPTLFSFFAKSTLIDKYDLSNLHEIASGGAPLSKEVGEAVAKRFHLPGIRQGYGLTETTSA 349
Cdd:cd17638 77 DVDAILEAIERERITVLPGPPTLFQSLLDHPGRKKFDLSSLRAAVTGAATVPVELVRRMRSELGFETVLTAYGLTEAGVA 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1216630836 350 ILITPEGD--DKPGAVGKVVPFFEAKVVDldtgktlgvnqRGELCVRGPMIMSGYVNNPEATNALIDKDGWLHSGDIAYW 427
Cdd:cd17638 157 TMCRPGDDaeTVATTCGRACPGFEVRIAD-----------DGEVLVRGYNVMQGYLDDPEATAEAIDADGWLHTGDVGEL 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1216630836 428 DEDEHFFIVDRLKSLIKYKGYQVAPAELESILLQHPNIFDAGVAGLPDDDAGELPAAVVVLEHGKTMTEKEIVDYVASQV 507
Cdd:cd17638 226 DERGYLRITDRLKDMYIVGGFNVYPAEVEGALAEHPGVAQVAVIGVPDERMGEVGKAFVVARPGVTLTEEDVIAWCRERL 305
|
330 340
....*....|....*....|....
gi 1216630836 508 TTAKKLRgGVVFVDEVPKGLTGKL 531
Cdd:cd17638 306 ANYKVPR-FVRFLDELPRNASGKV 328
|
|
| PRK08751 |
PRK08751 |
long-chain fatty acid--CoA ligase; |
22-538 |
5.76e-53 |
|
long-chain fatty acid--CoA ligase;
Pssm-ID: 181546 [Multi-domain] Cd Length: 560 Bit Score: 188.93 E-value: 5.76e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1216630836 22 TAGEQLHKAMKRYALVPGTIAFTDAhievdITYAEYFEMSVRLAE-AMKRYGLNTNHRIVVCSENSLQFFMPVLGALFIG 100
Cdd:PRK08751 26 TVAEVFATSVAKFADRPAYHSFGKT-----ITYREADQLVEQFAAyLLGELQLKKGDRVALMMPNCLQYPIATFGVLRAG 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1216630836 101 VAVAPANDIYNERELLNSMGISQPTVVFVSKKGLQKILNVQKKLPIIQkiIIMDSKTDYQGF--QSMYTFVTSHLPPGFN 178
Cdd:PRK08751 101 LTVVNVNPLYTPRELKHQLIDSGASVLVVIDNFGTTVQQVIADTPVKQ--VITTGLGDMLGFpkAALVNFVVKYVKKLVP 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1216630836 179 EYDF-----------------VPESFDRDKTIALIMNSSGSTGLPKGVALPHRTACVRFSHARDPIFGNQIIPD--TAIL 239
Cdd:PRK08751 179 EYRIngairfrealalgrkhsMPTLQIEPDDIAFLQYTGGTTGVAKGAMLTHRNLVANMQQAHQWLAGTGKLEEgcEVVI 258
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1216630836 240 SVVPFHHGFGM------FTTLG---YLICGFRvvlmyrfEEELFLRSLQDYKIQSALLVPTLFSFFAKSTLIDKYDLSNL 310
Cdd:PRK08751 259 TALPLYHIFALtanglvFMKIGgcnHLISNPR-------DMPGFVKELKKTRFTAFTGVNTLFNGLLNTPGFDQIDFSSL 331
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1216630836 311 HEIASGGAPLSKEVGEAVAKRFHLPGIrQGYGLTETTSAILITP-EGDDKPGAVGKVVPFFEAKVVDlDTGKTLGVNQRG 389
Cdd:PRK08751 332 KMTLGGGMAVQRSVAERWKQVTGLTLV-EAYGLTETSPAACINPlTLKEYNGSIGLPIPSTDACIKD-DAGTVLAIGEIG 409
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1216630836 390 ELCVRGPMIMSGYVNNPEATNALIDKDGWLHSGDIAYWDEDEHFFIVDRLKSLIKYKGYQVAPAELESILLQHPNIFDAG 469
Cdd:PRK08751 410 ELCIKGPQVMKGYWKRPEETAKVMDADGWLHTGDIARMDEQGFVYIVDRKKDMILVSGFNVYPNEIEDVIAMMPGVLEVA 489
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1216630836 470 VAGLPDDDAGELpAAVVVLEHGKTMTEKEIVDYVASQVTTAKKLRgGVVFVDEVPKGLTGKLDARKIRE 538
Cdd:PRK08751 490 AVGVPDEKSGEI-VKVVIVKKDPALTAEDVKAHARANLTGYKQPR-IIEFRKELPKTNVGKILRRELRD 556
|
|
| PRK07529 |
PRK07529 |
AMP-binding domain protein; Validated |
201-543 |
9.64e-52 |
|
AMP-binding domain protein; Validated
Pssm-ID: 236043 [Multi-domain] Cd Length: 632 Bit Score: 187.08 E-value: 9.64e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1216630836 201 GSTGLPKGVALPHrtacvrfshardpifGNQII------------PDTAILSVVPFHHGFGMFTT-LGYLICGFRVVLM- 266
Cdd:PRK07529 223 GTTGMPKLAQHTH---------------GNEVAnawlgalllglgPGDTVFCGLPLFHVNALLVTgLAPLARGAHVVLAt 287
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1216630836 267 ---YRFEEEL--FLRSLQDYKIQSALLVPTLFSFFAKsTLIDKYDLSNLHEIASGGAPLSKEVGEAVAKRFHLPgIRQGY 341
Cdd:PRK07529 288 pqgYRGPGVIanFWKIVERYRINFLSGVPTVYAALLQ-VPVDGHDISSLRYALCGAAPLPVEVFRRFEAATGVR-IVEGY 365
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1216630836 342 GLTETTSAILITP-EGDDKPGAVGKVVPFFEAKVVDLD-TGKTL---GVNQRGELCVRGPMIMSGYVNnPEATNALIDKD 416
Cdd:PRK07529 366 GLTEATCVSSVNPpDGERRIGSVGLRLPYQRVRVVILDdAGRYLrdcAVDEVGVLCIAGPNVFSGYLE-AAHNKGLWLED 444
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1216630836 417 GWLHSGDIAYWDEDEHFFIVDRLKSLIKYKGYQVAPAELESILLQHPNIFDAGVAGLPDDDAGELPAAVVVLEHGKTMTE 496
Cdd:PRK07529 445 GWLNTGDLGRIDADGYFWLTGRAKDLIIRGGHNIDPAAIEEALLRHPAVALAAAVGRPDAHAGELPVAYVQLKPGASATE 524
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|..
gi 1216630836 497 KEIVDYVASQVTTAKKLRGGVVFVDEVPKGLTGK-----LDARKIREILIKA 543
Cdd:PRK07529 525 AELLAFARDHIAERAAVPKHVRILDALPKTAVGKifkpaLRRDAIRRVLRAA 576
|
|
| AAS_C |
cd05909 |
C-terminal domain of the acyl-acyl carrier protein synthetase (also called ... |
78-537 |
3.79e-51 |
|
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: 182.53 E-value: 3.79e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1216630836 78 RIVVCSENSLQFFMPVLGALFIGVAVAPANDIYNERELLNSMGISQPTVVFVSKKGLQKIlnVQKKLPIIQ---KIIIM- 153
Cdd:cd05909 33 NVGVMLPPSAGGALANFALALSGKVPVMLNYTAGLRELRACIKLAGIKTVLTSKQFIEKL--KLHHLFDVEydaRIVYLe 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1216630836 154 DSKTDYQGFQSMYTFVTSHLPPGFNEYDFVPESFDRDKTiALIMNSSGSTGLPKGVALPHR---------TACVRFShar 224
Cdd:cd05909 111 DLRAKISKADKCKAFLAGKFPPKWLLRIFGVAPVQPDDP-AVILFTSGSEGLPKGVVLSHKnllanveqiTAIFDPN--- 186
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1216630836 225 dpifgnqiiPDTAILSVVPFHHGFGMFTTLGY-LICGFRVVLMYR-FEEELFLRSLQDYKIQSALLVPTLFSFFAKStlI 302
Cdd:cd05909 187 ---------PEDVVFGALPFFHSFGLTGCLWLpLLSGIKVVFHPNpLDYKKIPELIYDKKATILLGTPTFLRGYARA--A 255
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1216630836 303 DKYDLSNLHEIASGGAPLSKEVGEAVAKRFHLPgIRQGYGLTETTSAILI-TPEGDDKPGAVGKVVPFFEAKVVDLDTGK 381
Cdd:cd05909 256 HPEDFSSLRLVVAGAEKLKDTLRQEFQEKFGIR-ILEGYGTTECSPVISVnTPQSPNKEGTVGRPLPGMEVKIVSVETHE 334
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1216630836 382 TLGVNQRGELCVRGPMIMSGYVNNPEATNALIdKDGWLHSGDIAYWDEDEHFFIVDRLKSLIKYKGYQVAPAELESILLQ 461
Cdd:cd05909 335 EVPIGEGGLLLVRGPNVMLGYLNEPELTSFAF-GDGWYDTGDIGKIDGEGFLTITGRLSRFAKIAGEMVSLEAIEDILSE 413
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1216630836 462 H-PNIFDAGVAGLPDDDAGElpaAVVVLEHGKTMTEKEIVDYV-ASQVTTAKKLRgGVVFVDEVPKGLTGKLDARKIR 537
Cdd:cd05909 414 IlPEDNEVAVVSVPDGRKGE---KIVLLTTTTDTDPSSLNDILkNAGISNLAKPS-YIHQVEEIPLLGTGKPDYVTLK 487
|
|
| PRK08974 |
PRK08974 |
long-chain-fatty-acid--CoA ligase FadD; |
72-545 |
3.95e-51 |
|
long-chain-fatty-acid--CoA ligase FadD;
Pssm-ID: 236359 [Multi-domain] Cd Length: 560 Bit Score: 184.10 E-value: 3.95e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1216630836 72 GLNTNHRIVVCSENSLQFFMPVLGALFIGVAVAPANDIYNEREL---LNSMGISqpTVVFVSK--KGLQKILNvqkKLPI 146
Cdd:PRK08974 70 GLKKGDRVALMMPNLLQYPIALFGILRAGMIVVNVNPLYTPRELehqLNDSGAK--AIVIVSNfaHTLEKVVF---KTPV 144
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1216630836 147 iqKIIIMDSKTDYQGF--QSMYTFVTS---------HLPPG--FNE-------YDFVPESFDRDkTIALIMNSSGSTGLP 206
Cdd:PRK08974 145 --KHVILTRMGDQLSTakGTLVNFVVKyikrlvpkyHLPDAisFRSalhkgrrMQYVKPELVPE-DLAFLQYTGGTTGVA 221
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1216630836 207 KGVALPHRTACVRFSHArDPIFGNQIIPDTA-ILSVVPFHHGFGM------FTTLG---YLICGFRVVlmyrfeeELFLR 276
Cdd:PRK08974 222 KGAMLTHRNMLANLEQA-KAAYGPLLHPGKElVVTALPLYHIFALtvncllFIELGgqnLLITNPRDI-------PGFVK 293
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1216630836 277 SLQDYKIQSALLVPTLFSFFAKSTLIDKYDLSNLHEIASGGAPlskeVGEAVAKRFH-LPGIR--QGYGLTETTSAILIT 353
Cdd:PRK08974 294 ELKKYPFTAITGVNTLFNALLNNEEFQELDFSSLKLSVGGGMA----VQQAVAERWVkLTGQYllEGYGLTECSPLVSVN 369
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1216630836 354 PEG-DDKPGAVGKVVPFFEAKVVDlDTGKTLGVNQRGELCVRGPMIMSGYVNNPEATNALIdKDGWLHSGDIAYWDEDEH 432
Cdd:PRK08974 370 PYDlDYYSGSIGLPVPSTEIKLVD-DDGNEVPPGEPGELWVKGPQVMLGYWQRPEATDEVI-KDGWLATGDIAVMDEEGF 447
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1216630836 433 FFIVDRLKSLIKYKGYQVAPAELESILLQHPNIFDAGVAGLPDDDAGELpAAVVVLEHGKTMTEKEIVDYVASQVTTAK- 511
Cdd:PRK08974 448 LRIVDRKKDMILVSGFNVYPNEIEDVVMLHPKVLEVAAVGVPSEVSGEA-VKIFVVKKDPSLTEEELITHCRRHLTGYKv 526
|
490 500 510
....*....|....*....|....*....|....*.
gi 1216630836 512 -KLrggVVFVDEVPKGLTGKLDARKIR-EILIKAKK 545
Cdd:PRK08974 527 pKL---VEFRDELPKSNVGKILRRELRdEARAKVDN 559
|
|
| PRK07786 |
PRK07786 |
long-chain-fatty-acid--CoA ligase; Validated |
33-538 |
5.18e-51 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 169098 [Multi-domain] Cd Length: 542 Bit Score: 183.44 E-value: 5.18e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1216630836 33 RYALV-PGTIAFTdaHIEVDITYAEYFEMSVRLAEAMKRYGLNTNHRIVVCSENSLQFFMPVLGALFIGVAVAPANDIYN 111
Cdd:PRK07786 25 RHALMqPDAPALR--FLGNTTTWRELDDRVAALAGALSRRGVGFGDRVLILMLNRTEFVESVLAANMLGAIAVPVNFRLT 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1216630836 112 ERELLNSMGISQPTVVFVSKKGLQKILNVQKKLPIIQKIIIMDSKTDYQGFQsmYTFVTSHLPPGFNEYDfVPESfdrdk 191
Cdd:PRK07786 103 PPEIAFLVSDCGAHVVVTEAALAPVATAVRDIVPLLSTVVVAGGSSDDSVLG--YEDLLAEAGPAHAPVD-IPND----- 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1216630836 192 TIALIMNSSGSTGLPKGVALPHRTACvrfSHARDPIFGNQI-IPDTAILSVVPFHHGFGMFTTLGYLICGFRVVL--MYR 268
Cdd:PRK07786 175 SPALIMYTSGTTGRPKGAVLTHANLT---GQAMTCLRTNGAdINSDVGFVGVPLFHIAGIGSMLPGLLLGAPTVIypLGA 251
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1216630836 269 FEEELFLRSLQDYKIQSALLVPTLFSFFAKSTLIDKYDLSnLHEIASGGAPLSKEVGEAVAKRFHLPGIRQGYGLTETtS 348
Cdd:PRK07786 252 FDPGQLLDVLEAEKVTGIFLVPAQWQAVCAEQQARPRDLA-LRVLSWGAAPASDTLLRQMAATFPEAQILAAFGQTEM-S 329
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1216630836 349 AILITPEGDD---KPGAVGKVVPFFEAKVVDlDTGKTLGVNQRGELCVRGPMIMSGYVNNPEATNALIDkDGWLHSGDIA 425
Cdd:PRK07786 330 PVTCMLLGEDairKLGSVGKVIPTVAARVVD-ENMNDVPVGEVGEIVYRAPTLMSGYWNNPEATAEAFA-GGWFHSGDLV 407
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1216630836 426 YWDEDEHFFIVDRLKSLIKYKGYQVAPAELESILLQHPNIFDAGVAGLPDDDAGELPAAVVVLEHG-KTMTEKEIVDYVA 504
Cdd:PRK07786 408 RQDEEGYVWVVDRKKDMIISGGENIYCAEVENVLASHPDIVEVAVIGRADEKWGEVPVAVAAVRNDdAALTLEDLAEFLT 487
|
490 500 510
....*....|....*....|....*....|....
gi 1216630836 505 SQVTTAKKLRgGVVFVDEVPKGLTGKLDARKIRE 538
Cdd:PRK07786 488 DRLARYKHPK-ALEIVDALPRNPAGKVLKTELRE 520
|
|
| ttLC_FACS_AEE21_like |
cd12118 |
Fatty acyl-CoA synthetases similar to LC-FACS from Thermus thermophiles and Arabidopsis; This ... |
47-538 |
7.93e-51 |
|
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: 181.34 E-value: 7.93e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1216630836 47 HIEVDITYAEYFEMSVRLAEAMKRYGLNTNHRIVVCSENSlqffmPVLGALFIGVAVAPAndiynereLLNSmgisqptv 126
Cdd:cd12118 25 YGDRRYTWRQTYDRCRRLASALAALGISRGDTVAVLAPNT-----PAMYELHFGVPMAGA--------VLNA-------- 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1216630836 127 vfvskkglqkiLNVQKKLPIIQ--------KIIIMDSKTDYQGFQSMytfvtshlppGFNEYDFVPESfDRDKTIALimN 198
Cdd:cd12118 84 -----------LNTRLDAEEIAfilrhseaKVLFVDREFEYEDLLAE----------GDPDFEWIPPA-DEWDPIAL--N 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1216630836 199 -SSGSTGLPKGVALPHRTAcvrFSHARDPIFGNQIIPDTAILSVVP-FH-----HGFGMFTTLGYLICgfrvvlMYRFEE 271
Cdd:cd12118 140 yTSGTTGRPKGVVYHHRGA---YLNALANILEWEMKQHPVYLWTLPmFHcngwcFPWTVAAVGGTNVC------LRKVDA 210
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1216630836 272 ELFLRSLQDYKIQSALLVPTLFSFFAKSTLIDKYDLSNLHEIASGGAPLSKEVGEAV-AKRFHlpgIRQGYGLTETTSAI 350
Cdd:cd12118 211 KAIYDLIEKHKVTHFCGAPTVLNMLANAPPSDARPLPHRVHVMTAGAPPPAAVLAKMeELGFD---VTHVYGLTETYGPA 287
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1216630836 351 LI---TPEGDDKPGA----------VGkVVPFFEAKVVDLDT-------GKTLGvnqrgELCVRGPMIMSGYVNNPEATN 410
Cdd:cd12118 288 TVcawKPEWDELPTEerarlkarqgVR-YVGLEEVDVLDPETmkpvprdGKTIG-----EIVFRGNIVMKGYLKNPEATA 361
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1216630836 411 ALIdKDGWLHSGDIAYWDEDEHFFIVDRLKSLIKYKGYQVAPAELESILLQHPNIFDAGVAGLPDDDAGELPAAVVVLEH 490
Cdd:cd12118 362 EAF-RGGWFHSGDLAVIHPDGYIEIKDRSKDIIISGGENISSVEVEGVLYKHPAVLEAAVVARPDEKWGEVPCAFVELKE 440
|
490 500 510 520
....*....|....*....|....*....|....*....|....*...
gi 1216630836 491 GKTMTEKEIVDYVASQVTTAKKLRgGVVFvDEVPKGLTGKLDARKIRE 538
Cdd:cd12118 441 GAKVTEEEIIAFCREHLAGFMVPK-TVVF-GELPKTSTGKIQKFVLRD 486
|
|
| PRK07059 |
PRK07059 |
Long-chain-fatty-acid--CoA ligase; Validated |
12-537 |
8.53e-51 |
|
Long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 235923 [Multi-domain] Cd Length: 557 Bit Score: 182.91 E-value: 8.53e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1216630836 12 PAPFYPLEDGTAGEQLHKAMKRYALVPgtiAFTDahIEVDITYAEYFEMSVRLAEAMKRYGLNTNHRIVVCSENSLQFFM 91
Cdd:PRK07059 14 PAEIDASQYPSLADLLEESFRQYADRP---AFIC--MGKAITYGELDELSRALAAWLQSRGLAKGARVAIMMPNVLQYPV 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1216630836 92 PVLGALFIGVAVAPANDIYNERELLNSMGISQPTVVFVSKK---GLQKILNvqkKLPIiqKIIIMDSKTDYQGFQS-MYT 167
Cdd:PRK07059 89 AIAAVLRAGYVVVNVNPLYTPRELEHQLKDSGAEAIVVLENfatTVQQVLA---KTAV--KHVVVASMGDLLGFKGhIVN 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1216630836 168 FVTSHLP--------PGFNEYD----------FVPESFDRDKtIALIMNSSGSTGLPKGVALPHRT--ACVRFSHA-RDP 226
Cdd:PRK07059 164 FVVRRVKkmvpawslPGHVRFNdalaegarqtFKPVKLGPDD-VAFLQYTGGTTGVSKGATLLHRNivANVLQMEAwLQP 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1216630836 227 IFGNQIIPDT-AILSVVPFHHGFGMftTLGYLI---CGFRVVLMYRFEE-ELFLRSLQDYKIQSALLVPTLFSFFAKSTL 301
Cdd:PRK07059 243 AFEKKPRPDQlNFVCALPLYHIFAL--TVCGLLgmrTGGRNILIPNPRDiPGFIKELKKYQVHIFPAVNTLYNALLNNPD 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1216630836 302 IDKYDLSNLhEIASGGAplsKEVGEAVAKR-FHLPG--IRQGYGLTETTSAILITP-EGDDKPGAVGKVVPFFEAKVVDl 377
Cdd:PRK07059 321 FDKLDFSKL-IVANGGG---MAVQRPVAERwLEMTGcpITEGYGLSETSPVATCNPvDATEFSGTIGLPLPSTEVSIRD- 395
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1216630836 378 DTGKTLGVNQRGELCVRGPMIMSGYVNNPEATNALIDKDGWLHSGDIAYWDEDEHFFIVDRLKSLIKYKGYQVAPAELES 457
Cdd:PRK07059 396 DDGNDLPLGEPGEICIRGPQVMAGYWNRPDETAKVMTADGFFRTGDVGVMDERGYTKIVDRKKDMILVSGFNVYPNEIEE 475
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1216630836 458 ILLQHPNIFDAGVAGLPDDDAGELPAAVVVlEHGKTMTEKEIVDYVASQVTTAKKLRgGVVFVDEVPKGLTGKLDARKIR 537
Cdd:PRK07059 476 VVASHPGVLEVAAVGVPDEHSGEAVKLFVV-KKDPALTEEDVKAFCKERLTNYKRPK-FVEFRTELPKTNVGKILRRELR 553
|
|
| PRK12492 |
PRK12492 |
long-chain-fatty-acid--CoA ligase; Provisional |
25-539 |
1.43e-50 |
|
long-chain-fatty-acid--CoA ligase; Provisional
Pssm-ID: 171539 [Multi-domain] Cd Length: 562 Bit Score: 182.33 E-value: 1.43e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1216630836 25 EQLHKAMKRYALVPgtiAFTDahIEVDITYAEYFEMSVRLAEAMKRY-GLNTNHRIVVCSENSLQFFMPVLGALFIGVAV 103
Cdd:PRK12492 28 EVFERSCKKFADRP---AFSN--LGVTLSYAELERHSAAFAAYLQQHtDLVPGDRIAVQMPNVLQYPIAVFGALRAGLIV 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1216630836 104 APANDIYNERELLNSMGISQP-TVVFVSKKGLQkilnVQKKLP--IIQKII---IMDSKTDYQGFQsMYTFVTS------ 171
Cdd:PRK12492 103 VNTNPLYTAREMRHQFKDSGArALVYLNMFGKL----VQEVLPdtGIEYLIeakMGDLLPAAKGWL-VNTVVDKvkkmvp 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1216630836 172 --HLPP--GFNE---------YDFVPESFDrdkTIALIMNSSGSTGLPKGVALPHRT---------ACVRfSHARDpifG 229
Cdd:PRK12492 178 ayHLPQavPFKQalrqgrglsLKPVPVGLD---DIAVLQYTGGTTGLAKGAMLTHGNlvanmlqvrACLS-QLGPD---G 250
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1216630836 230 NQIIPD--TAILSVVPFHHGFGmFTT--LGYLICGFRVVLMYRFEE-ELFLRSLQDYKIQSALLVPTLFSFFAKSTLIDK 304
Cdd:PRK12492 251 QPLMKEgqEVMIAPLPLYHIYA-FTAncMCMMVSGNHNVLITNPRDiPGFIKELGKWRFSALLGLNTLFVALMDHPGFKD 329
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1216630836 305 YDLSNLHEIASGGAPLSKevgeAVAKRF-HLPGIR--QGYGLTETTSAILITPEGD-DKPGAVGKVVPFFEAKVVDlDTG 380
Cdd:PRK12492 330 LDFSALKLTNSGGTALVK----ATAERWeQLTGCTivEGYGLTETSPVASTNPYGElARLGTVGIPVPGTALKVID-DDG 404
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1216630836 381 KTLGVNQRGELCVRGPMIMSGYVNNPEATNALIDKDGWLHSGDIAYWDEDEHFFIVDRLKSLIKYKGYQVAPAELESILL 460
Cdd:PRK12492 405 NELPLGERGELCIKGPQVMKGYWQQPEATAEALDAEGWFKTGDIAVIDPDGFVRIVDRKKDLIIVSGFNVYPNEIEDVVM 484
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1216630836 461 QHPNIFDAGVAGLPDDDAGELPAAVVVLEHGkTMTEKEIVDYVASQVtTAKKLRGGVVFVDEVPKGLTGKLDARKIREI 539
Cdd:PRK12492 485 AHPKVANCAAIGVPDERSGEAVKLFVVARDP-GLSVEELKAYCKENF-TGYKVPKHIVLRDSLPMTPVGKILRRELRDI 561
|
|
| PRK13391 |
PRK13391 |
acyl-CoA synthetase; Provisional |
52-538 |
1.47e-50 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 184022 [Multi-domain] Cd Length: 511 Bit Score: 181.43 E-value: 1.47e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1216630836 52 ITYAEYFEMSVRLAEAMKRYGLNTNHRIVVCSENSLQFFMPVLGALFIGVAVAPANDIYNERELLNSMGISQPTVVFVSK 131
Cdd:PRK13391 25 VTYRELDERSNRLAHLFRSLGLKRGDHVAIFMENNLRYLEVCWAAERSGLYYTCVNSHLTPAEAAYIVDDSGARALITSA 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1216630836 132 KGLQKILNVQKKLPIIQKIIIMDSKTDYQGFQSmYTFVTSHLPPGfneydfvpeSFDRDKTIALIMNSSGSTGLPKGV-- 209
Cdd:PRK13391 105 AKLDVARALLKQCPGVRHRLVLDGDGELEGFVG-YAEAVAGLPAT---------PIADESLGTDMLYSSGTTGRPKGIkr 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1216630836 210 ALPHR--TACVRFSHARDPIFGnqIIPDTAILSVVPFHHGFGMFTTLGYLICGFRVVLMYRFEEELFLRSLQDYKIQSAL 287
Cdd:PRK13391 175 PLPEQppDTPLPLTAFLQRLWG--FRSDMVYLSPAPLYHSAPQRAVMLVIRLGGTVIVMEHFDAEQYLALIEEYGVTHTQ 252
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1216630836 288 LVPTLFSFFAK--STLIDKYDLSNLHEIASGGAPLSKEVGEAVAKRFHlPGIRQGYGLTETTSAILI-TPEGDDKPGAVG 364
Cdd:PRK13391 253 LVPTMFSRMLKlpEEVRDKYDLSSLEVAIHAAAPCPPQVKEQMIDWWG-PIIHEYYAATEGLGFTACdSEEWLAHPGTVG 331
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1216630836 365 KVVpFFEAKVVDlDTGKTLGVNQRGELCVRGPMIMSgYVNNPEATNALIDKDG-WLHSGDIAYWDEDEHFFIVDRLKSLI 443
Cdd:PRK13391 332 RAM-FGDLHILD-DDGAELPPGEPGTIWFEGGRPFE-YLNDPAKTAEARHPDGtWSTVGDIGYVDEDGYLYLTDRAAFMI 408
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1216630836 444 KYKGYQVAPAELESILLQHPNIFDAGVAGLPDDDAGELPAAVVVLEHGKTMTE---KEIVDYVASQVTTAKKLRgGVVFV 520
Cdd:PRK13391 409 ISGGVNIYPQEAENLLITHPKVADAAVFGVPNEDLGEEVKAVVQPVDGVDPGPalaAELIAFCRQRLSRQKCPR-SIDFE 487
|
490
....*....|....*...
gi 1216630836 521 DEVPKGLTGKLDARKIRE 538
Cdd:PRK13391 488 DELPRLPTGKLYKRLLRD 505
|
|
| CHC_CoA_lg |
cd05903 |
Cyclohexanecarboxylate-CoA ligase (also called cyclohex-1-ene-1-carboxylate:CoA ligase); ... |
53-538 |
2.76e-50 |
|
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: 178.73 E-value: 2.76e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1216630836 53 TYAEYFEMSVRLAEAMKRYGLNTNHRIVVCSENSLQFFMPVLGALFIGVAVAPANDIYNERELlnsmgisqptvVFVSKK 132
Cdd:cd05903 3 TYSELDTRADRLAAGLAALGVGPGDVVAFQLPNWWEFAVLYLACLRIGAVTNPILPFFREHEL-----------AFILRR 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1216630836 133 GLQKILnvqkklpiiqkiIIMDSktdyqgfqsmytfvtshlppgFNEYDFVPESFDrdktIALIMNSSGSTGLPKGVALP 212
Cdd:cd05903 72 AKAKVF------------VVPER---------------------FRQFDPAAMPDA----VALLLFTSGTTGEPKGVMHS 114
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1216630836 213 HRTAcvrFSHARDPIFGNQIIPDTAILSVVPFHH--GFGMFTTLGYLIcGFRVVLMYRFEEELFLRSLQDYKIQSALLVP 290
Cdd:cd05903 115 HNTL---SASIRQYAERLGLGPGDVFLVASPMAHqtGFVYGFTLPLLL-GAPVVLQDIWDPDKALALMREHGVTFMMGAT 190
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1216630836 291 TLFSFFAKSTLIDKYDLSNLHEIASGGAPLSKEVGEAVAKRFHLPGIRqGYGLTETTSAILITPEGDDKPGAV--GKVVP 368
Cdd:cd05903 191 PFLTDLLNAVEEAGEPLSRLRTFVCGGATVPRSLARRAAELLGAKVCS-AYGSTECPGAVTSITPAPEDRRLYtdGRPLP 269
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1216630836 369 FFEAKVVDlDTGKTLGVNQRGELCVRGPMIMSGYVNNPEaTNALIDKDGWLHSGDIAYWDEDEHFFIVDRLKSLIKYKGY 448
Cdd:cd05903 270 GVEIKVVD-DTGATLAPGVEGELLSRGPSVFLGYLDRPD-LTADAAPEGWFRTGDLARLDEDGYLRITGRSKDIIIRGGE 347
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1216630836 449 QVAPAELESILLQHPNIFDAGVAGLPDDDAGELPAAVVVLEHGKTMTEKEIVDYVASQVTTAKKLRGGVVFVDEVPKGLT 528
Cdd:cd05903 348 NIPVLEVEDLLLGHPGVIEAAVVALPDERLGERACAVVVTKSGALLTFDELVAYLDRQGVAKQYWPERLVHVDDLPRTPS 427
|
490
....*....|
gi 1216630836 529 GKLDARKIRE 538
Cdd:cd05903 428 GKVQKFRLRE 437
|
|
| ACLS-CaiC |
cd17637 |
acyl-CoA synthetase (AMP-forming)/AMP-acid ligase II; This family contains fatty acid CoA ... |
196-532 |
7.03e-50 |
|
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: 174.77 E-value: 7.03e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1216630836 196 IMNSSGSTGLPKGVALPHR---TACVRFSHARdpifgnQIIPDTAILSVVPFHHGFGMFTTLGYLICGFRVVLMYRFEEE 272
Cdd:cd17637 5 IIHTAAVAGRPRGAVLSHGnliAANLQLIHAM------GLTEADVYLNMLPLFHIAGLNLALATFHAGGANVVMEKFDPA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1216630836 273 LFLRSLQDYKIqsallvpTLFSFFAK--STLIDK-----YDLSNLHEIASGGAPlskevgeAVAKRFH-LPGIR--QGYG 342
Cdd:cd17637 79 EALELIEEEKV-------TLMGSFPPilSNLLDAaeksgVDLSSLRHVLGLDAP-------ETIQRFEeTTGATfwSLYG 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1216630836 343 LTETTSAILITPEgDDKPGAVGKVVPFFEAKVVDlDTGKTLGVNQRGELCVRGPMIMSGYVNNPEATNALIdKDGWLHSG 422
Cdd:cd17637 145 QTETSGLVTLSPY-RERPGSAGRPGPLVRVRIVD-DNDRPVPAGETGEIVVRGPLVFQGYWNLPELTAYTF-RNGWHHTG 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1216630836 423 DIAYWDEDEHFFIVDRL--KSLIKYKGYQVAPAELESILLQHPNIFDAGVAGLPDDDAGELPAAVVVLEHGKTMTEKEIV 500
Cdd:cd17637 222 DLGRFDEDGYLWYAGRKpeKELIKPGGENVYPAEVEKVILEHPAIAEVCVIGVPDPKWGEGIKAVCVLKPGATLTADELI 301
|
330 340 350
....*....|....*....|....*....|..
gi 1216630836 501 DYVASQVTTAKKLRgGVVFVDEVPKGLTGKLD 532
Cdd:cd17637 302 EFVGSRIARYKKPR-YVVFVEALPKTADGSID 332
|
|
| PRK07787 |
PRK07787 |
acyl-CoA synthetase; Validated |
49-537 |
1.00e-49 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236096 [Multi-domain] Cd Length: 471 Bit Score: 178.26 E-value: 1.00e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1216630836 49 EVDITYAEYFEMSVRLAEamkryGLNTNHRIVVCSENSLQFFMPVLGALFIGVAVAPANDIYNERELLNSMGISQPTVVF 128
Cdd:PRK07787 23 GRVLSRSDLAGAATAVAE-----RVAGARRVAVLATPTLATVLAVVGALIAGVPVVPVPPDSGVAERRHILADSGAQAWL 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1216630836 129 VSKKGlqkilnVQKKLPIIQKIIIMDSktdyqgfqsmytfvtSHLPPgfnEYDfvPESfdrdktIALIMNSSGSTGLPKG 208
Cdd:PRK07787 98 GPAPD------DPAGLPHVPVRLHARS---------------WHRYP---EPD--PDA------PALIVYTSGTTGPPKG 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1216630836 209 VALPHR--TACVR-FSHARdpifgnQIIPDTAILSVVP-FH-HGFgMFTTLGYLICGFRVVLMYRFEEELFLRSLQDyki 283
Cdd:PRK07787 146 VVLSRRaiAADLDaLAEAW------QWTADDVLVHGLPlFHvHGL-VLGVLGPLRIGNRFVHTGRPTPEAYAQALSE--- 215
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1216630836 284 QSALL--VPTLFSFFAKSTLIDKYdLSNLHEIASGGAPLSKEVGEAVAkrfHLPGIR--QGYGLTETtsaiLIT----PE 355
Cdd:PRK07787 216 GGTLYfgVPTVWSRIAADPEAARA-LRGARLLVSGSAALPVPVFDRLA---ALTGHRpvERYGMTET----LITlstrAD 287
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1216630836 356 GDDKPGAVGKVVPFFEAKVVDlDTGKTLGVNQR--GELCVRGPMIMSGYVNNPEATNALIDKDGWLHSGDIAYWDEDEHF 433
Cdd:PRK07787 288 GERRPGWVGLPLAGVETRLVD-EDGGPVPHDGEtvGELQVRGPTLFDGYLNRPDATAAAFTADGWFRTGDVAVVDPDGMH 366
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1216630836 434 FIVDRlKS--LIKYKGYQVAPAELESILLQHPNIFDAGVAGLPDDDAGELPAAVVVleHGKTMTEKEIVDYVASQVTTAK 511
Cdd:PRK07787 367 RIVGR-EStdLIKSGGYRIGAGEIETALLGHPGVREAAVVGVPDDDLGQRIVAYVV--GADDVAADELIDFVAQQLSVHK 443
|
490 500
....*....|....*....|....*.
gi 1216630836 512 KLRgGVVFVDEVPKGLTGKLDARKIR 537
Cdd:PRK07787 444 RPR-EVRFVDALPRNAMGKVLKKQLL 468
|
|
| MACS_like_4 |
cd05969 |
Uncharacterized subfamily of Acetyl-CoA synthetase like family (ACS); This family is most ... |
53-544 |
1.44e-49 |
|
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: 176.92 E-value: 1.44e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1216630836 53 TYAEYFEMSVRLAEAMKRYGLNTNHRIVVCSENSLQFFMPVLGALFIGVAVAPANDIYNERELLNSMGISQPTVVFVSkk 132
Cdd:cd05969 2 TFAQLKVLSARFANVLKSLGVGKGDRVFVLSPRSPELYFSMLGIGKIGAVICPLFSAFGPEAIRDRLENSEAKVLITT-- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1216630836 133 glqkilnvqkklpiiqkiiimdsktdyqgfqsmytfvtshlppgfneydfvPESFDRD--KTIALIMNSSGSTGLPKGVA 210
Cdd:cd05969 80 ---------------------------------------------------EELYERTdpEDPTLLHYTSGTTGTPKGVL 108
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1216630836 211 LPHR-------TACVRFSHARDPIFGNQIIP----DTAILSVVPFHHGFGMfttlgylicgfrVVLMYRFEEELFLRSLQ 279
Cdd:cd05969 109 HVHDamifyyfTGKYVLDLHPDDIYWCTADPgwvtGTVYGIWAPWLNGVTN------------VVYEGRFDAESWYGIIE 176
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1216630836 280 DYKIQSALLVPTLFSFFAKS--TLIDKYDLSNLHEIASGGAPLSKEVGEAVAKRFHLPgIRQGYGLTETtSAILIT--PE 355
Cdd:cd05969 177 RVKVTVWYTAPTAIRMLMKEgdELARKYDLSSLRFIHSVGEPLNPEAIRWGMEVFGVP-IHDTWWQTET-GSIMIAnyPC 254
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1216630836 356 GDDKPGAVGKVVPFFEAKVVDLDtGKTLGVNQRGELCVRG--PMIMSGYVNNPEATNALIdKDGWLHSGDIAYWDEDEHF 433
Cdd:cd05969 255 MPIKPGSMGKPLPGVKAAVVDEN-GNELPPGTKGILALKPgwPSMFRGIWNDEERYKNSF-IDGWYLTGDLAYRDEDGYF 332
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1216630836 434 FIVDRLKSLIKYKGYQVAPAELESILLQHPNIFDAGVAGLPDDDAGELPAAVVVLEHGKTMTEK---EIVDYVasqvttA 510
Cdd:cd05969 333 WFVGRADDIIKTSGHRVGPFEVESALMEHPAVAEAGVIGKPDPLRGEIIKAFISLKEGFEPSDElkeEIINFV------R 406
|
490 500 510
....*....|....*....|....*....|....*....
gi 1216630836 511 KKLRGGVV-----FVDEVPKGLTGKLDARkireiLIKAK 544
Cdd:cd05969 407 QKLGAHVApreieFVDNLPKTRSGKIMRR-----VLKAK 440
|
|
| ABCL |
cd05958 |
2-aminobenzoate-CoA ligase (ABCL); ABCL catalyzes the initial step in the 2-aminobenzoate ... |
193-537 |
2.13e-49 |
|
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: 176.51 E-value: 2.13e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1216630836 193 IALIMNSSGSTGLPKGVALPHRT---ACVRFSHArdpIFGNQiiPDTAILSVVPFHHGFGMFTTLGY-LICGFRVVLMYR 268
Cdd:cd05958 99 ICILAFTSGTTGAPKATMHFHRDplaSADRYAVN---VLRLR--EDDRFVGSPPLAFTFGLGGVLLFpFGVGASGVLLEE 173
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1216630836 269 FEEELFLRSLQDYKIQSALLVPTLFSFFAKSTLIDKYDLSNLHEIASGGAPLSKEVGEAVAKRFHLPgIRQGYGLTETTS 348
Cdd:cd05958 174 ATPDLLLSAIARYKPTVLFTAPTAYRAMLAHPDAAGPDLSSLRKCVSAGEALPAALHRAWKEATGIP-IIDGIGSTEMFH 252
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1216630836 349 AILITPEGDDKPGAVGKVVPFFEAKVVDlDTGKTLGVNQRGELCVRGPmimSGYVNNPEATNALIDKDGWLHSGDIAYWD 428
Cdd:cd05958 253 IFISARPGDARPGATGKPVPGYEAKVVD-DEGNPVPDGTIGRLAVRGP---TGCRYLADKRQRTYVQGGWNITGDTYSRD 328
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1216630836 429 EDEHFFIVDRLKSLIKYKGYQVAPAELESILLQHPNIFDAGVAGLPDDDAGELPAAVVVLEHGKTMTE---KEIVDYVAS 505
Cdd:cd05958 329 PDGYFRHQGRSDDMIVSGGYNIAPPEVEDVLLQHPAVAECAVVGHPDESRGVVVKAFVVLRPGVIPGPvlaRELQDHAKA 408
|
330 340 350
....*....|....*....|....*....|..
gi 1216630836 506 QVTTAKKLRgGVVFVDEVPKGLTGKLDARKIR 537
Cdd:cd05958 409 HIAPYKYPR-AIEFVTELPRTATGKLQRFALR 439
|
|
| FACL_like_4 |
cd05944 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
193-537 |
2.84e-49 |
|
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: 174.21 E-value: 2.84e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1216630836 193 IALIMNSSGSTGLPKGValPHRTACVRFSH---ARDPIFGnqiiPDTAILSVVPFHHGFGMFTTLGYLIC-GFRVVLM-- 266
Cdd:cd05944 4 VAAYFHTGGTTGTPKLA--QHTHSNEVYNAwmlALNSLFD----PDDVLLCGLPLFHVNGSVVTLLTPLAsGAHVVLAgp 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1216630836 267 --YR----FEEelFLRSLQDYKIQSALLVPTLFSffAKSTLIDKYDLSNLHEIASGGAPLSKEVGEAVAKRFHLPgIRQG 340
Cdd:cd05944 78 agYRnpglFDN--FWKLVERYRITSLSTVPTVYA--ALLQVPVNADISSLRFAMSGAAPLPVELRARFEDATGLP-VVEG 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1216630836 341 YGLTETTSAILIT-PEGDDKPGAVGKVVPFFEAKVVDLD----TGKTLGVNQRGELCVRGPMIMSGYVNNPEATNALIDk 415
Cdd:cd05944 153 YGLTEATCLVAVNpPDGPKRPGSVGLRLPYARVRIKVLDgvgrLLRDCAPDEVGEICVAGPGVFGGYLYTEGNKNAFVA- 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1216630836 416 DGWLHSGDIAYWDEDEHFFIVDRLKSLIKYKGYQVAPAELESILLQHPNIFDAGVAGLPDDDAGELPAAVVVLEHGKTMT 495
Cdd:cd05944 232 DGWLNTGDLGRLDADGYLFITGRAKDLIIRGGHNIDPALIEEALLRHPAVAFAGAVGQPDAHAGELPVAYVQLKPGAVVE 311
|
330 340 350 360
....*....|....*....|....*....|....*....|..
gi 1216630836 496 EKEIVDYVASQVTTAKKLRGGVVFVDEVPKGLTGKLDARKIR 537
Cdd:cd05944 312 EEELLAWARDHVPERAAVPKHIEVLEELPVTAVGKVFKPALR 353
|
|
| PRK06087 |
PRK06087 |
medium-chain fatty-acid--CoA ligase; |
20-542 |
4.44e-49 |
|
medium-chain fatty-acid--CoA ligase;
Pssm-ID: 180393 [Multi-domain] Cd Length: 547 Bit Score: 178.02 E-value: 4.44e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1216630836 20 DGTAGEQLHKAMKRYalvPGTIAFTDAHiEVDITYAEYFEMSVRLAEAMKRYGLNTNHRIVVCSENSLQFFMPVLGALFI 99
Cdd:PRK06087 22 DASLADYWQQTARAM---PDKIAVVDNH-GASYTYSALDHAASRLANWLLAKGIEPGDRVAFQLPGWCEFTIIYLACLKV 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1216630836 100 GVAVAPANDIYNERELLNSMGISQPTVVFV-----SKKGLQKILNVQKKLPIIQKIIIMDSKTdyqgfQSMYTFVTSH-L 173
Cdd:PRK06087 98 GAVSVPLLPSWREAELVWVLNKCQAKMFFAptlfkQTRPVDLILPLQNQLPQLQQIVGVDKLA-----PATSSLSLSQiI 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1216630836 174 PPGFNEYDFVPESFDrdkTIALIMNSSGSTGLPKGVALPHRTacVRFSHaRDPIFGNQIIPDTAILSVVPFHHGFGMF-- 251
Cdd:PRK06087 173 ADYEPLTTAITTHGD---ELAAVLFTSGTEGLPKGVMLTHNN--ILASE-RAYCARLNLTWQDVFMMPAPLGHATGFLhg 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1216630836 252 TTLGYLIcGFRVVLMYRFEEELFLRSLQDYKIqSALLVPTLFSFFAKSTL-IDKYDLSNLHEIASGGAPLSKEVgeavAK 330
Cdd:PRK06087 247 VTAPFLI-GARSVLLDIFTPDACLALLEQQRC-TCMLGATPFIYDLLNLLeKQPADLSALRFFLCGGTTIPKKV----AR 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1216630836 331 RFHLPGIR--QGYGLTETTSAILITPegdDKP-----GAVGKVVPFFEAKVVDlDTGKTLGVNQRGELCVRGPMIMSGYV 403
Cdd:PRK06087 321 ECQQRGIKllSVYGSTESSPHAVVNL---DDPlsrfmHTDGYAAAGVEIKVVD-EARKTLPPGCEGEEASRGPNVFMGYL 396
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1216630836 404 NNPEATNALIDKDGWLHSGDIAYWDEDEHFFIVDRLKSLIKYKGYQVAPAELESILLQHPNIFDAGVAGLPDDDAGELPA 483
Cdd:PRK06087 397 DEPELTARALDEEGWYYSGDLCRMDEAGYIKITGRKKDIIVRGGENISSREVEDILLQHPKIHDACVVAMPDERLGERSC 476
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1216630836 484 AVVVL-EHGKTMTEKEIVDYVASQVTTAKKLRGGVVFVDEVPKGLTGKLDARKIREILIK 542
Cdd:PRK06087 477 AYVVLkAPHHSLTLEEVVAFFSRKRVAKYKYPEHIVVIDKLPRTASGKIQKFLLRKDIMR 536
|
|
| PRK06145 |
PRK06145 |
acyl-CoA synthetase; Validated |
51-538 |
1.24e-48 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 102207 [Multi-domain] Cd Length: 497 Bit Score: 175.84 E-value: 1.24e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1216630836 51 DITYAEyFEMSVRLAEAM-KRYGLNTNHRIVVCSENSLQFFMPVLGALFIGVAVAPANdiynerellnsMGISQPTVVFV 129
Cdd:PRK06145 27 EISYAE-FHQRILQAAGMlHARGIGQGDVVALLMKNSAAFLELAFAASYLGAVFLPIN-----------YRLAADEVAYI 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1216630836 130 SKKGLQKILNVQKKLPIIQKIIIMDSKTDYQGFQSMYTFVTSHLPpgfneydFVPESFDRDKTIALIMNSSGSTGLPKGV 209
Cdd:PRK06145 95 LGDAGAKLLLVDEEFDAIVALETPKIVIDAAAQADSRRLAQGGLE-------IPPQAAVAPTDLVRLMYTSGTTDRPKGV 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1216630836 210 AlpHRTACVRFSHArDPIFGNQIIPDTAILSVVPFHH-GFGMFTTLGYLICGFRVVLMYRFEEELFLRSLQDYKIQSALL 288
Cdd:PRK06145 168 M--HSYGNLHWKSI-DHVIALGLTASERLLVVGPLYHvGAFDLPGIAVLWVGGTLRIHREFDPEAVLAAIERHRLTCAWM 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1216630836 289 VPTLFSFFAKSTLIDKYDLSNLHEIASGGAPLSKEVGEAVAKRFHLPGIRQGYGLTETTSAILITPEGD--DKPGAVGKV 366
Cdd:PRK06145 245 APVMLSRVLTVPDRDRFDLDSLAWCIGGGEKTPESRIRDFTRVFTRARYIDAYGLTETCSGDTLMEAGReiEKIGSTGRA 324
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1216630836 367 VPFFEAKVVDlDTGKTLGVNQRGELCVRGPMIMSGYVNNPEATNALIdKDGWLHSGDIAYWDEDEHFFIVDRLKSLIKYK 446
Cdd:PRK06145 325 LAHVEIRIAD-GAGRWLPPNMKGEICMRGPKVTKGYWKDPEKTAEAF-YGDWFRSGDVGYLDEEGFLYLTDRKKDMIISG 402
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1216630836 447 GYQVAPAELESILLQHPNIFDAGVAGLPDDDAGELPAAVVVLEHGKTMTEKEIVDYVASQVTTAKKLRGGVVfVDEVPKG 526
Cdd:PRK06145 403 GENIASSEVERVIYELPEVAEAAVIGVHDDRWGERITAVVVLNPGATLTLEALDRHCRQRLASFKVPRQLKV-RDELPRN 481
|
490
....*....|..
gi 1216630836 527 LTGKLDARKIRE 538
Cdd:PRK06145 482 PSGKVLKRVLRD 493
|
|
| PRK04319 |
PRK04319 |
acetyl-CoA synthetase; Provisional |
43-538 |
1.30e-48 |
|
acetyl-CoA synthetase; Provisional
Pssm-ID: 235279 [Multi-domain] Cd Length: 570 Bit Score: 177.39 E-value: 1.30e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1216630836 43 FTDAHIEVDITYAEYFEMSVRLAEAMKRYGLNTNHRIVVCSENSLQFFMPVLGALFIGVAVAPANDIYNERELLNSMGIS 122
Cdd:PRK04319 65 YLDASRKEKYTYKELKELSNKFANVLKELGVEKGDRVFIFMPRIPELYFALLGALKNGAIVGPLFEAFMEEAVRDRLEDS 144
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1216630836 123 QPTVVFVSKKGLQKIlnVQKKLPIIQKIIIMDSKTDYQGfqsmytfVTSHLPPGFNEY--DFVPESFDRDKTiALIMNSS 200
Cdd:PRK04319 145 EAKVLITTPALLERK--PADDLPSLKHVLLVGEDVEEGP-------GTLDFNALMEQAsdEFDIEWTDREDG-AILHYTS 214
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1216630836 201 GSTGLPKGVALPHRTACVRFSHAR---------------DP---------IFGnqiipdtailsvvPFHHGFGMfttlgy 256
Cdd:PRK04319 215 GSTGKPKGVLHVHNAMLQHYQTGKyvldlheddvywctaDPgwvtgtsygIFA-------------PWLNGATN------ 275
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1216630836 257 licgfrVVLMYRFEEELFLRSLQDYKIQSALLVPTLFSFF--AKSTLIDKYDLSNLHEIASGGAPLSKEV---GEAVakr 331
Cdd:PRK04319 276 ------VIDGGRFSPERWYRILEDYKVTVWYTAPTAIRMLmgAGDDLVKKYDLSSLRHILSVGEPLNPEVvrwGMKV--- 346
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1216630836 332 FHLPgIRQGYGLTETtSAILI--TPEGDDKPGAVGKVVPFFEAKVVDlDTGKTLGVNQRGELCVRG--PMIMSGYVNNPE 407
Cdd:PRK04319 347 FGLP-IHDNWWMTET-GGIMIanYPAMDIKPGSMGKPLPGIEAAIVD-DQGNELPPNRMGNLAIKKgwPSMMRGIWNNPE 423
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1216630836 408 ATNALIdKDGWLHSGDIAYWDEDEHFFIVDRLKSLIKYKGYQVAPAELESILLQHPNIFDAGVAGLPDDDAGELPAAVVV 487
Cdd:PRK04319 424 KYESYF-AGDWYVSGDSAYMDEDGYFWFQGRVDDVIKTSGERVGPFEVESKLMEHPAVAEAGVIGKPDPVRGEIIKAFVA 502
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1216630836 488 LEHGKTMTE---KEIVDYVasqvttaKKLRGGVV------FVDEVPKGLTGKLDAR--KIRE 538
Cdd:PRK04319 503 LRPGYEPSEelkEEIRGFV-------KKGLGAHAapreieFKDKLPKTRSGKIMRRvlKAWE 557
|
|
| EntE |
COG1021 |
EntE, 2,3-dihydroxybenzoate-AMP synthase component of non-ribosomal peptide synthetase ... |
19-540 |
5.31e-48 |
|
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: 174.95 E-value: 5.31e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1216630836 19 EDGTAGEQLHKAMKRYalvPGTIAFTDAHIEvdITYAEYFEMSVRLAEAMKRYGLNTNHRIVVCSENSLQFFMPVLGALF 98
Cdd:COG1021 23 RGETLGDLLRRRAERH---PDRIAVVDGERR--LSYAELDRRADRLAAGLLALGLRPGDRVVVQLPNVAEFVIVFFALFR 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1216630836 99 IG---VAVAPAndiYNERELLNSMGISQPTVVFVSKK----GLQKILN-VQKKLPIIQKIIIMDSKTDYQGFQSMYTFVT 170
Cdd:COG1021 98 AGaipVFALPA---HRRAEISHFAEQSEAVAYIIPDRhrgfDYRALAReLQAEVPSLRHVLVVGDAGEFTSLDALLAAPA 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1216630836 171 SHLPPGfneydfvPESFDrdktIALIMNSSGSTGLPKGVALPHRT-AC-VRFShARdpIFGnqIIPDTAILSVVPFHHGF 248
Cdd:COG1021 175 DLSEPR-------PDPDD----VAFFQLSGGTTGLPKLIPRTHDDyLYsVRAS-AE--ICG--LDADTVYLAALPAAHNF 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1216630836 249 GM--FTTLGYLICGFRVVLMYRFEEELFLRSLQDYKIQSALLVPTLFSFFAKSTLIDKYDLSNLHEIASGGAPLSKEVGE 326
Cdd:COG1021 239 PLssPGVLGVLYAGGTVVLAPDPSPDTAFPLIERERVTVTALVPPLALLWLDAAERSRYDLSSLRVLQVGGAKLSPELAR 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1216630836 327 AVAKRFHlPGIRQGYGLTEttSAILITPEGDD---------KPgavgkVVPFFEAKVVDlDTGKTLGVNQRGELCVRGPM 397
Cdd:COG1021 319 RVRPALG-CTLQQVFGMAE--GLVNYTRLDDPeevilttqgRP-----ISPDDEVRIVD-EDGNPVPPGEVGELLTRGPY 389
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1216630836 398 IMSGYVNNPEAtNAL-IDKDGWLHSGDIAYWDEDEHFFIVDRLKSLIKYKGYQVAPAELESILLQHPNIFDAGVAGLPDD 476
Cdd:COG1021 390 TIRGYYRAPEH-NARaFTPDGFYRTGDLVRRTPDGYLVVEGRAKDQINRGGEKIAAEEVENLLLAHPAVHDAAVVAMPDE 468
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1216630836 477 DAGELPAAVVVLeHGKTMTEKEIVDYVASQVTTAKKLRGGVVFVDEVPKGLTGKLDARKIREIL 540
Cdd:COG1021 469 YLGERSCAFVVP-RGEPLTLAELRRFLRERGLAAFKLPDRLEFVDALPLTAVGKIDKKALRAAL 531
|
|
| PRK08276 |
PRK08276 |
long-chain-fatty-acid--CoA ligase; Validated |
41-538 |
5.72e-48 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236215 [Multi-domain] Cd Length: 502 Bit Score: 173.94 E-value: 5.72e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1216630836 41 IAFTDAHIevdiTYAEYFEMSVRLAEAMKRYGLNTNHRIVVCSENSLQFFMPVLGALFIGVAVAPANDIYNERELLNSMG 120
Cdd:PRK08276 5 MAPSGEVV----TYGELEARSNRLAHGLRALGLREGDVVAILLENNPEFFEVYWAARRSGLYYTPINWHLTAAEIAYIVD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1216630836 121 ISQPTVVFVSKKGLQKILNVQKKLPIIQKIIIMDSKTdyqgfqsmytfvtshlPPGFNEY----DFVPESFDRDKTIALI 196
Cdd:PRK08276 81 DSGAKVLIVSAALADTAAELAAELPAGVPLLLVVAGP----------------VPGFRSYeealAAQPDTPIADETAGAD 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1216630836 197 MN-SSGSTGLPKGV--ALPHRTACVR-FSHARDPIFGNQIIPDTAILSVVPFHHG----FGMFTtlgyLICGFRVVLMYR 268
Cdd:PRK08276 145 MLySSGTTGRPKGIkrPLPGLDPDEApGMMLALLGFGMYGGPDSVYLSPAPLYHTaplrFGMSA----LALGGTVVVMEK 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1216630836 269 FEEELFLRSLQDYKIQSALLVPTLFSFFAKstLID----KYDLSNLHEIASGGAPLSKEVgeavaKRFHL----PGIRQG 340
Cdd:PRK08276 221 FDAEEALALIERYRVTHSQLVPTMFVRMLK--LPEevraRYDVSSLRVAIHAAAPCPVEV-----KRAMIdwwgPIIHEY 293
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1216630836 341 YGLTETTSAILITPEgD--DKPGAVGKVVpFFEAKVVDlDTGKTLGVNQRGELCVRGPMIMSGYVNNPEATNALIDKDGW 418
Cdd:PRK08276 294 YASSEGGGVTVITSE-DwlAHPGSVGKAV-LGEVRILD-EDGNELPPGEIGTVYFEMDGYPFEYHNDPEKTAAARNPHGW 370
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1216630836 419 LHSGDIAYWDEDEHFFIVDRLKSLIKYKGYQVAPAELESILLQHPNIFDAGVAGLPDDDAGELPAAVVVLEHGKTMTE-- 496
Cdd:PRK08276 371 VTVGDVGYLDEDGYLYLTDRKSDMIISGGVNIYPQEIENLLVTHPKVADVAVFGVPDEEMGERVKAVVQPADGADAGDal 450
|
490 500 510 520
....*....|....*....|....*....|....*....|...
gi 1216630836 497 -KEIVDYVASQVTTAKKLRgGVVFVDEVPKGLTGKLDARKIRE 538
Cdd:PRK08276 451 aAELIAWLRGRLAHYKCPR-SIDFEDELPRTPTGKLYKRRLRD 492
|
|
| MACS_like_3 |
cd05971 |
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the ... |
194-537 |
9.71e-48 |
|
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: 171.85 E-value: 9.71e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1216630836 194 ALIMNSSGSTGLPKGVALPHRtacVRFSHARDPIFGNQIIPDTAILSVVPFHHGF--GMFTTL-GYLICGFRVVL--MYR 268
Cdd:cd05971 91 ALIIYTSGTTGPPKGALHAHR---VLLGHLPGVQFPFNLFPRDGDLYWTPADWAWigGLLDVLlPSLYFGVPVLAhrMTK 167
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1216630836 269 FEEELFLRSLQDYKIQSALLVPTLFSFFAKSTLIDKYDLSNLHEIASGGAPLSKEVGEAVAKRFHLPgIRQGYGLTE--- 345
Cdd:cd05971 168 FDPKAALDLMSRYGVTTAFLPPTALKMMRQQGEQLKHAQVKLRAIATGGESLGEELLGWAREQFGVE-VNEFYGQTEcnl 246
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1216630836 346 --TTSAILitpeGDDKPGAVGKVVPFFEAKVVDlDTGKTLGVNQRGELCVR--GPMIMSGYVNNPEATNALIdKDGWLHS 421
Cdd:cd05971 247 viGNCSAL----FPIKPGSMGKPIPGHRVAIVD-DNGTPLPPGEVGEIAVElpDPVAFLGYWNNPSATEKKM-AGDWLLT 320
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1216630836 422 GDIAYWDEDEHFFIVDRLKSLIKYKGYQVAPAELESILLQHPNIFDAGVAGLPDDDAGELPAAVVVLEHGKTMTE---KE 498
Cdd:cd05971 321 GDLGRKDSDGYFWYVGRDDDVITSSGYRIGPAEIEECLLKHPAVLMAAVVGIPDPIRGEIVKAFVVLNPGETPSDalaRE 400
|
330 340 350
....*....|....*....|....*....|....*....
gi 1216630836 499 IVDYVASQVTTAKKLRgGVVFVDEVPKGLTGKLDARKIR 537
Cdd:cd05971 401 IQELVKTRLAAHEYPR-EIEFVNELPRTATGKIRRRELR 438
|
|
| BACL_like |
cd05929 |
Bacterial Bile acid CoA ligases and similar proteins; Bile acid-Coenzyme A ligase catalyzes ... |
195-538 |
9.86e-47 |
|
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: 170.25 E-value: 9.86e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1216630836 195 LIMNSSGSTGLPKGV--ALPHRTACVrfSHARDPIFGNQIIPDTAILSVVPFHHGFGMFTTLGYLICGFRVVLMYRFEEE 272
Cdd:cd05929 129 KMLYSGGTTGRPKGIkrGLPGGPPDN--DTLMAAALGFGPGADSVYLSPAPLYHAAPFRWSMTALFMGGTLVLMEKFDPE 206
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1216630836 273 LFLRSLQDYKIQSALLVPTLFSFFAK--STLIDKYDLSNLHEIASGGAPLSKEVGEAVakrFHL--PGIRQGYGLTETTS 348
Cdd:cd05929 207 EFLRLIERYRVTFAQFVPTMFVRLLKlpEAVRNAYDLSSLKRVIHAAAPCPPWVKEQW---IDWggPIIWEYYGGTEGQG 283
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1216630836 349 AILITpeGDD---KPGAVGKVVpFFEAKVVDLDtGKTLGVNQRGELCVRGPMiMSGYVNNPEATNALIDKDGWLHSGDIA 425
Cdd:cd05929 284 LTIIN--GEEwltHPGSVGRAV-LGKVHILDED-GNEVPPGEIGEVYFANGP-GFEYTNDPEKTAAARNEGGWSTLGDVG 358
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1216630836 426 YWDEDEHFFIVDRLKSLIKYKGYQVAPAELESILLQHPNIFDAGVAGLPDDDAGELPAAVV---VLEHGKTMTEKEIVDY 502
Cdd:cd05929 359 YLDEDGYLYLTDRRSDMIISGGVNIYPQEIENALIAHPKVLDAAVVGVPDEELGQRVHAVVqpaPGADAGTALAEELIAF 438
|
330 340 350
....*....|....*....|....*....|....*.
gi 1216630836 503 VASQVTTAKKLRgGVVFVDEVPKGLTGKLDARKIRE 538
Cdd:cd05929 439 LRDRLSRYKCPR-SIEFVAELPRDDTGKLYRRLLRD 473
|
|
| PRK13295 |
PRK13295 |
cyclohexanecarboxylate-CoA ligase; Reviewed |
38-540 |
1.98e-46 |
|
cyclohexanecarboxylate-CoA ligase; Reviewed
Pssm-ID: 171961 [Multi-domain] Cd Length: 547 Bit Score: 170.62 E-value: 1.98e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1216630836 38 PGTIAFTDAHIE----VDITYAEYFEMSVRLAEAMKRYGLNTNHriVVCSE--NSLQFFMPVLGALFIGVAVAPANDIYN 111
Cdd:PRK13295 38 PDKTAVTAVRLGtgapRRFTYRELAALVDRVAVGLARLGVGRGD--VVSCQlpNWWEFTVLYLACSRIGAVLNPLMPIFR 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1216630836 112 ERELLNSMGISQPTVVFVSK--KGL---QKILNVQKKLPIIQKIIIMDSKTDyQGFQSMYTfvtshlPPGFNEYDFVPES 186
Cdd:PRK13295 116 ERELSFMLKHAESKVLVVPKtfRGFdhaAMARRLRPELPALRHVVVVGGDGA-DSFEALLI------TPAWEQEPDAPAI 188
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1216630836 187 FDRDKT----IALIMNSSGSTGLPKGVAlphrtacvrfsHARDPIFGNqIIP---------DTAILSVVPFHH--GFgMF 251
Cdd:PRK13295 189 LARLRPgpddVTQLIYTSGTTGEPKGVM-----------HTANTLMAN-IVPyaerlglgaDDVILMASPMAHqtGF-MY 255
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1216630836 252 TTLGYLICGFRVVLMYRFEEELFLRSLQDYKIQSALLVPTLFSFFAKSTLIDKYDLSNLHEIASGGAPLSKEVGEAVAKR 331
Cdd:PRK13295 256 GLMMPVMLGATAVLQDIWDPARAAELIRTEGVTFTMASTPFLTDLTRAVKESGRPVSSLRTFLCAGAPIPGALVERARAA 335
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1216630836 332 FHLPgIRQGYGLTETTSAILITPEGDDKPGAV--GKVVPFFEAKVVDLDtGKTLGVNQRGELCVRGPMIMSGYVNNPEAT 409
Cdd:PRK13295 336 LGAK-IVSAWGMTENGAVTLTKLDDPDERASTtdGCPLPGVEVRVVDAD-GAPLPAGQIGRLQVRGCSNFGGYLKRPQLN 413
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1216630836 410 NalIDKDGWLHSGDIAYWDEDEHFFIVDRLKSLIKYKGYQVAPAELESILLQHPNIFDAGVAGLPDDDAGELPAAVVVLE 489
Cdd:PRK13295 414 G--TDADGWFDTGDLARIDADGYIRISGRSKDVIIRGGENIPVVEIEALLYRHPAIAQVAIVAYPDERLGERACAFVVPR 491
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|.
gi 1216630836 490 HGKTMTEKEIVDYVASQVTTAKKLRGGVVFVDEVPKGLTGKLDARKIREIL 540
Cdd:PRK13295 492 PGQSLDFEEMVEFLKAQKVAKQYIPERLVVRDALPRTPSGKIQKFRLREML 542
|
|
| PRK12406 |
PRK12406 |
long-chain-fatty-acid--CoA ligase; Provisional |
199-538 |
2.61e-46 |
|
long-chain-fatty-acid--CoA ligase; Provisional
Pssm-ID: 183506 [Multi-domain] Cd Length: 509 Bit Score: 169.88 E-value: 2.61e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1216630836 199 SSGSTGLPKGV----ALPHRTAcvRFSHARDPIFGnqIIPDTAILSVVPFHH----GFGMFT-TLGYLIcgfrvVLMYRF 269
Cdd:PRK12406 160 TSGTTGHPKGVrraaPTPEQAA--AAEQMRALIYG--LKPGIRALLTGPLYHsapnAYGLRAgRLGGVL-----VLQPRF 230
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1216630836 270 EEELFLRSLQDYKIQSALLVPTLFSFFAK--STLIDKYDLSNLHEIASGGAPLSKEVGEAVAKRFHlPGIRQGYGLTETT 347
Cdd:PRK12406 231 DPEELLQLIERHRITHMHMVPTMFIRLLKlpEEVRAKYDVSSLRHVIHAAAPCPADVKRAMIEWWG-PVIYEYYGSTESG 309
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1216630836 348 SAILITPEGD-DKPGAVGKVVPFFEAKVVDlDTGKTLGVNQRGELCVRGP-MIMSGYVNNPEAtNALIDKDGWLHSGDIA 425
Cdd:PRK12406 310 AVTFATSEDAlSHPGTVGKAAPGAELRFVD-EDGRPLPQGEIGEIYSRIAgNPDFTYHNKPEK-RAEIDRGGFITSGDVG 387
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1216630836 426 YWDEDEHFFIVDRLKSLIKYKGYQVAPAELESILLQHPNIFDAGVAGLPDDDAGELPAAVVVLEHGKTMTEKEIVDYVAS 505
Cdd:PRK12406 388 YLDADGYLFLCDRKRDMVISGGVNIYPAEIEAVLHAVPGVHDCAVFGIPDAEFGEALMAVVEPQPGATLDEADIRAQLKA 467
|
330 340 350
....*....|....*....|....*....|...
gi 1216630836 506 QVTTAKKLRgGVVFVDEVPKGLTGKLDARKIRE 538
Cdd:PRK12406 468 RLAGYKVPK-HIEIMAELPREDSGKIFKRRLRD 499
|
|
| PRK07514 |
PRK07514 |
malonyl-CoA synthase; Validated |
52-530 |
1.92e-45 |
|
malonyl-CoA synthase; Validated
Pssm-ID: 181011 [Multi-domain] Cd Length: 504 Bit Score: 166.97 E-value: 1.92e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1216630836 52 ITYAEYFEMSVRLAEAMKRYGLNTNHRIVVCSENSLQFFMPVLGALFIGVAVAPANDIYNERELLNSMGISQPTVVFVSk 131
Cdd:PRK07514 29 YTYGDLDAASARLANLLVALGVKPGDRVAVQVEKSPEALALYLATLRAGAVFLPLNTAYTLAELDYFIGDAEPALVVCD- 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1216630836 132 kglqkilnvQKKLPIIQKIiimdskTDYQGFQSMYTF----------VTSHLPPgfneyDFVPESFDRDKtIALIMNSSG 201
Cdd:PRK07514 108 ---------PANFAWLSKI------AAAAGAPHVETLdadgtgslleAAAAAPD-----DFETVPRGADD-LAAILYTSG 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1216630836 202 STGLPKGVALPHRT----ACV-----RFShardpifgnqiiPDTAILSVVPFHHGFGMF-TTLGYLICGFRVVLMYRFEE 271
Cdd:PRK07514 167 TTGRSKGAMLSHGNllsnALTlvdywRFT------------PDDVLIHALPIFHTHGLFvATNVALLAGASMIFLPKFDP 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1216630836 272 ELFLRSLQdykiQSALL--VPTLFSFFAKSTLIDKYDLSNLHEIASGGAPLSKEVGEAVAKRF-HlpGIRQGYGLTETts 348
Cdd:PRK07514 235 DAVLALMP----RATVMmgVPTFYTRLLQEPRLTREAAAHMRLFISGSAPLLAETHREFQERTgH--AILERYGMTET-- 306
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1216630836 349 aILIT--P-EGDDKPGAVGKVVPFFEAKVVDLDTGKTLGVNQRGELCVRGPMIMSGYVNNPEATNALIDKDGWLHSGDIA 425
Cdd:PRK07514 307 -NMNTsnPyDGERRAGTVGFPLPGVSLRVTDPETGAELPPGEIGMIEVKGPNVFKGYWRMPEKTAEEFRADGFFITGDLG 385
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1216630836 426 YWDEDEHFFIVDRLKSLIKYKGYQVAPAELESILLQHPNIFDAGVAGLPDDDAGELPAAVVVLEHGKTMTEKEIVDYVAS 505
Cdd:PRK07514 386 KIDERGYVHIVGRGKDLIISGGYNVYPKEVEGEIDELPGVVESAVIGVPHPDFGEGVTAVVVPKPGAALDEAAILAALKG 465
|
490 500
....*....|....*....|....*.
gi 1216630836 506 QVttAK-KLRGGVVFVDEVPKGLTGK 530
Cdd:PRK07514 466 RL--ARfKQPKRVFFVDELPRNTMGK 489
|
|
| PRK06155 |
PRK06155 |
crotonobetaine/carnitine-CoA ligase; Provisional |
53-543 |
3.27e-45 |
|
crotonobetaine/carnitine-CoA ligase; Provisional
Pssm-ID: 235719 [Multi-domain] Cd Length: 542 Bit Score: 167.24 E-value: 3.27e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1216630836 53 TYAEYFEMSVRLAEAMKRYGLNTNHRIVVCSENSLQFFMPVLGALFIGVAVAPANDIYNERELLNSMGISQPTVVFVSKK 132
Cdd:PRK06155 48 TYAEAARAAAAAAHALAAAGVKRGDRVALMCGNRIEFLDVFLGCAWLGAIAVPINTALRGPQLEHILRNSGARLLVVEAA 127
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1216630836 133 GLQKILNVQKKLPIIQKIIIMDSKtdyqgfqsmytfVTSHLPPGFNEYDFVP--ESFD----RDKTIALIMNSSGSTGLP 206
Cdd:PRK06155 128 LLAALEAADPGDLPLPAVWLLDAP------------ASVSVPAGWSTAPLPPldAPAPaaavQPGDTAAILYTSGTTGPS 195
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1216630836 207 KGVALPHrtacvrfshARDPIFGN------QIIPDTAILSVVPFHHGFGMFTTLGYLICGFRVVLMYRFEEELFLRSLQD 280
Cdd:PRK06155 196 KGVCCPH---------AQFYWWGRnsaedlEIGADDVLYTTLPLFHTNALNAFFQALLAGATYVLEPRFSASGFWPAVRR 266
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1216630836 281 YKIQSALLVPTLFSFFAKSTlidKYDLSNLHEIASGGAP-LSKEVGEAVAKRFHLPgIRQGYGLTETTSAILITPeGDDK 359
Cdd:PRK06155 267 HGATVTYLLGAMVSILLSQP---ARESDRAHRVRVALGPgVPAALHAAFRERFGVD-LLDGYGSTETNFVIAVTH-GSQR 341
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1216630836 360 PGAVGKVVPFFEAKVVDlDTGKTLGVNQRGELCVRG--PM-IMSGYVNNPEATNALIdKDGWLHSGDIAYWDEDEHFFIV 436
Cdd:PRK06155 342 PGSMGRLAPGFEARVVD-EHDQELPDGEPGELLLRAdePFaFATGYFGMPEKTVEAW-RNLWFHTGDRVVRDADGWFRFV 419
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1216630836 437 DRLKSLIKYKGYQVAPAELESILLQHPNIFDAGVAGLPDDDAGELPAAVVVLEHGKTMTEKEIVDYVASQVTTAKKLRgG 516
Cdd:PRK06155 420 DRIKDAIRRRGENISSFEVEQVLLSHPAVAAAAVFPVPSELGEDEVMAAVVLRDGTALEPVALVRHCEPRLAYFAVPR-Y 498
|
490 500
....*....|....*....|....*..
gi 1216630836 517 VVFVDEVPKGLTGKLDARKIREILIKA 543
Cdd:PRK06155 499 VEFVAALPKTENGKVQKFVLREQGVTA 525
|
|
| PRK08633 |
PRK08633 |
2-acyl-glycerophospho-ethanolamine acyltransferase; Validated |
22-539 |
2.22e-44 |
|
2-acyl-glycerophospho-ethanolamine acyltransferase; Validated
Pssm-ID: 236315 [Multi-domain] Cd Length: 1146 Bit Score: 168.95 E-value: 2.22e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1216630836 22 TAGEQLHKAMKRyalVPGTIAFTDAhIEVDITYAEYFEMSVRLAEAMKRYGLNTNHrIVVCSENSLQFFMPVLGALFIGV 101
Cdd:PRK08633 616 PLAEAWIDTAKR---NWSRLAVADS-TGGELSYGKALTGALALARLLKRELKDEEN-VGILLPPSVAGALANLALLLAGK 690
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1216630836 102 AVAPANDIYNERELLNSMGISQPTVVFVSKKGLQKI--LNVQKKLPIIQKIIIM-DSKTDYQGFQSMYTFVTSHLPPGFN 178
Cdd:PRK08633 691 VPVNLNYTASEAALKSAIEQAQIKTVITSRKFLEKLknKGFDLELPENVKVIYLeDLKAKISKVDKLTALLAARLLPARL 770
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1216630836 179 EYDFVPESFDRDKTIALIMnSSGSTGLPKGVALPHRTacvrfshardpIFGN-----QIIP---DTAILSVVPFHHGFGM 250
Cdd:PRK08633 771 LKRLYGPTFKPDDTATIIF-SSGSEGEPKGVMLSHHN-----------ILSNieqisDVFNlrnDDVILSSLPFFHSFGL 838
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1216630836 251 -FTTLGYLICGFRVVLMYRFEEELFLRSLQDyKIQSALLV--PTLFSFFAKSTLIDKYDLSNLHEIASGGAPLSKEVGEA 327
Cdd:PRK08633 839 tVTLWLPLLEGIKVVYHPDPTDALGIAKLVA-KHRATILLgtPTFLRLYLRNKKLHPLMFASLRLVVAGAEKLKPEVADA 917
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1216630836 328 VAKRFHLPgIRQGYGLTETTSAILI-TP---EGDD------KPGAVGKVVPFFEAKVVDLDTGKTLGVNQRGELCVRGPM 397
Cdd:PRK08633 918 FEEKFGIR-ILEGYGATETSPVASVnLPdvlAADFkrqtgsKEGSVGMPLPGVAVRIVDPETFEELPPGEDGLILIGGPQ 996
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1216630836 398 IMSGYVNNPEATNALI---DKDGWLHSGDIAYWDEDEHFFIVDRLKSLIKYKGYQVAPAELESILLQhpnIFDAG----- 469
Cdd:PRK08633 997 VMKGYLGDPEKTAEVIkdiDGIGWYVTGDKGHLDEDGFLTITDRYSRFAKIGGEMVPLGAVEEELAK---ALGGEevvfa 1073
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1216630836 470 VAGLPDDDAGElpaAVVVLEHGKTMTEKEIVDYVASQVTTAKKLRGGVVFVDEVPKGLTGKLDARKIREI 539
Cdd:PRK08633 1074 VTAVPDEKKGE---KLVVLHTCGAEDVEELKRAIKESGLPNLWKPSRYFKVEALPLLGSGKLDLKGLKEL 1140
|
|
| PRK07470 |
PRK07470 |
acyl-CoA synthetase; Validated |
199-540 |
2.39e-44 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 180988 [Multi-domain] Cd Length: 528 Bit Score: 164.44 E-value: 2.39e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1216630836 199 SSGSTGLPKGVALPHRT-ACVRFSHARDpifgnqIIPDT----AILSVVPFHHGFGMfttlgYLIC----GFRVVLMY-- 267
Cdd:PRK07470 171 TSGTTGRPKAAVLTHGQmAFVITNHLAD------LMPGTteqdASLVVAPLSHGAGI-----HQLCqvarGAATVLLPse 239
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1216630836 268 RFEEELFLRSLQDYKIQSALLVPTLFSFFAKSTLIDKYDLSNLHEIASGGAPLSKEVGEAVAKRFHlPGIRQGYGLTETT 347
Cdd:PRK07470 240 RFDPAEVWALVERHRVTNLFTVPTILKMLVEHPAVDRYDHSSLRYVIYAGAPMYRADQKRALAKLG-KVLVQYFGLGEVT 318
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1216630836 348 SAILITP----EGDDKP----GAVGKVVPFFEAKVVDlDTGKTLGVNQRGELCVRGPMIMSGYVNNPEAtNALIDKDGWL 419
Cdd:PRK07470 319 GNITVLPpalhDAEDGPdariGTCGFERTGMEVQIQD-DEGRELPPGETGEICVIGPAVFAGYYNNPEA-NAKAFRDGWF 396
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1216630836 420 HSGDIAYWDEDEHFFIVDRLKSLIKYKGYQVAPAELESILLQHPNIFDAGVAGLPDDDAGELPAAVVVLEHGKTMTEKEI 499
Cdd:PRK07470 397 RTGDLGHLDARGFLYITGRASDMYISGGSNVYPREIEEKLLTHPAVSEVAVLGVPDPVWGEVGVAVCVARDGAPVDEAEL 476
|
330 340 350 360
....*....|....*....|....*....|....*....|..
gi 1216630836 500 VDYVASQVttAK-KLRGGVVFVDEVPKGLTGKLDARKIREIL 540
Cdd:PRK07470 477 LAWLDGKV--ARyKLPKRFFFWDALPKSGYGKITKKMVREEL 516
|
|
| 23DHB-AMP_lg |
cd05920 |
2,3-dihydroxybenzoate-AMP ligase; 2,3-dihydroxybenzoate-AMP ligase activates 2, ... |
19-532 |
9.93e-44 |
|
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: 162.11 E-value: 9.93e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1216630836 19 EDGTAGEQLHKAMKRYalvPGTIAFTDAhiEVDITYAEYFEMSVRLAEAMKRYGLNTNHRIVVCSENSLQFFMPVLGALF 98
Cdd:cd05920 13 QDEPLGDLLARSAARH---PDRIAVVDG--DRRLTYRELDRRADRLAAGLRGLGIRPGDRVVVQLPNVAEFVVLFFALLR 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1216630836 99 IGVAVAPANDIYNERELLNSMGISQPTVVFVSKKglqkilnvqkklpiiqkiiimdsktdYQGFQSMYTFVTSHlppgfn 178
Cdd:cd05920 88 LGAVPVLALPSHRRSELSAFCAHAEAVAYIVPDR--------------------------HAGFDHRALARELA------ 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1216630836 179 eyDFVPEsfdrdktIALIMNSSGSTGLPKGVALPHR------TACVRFSHardpifgnqIIPDTAILSVVPFHHGFGMFT 252
Cdd:cd05920 136 --ESIPE-------VALFLLSGGTTGTPKLIPRTHNdyaynvRASAEVCG---------LDQDTVYLAVLPAAHNFPLAC 197
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1216630836 253 --TLGYLICGFRVVLMYRFEEELFLRSLQDYKIQSALLVPTLFSFFAKSTLIDKYDLSNLHEIASGGAPLSKEVGEAVAK 330
Cdd:cd05920 198 pgVLGTLLAGGRVVLAPDPSPDAAFPLIEREGVTVTALVPALVSLWLDAAASRRADLSSLRLLQVGGARLSPALARRVPP 277
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1216630836 331 RFHlPGIRQGYGLTETtsaiLITPEGDDKPGAV-----GK-VVPFFEAKVVDLDtGKTLGVNQRGELCVRGPMIMSGYVN 404
Cdd:cd05920 278 VLG-CTLQQVFGMAEG----LLNYTRLDDPDEViihtqGRpMSPDDEIRVVDEE-GNPVPPGEEGELLTRGPYTIRGYYR 351
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1216630836 405 NPEATNALIDKDGWLHSGDIAYWDEDEHFFIVDRLKSLIKYKGYQVAPAELESILLQHPNIFDAGVAGLPDDDAGELPAA 484
Cdd:cd05920 352 APEHNARAFTPDGFYRTGDLVRRTPDGYLVVEGRIKDQINRGGEKIAAEEVENLLLRHPAVHDAAVVAMPDELLGERSCA 431
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*.
gi 1216630836 485 VVVLEHGKT--------MTEKEIVDYvasqvttakKLRGGVVFVDEVPKGLTGKLD 532
Cdd:cd05920 432 FVVLRDPPPsaaqlrrfLRERGLAAY---------KLPDRIEFVDSLPLTAVGKID 478
|
|
| BCL_like |
cd05919 |
Benzoate CoA ligase (BCL) and similar adenylate forming enzymes; This family contains benzoate ... |
47-537 |
1.94e-43 |
|
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: 160.32 E-value: 1.94e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1216630836 47 HIEVDITYAEYFEMSVRLAEAMKRYGLNTNHRIVVCSENSLQFFMPVLGALFIGVAVAPANDIYNERELLNSMGISQPTV 126
Cdd:cd05919 6 AADRSVTYGQLHDGANRLGSALRNLGVSSGDRVLLLMLDSPELVQLFLGCLARGAIAVVINPLLHPDDYAYIARDCEARL 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1216630836 127 VFVSkkglqkilnvqkklpiiqkiiimdsktdyqgfqsmytfvtshlppgfneydfvpesfdrDKTIALIMNSSGSTGLP 206
Cdd:cd05919 86 VVTS-----------------------------------------------------------ADDIAYLLYSSGTTGPP 106
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1216630836 207 KGVALPHR---TACVRFSHardPIFGnqIIPDTAILSVVPFHHGFGMFTTL-GYLICGFRVVLM--YRFEEELFLRSLQd 280
Cdd:cd05919 107 KGVMHAHRdplLFADAMAR---EALG--LTPGDRVFSSAKMFFGYGLGNSLwFPLAVGASAVLNpgWPTAERVLATLAR- 180
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1216630836 281 YKIQSALLVPTLFSFFAKSTLIDKYDLSNLHEIASGGAPLSKEVGEAVAKRFHLPgIRQGYGLTETTSAILITPEGDDKP 360
Cdd:cd05919 181 FRPTVLYGVPTFYANLLDSCAGSPDALRSLRLCVSAGEALPRGLGERWMEHFGGP-ILDGIGATEVGHIFLSNRPGAWRL 259
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1216630836 361 GAVGKVVPFFEAKVVDlDTGKTLGVNQRGELCVRGPMIMSGYVNNPEATNALIdKDGWLHSGDIAYWDEDEHFFIVDRLK 440
Cdd:cd05919 260 GSTGRPVPGYEIRLVD-EEGHTIPPGEEGDLLVRGPSAAVGYWNNPEKSRATF-NGGWYRTGDKFCRDADGWYTHAGRAD 337
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1216630836 441 SLIKYKGYQVAPAELESILLQHPNIFDAGVAGLPDDDAGELPAAVVVLEHGKTMTEK---EIVDYVASQVtTAKKLRGGV 517
Cdd:cd05919 338 DMLKVGGQWVSPVEVESLIIQHPAVAEAAVVAVPESTGLSRLTAFVVLKSPAAPQESlarDIHRHLLERL-SAHKVPRRI 416
|
490 500
....*....|....*....|
gi 1216630836 518 VFVDEVPKGLTGKLDARKIR 537
Cdd:cd05919 417 AFVDELPRTATGKLQRFKLR 436
|
|
| PtmA |
cd17636 |
long-chain fatty acid CoA ligase (FadD); This family contains fatty acid CoA ligases, ... |
195-532 |
1.10e-42 |
|
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: 155.54 E-value: 1.10e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1216630836 195 LIMNSSGSTGLPKGVALPHRTAcvrFSHARDPIFGNQIIPDTAILSVVP-FHHGFgMFTTLGYLICGFRVVLMYRFEEEL 273
Cdd:cd17636 4 LAIYTAAFSGRPNGALLSHQAL---LAQALVLAVLQAIDEGTVFLNSGPlFHIGT-LMFTLATFHAGGTNVFVRRVDAEE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1216630836 274 FLRSLQDYKIQSALLVPTLFSFFAKSTLIDKYDLSNLHeiASGGAPLSKEVGEAVAKRF-HLPGirqGYGLTETTSAILI 352
Cdd:cd17636 80 VLELIEAERCTHAFLLPPTIDQIVELNADGLYDLSSLR--SSPAAPEWNDMATVDTSPWgRKPG---GYGQTEVMGLATF 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1216630836 353 TPEGDDKPGAVGKVVPFFEAKVVDLDtGKTLGVNQRGELCVRGPMIMSGYVNNPEaTNALIDKDGWLHSGDIAYWDEDEH 432
Cdd:cd17636 155 AALGGGAIGGAGRPSPLVQVRILDED-GREVPDGEVGEIVARGPTVMAGYWNRPE-VNARRTRGGWHHTNDLGRREPDGS 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1216630836 433 FFIVDRLKSLIKYKGYQVAPAELESILLQHPNIFDAGVAGLPDDDAGELPAAVVVLEHGKTMTEKEIVDYVASQVTTAKK 512
Cdd:cd17636 233 LSFVGPKTRMIKSGAENIYPAEVERCLRQHPAVADAAVIGVPDPRWAQSVKAIVVLKPGASVTEAELIEHCRARIASYKK 312
|
330 340
....*....|....*....|
gi 1216630836 513 LRgGVVFVDEVPKGLTGKLD 532
Cdd:cd17636 313 PK-SVEFADALPRTAGGADD 331
|
|
| LC_FACL_like |
cd05914 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); The members of this family are ... |
47-531 |
1.86e-42 |
|
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: 157.99 E-value: 1.86e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1216630836 47 HIEVDITYAEYFEMSVRLAEAMKRYGLNTNHRIVVCSENSLQFFMPVLGALFIGVAVAPANDIYNERELLNSMGISQPTV 126
Cdd:cd05914 3 YGGEPLTYKDLADNIAKFALLLKINGVGTGDRVALMGENRPEWGIAFFAIWTYGAIAVPILAEFTADEVHHILNHSEAKA 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1216630836 127 VFVSkkglqkilnvqkklpiiqkiiimdsktdyqgfqsmytfvtshlppgfneydfvpesfDRDKTiALIMNSSGSTGLP 206
Cdd:cd05914 83 IFVS---------------------------------------------------------DEDDV-ALINYTSGTTGNS 104
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1216630836 207 KGVALPHRT--ACVRFSHARDPifgnqIIPDTAILSVVPFHHGFGMFTTLGY-LICGFRVVLMYRFEEELfLRSLQDYKI 283
Cdd:cd05914 105 KGVMLTYRNivSNVDGVKEVVL-----LGKGDKILSILPLHHIYPLTFTLLLpLLNGAHVVFLDKIPSAK-IIALAFAQV 178
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1216630836 284 QSALLVPTLFSFF--AKSTLIDKYDLS-----------------------------NLHEIASGGAPLSKEVgEAVAKRF 332
Cdd:cd05914 179 TPTLGVPVPLVIEkiFKMDIIPKLTLKkfkfklakkinnrkirklafkkvheafggNIKEFVIGGAKINPDV-EEFLRTI 257
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1216630836 333 HLPGIrQGYGLTETTSAILITPEGDDKPGAVGKVVPFFEAKVVDLDTGktlgvNQRGELCVRGPMIMSGYVNNPEATNAL 412
Cdd:cd05914 258 GFPYT-IGYGMTETAPIISYSPPNRIRLGSAGKVIDGVEVRIDSPDPA-----TGEGEIIVRGPNVMKGYYKNPEATAEA 331
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1216630836 413 IDKDGWLHSGDIAYWDEDEHFFIVDRLKSLI-KYKGYQVAPAELESILLQHPNIFDAGVaGLPDDDAGEL----PAAVVV 487
Cdd:cd05914 332 FDKDGWFHTGDLGKIDAEGYLYIRGRKKEMIvLSSGKNIYPEEIEAKINNMPFVLESLV-VVQEKKLVALayidPDFLDV 410
|
490 500 510 520
....*....|....*....|....*....|....*....|....*...
gi 1216630836 488 LEHGKTMTEK----EIVDYVASQVTTAKKLRGGVVFVDEVPKGLTGKL 531
Cdd:cd05914 411 KALKQRNIIDaikwEVRDKVNQKVPNYKKISKVKIVKEEFEKTPKGKI 458
|
|
| PLN02860 |
PLN02860 |
o-succinylbenzoate-CoA ligase |
53-514 |
3.44e-42 |
|
o-succinylbenzoate-CoA ligase
Pssm-ID: 215464 [Multi-domain] Cd Length: 563 Bit Score: 159.19 E-value: 3.44e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1216630836 53 TYAEYFEMSVRLAEAMKRYGLNTNHRIVVCSENSLQFFMPVLGALFIGVAVAPANDIYNERELLNSMGISQPtVVFVSKK 132
Cdd:PLN02860 34 TGHEFVDGVLSLAAGLLRLGLRNGDVVAIAALNSDLYLEWLLAVACAGGIVAPLNYRWSFEEAKSAMLLVRP-VMLVTDE 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1216630836 133 GLQK--ILNVQKKLPIIQKIIIMDSKTDYQGFQSMYTFVTSHL------PPGFNeYDFVPESfdrdktIALIMNSSGSTG 204
Cdd:PLN02860 113 TCSSwyEELQNDRLPSLMWQVFLESPSSSVFIFLNSFLTTEMLkqralgTTELD-YAWAPDD------AVLICFTSGTTG 185
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1216630836 205 LPKGVALPHRtACVRFSHARDPIFGNQiiPDTAILSVVPFHHGFGMFTTLGYLICGFRVVLMYRFEEELFLRSLQDYKIQ 284
Cdd:PLN02860 186 RPKGVTISHS-ALIVQSLAKIAIVGYG--EDDVYLHTAPLCHIGGLSSALAMLMVGACHVLLPKFDAKAALQAIKQHNVT 262
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1216630836 285 SALLVPTLFS---FFAKSTLIDKYDLSnLHEIASGGAPLSKEVGEAVAKRFHLPGIRQGYGLTET--------------- 346
Cdd:PLN02860 263 SMITVPAMMAdliSLTRKSMTWKVFPS-VRKILNGGGSLSSRLLPDAKKLFPNAKLFSAYGMTEAcssltfmtlhdptle 341
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1216630836 347 TSAILITPEGDDKPGA--------VGKVVPFFEAKVVDLDTGKTlgvnqrGELCVRGPMIMSGYVNNPEATNALIDKDGW 418
Cdd:PLN02860 342 SPKQTLQTVNQTKSSSvhqpqgvcVGKPAPHVELKIGLDESSRV------GRILTRGPHVMLGYWGQNSETASVLSNDGW 415
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1216630836 419 LHSGDIAYWDEDEHFFIVDRLKSLIKYKGYQVAPAELESILLQHPNIFDAGVAGLPDDDAGELPAAVVVLEHGKTMTEKE 498
Cdd:PLN02860 416 LDTGDIGWIDKAGNLWLIGRSNDRIKTGGENVYPEEVEAVLSQHPGVASVVVVGVPDSRLTEMVVACVRLRDGWIWSDNE 495
|
490
....*....|....*.
gi 1216630836 499 IVDYVASQVTTAKKLR 514
Cdd:PLN02860 496 KENAKKNLTLSSETLR 511
|
|
| CBAL |
cd05923 |
4-Chlorobenzoate-CoA ligase (CBAL); CBAL catalyzes the conversion of 4-chlorobenzoate (4-CB) ... |
22-534 |
3.92e-42 |
|
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: 157.67 E-value: 3.92e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1216630836 22 TAGEQLHKAMKRyalVPGTIAFTDAHIEVDITYAEYFEMSVRLAEAMKRYGLNTNHRIVVCSENSLQFFMPVLGALFIGV 101
Cdd:cd05923 2 TVFEMLRRAASR---APDACAIADPARGLRLTYSELRARIEAVAARLHARGLRPGQRVAVVLPNSVEAVIALLALHRLGA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1216630836 102 AVAPANDIYNEREL--LNSMGISQPTVVFVSKKGLQKIlnvqkklpiIQKIIIMDSKTDYQGFQSMYTFVTSHLPPGfne 179
Cdd:cd05923 79 VPALINPRLKAAELaeLIERGEMTAAVIAVDAQVMDAI---------FQSGVRVLALSDLVGLGEPESAGPLIEDPP--- 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1216630836 180 ydfvpesfDRDKTIALIMNSSGSTGLPKGVALPHRTACVR---FSHARDPIFGNQiipdTAILSVVPFHHGFGMFTTL-G 255
Cdd:cd05923 147 --------REPEQPAFVFYTSGTTGLPKGAVIPQRAAESRvlfMSTQAGLRHGRH----NVVLGLMPLYHVIGFFAVLvA 214
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1216630836 256 YLICGFRVVLMYRFEEELFLRSLQDYKIQSALLVPTLFSFFAKSTLIDKYDLSNLHEIASGGAPLSKEVGEAVAKrfHLP 335
Cdd:cd05923 215 ALALDGTYVVVEEFDPADALKLIEQERVTSLFATPTHLDALAAAAEFAGLKLSSLRHVTFAGATMPDAVLERVNQ--HLP 292
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1216630836 336 GIRQG-YGLTETTSAiLITPegDDKPGAVGKVVPFFEAKVVDLDTG--KTLGVNQRGELCVR--GPMIMSGYVNNPEATN 410
Cdd:cd05923 293 GEKVNiYGTTEAMNS-LYMR--DARTGTEMRPGFFSEVRIVRIGGSpdEALANGEEGELIVAaaADAAFTGYLNQPEATA 369
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1216630836 411 ALIdKDGWLHSGDIAYWDEDEHFFIVDRLKSLIKYKGYQVAPAELESILLQHPNIFDAGVAGLPDDDAGELPAAVVVLEH 490
Cdd:cd05923 370 KKL-QDGWYRTGDVGYVDPSGDVRILGRVDDMIISGGENIHPSEIERVLSRHPGVTEVVVIGVADERWGQSVTACVVPRE 448
|
490 500 510 520
....*....|....*....|....*....|....*....|....*
gi 1216630836 491 GkTMTEKEIVDY-VASQVTTAKKLRgGVVFVDEVPKGLTGKLDAR 534
Cdd:cd05923 449 G-TLSADELDQFcRASELADFKRPR-RYFFLDELPKNAMNKVLRR 491
|
|
| caiC |
PRK08008 |
putative crotonobetaine/carnitine-CoA ligase; Validated |
53-537 |
4.51e-42 |
|
putative crotonobetaine/carnitine-CoA ligase; Validated
Pssm-ID: 181195 [Multi-domain] Cd Length: 517 Bit Score: 157.92 E-value: 4.51e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1216630836 53 TYAEYFEMSVRLAEAMKRYGLNTNHRIVVCSENSLQFFMPVLGALFIGVAVAPANDIYNERELLNSMGISQPTVVFVSKK 132
Cdd:PRK08008 39 SYLELNEEINRTANLFYSLGIRKGDKVALHLDNCPEFIFCWFGLAKIGAIMVPINARLLREESAWILQNSQASLLVTSAQ 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1216630836 133 GLQKILNVQKKLPI-IQKIIIMDSKTDYQGFQSMYTFVTSHLPPGFNEYdfVPESFDrdkTIALIMNSSGSTGLPKGVAL 211
Cdd:PRK08008 119 FYPMYRQIQQEDATpLRHICLTRVALPADDGVSSFTQLKAQQPATLCYA--PPLSTD---DTAEILFTSGTTSRPKGVVI 193
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1216630836 212 PHrtACVRFSHardpIFG---NQIIPDTAILSVVP-FHHGFGMFTTLGYLICGFRVVLMYRFEEELFLRSLQDYK----- 282
Cdd:PRK08008 194 TH--YNLRFAG----YYSawqCALRDDDVYLTVMPaFHIDCQCTAAMAAFSAGATFVLLEKYSARAFWGQVCKYRatite 267
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1216630836 283 -----IQSALLVPTL----------FSFFakstlidkydlsnLHeiasggapLSKEVGEAVAKRFhlpGIR--QGYGLTE 345
Cdd:PRK08008 268 cipmmIRTLMVQPPSandrqhclreVMFY-------------LN--------LSDQEKDAFEERF---GVRllTSYGMTE 323
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1216630836 346 TTSAILITPEGDDK--PgAVGKVVPFFEAKVVDlDTGKTLGVNQRGELCVRG---PMIMSGYVNNPEATNALIDKDGWLH 420
Cdd:PRK08008 324 TIVGIIGDRPGDKRrwP-SIGRPGFCYEAEIRD-DHNRPLPAGEIGEICIKGvpgKTIFKEYYLDPKATAKVLEADGWLH 401
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1216630836 421 SGDIAYWDEDEHFFIVDRLKSLIKYKGYQVAPAELESILLQHPNIFDAGVAGLPDDDAGELPAAVVVLEHGKTMTEKEIV 500
Cdd:PRK08008 402 TGDTGYVDEEGFFYFVDRRCNMIKRGGENVSCVELENIIATHPKIQDIVVVGIKDSIRDEAIKAFVVLNEGETLSEEEFF 481
|
490 500 510
....*....|....*....|....*....|....*...
gi 1216630836 501 DYVASQVttAK-KLRGGVVFVDEVPKGLTGKLDARKIR 537
Cdd:PRK08008 482 AFCEQNM--AKfKVPSYLEIRKDLPRNCSGKIIKKNLK 517
|
|
| PRK07798 |
PRK07798 |
acyl-CoA synthetase; Validated |
52-539 |
4.23e-41 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236100 [Multi-domain] Cd Length: 533 Bit Score: 155.43 E-value: 4.23e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1216630836 52 ITYAEYFEMSVRLAEAMKRYGLNTNHRIVVCSENSLQFFMPVLGALFIGVAVAPANDIYNERELLNSMGISQPTVVFVSK 131
Cdd:PRK07798 29 LTYAELEERANRLAHYLIAQGLGPGDHVGIYARNRIEYVEAMLGAFKARAVPVNVNYRYVEDELRYLLDDSDAVALVYER 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1216630836 132 KGLQKILNVQKKLPIIQKIIIMDSKTDYQGFQ---SMYTFVTShlppGFNEYDFVPESFDrDktiALIMNSSGSTGLPKG 208
Cdd:PRK07798 109 EFAPRVAEVLPRLPKLRTLVVVEDGSGNDLLPgavDYEDALAA----GSPERDFGERSPD-D---LYLLYTGGTTGMPKG 180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1216630836 209 VALphRTACVRFSH--ARDPIFGNQI------------IPDTAILSVVPFHHGFGMFTTLGYLICGFRVVL--MYRFEEE 272
Cdd:PRK07798 181 VMW--RQEDIFRVLlgGRDFATGEPIedeeelakraaaGPGMRRFPAPPLMHGAGQWAAFAALFSGQTVVLlpDVRFDAD 258
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1216630836 273 LFLRSLQDYKIQSALLVPTLFsffAKStLID------KYDLSNLHEIASGGAPLSKEVGEAVAKrfHLPG--IRQGYGLT 344
Cdd:PRK07798 259 EVWRTIEREKVNVITIVGDAM---ARP-LLDaleargPYDLSSLFAIASGGALFSPSVKEALLE--LLPNvvLTDSIGSS 332
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1216630836 345 ETTSAILITPegddKPGAVGKVVPFFEA----KVVDLDTGKTL-GVNQRGELCVRGPmIMSGYVNNPEATNAL---IDKD 416
Cdd:PRK07798 333 ETGFGGSGTV----AKGAVHTGGPRFTIgprtVVLDEDGNPVEpGSGEIGWIARRGH-IPLGYYKDPEKTAETfptIDGV 407
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1216630836 417 GWLHSGDIAYWDEDEHFFIVDRLKSLIKYKGYQVAPAELESILLQHPNIFDAGVAGLPDDDAGELPAAVVVLEHGKTMTE 496
Cdd:PRK07798 408 RYAIPGDRARVEADGTITLLGRGSVCINTGGEKVFPEEVEEALKAHPDVADALVVGVPDERWGQEVVAVVQLREGARPDL 487
|
490 500 510 520
....*....|....*....|....*....|....*....|...
gi 1216630836 497 KEIVDYVASQVTTAKKLRgGVVFVDEVPKGLTGKLDARKIREI 539
Cdd:PRK07798 488 AELRAHCRSSLAGYKVPR-AIWFVDEVQRSPAGKADYRWAKEQ 529
|
|
| A_NRPS |
cd05930 |
The adenylation domain of nonribosomal peptide synthetases (NRPS); The adenylation (A) domain ... |
194-535 |
1.69e-40 |
|
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: 152.30 E-value: 1.69e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1216630836 194 ALIMNSSGSTGLPKGVALPHRTACVRFSHARDPIfgnQIIPDTAILSVVPFHHGFGMFTTLGYLICGFRVVLM---YRFE 270
Cdd:cd05930 96 AYVIYTSGSTGKPKGVMVEHRGLVNLLLWMQEAY---PLTPGDRVLQFTSFSFDVSVWEIFGALLAGATLVVLpeeVRKD 172
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1216630836 271 EELFLRSLQDYKIQSALLVPTLFSFFAKStlIDKYDLSNLHEIASGGAPLSKEVGEAVAKRFHLPGIRQGYGLTETTsaI 350
Cdd:cd05930 173 PEALADLLAEEGITVLHLTPSLLRLLLQE--LELAALPSLRLVLVGGEALPPDLVRRWRELLPGARLVNLYGPTEAT--V 248
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1216630836 351 LIT----PEGDDKPGAV--GKVVPFFEAKVVDlDTGKTLGVNQRGELCVRGPMIMSGYVNNPEATNALIDKD-----GWL 419
Cdd:cd05930 249 DATyyrvPPDDEEDGRVpiGRPIPNTRVYVLD-ENLRPVPPGVPGELYIGGAGLARGYLNRPELTAERFVPNpfgpgERM 327
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1216630836 420 H-SGDIAYWDEDEHFFIVDRLKSLIKYKGYQVAPAELESILLQHPNIFDAGVAGLPDDDAGELPAAVVVLEHGKTMTEKE 498
Cdd:cd05930 328 YrTGDLVRWLPDGNLEFLGRIDDQVKIRGYRIELGEIEAALLAHPGVREAAVVAREDGDGEKRLVAYVVPDEGGELDEEE 407
|
330 340 350 360
....*....|....*....|....*....|....*....|..
gi 1216630836 499 IVDYVASQ-----VTTAkklrggVVFVDEVPKGLTGKLDARK 535
Cdd:cd05930 408 LRAHLAERlpdymVPSA------FVVLDALPLTPNGKVDRKA 443
|
|
| PRK06164 |
PRK06164 |
acyl-CoA synthetase; Validated |
11-538 |
2.62e-40 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 235722 [Multi-domain] Cd Length: 540 Bit Score: 153.36 E-value: 2.62e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1216630836 11 GPAPFYPLEDGTAGEQlhkamkryalvPGTIAFTDAhiEVDITYAEYFEMSVRLAEAMKRYGLNTNHRIVV----CSEN- 85
Cdd:PRK06164 8 RADTLASLLDAHARAR-----------PDAVALIDE--DRPLSRAELRALVDRLAAWLAAQGVRRGDRVAVwlpnCIEWv 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1216630836 86 SLQFFMPVLGALFIGVavapaNDIYNERELLNSMGISQPTVVFV--SKKGLQ--KILN-VQKK-LPIIQKIIIMDSKTDY 159
Cdd:PRK06164 75 VLFLACARLGATVIAV-----NTRYRSHEVAHILGRGRARWLVVwpGFKGIDfaAILAaVPPDaLPPLRAIAVVDDAADA 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1216630836 160 QgfqSMYTFVTSHLPPGFNEYDFVP---ESFDRDKTIALIMNSSGSTGLPKGVALPHRTAcVRFSHARDPIFGnqIIPDT 236
Cdd:PRK06164 150 T---PAPAPGARVQLFALPDPAPPAaagERAADPDAGALLFTTSGTTSGPKLVLHRQATL-LRHARAIARAYG--YDPGA 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1216630836 237 AILSVVPFHHGFGMFTTLGYLICGFRVVLMYRFEEELFLRSLQDYKIQSALLVPTLFSFFAKSTLIDKyDLSNLHE--IA 314
Cdd:PRK06164 224 VLLAALPFCGVFGFSTLLGALAGGAPLVCEPVFDAARTARALRRHRVTHTFGNDEMLRRILDTAGERA-DFPSARLfgFA 302
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1216630836 315 SGGAPLSKEVGEAVAKRFHLPGIrqgYGLTETTSAILITPEGDD-----KPGAVgKVVPFFEAKVVDLDTGKTLGVNQRG 389
Cdd:PRK06164 303 SFAPALGELAALARARGVPLTGL---YGSSEVQALVALQPATDPvsvriEGGGR-PASPEARVRARDPQDGALLPDGESG 378
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1216630836 390 ELCVRGPMIMSGYVNNPEATNALIDKDGWLHSGDIAYWDEDEHFFIVDRLKSLIKYKGYQVAPAELESILLQHPNIFDAG 469
Cdd:PRK06164 379 EIEIRAPSLMRGYLDNPDATARALTDDGYFRTGDLGYTRGDGQFVYQTRMGDSLRLGGFLVNPAEIEHALEALPGVAAAQ 458
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1216630836 470 VAGLpDDDAGELPAAVVVLEHGKTMTEKEIVDYVASQVtTAKKLRGGVVFVDEVPKGLTG---KLDARKIRE 538
Cdd:PRK06164 459 VVGA-TRDGKTVPVAFVIPTDGASPDEAGLMAACREAL-AGFKVPARVQVVEAFPVTESAngaKIQKHRLRE 528
|
|
| PRK09088 |
PRK09088 |
acyl-CoA synthetase; Validated |
36-540 |
2.87e-40 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 181644 [Multi-domain] Cd Length: 488 Bit Score: 152.65 E-value: 2.87e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1216630836 36 LVPGTIAFTDAHIEVDITYAEYFEMSVRLAEAMKRYGLNTNHRIVVCSENS-----LQFFMPVLGALFIgvavaPANDIY 110
Cdd:PRK09088 7 LQPQRLAAVDLALGRRWTYAELDALVGRLAAVLRRRGCVDGERLAVLARNSvwlvaLHFACARVGAIYV-----PLNWRL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1216630836 111 NERELLNSMGISQPTVVfVSKKGLQkilnvqkklpiiqkiiimDSKTDYQGFQSMYTFVTSHLPpgfneyDFVPeSFDRD 190
Cdd:PRK09088 82 SASELDALLQDAEPRLL-LGDDAVA------------------AGRTDVEDLAAFIASADALEP------ADTP-SIPPE 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1216630836 191 KtIALIMNSSGSTGLPKGVALPHRTAcvrfshardpifgNQIIPDTAILSVVPFHHGF----GMFTTLGyLICGFRVVLM 266
Cdd:PRK09088 136 R-VSLILFTSGTSGQPKGVMLSERNL-------------QQTAHNFGVLGRVDAHSSFlcdaPMFHIIG-LITSVRPVLA 200
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1216630836 267 YR--------FEEELFLRSLQD--YKIQSALLVPTLFSFFAKSTLIDKYDLSNLHEIASGGAP-LSKEVGEAVAKrfhlp 335
Cdd:PRK09088 201 VGgsilvsngFEPKRTLGRLGDpaLGITHYFCVPQMAQAFRAQPGFDAAALRHLTALFTGGAPhAAEDILGWLDD----- 275
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1216630836 336 GIRQ--GYGLTETTSAILITPEG---DDKPGAVGKVVPFFEAKVVDlDTGKTLGVNQRGELCVRGPMIMSGYVNNPEATN 410
Cdd:PRK09088 276 GIPMvdGFGMSEAGTVFGMSVDCdviRAKAGAAGIPTPTVQTRVVD-DQGNDCPAGVPGELLLRGPNLSPGYWRRPQATA 354
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1216630836 411 ALIDKDGWLHSGDIAYWDEDEHFFIVDRLKSLIKYKGYQVAPAELESILLQHPNIFDAGVAGLPDDDAGELPAAVVVLEH 490
Cdd:PRK09088 355 RAFTGDGWFRTGDIARRDADGFFWVVDRKKDMFISGGENVYPAEIEAVLADHPGIRECAVVGMADAQWGEVGYLAIVPAD 434
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|.
gi 1216630836 491 GKTMTEKEIVDYVASQVttAK-KLRGGVVFVDEVPKGLTGKLDARKIREIL 540
Cdd:PRK09088 435 GAPLDLERIRSHLSTRL--AKyKVPKHLRLVDALPRTASGKLQKARLRDAL 483
|
|
| OSB_MenE-like |
cd17630 |
O-succinylbenzoic acid-CoA ligase; This family contains O-succinylbenzoyl-CoA (OSB-CoA) ... |
193-540 |
5.57e-40 |
|
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: 147.86 E-value: 5.57e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1216630836 193 IALIMNSSGSTGLPKGVALPHR--TACVRFSHARDPIFGnqiiPDTAILSVVPFHHGfGMFTTLGYLICGFRVVLMYRfe 270
Cdd:cd17630 2 LATVILTSGSTGTPKAVVHTAAnlLASAAGLHSRLGFGG----GDSWLLSLPLYHVG-GLAILVRSLLAGAELVLLER-- 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1216630836 271 EELFLRSLQDYKIQSALLVPT-LFSFFAKSTLIDkyDLSNLHEIASGGAPLSKEVGEAVAKRfHLPGIrQGYGLTETTSA 349
Cdd:cd17630 75 NQALAEDLAPPGVTHVSLVPTqLQRLLDSGQGPA--ALKSLRAVLLGGAPIPPELLERAADR-GIPLY-TTYGMTETASQ 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1216630836 350 ILITPEGDDKPGAVGKVVPFFEAKVVDldtgktlgvnqRGELCVRGPMIMSGYVNNPEATnaLIDKDGWLHSGDIAYWDE 429
Cdd:cd17630 151 VATKRPDGFGRGGVGVLLPGRELRIVE-----------DGEIWVGGASLAMGYLRGQLVP--EFNEDGWFTTKDLGELHA 217
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1216630836 430 DEHFFIVDRLKSLIKYKGYQVAPAELESILLQHPNIFDAGVAGLPDDDAGELPAAVVVLEHGKtmTEKEIVDYVASQVTT 509
Cdd:cd17630 218 DGRLTVLGRADNMIISGGENIQPEEIEAALAAHPAVRDAFVVGVPDEELGQRPVAVIVGRGPA--DPAELRAWLKDKLAR 295
|
330 340 350
....*....|....*....|....*....|.
gi 1216630836 510 AKKLRgGVVFVDEVPKGLTGKLDARKIREIL 540
Cdd:cd17630 296 FKLPK-RIYPVPELPRTGGGKVDRRALRAWL 325
|
|
| MACS_euk |
cd05928 |
Eukaryotic Medium-chain acyl-CoA synthetase (MACS or ACSM); MACS catalyzes the two-step ... |
196-538 |
1.55e-39 |
|
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: 151.08 E-value: 1.55e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1216630836 196 IMNSSGSTGLPKGVALPHR------TACVRFSHARDP--IFGNqiIPDT-----AILSVV-PFHHGFGMFttlgylicgf 261
Cdd:cd05928 179 IYFTSGTTGSPKMAEHSHSslglglKVNGRYWLDLTAsdIMWN--TSDTgwiksAWSSLFePWIQGACVF---------- 246
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1216630836 262 rVVLMYRFEEELFLRSLQDYKIQSALLVPTLFSFFAKSTLiDKYDLSNLHEIASGGAPLSKEVGEAVAKRFHLPgIRQGY 341
Cdd:cd05928 247 -VHHLPRFDPLVILKTLSSYPITTFCGAPTVYRMLVQQDL-SSYKFPSLQHCVTGGEPLNPEVLEKWKAQTGLD-IYEGY 323
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1216630836 342 GLTETTsAILITPEGDD-KPGAVGKVVPFFEAKVVDlDTGKTLGVNQRGELCVR-GPM----IMSGYVNNPEATNALIDK 415
Cdd:cd05928 324 GQTETG-LICANFKGMKiKPGSMGKASPPYDVQIID-DNGNVLPPGTEGDIGIRvKPIrpfgLFSGYVDNPEKTAATIRG 401
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1216630836 416 DGWLhSGDIAYWDEDEHFFIVDRLKSLIKYKGYQVAPAELESILLQHPNIFDAGVAGLPDDDAGELPAAVVVL-----EH 490
Cdd:cd05928 402 DFYL-TGDRGIMDEDGYFWFMGRADDVINSSGYRIGPFEVESALIEHPAVVESAVVSSPDPIRGEVVKAFVVLapqflSH 480
|
330 340 350 360
....*....|....*....|....*....|....*....|....*...
gi 1216630836 491 GKTMTEKEIVDYVASqVTTAKKLRGGVVFVDEVPKGLTGKLDARKIRE 538
Cdd:cd05928 481 DPEQLTKELQQHVKS-VTAPYKYPRKVEFVQELPKTVTGKIQRNELRD 527
|
|
| AFD_YhfT-like |
cd17633 |
fatty acid-CoA ligase VraA; This family of acyl-CoA ligases includes Bacillus subtilis YhfT, ... |
199-532 |
2.26e-39 |
|
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: 146.01 E-value: 2.26e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1216630836 199 SSGSTGLPKGVALPHRTACVRFSHARDpIFgnQIIPDTAILSVVPFHHGFGMFTTLGYLICGFRVVLMYRFEEELFLRSL 278
Cdd:cd17633 8 TSGTTGLPKAYYRSERSWIESFVCNED-LF--NISGEDAILAPGPLSHSLFLYGAISALYLGGTFIGQRKFNPKSWIRKI 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1216630836 279 QDYKIQSALLVPTLFSFFAKSTLIDkydlSNLHEIASGGAPLSKEVGEAVAKRFHLPGIRQGYGLTETTSAILITPEGDD 358
Cdd:cd17633 85 NQYNATVIYLVPTMLQALARTLEPE----SKIKSIFSSGQKLFESTKKKLKNIFPKANLIEFYGTSELSFITYNFNQESR 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1216630836 359 KPGAVGKVVPFFEAKVVDLDTGKTlgvnqrGELCVRGPMIMSGYVNNPEatnalIDKDGWLHSGDIAYWDEDEHFFIVDR 438
Cdd:cd17633 161 PPNSVGRPFPNVEIEIRNADGGEI------GKIFVKSEMVFSGYVRGGF-----SNPDGWMSVGDIGYVDEEGYLYLVGR 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1216630836 439 LKSLIKYKGYQVAPAELESILLQHPNIFDAGVAGLPDDDAGELPAAVVVlehGKTMTEKEIVDYVASQVTTAKKLRgGVV 518
Cdd:cd17633 230 ESDMIIIGGINIFPTEIESVLKAIPGIEEAIVVGIPDARFGEIAVALYS---GDKLTYKQLKRFLKQKLSRYEIPK-KII 305
|
330
....*....|....
gi 1216630836 519 FVDEVPKGLTGKLD 532
Cdd:cd17633 306 FVDSLPYTSSGKIA 319
|
|
| LC-FACS_euk |
cd05927 |
Eukaryotic long-chain fatty acid CoA synthetase (LC-FACS); The members of this family are ... |
52-463 |
4.44e-39 |
|
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: 150.06 E-value: 4.44e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1216630836 52 ITYAEYFEMSVRLAEAMKRYGLNT--NHRIVVCSENSLQFFMPVLGALFIGVAVAPandiynereLLNSMGISqpTVVFV 129
Cdd:cd05927 6 ISYKEVAERADNIGSALRSLGGKPapASFVGIYSINRPEWIISELACYAYSLVTVP---------LYDTLGPE--AIEYI 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1216630836 130 SKKGLQKILNVQKKLPIIQKIIIMDsktdyQGFQsmytfvtshlppgfNEYDFVPESFDrdkTIALIMNSSGSTGLPKGV 209
Cdd:cd05927 75 LNHAEISIVFCDAGVKVYSLEEFEK-----LGKK--------------NKVPPPPPKPE---DLATICYTSGTTGNPKGV 132
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1216630836 210 ALPHR---TACVRFSHArdPIFGNQIIPDTAILSVVPFHHGFGMFTTLGYLICGFRVVLmYRFEEELFLRSLQDYKIQSA 286
Cdd:cd05927 133 MLTHGnivSNVAGVFKI--LEILNKINPTDVYISYLPLAHIFERVVEALFLYHGAKIGF-YSGDIRLLLDDIKALKPTVF 209
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1216630836 287 LLVPTLF--------------SFFAK---------------------STLIDKYDLS--------NLHEIASGGAPLSKE 323
Cdd:cd05927 210 PGVPRVLnriydkifnkvqakGPLKRklfnfalnyklaelrsgvvraSPFWDKLVFNkikqalggNVRLMLTGSAPLSPE 289
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1216630836 324 VGEAVAKRFHLPgIRQGYGLTETTSAILITPEGDDKPGAVGKVVPFFEAKVVDL-DTGKT-LGVNQRGELCVRGPMIMSG 401
Cdd:cd05927 290 VLEFLRVALGCP-VLEGYGQTECTAGATLTLPGDTSVGHVGGPLPCAEVKLVDVpEMNYDaKDPNPRGEVCIRGPNVFSG 368
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1216630836 402 YVNNPEATNALIDKDGWLHSGDIAYWDEDEHFFIVDRLKSLIKY-KGYQVAPAELESILLQHP 463
Cdd:cd05927 369 YYKDPEKTAEALDEDGWLHTGDIGEWLPNGTLKIIDRKKNIFKLsQGEYVAPEKIENIYARSP 431
|
|
| DltA |
cd05945 |
D-alanine:D-alanyl carrier protein ligase (DltA) and similar proteins; This family includes ... |
52-536 |
3.55e-38 |
|
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: 145.85 E-value: 3.55e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1216630836 52 ITYAEYFEMSVRLAEAMKRYGLNTNHRIVVCSENSLQFFMPVLGALFIGVAVAPANDIYNERELLNSMGISQPTVVFVSK 131
Cdd:cd05945 17 LTYRELKERADALAAALASLGLDAGDPVVVYGHKSPDAIAAFLAALKAGHAYVPLDASSPAERIREILDAAKPALLIADG 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1216630836 132 KGLqkilnvqkklpiiqkiiimdsktdyqgfqsmytfvtshlppgfneydfvpesfdrdktiALIMNSSGSTGLPKGVAL 211
Cdd:cd05945 97 DDN-----------------------------------------------------------AYIIFTSGSTGRPKGVQI 117
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1216630836 212 PHRtACVRFSHARDPIFgnQIIPDTAILSVVPFHHGFGMFTTLGYLICGFRVVL----MYRFEEELFlRSLQDYKIQSAL 287
Cdd:cd05945 118 SHD-NLVSFTNWMLSDF--PLGPGDVFLNQAPFSFDLSVMDLYPALASGATLVPvprdATADPKQLF-RFLAEHGITVWV 193
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1216630836 288 LVPTLFSFFAKSTLIDKYDLSNLHEIASGGAPLSKEVGEAVAKRFHLPGIRQGYGLTETT---SAILITPE--GDDKPGA 362
Cdd:cd05945 194 STPSFAAMCLLSPTFTPESLPSLRHFLFCGEVLPHKTARALQQRFPDARIYNTYGPTEATvavTYIEVTPEvlDGYDRLP 273
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1216630836 363 VGKVVPFFEAKVVDlDTGKTLGVNQRGELCVRGPMIMSGYVNNPEATNA---LIDKDGWLHSGDIAYWDEDEHFFIVDRL 439
Cdd:cd05945 274 IGYAKPGAKLVILD-EDGRPVPPGEKGELVISGPSVSKGYLNNPEKTAAaffPDEGQRAYRTGDLVRLEADGLLFYRGRL 352
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1216630836 440 KSLIKYKGYQVAPAELESILLQHPNIFDAGVAGLPDDDAGELPAAVVVLEHG----KTMTEKE-----IVDYVASQvtta 510
Cdd:cd05945 353 DFQVKLNGYRIELEEIEAALRQVPGVKEAVVVPKYKGEKVTELIAFVVPKPGaeagLTKAIKAelaerLPPYMIPR---- 428
|
490 500
....*....|....*....|....*.
gi 1216630836 511 kklrgGVVFVDEVPKGLTGKLDARKI 536
Cdd:cd05945 429 -----RFVYLDELPLNANGKIDRKAL 449
|
|
| FADD10 |
cd17635 |
adenylate forming domain, fatty acid CoA ligase (FadD10); This family contains long chain ... |
193-531 |
5.48e-38 |
|
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: 142.78 E-value: 5.48e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1216630836 193 IALIMNSSGSTGLPKGVALPHRTACVRFSHARdpIFGNQIIPDTAILSVVPFHHGFGMFTTLGYLIC-GFRVVLMYRFEE 271
Cdd:cd17635 3 PLAVIFTSGTTGEPKAVLLANKTFFAVPDILQ--KEGLNWVVGDVTYLPLPATHIGGLWWILTCLIHgGLCVTGGENTTY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1216630836 272 ELFLRSLQDYKIQSALLVPTLFSFFAKSTLIDKYDLSNLHEIASGGA-PLSKEVgeAVAKRFHLPGIRQGYGLTETTSAI 350
Cdd:cd17635 81 KSLFKILTTNAVTTTCLVPTLLSKLVSELKSANATVPSLRLIGYGGSrAIAADV--RFIEATGLTNTAQVYGLSETGTAL 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1216630836 351 LItPEGDDKP--GAVGKVVPFFEAKVVDLDtGKTLGVNQRGELCVRGPMIMSGYVNNPEATNALIdKDGWLHSGDIAYWD 428
Cdd:cd17635 159 CL-PTDDDSIeiNAVGRPYPGVDVYLAATD-GIAGPSASFGTIWIKSPANMLGYWNNPERTAEVL-IDGWVNTGDLGERR 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1216630836 429 EDEHFFIVDRLKSLIKYKGYQVAPAELESILLQHPNIFDAGVAGLPDDDAGELPAAVVV----LEHGKTMTEKEIVDYVA 504
Cdd:cd17635 236 EDGFLFITGRSSESINCGGVKIAPDEVERIAEGVSGVQECACYEISDEEFGELVGLAVVasaeLDENAIRALKHTIRREL 315
|
330 340
....*....|....*....|....*..
gi 1216630836 505 SQVTTAKKlrggVVFVDEVPKGLTGKL 531
Cdd:cd17635 316 EPYARPST----IVIVTDIPRTQSGKV 338
|
|
| LC_FACS_euk1 |
cd17639 |
Eukaryotic long-chain fatty acid CoA synthetase (LC-FACS), including fungal proteins; The ... |
52-465 |
1.16e-37 |
|
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: 145.44 E-value: 1.16e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1216630836 52 ITYAEYFEMSVRLAEAMKRYGLNTNHRIVVCSENSLQFFMPVLGALFIGVAVAPANDIYNERELLNSMgiSQPTVvfvsk 131
Cdd:cd17639 6 MSYAEVWERVLNFGRGLVELGLKPGDKVAIFAETRAEWLITALGCWSQNIPIVTVYATLGEDALIHSL--NETEC----- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1216630836 132 kglqkilnvqkklpiiqKIIIMDSKTDyqgfqsmytfvtshlppgfneydfvpesfdrdkTIALIMNSSGSTGLPKGVAL 211
Cdd:cd17639 79 -----------------SAIFTDGKPD---------------------------------DLACIMYTSGSTGNPKGVML 108
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1216630836 212 PHRTaCVRFSHARDPIFGNQIIPDTAILSVVPFHH-----------------GFGMFTTLGYLICG--------FRVVLM 266
Cdd:cd17639 109 THGN-LVAGIAGLGDRVPELLGPDDRYLAYLPLAHifelaaenvclyrggtiGYGSPRTLTDKSKRgckgdlteFKPTLM 187
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1216630836 267 Y---------------------RFEEELFLRSLQdYKiQSALLVPTLFSF-----FAKstlIDKYDLSNLHEIASGGAPL 320
Cdd:cd17639 188 VgvpaiwdtirkgvlaklnpmgGLKRTLFWTAYQ-SK-LKALKEGPGTPLldelvFKK---VRAALGGRLRYMLSGGAPL 262
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1216630836 321 SKEvgeavAKRF---HLPGIRQGYGLTETTSAILITPEGDDKPGAVGKVVPFFEAKVVDLDTGK--TLGVNQRGELCVRG 395
Cdd:cd17639 263 SAD-----TQEFlniVLCPVIQGYGLTETCAGGTVQDPGDLETGRVGPPLPCCEIKLVDWEEGGysTDKPPPRGEILIRG 337
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1216630836 396 PMIMSGYVNNPEATNALIDKDGWLHSGDIAYWDEDEHFFIVDRLKSLIKYK-GYQVAPAELESILLQHPNI 465
Cdd:cd17639 338 PNVFKGYYKNPEKTKEAFDGDGWFHTGDIGEFHPDGTLKIIDRKKDLVKLQnGEYIALEKLESIYRSNPLV 408
|
|
| AA-adenyl-dom |
TIGR01733 |
amino acid adenylation domain; This model represents a domain responsible for the specific ... |
53-470 |
1.61e-37 |
|
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: 143.17 E-value: 1.61e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1216630836 53 TYAEYFEMSVRLAEAMKRY-GLNTNHRIVVCSENSLQFFMPVLGALFIGVAVAPandiynerellnsMGISQPTvvfvsk 131
Cdd:TIGR01733 1 TYRELDERANRLARHLRAAgGVGPGDRVAVLLERSAELVVAILAVLKAGAAYVP-------------LDPAYPA------ 61
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1216630836 132 KGLQKILNVqkklpIIQKIIIMDSktDYQGFQSMYTFVTSHLPPGFNEYD------FVPESFDRDKTIALIMNSSGSTGL 205
Cdd:TIGR01733 62 ERLAFILED-----AGARLLLTDS--ALASRLAGLVLPVILLDPLELAALddapapPPPDAPSGPDDLAYVIYTSGSTGR 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1216630836 206 PKGVALPHRTACVRFSHARDPIFGNqiiPDTAILSVVPFHHGFGMFTTLGYLICGFRVVLMY----RFEEELFLRSLQDY 281
Cdd:TIGR01733 135 PKGVVVTHRSLVNLLAWLARRYGLD---PDDRVLQFASLSFDASVEEIFGALLAGATLVVPPedeeRDDAALLAALIAEH 211
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1216630836 282 KIQSALLVPTLFSFFAKStliDKYDLSNLHEIASGGAPLSKEVGEAVAKRFHLPGIRQGYGLTETT---SAILITPEGDD 358
Cdd:TIGR01733 212 PVTVLNLTPSLLALLAAA---LPPALASLRLVILGGEALTPALVDRWRARGPGARLINLYGPTETTvwsTATLVDPDDAP 288
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1216630836 359 KPGAV--GKVVPFFEAKVVDlDTGKTLGVNQRGELCVRGPMIMSGYVNNPEATN--------ALIDKDGWLHSGDIAYWD 428
Cdd:TIGR01733 289 RESPVpiGRPLANTRLYVLD-DDLRPVPVGVVGELYIGGPGVARGYLNRPELTAerfvpdpfAGGDGARLYRTGDLVRYL 367
|
410 420 430 440
....*....|....*....|....*....|....*....|..
gi 1216630836 429 EDEHFFIVDRLKSLIKYKGYQVAPAELESILLQHPNIFDAGV 470
Cdd:TIGR01733 368 PDGNLEFLGRIDDQVKIRGYRIELGEIEAALLRHPGVREAVV 409
|
|
| PRK05852 |
PRK05852 |
fatty acid--CoA ligase family protein; |
50-538 |
2.54e-37 |
|
fatty acid--CoA ligase family protein;
Pssm-ID: 235625 [Multi-domain] Cd Length: 534 Bit Score: 145.03 E-value: 2.54e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1216630836 50 VDITYAEYFEMSVRLAEAMKRYGLNTNHRIVVCSENSLQFFMPVLGALFIGVAVAPANDIYNERELLNSMGISQPTVVFV 129
Cdd:PRK05852 42 IAISYRDLARLVDDLAGQLTRSGLLPGDRVALRMGSNAEFVVALLAASRADLVVVPLDPALPIAEQRVRSQAAGARVVLI 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1216630836 130 SKKGL-QKILNVQKKLPIiqKIIIMDSKTDYQGFQSMYTFVTSHLPPGFNeydfVPESFDRDKtiALIMNSSGSTGLPKG 208
Cdd:PRK05852 122 DADGPhDRAEPTTRWWPL--TVNVGGDSGPSGGTLSVHLDAATEPTPATS----TPEGLRPDD--AMIMFTGGTTGLPKM 193
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1216630836 209 VALPHRTACvrfSHARDPIFGNQIIPDTAILSVVPFHHGFGMFTTLGYLICGFRVVLM---YRFEEELFLRSLQDYKIQS 285
Cdd:PRK05852 194 VPWTHANIA---SSVRAIITGYRLSPRDATVAVMPLYHGHGLIAALLATLASGGAVLLparGRFSAHTFWDDIKAVGATW 270
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1216630836 286 ALLVPTLFSFFAK--STLIDKYDLSNLHEIASGGAPLSKEVGEAVAKRFHLPGIrQGYGLTETTSAILITP-EGDDK--- 359
Cdd:PRK05852 271 YTAVPTIHQILLEraATEPSGRKPAALRFIRSCSAPLTAETAQALQTEFAAPVV-CAFGMTEATHQVTTTQiEGIGQten 349
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1216630836 360 ----PGAVGKVVPFfEAKVVDLDtGKTLGVNQRGELCVRGPMIMSGYVNNPEATNALIdKDGWLHSGDIAYWDEDEHFFI 435
Cdd:PRK05852 350 pvvsTGLVGRSTGA-QIRIVGSD-GLPLPAGAVGEVWLRGTTVVRGYLGDPTITAANF-TDGWLRTGDLGSLSAAGDLSI 426
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1216630836 436 VDRLKSLIKYKGYQVAPAELESILLQHPNIFDAGVAGLPDDDAGELPAAVVVLEHGKTMTEKEIVDYVASQVtTAKKLRG 515
Cdd:PRK05852 427 RGRIKELINRGGEKISPERVEGVLASHPNVMEAAVFGVPDQLYGEAVAAVIVPRESAPPTAEELVQFCRERL-AAFEIPA 505
|
490 500
....*....|....*....|...
gi 1216630836 516 GVVFVDEVPKGLTGKLDARKIRE 538
Cdd:PRK05852 506 SFQEASGLPHTAKGSLDRRAVAE 528
|
|
| PRK13390 |
PRK13390 |
acyl-CoA synthetase; Provisional |
52-537 |
3.08e-37 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 139538 [Multi-domain] Cd Length: 501 Bit Score: 144.38 E-value: 3.08e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1216630836 52 ITYAEYFEMSVRLAEAMKRYGLNTNHRIVVCSENSLQFFMPVLGALFIGVAVAPANDIYNERELLNSMGISQPTVVFVSK 131
Cdd:PRK13390 25 VSYRQLDDDSAALARVLYDAGLRTGDVVALLSDNSPEALVVLWAALRSGLYITAINHHLTAPEADYIVGDSGARVLVASA 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1216630836 132 KGLQKILNVQKKLPIIqkiIIMDSKTDyqGFQSMYTFVTSHLPPgfneydfvpesFDRDKTIALIMNSSGSTGLPKGVA- 210
Cdd:PRK13390 105 ALDGLAAKVGADLPLR---LSFGGEID--GFGSFEAALAGAGPR-----------LTEQPCGAVMLYSSGTTGFPKGIQp 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1216630836 211 -LPHRTAcvrfSHARDPI-------FGnqIIPDTAILSVVPFHHGF-----GMFTTLGYlicgfRVVLMYRFEEELFLRS 277
Cdd:PRK13390 169 dLPGRDV----DAPGDPIvaiarafYD--ISESDIYYSSAPIYHAAplrwcSMVHALGG-----TVVLAKRFDAQATLGH 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1216630836 278 LQDYKIQSALLVPTLFSFFAK--STLIDKYDLSNLHEIASGGAPLSKEVGEAVAKRFHlPGIRQGYGLTETTSAILI-TP 354
Cdd:PRK13390 238 VERYRITVTQMVPTMFVRLLKldADVRTRYDVSSLRAVIHAAAPCPVDVKHAMIDWLG-PIVYEYYSSTEAHGMTFIdSP 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1216630836 355 EGDDKPGAVGKVVpFFEAKVVDlDTGKTLGVNQRGELCVRGPMIMSGYVNNPEATNALIDKDG--WLHSGDIAYWDEDEH 432
Cdd:PRK13390 317 DWLAHPGSVGRSV-LGDLHICD-DDGNELPAGRIGTVYFERDRLPFRYLNDPEKTAAAQHPAHpfWTTVGDLGSVDEDGY 394
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1216630836 433 FFIVDRLKSLIKYKGYQVAPAELESILLQHPNIFDAGVAGLPDDDAGELPAAVVVLEHGKTMTE---KEIVDYVASQVTT 509
Cdd:PRK13390 395 LYLADRKSFMIISGGVNIYPQETENALTMHPAVHDVAVIGVPDPEMGEQVKAVIQLVEGIRGSDelaRELIDYTRSRIAH 474
|
490 500
....*....|....*....|....*...
gi 1216630836 510 AKKLRgGVVFVDEVPKGLTGKLDARKIR 537
Cdd:PRK13390 475 YKAPR-SVEFVDELPRTPTGKLVKGLLR 501
|
|
| PrpE |
cd05967 |
Propionyl-CoA synthetase (PrpE); EC 6.2.1.17: propanoate:CoA ligase (AMP-forming) or ... |
196-539 |
1.26e-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: 144.00 E-value: 1.26e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1216630836 196 IMNSSGSTGLPKGVALPHRTACVRFSHARDPIFGnqIIPDTAILS------VVpfHHGFGMFttlGYLICGFRVVLmyrF 269
Cdd:cd05967 235 ILYTSGTTGKPKGVVRDNGGHAVALNWSMRNIYG--IKPGDVWWAasdvgwVV--GHSYIVY---GPLLHGATTVL---Y 304
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1216630836 270 EEE--------LFLRSLQDYKIQSALLVPTLFSFFAK----STLIDKYDLSNLHEIASGGAPLSKEVGEAVAKRFHLPGI 337
Cdd:cd05967 305 EGKpvgtpdpgAFWRVIEKYQVNALFTAPTAIRAIRKedpdGKYIKKYDLSSLRTLFLAGERLDPPTLEWAENTLGVPVI 384
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1216630836 338 RQgYGLTETTSAILITPEGDD----KPGAVGKVVPFFEAKVVDlDTGKTLGVNQRGELCVRGPM---IMSGYVNNPEA-- 408
Cdd:cd05967 385 DH-WWQTETGWPITANPVGLEplpiKAGSPGKPVPGYQVQVLD-EDGEPVGPNELGNIVIKLPLppgCLLTLWKNDERfk 462
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1216630836 409 TNALIDKDGWLHSGDIAYWDEDEHFFIVDRLKSLIKYKGYQVAPAELESILLQHPNIFDAGVAGLPDDDAGELPAAVVVL 488
Cdd:cd05967 463 KLYLSKFPGYYDTGDAGYKDEDGYLFIMGRTDDVINVAGHRLSTGEMEESVLSHPAVAECAVVGVRDELKGQVPLGLVVL 542
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*...
gi 1216630836 489 EHGKTMT----EKEIVDYVASQ---VTTAKKlrggVVFVDEVPKGLTGKLDARKIREI 539
Cdd:cd05967 543 KEGVKITaeelEKELVALVREQigpVAAFRL----VIFVKRLPKTRSGKILRRTLRKI 596
|
|
| A_NRPS_TubE_like |
cd05906 |
The adenylation domain (A domain) of a family of nonribosomal peptide synthetases (NRPSs) ... |
12-540 |
2.96e-36 |
|
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: 142.04 E-value: 2.96e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1216630836 12 PAPFYPLEDGTAGEQLHKAMKRYALVpGTIAFTDAHIEVDITYAEYFEMSVRLAEAMKRYGLNTNHRIV-VCSENslQFF 90
Cdd:cd05906 1 PLHRPEGAPRTLLELLLRAAERGPTK-GITYIDADGSEEFQSYQDLLEDARRLAAGLRQLGLRPGDSVIlQFDDN--EDF 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1216630836 91 MPVLGALFIG------VAVAPANDIYNER--------ELLNsmgisQPtVVFVSKKGLQKILNVQKKLPI-IQKIIIMDS 155
Cdd:cd05906 78 IPAFWACVLAgfvpapLTVPPTYDEPNARlrklrhiwQLLG-----SP-VVLTDAELVAEFAGLETLSGLpGIRVLSIEE 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1216630836 156 KTDYQGfqsmytfvtshlppgfnEYDFVPESFDrdkTIALIMNSSGSTGLPKGVALPHRTACVRFSHArdpIFGNQIIPD 235
Cdd:cd05906 152 LLDTAA-----------------DHDLPQSRPD---DLALLMLTSGSTGFPKAVPLTHRNILARSAGK---IQHNGLTPQ 208
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1216630836 236 TAILSVVPFHH--GFGMFTTLG-YLICG-FRV----VLMyrfEEELFLRSLQDYKIQsallvptlFSF---FAKSTLID- 303
Cdd:cd05906 209 DVFLNWVPLDHvgGLVELHLRAvYLGCQqVHVpteeILA---DPLRWLDLIDRYRVT--------ITWapnFAFALLNDl 277
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1216630836 304 -------KYDLSNLHEIASGGAPLSKEVGEAVA---KRFHLPG--IRQGYGLTETTSAIL--ITPEGDDKPGA-----VG 364
Cdd:cd05906 278 leeiedgTWDLSSLRYLVNAGEAVVAKTIRRLLrllEPYGLPPdaIRPAFGMTETCSGVIysRSFPTYDHSQAlefvsLG 357
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1216630836 365 KVVPFFEAKVVDlDTGKTLGVNQRGELCVRGPMIMSGYVNNPEATNALIDKDGWLHSGDIAYWDeDEHFFIVDRLKSLIK 444
Cdd:cd05906 358 RPIPGVSMRIVD-DEGQLLPEGEVGRLQVRGPVVTKGYYNNPEANAEAFTEDGWFRTGDLGFLD-NGNLTITGRTKDTII 435
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1216630836 445 YKGYQVAPAELESILLQHPNI---FDAGVAGLPDDDAGE------LPAAVVVLEHGKTMteKEIVDYVASQVTTAKKLrg 515
Cdd:cd05906 436 VNGVNYYSHEIEAAVEEVPGVepsFTAAFAVRDPGAETEelaiffVPEYDLQDALSETL--RAIRSVVSREVGVSPAY-- 511
|
570 580
....*....|....*....|....*..
gi 1216630836 516 gVVFV--DEVPKGLTGKLDARKIREIL 540
Cdd:cd05906 512 -LIPLpkEEIPKTSLGKIQRSKLKAAF 537
|
|
| PLN03102 |
PLN03102 |
acyl-activating enzyme; Provisional |
53-539 |
4.47e-36 |
|
acyl-activating enzyme; Provisional
Pssm-ID: 215576 [Multi-domain] Cd Length: 579 Bit Score: 142.08 E-value: 4.47e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1216630836 53 TYAEYFEMSVRLAEAMKRYGLNTNHRIVVCSENS-----LQFFMPVLGALfigvaVAPANDIYNERELLNSMGISQPTVV 127
Cdd:PLN03102 41 TWPQTYDRCCRLAASLISLNITKNDVVSVLAPNTpamyeMHFAVPMAGAV-----LNPINTRLDATSIAAILRHAKPKIL 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1216630836 128 FVSKKG---LQKILNV------QKKLPIIQkIIIMDSKT-------DYQGFQSMYTFVTSHLPPGF---NEYDfvPESFD 188
Cdd:PLN03102 116 FVDRSFeplAREVLHLlssedsNLNLPVIF-IHEIDFPKrpsseelDYECLIQRGEPTPSLVARMFriqDEHD--PISLN 192
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1216630836 189 RdktialimnSSGSTGLPKGVALPHRTAcvrFSHARDPIFGNQIIPDTAILSVVPFHHGFGMFTTLGYLICGFRVVLMYR 268
Cdd:PLN03102 193 Y---------TSGTTADPKGVVISHRGA---YLSTLSAIIGWEMGTCPVYLWTLPMFHCNGWTFTWGTAARGGTSVCMRH 260
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1216630836 269 FEEELFLRSLQDYKIQSALLVPTLFSFFAKSTLIDKYDLSNLHEIASGGAPLSKEVGEAVAKR-FHlpgIRQGYGLTETT 347
Cdd:PLN03102 261 VTAPEIYKNIEMHNVTHMCCVPTVFNILLKGNSLDLSPRSGPVHVLTGGSPPPAALVKKVQRLgFQ---VMHAYGLTEAT 337
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1216630836 348 SAILIT---------PEGDDKPGAVGKVVPFFEAKVVDLDTGKTLGVNQR-----GELCVRGPMIMSGYVNNPEATNALI 413
Cdd:PLN03102 338 GPVLFCewqdewnrlPENQQMELKARQGVSILGLADVDVKNKETQESVPRdgktmGEIVIKGSSIMKGYLKNPKATSEAF 417
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1216630836 414 dKDGWLHSGDIAYWDEDEHFFIVDRLKSLIKYKGYQVAPAELESILLQHPNIFDAGVAGLPDDDAGELPAAVVVLEHGKT 493
Cdd:PLN03102 418 -KHGWLNTGDVGVIHPDGHVEIKDRSKDIIISGGENISSVEVENVLYKYPKVLETAVVAMPHPTWGETPCAFVVLEKGET 496
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*
gi 1216630836 494 MTEKEIVDYVASQVTTAKKLRGG---------VVFVDEVPKGLTGKLDARKIREI 539
Cdd:PLN03102 497 TKEDRVDKLVTRERDLIEYCRENlphfmcprkVVFLQELPKNGNGKILKPKLRDI 551
|
|
| MACS_like_2 |
cd05973 |
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the ... |
195-531 |
5.27e-35 |
|
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: 136.88 E-value: 5.27e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1216630836 195 LIMNSSGSTGLPKGVALPHRTACVRFSHARDPIfgnQIIPDTAILSVVPFHHGFGMF-TTLGYLICGFRVVLMYR-FEEE 272
Cdd:cd05973 92 VMMFTSGTTGLPKGVPVPLRALAAFGAYLRDAV---DLRPEDSFWNAADPGWAYGLYyAITGPLALGHPTILLEGgFSVE 168
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1216630836 273 LFLRSLQDYKIQSALLVPTLF-SFFAKSTLIDKYDLSNLHEIASGGAPLSKEVGEAVAKRFHLPgIRQGYGLTETtSAIL 351
Cdd:cd05973 169 STWRVIERLGVTNLAGSPTAYrLLMAAGAEVPARPKGRLRRVSSAGEPLTPEVIRWFDAALGVP-IHDHYGQTEL-GMVL 246
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1216630836 352 ITPEGDDKP---GAVGKVVPFFEAKVVDLDtGKTLGVNQRGELCV---RGP-MIMSGYVNNPEATNAlidkDGWLHSGDI 424
Cdd:cd05973 247 ANHHALEHPvhaGSAGRAMPGWRVAVLDDD-GDELGPGEPGRLAIdiaNSPlMWFRGYQLPDTPAID----GGYYLTGDT 321
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1216630836 425 AYWDEDEHFFIVDRLKSLIKYKGYQVAPAELESILLQHPNIFDAGVAGLPDDDAGELPAAVVVLEHGKTMT---EKEIVD 501
Cdd:cd05973 322 VEFDPDGSFSFIGRADDVITMSGYRIGPFDVESALIEHPAVAEAAVIGVPDPERTEVVKAFVVLRGGHEGTpalADELQL 401
|
330 340 350
....*....|....*....|....*....|
gi 1216630836 502 YVASQVTTAKKLRgGVVFVDEVPKGLTGKL 531
Cdd:cd05973 402 HVKKRLSAHAYPR-TIHFVDELPKTPSGKI 430
|
|
| FAAL |
cd05931 |
Fatty acyl-AMP ligase (FAAL); FAAL belongs to the class I adenylate forming enzyme family and ... |
32-538 |
6.99e-35 |
|
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: 138.14 E-value: 6.99e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1216630836 32 KRYALVPGTIAFT----DAHIEVDITYAEYFEMSVRLAEAMKRYGLnTNHRIVVCSENSLQFFMPVLGALFIGVAVAPAN 107
Cdd:cd05931 1 RRAAARPDRPAYTflddEGGREETLTYAELDRRARAIAARLQAVGK-PGDRVLLLAPPGLDFVAAFLGCLYAGAIAVPLP 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1216630836 108 DIYNERE---LLNSMGISQPTVVFVSKK---GLQKILNVQKKLPIIQkIIIMDSKTDyqgfqsmytfvtshLPPGfneyD 181
Cdd:cd05931 80 PPTPGRHaerLAAILADAGPRVVLTTAAalaAVRAFAASRPAAGTPR-LLVVDLLPD--------------TSAA----D 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1216630836 182 FVPESFDRDkTIALIMNSSGSTGLPKGVALPHRTAcvrFSHARDPIFGNQIIPDTAILSVVPFHHGFGMFTTLGY-LICG 260
Cdd:cd05931 141 WPPPSPDPD-DIAYLQYTSGSTGTPKGVVVTHRNL---LANVRQIRRAYGLDPGDVVVSWLPLYHDMGLIGGLLTpLYSG 216
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1216630836 261 FRVVLM---------YRFeeelfLRSLQDYKIQ-SAllVPTlfsfFA--------KSTLIDKYDLSNLHEIASGGAPLSK 322
Cdd:cd05931 217 GPSVLMspaaflrrpLRW-----LRLISRYRATiSA--APN----FAydlcvrrvRDEDLEGLDLSSWRVALNGAEPVRP 285
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1216630836 323 EVGEAVAKRF---------HLPGirqgYGLTETTSAILITPEGD---------------------DKPGAV-----GKVV 367
Cdd:cd05931 286 ATLRRFAEAFapfgfrpeaFRPS----YGLAEATLFVSGGPPGTgpvvlrvdrdalagravavaaDDPAARelvscGRPL 361
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1216630836 368 PFFEAKVVDLDTGKTLGVNQRGELCVRGPMIMSGYVNNPEATNAL------IDKDGWLHSGDIAYWDEDEhFFIVDRLKS 441
Cdd:cd05931 362 PDQEVRIVDPETGRELPDGEVGEIWVRGPSVASGYWGRPEATAETfgalaaTDEGGWLRTGDLGFLHDGE-LYITGRLKD 440
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1216630836 442 LIKYKGYQVAPAELESILLQHPNIFDAGVA---GLPDDDAGELpaaVVVLEHGKTMTE---KEIVDYVASQVTTAKKLR- 514
Cdd:cd05931 441 LIIVRGRNHYPQDIEATAEEAHPALRPGCVaafSVPDDGEERL---VVVAEVERGADPadlAAIAAAIRAAVAREHGVAp 517
|
570 580
....*....|....*....|....*.
gi 1216630836 515 GGVVFV--DEVPKGLTGKLDARKIRE 538
Cdd:cd05931 518 ADVVLVrpGSIPRTSSGKIQRRACRA 543
|
|
| FACL_like_5 |
cd05924 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
195-534 |
1.86e-33 |
|
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: 130.97 E-value: 1.86e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1216630836 195 LIMNSSGSTGLPKGVALPHRTACVRFSHARDPIFGNQII-----------PDTAILSVVPFHHGFGMFTTLGYLICGFRV 263
Cdd:cd05924 7 YILYTGGTTGMPKGVMWRQEDIFRMLMGGADFGTGEFTPsedahkaaaaaAGTVMFPAPPLMHGTGSWTAFGGLLGGQTV 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1216630836 264 VLM-YRFEEELFLRSLQDYKIQSALLVPTLFsffAKStLIDK------YDLSNLHEIASGGAPLSKEVGEAVAKRFHLPG 336
Cdd:cd05924 87 VLPdDRFDPEEVWRTIEKHKVTSMTIVGDAM---ARP-LIDAlrdagpYDLSSLFAISSGGALLSPEVKQGLLELVPNIT 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1216630836 337 IRQGYGLTETTS-AILITPEGDDKPGAVGKVVPffEAKVVDLDTGKTL-GVNQRGELCVRGpMIMSGYVNNPEAT-NALI 413
Cdd:cd05924 163 LVDAFGSSETGFtGSGHSAGSGPETGPFTRANP--DTVVLDDDGRVVPpGSGGVGWIARRG-HIPLGYYGDEAKTaETFP 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1216630836 414 DKDG--WLHSGDIAYWDEDEHFFIVDRLKSLIKYKGYQVAPAELESILLQHPNIFDAGVAGLPDDDAGELPAAVVVLEHG 491
Cdd:cd05924 240 EVDGvrYAVPGDRATVEADGTVTLLGRGSVCINTGGEKVFPEEVEEALKSHPAVYDVLVVGRPDERWGQEVVAVVQLREG 319
|
330 340 350 360
....*....|....*....|....*....|....*....|...
gi 1216630836 492 KTMTEKEIVDYVASQVtTAKKLRGGVVFVDEVPKGLTGKLDAR 534
Cdd:cd05924 320 AGVDLEELREHCRTRI-ARYKLPKQVVFVDEIERSPAGKADYR 361
|
|
| ttLC_FACS_like |
cd05915 |
Fatty acyl-CoA synthetases similar to LC-FACS from Thermus thermophiles; This family includes ... |
31-538 |
2.36e-33 |
|
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: 133.33 E-value: 2.36e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1216630836 31 MKRYALVPGTIAFTDahieVDITYAEYFEMSVRLAEAMKRYGLNTNHRIVVCSENslqffMPVLGALFIGVAVAPA---- 106
Cdd:cd05915 8 FGRKEVVSRLHTGEV----HRTTYAEVYQRARRLMGGLRALGVGVGDRVATLGFN-----HFRHLEAYFAVPGMGAvlht 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1216630836 107 -NDIYNERELLNSMGISQPTVVFVSKKGLQKilnVQKKLPIIQKIiiMDSKTDYQGFQSMYTFVTSHLPpgfneyDFVP- 184
Cdd:cd05915 79 aNPRLSPKEIAYILNHAEDKVLLFDPNLLPL---VEAIRGELKTV--QHFVVMDEKAPEGYLAYEEALG------EEADp 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1216630836 185 ESFDRDKTIALIMnSSGSTGLPKGVALPHRTAcvrFSHARDPIFGNQII--PDTAILSVVPFHHGFG-----MFTTLGYL 257
Cdd:cd05915 148 VRVPERAACGMAY-TTGTTGLPKGVVYSHRAL---VLHSLAASLVDGTAlsEKDVVLPVVPMFHVNAwclpyAATLVGAK 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1216630836 258 ICGFRVVLmyrfEEELFLRSLQDYKIQSALLVPTLFSFFAKSTLIDKYDLSNLHEIASGGAPlSKEVGEAVaKRFHLPGI 337
Cdd:cd05915 224 QVLPGPRL----DPASLVELFDGEGVTFTAGVPTVWLALADYLESTGHRLKTLRRLVVGGSA-APRSLIAR-FERMGVEV 297
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1216630836 338 RQGYGLTET---TSAILITPEGDDKP-------GAVGKVVPFFEAkvVDLDTGKTLGVNQRGE----LCVRGPMIMSGYV 403
Cdd:cd05915 298 RQGYGLTETspvVVQNFVKSHLESLSeeekltlKAKTGLPIPLVR--LRVADEEGRPVPKDGKalgeVQLKGPWITGGYY 375
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1216630836 404 NNPEATNALIDKDGWLHSGDIAYWDEDEHFFIVDRLKSLIKYKGYQVAPAELESILLQHPNIFDAGVAGLPDDDAGELPA 483
Cdd:cd05915 376 GNEEATRSALTPDGFFRTGDIAVWDEEGYVEIKDRLKDLIKSGGEWISSVDLENALMGHPKVKEAAVVAIPHPKWQERPL 455
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*
gi 1216630836 484 AVVVLEHGKTmTEKEIVDYVASQVTTAKKLRGGVVFVDEVPKGLTGKLDARKIRE 538
Cdd:cd05915 456 AVVVPRGEKP-TPEELNEHLLKAGFAKWQLPDAYVFAEEIPRTSAGKFLKRALRE 509
|
|
| PRK07638 |
PRK07638 |
acyl-CoA synthetase; Validated |
29-545 |
4.27e-33 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236071 [Multi-domain] Cd Length: 487 Bit Score: 132.21 E-value: 4.27e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1216630836 29 KAMKRYA-LVPGTIAFTDAhiEVDITYAEYFEMSVRLAEAMkRYGLNTNHRIVVCSENSLQFFMPVLGALFIGVAVAPAN 107
Cdd:PRK07638 5 KEYKKHAsLQPNKIAIKEN--DRVLTYKDWFESVCKVANWL-NEKESKNKTIAILLENRIEFLQLFAGAAMAGWTCVPLD 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1216630836 108 DIYNERELLNSMGISQPTVVFVSKKGLQKILNVQKKLpiiqkIIIMDSKTDYQGFQSMYTFVTS--HLP--PGFneydfv 183
Cdd:PRK07638 82 IKWKQDELKERLAISNADMIVTERYKLNDLPDEEGRV-----IEIDEWKRMIEKYLPTYAPIENvqNAPfyMGF------ 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1216630836 184 pesfdrdktialimnSSGSTGLPKGVALPHRTACVRFSHARDPIfgnQIIPDTAIL---SVVPFHHGFGMFTTLgYLicG 260
Cdd:PRK07638 151 ---------------TSGSTGKPKAFLRAQQSWLHSFDCNVHDF---HMKREDSVLiagTLVHSLFLYGAISTL-YV--G 209
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1216630836 261 FRVVLMYRFEEELFLRSLQDYKIQSALLVPTLFSFFAKstlIDKYdLSNLHEIASGGAPLSKEVGEAVAKRFHLPGIRQG 340
Cdd:PRK07638 210 QTVHLMRKFIPNQVLDKLETENISVMYTVPTMLESLYK---ENRV-IENKMKIISSGAKWEAEAKEKIKNIFPYAKLYEF 285
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1216630836 341 YGLTETTSAILITPEGDD-KPGAVGKvvPFFEAKV-VDLDTGKTLGVNQRGELCVRGPMIMSGYVNNPEATNALiDKDGW 418
Cdd:PRK07638 286 YGASELSFVTALVDEESErRPNSVGR--PFHNVQVrICNEAGEEVQKGEIGTVYVKSPQFFMGYIIGGVLAREL-NADGW 362
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1216630836 419 LHSGDIAYWDEDEHFFIVDRLKSLIKYKGYQVAPAELESILLQHPNIFDAGVAGLPDDDAGELPAAVVvleHGKTmTEKE 498
Cdd:PRK07638 363 MTVRDVGYEDEEGFIYIVGREKNMILFGGINIFPEEIESVLHEHPAVDEIVVIGVPDSYWGEKPVAII---KGSA-TKQQ 438
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|
gi 1216630836 499 IVDYVASQVTTAKKLRgGVVFVDEVPKGLTGKLD---ARKIREILIKAKK 545
Cdd:PRK07638 439 LKSFCLQRLSSFKIPK-EWHFVDEIPYTNSGKIArmeAKSWIENQEKIYE 487
|
|
| PRK06018 |
PRK06018 |
putative acyl-CoA synthetase; Provisional |
53-538 |
5.14e-33 |
|
putative acyl-CoA synthetase; Provisional
Pssm-ID: 235673 [Multi-domain] Cd Length: 542 Bit Score: 132.57 E-value: 5.14e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1216630836 53 TYAEYFEMSVRLAEAMKRYGLNTNHRIVVCSENSLQFFMPVLGALFIGVAVAPANDIYNERELLNSMGISQPTVVFVSKK 132
Cdd:PRK06018 41 TYAQIHDRALKVSQALDRDGIKLGDRVATIAWNTWRHLEAWYGIMGIGAICHTVNPRLFPEQIAWIINHAEDRVVITDLT 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1216630836 133 GLQKILNVQKKLPIIQKIIIMDSKtdyqgfqsmytfvtSHLP----PGFNEY---------DFVPESFDRDkTIALIMNS 199
Cdd:PRK06018 121 FVPILEKIADKLPSVERYVVLTDA--------------AHMPqttlKNAVAYeewiaeadgDFAWKTFDEN-TAAGMCYT 185
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1216630836 200 SGSTGLPKGVALPHRTacvRFSHArdpIFGNQiiPDT-------AILSVVPFHHGFGMFTTLGYLICGFRVVL------- 265
Cdd:PRK06018 186 SGTTGDPKGVLYSHRS---NVLHA---LMANN--GDAlgtsaadTMLPVVPLFHANSWGIAFSAPSMGTKLVMpgakldg 257
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1216630836 266 --MYrfeeELflrsLQDYKIQSALLVPTLFSFFAKSTLIDKYDLSNLHEIASGGAPLSkevgEAVAKRFHLPGI--RQGY 341
Cdd:PRK06018 258 asVY----EL----LDTEKVTFTAGVPTVWLMLLQYMEKEGLKLPHLKMVVCGGSAMP----RSMIKAFEDMGVevRHAW 325
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1216630836 342 GLTET----TSAILiTPEGDDKPGAVGKVV-------PF-FEAKVVDlDTGKTLGVNQR--GELCVRGPMIMSGYVnnpE 407
Cdd:PRK06018 326 GMTEMsplgTLAAL-KPPFSKLPGDARLDVlqkqgypPFgVEMKITD-DAGKELPWDGKtfGRLKVRGPAVAAAYY---R 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1216630836 408 ATNALIDKDGWLHSGDIAYWDEDEHFFIVDRLKSLIKYKGYQVAPAELESILLQHPNIFDAGVAGLPDDDAGELPAAVVV 487
Cdd:PRK06018 401 VDGEILDDDGFFDTGDVATIDAYGYMRITDRSKDVIKSGGEWISSIDLENLAVGHPKVAEAAVIGVYHPKWDERPLLIVQ 480
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|..
gi 1216630836 488 LEHGKTMTEKEIVDYVASQVttAK-KLRGGVVFVDEVPKGLTGKLDARKIRE 538
Cdd:PRK06018 481 LKPGETATREEILKYMDGKI--AKwWMPDDVAFVDAIPHTATGKILKTALRE 530
|
|
| LC_FACS_like |
cd17640 |
Long-chain fatty acid CoA synthetase; This family includes long-chain fatty acid (C12-C20) CoA ... |
52-472 |
1.59e-32 |
|
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: 130.17 E-value: 1.59e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1216630836 52 ITYAEYFEMSVRLAEAMKRYGLNTNHRIVVCSENSLQFFMPVLGALFIGVAVAPANDIYNERELLNSMGISQPTVVFVSk 131
Cdd:cd17640 6 ITYKDLYQEILDFAAGLRSLGVKAGEKVALFADNSPRWLIADQGIMALGAVDVVRGSDSSVEELLYILNHSESVALVVE- 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1216630836 132 kglqkilnvqkklpiiqkiiimdsktdyqgfqsmytfvtshlppgfneydfvpesfDRDKTIALIMNSSGSTGLPKGVAL 211
Cdd:cd17640 85 --------------------------------------------------------NDSDDLATIIYTSGTTGNPKGVML 108
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1216630836 212 PHRTACVRFSHARDPIfgnQIIPDTAILSVVPFHHGFGMFTTLGYLICGfrVVLMY---RFeeelFLRSLQDYKIQSALL 288
Cdd:cd17640 109 THANLLHQIRSLSDIV---PPQPGDRFLSILPIWHSYERSAEYFIFACG--CSQAYtsiRT----LKDDLKRVKPHYIVS 179
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1216630836 289 VPTLF-------------SFFAKSTLIDKYDLSNLHEIA-SGGAPLSKEVgeavAKRFHLPGIR--QGYGLTETTSAILI 352
Cdd:cd17640 180 VPRLWeslysgiqkqvskSSPIKQFLFLFFLSGGIFKFGiSGGGALPPHV----DTFFEAIGIEvlNGYGLTETSPVVSA 255
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1216630836 353 TPEGDDKPGAVGKVVPFFEAKVVDLDTGKTLGVNQRGELCVRGPMIMSGYVNNPEATNALIDKDGWLHSGDIAYWDEDEH 432
Cdd:cd17640 256 RRLKCNVRGSVGRPLPGTEIKIVDPEGNVVLPPGEKGIVWVRGPQVMKGYYKNPEATSKVLDSDGWFNTGDLGWLTCGGE 335
|
410 420 430 440
....*....|....*....|....*....|....*....|.
gi 1216630836 433 FFIVDRLKSLIKYK-GYQVAPAELESILLQHPNIFDAGVAG 472
Cdd:cd17640 336 LVLTGRAKDTIVLSnGENVEPQPIEEALMRSPFIEQIMVVG 376
|
|
| LC_FACS_bac |
cd05932 |
Bacterial long-chain fatty acid CoA synthetase (LC-FACS), including Marinobacter ... |
50-488 |
5.05e-32 |
|
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: 129.13 E-value: 5.05e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1216630836 50 VDITYAEYFEMSVRLAEAMKRYGLNTNHRIVVCSENSLQFFMPVLG---ALFIGVAVAPANDIYNERELLNSmgiSQPTV 126
Cdd:cd05932 5 VEFTWGEVADKARRLAAALRALGLEPGSKIALISKNCAEWFITDLAiwmAGHISVPLYPTLNPDTIRYVLEH---SESKA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1216630836 127 VFVSKkgLQKILNVQKKLP--IIQKII----IMDSKTDYQGFQSMYTFVTSHLPPGfneydfvpesfdrDKTIALIMNSS 200
Cdd:cd05932 82 LFVGK--LDDWKAMAPGVPegLISISLpppsAANCQYQWDDLIAQHPPLEERPTRF-------------PEQLATLIYTS 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1216630836 201 GSTGLPKGVAlpHRTACVRFSHARDpIFGNQIIPDTAILSVVPFHHGFG-MFTTLGYLICGFRVVlmyrFEEEL--FLRS 277
Cdd:cd05932 147 GTTGQPKGVM--LTFGSFAWAAQAG-IEHIGTEENDRMLSYLPLAHVTErVFVEGGSLYGGVLVA----FAESLdtFVED 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1216630836 278 LQDYKIQSALLVPTLFSFFAKStLIDKYDLSNLHEI--------------------------ASGGAPLSkevgEAVAKR 331
Cdd:cd05932 220 VQRARPTLFFSVPRLWTKFQQG-VQDKIPQQKLNLLlkipvvnslvkrkvlkglgldqcrlaGCGSAPVP----PALLEW 294
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1216630836 332 FHLPG--IRQGYGLTETTSAILITPEGDDKPGAVGKVVPFFEAKVVDldtgktlgvnqRGELCVRGPMIMSGYVNNPEAT 409
Cdd:cd05932 295 YRSLGlnILEAYGMTENFAYSHLNYPGRDKIGTVGNAGPGVEVRISE-----------DGEILVRSPALMMGYYKDPEAT 363
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1216630836 410 NALIDKDGWLHSGDIAYWDEDEHFFIVDRLKSLIKY-KGYQVAPAELESILLQHPNIFDAGV--AGLPDddagelPAAVV 486
Cdd:cd05932 364 AEAFTADGFLRTGDKGELDADGNLTITGRVKDIFKTsKGKYVAPAPIENKLAEHDRVEMVCVigSGLPA------PLALV 437
|
..
gi 1216630836 487 VL 488
Cdd:cd05932 438 VL 439
|
|
| LC_FACS_bac1 |
cd17641 |
bacterial long-chain fatty acid CoA synthetase; The members of this family are bacterial ... |
52-472 |
1.06e-31 |
|
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: 129.08 E-value: 1.06e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1216630836 52 ITYAEYFEMSVRLAEAMKRYGLNTNHRIVVCSENSLQFFMPVLGALFIG-VAVAPANDIYNER--ELLNSMGisqPTVVF 128
Cdd:cd17641 12 FTWADYADRVRAFALGLLALGVGRGDVVAILGDNRPEWVWAELAAQAIGaLSLGIYQDSMAEEvaYLLNYTG---ARVVI 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1216630836 129 VS-KKGLQKILNVQKKLPIIQKIIIMDSKTDYQGFQSMYTFVTSHLPPGFNEYDFVPESFDRD------KTIALIMNSSG 201
Cdd:cd17641 89 AEdEEQVDKLLEIADRIPSVRYVIYCDPRGMRKYDDPRLISFEDVVALGRALDRRDPGLYEREvaagkgEDVAVLCTTSG 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1216630836 202 STGLPKGVALPHRTAcvrFSHARDPIFGNQIIPDTAILSVVPFHH-GFGMFTTLGYLICGF------------------- 261
Cdd:cd17641 169 TTGKPKLAMLSHGNF---LGHCAAYLAADPLGPGDEYVSVLPLPWiGEQMYSVGQALVCGFivnfpeepetmmedlreig 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1216630836 262 -RVVL--------------------------MYRFEEELFLRSL-QDYKIQSALLVPTLFSFFAKSTLI----DKYDLSN 309
Cdd:cd17641 246 pTFVLlpprvwegiaadvrarmmdatpfkrfMFELGMKLGLRALdRGKRGRPVSLWLRLASWLADALLFrplrDRLGFSR 325
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1216630836 310 LHEIASGGAPLskevGEAVAKRFHLPGI--RQGYGLTETTSAILITPEGDDKPGAVGkvVPFFEAKVvdldtgktlGVNQ 387
Cdd:cd17641 326 LRSAATGGAAL----GPDTFRFFHAIGVplKQLYGQTELAGAYTVHRDGDVDPDTVG--VPFPGTEV---------RIDE 390
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1216630836 388 RGELCVRGPMIMSGYVNNPEATNALIDKDGWLHSGDIAYWDEDEHFFIVDRLKSLIK-YKGYQVAPAELESILLQHPNIF 466
Cdd:cd17641 391 VGEILVRSPGVFVGYYKNPEATAEDFDEDGWLHTGDAGYFKENGHLVVIDRAKDVGTtSDGTRFSPQFIENKLKFSPYIA 470
|
....*.
gi 1216630836 467 DAGVAG 472
Cdd:cd17641 471 EAVVLG 476
|
|
| ACSBG_like |
cd05933 |
Bubblegum-like very long-chain fatty acid CoA synthetase (VL-FACS); This family of very ... |
52-456 |
3.30e-31 |
|
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: 127.86 E-value: 3.30e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1216630836 52 ITYAEYFEMSVRLAEAMKRYGLNTNHRIVVCSENSLQFFMPVLGALFIG---VAVAPANDIYNERELLNSmgiSQPTVVF 128
Cdd:cd05933 9 LTYKEYYEACRQAAKAFLKLGLERFHGVGILGFNSPEWFIAAVGAIFAGgiaVGIYTTNSPEACQYVAET---SEANILV 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1216630836 129 V-SKKGLQKILNVQKKLPIIQKIII--------MDSKTDYQGFQSMYTFVTSHlppgfnEYDFVPESFDRDKTIALIMNS 199
Cdd:cd05933 86 VeNQKQLQKILQIQDKLPHLKAIIQykeplkekEPNLYSWDEFMELGRSIPDE------QLDAIISSQKPNQCCTLIYTS 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1216630836 200 sGSTGLPKGVALPHRT------ACVRFSHARDPIFGNQIIpdtaiLSVVPFHH----GFGMFTTL--------------- 254
Cdd:cd05933 160 -GTTGMPKGVMLSHDNitwtakAASQHMDLRPATVGQESV-----VSYLPLSHiaaqILDIWLPIkvggqvyfaqpdalk 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1216630836 255 GYLICGFRVV----------LMYRFEEELFLRSLQDYKIQSALLV-------------------PTLFSFFAKSTLIDK- 304
Cdd:cd05933 234 GTLVKTLREVrptafmgvprVWEKIQEKMKAVGAKSGTLKRKIASwakgvgletnlklmggespSPLFYRLAKKLVFKKv 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1216630836 305 ---YDLSNLHEIASGGAPLSKEVgeavaKRFHLP---GIRQGYGLTETTSAILITPEGDDKPGAVGKVVPFFEAKVVDLD 378
Cdd:cd05933 314 rkaLGLDRCQKFFTGAAPISRET-----LEFFLSlniPIMELYGMSETSGPHTISNPQAYRLLSCGKALPGCKTKIHNPD 388
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1216630836 379 TgktlgvNQRGELCVRGPMIMSGYVNNPEATNALIDKDGWLHSGDIAYWDEDEHFFIVDRLKSLIKYKGYQ-VAPAELE 456
Cdd:cd05933 389 A------DGIGEICFWGRHVFMGYLNMEDKTEEAIDEDGWLHSGDLGKLDEDGFLYITGRIKELIITAGGEnVPPVPIE 461
|
|
| A_NRPS_VisG_like |
cd17651 |
similar to adenylation domain of virginiamycin S synthetase; This family of the adenylation (A) ... |
35-534 |
6.70e-31 |
|
similar to adenylation domain of virginiamycin S synthetase; This family of the adenylation (A) domain of nonribosomal peptide synthases (NRPS) includes virginiamycin S synthetase (VisG) in Streptomyces virginiae; VisG is involved in virginiamycin S (VS) biosynthesis as the provider of an L-pheGly molecule, a highly specific substrate for the last condensation step by VisF. This family also includes linear gramicidin synthetase B (LgrB) in Brevibacillus brevis. Substrate specificity analysis using residues of the substrate-binding pockets of all 16 adenylation domains has shown good agreement of the substrate amino acids predicted with the sequence of linear gramicidin. The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester bond to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.
Pssm-ID: 341306 [Multi-domain] Cd Length: 491 Bit Score: 125.92 E-value: 6.70e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1216630836 35 ALVPGTIAFTDAHIEVdiTYAEYFEMSVRLAEAMKRYGLNTNHRIVVCSENSLQFFMPVLGALFIGVAVAPANDIYNERE 114
Cdd:cd17651 6 ARTPDAPALVAEGRRL--TYAELDRRANRLAHRLRARGVGPGDLVALCARRSAELVVALLAILKAGAAYVPLDPAYPAER 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1216630836 115 LLNSMGISQPTVVfVSKKGLQKILNVQKKLPIIQKIIIMDSKTDyqgfqsmytfvTSHLPPgfneydfvpesFDRDKTiA 194
Cdd:cd17651 84 LAFMLADAGPVLV-LTHPALAGELAVELVAVTLLDQPGAAAGAD-----------AEPDPA-----------LDADDL-A 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1216630836 195 LIMNSSGSTGLPKGVALPHRTAcVRFSHARDPIFGnqIIPDTAILSVVPFhhGFGMFT--TLGYLICGFRVVLM---YRF 269
Cdd:cd17651 140 YVIYTSGSTGRPKGVVMPHRSL-ANLVAWQARASS--LGPGARTLQFAGL--GFDVSVqeIFSTLCAGATLVLPpeeVRT 214
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1216630836 270 EEELFLRSLQDYKIQSALLVPTLFSFFAKSTLIDKYDLSNLHEIASGGAPLSkeVGEAVAKRF-HLPGIR--QGYGLTET 346
Cdd:cd17651 215 DPPALAAWLDEQRISRVFLPTVALRALAEHGRPLGVRLAALRYLLTGGEQLV--LTEDLREFCaGLPGLRlhNHYGPTET 292
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1216630836 347 TSAILITPEGD----DKPGAVGKVVPFFEAKVVDLDtGKTLGVNQRGELCVRGPMIMSGYVNNPEATNALIDKDGWL--- 419
Cdd:cd17651 293 HVVTALSLPGDpaawPAPPPIGRPIDNTRVYVLDAA-LRPVPPGVPGELYIGGAGLARGYLNRPELTAERFVPDPFVpga 371
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1216630836 420 ---HSGDIAYWDEDEHFFIVDRLKSLIKYKGYQVAPAELESILLQHPNIFDAGVAGLPDDDAGELPAAVVVLEHGKTMTE 496
Cdd:cd17651 372 rmyRTGDLARWLPDGELEFLGRADDQVKIRGFRIELGEIEAALARHPGVREAVVLAREDRPGEKRLVAYVVGDPEAPVDA 451
|
490 500 510
....*....|....*....|....*....|....*...
gi 1216630836 497 KEIVDYVASQVtTAKKLRGGVVFVDEVPKGLTGKLDAR 534
Cdd:cd17651 452 AELRAALATHL-PEYMVPSAFVLLDALPLTPNGKLDRR 488
|
|
| MACS_like_1 |
cd05974 |
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the ... |
268-538 |
7.86e-31 |
|
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: 124.60 E-value: 7.86e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1216630836 268 RFEEELFLRSLQDYKIQSALLVPTLFSFFAKSTLIdKYDLSnLHEIASGGAPLSKEVGEAVAKRFHLPgIRQGYGLTETT 347
Cdd:cd05974 162 RFDAKRVLAALVRYGVTTLCAPPTVWRMLIQQDLA-SFDVK-LREVVGAGEPLNPEVIEQVRRAWGLT-IRDGYGQTETT 238
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1216630836 348 SAILITPEGDDKPGAVGKVVPFFEAKVVDLDTGKTlgvnQRGELCV-----RGPMIMSGYVNNPEATNALIdKDGWLHSG 422
Cdd:cd05974 239 ALVGNSPGQPVKAGSMGRPLPGYRVALLDPDGAPA----TEGEVALdlgdtRPVGLMKGYAGDPDKTAHAM-RGGYYRTG 313
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1216630836 423 DIAYWDEDEHFFIVDRLKSLIKYKGYQVAPAELESILLQHPNIFDAGVAGLPDDDAGELPAAVVVLEHG---KTMTEKEI 499
Cdd:cd05974 314 DIAMRDEDGYLTYVGRADDVFKSSDYRISPFELESVLIEHPAVAEAAVVPSPDPVRLSVPKAFIVLRAGyepSPETALEI 393
|
250 260 270
....*....|....*....|....*....|....*....
gi 1216630836 500 VDYVASQVTTAKKLRgGVVFVdEVPKGLTGKLDARKIRE 538
Cdd:cd05974 394 FRFSRERLAPYKRIR-RLEFA-ELPKTISGKIRRVELRR 430
|
|
| A_NRPS_Bac |
cd17655 |
bacitracin synthetase and related proteins; This family of the adenylation (A) domain of ... |
52-538 |
1.45e-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: 1.45e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1216630836 52 ITYAEYFEMSVRLAEAMKRYGLNTNHRIVVCSENSLQFFMPVLGALFIGVAVAPANDIYNERELLNSMGISQPTVVFVSK 131
Cdd:cd17655 23 LTYRELNERANQLARTLREKGVGPDTIVGIMAERSLEMIVGILGILKAGGAYLPIDPDYPEERIQYILEDSGADILLTQS 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1216630836 132 KglqkilnVQKKLPIIQKIIIMDSKTdyqgfqsMYTFVTSHLPPGFNEYDfvpesfdrdktIALIMNSSGSTGLPKGVAL 211
Cdd:cd17655 103 H-------LQPPIAFIGLIDLLDEDT-------IYHEESENLEPVSKSDD-----------LAYVIYTSGSTGKPKGVMI 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1216630836 212 PHRtACVRFSHArdpiFGNQIIPDTA--ILSVVPFHHGFGMFTTLGYLICGFRVVLmYRFEE----ELFLRSLQDYKIQS 285
Cdd:cd17655 158 EHR-GVVNLVEW----ANKVIYQGEHlrVALFASISFDASVTEIFASLLSGNTLYI-VRKETvldgQALTQYIRQNRITI 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1216630836 286 ALLVPTLFSFFAKstlIDKYDLSNLHEIASGGAPLSKEVGEAVAKRFHL-PGIRQGYGLTETT---SAILITPEGDDKPG 361
Cdd:cd17655 232 IDLTPAHLKLLDA---ADDSEGLSLKHLIVGGEALSTELAKKIIELFGTnPTITNAYGPTETTvdaSIYQYEPETDQQVS 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1216630836 362 A-VGKvvPFFEAKVVDLDT-GKTLGVNQRGELCVRGPMIMSGYVNNPEATNALIDKDGWL------HSGDIAYWDEDEHF 433
Cdd:cd17655 309 VpIGK--PLGNTRIYILDQyGRPQPVGVAGELYIGGEGVARGYLNRPELTAEKFVDDPFVpgermyRTGDLARWLPDGNI 386
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1216630836 434 FIVDRLKSLIKYKGYQVAPAELESILLQHPNIFDAGVAGLPDDDAGELPAAVVVlehgktmTEKEIvdyVASQVTT--AK 511
Cdd:cd17655 387 EFLGRIDHQVKIRGYRIELGEIEARLLQHPDIKEAVVIARKDEQGQNYLCAYIV-------SEKEL---PVAQLREflAR 456
|
490 500 510
....*....|....*....|....*....|..
gi 1216630836 512 KLRGGVV---FV--DEVPKGLTGKLDARKIRE 538
Cdd:cd17655 457 ELPDYMIpsyFIklDEIPLTPNGKVDRKALPE 488
|
|
| PRK13382 |
PRK13382 |
bile acid CoA ligase; |
52-538 |
3.92e-30 |
|
bile acid CoA ligase;
Pssm-ID: 172019 [Multi-domain] Cd Length: 537 Bit Score: 124.10 E-value: 3.92e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1216630836 52 ITYAEYFEMSVRLAEAMKRYGLNTNHRIVVCSENSLQFFMPVLGALFIGVAVApandiynereLLNSMGISQPTVVFVSK 131
Cdd:PRK13382 69 LTWRELDERSDALAAALQALPIGEPRVVGIMCRNHRGFVEALLAANRIGADIL----------LLNTSFAGPALAEVVTR 138
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1216630836 132 KGLQKILNVQKKLPIIQKII--------IMDSkTDYQGFQSMYTFVTSHLPpgfneyDFVPESFDRDKTIALimnSSGST 203
Cdd:PRK13382 139 EGVDTVIYDEEFSATVDRALadcpqatrIVAW-TDEDHDLTVEVLIAAHAG------QRPEPTGRKGRVILL---TSGTT 208
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1216630836 204 GLPKGvalphrtacvrfshARDPIFGNqIIPDTAILSVVPFHHG------FGMFTTLGY--------LICgfRVVLMYRF 269
Cdd:PRK13382 209 GTPKG--------------ARRSGPGG-IGTLKAILDRTPWRAEeptvivAPMFHAWGFsqlvlaasLAC--TIVTRRRF 271
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1216630836 270 EEELFLRSLQDYKIQSALLVPTLFSFF--AKSTLIDKYDLSNLHEIASGGAPLSKEVGEAVAKRFHlPGIRQGYGLTETT 347
Cdd:PRK13382 272 DPEATLDLIDRHRATGLAVVPVMFDRImdLPAEVRNRYSGRSLRFAAASGSRMRPDVVIAFMDQFG-DVIYNNYNATEAG 350
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1216630836 348 SAILITPEGDDK-PGAVGKVVPFFEAKVVDLDtGKTLGVNQRGELCVRGPMIMSGYVnnPEATNALIDkdGWLHSGDIAY 426
Cdd:PRK13382 351 MIATATPADLRAaPDTAGRPAEGTEIRILDQD-FREVPTGEVGTIFVRNDTQFDGYT--SGSTKDFHD--GFMASGDVGY 425
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1216630836 427 WDEDEHFFIVDRLKSLIKYKGYQVAPAELESILLQHPNIFDAGVAGLPDDDAGELPAAVVVLEHGKTMTEKEIVDYVASQ 506
Cdd:PRK13382 426 LDENGRLFVVGRDDEMIVSGGENVYPIEVEKTLATHPDVAEAAVIGVDDEQYGQRLAAFVVLKPGASATPETLKQHVRDN 505
|
490 500 510
....*....|....*....|....*....|..
gi 1216630836 507 VTTAKKLRgGVVFVDEVPKGLTGKLDARKIRE 538
Cdd:PRK13382 506 LANYKVPR-DIVVLDELPRGATGKILRRELQA 536
|
|
| A_NRPS_Srf_like |
cd12117 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including Bacillus subtilis ... |
35-534 |
1.82e-29 |
|
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: 121.54 E-value: 1.82e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1216630836 35 ALVPGTIAFTDAhiEVDITYAEYFEMSVRLAEAMKRYGLNTNHRIVVCSENSLQFFMPVLGALFIGVAVAPANDIYNE-- 112
Cdd:cd12117 8 ARTPDAVAVVYG--DRSLTYAELNERANRLARRLRAAGVGPGDVVGVLAERSPELVVALLAVLKAGAAYVPLDPELPAer 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1216630836 113 -RELLNSmgiSQPTVVfVSKKGLQKILNVQKKLPIIQkiiimdsktdyqgfQSMYTFVTSHLPPGFNeydfvPESfdrdk 191
Cdd:cd12117 86 lAFMLAD---AGAKVL-LTDRSLAGRAGGLEVAVVID--------------EALDAGPAGNPAVPVS-----PDD----- 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1216630836 192 tIALIMNSSGSTGLPKGVALPHRtACVRFshARDPIFGnQIIPDTAILSVVPfhHGF--GMFTTLGYLICGFRVVLMyrf 269
Cdd:cd12117 138 -LAYVMYTSGSTGRPKGVAVTHR-GVVRL--VKNTNYV-TLGPDDRVLQTSP--LAFdaSTFEIWGALLNGARLVLA--- 207
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1216630836 270 EEELFL--RSLQDY----KIQSALLVPTLFSFFAKStliDKYDLSNLHEIASGGAPLS-KEVGEAVAkrfHLPGIR--QG 340
Cdd:cd12117 208 PKGTLLdpDALGALiaeeGVTVLWLTAALFNQLADE---DPECFAGLRELLTGGEVVSpPHVRRVLA---ACPGLRlvNG 281
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1216630836 341 YGLTETT--SAILITPEGDDKPGAV--GKVVPFFEAKVVDlDTGKTLGVNQRGELCVRGPMIMSGYVNNPEATNALIDKD 416
Cdd:cd12117 282 YGPTENTtfTTSHVVTELDEVAGSIpiGRPIANTRVYVLD-EDGRPVPPGVPGELYVGGDGLALGYLNRPALTAERFVAD 360
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1216630836 417 GWL------HSGDIAYWDEDEHFFIVDRLKSLIKYKGYQVAPAELESILLQHPNIFDAGVAGLPDDDAGELPAAVVVLEH 490
Cdd:cd12117 361 PFGpgerlyRTGDLARWLPDGRLEFLGRIDDQVKIRGFRIELGEIEAALRAHPGVREAVVVVREDAGGDKRLVAYVVAEG 440
|
490 500 510 520
....*....|....*....|....*....|....*....|....*....
gi 1216630836 491 GktmtekeiVDYVASQVTTAKKLRGG-----VVFVDEVPKGLTGKLDAR 534
Cdd:cd12117 441 A--------LDAAELRAFLRERLPAYmvpaaFVVLDELPLTANGKVDRR 481
|
|
| PRK07867 |
PRK07867 |
acyl-CoA synthetase; Validated |
181-538 |
1.89e-29 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236120 [Multi-domain] Cd Length: 529 Bit Score: 122.10 E-value: 1.89e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1216630836 181 DFVPESFDRDKTIALIMnSSGSTGLPKGVALPHRTACV-------RFSHARDpifgnqiipDTAILSVVPFHHGFGMFTT 253
Cdd:PRK07867 143 EPPFRVADPDDLFMLIF-TSGTSGDPKAVRCTHRKVASagvmlaqRFGLGPD---------DVCYVSMPLFHSNAVMAGW 212
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1216630836 254 LGYLICGFRVVLMYRFEEELFLRSLQDYKIQSALLVPTLFSF-FAKSTLIDkyDLSNLHEIASG--GAPLSKevgEAVAK 330
Cdd:PRK07867 213 AVALAAGASIALRRKFSASGFLPDVRRYGATYANYVGKPLSYvLATPERPD--DADNPLRIVYGneGAPGDI---ARFAR 287
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1216630836 331 RFhlpGIR--QGYGLTETtsAILITPEGDDKPGAVGKVVPffEAKVVDLDTGK------------TLGVNQRGELC-VRG 395
Cdd:PRK07867 288 RF---GCVvvDGFGSTEG--GVAITRTPDTPPGALGPLPP--GVAIVDPDTGTecppaedadgrlLNADEAIGELVnTAG 360
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1216630836 396 PMIMSGYVNNPEATNALIdKDGWLHSGDIAYWDEDEHFFIVDRLKSLIKYKGYQVAPAELESILLQHPNIFDAGVAGLPD 475
Cdd:PRK07867 361 PGGFEGYYNDPEADAERM-RGGVYWSGDLAYRDADGYAYFAGRLGDWMRVDGENLGTAPIERILLRYPDATEVAVYAVPD 439
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1216630836 476 DDAGELPAAVVVLEHGKTMTEKEIVDYVASQVTTAKKLRGGVV-FVDEVPKGLTGKLDARKIRE 538
Cdd:PRK07867 440 PVVGDQVMAALVLAPGAKFDPDAFAEFLAAQPDLGPKQWPSYVrVCAELPRTATFKVLKRQLSA 503
|
|
| PLN02479 |
PLN02479 |
acetate-CoA ligase |
31-549 |
2.56e-29 |
|
acetate-CoA ligase
Pssm-ID: 178097 [Multi-domain] Cd Length: 567 Bit Score: 121.88 E-value: 2.56e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1216630836 31 MKRYALVPGTIAfTDAHIEVDITYAEYFEMSVRLAEAMKRYGLNTNHRIVVCSENSLQFFMPVLGALFIGVAVAPANDIY 110
Cdd:PLN02479 26 LERAAVVHPTRK-SVVHGSVRYTWAQTYQRCRRLASALAKRSIGPGSTVAVIAPNIPAMYEAHFGVPMAGAVVNCVNIRL 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1216630836 111 NERELLNSMGISQPTVVFVSKK------GLQKILNVQK----KLPIIqkIIIMDSKTDYQGFQSM-------YTfvtSHL 173
Cdd:PLN02479 105 NAPTIAFLLEHSKSEVVMVDQEfftlaeEALKILAEKKkssfKPPLL--IVIGDPTCDPKSLQYAlgkgaieYE---KFL 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1216630836 174 PPGFNEYDFVPESfDRDKTIALIMnSSGSTGLPKGVALPHRTACVrFSHARDPIFGnqiIPDTAI-LSVVPFHHGFGM-F 251
Cdd:PLN02479 180 ETGDPEFAWKPPA-DEWQSIALGY-TSGTTASPKGVVLHHRGAYL-MALSNALIWG---MNEGAVyLWTLPMFHCNGWcF 253
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1216630836 252 TTLGYLICGFRVVLMYRFEEELFlRSLQDYKIQSALLVPTLFSFFAKSTLIDKY-DLSNLHEIASGGAPLSKEVGEAVAK 330
Cdd:PLN02479 254 TWTLAALCGTNICLRQVTAKAIY-SAIANYGVTHFCAAPVVLNTIVNAPKSETIlPLPRVVHVMTAGAAPPPSVLFAMSE 332
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1216630836 331 RfhlpGIR--QGYGLTET---TSAILITPEGDDKPGAVG---------KVVPFFEAKVVDLDTGKTLGVNQR--GELCVR 394
Cdd:PLN02479 333 K----GFRvtHTYGLSETygpSTVCAWKPEWDSLPPEEQarlnarqgvRYIGLEGLDVVDTKTMKPVPADGKtmGEIVMR 408
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1216630836 395 GPMIMSGYVNNPEAtNALIDKDGWLHSGDIAYWDEDEHFFIVDRLKSLIKYKGYQVAPAELESILLQHPNIFDAGVAGLP 474
Cdd:PLN02479 409 GNMVMKGYLKNPKA-NEEAFANGWFHSGDLGVKHPDGYIEIKDRSKDIIISGGENISSLEVENVVYTHPAVLEASVVARP 487
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1216630836 475 DDDAGELPAAVVVLEHG-----KTMTEKEIVDYVASQVtTAKKLRGGVVFvDEVPKGLTGKLDARKIREiliKAKKGGKI 549
Cdd:PLN02479 488 DERWGESPCAFVTLKPGvdksdEAALAEDIMKFCRERL-PAYWVPKSVVF-GPLPKTATGKIQKHVLRA---KAKEMGPV 562
|
|
| AACS_like |
cd05968 |
Uncharacterized acyl-CoA synthetase subfamily similar to Acetoacetyl-CoA synthetase; This ... |
52-541 |
2.76e-29 |
|
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: 122.21 E-value: 2.76e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1216630836 52 ITYAEYFEMSVRLAEAMKRYGLNTNHRIVVCSENSLQFFMPVLGALFIGVAVAPANDIYNERELLNSMGISQPTVVFV-- 129
Cdd:cd05968 92 LTYGELLYEVKRLANGLRALGVGKGDRVGIYLPMIPEIVPAFLAVARIGGIVVPIFSGFGKEAAATRLQDAEAKALITad 171
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1216630836 130 --SKKGlqKILNVQKKL-------PIIQKIIIM------DSKTDYqGFQSMYTFVTSHlPPGFneydfvpESFDRDKTIA 194
Cdd:cd05968 172 gfTRRG--REVNLKEEAdkacaqcPTVEKVVVVrhlgndFTPAKG-RDLSYDEEKETA-GDGA-------ERTESEDPLM 240
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1216630836 195 LIMnSSGSTGLPKGVAlpHRTACVRFSHARDPIFGNQIIPDTAILSVVPFHHGFGMFTTLGYLICGFRVVLM-----YRF 269
Cdd:cd05968 241 IIY-TSGTTGKPKGTV--HVHAGFPLKAAQDMYFQFDLKPGDLLTWFTDLGWMMGPWLIFGGLILGATMVLYdgapdHPK 317
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1216630836 270 EEELFlRSLQDYKIQSALLVPTLF-SFFAKST-LIDKYDLSNLHEIASGGAPLSKE----VGEAVAKRfHLPGIRQGYGl 343
Cdd:cd05968 318 ADRLW-RMVEDHEITHLGLSPTLIrALKPRGDaPVNAHDLSSLRVLGSTGEPWNPEpwnwLFETVGKG-RNPIINYSGG- 394
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1216630836 344 TETTSAIL----ITPEgddKPGAVGKVVPFFEAKVVDlDTGKTLgVNQRGELCVRGPMI-MS-GYVNNPEA-TNALIDK- 415
Cdd:cd05968 395 TEISGGILgnvlIKPI---KPSSFNGPVPGMKADVLD-ESGKPA-RPEVGELVLLAPWPgMTrGFWRDEDRyLETYWSRf 469
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1216630836 416 -DGWLHsGDIAYWDEDEHFFIVDRLKSLIKYKGYQVAPAELESILLQHPNIFDAGVAGLPDDDAGELPAAVVVLEHGKTM 494
Cdd:cd05968 470 dNVWVH-GDFAYYDEEGYFYILGRSDDTINVAGKRVGPAEIESVLNAHPAVLESAAIGVPHPVKGEAIVCFVVLKPGVTP 548
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|
gi 1216630836 495 TE---KEIVDYVASQVTTAKKLRgGVVFVDEVPKGLTGKLDARKIREILI 541
Cdd:cd05968 549 TEalaEELMERVADELGKPLSPE-RILFVKDLPKTRNAKVMRRVIRAAYL 597
|
|
| PRK08162 |
PRK08162 |
acyl-CoA synthetase; Validated |
31-551 |
2.72e-28 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236169 [Multi-domain] Cd Length: 545 Bit Score: 118.51 E-value: 2.72e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1216630836 31 MKRYALV-PGTIAFTdaHIEVDITYAEYFEMSVRLAEAMKRYGLNTNHRIVVCSENSlqffMPVLGALFiGVAVAPAndi 109
Cdd:PRK08162 24 LERAAEVyPDRPAVI--HGDRRRTWAETYARCRRLASALARRGIGRGDTVAVLLPNI----PAMVEAHF-GVPMAGA--- 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1216630836 110 ynereLLNSMGI--SQPTVVFVSKKGLQKILNV--------QKKLPII--QKIIIMD------------SKTDYQGFqsm 165
Cdd:PRK08162 94 -----VLNTLNTrlDAASIAFMLRHGEAKVLIVdtefaevaREALALLpgPKPLVIDvddpeypggrfiGALDYEAF--- 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1216630836 166 ytfvtshLPPGFNEYDFVPEsfdRDKTIALIMN-SSGSTGLPKGVALPHRTAcvrFSHArdpiFGNQI---IPDTAI-LS 240
Cdd:PRK08162 166 -------LASGDPDFAWTLP---ADEWDAIALNyTSGTTGNPKGVVYHHRGA---YLNA----LSNILawgMPKHPVyLW 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1216630836 241 VVP-FH-----HGFGMFTTLGYLICgfrvvlMYRFEEELFLRSLQDYKIQSALLVPTLFSFFAKSTLIDKYDLSNLHEIA 314
Cdd:PRK08162 229 TLPmFHcngwcFPWTVAARAGTNVC------LRKVDPKLIFDLIREHGVTHYCGAPIVLSALINAPAEWRAGIDHPVHAM 302
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1216630836 315 SGGAPLSKEVGEAVAKRfhlpGIR--QGYGLTET---TSAILITPEGDDKPG---AVGKV---VPFF---EAKVVDLDT- 379
Cdd:PRK08162 303 VAGAAPPAAVIAKMEEI----GFDltHVYGLTETygpATVCAWQPEWDALPLderAQLKArqgVRYPlqeGVTVLDPDTm 378
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1216630836 380 ------GKTLGvnqrgELCVRGPMIMSGYVNNPEATNALIdKDGWLHSGDIAYWDEDEHFFIVDRLKSLIKYKGYQVAPA 453
Cdd:PRK08162 379 qpvpadGETIG-----EIMFRGNIVMKGYLKNPKATEEAF-AGGWFHTGDLAVLHPDGYIKIKDRSKDIIISGGENISSI 452
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1216630836 454 ELESILLQHPNIFDAGVAGLPDDDAGELPAAVVVLEHGKTMTEKEIVDYVASQVTTAKKLRgGVVFvDEVPKGLTGKLDA 533
Cdd:PRK08162 453 EVEDVLYRHPAVLVAAVVAKPDPKWGEVPCAFVELKDGASATEEEIIAHCREHLAGFKVPK-AVVF-GELPKTSTGKIQK 530
|
570
....*....|....*...
gi 1216630836 534 RKIREiliKAKKGGKIAV 551
Cdd:PRK08162 531 FVLRE---QAKSLKAIDL 545
|
|
| A_NRPS_SidN3_like |
cd05918 |
The adenylation (A) domain of siderophore-synthesizing nonribosomal peptide synthetases (NRPS); ... |
200-540 |
5.19e-28 |
|
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: 117.26 E-value: 5.19e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1216630836 200 SGSTGLPKGVALPHRTACVRF-SHARdpIFGnqIIPDTAILSvvpF-HHGFG-----MFTTlgyLICGFRVVLMYrfEEE 272
Cdd:cd05918 115 SGSTGKPKGVVIEHRALSTSAlAHGR--ALG--LTSESRVLQ---FaSYTFDvsileIFTT---LAAGGCLCIPS--EED 182
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1216630836 273 L---FLRSLQDYKIQSALLVPTLFSffakstLIDKYDLSNLHEIASGGAPLSKEVGEAVAKRFHLpgiRQGYGLTETT-S 348
Cdd:cd05918 183 RlndLAGFINRLRVTWAFLTPSVAR------LLDPEDVPSLRTLVLGGEALTQSDVDTWADRVRL---INAYGPAECTiA 253
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1216630836 349 AILITPEGDDKPGAVGKVVPFFeAKVVDLDT-GKTLGVNQRGELCVRGPMIMSGYVNNPEATN-ALIDKDGWLH------ 420
Cdd:cd05918 254 ATVSPVVPSTDPRNIGRPLGAT-CWVVDPDNhDRLVPIGAVGELLIEGPILARGYLNDPEKTAaAFIEDPAWLKqegsgr 332
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1216630836 421 ------SGDIAYWDEDEHFFIVDRLKSLIKYKGYQVAPAELESILLQH-PNIFDAGVAGLPDDDAGELPAAVVVLEHGKT 493
Cdd:cd05918 333 grrlyrTGDLVRYNPDGSLEYVGRKDTQVKIRGQRVELGEIEHHLRQSlPGAKEVVVEVVKPKDGSSSPQLVAFVVLDGS 412
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1216630836 494 MTEK--------EIVDYVASQVTTAK-KLRGGV---------VFVDEVPKGLTGKLDARKIREIL 540
Cdd:cd05918 413 SSGSgdgdslflEPSDEFRALVAELRsKLRQRLpsymvpsvfLPLSHLPLTASGKIDRRALRELA 477
|
|
| PLN02736 |
PLN02736 |
long-chain acyl-CoA synthetase |
193-487 |
7.29e-27 |
|
long-chain acyl-CoA synthetase
Pssm-ID: 178337 [Multi-domain] Cd Length: 651 Bit Score: 115.20 E-value: 7.29e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1216630836 193 IALIMNSSGSTGLPKGVALPHRTACVRFSHARDPIfgnQIIPDTAILSVVPFHHGFGMFTTLGYLICGFRVvlmyRFEEE 272
Cdd:PLN02736 223 VATICYTSGTTGTPKGVVLTHGNLIANVAGSSLST---KFYPSDVHISYLPLAHIYERVNQIVMLHYGVAV----GFYQG 295
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1216630836 273 LFLRSLQDYkiqsALLVPTLFS-------------------------------FFAK----------STLIDKYDLSNLH 311
Cdd:PLN02736 296 DNLKLMDDL----AALRPTIFCsvprlynriydgitnavkesgglkerlfnaaYNAKkqalengknpSPMWDRLVFNKIK 371
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1216630836 312 E--------IASGGAPLSKEVGEAVakRFHLPG-IRQGYGLTETTSAILITPEGDDKPGAVGKVVPFFEAKVVDLDTGKT 382
Cdd:PLN02736 372 AklggrvrfMSSGASPLSPDVMEFL--RICFGGrVLEGYGMTETSCVISGMDEGDNLSGHVGSPNPACEVKLVDVPEMNY 449
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1216630836 383 LGVNQ---RGELCVRGPMIMSGYVNNPEATNALIDKDGWLHSGDIAYWDEDEHFFIVDRLKSLIKY-KGYQVAPAELESI 458
Cdd:PLN02736 450 TSEDQpypRGEICVRGPIIFKGYYKDEVQTREVIDEDGWLHTGDIGLWLPGGRLKIIDRKKNIFKLaQGEYIAPEKIENV 529
|
330 340
....*....|....*....|....*....
gi 1216630836 459 LLQHPNIFDAGVAGlpDDDAGELPAAVVV 487
Cdd:PLN02736 530 YAKCKFVAQCFVYG--DSLNSSLVAVVVV 556
|
|
| A_NRPS_GliP_like |
cd17653 |
nonribosomal peptide synthase GliP-like; This family includes the adenylation (A) domain of ... |
38-538 |
1.04e-26 |
|
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: 112.79 E-value: 1.04e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1216630836 38 PGTIAFTDAhiEVDITYAEYFEMSVRLAEAMKRYGLNTNHRIVVCSENSLQFFMPVLGALFIGVAVAPandiynerelln 117
Cdd:cd17653 11 PDAVAVESL--GGSLTYGELDAASNALANRLLQLGVVPGDVVPLLSDRSLEMLVAILAILKAGAAYVP------------ 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1216630836 118 smgisqptvvfvskkglqkilnVQKKLPIIQKIIIMDsktdyqgfQSMYTFVtshLPPgfneydfvpesfDRDKTIALIM 197
Cdd:cd17653 77 ----------------------LDAKLPSARIQAILR--------TSGATLL---LTT------------DSPDDLAYII 111
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1216630836 198 NSSGSTGLPKGVALPHR--TACVRFSHARdpiFGNQiiPDTAILSV--VPFHHGFG-MFTTLGYlicGFRVVLmyRFEEE 272
Cdd:cd17653 112 FTSGSTGIPKGVMVPHRgvLNYVSQPPAR---LDVG--PGSRVAQVlsIAFDACIGeIFSTLCN---GGTLVL--ADPSD 181
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1216630836 273 LFLRSLQdyKIQSALLVPTLFSffakstLIDKYDLSNLHEIASGGAPLSKEVGEAVAKRfhlPGIRQGYGLTETTSAILI 352
Cdd:cd17653 182 PFAHVAR--TVDALMSTPSILS------TLSPQDFPNLKTIFLGGEAVPPSLLDRWSPG---RRLYNAYGPTECTISSTM 250
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1216630836 353 TPEGDDKPGAVGKVVPffEAKVVDLDTGKTL-GVNQRGELCVRGPMIMSGYVNNPEATNA----LIDKDGWLH--SGDIA 425
Cdd:cd17653 251 TELLPGQPVTIGKPIP--NSTCYILDADLQPvPEGVVGEICISGVQVARGYLGNPALTASkfvpDPFWPGSRMyrTGDYG 328
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1216630836 426 YWDEDEHFFIVDRLKSLIKYKGYQVAPAELESILLQHPNIFDAGVAGLPDDdagELPAAVVvlehgktmteKEIVDYVAS 505
Cdd:cd17653 329 RWTEDGGLEFLGREDNQVKVRGFRINLEEIEEVVLQSQPEVTQAAAIVVNG---RLVAFVT----------PETVDVDGL 395
|
490 500 510
....*....|....*....|....*....|....*...
gi 1216630836 506 QVTTAKKLR-----GGVVFVDEVPKGLTGKLDARKIRE 538
Cdd:cd17653 396 RSELAKHLPsyavpDRIIALDSFPLTANGKVDRKALRE 433
|
|
| PRK06814 |
PRK06814 |
acyl-[ACP]--phospholipid O-acyltransferase; |
194-539 |
1.97e-26 |
|
acyl-[ACP]--phospholipid O-acyltransferase;
Pssm-ID: 235865 [Multi-domain] Cd Length: 1140 Bit Score: 114.29 E-value: 1.97e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1216630836 194 ALIMNSSGSTGLPKGVALPHR---------TACVRFsHARDPIFgnqiipdtailSVVPFHHGFGMFT-TLGYLICGFRV 263
Cdd:PRK06814 796 AVILFTSGSEGTPKGVVLSHRnllanraqvAARIDF-SPEDKVF-----------NALPVFHSFGLTGgLVLPLLSGVKV 863
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1216630836 264 VLM-----YRFEEELFlrslqdYKIQSALLV--PTLFSFFAKSTliDKYDLSNLHEIASGGAPLSKEVGEAVAKRFhlpG 336
Cdd:PRK06814 864 FLYpsplhYRIIPELI------YDTNATILFgtDTFLNGYARYA--HPYDFRSLRYVFAGAEKVKEETRQTWMEKF---G 932
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1216630836 337 IR--QGYGLTETTSAILITPEGDDKPGAVGKVVPFFEAKVVDLDtgktlGVNQRGELCVRGPMIMSGYV--NNPEATNAL 412
Cdd:PRK06814 933 IRilEGYGVTETAPVIALNTPMHNKAGTVGRLLPGIEYRLEPVP-----GIDEGGRLFVRGPNVMLGYLraENPGVLEPP 1007
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1216630836 413 idKDGWLHSGDIAYWDEDEHFFIVDRLKSLIKYKGYQVAPAELESILLQ-HPNIFDAGVAgLPDDDAGElpaAVVVLEHG 491
Cdd:PRK06814 1008 --ADGWYDTGDIVTIDEEGFITIKGRAKRFAKIAGEMISLAAVEELAAElWPDALHAAVS-IPDARKGE---RIILLTTA 1081
|
330 340 350 360
....*....|....*....|....*....|....*....|....*...
gi 1216630836 492 KTMTEKEIVDYVASQVTTAKKLRGGVVFVDEVPKGLTGKLDARKIREI 539
Cdd:PRK06814 1082 SDATRAAFLAHAKAAGASELMVPAEIITIDEIPLLGTGKIDYVAVTKL 1129
|
|
| A_NRPS_PvdJ-like |
cd17649 |
non-ribosomal peptide synthetase; This family of the adenylation (A) domain of nonribosomal ... |
53-534 |
4.92e-26 |
|
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: 110.92 E-value: 4.92e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1216630836 53 TYAEYFEMSVRLAEAMKRYGLNTNHRIVVCSENSLQFFMPVLGALFIGVAVAPAnDIYNERELLNSMgisqptvvfvskk 132
Cdd:cd17649 14 SYAELDARANRLAHRLRALGVGPEVRVGIALERSLEMVVALLAILKAGGAYVPL-DPEYPAERLRYM------------- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1216630836 133 glqkilnvqkklpiiqkiiIMDSKTdyqgfqsmyTFVTSHLPpgfneydfvpesfdrdKTIALIMNSSGSTGLPKGVALP 212
Cdd:cd17649 80 -------------------LEDSGA---------GLLLTHHP----------------RQLAYVIYTSGSTGTPKGVAVS 115
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1216630836 213 HrTACVRFSHARDPIFGnqIIPDTAILSVVPFHHGFGMFTTLGYLICGFRVVL----MYRFEEELfLRSLQDYKIQSALL 288
Cdd:cd17649 116 H-GPLAAHCQATAERYG--LTPGDRELQFASFNFDGAHEQLLPPLICGACVVLrpdeLWASADEL-AEMVRELGVTVLDL 191
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1216630836 289 VPTLFSFFAKSTLIDKYDL-SNLHEIASGGAPLSKEVgeavAKRFHLPGIR--QGYGLTETT-SAILITPEGDDKPGA-- 362
Cdd:cd17649 192 PPAYLQQLAEEADRTGDGRpPSLRLYIFGGEALSPEL----LRRWLKAPVRlfNAYGPTEATvTPLVWKCEAGAARAGas 267
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1216630836 363 --VGKVVPFFEAKVVDLDTGkTLGVNQRGELCVRGPMIMSGYVNNPEATNA--LIDKDG-----WLHSGDIAYWDEDEHF 433
Cdd:cd17649 268 mpIGRPLGGRSAYILDADLN-PVPVGVTGELYIGGEGLARGYLGRPELTAErfVPDPFGapgsrLYRTGDLARWRDDGVI 346
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1216630836 434 FIVDRLKSLIKYKGYQVAPAELESILLQHPNIFDAGVAGLPDDDAGELPAAVVV---------LEHGKTMTEKEIVDYVa 504
Cdd:cd17649 347 EYLGRVDHQVKIRGFRIELGEIEAALLEHPGVREAAVVALDGAGGKQLVAYVVLraaaaqpelRAQLRTALRASLPDYM- 425
|
490 500 510
....*....|....*....|....*....|
gi 1216630836 505 sqVTTAkklrggVVFVDEVPKGLTGKLDAR 534
Cdd:cd17649 426 --VPAH------LVFLARLPLTPNGKLDRK 447
|
|
| A_NRPS_Ta1_like |
cd12116 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including salinosporamide A ... |
38-535 |
7.23e-26 |
|
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: 110.84 E-value: 7.23e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1216630836 38 PGTIAFTDAHIEVdiTYAEYFEMSVRLAEAMKRYGLNTNHRIVVCSENSLQFFMPVLGALFIGVAVAPANDIY-NERell 116
Cdd:cd12116 1 PDATAVRDDDRSL--SYAELDERANRLAARLRARGVGPGDRVAVYLPRSARLVAAMLAVLKAGAAYVPLDPDYpADR--- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1216630836 117 nsmgisqptvvfvskkgLQKILNVQKKlpiiqKIIIMDSKTDYQGFQsmYTFVTSHLPPGFNEYDFVPESFDRDKTIALI 196
Cdd:cd12116 76 -----------------LRYILEDAEP-----ALVLTDDALPDRLPA--GLPVLLLALAAAAAAPAAPRTPVSPDDLAYV 131
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1216630836 197 MNSSGSTGLPKGVALPHRtACVRFSHA--RDPIFGnqiiPDTAILSVVPFhhGFGMFT--TLGYLICGFRVVLMYR---F 269
Cdd:cd12116 132 IYTSGSTGRPKGVVVSHR-NLVNFLHSmrERLGLG----PGDRLLAVTTY--AFDISLleLLLPLLAGARVVIAPRetqR 204
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1216630836 270 EEELFLRSLQDYKIQSALLVPTLFSFFAKSTLIDKYDLSNLheiaSGGAPLSkevgEAVAKRFHLPGIR--QGYGLTETT 347
Cdd:cd12116 205 DPEALARLIEAHSITVMQATPATWRMLLDAGWQGRAGLTAL----CGGEALP----PDLAARLLSRVGSlwNLYGPTETT 276
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1216630836 348 ---SAILITPEgdDKPGAVGKVVPFFEAKVVDlDTGKTLGVNQRGELCVRGPMIMSGYVNNPEATNALIDKDGWLHS--- 421
Cdd:cd12116 277 iwsTAARVTAA--AGPIPIGRPLANTQVYVLD-AALRPVPPGVPGELYIGGDGVAQGYLGRPALTAERFVPDPFAGPgsr 353
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1216630836 422 ----GDIAYWDEDEHFFIVDRLKSLIKYKGYQVAPAELESILLQHPNIFDAGVAGLPDDDAGELpAAVVVLEHGKTMTEK 497
Cdd:cd12116 354 lyrtGDLVRRRADGRLEYLGRADGQVKIRGHRIELGEIEAALAAHPGVAQAAVVVREDGGDRRL-VAYVVLKAGAAPDAA 432
|
490 500 510 520
....*....|....*....|....*....|....*....|...
gi 1216630836 498 EIVDYVASQ-----VTTAkklrggVVFVDEVPKGLTGKLDaRK 535
Cdd:cd12116 433 ALRAHLRATlpaymVPSA------FVRLDALPLTANGKLD-RK 468
|
|
| PRK08180 |
PRK08180 |
feruloyl-CoA synthase; Reviewed |
52-431 |
8.72e-26 |
|
feruloyl-CoA synthase; Reviewed
Pssm-ID: 236175 [Multi-domain] Cd Length: 614 Bit Score: 111.51 E-value: 8.72e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1216630836 52 ITYAEYFEMSVRLAEAMKRYGLNTNHRIVVCSENSLQFFMPVLGALFIGVAVAPANDIYNER-----ELLNSMGISQPTV 126
Cdd:PRK08180 70 LTYAEALERVRAIAQALLDRGLSAERPLMILSGNSIEHALLALAAMYAGVPYAPVSPAYSLVsqdfgKLRHVLELLTPGL 149
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1216630836 127 VFVS-----KKGLQKILNVQKKLPIIQKIIIMDSKTDYQgfqsmyTFVTSHLPPGfneydfVPESFDR--DKTIALIMNS 199
Cdd:PRK08180 150 VFADdgaafARALAAVVPADVEVVAVRGAVPGRAATPFA------ALLATPPTAA------VDAAHAAvgPDTIAKFLFT 217
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1216630836 200 SGSTGLPKGVALPHRTACV---------RFSHARDPIfgnqiipdtaILSVVPFHHGFGMFTTLGYlicgfrvVL----- 265
Cdd:PRK08180 218 SGSTGLPKAVINTHRMLCAnqqmlaqtfPFLAEEPPV----------LVDWLPWNHTFGGNHNLGI-------VLynggt 280
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1216630836 266 MY---------RFEEELflRSLQDykIQSALL--VPTLF---------------SFFakstlidkydlSNLHEIASGGAP 319
Cdd:PRK08180 281 LYiddgkptpgGFDETL--RNLRE--ISPTVYfnVPKGWemlvpalerdaalrrRFF-----------SRLKLLFYAGAA 345
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1216630836 320 LSKEVGE-----AVAKRFHLPGIRQGYGLTETTSAILITPEGDDKPGAVGKVVPFFEAKVVDLDtGKTlgvnqrgELCVR 394
Cdd:PRK08180 346 LSQDVWDrldrvAEATCGERIRMMTGLGMTETAPSATFTTGPLSRAGNIGLPAPGCEVKLVPVG-GKL-------EVRVK 417
|
410 420 430
....*....|....*....|....*....|....*...
gi 1216630836 395 GPMIMSGYVNNPEATNALIDKDGWLHSGDIAYW-DEDE 431
Cdd:PRK08180 418 GPNVTPGYWRAPELTAEAFDEEGYYRSGDAVRFvDPAD 455
|
|
| ACS-like |
cd17634 |
acetate-CoA ligase; This family includes acyl- and aryl-CoA ligases, as well as the ... |
52-531 |
1.03e-25 |
|
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: 111.13 E-value: 1.03e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1216630836 52 ITYAEYFEMSVRLAEAMKRYGLNTNHRIVVcsenslqfFMPV-------------LGALFIGV-------AVAPANDIYN 111
Cdd:cd17634 85 ISYRELHREVCRFAGTLLDLGVKKGDRVAI--------YMPMipeaavamlacarIGAVHSVIfggfapeAVAGRIIDSS 156
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1216630836 112 ERELLNSMGISQPTVVFVSKKGLQKILNVQkkLPIIQKIIIMD-SKTDYQGFQSM---YTFVTSHLPPGFNeydfvPESF 187
Cdd:cd17634 157 SRLLITADGGVRAGRSVPLKKNVDDALNPN--VTSVEHVIVLKrTGSDIDWQEGRdlwWRDLIAKASPEHQ-----PEAM 229
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1216630836 188 DRDKTIaLIMNSSGSTGLPKGVALPHR----TACVRFSHARDpIFGNQIIPDTAILSVVPFHHgfgmFTTLGYLICGFRV 263
Cdd:cd17634 230 NAEDPL-FILYTSGTTGKPKGVLHTTGgylvYAATTMKYVFD-YGPGDIYWCTADVGWVTGHS----YLLYGPLACGATT 303
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1216630836 264 VLmyrFE-------EELFLRSLQDYKIQSALLVPTLFSFFAKS--TLIDKYDLSNLHEIASGGAPLSKEVGEAVAKrfHL 334
Cdd:cd17634 304 LL---YEgvpnwptPARMWQVVDKHGVNILYTAPTAIRALMAAgdDAIEGTDRSSLRILGSVGEPINPEAYEWYWK--KI 378
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1216630836 335 PGIR----QGYGLTETTSAILITPEGDDKPGAVGKVVPFF--EAKVVDlDTGKTLGVNQRGELCVRGP---MIMSGYVNN 405
Cdd:cd17634 379 GKEKcpvvDTWWQTETGGFMITPLPGAIELKAGSATRPVFgvQPAVVD-NEGHPQPGGTEGNLVITDPwpgQTRTLFGDH 457
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1216630836 406 PEATNALIDK-DGWLHSGDIAYWDEDEHFFIVDRLKSLIKYKGYQVAPAELESILLQHPNIFDAGVAGLPDDDAGELPAA 484
Cdd:cd17634 458 ERFEQTYFSTfKGMYFSGDGARRDEDGYYWITGRSDDVINVAGHRLGTAEIESVLVAHPKVAEAAVVGIPHAIKGQAPYA 537
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|
gi 1216630836 485 VVVLEHGKTMTEK---EIVDYVASQVTTAKKLRgGVVFVDEVPKGLTGKL 531
Cdd:cd17634 538 YVVLNHGVEPSPElyaELRNWVRKEIGPLATPD-VVHWVDSLPKTRSGKI 586
|
|
| EntF |
COG1020 |
EntF, seryl-AMP synthase component of non-ribosomal peptide synthetase [Secondary metabolites ... |
200-489 |
1.23e-25 |
|
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: 112.26 E-value: 1.23e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1216630836 200 SGSTGLPKGVALPHRTAcVRFSHARDPIFGnqIIPDTAILSVVPFHHGFGMFTTLGYLICGFRVVLM---YRFEEELFLR 276
Cdd:COG1020 626 SGSTGRPKGVMVEHRAL-VNLLAWMQRRYG--LGPGDRVLQFASLSFDASVWEIFGALLSGATLVLAppeARRDPAALAE 702
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1216630836 277 SLQDYKIQSALLVPTLFsffakSTLID--KYDLSNLHEIASGGAPLSKEVGEAVAKRFhlPGIR--QGYGLTETT--SAI 350
Cdd:COG1020 703 LLARHRVTVLNLTPSLL-----RALLDaaPEALPSLRLVLVGGEALPPELVRRWRARL--PGARlvNLYGPTETTvdSTY 775
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1216630836 351 LITPEGDDKPGAV--GKVVPFFEAKVVDlDTGKTLGVNQRGELCVRGPMIMSGYVNNPEATNA-----LIDKDG--WLHS 421
Cdd:COG1020 776 YEVTPPDADGGSVpiGRPIANTRVYVLD-AHLQPVPVGVPGELYIGGAGLARGYLNRPELTAErfvadPFGFPGarLYRT 854
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1216630836 422 GDIAYWDEDEHFFIVDRLKSLIKYKGYQVAPAELESILLQHPNIFDAGVAGLPDDDAGELPAAVVVLE 489
Cdd:COG1020 855 GDLARWLPDGNLEFLGRADDQVKIRGFRIELGEIEAALLQHPGVREAVVVAREDAPGDKRLVAYVVPE 922
|
|
| A_NRPS_Sfm_like |
cd12115 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including Saframycin A gene ... |
194-532 |
2.68e-25 |
|
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: 108.56 E-value: 2.68e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1216630836 194 ALIMNSSGSTGLPKGVALPHRTACVRFSHARDpIFG----NQIIPDTAI---LSVvpfhhgFGMFTTLGyliCGFRVVLM 266
Cdd:cd12115 108 AYVIYTSGSTGRPKGVAIEHRNAAAFLQWAAA-AFSaeelAGVLASTSIcfdLSV------FELFGPLA---TGGKVVLA 177
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1216630836 267 yrfEEELFLRSLQDYKiQSALL--VPTlfsffAKSTLIDKYDL-SNLHEIASGGAPLSKEVGEAVAKRFHLPGIRQGYGL 343
Cdd:cd12115 178 ---DNVLALPDLPAAA-EVTLIntVPS-----AAAELLRHDALpASVRVVNLAGEPLPRDLVQRLYARLQVERVVNLYGP 248
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1216630836 344 TETT--SAILITPEGDDKPGAVGKVVPFFEAKVVDlDTGKTLGVNQRGELCVRGPMIMSGYVNNPEATNALIDKDGWL-- 419
Cdd:cd12115 249 SEDTtySTVAPVPPGASGEVSIGRPLANTQAYVLD-RALQPVPLGVPGELYIGGAGVARGYLGRPGLTAERFLPDPFGpg 327
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1216630836 420 ----HSGDIAYWDEDEHFFIVDRLKSLIKYKGYQVAPAELESILLQHPNIFDAGVAGLPDDDAGELPAAVVVLEHGKTMT 495
Cdd:cd12115 328 arlyRTGDLVRWRPDGLLEFLGRADNQVKVRGFRIELGEIEAALRSIPGVREAVVVAIGDAAGERRLVAYIVAEPGAAGL 407
|
330 340 350
....*....|....*....|....*....|....*..
gi 1216630836 496 EKEIVDYVAsQVTTAKKLRGGVVFVDEVPKGLTGKLD 532
Cdd:cd12115 408 VEDLRRHLG-TRLPAYMVPSRFVRLDALPLTPNGKID 443
|
|
| PRK05857 |
PRK05857 |
fatty acid--CoA ligase; |
27-551 |
5.27e-25 |
|
fatty acid--CoA ligase;
Pssm-ID: 180293 [Multi-domain] Cd Length: 540 Bit Score: 108.94 E-value: 5.27e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1216630836 27 LHKAMKRYALVPGTIAFTDAHIEVDITYAEYFEMSVRLAEAMKRYGLNTNHRIVVCSENSLQFFMPVLGALFIGVAVAPA 106
Cdd:PRK05857 17 LDRVFEQARQQPEAIALRRCDGTSALRYRELVAEVGGLAADLRAQSVSRGSRVLVISDNGPETYLSVLACAKLGAIAVMA 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1216630836 107 NDIYNERELLNSMGISQPTVVFV---SKKGLQKILNVQKKLPIIQKIIIMDSKTDYQGFQSMYtfvtshlPPGFNEYDfv 183
Cdd:PRK05857 97 DGNLPIAAIERFCQITDPAAALVapgSKMASSAVPEALHSIPVIAVDIAAVTRESEHSLDAAS-------LAGNADQG-- 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1216630836 184 pesfdRDKTIALIMnSSGSTGLPKGVALPHRT--ACVRFSHARDPIFGNQIIPDTAiLSVVPFHHGFGMFTTLGYLICGf 261
Cdd:PRK05857 168 -----SEDPLAMIF-TSGTTGEPKAVLLANRTffAVPDILQKEGLNWVTWVVGETT-YSPLPATHIGGLWWILTCLMHG- 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1216630836 262 rVVLMYRFEEELFLRS-LQDYKIQSALLVPTLFSFFAKSTLIDKYDLSNLHEIASGGaplSKEVGEAVakRF-HLPGIR- 338
Cdd:PRK05857 240 -GLCVTGGENTTSLLEiLTTNAVATTCLVPTLLSKLVSELKSANATVPSLRLVGYGG---SRAIAADV--RFiEATGVRt 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1216630836 339 -QGYGLTETTSAILITPEGDD-----KPGAVGKVVPFFEAKVVDLDTG-----KTLGVNQRGELCVRGPMIMSGYVNNPE 407
Cdd:PRK05857 314 aQVYGLSETGCTALCLPTDDGsivkiEAGAVGRPYPGVDVYLAATDGIgptapGAGPSASFGTLWIKSPANMLGYWNNPE 393
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1216630836 408 ATNALIdKDGWLHSGDIAYWDEDEHFFIVDRLKSLIKYKGYQVAPAELESILLQHPNIFDAGVAGLPDDDAGELPAAVVV 487
Cdd:PRK05857 394 RTAEVL-IDGWVNTGDLLERREDGFFYIKGRSSEMIICGGVNIAPDEVDRIAEGVSGVREAACYEIPDEEFGALVGLAVV 472
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1216630836 488 lehgkTMTEKEIVDYVASQVTTAKKLR---------GGVVFVDEVPKGLTGKLdarkIREILIKAKKGGKIAV 551
Cdd:PRK05857 473 -----ASAELDESAARALKHTIAARFRresepmarpSTIVIVTDIPRTQSGKV----MRASLAAAATADKARV 536
|
|
| A_NRPS_CmdD_like |
cd17652 |
similar to adenylation domain of chondramide synthase cmdD; This family of the adenylation (A) ... |
194-535 |
9.22e-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: 106.95 E-value: 9.22e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1216630836 194 ALIMNSSGSTGLPKGVALPHRTACvrfSHARDPIFGNQIIPDTAILSVVPFHHGFGMFTTLGYLICGFRVVLMYRfeEEL 273
Cdd:cd17652 96 AYVIYTSGSTGRPKGVVVTHRGLA---NLAAAQIAAFDVGPGSRVLQFASPSFDASVWELLMALLAGATLVLAPA--EEL 170
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1216630836 274 -----FLRSLQDYKIQSALLVPTLFSffakstLIDKYDLSNLHEIASGGAPLSKEvgeaVAKRFHlPGIR--QGYGLTET 346
Cdd:cd17652 171 lpgepLADLLREHRITHVTLPPAALA------ALPPDDLPDLRTLVVAGEACPAE----LVDRWA-PGRRmiNAYGPTET 239
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1216630836 347 T-SAILITPEGDDKPGAVGKVVPFFEAKVVDlDTGKTLGVNQRGELCVRGPMIMSGYVNNPEAT------NALIDKDGWL 419
Cdd:cd17652 240 TvCATMAGPLPGGGVPPIGRPVPGTRVYVLD-ARLRPVPPGVPGELYIAGAGLARGYLNRPGLTaerfvaDPFGAPGSRM 318
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1216630836 420 H-SGDIAYWDEDEHFFIVDRLKSLIKYKGYQVAPAELESILLQHPNIFDAgVAGLPDDDAGE--LpAAVVVLEHGKTMTE 496
Cdd:cd17652 319 YrTGDLARWRADGQLEFLGRADDQVKIRGFRIELGEVEAALTEHPGVAEA-VVVVRDDRPGDkrL-VAYVVPAPGAAPTA 396
|
330 340 350
....*....|....*....|....*....|....*....
gi 1216630836 497 KEIVDYVASQVtTAKKLRGGVVFVDEVPKGLTGKLDARK 535
Cdd:cd17652 397 AELRAHLAERL-PGYMVPAAFVVLDALPLTPNGKLDRRA 434
|
|
| PTZ00216 |
PTZ00216 |
acyl-CoA synthetase; Provisional |
308-463 |
1.11e-24 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 240316 [Multi-domain] Cd Length: 700 Bit Score: 108.53 E-value: 1.11e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1216630836 308 SNLHEIASGGAPLSKEVGEAVAKRFHLpgIRQGYGLTETT--SAILITpeGDDKPGAVGKVVPFFEAKVVDLDTGK-TLG 384
Cdd:PTZ00216 428 GRVRAMLSGGGPLSAATQEFVNVVFGM--VIQGWGLTETVccGGIQRT--GDLEPNAVGQLLKGVEMKLLDTEEYKhTDT 503
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1216630836 385 VNQRGELCVRGPMIMSGYVNNPEATNALIDKDGWLHSGDIAYWDEDEHFFIVDRLKSLIK-YKGYQVAPAELESILLQHP 463
Cdd:PTZ00216 504 PEPRGEILLRGPFLFKGYYKQEELTREVLDEDGWFHTGDVGSIAANGTLRIIGRVKALAKnCLGEYIALEALEALYGQNE 583
|
|
| entE |
PRK10946 |
(2,3-dihydroxybenzoyl)adenylate synthase; |
38-540 |
1.39e-24 |
|
(2,3-dihydroxybenzoyl)adenylate synthase;
Pssm-ID: 236803 [Multi-domain] Cd Length: 536 Bit Score: 107.38 E-value: 1.39e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1216630836 38 PGTIAFTDAhiEVDITYAEYFEMSVRLAEAMKRYGLNTNHRIVVCSENSLQFFMPVLGALFIGVAvaPANDIYNEREL-L 116
Cdd:PRK10946 37 SDAIAVICG--ERQFSYRELNQASDNLACSLRRQGIKPGDTALVQLGNVAEFYITFFALLKLGVA--PVNALFSHQRSeL 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1216630836 117 NSMGIS-QPTVVFVSKK-----GLQKILNVQKKLPIIQkIIIMDSKTDYQGFQSmytfVTSHLPPGFneyDFVPESFDRd 190
Cdd:PRK10946 113 NAYASQiEPALLIADRQhalfsDDDFLNTLVAEHSSLR-VVLLLNDDGEHSLDD----AINHPAEDF---TATPSPADE- 183
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1216630836 191 ktIALIMNSSGSTGLPKgvaLPHRTA-----CVRFShardpifgNQII---PDTAILSVVPFHHGFGMFT--TLGYLICG 260
Cdd:PRK10946 184 --VAFFQLSGGSTGTPK---LIPRTHndyyySVRRS--------VEICgftPQTRYLCALPAAHNYPMSSpgALGVFLAG 250
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1216630836 261 FRVVLMYRFEEELFLRSLQDYKIQSALLVPTLFSFF--AKSTLIDKYDLSNLHEIASGGAPLSkevgEAVAKRfhLPG-- 336
Cdd:PRK10946 251 GTVVLAPDPSATLCFPLIEKHQVNVTALVPPAVSLWlqAIAEGGSRAQLASLKLLQVGGARLS----ETLARR--IPAel 324
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1216630836 337 ---IRQGYGLTE---------TTSAILITPEG-----DDkpgavgkvvpffEAKVVDLDtGKTLGVNQRGELCVRGPMIM 399
Cdd:PRK10946 325 gcqLQQVFGMAEglvnytrldDSDERIFTTQGrpmspDD------------EVWVADAD-GNPLPQGEVGRLMTRGPYTF 391
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1216630836 400 SGYVNNPEATNALIDKDGWLHSGDIAYWDEDEHFFIVDRLKSLIKYKGYQVAPAELESILLQHPNIFDAGVAGLPDDDAG 479
Cdd:PRK10946 392 RGYYKSPQHNASAFDANGFYCSGDLVSIDPDGYITVVGREKDQINRGGEKIAAEEIENLLLRHPAVIHAALVSMEDELMG 471
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1216630836 480 ELPAAVVVLEHG-------KTMTEKEIVDYvasqvttakKLRGGVVFVDEVPKGLTGKLDARKIREIL 540
Cdd:PRK10946 472 EKSCAFLVVKEPlkavqlrRFLREQGIAEF---------KLPDRVECVDSLPLTAVGKVDKKQLRQWL 530
|
|
| PRK09192 |
PRK09192 |
fatty acyl-AMP ligase; |
193-543 |
1.51e-24 |
|
fatty acyl-AMP ligase;
Pssm-ID: 236403 [Multi-domain] Cd Length: 579 Bit Score: 107.40 E-value: 1.51e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1216630836 193 IALIMNSSGSTGLPKGVALPHRT--ACVRfSHARDpifGNQIIPDTAILSVVPFHHGFGMfttLGYLI----CGFRVVLM 266
Cdd:PRK09192 178 IAYLQYSSGSTRFPRGVIITHRAlmANLR-AISHD---GLKVRPGDRCVSWLPFYHDMGL---VGFLLtpvaTQLSVDYL 250
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1216630836 267 YrfEEELFLRSLQDYKIQS----ALLVPTLFSF-----FAKSTLIDKYDLSNLHEIASGGAPLSKEVGEAVAKRFHLPGI 337
Cdd:PRK09192 251 P--TRDFARRPLQWLDLISrnrgTISYSPPFGYelcarRVNSKDLAELDLSCWRVAGIGADMIRPDVLHQFAEAFAPAGF 328
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1216630836 338 RQ-----GYGLTETTSAILITPEG----------------------DDKPGAV------GKVVPFFEAKVVDlDTGKTLG 384
Cdd:PRK09192 329 DDkafmpSYGLAEATLAVSFSPLGsgivveevdrdrleyqgkavapGAETRRVrtfvncGKALPGHEIEIRN-EAGMPLP 407
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1216630836 385 VNQRGELCVRGPMIMSGYVNNPEATNALiDKDGWLHSGDIAYWDEDEhFFIVDRLKSLIKYKGYQVAPAELESILLQHPN 464
Cdd:PRK09192 408 ERVVGHICVRGPSLMSGYFRDEESQDVL-AADGWLDTGDLGYLLDGY-LYITGRAKDLIIINGRNIWPQDIEWIAEQEPE 485
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1216630836 465 IF--DAGVAGLPDDDaGELPAAVVVLEHGKTMTEKEIVDYVASQVTTAKKLRGGVVFV--DEVPKGLTGKLDARKIREIL 540
Cdd:PRK09192 486 LRsgDAAAFSIAQEN-GEKIVLLVQCRISDEERRGQLIHALAALVRSEFGVEAAVELVppHSLPRTSSGKLSRAKAKKRY 564
|
...
gi 1216630836 541 IKA 543
Cdd:PRK09192 565 LSG 567
|
|
| PLN02430 |
PLN02430 |
long-chain-fatty-acid-CoA ligase |
182-494 |
1.60e-24 |
|
long-chain-fatty-acid-CoA ligase
Pssm-ID: 178049 [Multi-domain] Cd Length: 660 Bit Score: 107.98 E-value: 1.60e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1216630836 182 FVPESFDrdktIALIMNSSGSTGLPKGVALPHRT--ACVRFSHARDPIFGNQIIPDTAILSVVPFHHgfgmfttlgylic 259
Cdd:PLN02430 215 NPPKPLD----ICTIMYTSGTSGDPKGVVLTHEAvaTFVRGVDLFMEQFEDKMTHDDVYLSFLPLAH------------- 277
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1216630836 260 gfrvvLMYRFEEELFLRS-----------------LQDYK-----------------IQSAL--LVPTLFSFFaksTLID 303
Cdd:PLN02430 278 -----ILDRMIEEYFFRKgasvgyyhgdlnalrddLMELKptllagvprvferihegIQKALqeLNPRRRLIF---NALY 349
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1216630836 304 KYDLSNLHE-----------------------------IASGGAPLSKEVgEAVAKRFHLPGIRQGYGLTETTSAILIT- 353
Cdd:PLN02430 350 KYKLAWMNRgyshkkaspmadflafrkvkaklggrlrlLISGGAPLSTEI-EEFLRVTSCAFVVQGYGLTETLGPTTLGf 428
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1216630836 354 PEGDDKPGAVGKVVPFFEAKVVDL-DTG-KTLGVNQRGELCVRGPMIMSGYVNNPEATNALIdKDGWLHSGDIAYWDEDE 431
Cdd:PLN02430 429 PDEMCMLGTVGAPAVYNELRLEEVpEMGyDPLGEPPRGEICVRGKCLFSGYYKNPELTEEVM-KDGWFHTGDIGEILPNG 507
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1216630836 432 HFFIVDRLKSLIKY-KGYQVAPAELESILLQHPNIFDAGVAGlpdDDAGELPAAVVVLEHGKTM 494
Cdd:PLN02430 508 VLKIIDRKKNLIKLsQGEYVALEYLENVYGQNPIVEDIWVYG---DSFKSMLVAVVVPNEENTN 568
|
|
| PRK13388 |
PRK13388 |
acyl-CoA synthetase; Provisional |
191-538 |
1.75e-24 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 237374 [Multi-domain] Cd Length: 540 Bit Score: 107.03 E-value: 1.75e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1216630836 191 KTIALIMNSSGSTGLPKGVALPH-------RTACVRFSHARDpifgnqiipDTAILSVVPFHHGFGMFTTLGYLICGFRV 263
Cdd:PRK13388 150 MDPFMLIFTSGTTGAPKAVRCSHgrlafagRALTERFGLTRD---------DVCYVSMPLFHSNAVMAGWAPAVASGAAV 220
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1216630836 264 VLMYRFEEELFLRSLQDYKIqsallvpTLFSFFAK------STLIDKYDLSNLHEIASGGAPlSKEVGEAVAKRFhlpGI 337
Cdd:PRK13388 221 ALPAKFSASGFLDDVRRYGA-------TYFNYVGKplayilATPERPDDADNPLRVAFGNEA-SPRDIAEFSRRF---GC 289
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1216630836 338 R--QGYGLTETtsAILITPEGDDKPGAVGKvvPFFEAKVVDLDTGKT-----LGVNQR--------GELCVR-GPMIMSG 401
Cdd:PRK13388 290 QveDGYGSSEG--AVIVVREPGTPPGSIGR--GAPGVAIYNPETLTEcavarFDAHGAllnadeaiGELVNTaGAGFFEG 365
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1216630836 402 YVNNPEATNALIdKDGWLHSGDIAYWDEDEHFFIVDRLKSLIKYKGYQVAPAELESILLQHPNIFDAGVAGLPDDDAGEL 481
Cdd:PRK13388 366 YYNNPEATAERM-RHGMYWSGDLAYRDADGWIYFAGRTADWMRVDGENLSAAPIERILLRHPAINRVAVYAVPDERVGDQ 444
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*...
gi 1216630836 482 PAAVVVLEHGKTMTEKEIVDYVASQVTTAKKLRGGVVFV-DEVPKGLTGKLDARKIRE 538
Cdd:PRK13388 445 VMAALVLRDGATFDPDAFAAFLAAQPDLGTKAWPRYVRIaADLPSTATNKVLKRELIA 502
|
|
| FCS |
cd05921 |
Feruloyl-CoA synthetase (FCS); Feruloyl-CoA synthetase is an essential enzyme in the feruloyl ... |
52-425 |
1.22e-23 |
|
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: 104.82 E-value: 1.22e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1216630836 52 ITYAEYFEMSVRLAEAMKRYGLNTNHRIVVCSENSLQFFMPVLGALFIGVAVAPANDIY-----NERELLNSMGISQPTV 126
Cdd:cd05921 26 VTYAEALRQVRAIAQGLLDLGLSAERPLLILSGNSIEHALMALAAMYAGVPAAPVSPAYslmsqDLAKLKHLFELLKPGL 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1216630836 127 VFVS-----KKGLQKILNVQKKLPIIQKIIIMDSKTDYQGFqsmytfvtSHLPPGFNeydfVPESFDR--DKTIALIMNS 199
Cdd:cd05921 106 VFAQdaapfARALAAIFPLGTPLVVSRNAVAGRGAISFAEL--------AATPPTAA----VDAAFAAvgPDTVAKFLFT 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1216630836 200 SGSTGLPKGVALPHRTACVRFSHARD--PIFGNqiiPDTAILSVVPFHHGFGMFTtlgylicGFRVVL-----MY----- 267
Cdd:cd05921 174 SGSTGLPKAVINTQRMLCANQAMLEQtyPFFGE---EPPVLVDWLPWNHTFGGNH-------NFNLVLynggtLYiddgk 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1216630836 268 ----RFEEELflRSLQDYKIQSALLVPTLFSFFAK-----STLIDKYdLSNLHEIASGGAPLSKEVGE-----AVAKRFH 333
Cdd:cd05921 244 pmpgGFEETL--RNLREISPTVYFNVPAGWEMLVAalekdEALRRRF-FKRLKLMFYAGAGLSQDVWDrlqalAVATVGE 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1216630836 334 LPGIRQGYGLTETTSAILITPEGDDKPGAVGKVVPFFEAKVVDLDtGKTlgvnqrgELCVRGPMIMSGYVNNPEATNALI 413
Cdd:cd05921 321 RIPMMAGLGATETAPTATFTHWPTERSGLIGLPAPGTELKLVPSG-GKY-------EVRVKGPNVTPGYWRQPELTAQAF 392
|
410
....*....|..
gi 1216630836 414 DKDGWLHSGDIA 425
Cdd:cd05921 393 DEEGFYCLGDAA 404
|
|
| PTZ00237 |
PTZ00237 |
acetyl-CoA synthetase; Provisional |
196-542 |
1.57e-23 |
|
acetyl-CoA synthetase; Provisional
Pssm-ID: 240325 [Multi-domain] Cd Length: 647 Bit Score: 104.82 E-value: 1.57e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1216630836 196 IMNSSGSTGLPKGVAL---PHRTACVRFSHARDPIFGNQIIPDTAILSVVPFHHGFGMFTTLGYLICGFRV-VLMYRFEE 271
Cdd:PTZ00237 259 ILYTSGTTGNSKAVVRsngPHLVGLKYYWRSIIEKDIPTVVFSHSSIGWVSFHGFLYGSLSLGNTFVMFEGgIIKNKHIE 338
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1216630836 272 ELFLRSLQDYKIQSALLVPTLFSFFAK-----STLIDKYDLSNLHEIASGGAPLSKEVGEAVAKRFHLPGIRqGYGLTET 346
Cdd:PTZ00237 339 DDLWNTIEKHKVTHTLTLPKTIRYLIKtdpeaTIIRSKYDLSNLKEIWCGGEVIEESIPEYIENKLKIKSSR-GYGQTEI 417
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1216630836 347 TSAILITPEGDDKP-GAVGKVVPFFEAKVVDLDtGKTLGVNQRGELCVRGPM---IMSGYVNNPEATNALIDK-DGWLHS 421
Cdd:PTZ00237 418 GITYLYCYGHINIPyNATGVPSIFIKPSILSED-GKELNVNEIGEVAFKLPMppsFATTFYKNDEKFKQLFSKfPGYYNS 496
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1216630836 422 GDIAYWDEDEHFFIVDRLKSLIKYKGYQVAPAELESILLQHPNIFDAGVAGLPDDDAGELPAAVVVLEHGKTMT------ 495
Cdd:PTZ00237 497 GDLGFKDENGYYTIVSRSDDQIKISGNKVQLNTIETSILKHPLVLECCSIGIYDPDCYNVPIGLLVLKQDQSNQsidlnk 576
|
330 340 350 360
....*....|....*....|....*....|....*....|....*...
gi 1216630836 496 -EKEIVDYVASQVTTAKKLRgGVVFVDEVPKGLTGKLdarkIREILIK 542
Cdd:PTZ00237 577 lKNEINNIITQDIESLAVLR-KIIIVNQLPKTKTGKI----PRQIISK 619
|
|
| A_NRPS_Cytc1-like |
cd17643 |
similar to adenylation domain of cytotrienin synthetase CytC1; This family of the adenylation ... |
194-532 |
1.66e-23 |
|
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: 103.54 E-value: 1.66e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1216630836 194 ALIMNSSGSTGLPKGVALPHRTACVRFSHARDPI-FGNQiipDtailSVVPFHH---GFGMFTTLGYLICGFRVVLM--- 266
Cdd:cd17643 96 AYVIYTSGSTGRPKGVVVSHANVLALFAATQRWFgFNED---D----VWTLFHSyafDFSVWEIWGALLHGGRLVVVpye 168
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1216630836 267 YRFEEELFLRSLQDYKIQSALLVPTLFSFFAKSTLIDKYDLSNLHEIASGGAPLSKEVGEAVAKRFHLPGIR--QGYGLT 344
Cdd:cd17643 169 VARSPEDFARLLRDEGVTVLNQTPSAFYQLVEAADRDGRDPLALRYVIFGGEALEAAMLRPWAGRFGLDRPQlvNMYGIT 248
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1216630836 345 ETT---SAILITPegDDKPGA----VGKVVPFFEAKVVDlDTGKTLGVNQRGELCVRGPMIMSGYVNNPEATNA--LIDK 415
Cdd:cd17643 249 ETTvhvTFRPLDA--ADLPAAaaspIGRPLPGLRVYVLD-ADGRPVPPGVVGELYVSGAGVARGYLGRPELTAErfVANP 325
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1216630836 416 DG-----WLHSGDIAYWDEDEHFFIVDRLKSLIKYKGYQVAPAELESILLQHPNIFDAGVAGLPDDDAGELPAAVVVLEH 490
Cdd:cd17643 326 FGgpgsrMYRTGDLARRLPDGELEYLGRADEQVKIRGFRIELGEIEAALATHPSVRDAAVIVREDEPGDTRLVAYVVADD 405
|
330 340 350 360
....*....|....*....|....*....|....*....|..
gi 1216630836 491 GKTMTEKEIVDYVAsQVTTAKKLRGGVVFVDEVPKGLTGKLD 532
Cdd:cd17643 406 GAAADIAELRALLK-ELLPDYMVPARYVPLDALPLTVNGKLD 446
|
|
| PRK07768 |
PRK07768 |
long-chain-fatty-acid--CoA ligase; Validated |
183-540 |
3.68e-23 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236091 [Multi-domain] Cd Length: 545 Bit Score: 103.15 E-value: 3.68e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1216630836 183 VPESFDRDktIALIMNSSGSTGLPKGVALPHRTAcvrFSHARDPIFGNQIIPDT-AILSVVPFHHGFGMfttLGYLIcgf 261
Cdd:PRK07768 146 PVETGEDD--LALMQLTSGSTGSPKAVQITHGNL---YANAEAMFVAAEFDVETdVMVSWLPLFHDMGM---VGFLT--- 214
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1216630836 262 rvVLMYRFEEELFLRSLqDYkIQSALLVPTLFSF----------FAKSTLI---------DKYDLSNLHEIASGGAPLSK 322
Cdd:PRK07768 215 --VPMYFGAELVKVTPM-DF-LRDPLLWAELISKyrgtmtaapnFAYALLArrlrrqakpGAFDLSSLRFALNGAEPIDP 290
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1216630836 323 EVGEA---VAKRFHLP--GIRQGYGLTETTSAILITPEGD---------------------DKPGA-----VGKVVPFFE 371
Cdd:PRK07768 291 ADVEDlldAGARFGLRpeAILPAYGMAEATLAVSFSPCGAglvvdevdadllaalrravpaTKGNTrrlatLGPPLPGLE 370
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1216630836 372 AKVVDLDtGKTLGVNQRGELCVRGPMIMSGYVNnPEATNALIDKDGWLHSGDIAYWDEDEHFFIVDRLKSLIKYKGYQVA 451
Cdd:PRK07768 371 VRVVDED-GQVLPPRGVGVIELRGESVTPGYLT-MDGFIPAQDADGWLDTGDLGYLTEEGEVVVCGRVKDVIIMAGRNIY 448
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1216630836 452 PAELESILLQHPNIFDAGVA--GLPDDDAGELPAavVVLE---HGKTMTEKEIVDYVASQVTTAKKLRGGVVFVDE---V 523
Cdd:PRK07768 449 PTDIERAAARVEGVRPGNAVavRLDAGHSREGFA--VAVEsnaFEDPAEVRRIRHQVAHEVVAEVGVRPRNVVVLGpgsI 526
|
410
....*....|....*..
gi 1216630836 524 PKGLTGKLDARKIREIL 540
Cdd:PRK07768 527 PKTPSGKLRRANAAELV 543
|
|
| PRK13383 |
PRK13383 |
acyl-CoA synthetase; Provisional |
38-531 |
5.21e-23 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 139531 [Multi-domain] Cd Length: 516 Bit Score: 102.38 E-value: 5.21e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1216630836 38 PGTIAFTDAhiEVDITYAEYFEMSVRLAEAMKRYGLNTNHRIVVCSENSLQFFMPVLGALFIGVAVAPANDIYNERELLN 117
Cdd:PRK13383 49 PGRTAIIDD--DGALSYRELQRATESLARRLTRDGVAPGRAVGVMCRNGRGFVTAVFAVGLLGADVVPISTEFRSDALAA 126
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1216630836 118 SMGISQPTVVFVSKKGLQKILNVQkklpiiQKIIIMDSKTdyqgfqsmytfVTSHlppgfneydfvpESFDRDKTIA--- 194
Cdd:PRK13383 127 ALRAHHISTVVADNEFAERIAGAD------DAVAVIDPAT-----------AGAE------------ESGGRPAVAApgr 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1216630836 195 LIMNSSGSTGLPKGVAlphrtacvRFSHARDPIFGNQIIPDTAILSV-------VPFHHGFGMFTTLGYLICGFRVVLMY 267
Cdd:PRK13383 178 IVLLTSGTTGKPKGVP--------RAPQLRSAVGVWVTILDRTRLRTgsrisvaMPMFHGLGLGMLMLTIALGGTVLTHR 249
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1216630836 268 RFEEELFLRSLQDYKIQSALLVPTLFSFFAKstLIDKYDLSN----LHEIASGGAPLSKEVGeavaKRF---HLPGIRQG 340
Cdd:PRK13383 250 HFDAEAALAQASLHRADAFTAVPVVLARILE--LPPRVRARNplpqLRVVMSSGDRLDPTLG----QRFmdtYGDILYNG 323
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1216630836 341 YGLTETTSAILITP-EGDDKPGAVGKVVPFFEAKVVDLDtGKTLGVNQRGELCVRGPMIMSGYVNNpeATNALIDkdGWL 419
Cdd:PRK13383 324 YGSTEVGIGALATPaDLRDAPETVGKPVAGCPVRILDRN-NRPVGPRVTGRIFVGGELAGTRYTDG--GGKAVVD--GMT 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1216630836 420 HSGDIAYWDEDEHFFIVDRLKSLIKYKGYQVAPAELESILLQHPNIFDAGVAGLPDDDAGELPAAVVVLEHGKTMTEKEI 499
Cdd:PRK13383 399 STGDMGYLDNAGRLFIVGREDDMIISGGENVYPRAVENALAAHPAVADNAVIGVPDERFGHRLAAFVVLHPGSGVDAAQL 478
|
490 500 510
....*....|....*....|....*....|..
gi 1216630836 500 VDYVASQVTTAKKLRgGVVFVDEVPKGLTGKL 531
Cdd:PRK13383 479 RDYLKDRVSRFEQPR-DINIVSSIPRNPTGKV 509
|
|
| A_NRPS_MycA_like |
cd05908 |
The adenylation domain of nonribosomal peptide synthetases (NRPS) similar to mycosubtilin ... |
193-538 |
9.02e-23 |
|
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: 101.80 E-value: 9.02e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1216630836 193 IALIMNSSGSTGLPKGVALPHRTacvrFSHARDPIfGNQIIPDT--AILSVVPFHHGFGMFTtlGYLICGFRVVLMYRFE 270
Cdd:cd05908 108 LAFIQFSSGSTGDPKGVMLTHEN----LVHNMFAI-LNSTEWKTkdRILSWMPLTHDMGLIA--FHLAPLIAGMNQYLMP 180
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1216630836 271 EELFLR--SLQDYKIQ----SALLVPT----LFSFFAKSTLIDKYDLSNLHEIASGGAPLSKEVGEAVAKRFHLPGIRQG 340
Cdd:cd05908 181 TRLFIRrpILWLKKASehkaTIVSSPNfgykYFLKTLKPEKANDWDLSSIRMILNGAEPIDYELCHEFLDHMSKYGLKRN 260
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1216630836 341 -----YGLTETTSAILITPEG------------------------DDKPGA----VGKVVPFFEAKVVDlDTGKTLGVNQ 387
Cdd:cd05908 261 ailpvYGLAEASVGASLPKAQspfktitlgrrhvthgepepevdkKDSECLtfveVGKPIDETDIRICD-EDNKILPDGY 339
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1216630836 388 RGELCVRGPMIMSGYVNNPEATNALIDKDGWLHSGDIAYWdEDEHFFIVDRLKSLIKYKGYQVAPAELESILLQHPNIFD 467
Cdd:cd05908 340 IGHIQIRGKNVTPGYYNNPEATAKVFTDDGWLKTGDLGFI-RNGRLVITGREKDIIFVNGQNVYPHDIERIAEELEGVEL 418
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1216630836 468 AGVA--GLPDDDAGElPAAVVVLEHGKtmTEKEIVDYvASQVTTAKKLRGG-----VVFVDEVPKGLTGKLDARKIRE 538
Cdd:cd05908 419 GRVVacGVNNSNTRN-EEIFCFIEHRK--SEDDFYPL-GKKIKKHLNKRGGwqineVLPIRRIPKTTSGKVKRYELAQ 492
|
|
| PRK12582 |
PRK12582 |
acyl-CoA synthetase; Provisional |
52-481 |
1.25e-22 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 237144 [Multi-domain] Cd Length: 624 Bit Score: 102.05 E-value: 1.25e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1216630836 52 ITYAEYFEMSVRLAEAMKRYGLNTNHRIVVCSENSLQFFMPVLGALFIGVAVAPANDIY-----NERELLNSMGISQPTV 126
Cdd:PRK12582 81 VTYGEAKRAVDALAQALLDLGLDPGRPVMILSGNSIEHALMTLAAMQAGVPAAPVSPAYslmshDHAKLKHLFDLVKPRV 160
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1216630836 127 VFVSKKGL-QKILNVQKKLPIiqKIIIMDSKTDYQGFQSMYTFVTShlPPGfneyDFVPESFDR--DKTIALIMNSSGST 203
Cdd:PRK12582 161 VFAQSGAPfARALAALDLLDV--TVVHVTGPGEGIASIAFADLAAT--PPT----AAVAAAIAAitPDTVAKYLFTSGST 232
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1216630836 204 GLPKGVALPHRTAC--------VRfshARDPifgNQIIPDtaILSVVPFHH------GFGMFTTLG---YLICGFRVVLM 266
Cdd:PRK12582 233 GMPKAVINTQRMMCaniamqeqLR---PREP---DPPPPV--SLDWMPWNHtmggnaNFNGLLWGGgtlYIDDGKPLPGM 304
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1216630836 267 yrFEEELflRSLQDYKIQSALLVPTLFSFFAKSTLIDKyDL-----SNLHEIASGGAPLSKEVGE-----AVAKRFHLPG 336
Cdd:PRK12582 305 --FEETI--RNLREISPTVYGNVPAGYAMLAEAMEKDD-ALrrsffKNLRLMAYGGATLSDDLYErmqalAVRTTGHRIP 379
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1216630836 337 IRQGYGLTETTSAILITPEGDDKPGAVGKVVPFFEAKVVDldtgktlgVNQRGELCVRGPMIMSGYVNNPEATNALIDKD 416
Cdd:PRK12582 380 FYTGYGATETAPTTTGTHWDTERVGLIGLPLPGVELKLAP--------VGDKYEVRVKGPNVTPGYHKDPELTAAAFDEE 451
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1216630836 417 GWLHSGDIA-YWDEDehffivDRLKSLI-------KYK---GYQVAPAELESILLQ--HPNIFDAGVAGLPDDDAGEL 481
Cdd:PRK12582 452 GFYRLGDAArFVDPD------DPEKGLIfdgrvaeDFKlstGTWVSVGTLRPDAVAacSPVIHDAVVAGQDRAFIGLL 523
|
|
| PRK07008 |
PRK07008 |
long-chain-fatty-acid--CoA ligase; Validated |
199-540 |
1.84e-22 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 235908 [Multi-domain] Cd Length: 539 Bit Score: 100.94 E-value: 1.84e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1216630836 199 SSGSTGLPKGVALPHRTACVrfsHArdpiFGNQIiPDT-------AILSVVP-FH-HGFGmfttLGYL--ICGFRVVL-- 265
Cdd:PRK07008 184 TSGTTGNPKGALYSHRSTVL---HA----YGAAL-PDAmglsardAVLPVVPmFHvNAWG----LPYSapLTGAKLVLpg 251
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1216630836 266 -------MYR-FEEElflrslqdyKIQSALLVPTLFSFFAKSTLIDKYDLSNLHEIASGGAPLSKEVGEAVAKRFhlpGI 337
Cdd:PRK07008 252 pdldgksLYElIEAE---------RVTFSAGVPTVWLGLLNHMREAGLRFSTLRRTVIGGSACPPAMIRTFEDEY---GV 319
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1216630836 338 R--QGYGLTET----TSAILiTPEGDDKPGAV--------GKVVPFFEAKVVDlDTGKTL---GVNQrGELCVRGPMIMS 400
Cdd:PRK07008 320 EviHAWGMTEMsplgTLCKL-KWKHSQLPLDEqrkllekqGRVIYGVDMKIVG-DDGRELpwdGKAF-GDLQVRGPWVID 396
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1216630836 401 GYVNNpeATNALIDkdGWLHSGDIAYWDEDEHFFIVDRLKSLIKYKGYQVAPAELESILLQHPNIFDAGVAGLPDDDAGE 480
Cdd:PRK07008 397 RYFRG--DASPLVD--GWFPTGDVATIDADGFMQITDRSKDVIKSGGEWISSIDIENVAVAHPAVAEAACIACAHPKWDE 472
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1216630836 481 LPAAVVVLEHGKTMTEKEIVDYVASQVttAK-KLRGGVVFVDEVPKGLTGKLDARKIREIL 540
Cdd:PRK07008 473 RPLLVVVKRPGAEVTREELLAFYEGKV--AKwWIPDDVVFVDAIPHTATGKLQKLKLREQF 531
|
|
| PLN02387 |
PLN02387 |
long-chain-fatty-acid-CoA ligase family protein |
52-463 |
2.21e-22 |
|
long-chain-fatty-acid-CoA ligase family protein
Pssm-ID: 215217 [Multi-domain] Cd Length: 696 Bit Score: 101.35 E-value: 2.21e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1216630836 52 ITYAEYFEMSVRLAEAMKRYGLNTNHRIVVCSENSLQFFMPVLGALFIGVAVApanDIY---NERELLNSMGISQPTVVF 128
Cdd:PLN02387 107 ITYGQVFERVCNFASGLVALGHNKEERVAIFADTRAEWLIALQGCFRQNITVV---TIYaslGEEALCHSLNETEVTTVI 183
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1216630836 129 VSKKGLQKILNVQKKLPIIQKIIIMD---SKTDYQGFQSMYTFVTShlppgFNEYD------FVPESFDRDKTIALIMNS 199
Cdd:PLN02387 184 CDSKQLKKLIDISSQLETVKRVIYMDdegVDSDSSLSGSSNWTVSS-----FSEVEklgkenPVDPDLPSPNDIAVIMYT 258
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1216630836 200 SGSTGLPKGVALPHrtacvrfshardpifGNQIIPDTAILSVVPFHHGFGMFttLGYLicgfrvVLMYRFE---EELFLR 276
Cdd:PLN02387 259 SGSTGLPKGVMMTH---------------GNIVATVAGVMTVVPKLGKNDVY--LAYL------PLAHILElaaESVMAA 315
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1216630836 277 S-----------LQDY--KIQ------SALLVPTLFSffAKSTLIDK-------------------YDLSNLHEIA---- 314
Cdd:PLN02387 316 VgaaigygspltLTDTsnKIKkgtkgdASALKPTLMT--AVPAILDRvrdgvrkkvdakgglakklFDIAYKRRLAaieg 393
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1216630836 315 ---------------------------------SGGAPLSKEVGEAVAKRFHLPgIRQGYGLTETTSAILITPEGDDKPG 361
Cdd:PLN02387 394 swfgawglekllwdalvfkkiravlggrirfmlSGGAPLSGDTQRFINICLGAP-IGQGYGLTETCAGATFSEWDDTSVG 472
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1216630836 362 AVGKVVPFFEAKVVDLDTGKTLGVNQ---RGELCVRGPMIMSGYVNNPEATNAL--IDKDG--WLHSGDIAYWDEDEHFF 434
Cdd:PLN02387 473 RVGPPLPCCYVKLVSWEEGGYLISDKpmpRGEIVIGGPSVTLGYFKNQEKTDEVykVDERGmrWFYTGDIGQFHPDGCLE 552
|
490 500 510
....*....|....*....|....*....|
gi 1216630836 435 IVDRLKSLIKYK-GYQVAPAELESILLQHP 463
Cdd:PLN02387 553 IIDRKKDIVKLQhGEYVSLGKVEAALSVSP 582
|
|
| A_NRPS_AB3403-like |
cd17646 |
Peptide Synthetase; The adenylation (A) domain of NRPS recognizes a specific amino acid or ... |
35-534 |
2.85e-22 |
|
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: 100.04 E-value: 2.85e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1216630836 35 ALVPGTIAFTDAhiEVDITYAEYFEMSVRLAEAMKRYGLNTNHRIVVCSENSLQFFMPVLGALFIGVAVAPAnDIYNERE 114
Cdd:cd17646 9 ARTPDAPAVVDE--GRTLTYRELDERANRLAHLLRARGVGPEDRVAVLLPRSADLVVALLAVLKAGAAYLPL-DPGYPAD 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1216630836 115 LLNSMGISQPTVVFVSKKGLQKILNVQKKLPIIQKIIimdsktdyqgfqsmytfvTSHLPPGfneydfVPESFDRDKTIA 194
Cdd:cd17646 86 RLAYMLADAGPAVVLTTADLAARLPAGGDVALLGDEA------------------LAAPPAT------PPLVPPRPDNLA 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1216630836 195 LIMNSSGSTGLPKGVALPHRTACVRFSHARDPIfgnQIIPDTAILSVVPFhhGF--GMFTTLGYLICGFRVVLMY---RF 269
Cdd:cd17646 142 YVIYTSGSTGRPKGVMVTHAGIVNRLLWMQDEY---PLGPGDRVLQKTPL--SFdvSVWELFWPLVAGARLVVARpggHR 216
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1216630836 270 EEELFLRSLQDYKIQSALLVPTLFSFFakstlidkydlsnLHEIASGGAPLSKEV---GEA----VAKRFH-LPGIR--Q 339
Cdd:cd17646 217 DPAYLAALIREHGVTTCHFVPSMLRVF-------------LAEPAAGSCASLRRVfcsGEAlppeLAARFLaLPGAElhN 283
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1216630836 340 GYGLTETT---SAILITPEGDDKPGAVGKVVPFFEAKVVDlDTGKTLGVNQRGELCVRGPMIMSGYVNNPEATNALIDKD 416
Cdd:cd17646 284 LYGPTEAAidvTHWPVRGPAETPSVPIGRPVPNTRLYVLD-DALRPVPVGVPGELYLGGVQLARGYLGRPALTAERFVPD 362
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1216630836 417 GWLH------SGDIAYWDEDEHFFIVDRLKSLIKYKGYQVAPAELESILLQHPNIFDAGVAGLPDDDAGE-LPAAVVVLE 489
Cdd:cd17646 363 PFGPgsrmyrTGDLARWRPDGALEFLGRSDDQVKIRGFRVEPGEIEAALAAHPAVTHAVVVARAAPAGAArLVGYVVPAA 442
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|
gi 1216630836 490 HGKTMTEKEIVDYVA-----SQVTTAkklrggVVFVDEVPKGLTGKLDAR 534
Cdd:cd17646 443 GAAGPDTAALRAHLAerlpeYMVPAA------FVVLDALPLTANGKLDRA 486
|
|
| PLN02861 |
PLN02861 |
long-chain-fatty-acid-CoA ligase |
52-472 |
8.45e-22 |
|
long-chain-fatty-acid-CoA ligase
Pssm-ID: 178452 [Multi-domain] Cd Length: 660 Bit Score: 99.53 E-value: 8.45e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1216630836 52 ITYAEYFEMSVRLAEAMKRYGLNTNHRIVVCSENSLQFFMPVLGALFIGVAVAPANDIYNERELLNSMGISQPTVVFVSK 131
Cdd:PLN02861 78 LTYKEVYDAAIRIGSAIRSRGVNPGDRCGIYGSNCPEWIIAMEACNSQGITYVPLYDTLGANAVEFIINHAEVSIAFVQE 157
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1216630836 132 KGLQKILNVQKKLPIIQKIII--------MDSKTDYQG--------FQSMYTfVTSHLPPgfneydfvpesfDRDKTIAL 195
Cdd:PLN02861 158 SKISSILSCLPKCSSNLKTIVsfgdvsseQKEEAEELGvscfsweeFSLMGS-LDCELPP------------KQKTDICT 224
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1216630836 196 IMNSSGSTGLPKGVALPHRTACVRFSHARDPIF--GNQIIPDTAILSVVPFHHGFGMF---------TTLGYLICGFRVV 264
Cdd:PLN02861 225 IMYTSGTTGEPKGVILTNRAIIAEVLSTDHLLKvtDRVATEEDSYFSYLPLAHVYDQVietyciskgASIGFWQGDIRYL 304
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1216630836 265 L-------------MYRFEEELFLRSLQdyKIQSA-LLVPTLFSFF---------------AKSTLIDKYDLSNLHE--- 312
Cdd:PLN02861 305 MedvqalkptifcgVPRVYDRIYTGIMQ--KISSGgMLRKKLFDFAynyklgnlrkglkqeEASPRLDRLVFDKIKEglg 382
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1216630836 313 -----IASGGAPLSKEVgEAVAKRFHLPGIRQGYGLTETTSAILiTPEGDDKP--GAVGKVVPFFEAKVVDL-DTG-KTL 383
Cdd:PLN02861 383 grvrlLLSGAAPLPRHV-EEFLRVTSCSVLSQGYGLTESCGGCF-TSIANVFSmvGTVGVPMTTIEARLESVpEMGyDAL 460
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1216630836 384 GVNQRGELCVRGPMIMSGYVNNPEATNALIdKDGWLHSGDIAYWDEDEHFFIVDRLKSLIKY-KGYQVAPAELESILLQH 462
Cdd:PLN02861 461 SDVPRGEICLRGNTLFSGYHKRQDLTEEVL-IDGWFHTGDIGEWQPNGAMKIIDRKKNIFKLsQGEYVAVENLENTYSRC 539
|
490
....*....|
gi 1216630836 463 PNIFDAGVAG 472
Cdd:PLN02861 540 PLIASIWVYG 549
|
|
| ACS |
cd05966 |
Acetyl-CoA synthetase (also known as acetate-CoA ligase and acetyl-activating enzyme); ... |
196-539 |
6.53e-21 |
|
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: 96.48 E-value: 6.53e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1216630836 196 IMNSSGSTGLPKGVAlpHRTA-----------CVrFSHARDPIFGNqiipdTAILSVVPFHHgfgmFTTLGYLICGFRVV 264
Cdd:cd05966 236 ILYTSGSTGKPKGVV--HTTGgyllyaattfkYV-FDYHPDDIYWC-----TADIGWITGHS----YIVYGPLANGATTV 303
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1216630836 265 LmyrFE-------EELFLRSLQDYKIQSALLVPTLFSFFAK--STLIDKYDLSNLHEIASGGAPLSKE--------VGEa 327
Cdd:cd05966 304 M---FEgtptypdPGRYWDIVEKHKVTIFYTAPTAIRALMKfgDEWVKKHDLSSLRVLGSVGEPINPEawmwyyevIGK- 379
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1216630836 328 vakrFHLPgIRQGYGLTETTSaILITP---EGDDKPGAVGKvvPFF--EAKVVDLDTGKtLGVNQRGELCVRGP---MIM 399
Cdd:cd05966 380 ----ERCP-IVDTWWQTETGG-IMITPlpgATPLKPGSATR--PFFgiEPAILDEEGNE-VEGEVEGYLVIKRPwpgMAR 450
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1216630836 400 SGYvNNPEA-TNALIDKD-GWLHSGDIAYWDEDEHFFIVDRLKSLIKYKGYQVAPAELESILLQHPNIFDAGVAGLPDDD 477
Cdd:cd05966 451 TIY-GDHERyEDTYFSKFpGYYFTGDGARRDEDGYYWITGRVDDVINVSGHRLGTAEVESALVAHPAVAEAAVVGRPHDI 529
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1216630836 478 AGELPAAVVVLEHGKTMT---EKEIVDYVASQ---VTTAKKlrggVVFVDEVPKGLTGKLDARKIREI 539
Cdd:cd05966 530 KGEAIYAFVTLKDGEEPSdelRKELRKHVRKEigpIATPDK----IQFVPGLPKTRSGKIMRRILRKI 593
|
|
| PRK05620 |
PRK05620 |
long-chain fatty-acid--CoA ligase; |
52-540 |
6.57e-21 |
|
long-chain fatty-acid--CoA ligase;
Pssm-ID: 180167 [Multi-domain] Cd Length: 576 Bit Score: 96.39 E-value: 6.57e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1216630836 52 ITYAEYFEMSVRLAEAMK-RYGLNTNHRI----VVCSENSLQFF-MPVLGALFigvavAPANDIYNERELLNSMGISQPT 125
Cdd:PRK05620 39 TTFAAIGARAAALAHALHdELGITGDQRVgsmmYNCAEHLEVLFaVACMGAVF-----NPLNKQLMNDQIVHIINHAEDE 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1216630836 126 VVFVSKKGLQKILNVQKKLPIIQKIIIMDSktdyqgfqSMYTFVTSHLPPGFNEYDFV------PESFD----RDKTIAL 195
Cdd:PRK05620 114 VIVADPRLAEQLGEILKECPCVRAVVFIGP--------SDADSAAAHMPEGIKVYSYEalldgrSTVYDwpelDETTAAA 185
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1216630836 196 IMNSSGSTGLPKGVALPHRTACVRFSHAR--DPIfgnQIIPDTAILSVVPFHHGFGMFTTLGYLICGFRVVLMYR-FEEE 272
Cdd:PRK05620 186 ICYSTGTTGAPKGVVYSHRSLYLQSLSLRttDSL---AVTHGESFLCCVPIYHVLSWGVPLAAFMSGTPLVFPGPdLSAP 262
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1216630836 273 LFLRSLQDYKIQSALLVPT----LFSFFAKSTLidkyDLSNLHEIASGGAPLSKEVGEAVAKRFHLPGIrQGYGLTETTS 348
Cdd:PRK05620 263 TLAKIIATAMPRVAHGVPTlwiqLMVHYLKNPP----ERMSLQEIYVGGSAVPPILIKAWEERYGVDVV-HVWGMTETSP 337
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1216630836 349 AILIT--PEG------DDKPGAVGKVVPFFEAKVVDldTGKTLGVNQR--GELCVRGPMIMSGYVNNP------------ 406
Cdd:PRK05620 338 VGTVArpPSGvsgearWAYRVSQGRFPASLEYRIVN--DGQVMESTDRneGEIQVRGNWVTASYYHSPteegggaastfr 415
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1216630836 407 ----EATNALIDKDGWLHSGDIAYWDEDEHFFIVDRLKSLIKYKGYQVAPAELESILLQHPNIFDAGVAGLPDDDAGELP 482
Cdd:PRK05620 416 gedvEDANDRFTADGWLRTGDVGSVTRDGFLTIHDRARDVIRSGGEWIYSAQLENYIMAAPEVVECAVIGYPDDKWGERP 495
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1216630836 483 AAVVVLEHGKTMTEkeivdyvasqvTTAKKLRGGV-------------VFVDEVPKGLTGKLDARKIREIL 540
Cdd:PRK05620 496 LAVTVLAPGIEPTR-----------ETAERLRDQLrdrlpnwmlpeywTFVDEIDKTSVGKFDKKDLRQHL 555
|
|
| FATP_chFAT1_like |
cd05937 |
Uncharacterized subfamily of bifunctional fatty acid transporter/very-long-chain acyl-CoA ... |
53-489 |
1.02e-20 |
|
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: 95.19 E-value: 1.02e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1216630836 53 TYAEYFEMSVRLAEAMK-RYGLNTNHRIVVCSENSLQFFMPVLGALFIGVAVAPANdiYNERE--LLNSMGISQPTVVFV 129
Cdd:cd05937 7 TYSETYDLVLRYAHWLHdDLGVQAGDFVAIDLTNSPEFVFLWLGLWSIGAAPAFIN--YNLSGdpLIHCLKLSGSRFVIV 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1216630836 130 skkglqkilnvqkklpiiqkiiimdsktdyqgfqsmytfvtshlppgfneydfvpesfDRDKTIALIMnSSGSTGLPKGV 209
Cdd:cd05937 85 ----------------------------------------------------------DPDDPAILIY-TSGTTGLPKAA 105
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1216630836 210 ALPHR---TACVRFSHardpIFGNQiiPDTAILSVVPFHHGFGMFTTLGY-LICGFRVVLMYRFEEELFLRSLQDYKIQS 285
Cdd:cd05937 106 AISWRrtlVTSNLLSH----DLNLK--NGDRTYTCMPLYHGTAAFLGACNcLMSGGTLALSRKFSASQFWKDVRDSGATI 179
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1216630836 286 ALLVPTLFSFFAkSTLIDKYDLSNLHEIASGGApLSKEVGEAVAKRFHLPGIRQGYGLTETTSAILITPEGDDKPGAVGK 365
Cdd:cd05937 180 IQYVGELCRYLL-STPPSPYDRDHKVRVAWGNG-LRPDIWERFRERFNVPEIGEFYAATEGVFALTNHNVGDFGAGAIGH 257
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1216630836 366 VVP----FFEAKVV----DLDTGKTLGVNQRGeLCVRGP------MIM----------SGYVNNPEAT------NALIDK 415
Cdd:cd05937 258 HGLirrwKFENQVVlvkmDPETDDPIRDPKTG-FCVRAPvgepgeMLGrvpfknreafQGYLHNEDATesklvrDVFRKG 336
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1216630836 416 DGWLHSGDIAYWDEDEHFFIVDRLKSLIKYKGYQVAPAELESILLQHPNIFDAGVAG--LPDDDaGELPAAVVVLE 489
Cdd:cd05937 337 DIYFRTGDLLRQDADGRWYFLDRLGDTFRWKSENVSTTEVADVLGAHPDIAEANVYGvkVPGHD-GRAGCAAITLE 411
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
17-534 |
3.14e-20 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 95.41 E-value: 3.14e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1216630836 17 PLEDGTAGEQLHKAM-KRYALVPGTIA--FTDAHIevdiTYAEYFEMSVRLAEAMKRYGLNTNHRIVVCSENSLQFFMPV 93
Cdd:PRK12316 1995 TPEAYPRGPGVHQRIaEQAARAPEAIAvvFGDQHL----SYAELDSRANRLAHRLRARGVGPEVRVAIAAERSFELVVAL 2070
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1216630836 94 LGALFIGVAVAPANDIYNERELLNSMGISQPTVVfVSKKGLQKILNVQKKLPIIQkiiiMDSKTDYQGFqsmytfvtshl 173
Cdd:PRK12316 2071 LAVLKAGGAYVPLDPNYPAERLAYMLEDSGAALL-LTQRHLLERLPLPAGVARLP----LDRDAEWADY----------- 2134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1216630836 174 PPGFNEYDFVPEsfdrdkTIALIMNSSGSTGLPKGVALPHrTACVRFSHARDPIFGnqIIPDTAILSVVPFHHGFGMFTT 253
Cdd:PRK12316 2135 PDTAPAVQLAGE------NLAYVIYTSGSTGLPKGVAVSH-GALVAHCQAAGERYE--LSPADCELQFMSFSFDGAHEQW 2205
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1216630836 254 LGYLICGFRVVLM---YRFEEELFlRSLQDYKIQSALLVPTLFSFFAKSTLIDKYDLsNLHEIASGGAPLSKEVGEAVAK 330
Cdd:PRK12316 2206 FHPLLNGARVLIRddeLWDPEQLY-DEMERHGVTILDFPPVYLQQLAEHAERDGRPP-AVRVYCFGGEAVPAASLRLAWE 2283
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1216630836 331 RFHLPGIRQGYGLTETTSAILITPEGDDKPGA-----VGKVVPFFEAKVVDLDTgKTLGVNQRGELCVRGPMIMSGYVNN 405
Cdd:PRK12316 2284 ALRPVYLFNGYGPTEAVVTPLLWKCRPQDPCGaayvpIGRALGNRRAYILDADL-NLLAPGMAGELYLGGEGLARGYLNR 2362
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1216630836 406 PEATNALIDKDGWLH-------SGDIAYWDEDEHFFIVDRLKSLIKYKGYQVAPAELESILLQHPNIFDAGVAGLpDDDA 478
Cdd:PRK12316 2363 PGLTAERFVPDPFSAsgerlyrTGDLARYRADGVVEYLGRIDHQVKIRGFRIELGEIEARLQAHPAVREAVVVAQ-DGAS 2441
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*.
gi 1216630836 479 GELPAAVVVLEHGKTMTEKEIVDYVAsQVTTAKKLRGGVVFVDEVPKGLTGKLDAR 534
Cdd:PRK12316 2442 GKQLVAYVVPDDAAEDLLAELRAWLA-ARLPAYMVPAHWVVLERLPLNPNGKLDRK 2496
|
|
| PRK09274 |
PRK09274 |
peptide synthase; Provisional |
52-497 |
5.59e-20 |
|
peptide synthase; Provisional
Pssm-ID: 236443 [Multi-domain] Cd Length: 552 Bit Score: 93.42 E-value: 5.59e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1216630836 52 ITYAEYFEMSVRLAEAMKRYGLNTNHRIVVCSENSLQFFmPVLGALF----IGVAVAPANDIYNereLLNSMGISQPTVV 127
Cdd:PRK09274 42 LSFAELDARSDAIAHGLNAAGIGRGMRAVLMVTPSLEFF-ALTFALFkagaVPVLVDPGMGIKN---LKQCLAEAQPDAF 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1216630836 128 F-VSKKGLQKILNVQKKLPIIQKIIIMDSKtdyqgFQSMYTFVTSHLPPGFNEYDFVPesFDRDKTiALIMNSSGSTGLP 206
Cdd:PRK09274 118 IgIPKAHLARRLFGWGKPSVRRLVTVGGRL-----LWGGTTLATLLRDGAAAPFPMAD--LAPDDM-AAILFTSGSTGTP 189
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1216630836 207 KGVALPHRTACVRFSHARDpIFGnqIIPDTAILSVVPFhhgFGMFTtlgyLICGFRVVLMY-------RFEEELFLRSLQ 279
Cdd:PRK09274 190 KGVVYTHGMFEAQIEALRE-DYG--IEPGEIDLPTFPL---FALFG----PALGMTSVIPDmdptrpaTVDPAKLFAAIE 259
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1216630836 280 DYKIQSALLVPTLFSFFAKSTLIDKYDLSNLHEIASGGAPLSKEVGEAVAKRFHlPGIR--QGYGLTE-------TTSAI 350
Cdd:PRK09274 260 RYGVTNLFGSPALLERLGRYGEANGIKLPSLRRVISAGAPVPIAVIERFRAMLP-PDAEilTPYGATEalpissiESREI 338
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1216630836 351 L-----ITPEGDdkpGA-VGKVVPFFEAKVVDLDTG--------KTLGVNQRGELCVRGPMIMSGYVNNPEAT--NALID 414
Cdd:PRK09274 339 LfatraATDNGA---GIcVGRPVDGVEVRIIAISDApipewddaLRLATGEIGEIVVAGPMVTRSYYNRPEATrlAKIPD 415
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1216630836 415 KDG--WLHSGDIAYWDEDEHFFI----VDRLKSLIK-YKGYQVapaelESILLQHPNIFDAGVAGLPdDDAGELPAAVVV 487
Cdd:PRK09274 416 GQGdvWHRMGDLGYLDAQGRLWFcgrkAHRVETAGGtLYTIPC-----ERIFNTHPGVKRSALVGVG-VPGAQRPVLCVE 489
|
490
....*....|
gi 1216630836 488 LEHGKTMTEK 497
Cdd:PRK09274 490 LEPGVACSKS 499
|
|
| A_NRPS_ProA |
cd17656 |
gramicidin S synthase 2, also known as ATP-dependent proline adenylase; This family of the ... |
45-536 |
6.00e-20 |
|
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: 92.92 E-value: 6.00e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1216630836 45 DAHIEVD----ITYAEYFEMSVRLAEAMKRYGLNTNHRIVVCSENSLQFFMPVLGALFIGVAVAPANDIYNERELLNSMG 120
Cdd:cd17656 3 DAVAVVFenqkLTYRELNERSNQLARFLREKGVKKDSIVAIMMERSAEMIVGILGILKAGGAFVPIDPEYPEERRIYIML 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1216630836 121 ISQPTVVfVSKKGLQKILNVQKKlpiiqkIIIMDSKTDYQGFQSMYTFVtshlppgFNEYDfvpesfdrdktIALIMNSS 200
Cdd:cd17656 83 DSGVRVV-LTQRHLKSKLSFNKS------TILLEDPSISQEDTSNIDYI-------NNSDD-----------LLYIIYTS 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1216630836 201 GSTGLPKGVALPHRTACVRFSHARD---PIFGNQIIPDTAILSVVPFHHGFGMFTTLG--YLIcgfrvvlmyRFEEELFL 275
Cdd:cd17656 138 GTTGKPKGVQLEHKNMVNLLHFEREktnINFSDKVLQFATCSFDVCYQEIFSTLLSGGtlYII---------REETKRDV 208
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1216630836 276 RSLQDY----KIQSALLVPTLFSFFAKSTLIDKYDLSNLHEIASGGAPL--SKEVGEAVAKR-FHLpgiRQGYGLTET-- 346
Cdd:cd17656 209 EQLFDLvkrhNIEVVFLPVAFLKFIFSEREFINRFPTCVKHIITAGEQLviTNEFKEMLHEHnVHL---HNHYGPSEThv 285
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1216630836 347 TSAILITPEgDDKP--GAVGKvvPFFEAKVVDLDTGKTL---GVnqRGELCVRGPMIMSGYVNNPEATNALIDKDGW--- 418
Cdd:cd17656 286 VTTYTINPE-AEIPelPPIGK--PISNTWIYILDQEQQLqpqGI--VGELYISGASVARGYLNRQELTAEKFFPDPFdpn 360
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1216630836 419 ---LHSGDIAYWDEDEHFFIVDRLKSLIKYKGYQVAPAELESILLQHPNIFDAGVAGLPDDDAGELPAAVVVLEhgKTMT 495
Cdd:cd17656 361 ermYRTGDLARYLPDGNIEFLGRADHQVKIRGYRIELGEIEAQLLNHPGVSEAVVLDKADDKGEKYLCAYFVME--QELN 438
|
490 500 510 520
....*....|....*....|....*....|....*....|.
gi 1216630836 496 EKEIVDYVASQVtTAKKLRGGVVFVDEVPKGLTGKLDARKI 536
Cdd:cd17656 439 ISQLREYLAKQL-PEYMIPSFFVPLDQLPLTPNGKVDRKAL 478
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
49-535 |
1.07e-19 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 93.87 E-value: 1.07e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1216630836 49 EVDITYAEYFEMSVRLAEAMKRYGLNTNHRIVVCSENSLQFFMPVLGALFIGVAVAPANDIYNERELLNSMGISQPTVVF 128
Cdd:PRK12316 4574 EEKLTYAELNRRANRLAHALIARGVGPEVLVGIAMERSAEMMVGLLAVLKAGGAYVPLDPEYPRERLAYMMEDSGAALLL 4653
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1216630836 129 VSKKGLQKilnvqkkLPIIQKI--IIMDSKTDYQGFQSMYTFVTSHlppgfneydfvPESfdrdktIALIMNSSGSTGLP 206
Cdd:PRK12316 4654 TQSHLLQR-------LPIPDGLasLALDRDEDWEGFPAHDPAVRLH-----------PDN------LAYVIYTSGSTGRP 4709
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1216630836 207 KGVALPHRtACVRFSHARDPIFGnqIIPDTAILSVVPFHHGFGMFTTLGYLICGFRVVLM--YRFEEELFLRSLQDYKIQ 284
Cdd:PRK12316 4710 KGVAVSHG-SLVNHLHATGERYE--LTPDDRVLQFMSFSFDGSHEGLYHPLINGASVVIRddSLWDPERLYAEIHEHRVT 4786
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1216630836 285 SALLVPTLFSFFAKSTLIDKyDLSNLHEIASGGAPLSKEVGEAVAKRFHLPGIRQGYGLTETT-SAILITPEGDDKPGA- 362
Cdd:PRK12316 4787 VLVFPPVYLQQLAEHAERDG-EPPSLRVYCFGGEAVAQASYDLAWRALKPVYLFNGYGPTETTvTVLLWKARDGDACGAa 4865
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1216630836 363 ---VGKVVPFFEAKVVDlDTGKTLGVNQRGELCVRGPMIMSGYVNNPEAT------NALIDKDGWLH-SGDIAYWDEDEH 432
Cdd:PRK12316 4866 ympIGTPLGNRSGYVLD-GQLNPLPVGVAGELYLGGEGVARGYLERPALTaerfvpDPFGAPGGRLYrTGDLARYRADGV 4944
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1216630836 433 FFIVDRLKSLIKYKGYQVAPAELESILLQHPNIFDAGVAGLPDDDAGELPAAVVVlehgktmTEKEIVDYVASQVTTAKK 512
Cdd:PRK12316 4945 IDYLGRVDHQVKIRGFRIELGEIEARLREHPAVREAVVIAQEGAVGKQLVGYVVP-------QDPALADADEAQAELRDE 5017
|
490 500 510
....*....|....*....|....*....|....*.
gi 1216630836 513 LRGGV-------------VFVDEVPKGLTGKLDaRK 535
Cdd:PRK12316 5018 LKAALrerlpeymvpahlVFLARMPLTPNGKLD-RK 5052
|
|
| PLN02614 |
PLN02614 |
long-chain acyl-CoA synthetase |
53-458 |
4.88e-19 |
|
long-chain acyl-CoA synthetase
Pssm-ID: 166255 [Multi-domain] Cd Length: 666 Bit Score: 90.85 E-value: 4.88e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1216630836 53 TYAEYFEMSVRLAEAMKRYGLNTNHRIVVCSENSLQFFMPVLGALFIGVAVAPANDIYNERELLNSMGISQPTVVFVSKK 132
Cdd:PLN02614 81 TYQEVYDIVIKLGNSLRSVGVKDEAKCGIYGANSPEWIISMEACNAHGLYCVPLYDTLGAGAVEFIISHSEVSIVFVEEK 160
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1216630836 133 GLQKILNVQKKLPIIQKIIIM------DSKTDYQGFQSMYTFVTSHLPPG-FNEYDFvpeSFDRDKTIALIMNSSGSTGL 205
Cdd:PLN02614 161 KISELFKTCPNSTEYMKTVVSfggvsrEQKEEAETFGLVIYAWDEFLKLGeGKQYDL---PIKKKSDICTIMYTSGTTGD 237
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1216630836 206 PKGVALPHR------TACVRFSHARDPIFGNQIIpdtaILSVVPFHHGFGM-----FTTLGYLIcGFrvvlmYRFEEELF 274
Cdd:PLN02614 238 PKGVMISNEsivtliAGVIRLLKSANAALTVKDV----YLSYLPLAHIFDRvieecFIQHGAAI-GF-----WRGDVKLL 307
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1216630836 275 LRSLQDYKIQSALLVPTLFS--------------FFAK-----------------------STLIDKYDLS--------N 309
Cdd:PLN02614 308 IEDLGELKPTIFCAVPRVLDrvysglqkklsdggFLKKfvfdsafsykfgnmkkgqshveaSPLCDKLVFNkvkqglggN 387
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1216630836 310 LHEIASGGAPLSKEVgEAVAKRFHLPGIRQGYGLTETTSAILIT-PEGDDKPGAVGKVVPFFEAKVVDLDTGK--TLGVN 386
Cdd:PLN02614 388 VRIILSGAAPLASHV-ESFLRVVACCHVLQGYGLTESCAGTFVSlPDELDMLGTVGPPVPNVDIRLESVPEMEydALAST 466
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1216630836 387 QRGELCVRGPMIMSGYVNNPEATNALIdKDGWLHSGDIAYWDEDEHFFIVDRLKSLIKY-KGYQVAPAELESI 458
Cdd:PLN02614 467 PRGEICIRGKTLFSGYYKREDLTKEVL-IDGWLHTGDVGEWQPNGSMKIIDRKKNIFKLsQGEYVAVENIENI 538
|
|
| PRK08043 |
PRK08043 |
bifunctional acyl-ACP--phospholipid O-acyltransferase/long-chain-fatty-acid--ACP ligase; |
194-458 |
6.46e-19 |
|
bifunctional acyl-ACP--phospholipid O-acyltransferase/long-chain-fatty-acid--ACP ligase;
Pssm-ID: 181207 [Multi-domain] Cd Length: 718 Bit Score: 90.54 E-value: 6.46e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1216630836 194 ALIMNSSGSTGLPKGVAlphrtacvrfsHARDPIFGN--QI------IPDTAILSVVPFHHGFGMftTLGY---LICGFR 262
Cdd:PRK08043 368 ALILFTSGSEGHPKGVV-----------HSHKSLLANveQIktiadfTPNDRFMSALPLFHSFGL--TVGLftpLLTGAE 434
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1216630836 263 VVLM-----YRFEEELFlrslqdYKIQSALLvptlfsfFAKSTLI-------DKYDLSNLHEIASGGAPLSKEVGEAVAK 330
Cdd:PRK08043 435 VFLYpsplhYRIVPELV------YDRNCTVL-------FGTSTFLgnyarfaNPYDFARLRYVVAGAEKLQESTKQLWQD 501
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1216630836 331 RFhlpGIR--QGYGLTETTSAILITPEGDDKPGAVGKVVPFFEAKVVDLDtgktlGVNQRGELCVRGPMIMSGY--VNN- 405
Cdd:PRK08043 502 KF---GLRilEGYGVTECAPVVSINVPMAAKPGTVGRILPGMDARLLSVP-----GIEQGGRLQLKGPNIMNGYlrVEKp 573
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*....
gi 1216630836 406 -----PEATNALIDKD-GWLHSGDIAYWDEDEHFFIVDRLKSLIKYKGYQVApaeLESI 458
Cdd:PRK08043 574 gvlevPTAENARGEMErGWYDTGDIVRFDEQGFVQIQGRAKRFAKIAGEMVS---LEMV 629
|
|
| A_NRPS_LgrA-like |
cd17645 |
adenylation (A) domain of linear gramicidin synthetase (LgrA) and similar proteins; This ... |
193-536 |
9.68e-19 |
|
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: 88.77 E-value: 9.68e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1216630836 193 IALIMNSSGSTGLPKGVALPHRtACVRFSHARDPIFGNQIIPDTAILSVVPFH-HGFGMFTtlgYLICGFRVVLMYRfEE 271
Cdd:cd17645 106 LAYVIYTSGSTGLPKGVMIEHH-NLVNLCEWHRPYFGVTPADKSLVYASFSFDaSAWEIFP---HLTAGAALHVVPS-ER 180
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1216630836 272 ELFLRSLQDYKIQSALLVPTLFSFFAKSTLidKYDLSNLHEIASGGAPLSKevgeAVAKRFHLpgiRQGYGLTETTsaIL 351
Cdd:cd17645 181 RLDLDALNDYFNQEGITISFLPTGAAEQFM--QLDNQSLRVLLTGGDKLKK----IERKGYKL---VNNYGPTENT--VV 249
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1216630836 352 ITPEGDDKPGA---VGKvvPFFEAKVVDLDTGKTL---GVNqrGELCVRGPMIMSGYVNNPEAT------NALIDKDGWL 419
Cdd:cd17645 250 ATSFEIDKPYAnipIGK--PIDNTRVYILDEALQLqpiGVA--GELCIAGEGLARGYLNRPELTaekfivHPFVPGERMY 325
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1216630836 420 HSGDIAYWDEDEHFFIVDRLKSLIKYKGYQVAPAELESILLQHPNIFDAGVAGLPDDDAGELPAAVVV----LEHG--KT 493
Cdd:cd17645 326 RTGDLAKFLPDGNIEFLGRLDQQVKIRGYRIEPGEIEPFLMNHPLIELAAVLAKEDADGRKYLVAYVTapeeIPHEelRE 405
|
330 340 350 360
....*....|....*....|....*....|....*....|...
gi 1216630836 494 MTEKEIVDYVASQVttakklrggVVFVDEVPKGLTGKLDARKI 536
Cdd:cd17645 406 WLKNDLPDYMIPTY---------FVHLKALPLTANGKVDRKAL 439
|
|
| PRK12467 |
PRK12467 |
peptide synthase; Provisional |
49-535 |
1.15e-18 |
|
peptide synthase; Provisional
Pssm-ID: 237108 [Multi-domain] Cd Length: 3956 Bit Score: 90.61 E-value: 1.15e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1216630836 49 EVDITYAEYFEMSVRLAEAMKRYGLNTNHRIVVCSENSLQFFMPVLGALFIGVAVAPAnDIYNERELLNSMgisqptvvf 128
Cdd:PRK12467 1597 EQELTYGELNRRANRLAHRLIALGVGPEVLVGIAVERSLEMVVGLLAILKAGGAYVPL-DPEYPRERLAYM--------- 1666
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1216630836 129 VSKKGLQKIL---NVQKKLPII--QKIIIMDSKTDYQGFQSMYTfvtshlppgfneydfvPESFDRDKTIALIMNSSGST 203
Cdd:PRK12467 1667 IEDSGIELLLtqsHLQARLPLPdgLRSLVLDQEDDWLEGYSDSN----------------PAVNLAPQNLAYVIYTSGST 1730
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1216630836 204 GLPKGVALPHrTACVRFSHARDPIFgnQIIPDTAILSVVPFHHGFGMFTTLGYLICGFRVVLMyRFEE----ELFLRSLQ 279
Cdd:PRK12467 1731 GRPKGAGNRH-GALVNRLCATQEAY--QLSAADVVLQFTSFAFDVSVWELFWPLINGARLVIA-PPGAhrdpEQLIQLIE 1806
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1216630836 280 DYKIQSALLVPTLFSFFAKSTLIDKYDLSnLHEIASGGAPLSKEVGEAVAKRFHLPGIRQGYGLTETT------SAILIT 353
Cdd:PRK12467 1807 RQQVTTLHFVPSMLQQLLQMDEQVEHPLS-LRRVVCGGEALEVEALRPWLERLPDTGLFNLYGPTETAvdvthwTCRRKD 1885
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1216630836 354 PEGDDkpgAVGKVVPFFEAKVVDLDTGKTL---GVnqRGELCVRGPMIMSGYVNNPEAT------NALIDKDGWLH-SGD 423
Cdd:PRK12467 1886 LEGRD---SVPIGQPIANLSTYILDASLNPvpiGV--AGELYLGGVGLARGYLNRPALTaerfvaDPFGTVGSRLYrTGD 1960
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1216630836 424 IAYWDEDEHFFIVDRLKSLIKYKGYQVAPAELESILLQHPNIFDAGVagLPDDDAG--ELPAAVVVlehgktmTEKEIVD 501
Cdd:PRK12467 1961 LARYRADGVIEYLGRIDHQVKIRGFRIELGEIEARLREQGGVREAVV--IAQDGANgkQLVAYVVP-------TDPGLVD 2031
|
490 500 510 520
....*....|....*....|....*....|....*....|....*..
gi 1216630836 502 YVASQVTTAKKLRGGV-------------VFVDEVPKGLTGKLDaRK 535
Cdd:PRK12467 2032 DDEAQVALRAILKNHLkaslpeymvpahlVFLARMPLTPNGKLD-RK 2077
|
|
| PRK00174 |
PRK00174 |
acetyl-CoA synthetase; Provisional |
344-539 |
1.51e-18 |
|
acetyl-CoA synthetase; Provisional
Pssm-ID: 234677 [Multi-domain] Cd Length: 637 Bit Score: 89.04 E-value: 1.51e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1216630836 344 TETtSAILITP-EG--DDKPGAVGKvvPFF--EAKVVDlDTGKTLGVNQRGELCVRGP---MIMSGYvNNPEAtnaLID- 414
Cdd:PRK00174 405 TET-GGIMITPlPGatPLKPGSATR--PLPgiQPAVVD-EEGNPLEGGEGGNLVIKDPwpgMMRTIY-GDHER---FVKt 476
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1216630836 415 -----KDGWLhSGDIAYWDEDEHFFIVDRLKSLIKYKGYQVAPAELESILLQHPNIFDAGVAGLPDDDAGELPAAVVVLE 489
Cdd:PRK00174 477 yfstfKGMYF-TGDGARRDEDGYYWITGRVDDVLNVSGHRLGTAEIESALVAHPKVAEAAVVGRPDDIKGQGIYAFVTLK 555
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1216630836 490 HGKTMTE---KEIVDYVASQV---TTAKKLRggvvFVDEVPKGLTGKLDARKIREI 539
Cdd:PRK00174 556 GGEEPSDelrKELRNWVRKEIgpiAKPDVIQ----FAPGLPKTRSGKIMRRILRKI 607
|
|
| PRK06334 |
PRK06334 |
long chain fatty acid--[acyl-carrier-protein] ligase; Validated |
186-479 |
3.25e-18 |
|
long chain fatty acid--[acyl-carrier-protein] ligase; Validated
Pssm-ID: 180533 [Multi-domain] Cd Length: 539 Bit Score: 87.95 E-value: 3.25e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1216630836 186 SFDRDKT-IALIMNSSGSTGLPKGVALPHRT------ACVRFSharDPIfgnqiiPDTAILSVVPFHHGFGMFT-TLGYL 257
Cdd:PRK06334 177 VSDKDPEdVAVILFTSGTEKLPKGVPLTHANllanqrACLKFF---SPK------EDDVMMSFLPPFHAYGFNScTLFPL 247
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1216630836 258 ICGFRVVLMYR-FEEELFLRSLQDYKIQSALLVPTLFSFFAKSTLIDKYDLSNLHEIASGGAPLSKEVGEAVAKRFHLPG 336
Cdd:PRK06334 248 LSGVPVVFAYNpLYPKKIVEMIDEAKVTFLGSTPVFFDYILKTAKKQESCLPSLRFVVIGGDAFKDSLYQEALKTFPHIQ 327
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1216630836 337 IRQGYGLTETTSAILITPEGDDK-PGAVGKVVPFFEAKVVDLDTGKTLGVNQRGELCVRGPMIMSGYV-NNPEATNALID 414
Cdd:PRK06334 328 LRQGYGTTECSPVITINTVNSPKhESCVGMPIRGMDVLIVSEETKVPVSSGETGLVLTRGTSLFSGYLgEDFGQGFVELG 407
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1216630836 415 KDGWLHSGDIAYWDEDEHFFIVDRLKSLIKYKGYQVAPAELESILLQHpnifdagvAGLPDDDAG 479
Cdd:PRK06334 408 GETWYVTGDLGYVDRHGELFLKGRLSRFVKIGAEMVSLEALESILMEG--------FGQNAADHA 464
|
|
| FATP_FACS |
cd05940 |
Fatty acid transport proteins (FATP) play dual roles as fatty acid transporters and its ... |
52-474 |
3.70e-18 |
|
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: 87.02 E-value: 3.70e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1216630836 52 ITYAEYFEMSVRLAEAMKRYGLNTNHRIVVCSENSLQFFMPVLGALFIGVAVAPANdiYNER--ELLNSMGISQPTVVFV 129
Cdd:cd05940 4 LTYAELDAMANRYARWLKSLGLKPGDVVALFMENRPEYVLLWLGLVKIGAVAALIN--YNLRgeSLAHCLNVSSAKHLVV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1216630836 130 skkglqkilnvqkklpiiqkiiimdsktdyqgfqsmytfvtshlppgfneydfvpesfDRdktiALIMNSSGSTGLPKGV 209
Cdd:cd05940 82 ----------------------------------------------------------DA----ALYIYTSGTTGLPKAA 99
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1216630836 210 ALPHRTaCVRFSHARDPIFGNqiIPDTAILSVVPFHHGFGMFTTLG-YLICGFRVVLMYRFEEELFLRSLQDYKIqsall 288
Cdd:cd05940 100 IISHRR-AWRGGAFFAGSGGA--LPSDVLYTCLPLYHSTALIVGWSaCLASGATLVIRKKFSASNFWDDIRKYQA----- 171
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1216630836 289 vpTLFSFFAKstlIDKY-------DLSNLHEI-ASGGAPLSKEVGEAVAKRFHLPGIRQGYGLTETTSAiLITPEGddKP 360
Cdd:cd05940 172 --TIFQYIGE---LCRYllnqppkPTERKHKVrMIFGNGLRPDIWEEFKERFGVPRIAEFYAATEGNSG-FINFFG--KP 243
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1216630836 361 GAVGkVVPFFEAKV-------VDLDTGKTL----------GVNQRGELCVR----GPMImsGYVNNPEAT-----NALID 414
Cdd:cd05940 244 GAIG-RNPSLLRKVaplalvkYDLESGEPIrdaegrcikvPRGEPGLLISRinplEPFD--GYTDPAATEkkilrDVFKK 320
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1216630836 415 KDGWLHSGDIAYWDEDEHFFIVDRLKSLIKYKGYQVAPAELESILLQHPNIFDAGVAGLP 474
Cdd:cd05940 321 GDAWFNTGDLMRLDGEGFWYFVDRLGDTFRWKGENVSTTEVAAVLGAFPGVEEANVYGVQ 380
|
|
| PRK12467 |
PRK12467 |
peptide synthase; Provisional |
52-535 |
3.91e-18 |
|
peptide synthase; Provisional
Pssm-ID: 237108 [Multi-domain] Cd Length: 3956 Bit Score: 88.68 E-value: 3.91e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1216630836 52 ITYAEYFEMSVRLAEAMKRYGLNTNHRIVVCSENSLQFFMPVLGALFIGVAVAPANDIYnERELLNSMGISQPTVVFVSK 131
Cdd:PRK12467 538 LSYAELNRQANRLAHVLIAAGVGPDVLVGIAVERSIEMVVGLLAVLKAGGAYVPLDPEY-PQDRLAYMLDDSGVRLLLTQ 616
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1216630836 132 KGLQKILNVQKKLPIIqkiiIMDSKTDYqgfqsmytfvTSHLPPGFNEYDFVPESfdrdktIALIMNSSGSTGLPKGVAL 211
Cdd:PRK12467 617 SHLLAQLPVPAGLRSL----CLDEPADL----------LCGYSGHNPEVALDPDN------LAYVIYTSGSTGQPKGVAI 676
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1216630836 212 PHRtACVRF--SHARDPifgnQIIPDTAILSVVPFHHGFGMFTTLGYLICGFRVVLMYR---FEEELFLRSLQDYKIQSA 286
Cdd:PRK12467 677 SHG-ALANYvcVIAERL----QLAADDSMLMVSTFAFDLGVTELFGALASGATLHLLPPdcaRDAEAFAALMADQGVTVL 751
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1216630836 287 LLVPTLFSFFAKSTLIDKydLSNLHEIASGGAPLskEVGEAVAKRFHLPGIR--QGYGLTETTSAILITPEGDDK--PGA 362
Cdd:PRK12467 752 KIVPSHLQALLQASRVAL--PRPQRALVCGGEAL--QVDLLARVRALGPGARliNHYGPTETTVGVSTYELSDEErdFGN 827
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1216630836 363 VGKVVPFFEAKVVDLDTG-KTLGVNQRGELCVRGPMIMSGYVNNP--EATNALIDKDG-----WLHSGDIAYWDEDEHFF 434
Cdd:PRK12467 828 VPIGQPLANLGLYILDHYlNPVPVGVVGELYIGGAGLARGYHRRPalTAERFVPDPFGadggrLYRTGDLARYRADGVIE 907
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1216630836 435 IVDRLKSLIKYKGYQVAPAELESILLQHPNIFDAGVAGLPDDDAGELPAAVV---VLEHGKTMTEKEIVDYVASQVTTAK 511
Cdd:PRK12467 908 YLGRMDHQVKIRGFRIELGEIEARLLAQPGVREAVVLAQPGDAGLQLVAYLVpaaVADGAEHQATRDELKAQLRQVLPDY 987
|
490 500
....*....|....*....|....
gi 1216630836 512 KLRGGVVFVDEVPKGLTGKLDaRK 535
Cdd:PRK12467 988 MVPAHLLLLDSLPLTPNGKLD-RK 1010
|
|
| PRK09029 |
PRK09029 |
O-succinylbenzoic acid--CoA ligase; Provisional |
63-496 |
6.70e-18 |
|
O-succinylbenzoic acid--CoA ligase; Provisional
Pssm-ID: 236363 [Multi-domain] Cd Length: 458 Bit Score: 86.46 E-value: 6.70e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1216630836 63 RLAEAMKRYGLNTNHRIVVCSENSLQFFMPVLGALFIGVAVAPANdiynerellnsmgiSQPTVVFvskkgLQKILNVQK 142
Cdd:PRK09029 40 QLAAGFAQQGVVEGSGVALRGKNSPETLLAYLALLQCGARVLPLN--------------PQLPQPL-----LEELLPSLT 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1216630836 143 klpiIQKIIIMDSKTDYQGfqsmytfVTSHLPPGFNEYDFVPESFDRDKTIALimnSSGSTGLPKGVALPHRT------- 215
Cdd:PRK09029 101 ----LDFALVLEGENTFSA-------LTSLHLQLVEGAHAVAWQPQRLATMTL---TSGSTGLPKAAVHTAQAhlasaeg 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1216630836 216 --ACVRFSHArdpifgnqiipDTAILSVvPFHHGFGMFTTLGYLICGFRVVLMyrfEEELFLRSLQDykIQSALLVPT-- 291
Cdd:PRK09029 167 vlSLMPFTAQ-----------DSWLLSL-PLFHVSGQGIVWRWLYAGATLVVR---DKQPLEQALAG--CTHASLVPTql 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1216630836 292 --LFSFFAKSTLidkydlsnLHEIASGGAPLSKEVGEAVAKRfhlpGIRQ--GYGLTETTSAILITpEGDDKPGaVGKVV 367
Cdd:PRK09029 230 wrLLDNRSEPLS--------LKAVLLGGAAIPVELTEQAEQQ----GIRCwcGYGLTEMASTVCAK-RADGLAG-VGSPL 295
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1216630836 368 PFFEAKVVDldtgktlgvnqrGELCVRGPMIMSGYVNNPEATnALIDKDGWLHSGDIAYWDEDEhFFIVDRLKSLIKYKG 447
Cdd:PRK09029 296 PGREVKLVD------------GEIWLRGASLALGYWRQGQLV-PLVNDEGWFATRDRGEWQNGE-LTILGRLDNLFFSGG 361
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|.
gi 1216630836 448 YQVAPAELESILLQHPNIFDAGVagLPDDDA--GELPAAVVVLEHGKTMTE 496
Cdd:PRK09029 362 EGIQPEEIERVINQHPLVQQVFV--VPVADAefGQRPVAVVESDSEAAVVN 410
|
|
| PRK07824 |
PRK07824 |
o-succinylbenzoate--CoA ligase; |
190-538 |
7.93e-18 |
|
o-succinylbenzoate--CoA ligase;
Pssm-ID: 236108 [Multi-domain] Cd Length: 358 Bit Score: 85.10 E-value: 7.93e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1216630836 190 DKTIALIMNSSGSTGLPKGvALPHRTACVRFSHARDPIFGNqiiPDTAILsVVPFHHGFGMFTTLGYLICGFRVV---LM 266
Cdd:PRK07824 34 DDDVALVVATSGTTGTPKG-AMLTAAALTASADATHDRLGG---PGQWLL-ALPAHHIAGLQVLVRSVIAGSEPVeldVS 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1216630836 267 YRFEEELFLRSLQ----DYKIQSalLVPTLFSFfAKSTLIDKYDLSNLHEIASGGAPLSKEVGEAVAKrfhlPGIR--QG 340
Cdd:PRK07824 109 AGFDPTALPRAVAelggGRRYTS--LVPMQLAK-ALDDPAATAALAELDAVLVGGGPAPAPVLDAAAA----AGINvvRT 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1216630836 341 YGLTETTSailitpegddkpGAVGKVVPFFEAKVVDLDTGKTLGvnqrgelcvrGPMIMSGYVNNPEatNALIDKDGWLH 420
Cdd:PRK07824 182 YGMSETSG------------GCVYDGVPLDGVRVRVEDGRIALG----------GPTLAKGYRNPVD--PDPFAEPGWFR 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1216630836 421 SGDIAYWDeDEHFFIVDRLKSLIKYKGYQVAPAELESILLQHPNIFDAGVAGLPDDDAGELPAAVVVLEHGKTMTEKEIV 500
Cdd:PRK07824 238 TDDLGALD-DGVLTVLGRADDAISTGGLTVLPQVVEAALATHPAVADCAVFGLPDDRLGQRVVAAVVGDGGPAPTLEALR 316
|
330 340 350 360
....*....|....*....|....*....|....*....|.
gi 1216630836 501 DYVASQ--VTTA-KKLRggvvFVDEVPKGLTGKLDARKIRE 538
Cdd:PRK07824 317 AHVARTldRTAApRELH----VVDELPRRGIGKVDRRALVR 353
|
|
| PRK08279 |
PRK08279 |
long-chain-acyl-CoA synthetase; Validated |
52-506 |
8.27e-18 |
|
long-chain-acyl-CoA synthetase; Validated
Pssm-ID: 236217 [Multi-domain] Cd Length: 600 Bit Score: 86.85 E-value: 8.27e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1216630836 52 ITYAEYFEMSVRLAEAMKRYGLNTNHRIVVCSENSLQFFMPVLGALFIGVAVAPANdiYNERE--LLNSMGISQPTVVFV 129
Cdd:PRK08279 63 ISYAELNARANRYAHWAAARGVGKGDVVALLMENRPEYLAAWLGLAKLGAVVALLN--TQQRGavLAHSLNLVDAKHLIV 140
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1216630836 130 SKKGLQKILNVQKKLPIIQKIIIMDSKTDYQgfqsmytfvtshlPPGFNEYDFVPESFDRD----------KTIALIMNS 199
Cdd:PRK08279 141 GEELVEAFEEARADLARPPRLWVAGGDTLDD-------------PEGYEDLAAAAAGAPTTnpasrsgvtaKDTAFYIYT 207
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1216630836 200 SGSTGLPKGValphrtacvRFSHAR----DPIFGN--QIIPDTAILSVVPFHHGFGMFTTLGYLIC-GFRVVLMYRFEEE 272
Cdd:PRK08279 208 SGTTGLPKAA---------VMSHMRwlkaMGGFGGllRLTPDDVLYCCLPLYHNTGGTVAWSSVLAaGATLALRRKFSAS 278
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1216630836 273 LFLRSLQDYKIqsallvpTLFSFFAKstlIDKYDLS----------NLHEIAsgGAPLSKEVGEAVAKRFHLPGIRQGYG 342
Cdd:PRK08279 279 RFWDDVRRYRA-------TAFQYIGE---LCRYLLNqppkptdrdhRLRLMI--GNGLRPDIWDEFQQRFGIPRILEFYA 346
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1216630836 343 LTETTSAiLITPEGddKPGAVGKVvPFFEAK---VV--DLDTGKTL----------GVNQRGELCV----RGPMimSGYv 403
Cdd:PRK08279 347 ASEGNVG-FINVFN--FDGTVGRV-PLWLAHpyaIVkyDVDTGEPVrdadgrcikvKPGEVGLLIGritdRGPF--DGY- 419
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1216630836 404 NNPEATNALI------DKDGWLHSGDIAYWDEDEHFFIVDRLKSLIKYKGYQVAPAELESILLQHPNIFDAGVAG--LPD 475
Cdd:PRK08279 420 TDPEASEKKIlrdvfkKGDAWFNTGDLMRDDGFGHAQFVDRLGDTFRWKGENVATTEVENALSGFPGVEEAVVYGveVPG 499
|
490 500 510
....*....|....*....|....*....|...
gi 1216630836 476 DD--AGelpAAVVVLEHGKTMTEKEIVDYVASQ 506
Cdd:PRK08279 500 TDgrAG---MAAIVLADGAEFDLAALAAHLYER 529
|
|
| PRK05691 |
PRK05691 |
peptide synthase; Validated |
193-480 |
1.11e-17 |
|
peptide synthase; Validated
Pssm-ID: 235564 [Multi-domain] Cd Length: 4334 Bit Score: 87.53 E-value: 1.11e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1216630836 193 IALIMNSSGSTGLPKGVALPHRTACVRFSHARDPiFGNQIIPDTAILSVVPFHHGFGMFTTLGYLI-CGFRVVLM---YR 268
Cdd:PRK05691 168 IAFLQYTSGSTALPKGVQVSHGNLVANEQLIRHG-FGIDLNPDDVIVSWLPLYHDMGLIGGLLQPIfSGVPCVLMspaYF 246
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1216630836 269 FEEEL-FLRSLQDY--KIQSAllvPT----LFSFFAKSTLIDKYDLSNLHEIASGGAPLSKEVGEAVAKRFHLPGIRQ-- 339
Cdd:PRK05691 247 LERPLrWLEAISEYggTISGG---PDfayrLCSERVSESALERLDLSRWRVAYSGSEPIRQDSLERFAEKFAACGFDPds 323
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1216630836 340 ---GYGLTETTSAILITPEG--------DDK--------PGAvGKVV-------PFFEAKVVDLDTGKTLGVNQRGELCV 393
Cdd:PRK05691 324 ffaSYGLAEATLFVSGGRRGqgipalelDAEalarnraePGT-GSVLmscgrsqPGHAVLIVDPQSLEVLGDNRVGEIWA 402
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1216630836 394 RGPMIMSGYVNNPEAT-NALIDKDG--WLHSGDIAYWDEDEhFFIVDRLKSLIKYKGYQVAPAELESILLQHPNIFDAG- 469
Cdd:PRK05691 403 SGPSIAHGYWRNPEASaKTFVEHDGrtWLRTGDLGFLRDGE-LFVTGRLKDMLIVRGHNLYPQDIEKTVEREVEVVRKGr 481
|
330
....*....|.
gi 1216630836 470 VAGLPDDDAGE 480
Cdd:PRK05691 482 VAAFAVNHQGE 492
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
16-534 |
1.21e-17 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 87.32 E-value: 1.21e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1216630836 16 YPLEDGtageqLHKAMK-RYALVPGTIAFtdAHIEVDITYAEYFEMSVRLAEAMKRYGLNTNHRIVVCSENSLQFFMPVL 94
Cdd:PRK12316 507 YPLQRG-----VHRLFEeQVERTPEAPAL--AFGEETLDYAELNRRANRLAHALIERGVGPDVLVGVAMERSIEMVVALL 579
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1216630836 95 GALFIGVAVAPANDIYNErELLNSMgisqptvvfVSKKGLQKILN---VQKKLPIIQKIIIMDsktdyqgfqsmYTFVTS 171
Cdd:PRK12316 580 AILKAGGAYVPLDPEYPA-ERLAYM---------LEDSGVQLLLSqshLGRKLPLAAGVQVLD-----------LDRPAA 638
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1216630836 172 HLPpgfNEYDFVPESFDRDKTIALIMNSSGSTGLPKGVALPHRTACVRFSHARDPIfgnQIIPDTAILSVVPFHHGFGMF 251
Cdd:PRK12316 639 WLE---GYSEENPGTELNPENLAYVIYTSGSTGKPKGAGNRHRALSNRLCWMQQAY---GLGVGDTVLQKTPFSFDVSVW 712
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1216630836 252 TTLGYLICGFRVVLM---YRFEEELFLRSLQDYKIQSALLVPTLFSFFAKSTLIDkyDLSNLHEIASGGAPLSKEVGEAV 328
Cdd:PRK12316 713 EFFWPLMSGARLVVAapgDHRDPAKLVELINREGVDTLHFVPSMLQAFLQDEDVA--SCTSLRRIVCSGEALPADAQEQV 790
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1216630836 329 AKRFHLPGIRQGYGLTETTsaILIT-----PEGDDKPgAVGKVVPFFEAKVVDLDTGKT-LGVnqRGELCVRGPMIMSGY 402
Cdd:PRK12316 791 FAKLPQAGLYNLYGPTEAA--IDVThwtcvEEGGDSV-PIGRPIANLACYILDANLEPVpVGV--LGELYLAGRGLARGY 865
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1216630836 403 VNNPEAT------NALIDKDGWLHSGDIAYWDEDEHFFIVDRLKSLIKYKGYQVAPAELESILLQHPNIFDAGVAGL--- 473
Cdd:PRK12316 866 HGRPGLTaerfvpSPFVAGERMYRTGDLARYRADGVIEYAGRIDHQVKLRGLRIELGEIEARLLEHPWVREAAVLAVdgk 945
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1216630836 474 -------PDDDAGELPAAVvvlehgKTMTEKEIVDY-VASQvttakklrggVVFVDEVPKGLTGKLDAR 534
Cdd:PRK12316 946 qlvgyvvLESEGGDWREAL------KAHLAASLPEYmVPAQ----------WLALERLPLTPNGKLDRK 998
|
|
| PRK05850 |
PRK05850 |
acyl-CoA synthetase; Validated |
32-510 |
1.95e-17 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 235624 [Multi-domain] Cd Length: 578 Bit Score: 85.38 E-value: 1.95e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1216630836 32 KRYALVPGTIAFTDAHIEVD-------ITYAEYFEMSVRLAEAMKRYGlNTNHRIVVCSENSLQFFMPVLGALFIG-VAV 103
Cdd:PRK05850 9 ERASLQPDDAAFTFIDYEQDpagvaetLTWSQLYRRTLNVAEELRRHG-STGDRAVILAPQGLEYIVAFLGALQAGlIAV 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1216630836 104 ---APANDIYNERelLNS-MGISQPTVVFVSKKglqkilnvqkklpiiqkiiIMDSKTDYQGFQSMYTfvtshlPPGFNE 179
Cdd:PRK05850 88 plsVPQGGAHDER--VSAvLRDTSPSVVLTTSA-------------------VVDDVTEYVAPQPGQS------APPVIE 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1216630836 180 YDF---------VPESFDRDKTiALIMNSSGSTGLPKGVALPHRTACVRFSH-ARD--PIFGNQIIPDTAILSVVPFHHG 247
Cdd:PRK05850 141 VDLldldsprgsDARPRDLPST-AYLQYTSGSTRTPAGVMVSHRNVIANFEQlMSDyfGDTGGVPPPDTTVVSWLPFYHD 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1216630836 248 FGMFttLGY---LICGFRVVLMyrfEEELFLRSLQDYkIQSALLVPTLFSF---FA------KSTLID--KYDLSNLHEI 313
Cdd:PRK05850 220 MGLV--LGVcapILGGCPAVLT---SPVAFLQRPARW-MQLLASNPHAFSAapnFAfelavrKTSDDDmaGLDLGGVLGI 293
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1216630836 314 ASGgaplSKEVGEAVAKRF-------HLP--GIRQGYGLTETTsAILITPEGDDKPGAV---------GKVVPF-FEA-- 372
Cdd:PRK05850 294 ISG----SERVHPATLKRFadrfapfNLRetAIRPSYGLAEAT-VYVATREPGQPPESVrfdyeklsaGHAKRCeTGGgt 368
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1216630836 373 -------------KVVDLDTGKTLGVNQRGELCVRGPMIMSGYVNNPEATN-----ALIDK-----DG-WLHSGDIAYWD 428
Cdd:PRK05850 369 plvsygsprsptvRIVDPDTCIECPAGTVGEIWVHGDNVAAGYWQKPEETErtfgaTLVDPspgtpEGpWLRTGDLGFIS 448
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1216630836 429 EDEhFFIVDRLKSLIKYKGYQVAPAELESILLQhpnIFDAGVAGL--PDDDAGELPAAVVVLEHGKTMTE-KEIVDYVAS 505
Cdd:PRK05850 449 EGE-LFIVGRIKDLLIVDGRNHYPDDIEATIQE---ITGGRVAAIsvPDDGTEKLVAIIELKKRGDSDEEaMDRLRTVKR 524
|
....*
gi 1216630836 506 QVTTA 510
Cdd:PRK05850 525 EVTSA 529
|
|
| prpE |
PRK10524 |
propionyl-CoA synthetase; Provisional |
196-539 |
3.20e-17 |
|
propionyl-CoA synthetase; Provisional
Pssm-ID: 182517 [Multi-domain] Cd Length: 629 Bit Score: 85.00 E-value: 3.20e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1216630836 196 IMNSSGSTGLPKGVALPHRTACVRFSHARDPIFGNQiipdtailsvvpfhHGFGMFTT-------------LGYLICGFR 262
Cdd:PRK10524 238 ILYTSGTTGKPKGVQRDTGGYAVALATSMDTIFGGK--------------AGETFFCAsdigwvvghsyivYAPLLAGMA 303
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1216630836 263 VVlMYrfeEELFLRS--------LQDYKIQSALLVPTLFSFFAKS--TLIDKYDLSNLHEIASGGAPLSKEVGEAVAKRF 332
Cdd:PRK10524 304 TI-MY---EGLPTRPdagiwwriVEKYKVNRMFSAPTAIRVLKKQdpALLRKHDLSSLRALFLAGEPLDEPTASWISEAL 379
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1216630836 333 HLPgIRQGYGLTETTSAIL-ITPEGDDKP---GAVGKVVPFFEAKVVDLDTGKTLGVNQRGELCVRGPM----------- 397
Cdd:PRK10524 380 GVP-VIDNYWQTETGWPILaIARGVEDRPtrlGSPGVPMYGYNVKLLNEVTGEPCGPNEKGVLVIEGPLppgcmqtvwgd 458
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1216630836 398 ---IMSGYvnnpeatnalidkdgWLHSGDIAY----W---DEDEHFFIVDRLKSLIKYKGYQVAPAELESILLQHPNIFD 467
Cdd:PRK10524 459 ddrFVKTY---------------WSLFGRQVYstfdWgirDADGYYFILGRTDDVINVAGHRLGTREIEESISSHPAVAE 523
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1216630836 468 AGVAGLPDDDAGELPAAVVVLEHGKTMT--------EKEIVDYVASQV-TTAKKLRggVVFVDEVPKGLTGKLDARKIRE 538
Cdd:PRK10524 524 VAVVGVKDALKGQVAVAFVVPKDSDSLAdrearlalEKEIMALVDSQLgAVARPAR--VWFVSALPKTRSGKLLRRAIQA 601
|
.
gi 1216630836 539 I 539
Cdd:PRK10524 602 I 602
|
|
| A_NRPS_acs4 |
cd17654 |
acyl-CoA synthetase family member 4; This family of the adenylation (A) domain of nonribosomal ... |
50-532 |
3.62e-17 |
|
acyl-CoA synthetase family member 4; This family of the adenylation (A) domain of nonribosomal peptide synthases (NRPS) contains acyl-CoA synthethase family member 4, also known as 2-aminoadipic 6-semialdehyde dehydrogenase or aminoadipate-semialdehyde dehydrogenase, most of which are uncharacterized. Acyl-CoA synthetase catalyzes the initial reaction in fatty acid metabolism, by forming a thioester with CoA. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.
Pssm-ID: 341309 [Multi-domain] Cd Length: 449 Bit Score: 84.06 E-value: 3.62e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1216630836 50 VDITYAEYFEMSVRLAEAMKRYGLNTNHRIVVCSENSLQFFMPVLGALFIGVAVAPandiynerelLNSMGISQPTVVFV 129
Cdd:cd17654 15 TTVSYADLAEKISNLSNFLRKKFQTEERAIGLRCDRGTESPVAILAILFLGAAYAP----------IDPASPEQRSLTVM 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1216630836 130 SKKGLQKIL----NVQKKLPIIQKIIIMDSKTDYqgfqsmytfvtshlppgfneydfvpesfdrdkTIALIMNSSGSTGL 205
Cdd:cd17654 85 KKCHVSYLLqnkeLDNAPLSFTPEHRHFNIRTDE--------------------------------CLAYVIHTSGTTGT 132
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1216630836 206 PKGVALPHRtaCVR--FSHARD--PIFGNQIIPDTAIL----SVVPFhhgFGMFTTLGYLICgfrVVLMYRFEEELFLRS 277
Cdd:cd17654 133 PKIVAVPHK--CILpnIQHFRSlfNITSEDILFLTSPLtfdpSVVEI---FLSLSSGATLLI---VPTSVKVLPSKLADI 204
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1216630836 278 L-QDYKIQSALLVPTLFSFF----AKSTLIDKydLSNLHEIASGGAPLSKEVgEAVAKRFHLPGIR--QGYGLTETTS-A 349
Cdd:cd17654 205 LfKRHRITVLQATPTLFRRFgsqsIKSTVLSA--TSSLRVLALGGEPFPSLV-ILSSWRGKGNRTRifNIYGITEVSCwA 281
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1216630836 350 IL-ITPEGdDKPGAVGKVVPFFEAKVVDLDTGKTLGVNQRGELCVRGpmIMSGYVNNPEATnalidkdgWLHSGDIAYWD 428
Cdd:cd17654 282 LAyKVPEE-DSPVQLGSPLLGTVIEVRDQNGSEGTGQVFLGGLNRVC--ILDDEVTVPKGT--------MRATGDFVTVK 350
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1216630836 429 EDEHFFiVDRLKSLIKYKGYQVAPAELESILLQHPNIFDAGVAgLPDDdagELPAAVVVLEHGKTMTEKEIVDYVASqvt 508
Cdd:cd17654 351 DGELFF-LGRKDSQIKRRGKRINLDLIQQVIESCLGVESCAVT-LSDQ---QRLIAFIVGESSSSRIHKELQLTLLS--- 422
|
490 500
....*....|....*....|....
gi 1216630836 509 tAKKLRGGVVFVDEVPKGLTGKLD 532
Cdd:cd17654 423 -SHAIPDTFVQIDKLPLTSHGKVD 445
|
|
| PRK07769 |
PRK07769 |
long-chain-fatty-acid--CoA ligase; Validated |
78-456 |
1.30e-16 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 181109 [Multi-domain] Cd Length: 631 Bit Score: 83.24 E-value: 1.30e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1216630836 78 RIVVCSENSLQFFMPVLGALFIG-VAV---APANDIYNEReLLNSMGISQPTVVFVSKKGLQKILNVQKKLPIIQK--II 151
Cdd:PRK07769 81 RVAILAPQNLDYLIAFFGALYAGrIAVplfDPAEPGHVGR-LHAVLDDCTPSAILTTTDSAEGVRKFFRARPAKERprVI 159
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1216630836 152 IMDSKTDYQGfqSMYtfvtshlppgfneydfVPESFDRDkTIALIMNSSGSTGLPKGVALPHRTACVRFSHARDPIFGNQ 231
Cdd:PRK07769 160 AVDAVPDEVG--ATW----------------VPPEANED-TIAYLQYTSGSTRIPAGVQITHLNLPTNVLQVIDALEGQE 220
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1216630836 232 iipDTAILSVVPFHHGFGMFTTLGYLICGFRVVLM---------YRFEEELFLRSLQDYKIQSALlvPTlFSF-FAKSTL 301
Cdd:PRK07769 221 ---GDRGVSWLPFFHDMGLITVLLPALLGHYITFMspaafvrrpGRWIRELARKPGGTGGTFSAA--PN-FAFeHAAARG 294
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1216630836 302 IDK-----YDLSNLHEIASGGAPLS----KEVGEAVAKrFHLP--GIRQGYGLTETTSAILITPEGD------------- 357
Cdd:PRK07769 295 LPKdgeppLDLSNVKGLLNGSEPVSpasmRKFNEAFAP-YGLPptAIKPSYGMAEATLFVSTTPMDEeptviyvdrdeln 373
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1216630836 358 ---------DKPGAV-----GKVVPFFEAKVVDLDTGKTLGVNQRGELCVRGPMIMSGYVNNPEATNALI---------- 413
Cdd:PRK07769 374 agrfvevpaDAPNAVaqvsaGKVGVSEWAVIVDPETASELPDGQIGEIWLHGNNIGTGYWGKPEETAATFqnilksrlse 453
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|
gi 1216630836 414 -------DKDGWLHSGDIAYWdEDEHFFIVDRLKSLIKYKGYQVAPAELE 456
Cdd:PRK07769 454 shaegapDDALWVRTGDYGVY-FDGELYITGRVKDLVIIDGRNHYPQDLE 502
|
|
| AMP-binding_C |
pfam13193 |
AMP-binding enzyme C-terminal domain; This is a small domain that is found C terminal to ... |
454-530 |
1.37e-16 |
|
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: 74.50 E-value: 1.37e-16
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1216630836 454 ELESILLQHPNIFDAGVAGLPDDDAGELPAAVVVLEHGKTMTEKEIVDYVASQVTTAKKLRgGVVFVDEVPKGLTGK 530
Cdd:pfam13193 1 EVESALVSHPAVAEAAVVGVPDELKGEAPVAFVVLKPGVELLEEELVAHVREELGPYAVPK-EVVFVDELPKTRSGK 76
|
|
| PRK12467 |
PRK12467 |
peptide synthase; Provisional |
49-535 |
1.95e-16 |
|
peptide synthase; Provisional
Pssm-ID: 237108 [Multi-domain] Cd Length: 3956 Bit Score: 83.29 E-value: 1.95e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1216630836 49 EVDITYAEYFEMSVRLAEAMKRYGLNTNHRIVVCSENSLQFFMPVLGALFIGVAVAPAnDIYNERELLNSMgisqptvvf 128
Cdd:PRK12467 3118 DQQLSYAELNRRANRLAHRLIAIGVGPDVLVGVAVERSVEMIVALLAVLKAGGAYVPL-DPEYPRERLAYM--------- 3187
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1216630836 129 VSKKGLQKILNVQ---KKLPIIQ--KIIIMDsKTDYQGfqsmytfvtshlppgfnEYDFVPESFDRDKTIALIMNSSGST 203
Cdd:PRK12467 3188 IEDSGVKLLLTQAhllEQLPAPAgdTALTLD-RLDLNG-----------------YSENNPSTRVMGENLAYVIYTSGST 3249
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1216630836 204 GLPKGVALPHrTACVRFSHARDPIFGnqIIPDTAILSVVPFHHGFGMFTTLGYLICGFRVVLM---YRFEEELFlRSLQD 280
Cdd:PRK12467 3250 GKPKGVGVRH-GALANHLCWIAEAYE--LDANDRVLLFMSFSFDGAQERFLWTLICGGCLVVRdndLWDPEELW-QAIHA 3325
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1216630836 281 YKIQSALLVPTLFSFFAKSTliDKYDLSNLHEIASGGAPLSKEVGEAVAKRFHLPGIRQGYGLTETT-SAILITPEGDDK 359
Cdd:PRK12467 3326 HRISIACFPPAYLQQFAEDA--GGADCASLDIYVFGGEAVPPAAFEQVKRKLKPRGLTNGYGPTEAVvTVTLWKCGGDAV 3403
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1216630836 360 PGA----VGKVVPFFEAKVVDlDTGKTLGVNQRGELCVRGPMIMSGYVNNPEAT------NALIDKDGWLH-SGDIAYWD 428
Cdd:PRK12467 3404 CEApyapIGRPVAGRSIYVLD-GQLNPVPVGVAGELYIGGVGLARGYHQRPSLTaerfvaDPFSGSGGRLYrTGDLARYR 3482
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1216630836 429 EDEHFFIVDRLKSLIKYKGYQVAPAELESILLQHPNIFDAGVAGLPDDDAGELPAAVVVLEHGKTMTEK-------EIVD 501
Cdd:PRK12467 3483 ADGVIEYLGRIDHQVKIRGFRIELGEIEARLLQHPSVREAVVLARDGAGGKQLVAYVVPADPQGDWRETlrdhlaaSLPD 3562
|
490 500 510
....*....|....*....|....*....|....*
gi 1216630836 502 Y-VASQvttakklrggVVFVDEVPKGLTGKLDaRK 535
Cdd:PRK12467 3563 YmVPAQ----------LLVLAAMPLGPNGKVD-RK 3586
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
16-535 |
6.20e-16 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 81.93 E-value: 6.20e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1216630836 16 YPLEDGTagEQLHKAMKRYALVPGTIAFTDAHIevdiTYAEYFEMSVRLAEAMKRYGLNTNHRIVVCSENSLQFFMPVLG 95
Cdd:PRK12316 3053 YPLERGV--HRLFEEQVERTPDAVALAFGEQRL----SYAELNRRANRLAHRLIERGVGPDVLVGVAVERSLEMVVGLLA 3126
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1216630836 96 ALFIGVAVAPANDIYNERELLNSMGISqptvvfvskkGLQKILNVQK-KLPIIQKIIIMDSKTDYQGFQSMYtfvtshlp 174
Cdd:PRK12316 3127 ILKAGGAYVPLDPEYPEERLAYMLEDS----------GAQLLLSQSHlRLPLAQGVQVLDLDRGDENYAEAN-------- 3188
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1216630836 175 pgfneydfvPESFDRDKTIALIMNSSGSTGLPKGVALPHRTACvrfSHARDPIFGNQIIPDTAILSVVPFHHGFGMFTTL 254
Cdd:PRK12316 3189 ---------PAIRTMPENLAYVIYTSGSTGKPKGVGIRHSALS---NHLCWMQQAYGLGVGDRVLQFTTFSFDVFVEELF 3256
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1216630836 255 GYLICGFRVVLMYRfEEELFLRSLQDYKIQSALLVPTLFSFFAKSTL--IDKYDLSNLHEIASGGAPLSkevGEAVAKRF 332
Cdd:PRK12316 3257 WPLMSGARVVLAGP-EDWRDPALLVELINSEGVDVLHAYPSMLQAFLeeEDAHRCTSLKRIVCGGEALP---ADLQQQVF 3332
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1216630836 333 HLPGIRQGYGLTETTSAILITPEGDDKPGA--VGKVVPFFEAKVVDlDTGKTLGVNQRGELCVRGPMIMSGYVNNPEAT- 409
Cdd:PRK12316 3333 AGLPLYNLYGPTEATITVTHWQCVEEGKDAvpIGRPIANRACYILD-GSLEPVPVGALGELYLGGEGLARGYHNRPGLTa 3411
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1216630836 410 -----NALIDKDGWLHSGDIAYWDEDEHFFIVDRLKSLIKYKGYQVAPAELESILLQHPNIFDAGVAG----------LP 474
Cdd:PRK12316 3412 erfvpDPFVPGERLYRTGDLARYRADGVIEYIGRVDHQVKIRGFRIELGEIEARLLEHPWVREAVVLAvdgrqlvayvVP 3491
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1216630836 475 DDDAGELPAAVvvlehgKTMTEKEIVDY-VASQvttakklrggVVFVDEVPKGLTGKLDaRK 535
Cdd:PRK12316 3492 EDEAGDLREAL------KAHLKASLPEYmVPAH----------LLFLERMPLTPNGKLD-RK 3536
|
|
| A_NRPS_TlmIV_like |
cd12114 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including ... |
38-534 |
1.03e-15 |
|
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: 79.62 E-value: 1.03e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1216630836 38 PGTIAFTDAhiEVDITYAEYFEMSVRLAEAMKRYGLNTNHRIVVCSENSLQFFMPVLGALFIGVAVAPandiynerelln 117
Cdd:cd12114 1 PDATAVICG--DGTLTYGELAERARRVAGALKAAGVRPGDLVAVTLPKGPEQVVAVLGILAAGAAYVP------------ 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1216630836 118 sMGISQPtvvfvsKKGLQKILNVQKklpiiQKIIIMDSkTDYQGFQSMYTFVTSHLPPGFNEYDFVPESFDRDKTiALIM 197
Cdd:cd12114 67 -VDIDQP------AARREAILADAG-----ARLVLTDG-PDAQLDVAVFDVLILDLDALAAPAPPPPVDVAPDDL-AYVI 132
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1216630836 198 NSSGSTGLPKGVALPHRtACV--------RFshardpifgnQIIPDTAILSVVPFHHGFGMFTTLGYLICGFRVVLMYRF 269
Cdd:cd12114 133 FTSGSTGTPKGVMISHR-AALntildinrRF----------AVGPDDRVLALSSLSFDLSVYDIFGALSAGATLVLPDEA 201
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1216630836 270 EEE---LFLRSLQDYKIQSALLVPTLFSFFAKSTLIDKYDLSNLHEIASGG--APLSKEvgEAVAKRFhlPGIRQ---Gy 341
Cdd:cd12114 202 RRRdpaHWAELIERHGVTLWNSVPALLEMLLDVLEAAQALLPSLRLVLLSGdwIPLDLP--ARLRALA--PDARLislG- 276
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1216630836 342 GLTETT--SAILITPEGDDKPGAV--GKVVPFFEAKVVDlDTGKTLGVNQRGELCVRGPMIMSGYVNNPEATNA--LIDK 415
Cdd:cd12114 277 GATEASiwSIYHPIDEVPPDWRSIpyGRPLANQRYRVLD-PRGRDCPDWVPGELWIGGRGVALGYLGDPELTAArfVTHP 355
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1216630836 416 DG--WLHSGDIAYWDEDEHFFIVDRLKSLIKYKGYQVAPAELESILLQHPNIFDAGVAGLPDDDAGELpAAVVVLEHGKT 493
Cdd:cd12114 356 DGerLYRTGDLGRYRPDGTLEFLGRRDGQVKVRGYRIELGEIEAALQAHPGVARAVVVVLGDPGGKRL-AAFVVPDNDGT 434
|
490 500 510 520
....*....|....*....|....*....|....*....|.
gi 1216630836 494 MTEKEIVDYVASQVTTAKKLRGGVVFVDEVPKGLTGKLDAR 534
Cdd:cd12114 435 PIAPDALRAFLAQTLPAYMIPSRVIALEALPLTANGKVDRA 475
|
|
| A_NRPS_PpsD_like |
cd17650 |
similar to adenylation domain of plipastatin synthase (PpsD); This family of the adenylation ... |
193-534 |
1.68e-15 |
|
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: 79.05 E-value: 1.68e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1216630836 193 IALIMNSSGSTGLPKGVALPHRTAcVRFSHARDPIFGNQIIPdTAILSVVPFhhGFGMFTT--LGYLICGFRVVLM---Y 267
Cdd:cd17650 95 LAYVIYTSGTTGKPKGVMVEHRNV-AHAAHAWRREYELDSFP-VRLLQMASF--SFDVFAGdfARSLLNGGTLVICpdeV 170
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1216630836 268 RFEEELFLRSLQDYKIQSALLVPTLFSFFAKSTLIDKYDLSNLHEIASGGAPLSKEVGEAVAKRFhLPGIR--QGYGLTE 345
Cdd:cd17650 171 KLDPAALYDLILKSRITLMESTPALIRPVMAYVYRNGLDLSAMRLLIVGSDGCKAQDFKTLAARF-GQGMRiiNSYGVTE 249
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1216630836 346 TTSAILITPEGDDKPGA-----VGKVVPFFEAKVVDlDTGKTLGVNQRGELCVRGPMIMSGYVNNPEAT------NALID 414
Cdd:cd17650 250 ATIDSTYYEEGRDPLGDsanvpIGRPLPNTAMYVLD-ERLQPQPVGVAGELYIGGAGVARGYLNRPELTaerfveNPFAP 328
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1216630836 415 KDGWLHSGDIAYWDEDEHFFIVDRLKSLIKYKGYQVAPAELESILLQHPNIFDAGVAGLPDDDAGELPAAVVVLEHgkTM 494
Cdd:cd17650 329 GERMYRTGDLARWRADGNVELLGRVDHQVKIRGFRIELGEIESQLARHPAIDEAVVAVREDKGGEARLCAYVVAAA--TL 406
|
330 340 350 360
....*....|....*....|....*....|....*....|
gi 1216630836 495 TEKEIVDYVASQVTTAkKLRGGVVFVDEVPKGLTGKLDAR 534
Cdd:cd17650 407 NTAELRAFLAKELPSY-MIPSYYVQLDALPLTPNGKVDRR 445
|
|
| PRK05691 |
PRK05691 |
peptide synthase; Validated |
52-538 |
1.71e-15 |
|
peptide synthase; Validated
Pssm-ID: 235564 [Multi-domain] Cd Length: 4334 Bit Score: 80.21 E-value: 1.71e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1216630836 52 ITYAEYFEMSVRLAEAMKRYGLNTNHRIVVCSENSLQFFMPVLGALFIGVAVAPANDIYNERELLNSMGISQPTVVFVSK 131
Cdd:PRK05691 1157 LDYAELHAQANRLAHYLRDKGVGPDVCVAIAAERSPQLLVGLLAILKAGGAYVPLDPDYPAERLAYMLADSGVELLLTQS 1236
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1216630836 132 KGLQKILNVQKKLPIIQKIIIMDSKTDYqgfqsmytfvtshlPPGFNEYDfvpesfdrdKTIALIMNSSGSTGLPKGVAL 211
Cdd:PRK05691 1237 HLLERLPQAEGVSAIALDSLHLDSWPSQ--------------APGLHLHG---------DNLAYVIYTSGSTGQPKGVGN 1293
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1216630836 212 PHRTACVRFSHARDPIfgnQIIPDTAILSVVPFHHGFGMFTTLGYLICGFRVVLMYRFEE---ELFLRSLQDYKIQSALL 288
Cdd:PRK05691 1294 THAALAERLQWMQATY---ALDDSDVLMQKAPISFDVSVWECFWPLITGCRLVLAGPGEHrdpQRIAELVQQYGVTTLHF 1370
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1216630836 289 VPTLFSFFAKSTLIDkyDLSNLHEIASGGAPLSKEVGEAVAKRfhLPGIR--QGYGLTETtsAILIT------PEGDDKP 360
Cdd:PRK05691 1371 VPPLLQLFIDEPLAA--ACTSLRRLFSGGEALPAELRNRVLQR--LPQVQlhNRYGPTET--AINVThwqcqaEDGERSP 1444
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1216630836 361 gaVGKVVPFFEAKVVDLDTGKT-LGVnqRGELCVRGPMIMSGYVNNP--EATNALIDKDG-----WLHSGDIAYWDEDEH 432
Cdd:PRK05691 1445 --IGRPLGNVLCRVLDAELNLLpPGV--AGELCIGGAGLARGYLGRPalTAERFVPDPLGedgarLYRTGDRARWNADGA 1520
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1216630836 433 FFIVDRLKSLIKYKGYQVAPAELESILLQHPNIFDAGVAgLPDDDAGE--------LPAAVVVLEHGKTMTEKEIVDY-V 503
Cdd:PRK05691 1521 LEYLGRLDQQVKLRGFRVEPEEIQARLLAQPGVAQAAVL-VREGAAGAqlvgyytgEAGQEAEAERLKAALAAELPEYmV 1599
|
490 500 510
....*....|....*....|....*....|....*
gi 1216630836 504 ASQvttakklrggVVFVDEVPKGLTGKLDARKIRE 538
Cdd:PRK05691 1600 PAQ----------LIRLDQMPLGPSGKLDRRALPE 1624
|
|
| A_NRPS_ACVS-like |
cd17648 |
N-(5-amino-5-carboxypentanoyl)-L-cysteinyl-D-valine synthase; This family contains ACV ... |
191-536 |
4.85e-15 |
|
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: 77.44 E-value: 4.85e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1216630836 191 KTIALIMNSSGSTGLPKGVALPHRTAcVRFSHARDPIFGNQIIPDTAILSVVPFHHGFGMFTTLGYLICGFRVVLM---Y 267
Cdd:cd17648 94 TDLAYAIYTSGTTGKPKGVLVEHGSV-VNLRTSLSERYFGRDNGDEAVLFFSNYVFDFFVEQMTLALLNGQKLVVPpdeM 172
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1216630836 268 RFEEELFLRSLQDYKIqsallvpTLFSffAKSTLIDKYDLS---NLHEIASGGAPLSKEVGEAVAKRFhlPG-IRQGYGL 343
Cdd:cd17648 173 RFDPDRFYAYINREKV-------TYLS--GTPSVLQQYDLArlpHLKRVDAAGEEFTAPVFEKLRSRF--AGlIINAYGP 241
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1216630836 344 TETTSAILITPEGDDKP--GAVGKVVPFFEAKVVDLDTgKTLGVNQRGELCVRGPMIMSGYVNNPEAT------------ 409
Cdd:cd17648 242 TETTVTNHKRFFPGDQRfdKSLGRPVRNTKCYVLNDAM-KRVPVGAVGELYLGGDGVARGYLNRPELTaerflpnpfqte 320
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1216630836 410 -------NALIDKDG----WLHSGDIAYwdedehffiVDRLKSLIKYKGYQVAPAELESILLQHPNIFDAGVagLPDDDA 478
Cdd:cd17648 321 qerargrNARLYKTGdlvrWLPSGELEY---------LGRNDFQVKIRGQRIEPGEVEAALASYPGVRECAV--VAKEDA 389
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1216630836 479 GELPAAVV-------VLEHGkTMTEKEIVDYVASQVTTAkKLRGGVVFVDEVPKGLTGKLDARKI 536
Cdd:cd17648 390 SQAQSRIQkylvgyyLPEPG-HVPESDLLSFLRAKLPRY-MVPARLVRLEGIPVTINGKLDVRAL 452
|
|
| PRK04813 |
PRK04813 |
D-alanine--poly(phosphoribitol) ligase subunit DltA; |
38-536 |
5.47e-15 |
|
D-alanine--poly(phosphoribitol) ligase subunit DltA;
Pssm-ID: 235313 [Multi-domain] Cd Length: 503 Bit Score: 77.63 E-value: 5.47e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1216630836 38 PGTIAFtdAHIEVDITYAEYFEMSVRLAEAMKRYGLNTNHRIVVCSENSlqFFMPV--LGALFIGVAVAPAnDIYNEREL 115
Cdd:PRK04813 16 PDFPAY--DYLGEKLTYGQLKEDSDALAAFIDSLKLPDKSPIIVFGHMS--PEMLAtfLGAVKAGHAYIPV-DVSSPAER 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1216630836 116 LNS-MGISQPTVVFVSKKGLQKILNVqkklPIIQKIIIMDSKtdyqgfqsmytfvtshlppgFNEYDFVPESFDRDKTIA 194
Cdd:PRK04813 91 IEMiIEVAKPSLIIATEELPLEILGI----PVITLDELKDIF--------------------ATGNPYDFDHAVKGDDNY 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1216630836 195 LIMNSSGSTGLPKGVALPHRT-------ACVRFSHARDPIFGNQIiP---DTAILSVVPfhhgfgMFTTLGYLICGFRVV 264
Cdd:PRK04813 147 YIIFTSGTTGKPKGVQISHDNlvsftnwMLEDFALPEGPQFLNQA-PysfDLSVMDLYP------TLASGGTLVALPKDM 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1216630836 265 LMyRFEEeLFlRSLQDYKI----------QSALLVPTLfsffakstliDKYDLSNLHEIASGGAPLSKEVGEAVAKRFHL 334
Cdd:PRK04813 220 TA-NFKQ-LF-ETLPQLPInvwvstpsfaDMCLLDPSF----------NEEHLPNLTHFLFCGEELPHKTAKKLLERFPS 286
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1216630836 335 PGIRQGYGLTETT---SAILITPEGDDK--PGAVGKVVPFFEAKVVDlDTGKTLGVNQRGELCVRGPMIMSGYVNNPEAT 409
Cdd:PRK04813 287 ATIYNTYGPTEATvavTSIEITDEMLDQykRLPIGYAKPDSPLLIID-EEGTKLPDGEQGEIVISGPSVSKGYLNNPEKT 365
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1216630836 410 N-ALIDKDGW--LHSGDIAYWDeDEHFFIVDRLKSLIKYKGYQVapaELESI---LLQHPNIFDAGVAGLPDDDAGELPA 483
Cdd:PRK04813 366 AeAFFTFDGQpaYHTGDAGYLE-DGLLFYQGRIDFQIKLNGYRI---ELEEIeqnLRQSSYVESAVVVPYNKDHKVQYLI 441
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1216630836 484 AVVVLEHGKtmTEKEIvdyvasQVTTA--KKLRGGV---------VFVDEVPKGLTGKLDARKI 536
Cdd:PRK04813 442 AYVVPKEED--FEREF------ELTKAikKELKERLmeymiprkfIYRDSLPLTPNGKIDRKAL 497
|
|
| PRK05851 |
PRK05851 |
long-chain-fatty acid--ACP ligase MbtM; |
296-531 |
9.61e-15 |
|
long-chain-fatty acid--ACP ligase MbtM;
Pssm-ID: 180289 [Multi-domain] Cd Length: 525 Bit Score: 76.73 E-value: 9.61e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1216630836 296 FAKStLIDKY-------DLSNLHEIASGGAPLSKE----VGEAVAkRFHL-PG-IRQGYGLTETTSAI------------ 350
Cdd:PRK05851 254 FAYN-LIGKYarrvsdvDLGALRVALNGGEPVDCDgferFATAMA-PFGFdAGaAAPSYGLAESTCAVtvpvpgiglrvd 331
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1216630836 351 -LITPEGD--DKPGAVGKVVPFFEAKVVDLDTGKTLGVNQRGELCVRGPMIMSGYVNNPEatnalIDKDGWLHSGDIAYW 427
Cdd:PRK05851 332 eVTTDDGSgaRRHAVLGNPIPGMEVRISPGDGAAGVAGREIGEIEIRGASMMSGYLGQAP-----IDPDDWFPTGDLGYL 406
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1216630836 428 DEDEhFFIVDRLKSLIKYKGYQVAPAELESILLQHPNIFDAGVAGLPDDDAGELPAAVVVLEH---GKTMTEKEIVDYVA 504
Cdd:PRK05851 407 VDGG-LVVCGRAKELITVAGRNIFPTEIERVAAQVRGVREGAVVAVGTGEGSARPGLVIAAEFrgpDEAGARSEVVQRVA 485
|
250 260 270
....*....|....*....|....*....|.
gi 1216630836 505 SQ--VTTAKklrggVVFVD--EVPKGLTGKL 531
Cdd:PRK05851 486 SEcgVVPSD-----VVFVApgSLPRTSSGKL 511
|
|
| PRK07445 |
PRK07445 |
O-succinylbenzoic acid--CoA ligase; Reviewed |
307-541 |
1.27e-14 |
|
O-succinylbenzoic acid--CoA ligase; Reviewed
Pssm-ID: 236019 [Multi-domain] Cd Length: 452 Bit Score: 76.19 E-value: 1.27e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1216630836 307 LSNLHEIASGGAPLSKEVGEAvAKRFHLPgIRQGYGLTETTSAIL-ITPE----GDDkpgAVGKVVPffEAKVvdldtgk 381
Cdd:PRK07445 229 LAQFRTILLGGAPAWPSLLEQ-ARQLQLR-LAPTYGMTETASQIAtLKPDdflaGNN---SSGQVLP--HAQI------- 294
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1216630836 382 TLGVNQRGELCVRGPMIMSGYVnnPEatnaLIDKDGWLHSGDIAYWDEDEHFFIVDRLKSLIKYKGYQVAPAELESILLQ 461
Cdd:PRK07445 295 TIPANQTGNITIQAQSLALGYY--PQ----ILDSQGIFETDDLGYLDAQGYLHILGRNSQKIITGGENVYPAEVEAAILA 368
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1216630836 462 HPNIFDAGVAGLPDDDAGELPAAVVVLEHGKTMTEkEIVDYVASQVTTAKKLRGGVVfVDEVPKGLTGKLDARKIREILI 541
Cdd:PRK07445 369 TGLVQDVCVLGLPDPHWGEVVTAIYVPKDPSISLE-ELKTAIKDQLSPFKQPKHWIP-VPQLPRNPQGKINRQQLQQIAV 446
|
|
| PRK06060 |
PRK06060 |
p-hydroxybenzoic acid--AMP ligase FadD22; |
289-531 |
3.83e-14 |
|
p-hydroxybenzoic acid--AMP ligase FadD22;
Pssm-ID: 180374 [Multi-domain] Cd Length: 705 Bit Score: 75.45 E-value: 3.83e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1216630836 289 VPTLFSFFAKSTLIDKYdlSNLHEIASGGAPLSKEVGEAVAKRFHLPGIRQGYGLTETTSAILITPEGDDKPGAVGKVVP 368
Cdd:PRK06060 243 VPNFFARVIDSCSPDSF--RSLRCVVSAGEALELGLAERLMEFFGGIPILDGIGSTEVGQTFVSNRVDEWRLGTLGRVLP 320
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1216630836 369 FFEAKVVDLDtGKTLGVNQRGELCVRGPMIMSGYVNNPEatnALIDKDGWLHSGDIAYWDEDEHFFIVDRLKSLIKYKGY 448
Cdd:PRK06060 321 PYEIRVVAPD-GTTAGPGVEGDLWVRGPAIAKGYWNRPD---SPVANEGWLDTRDRVCIDSDGWVTYRCRADDTEVIGGV 396
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1216630836 449 QVAPAELESILLQHPNIFDAGVAGLPDDDAGELPAAVVVLEHGKTMTEKEIVDYVASQVT--TAKKLRGGVVFVDEVPKG 526
Cdd:PRK06060 397 NVDPREVERLIIEDEAVAEAAVVAVRESTGASTLQAFLVATSGATIDGSVMRDLHRGLLNrlSAFKVPHRFAVVDRLPRT 476
|
....*
gi 1216630836 527 LTGKL 531
Cdd:PRK06060 477 PNGKL 481
|
|
| AFD_CAR-like |
cd17632 |
adenylation domain of carboxylic acid reductase (CAR); This family contains the adenylation ... |
190-465 |
4.03e-14 |
|
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: 75.18 E-value: 4.03e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1216630836 190 DKTIALIMNSSGSTGLPKGVALPHRTAcVRFSHARDPIFGNQiiPDTAI-LSVVPFHHGFG---MFTTL-----GY---- 256
Cdd:cd17632 222 DDPLALLIYTSGSTGTPKGAMYTERLV-ATFWLKVSSIQDIR--PPASItLNFMPMSHIAGrisLYGTLarggtAYfaaa 298
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1216630836 257 -----------LICGFRVVLMYRFEEELFLR--SLQDYKIQSALLVPTLfSFFAKSTLIDKYDLSNLHEIASGGAPLSKE 323
Cdd:cd17632 299 sdmstlfddlaLVRPTELFLVPRVCDMLFQRyqAELDRRSVAGADAETL-AERVKAELRERVLGGRLLAAVCGSAPLSAE 377
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1216630836 324 VGEAVAKRFHLPgIRQGYGLTETTSAILItpegddkpgavGKVV--PFFEAKVVDL-DTG--KTLGVNQRGELCVRGPMI 398
Cdd:cd17632 378 MKAFMESLLDLD-LHDGYGSTEAGAVILD-----------GVIVrpPVLDYKLVDVpELGyfRTDRPHPRGELLVKTDTL 445
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1216630836 399 MSGYVNNPEATNALIDKDGWLHSGDIAYWDEDEHFFIVDRLKSLIKY-KGYQVAPAELESILLQHPNI 465
Cdd:cd17632 446 FPGYYKRPEVTAEVFDEDGFYRTGDVMAELGPDRLVYVDRRNNVLKLsQGEFVTVARLEAVFAASPLV 513
|
|
| PTZ00342 |
PTZ00342 |
acyl-CoA synthetase; Provisional |
309-444 |
1.24e-13 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 240370 [Multi-domain] Cd Length: 746 Bit Score: 73.60 E-value: 1.24e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1216630836 309 NLHEIASGGAPLSKEVGEAVAKRFHLpGIRQGYGLTETTSAILITPEGDDKPGAVG-KVVPFFEAKVVDLDTGKTLGVNQ 387
Cdd:PTZ00342 462 NLEVILNGGGKLSPKIAEELSVLLNV-NYYQGYGLTETTGPIFVQHADDNNTESIGgPISPNTKYKVRTWETYKATDTLP 540
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*..
gi 1216630836 388 RGELCVRGPMIMSGYVNNPEATNALIDKDGWLHSGDIAYWDEDEHFFIVDRLKSLIK 444
Cdd:PTZ00342 541 KGELLIKSDSIFSGYFLEKEQTKNAFTEDGYFKTGDIVQINKNGSLTFLDRSKGLVK 597
|
|
| hsFATP4_like |
cd05939 |
Fatty acid transport proteins (FATP), including FATP4 and FATP1, and similar proteins; Fatty ... |
53-537 |
1.17e-12 |
|
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: 70.15 E-value: 1.17e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1216630836 53 TYAEYFEMSVRLAEAMKRYGLNTNHRIVVCSENSLQFFMPVLGALFIGVAVAPANDIYNERELLNSMGISQPTVVFVSKk 132
Cdd:cd05939 5 TFRELNEYSNKVANFFQAQGYRSGDVVALFMENRLEFVALWLGLAKIGVETALINSNLRLESLLHCITVSKAKALIFNL- 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1216630836 133 gLQKILNVQKKLPIIQKIIIMDSKTDYqgfqsMYTfvtshlppgfneydfvpesfdrdktialimnsSGSTGLPKGVALP 212
Cdd:cd05939 84 -LDPLLTQSSTEPPSQDDVNFRDKLFY-----IYT--------------------------------SGTTGLPKAAVIV 125
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1216630836 213 HrtacVRF-SHARDPIFGNQIIPDTAILSVVPFHHGFGMFTTLGY-LICGFRVVLMYRFEEELFLRSLQDYKIQSALLVP 290
Cdd:cd05939 126 H----SRYyRIAAGAYYAFGMRPEDVVYDCLPLYHSAGGIMGVGQaLLHGSTVVIRKKFSASNFWDDCVKYNCTIVQYIG 201
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1216630836 291 TLFSFFAKSTLIDKYDLSNLHEIASGGapLSKEVGEAVAKRFHLPGIRQGYGLTETTSAILitpEGDDKPGAVGkVVPFF 370
Cdd:cd05939 202 EICRYLLAQPPSEEEQKHNVRLAVGNG--LRPQIWEQFVRRFGIPQIGEFYGATEGNSSLV---NIDNHVGACG-FNSRI 275
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1216630836 371 EAKV-------VDLDTGKTLgvNQRGELCVR------GPMI-----------MSGYVNNpEATNALIDKDGWLH------ 420
Cdd:cd05939 276 LPSVypirlikVDEDTGELI--RDSDGLCIPcqpgepGLLVgkiiqndplrrFDGYVNE-GATNKKIARDVFKKgdsafl 352
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1216630836 421 SGDIAYWDEDEHFFIVDRLKSLIKYKGYQVAPAELESILLQHPNIFDAGVAGLpdddagELP--------AAVVVLEhgk 492
Cdd:cd05939 353 SGDVLVMDELGYLYFKDRTGDTFRWKGENVSTTEVEGILSNVLGLEDVVVYGV------EVPgvegragmAAIVDPE--- 423
|
490 500 510 520
....*....|....*....|....*....|....*....|....*...
gi 1216630836 493 tmtEKEIVDYVASQVTTAKKLRGGVVFV---DEVPKGLTGKLDARKIR 537
Cdd:cd05939 424 ---RKVDLDRFSAVLAKSLPPYARPQFIrllPEVDKTGTFKLQKTDLQ 468
|
|
| FACL_like_1 |
cd05910 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
194-465 |
1.30e-12 |
|
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: 69.80 E-value: 1.30e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1216630836 194 ALIMNSSGSTGLPKGVALPHRTACVRFSHARDpIFGnqIIPDTAILSVVPFHHGFGMFTTLGYLICGFRVVLMYRFEEEL 273
Cdd:cd05910 88 AAILFTSGSTGTPKGVVYRHGTFAAQIDALRQ-LYG--IRPGEVDLATFPLFALFGPALGLTSVIPDMDPTRPARADPQK 164
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1216630836 274 FLRSLQDYKIQSALLVPTLFSFFAKSTLIDKYDLSNLHEIASGGAPLSKEVGEAVAKRFHlPG--IRQGYGLTET----- 346
Cdd:cd05910 165 LVGAIRQYGVSIVFGSPALLERVARYCAQHGITLPSLRRVLSAGAPVPIALAARLRKMLS-DEaeILTPYGATEAlpvss 243
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1216630836 347 --TSAILITPEGDDKPGA---VGKVVPFFEAKVVDLDTGKTLGVNQR--------GELCVRGPMIMSGYVNNPEATNALI 413
Cdd:cd05910 244 igSRELLATTTAATSGGAgtcVGRPIPGVRVRIIEIDDEPIAEWDDTlelprgeiGEITVTGPTVTPTYVNRPVATALAK 323
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*.
gi 1216630836 414 DKDG----WLHSGDIAYWDEDEHFFIVDRLKSLIKYKGYQVAPAELESILLQHPNI 465
Cdd:cd05910 324 IDDNsegfWHRMGDLGYLDDEGRLWFCGRKAHRVITTGGTLYTEPVERVFNTHPGV 379
|
|
| A_NRPS_ApnA-like |
cd17644 |
similar to adenylation domain of anabaenopeptin synthetase (ApnA); This family of the ... |
193-534 |
6.17e-12 |
|
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: 67.85 E-value: 6.17e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1216630836 193 IALIMNSSGSTGLPKGVALPHRtACVRFSH---------ARDPIFGNQIIP-DTAILSVVPfhhgfgMFTTLGYLIcgFR 262
Cdd:cd17644 108 LAYVIYTSGSTGKPKGVMIEHQ-SLVNLSHglikeygitSSDRVLQFASIAfDVAAEEIYV------TLLSGATLV--LR 178
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1216630836 263 VVLMyRFEEELFLRSLQDYKIQSALLVPTLFSFFAKSTLIDKYDL-SNLHEIASGGAPLSKEVGEAVAKRF-HLPGIRQG 340
Cdd:cd17644 179 PEEM-RSSLEDFVQYIQQWQLTVLSLPPAYWHLLVLELLLSTIDLpSSLRLVIVGGEAVQPELVRQWQKNVgNFIQLINV 257
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1216630836 341 YGLTE-TTSAILITPEGDDKPG----AVGKVVPFFEAKVVDlDTGKTLGVNQRGELCVRGPMIMSGYVNNPEATNALIDK 415
Cdd:cd17644 258 YGPTEaTIAATVCRLTQLTERNitsvPIGRPIANTQVYILD-ENLQPVPVGVPGELHIGGVGLARGYLNRPELTAEKFIS 336
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1216630836 416 DGWLHS--------GDIAYWDEDEHFFIVDRLKSLIKYKGYQVAPAELESILLQHPNIfdagvaglpdddagelpAAVVV 487
Cdd:cd17644 337 HPFNSSeserlyktGDLARYLPDGNIEYLGRIDNQVKIRGFRIELGEIEAVLSQHNDV-----------------KTAVV 399
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1216630836 488 LEHGKTMTEKEIVDYVASQVTTA---KKLR-------------GGVVFVDEVPKGLTGKLDAR 534
Cdd:cd17644 400 IVREDQPGNKRLVAYIVPHYEESpstVELRqflkaklpdymipSAFVVLEELPLTPNGKIDRR 462
|
|
| PRK08308 |
PRK08308 |
acyl-CoA synthetase; Validated |
195-538 |
7.36e-11 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236231 [Multi-domain] Cd Length: 414 Bit Score: 64.29 E-value: 7.36e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1216630836 195 LIMNSSGSTGLPKGVALPHrTACVRFSHARDPIFgnQIIPDTAILSVVPFHHGFGmfttlgyLICGF--------RVVLM 266
Cdd:PRK08308 105 LLQYSSGTTGEPKLIRRSW-TEIDREIEAYNEAL--NCEQDETPIVACPVTHSYG-------LICGVlaaltrgsKPVII 174
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1216630836 267 YRFEEELFLRSLQDYKIQSALLVPTLFSFFAKSTLIDKydlsNLHEIASGGAPLSKEVGEAVAKR-FHLpgiRQGYGLTE 345
Cdd:PRK08308 175 TNKNPKFALNILRNTPQHILYAVPLMLHILGRLLPGTF----QFHAVMTSGTPLPEAWFYKLRERtTYM---MQQYGCSE 247
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1216630836 346 TtSAILITPEGDDkPGAVGKVVPFfeakvVDLDTGKtlGVNQRGELCVRgpmimsgyVNNPEatnalidkdgwLHSGDIA 425
Cdd:PRK08308 248 A-GCVSICPDMKS-HLDLGNPLPH-----VSVSAGS--DENAPEEIVVK--------MGDKE-----------IFTKDLG 299
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1216630836 426 YWDEDEHFFIVDRLKSLIKYKGYQVAPAELESILLQHPNIFDAGVAGLPDDDAGELPAAVVVLEHgkTMTEKEIVDYVAS 505
Cdd:PRK08308 300 YKSERGTLHFMGRMDDVINVSGLNVYPIEVEDVMLRLPGVQEAVVYRGKDPVAGERVKAKVISHE--EIDPVQLREWCIQ 377
|
330 340 350
....*....|....*....|....*....|...
gi 1216630836 506 QVtTAKKLRGGVVFVDEVPKGLTGKLdARKIRE 538
Cdd:PRK08308 378 HL-APYQVPHEIESVTEIPKNANGKV-SRKLLE 408
|
|
| Dip2 |
cd05905 |
Disco-interacting protein 2 (Dip2); Dip2 proteins show sequence similarity to other members of ... |
50-489 |
1.17e-10 |
|
Disco-interacting protein 2 (Dip2); Dip2 proteins show sequence similarity to other members of the adenylate forming enzyme family, including insect luciferase, acetyl CoA ligases and the adenylation domain of nonribosomal peptide synthetases (NRPS). However, its function may have diverged from other members of the superfamily. In mouse embryo, Dip2 homolog A plays an important role in the development of both vertebrate and invertebrate nervous systems. Dip2A appears to regulate cell growth and the arrangement of cells in organs. Biochemically, Dip2A functions as a receptor of FSTL1, an extracellular glycoprotein, and may play a role as a cardiovascular protective agent.
Pssm-ID: 341231 [Multi-domain] Cd Length: 571 Bit Score: 63.91 E-value: 1.17e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1216630836 50 VDITYAEYFEMSVRLAEAM-KRYGLNTNHRIVVCSENSLQFFMPVLGALFIGVAVAPAN--DIYNE-RELLNSMGISQPT 125
Cdd:cd05905 13 TTLTWGKLLSRAEKIAAVLqKKVGLKPGDRVALMYPDPLDFVAAFYGCLYAGVVPIPIEppDISQQlGFLLGTCKVRVAL 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1216630836 126 VVFVSKKGLQKILNVQKklpiiQKIIIMDSKtdyqGFQSMYTFVTSHLPPGFNEYDFVPESFDRDKTIALIMNSSGSTGL 205
Cdd:cd05905 93 TVEACLKGLPKKLLKSK-----TAAEIAKKK----GWPKILDFVKIPKSKRSKLKKWGPHPPTRDGDTAYIEYSFSSDGS 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1216630836 206 PKGVALPHRTAcvrFSHARDPIFGNQIIPDTAILSVVPFHHGFG-MFTTLGYLICGFRVVLMYRFEEE----LFLRSLQD 280
Cdd:cd05905 164 LSGVAVSHSSL---LAHCRALKEACELYESRPLVTVLDFKSGLGlWHGCLLSVYSGHHTILIPPELMKtnplLWLQTLSQ 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1216630836 281 YKIQSALLvptLFSFFAKSTLIDKYDLSNLHE-----------IASGGAPLSKEVGEAVAKRFHLPGIR----------- 338
Cdd:cd05905 241 YKVRDAYV---KLRTLHWCLKDLSSTLASLKNrdvnlsslrmcMVPCENRPRISSCDSFLKLFQTLGLSpravstefgtr 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1216630836 339 -------QGYGLTETTSAIL---------ITPEGDDKPGA-----VGKVVPFFEAKVVDLDTGKTLGVNQRGELCVRGPM 397
Cdd:cd05905 318 vnpficwQGTSGPEPSRVYLdmralrhgvVRLDERDKPNSlplqdSGKVLPGAQVAIVNPETKGLCKDGEIGEIWVNSPA 397
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1216630836 398 IMSGYVNNPEATNAL------------IDKDGWLHSGDIAYWDEDEHF----------FIVDRLKSLIKYKGYQVAPAEL 455
Cdd:cd05905 398 NASGYFLLDGETNDTfkvfpstrlstgITNNSYARTGLLGFLRPTKCTdlnveehdllFVVGSIDETLEVRGLRHHPSDI 477
|
490 500 510
....*....|....*....|....*....|....*
gi 1216630836 456 E-SILLQHPNIFDAGVAglpddDAGELPaaVVVLE 489
Cdd:cd05905 478 EaTVMRVHPYRGRCAVF-----SITGLV--VVVAE 505
|
|
| AACS |
cd05943 |
Acetoacetyl-CoA synthetase (acetoacetate-CoA ligase, AACS); AACS is a cytosolic ligase that ... |
51-542 |
1.96e-10 |
|
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: 63.44 E-value: 1.96e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1216630836 51 DITYAEYFEMSVRLAEAMKRYGLNTNHRIVVCSENSLQFFMPVLGALFIG---VAVAPanDiYNERELLNSMGISQPTVV 127
Cdd:cd05943 98 EVTWAELRRRVARLAAALRALGVKPGDRVAGYLPNIPEAVVAMLATASIGaiwSSCSP--D-FGVPGVLDRFGQIEPKVL 174
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1216630836 128 F----VSKKG-----LQKILNVQKKLP-IIQKIIIMDSKTDYQG-------FQSMYTFVTSHLPPgfnEYDFVPESFDRD 190
Cdd:cd05943 175 FavdaYTYNGkrhdvREKVAELVKGLPsLLAVVVVPYTVAAGQPdlskiakALTLEDFLATGAAG---ELEFEPLPFDHP 251
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1216630836 191 ktiALIMNSSGSTGLPKGVAlpHRTACVRFSHARDPIFGNQIIP-DTailsvvpfhhgFGMFTTLGY---------LICG 260
Cdd:cd05943 252 ---LYILYSSGTTGLPKCIV--HGAGGTLLQHLKEHILHCDLRPgDR-----------LFYYTTCGWmmwnwlvsgLAVG 315
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1216630836 261 FRVVL-----MYRFEEELFlrSLQDyKIQSALLV--PTLFSFFAKSTLI--DKYDLSNLHEIASGGAPLSKE----VGEA 327
Cdd:cd05943 316 ATIVLydgspFYPDTNALW--DLAD-EEGITVFGtsAKYLDALEKAGLKpaETHDLSSLRTILSTGSPLKPEsfdyVYDH 392
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1216630836 328 VAKRFHLPGIRQGyglTETTSAILIT-PEGDDKPGAVGKVVPFFEAKVVDlDTGKTLgVNQRGEL-CVRG-PMIMSGYVN 404
Cdd:cd05943 393 IKPDVLLASISGG---TDIISCFVGGnPLLPVYRGEIQCRGLGMAVEAFD-EEGKPV-WGEKGELvCTKPfPSMPVGFWN 467
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1216630836 405 NPEAT---NALIDK-DG-WLHsGDIAYWDEDEHFFIVDRLKSLIKYKGYQVAPAELESILLQHPNIFDAGVAGLPDDDAG 479
Cdd:cd05943 468 DPDGSryrAAYFAKyPGvWAH-GDWIEITPRGGVVILGRSDGTLNPGGVRIGTAEIYRVVEKIPEVEDSLVVGQEWKDGD 546
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1216630836 480 ELPAAVVVLEHGKTMTEkEIVDYVASQVTTAKKLR---GGVVFVDEVPKGLTGkldarKIREILIK 542
Cdd:cd05943 547 ERVILFVKLREGVELDD-ELRKRIRSTIRSALSPRhvpAKIIAVPDIPRTLSG-----KKVEVAVK 606
|
|
| PRK12476 |
PRK12476 |
putative fatty-acid--CoA ligase; Provisional |
122-537 |
4.80e-10 |
|
putative fatty-acid--CoA ligase; Provisional
Pssm-ID: 171527 [Multi-domain] Cd Length: 612 Bit Score: 62.07 E-value: 4.80e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1216630836 122 SQPTVVFVSKKGLQKILNVQKKLPIIQK--IIIMDSKTDYQGfqsmytfvtshlppgfneYDFVPESFDRDKtIALIMNS 199
Cdd:PRK12476 141 AEPTVVLTTTAAAEAVEGFLRNLPRLRRprVIAIDAIPDSAG------------------ESFVPVELDTDD-VSHLQYT 201
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1216630836 200 SGSTGLPKGVALPHRTACVRFSHArdPIFGNQIIPDTAILSVVPFHHGFG----MFTTLgyliCGFRVVLM--------- 266
Cdd:PRK12476 202 SGSTRPPVGVEITHRAVGTNLVQM--ILSIDLLDRNTHGVSWLPLYHDMGlsmiGFPAV----YGGHSTLMsptafvrrp 275
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1216630836 267 YRFEEELFLRSLQDYKIQSAllvPTL-FSFFAKSTLI---DKYDLSNLHEIaSGGAPLSKEVGEAVAKRFH---LP--GI 337
Cdd:PRK12476 276 QRWIKALSEGSRTGRVVTAA---PNFaYEWAAQRGLPaegDDIDLSNVVLI-IGSEPVSIDAVTTFNKAFApygLPrtAF 351
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1216630836 338 RQGYGLTETT------------SAILITPEG----------DDKPGAV-----GKVVPFFEAKVVDLDTGKTLGVNQRGE 390
Cdd:PRK12476 352 KPSYGIAEATlfvatiapdaepSVVYLDREQlgagravrvaADAPNAVahvscGQVARSQWAVIVDPDTGAELPDGEVGE 431
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1216630836 391 LCVRGPMIMSGYVNNPEAT-----NAL-------------IDKDGWLHSGDIAYWDEDEhFFIVDRLKSLIKYKGYQVAP 452
Cdd:PRK12476 432 IWLHGDNIGRGYWGRPEETertfgAKLqsrlaegshadgaADDGTWLRTGDLGVYLDGE-LYITGRIADLIVIDGRNHYP 510
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1216630836 453 AELESILLQHPNIFDAG-VAG--LPDDDAGELpaaVVVLEH--GKTMTE-KEIVDYVASQVTTAKKLR-GGVVFVDE--V 523
Cdd:PRK12476 511 QDIEATVAEASPMVRRGyVTAftVPAEDNERL---VIVAERaaGTSRADpAPAIDAIRAAVSRRHGLAvADVRLVPAgaI 587
|
490
....*....|....
gi 1216630836 524 PKGLTGKLDARKIR 537
Cdd:PRK12476 588 PRTTSGKLARRACR 601
|
|
| PLN02654 |
PLN02654 |
acetate-CoA ligase |
347-539 |
2.77e-08 |
|
acetate-CoA ligase
Pssm-ID: 215353 [Multi-domain] Cd Length: 666 Bit Score: 56.44 E-value: 2.77e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1216630836 347 TSAILITP---EGDDKPGAVgkVVPFFEAKVVDLD-TGKTLGVNQRGELCVRG--PMIMSGYVNNPE--ATNALIDKDGW 418
Cdd:PLN02654 437 TGGFMITPlpgAWPQKPGSA--TFPFFGVQPVIVDeKGKEIEGECSGYLCVKKswPGAFRTLYGDHEryETTYFKPFAGY 514
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1216630836 419 LHSGDIAYWDEDEHFFIVDRLKSLIKYKGYQVAPAELESILLQHPNIFDAGVAGLPDDDAGELPAAVVVLEHGKTMTEke 498
Cdd:PLN02654 515 YFSGDGCSRDKDGYYWLTGRVDDVINVSGHRIGTAEVESALVSHPQCAEAAVVGIEHEVKGQGIYAFVTLVEGVPYSE-- 592
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 1216630836 499 ivDYVASQVTTAKKLRGGVVFVDEV------PKGLTGKLDARKIREI 539
Cdd:PLN02654 593 --ELRKSLILTVRNQIGAFAAPDKIhwapglPKTRSGKIMRRILRKI 637
|
|
| entF |
PRK10252 |
enterobactin non-ribosomal peptide synthetase EntF; |
16-535 |
4.18e-08 |
|
enterobactin non-ribosomal peptide synthetase EntF;
Pssm-ID: 236668 [Multi-domain] Cd Length: 1296 Bit Score: 56.21 E-value: 4.18e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1216630836 16 YPLEDGTAGEQLHKAMKRyalVPGTIAFTDAHIEVdiTYAEYFEMSVRLAEAMKRYGLNTNHRIVVCSENSLQFFMPVLG 95
Cdd:PRK10252 453 VEIPETTLSALVAQQAAK---TPDAPALADARYQF--SYREMREQVVALANLLRERGVKPGDSVAVALPRSVFLTLALHA 527
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1216630836 96 ALFIGVAVAPANDIYNERELLNSMGISQPTVVFVSKkglqkilNVQKKLPIIQKIIImdsktdyqgfqsmYTFVTSHLPP 175
Cdd:PRK10252 528 IVEAGAAWLPLDTGYPDDRLKMMLEDARPSLLITTA-------DQLPRFADVPDLTS-------------LCYNAPLAPQ 587
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1216630836 176 gfneyDFVPESFDRDKTIALIMNSSGSTGLPKGVALPHRTACVRFSHARD--PIFGNQII----PDTAILSVVPFHHGFg 249
Cdd:PRK10252 588 -----GAAPLQLSQPHHTAYIIFTSGSTGRPKGVMVGQTAIVNRLLWMQNhyPLTADDVVlqktPCSFDVSVWEFFWPF- 661
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1216630836 250 mfttlgylICGFRVVLM----YRFEEELfLRSLQDYKIQSALLVPTLFSFFAKSTLID--KYDLSNLHEIASGGAPLSKE 323
Cdd:PRK10252 662 --------IAGAKLVMAepeaHRDPLAM-QQFFAEYGVTTTHFVPSMLAAFVASLTPEgaRQSCASLRQVFCSGEALPAD 732
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1216630836 324 VGEAVAKRFHLPgIRQGYGLTEttSAILIT--P-EGDDKPGAVGKVVPF-FEA-----KVVDlDTGKTLGVNQRGELCVR 394
Cdd:PRK10252 733 LCREWQQLTGAP-LHNLYGPTE--AAVDVSwyPaFGEELAAVRGSSVPIgYPVwntglRILD-ARMRPVPPGVAGDLYLT 808
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1216630836 395 GPMIMSGYVNNPEATNALIDKDGWL------HSGDIAYWDEDEHFFIVDRLKSLIKYKGYQVAPAELESILLQHPNIFDA 468
Cdd:PRK10252 809 GIQLAQGYLGRPDLTASRFIADPFApgermyRTGDVARWLDDGAVEYLGRSDDQLKIRGQRIELGEIDRAMQALPDVEQA 888
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1216630836 469 GVaglpdddagelpAAVVVLEHGKTM-TEKEIVDYVASQ-------VTTAKKLRGG-------VVFV--DEVPKGLTGKL 531
Cdd:PRK10252 889 VT------------HACVINQAAATGgDARQLVGYLVSQsglpldtSALQAQLRERlpphmvpVVLLqlDQLPLSANGKL 956
|
....
gi 1216630836 532 DaRK 535
Cdd:PRK10252 957 D-RK 959
|
|
| PRK05691 |
PRK05691 |
peptide synthase; Validated |
194-534 |
2.94e-07 |
|
peptide synthase; Validated
Pssm-ID: 235564 [Multi-domain] Cd Length: 4334 Bit Score: 53.63 E-value: 2.94e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1216630836 194 ALIMNSSGSTGLPKGVALPHRTACVrfsHARDPI--FGNQiiPDTAILSVVPFHHGFGMFTTLGYLICGFRVVLMYR--F 269
Cdd:PRK05691 2336 AYLIYTSGSTGKPKGVVVSHGEIAM---HCQAVIerFGMR--ADDCELHFYSINFDAASERLLVPLLCGARVVLRAQgqW 2410
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1216630836 270 EEELFLRSLQDYKIQSALLVPTLFSFFAKsTLIDKYDLSNLHEIASGGAPLSKEvgeavakrfHLPGIRQ---------G 340
Cdd:PRK05691 2411 GAEEICQLIREQQVSILGFTPSYGSQLAQ-WLAGQGEQLPVRMCITGGEALTGE---------HLQRIRQafapqlffnA 2480
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1216630836 341 YGLTETTSAILITPEGDDKP-GA----VGKVVPFFEAKVVDLD-----TGKTlgvnqrGELCVRGPMIMSGY-------- 402
Cdd:PRK05691 2481 YGPTETVVMPLACLAPEQLEeGAasvpIGRVVGARVAYILDADlalvpQGAT------GELYVGGAGLAQGYhdrpglta 2554
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1216630836 403 ---VNNPEATNAlidkdGWLH-SGDIAYWDEDEHFFIVDRLKSLIKYKGYQVAPAELESILLQHPNIFDAGVAGLpDDDA 478
Cdd:PRK05691 2555 erfVADPFAADG-----GRLYrTGDLVRLRADGLVEYVGRIDHQVKIRGFRIELGEIESRLLEHPAVREAVVLAL-DTPS 2628
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1216630836 479 GelpaavvvlehgktmteKEIVDYVASQVTTAK-----KLRGGV-----------------VFVDEVPKGLTGKLDAR 534
Cdd:PRK05691 2629 G-----------------KQLAGYLVSAVAGQDdeaqaALREALkahlkqqlpdymvpahlILLDSLPLTANGKLDRR 2689
|
|
| PaaK |
COG1541 |
Phenylacetate-coenzyme A ligase PaaK, adenylate-forming domain family [Coenzyme transport and ... |
275-537 |
3.92e-07 |
|
Phenylacetate-coenzyme A ligase PaaK, adenylate-forming domain family [Coenzyme transport and metabolism];
Pssm-ID: 441150 [Multi-domain] Cd Length: 423 Bit Score: 52.46 E-value: 3.92e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1216630836 275 LRSLQDYKiQSALL-VPTlfsfFAKsTLIDK-----YDLSNLH-EIAS-GGAPLSKEVGEAVAKRFHLPgIRQGYGLTET 346
Cdd:COG1541 168 LRLMQDFG-PTVLVgTPS----YLL-YLAEVaeeegIDPRDLSlKKGIfGGEPWSEEMRKEIEERWGIK-AYDIYGLTEV 240
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1216630836 347 TSAILItpEGDDKPGAVgkvvpFFE----AKVVDLDTGKTLGVNQRGELCVrgpmimsgyvnnpeaTNalIDKDGW---- 418
Cdd:COG1541 241 GPGVAY--ECEAQDGLH-----IWEdhflVEIIDPETGEPVPEGEEGELVV---------------TT--LTKEAMplir 296
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1216630836 419 LHSGDIAYWDEDE---------HFFIVDRLKSLIKYKGYQVAPAELESILLQHPNIFDAGVAGLpdDDAGELPAAVVVLE 489
Cdd:COG1541 297 YRTGDLTRLLPEPcpcgrthprIGRILGRADDMLIIRGVNVFPSQIEEVLLRIPEVGPEYQIVV--DREGGLDELTVRVE 374
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|.
gi 1216630836 490 HGKTMTEKEIVDYVASQVTTAKKLRGGVVFVDevPKGL---TGKldARKIR 537
Cdd:COG1541 375 LAPGASLEALAEAIAAALKAVLGLRAEVELVE--PGSLprsEGK--AKRVI 421
|
|
| PRK05691 |
PRK05691 |
peptide synthase; Validated |
389-535 |
3.32e-04 |
|
peptide synthase; Validated
Pssm-ID: 235564 [Multi-domain] Cd Length: 4334 Bit Score: 44.00 E-value: 3.32e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1216630836 389 GELCVRGPMIMSGYVNNPEAT-NALIDK------DGWLHSGDIAYWDEDEHFFIVDRLKSLIKYKGYQVAPAELESILLQ 461
Cdd:PRK05691 4067 GELCVAGTGVGRGYVGDPLRTaLAFVPHpfgapgERLYRTGDLARRRSDGVLEYVGRIDHQVKIRGYRIELGEIEARLHE 4146
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1216630836 462 HPNIFDAGVA---GLPDDD-AGELPAAVVVLEHG------KTMTEKEIVDYVASQvttakklrgGVVFVDEVPKGLTGKL 531
Cdd:PRK05691 4147 QAEVREAAVAvqeGVNGKHlVGYLVPHQTVLAQGalleriKQRLRAELPDYMVPL---------HWLWLDRLPLNANGKL 4217
|
....
gi 1216630836 532 DaRK 535
Cdd:PRK05691 4218 D-RK 4220
|
|
| |
