|
Name |
Accession |
Description |
Interval |
E-value |
| CaiA |
COG1960 |
Acyl-CoA dehydrogenase related to the alkylation response protein AidB [Lipid transport and ... |
1-374 |
8.89e-125 |
|
Acyl-CoA dehydrogenase related to the alkylation response protein AidB [Lipid transport and metabolism]; Acyl-CoA dehydrogenase related to the alkylation response protein AidB is part of the Pathway/BioSystem: Fatty acid biosynthesis
Pssm-ID: 441563 [Multi-domain] Cd Length: 381 Bit Score: 364.93 E-value: 8.89e-125
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2664202365 1 MSSALTPAQARAQKEFRAFAERHIAPYADEYHRAQRTPPEAVKQLAAEGLLGLSVPEEYGGGGCDAVTLGLLAGELGRAC 80
Cdd:COG1960 1 MDFELTEEQRALRDEVREFAEEEIAPEAREWDREGEFPRELWRKLAELGLLGLTIPEEYGGLGLSLVELALVLEELARAD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2664202365 81 SSLRSLLTVHTMVAHAIVRWGSRSLKEYWLPRLARGESIGALAVSEPDVGSDAGSVTSRLTRDGDDWVLDGHKKWTTYGE 160
Cdd:COG1960 81 ASLALPVGVHNGAAEALLRFGTEEQKERYLPRLASGEWIGAFALTEPGAGSDAAALRTTAVRDGDGYVLNGQKTFITNAP 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2664202365 161 TADVYLVVGRSEE-----GPTAVLVERGTEGLRTELIEDLIGIRASMTANVYFDGCRVPGGNLLARPGLGVSHVVgAALD 235
Cdd:COG1960 161 VADVILVLARTDPaaghrGISLFLVPKDTPGVTVGRIEDKMGLRGSDTGELFFDDVRVPAENLLGEEGKGFKIAM-STLN 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2664202365 236 LGRYTVGWGCVGILDACVEASVDYAAERHQFGSAIKDHQLVRRLITNMYTDARAARLLCLEAGRLRDRRDPGALAgTSTA 315
Cdd:COG1960 240 AGRLGLAAQALGIAEAALELAVAYAREREQFGRPIADFQAVQHRLADMAAELEAARALVYRAAWLLDAGEDAALE-AAMA 318
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*....
gi 2664202365 316 KYFASSAATRAAADAVQIHGANGCSSDFPVQRYLGDSRVMEIIEGSSQIHQVGLAEYAF 374
Cdd:COG1960 319 KLFATEAALEVADEALQIHGGYGYTREYPLERLYRDARILTIYEGTNEIQRLIIARRLL 377
|
|
| SCAD_SBCAD |
cd01158 |
Short chain acyl-CoA dehydrogenases and eukaryotic short/branched chain acyl-CoA ... |
17-370 |
7.60e-102 |
|
Short chain acyl-CoA dehydrogenases and eukaryotic short/branched chain acyl-CoA dehydrogenases; Short chain acyl-CoA dehydrogenase (SCAD). SCAD is a mitochondrial beta-oxidation enzyme. It catalyzes the alpha,beta dehydrogenation of the corresponding trans-enoyl-CoA by FAD, which becomes reduced. The reduced form of SCAD is reoxidized in the oxidative half-reaction by electron-transferring flavoprotein (ETF), from which the electrons are transferred to the mitochondrial respiratory chain coupled with ATP synthesis. This subgroup also contains the eukaryotic short/branched chain acyl-CoA dehydrogenase(SBCAD), the bacterial butyryl-CoA dehydorgenase(BCAD) and 2-methylbutyryl-CoA dehydrogenase, which is involved in isoleucine catabolism. These enzymes are homotetramers.
Pssm-ID: 173847 [Multi-domain] Cd Length: 373 Bit Score: 306.50 E-value: 7.60e-102
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2664202365 17 RAFAERHIAPYADEYHRAQRTPPEAVKQLAAEGLLGLSVPEEYGGGGCDAVTLGLLAGELGRACSSLRSLLTVH-TMVAH 95
Cdd:cd01158 11 RDFAEKEIAPLAAEMDEKGEFPREVIKEMAELGLMGIPIPEEYGGAGLDFLAYAIAIEELAKVDASVAVIVSVHnSLGAN 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2664202365 96 AIVRWGSRSLKEYWLPRLARGESIGALAVSEPDVGSDAGSVTSRLTRDGDDWVLDGHKKWTTYGETADVYLVVGRSEE-- 173
Cdd:cd01158 91 PIIKFGTEEQKKKYLPPLATGEKIGAFALSEPGAGSDAAALKTTAKKDGDDYVLNGSKMWITNGGEADFYIVFAVTDPsk 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2664202365 174 ---GPTAVLVERGTEGLRTELIEDLIGIRASMTANVYFDGCRVPGGNLLARPGLGVSHVVGaALDLGRYTVGWGCVGILD 250
Cdd:cd01158 171 gyrGITAFIVERDTPGLSVGKKEDKLGIRGSSTTELIFEDVRVPKENILGEEGEGFKIAMQ-TLDGGRIGIAAQALGIAQ 249
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2664202365 251 ACVEASVDYAAERHQFGSAIKDHQLVRRLITNMYTDARAARLLCLEAGRLRDRRDPGALAgTSTAKYFASSAATRAAADA 330
Cdd:cd01158 250 AALDAAVDYAKERKQFGKPIADFQGIQFKLADMATEIEAARLLTYKAARLKDNGEPFIKE-AAMAKLFASEVAMRVTTDA 328
|
330 340 350 360
....*....|....*....|....*....|....*....|
gi 2664202365 331 VQIHGANGCSSDFPVQRYLGDSRVMEIIEGSSQIHQVGLA 370
Cdd:cd01158 329 VQIFGGYGYTKDYPVERYYRDAKITEIYEGTSEIQRLVIA 368
|
|
| GCD |
cd01151 |
Glutaryl-CoA dehydrogenase; Glutaryl-CoA dehydrogenase (GCD). GCD is an acyl-CoA dehydrogenase, ... |
2-370 |
4.41e-81 |
|
Glutaryl-CoA dehydrogenase; Glutaryl-CoA dehydrogenase (GCD). GCD is an acyl-CoA dehydrogenase, which catalyzes the oxidative decarboxylation of glutaryl-CoA to crotonyl-CoA and carbon dioxide in the catabolism of lysine, hydroxylysine, and tryptophan. It uses electron transfer flavoprotein (ETF) as an electron acceptor. GCD is a homotetramer. GCD deficiency leads to a severe neurological disorder in humans.
Pssm-ID: 173840 [Multi-domain] Cd Length: 386 Bit Score: 253.43 E-value: 4.41e-81
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2664202365 2 SSALTPAQARAQKEFRAFAERHIAPYADEYHRAQRTPPEAVKQLAAEGLLGLSvPEEYGGGGCDAVTLGLLAGELGRACS 81
Cdd:cd01151 10 DDLLTEEERAIRDTAREFCQEELAPRVLEAYREEKFDRKIIEEMGELGLLGAT-IKGYGCAGLSSVAYGLIAREVERVDS 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2664202365 82 SLRSLLTVHT-MVAHAIVRWGSRSLKEYWLPRLARGESIGALAVSEPDVGSDAGSVTSRLTRDGDDWVLDGHKKWTTYGE 160
Cdd:cd01151 89 GYRSFMSVQSsLVMLPIYDFGSEEQKQKYLPKLASGELIGCFGLTEPNHGSDPGGMETRARKDGGGYKLNGSKTWITNSP 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2664202365 161 TADVYLVVGRSEE--GPTAVLVERGTEGLRTELIEDLIGIRASMTANVYFDGCRVPGGNLLarPGLGVSHVVGAALDLGR 238
Cdd:cd01151 169 IADVFVVWARNDEtgKIRGFILERGMKGLSAPKIQGKFSLRASITGEIVMDNVFVPEENLL--PGAEGLRGPFKCLNNAR 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2664202365 239 YTVGWGCVGILDACVEASVDYAAERHQFGSAIKDHQLVRRLITNMYTDARAARLLCLEAGRLRDRrdpGALAG--TSTAK 316
Cdd:cd01151 247 YGIAWGALGAAEDCYHTARQYVLDRKQFGRPLAAFQLVQKKLADMLTEIALGLLACLRVGRLKDQ---GKATPeqISLLK 323
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....
gi 2664202365 317 YFASSAATRAAADAVQIHGANGCSSDFPVQRYLGDSRVMEIIEGSSQIHQVGLA 370
Cdd:cd01151 324 RNNCGKALEIARTAREMLGGNGISDEYHIIRHMVNLESVNTYEGTHDIHALILG 377
|
|
| ACAD |
cd00567 |
Acyl-CoA dehydrogenase; Both mitochondrial acyl-CoA dehydrogenases (ACAD) and peroxisomal ... |
7-365 |
4.30e-79 |
|
Acyl-CoA dehydrogenase; Both mitochondrial acyl-CoA dehydrogenases (ACAD) and peroxisomal acyl-CoA oxidases (AXO) catalyze the alpha,beta dehydrogenation of the corresponding trans-enoyl-CoA by FAD, which becomes reduced. The reduced form of ACAD is reoxidized in the oxidative half-reaction by electron-transferring flavoprotein (ETF), from which the electrons are transferred to the mitochondrial respiratory chain coupled with ATP synthesis. In contrast, AXO catalyzes a different oxidative half-reaction, in which the reduced FAD is reoxidized by molecular oxygen. The ACAD family includes the eukaryotic beta-oxidation enzymes, short (SCAD), medium (MCAD), long (LCAD) and very-long (VLCAD) chain acyl-CoA dehydrogenases. These enzymes all share high sequence similarity, but differ in their substrate specificities. The ACAD family also includes amino acid catabolism enzymes such as Isovaleryl-CoA dehydrogenase (IVD), short/branched chain acyl-CoA dehydrogenases(SBCAD), Isobutyryl-CoA dehydrogenase (IBDH), glutaryl-CoA deydrogenase (GCD) and Crotonobetainyl-CoA dehydrogenase. The mitochondrial ACAD's are generally homotetramers, except for VLCAD, which is a homodimer. Related enzymes include the SOS adaptive reponse proten aidB, Naphthocyclinone hydroxylase (NcnH), and and Dibenzothiophene (DBT) desulfurization enzyme C (DszC)
Pssm-ID: 173838 [Multi-domain] Cd Length: 327 Bit Score: 246.43 E-value: 4.30e-79
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2664202365 7 PAQARAQKEFRAFAERHIAPYADEYHRAQRTPPEAVKQLaaegllglsvpeeyggggcdavtlgllaGELgracsslrsl 86
Cdd:cd00567 1 EEQRELRDSAREFAAEELEPYARERRETPEEPWELLAEL----------------------------GLL---------- 42
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2664202365 87 ltvhtMVAHAIVRWGSRSLKEYWLPRLARGESIGALAVSEPDVGSDAGSVTSRLTRDGDDWVLDGHKKWTTYGETADVYL 166
Cdd:cd00567 43 -----LGAALLLAYGTEEQKERYLPPLASGEAIAAFALTEPGAGSDLAGIRTTARKDGDGYVLNGRKIFISNGGDADLFI 117
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2664202365 167 VVGRSEE------GPTAVLVERGTEGLRTELIEDLIGIRASMTANVYFDGCRVPGGNLLARPGLGVSHVVGAaLDLGRYT 240
Cdd:cd00567 118 VLARTDEegpghrGISAFLVPADTPGVTVGRIWDKMGMRGSGTGELVFDDVRVPEDNLLGEEGGGFELAMKG-LNVGRLL 196
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2664202365 241 VGWGCVGILDACVEASVDYAAERHQFGSAIKDHQLVRRLITNMYTDARAARLLCLEAGRLRDRRDPGALAGTSTAKYFAS 320
Cdd:cd00567 197 LAAVALGAARAALDEAVEYAKQRKQFGKPLAEFQAVQFKLADMAAELEAARLLLYRAAWLLDQGPDEARLEAAMAKLFAT 276
|
330 340 350 360
....*....|....*....|....*....|....*....|....*
gi 2664202365 321 SAATRAAADAVQIHGANGCSSDFPVQRYLGDSRVMEIIEGSSQIH 365
Cdd:cd00567 277 EAAREVADLAMQIHGGRGYSREYPVERYLRDARAARIAEGTAEIQ 321
|
|
| IVD |
cd01156 |
Isovaleryl-CoA dehydrogenase; Isovaleryl-CoA dehydrogenase (IVD) is an is an acyl-CoA ... |
4-364 |
7.61e-77 |
|
Isovaleryl-CoA dehydrogenase; Isovaleryl-CoA dehydrogenase (IVD) is an is an acyl-CoA dehydrogenase, which catalyzes the third step in leucine catabolism, the conversion of isovaleryl-CoA (3-methylbutyryl-CoA) into 3-methylcrotonyl-CoA. IVD is a homotetramer and has the greatest affinity for small branched chain substrates.
Pssm-ID: 173845 [Multi-domain] Cd Length: 376 Bit Score: 242.32 E-value: 7.61e-77
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2664202365 4 ALTPAQARAQKEFRAFAERHIAPYADEYHRAQRTPPEAVKQLAAEGLLGLSVPEEYGGGGCDAVTLGLLAGELGRACSSL 83
Cdd:cd01156 1 GLDDEIEMLRQSVREFAQKEIAPLAAKIDRDNEFPRDLWRKMGKLGLLGITAPEEYGGSGMGYLAHVIIMEEISRASGSV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2664202365 84 RSLLTVHT-MVAHAIVRWGSRSLKEYWLPRLARGESIGALAVSEPDVGSDAGSVTSRLTRDGDDWVLDGHKKWTTYGETA 162
Cdd:cd01156 81 ALSYGAHSnLCINQIYRNGSAAQKEKYLPKLISGEHIGALAMSEPNAGSDVVSMKLRAEKKGDRYVLNGSKMWITNGPDA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2664202365 163 DVYLVVGRSE-----EGPTAVLVERGTEGLRTELIEDLIGIRASMTANVYFDGCRVPGGNLLARPGLGVsHVVGAALDLG 237
Cdd:cd01156 161 DTLVVYAKTDpsagaHGITAFIVEKGMPGFSRAQKLDKLGMRGSNTCELVFEDCEVPEENILGGENKGV-YVLMSGLDYE 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2664202365 238 RYTVGWGCVGILDACVEASVDYAAERHQFGSAIKDHQLVRRLITNMYTDARAARLLCLEAGRL--RDRRDPGALAGtstA 315
Cdd:cd01156 240 RLVLAGGPIGIMQAALDVAIPYAHQRKQFGQPIGEFQLVQGKLADMYTRLNASRSYLYTVAKAcdRGNMDPKDAAG---V 316
|
330 340 350 360
....*....|....*....|....*....|....*....|....*....
gi 2664202365 316 KYFASSAATRAAADAVQIHGANGCSSDFPVQRYLGDSRVMEIIEGSSQI 364
Cdd:cd01156 317 ILYAAEKATQVALDAIQILGGNGYINDYPTGRLLRDAKLYEIGAGTSEI 365
|
|
| IBD |
cd01162 |
Isobutyryl-CoA dehydrogenase; Isobutyryl-CoA dehydrogenase (IBD) catalyzes the alpha, beta- ... |
5-376 |
3.44e-71 |
|
Isobutyryl-CoA dehydrogenase; Isobutyryl-CoA dehydrogenase (IBD) catalyzes the alpha, beta- dehydrogenation of short branched chain acyl-CoA intermediates in valine catabolism. It is predicted to be a homotetramer.
Pssm-ID: 173851 [Multi-domain] Cd Length: 375 Bit Score: 227.71 E-value: 3.44e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2664202365 5 LTPAQARAQKEFRAFAERHIAPYADEYHRAQRTPPEAVKQLAAEGLLGLSVPEEYGGGGCDAVTLGLLAGELGRACSSLR 84
Cdd:cd01162 1 LNEEQRAIQEVARAFAAKEMAPHAADWDQKKHFPVDVLRKAAELGFGGIYIRDDVGGSGLSRLDASIIFEALSTGCVSTA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2664202365 85 SLLTVHTMVAHAIVRWGSRSLKEYWLPRLARGESIGALAVSEPDVGSDAGSVTSRLTRDGDDWVLDGHKKWTTYGETADV 164
Cdd:cd01162 81 AYISIHNMCAWMIDSFGNDEQRERFLPDLCTMEKLASYCLTEPGSGSDAAALRTRAVREGDHYVLNGSKAFISGAGDSDV 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2664202365 165 YLVVGRS-EEGP---TAVLVERGTEGLRTELIEDLIGIRASMTANVYFDGCRVPGGNLLARPGLGVSHVVgAALDLGRYT 240
Cdd:cd01162 161 YVVMARTgGEGPkgiSCFVVEKGTPGLSFGANEKKMGWNAQPTRAVIFEDCRVPVENRLGGEGQGFGIAM-AGLNGGRLN 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2664202365 241 VGWGCVGILDACVEASVDYAAERHQFGSAIKDHQLVRRLITNMYTDARAARLLCLEAGRLRDRRDPGALAGTSTAKYFAS 320
Cdd:cd01162 240 IASCSLGAAQAALDLARAYLEERKQFGKPLADFQALQFKLADMATELVASRLMVRRAASALDRGDPDAVKLCAMAKRFAT 319
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*.
gi 2664202365 321 SAATRAAADAVQIHGANGCSSDFPVQRYLGDSRVMEIIEGSSQIHQVGLAEYAFQE 376
Cdd:cd01162 320 DECFDVANQALQLHGGYGYLKDYPVEQYVRDLRVHQILEGTNEIMRLIIARALLTR 375
|
|
| LCAD |
cd01160 |
Long chain acyl-CoA dehydrogenase; LCAD is an acyl-CoA dehydrogenases (ACAD), which is found ... |
17-364 |
5.40e-64 |
|
Long chain acyl-CoA dehydrogenase; LCAD is an acyl-CoA dehydrogenases (ACAD), which is found in the mitochondria of eukaryotes and in some prokaryotes. It catalyzes the alpha, beta dehydrogenation of the corresponding trans-enoyl-CoA by FAD, which becomes reduced. The reduced form of LCAD is reoxidized in the oxidative half-reaction by electron-transferring flavoprotein (ETF), from which the electrons are transferred to the mitochondrial respiratory chain coupled with ATP synthesis. LCAD acts as a homodimer.
Pssm-ID: 173849 [Multi-domain] Cd Length: 372 Bit Score: 208.89 E-value: 5.40e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2664202365 17 RAFAERHIAPYADEYHRAQRTPPEAVKQLAAEGLLGLSVPEEYGGGGCDAVTLGLLAGELGRA-CSSLRslLTVHT-MVA 94
Cdd:cd01160 11 RRFFAKEVAPFHHEWEKAGEVPREVWRKAGEQGLLGVGFPEEYGGIGGDLLSAAVLWEELARAgGSGPG--LSLHTdIVS 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2664202365 95 HAIVRWGSRSLKEYWLPRLARGESIGALAVSEPDVGSDAGSVTSRLTRDGDDWVLDGHKKWTTYGETADVYLVV------ 168
Cdd:cd01160 89 PYITRAGSPEQKERVLPQMVAGKKIGAIAMTEPGAGSDLQGIRTTARKDGDHYVLNGSKTFITNGMLADVVIVVartgge 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2664202365 169 GRSEEGPTAVLVERGTEGL-RTELIEDlIGIRASMTANVYFDGCRVPGGNLLARPGLGVSHVVGaALDLGRYTVGWGCVG 247
Cdd:cd01160 169 ARGAGGISLFLVERGTPGFsRGRKLKK-MGWKAQDTAELFFDDCRVPAENLLGEENKGFYYLMQ-NLPQERLLIAAGALA 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2664202365 248 ILDACVEASVDYAAERHQFGSAIKDHQLVRRLITNMYTDARAAR-LLCLEAGRLRDRRDPGALAgtSTAKYFASSAATRA 326
Cdd:cd01160 247 AAEFMLEETRNYVKQRKAFGKTLAQLQVVRHKIAELATKVAVTRaFLDNCAWRHEQGRLDVAEA--SMAKYWATELQNRV 324
|
330 340 350
....*....|....*....|....*....|....*...
gi 2664202365 327 AADAVQIHGANGCSSDFPVQRYLGDSRVMEIIEGSSQI 364
Cdd:cd01160 325 AYECVQLHGGWGYMREYPIARAYRDARVQPIYGGTTEI 362
|
|
| VLCAD |
cd01161 |
Very long chain acyl-CoA dehydrogenase; VLCAD is an acyl-CoA dehydrogenase (ACAD), which is ... |
17-375 |
1.40e-62 |
|
Very long chain acyl-CoA dehydrogenase; VLCAD is an acyl-CoA dehydrogenase (ACAD), which is found in the mitochondria of eukaryotes and in some bacteria. It catalyzes the alpha,beta dehydrogenation of the corresponding trans-enoyl-CoA by FAD, which becomes reduced. The reduced form of ACAD is reoxidized in the oxidative half-reaction by electron-transferring flavoprotein (ETF), from which the electrons are transferred to the mitochondrial respiratory chain coupled with ATP synthesis. VLCAD acts as a homodimer.
Pssm-ID: 173850 [Multi-domain] Cd Length: 409 Bit Score: 206.55 E-value: 1.40e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2664202365 17 RAFAERHIAPYADEYHRAQRTPPEAVKQLaaeGLLGLSVPEEYGGGGCDAVTLGLLAGELGRACSslrslLTVhTMVAH- 95
Cdd:cd01161 40 KFFEEVNDPAKNDQLEKIPRKTLTQLKEL---GLFGLQVPEEYGGLGLNNTQYARLAEIVGMDLG-----FSV-TLGAHq 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2664202365 96 -----AIVRWGSRSLKEYWLPRLARGESIGALAVSEPDVGSDAGSVTSR--LTRDGDDWVLDGHKKWTTYGETADVYLVV 168
Cdd:cd01161 111 sigfkGILLFGTEAQKEKYLPKLASGEWIAAFALTEPSSGSDAASIRTTavLSEDGKHYVLNGSKIWITNGGIADIFTVF 190
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2664202365 169 GRSE---------EGPTAVLVERGTEGLRTELIEDLIGIRASMTANVYFDGCRVPGGNLLARPGLGvsHVVGA-ALDLGR 238
Cdd:cd01161 191 AKTEvkdatgsvkDKITAFIVERSFGGVTNGPPEKKMGIKGSNTAEVYFEDVKIPVENVLGEVGDG--FKVAMnILNNGR 268
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2664202365 239 YTVGWGCVGILDACVEASVDYAAERHQFGSAIKDHQLVRRLITNMYTDARAARLLCLEAGRLRDRRDPGALA-GTSTAKY 317
Cdd:cd01161 269 FGMGAALIGTMKRCIEKAVDYANNRKQFGKKIHEFGLIQEKLANMAILQYATESMAYMTSGNMDRGLKAEYQiEAAISKV 348
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*...
gi 2664202365 318 FASSAATRAAADAVQIHGANGCSSDFPVQRYLGDSRVMEIIEGSSQIHQVGLAEYAFQ 375
Cdd:cd01161 349 FASEAAWLVVDEAIQIHGGMGFMREYGVERVLRDLRIFRIFEGTNEILRLFIALTGLQ 406
|
|
| PLN02519 |
PLN02519 |
isovaleryl-CoA dehydrogenase |
1-376 |
5.93e-57 |
|
isovaleryl-CoA dehydrogenase
Pssm-ID: 215284 [Multi-domain] Cd Length: 404 Bit Score: 191.63 E-value: 5.93e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2664202365 1 MSSALTPAQARAQKEFRA----FAERHIAPYADEYHRAQRTPPEA--VKQLAAEGLLGLSVPEEYGGGGCDAVTLGLLAG 74
Cdd:PLN02519 18 SSSSSSLLFDDTQLQFKEsvqqFAQENIAPHAAAIDATNSFPKDVnlWKLMGDFNLHGITAPEEYGGLGLGYLYHCIAME 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2664202365 75 ELGRACSSLRSLLTVHT-MVAHAIVRWGSRSLKEYWLPRLARGESIGALAVSEPDVGSDAGSVTSRLTRDGDDWVLDGHK 153
Cdd:PLN02519 98 EISRASGSVGLSYGAHSnLCINQLVRNGTPAQKEKYLPKLISGEHVGALAMSEPNSGSDVVSMKCKAERVDGGYVLNGNK 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2664202365 154 KWTTYGETADVYLVVGRSE-----EGPTAVLVERGTEGLRTELIEDLIGIRASMTANVYFDGCRVPGGNLLARPGLGVsH 228
Cdd:PLN02519 178 MWCTNGPVAQTLVVYAKTDvaagsKGITAFIIEKGMPGFSTAQKLDKLGMRGSDTCELVFENCFVPEENVLGQEGKGV-Y 256
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2664202365 229 VVGAALDLGRYTVGWGCVGILDACVEASVDYAAERHQFGSAIKDHQLVRRLITNMYTDARAARLLCLEAGRLRD--RRDP 306
Cdd:PLN02519 257 VMMSGLDLERLVLAAGPLGLMQACLDVVLPYVRQREQFGRPIGEFQFIQGKLADMYTSLQSSRSYVYSVARDCDngKVDR 336
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2664202365 307 GALAGTStakYFASSAATRAAADAVQIHGANGCSSDFPVQRYLGDSRVMEIIEGSSQIHQVGLAEYAFQE 376
Cdd:PLN02519 337 KDCAGVI---LCAAERATQVALQAIQCLGGNGYINEYPTGRLLRDAKLYEIGAGTSEIRRMLIGRELFKE 403
|
|
| MCAD |
cd01157 |
Medium chain acyl-CoA dehydrogenase; MCADs are mitochondrial beta-oxidation enzymes, which ... |
5-367 |
1.92e-55 |
|
Medium chain acyl-CoA dehydrogenase; MCADs are mitochondrial beta-oxidation enzymes, which catalyze the alpha,beta dehydrogenation of the corresponding medium chain acyl-CoA by FAD, which becomes reduced. The reduced form of MCAD is reoxidized in the oxidative half-reaction by electron-transferring flavoprotein (ETF), from which the electrons are transferred to the mitochondrial respiratory chain coupled with ATP synthesis. MCAD is a homotetramer.
Pssm-ID: 173846 [Multi-domain] Cd Length: 378 Bit Score: 187.02 E-value: 1.92e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2664202365 5 LTPAQARAQKEFRAFAERHIAPYADEYHRAQRTPPEAVKQLAAEGLLGLSVPEEYGGGGCDAVTLGLLAGELGRACSSLR 84
Cdd:cd01157 1 LTEQQKEFQETARKFAREEIIPVAAEYDKSGEYPWPLIKRAWELGLMNTHIPEDCGGLGLGTFDTCLITEELAYGCTGVQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2664202365 85 SLLTVHTMVAHAIVRWGSRSLKEYWLPRLARGESIGALAVSEPDVGSDAGSVTSRLTRDGDDWVLDGHKKWTTYGETADV 164
Cdd:cd01157 81 TAIEANSLGQMPVIISGNDEQKKKYLGRMTEEPLMCAYCVTEPGAGSDVAGIKTKAEKKGDEYIINGQKMWITNGGKANW 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2664202365 165 YLVVGRSEEGP--------TAVLVERGTEGLRTELIEDLIGIRASMTANVYFDGCRVPGGNLLARPGLGVSHVVGaALDL 236
Cdd:cd01157 161 YFLLARSDPDPkcpaskafTGFIVEADTPGIQPGRKELNMGQRCSDTRGITFEDVRVPKENVLIGEGAGFKIAMG-AFDK 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2664202365 237 GRYTVGWGCVGILDACVEASVDYAAERHQFGSAIKDHQLVRRLITNMYTDARAARLLCLEAGRLRD--RRDPgalAGTST 314
Cdd:cd01157 240 TRPPVAAGAVGLAQRALDEATKYALERKTFGKLIAEHQAVSFMLADMAMKVELARLAYQRAAWEVDsgRRNT---YYASI 316
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|...
gi 2664202365 315 AKYFASSAATRAAADAVQIHGANGCSSDFPVQRYLGDSRVMEIIEGSSQIHQV 367
Cdd:cd01157 317 AKAFAADIANQLATDAVQIFGGNGFNSEYPVEKLMRDAKIYQIYEGTSQIQRL 369
|
|
| PTZ00461 |
PTZ00461 |
isovaleryl-CoA dehydrogenase; Provisional |
6-371 |
1.58e-50 |
|
isovaleryl-CoA dehydrogenase; Provisional
Pssm-ID: 185640 [Multi-domain] Cd Length: 410 Bit Score: 174.74 E-value: 1.58e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2664202365 6 TPAQARAQKEFRAFAERHIAPYADEYHRAQRTPPEAVKQLAAEGLLGLSVPEEYGGGGCDAVTLGLLAGELGRACSSLRS 85
Cdd:PTZ00461 38 TPEHAALRETVAKFSREVVDKHAREDDINMHFNRDLFKQLGDLGVMGVTVPEADGGAGMDAVAAVIIHHELSKYDPGFCL 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2664202365 86 LLTVHTMV-AHAIVRWGSRSLKEYWLPRLARGESIGALAVSEPDVGSDAGSVTSRLTRDGD-DWVLDGHKKWTTYGETAD 163
Cdd:PTZ00461 118 AYLAHSMLfVNNFYYSASPAQRARWLPKVLTGEHVGAMGMSEPGAGTDVLGMRTTAKKDSNgNYVLNGSKIWITNGTVAD 197
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2664202365 164 VYLVVGRSEEGPTAVLVERGTEGLRTELIEDLIGIRASMTANVYFDGCRVPGGNLLARPGLGvshVVGAA--LDLGRYTV 241
Cdd:PTZ00461 198 VFLIYAKVDGKITAFVVERGTKGFTQGPKIDKCGMRASHMCQLFFEDVVVPAENLLGEEGKG---MVGMMrnLELERVTL 274
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2664202365 242 GWGCVGILDACVEASVDYAAERHQFGSAIKDHQLVRRLITNMYTDARAARLLCLEAGRLRDRRDPGALaGTSTAKYFASS 321
Cdd:PTZ00461 275 AAMAVGIAERSVELMTSYASERKAFGKPISNFGQIQRYIAEGYADTEAAKALVYSVSHNVHPGNKNRL-GSDAAKLFATP 353
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|
gi 2664202365 322 AATRAAADAVQIHGANGCSSDFPVQRYLGDSRVMEIIEGSSQIHQVGLAE 371
Cdd:PTZ00461 354 IAKKVADSAIQVMGGMGYSRDMPVERLWRDAKLLEIGGGTIEAHHKNITK 403
|
|
| ACAD_fadE5 |
cd01153 |
Putative acyl-CoA dehydrogenases similar to fadE5; Putative acyl-CoA dehydrogenase (ACAD). ... |
36-364 |
3.61e-40 |
|
Putative acyl-CoA dehydrogenases similar to fadE5; Putative acyl-CoA dehydrogenase (ACAD). Mitochondrial acyl-CoA dehydrogenases (ACAD) catalyze the alpha,beta dehydrogenation of the corresponding trans-enoyl-CoA by FAD, which becomes reduced. The reduced form of ACAD is reoxidized in the oxidative half-reaction by electron-transferring flavoprotein (ETF), from which the electrons are transferred to the mitochondrial respiratory chain coupled with ATP synthesis. The ACD family includes the eukaryotic beta-oxidation, as well as amino acid catabolism enzymes. These enzymes share high sequence similarity, but differ in their substrate specificities. The mitochondrial ACD's are generally homotetramers and have an active site glutamate at a conserved position.
Pssm-ID: 173842 [Multi-domain] Cd Length: 407 Bit Score: 147.15 E-value: 3.61e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2664202365 36 RTPP---EAVKQLAAEGLLGLSVPEEYGGGGCDAVTLGLLAGELGRACSSLRSLLTVHTMVAHaIVRWGSRSLKEYWLPR 112
Cdd:cd01153 33 VVPPpfkEALDAFAEAGWMALGVPEEYGGQGLPITVYSALAEIFSRGDAPLMYASGTQGAAAT-LLAHGTEAQREKWIPR 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2664202365 113 LARGESIGALAVSEPDVGSDAGSVTSRLTRDGD-DWVLDGHKKWTTYGETAD----VYLVVGRSEEGPTAV--------- 178
Cdd:cd01153 112 LAEGEWTGTMCLTEPDAGSDLGALRTKAVYQADgSWRINGVKRFISAGEHDMseniVHLVLARSEGAPPGVkglslflvp 191
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2664202365 179 --LVERGTEGLRTELIEDLIGIRASMTANVYFDGCRVPggnLLARPGLGVSHVVgAALDLGRYTVGWGCVGILDACVEAS 256
Cdd:cd01153 192 kfLDDGERNGVTVARIEEKMGLHGSPTCELVFDNAKGE---LIGEEGMGLAQMF-AMMNGARLGVGTQGTGLAEAAYLNA 267
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2664202365 257 VDYAAERHQFGSAIKD--------HQLVRR-LIT-----------NMYTdARAARLLCLEAGRLRDRRDPGALAG--TST 314
Cdd:cd01153 268 LAYAKERKQGGDLIKAapavtiihHPDVRRsLMTqkayaegsralDLYT-ATVQDLAERKATEGEDRKALSALADllTPV 346
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|
gi 2664202365 315 AKYFASSAATRAAADAVQIHGANGCSSDFPVQRYLGDSRVMEIIEGSSQI 364
Cdd:cd01153 347 VKGFGSEAALEAVSDAIQVHGGSGYTREYPIEQYYRDARITTIYEGTTGI 396
|
|
| Acyl-CoA_dh_N |
pfam02771 |
Acyl-CoA dehydrogenase, N-terminal domain; The N-terminal domain of Acyl-CoA dehydrogenase is ... |
6-117 |
9.70e-38 |
|
Acyl-CoA dehydrogenase, N-terminal domain; The N-terminal domain of Acyl-CoA dehydrogenase is an all-alpha domain.
Pssm-ID: 460686 [Multi-domain] Cd Length: 113 Bit Score: 132.20 E-value: 9.70e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2664202365 6 TPAQARAQKEFRAFAERHIAPYADEYHRAQRTPPEAVKQLAAEGLLGLSVPEEYGGGGCDAVTLGLLAGELGRACSSLRS 85
Cdd:pfam02771 1 TEEQEALRDTVREFAEEEIAPHAAEWDEEGEFPRELWKKLGELGLLGITIPEEYGGAGLDYLAYALVAEELARADASVAL 80
|
90 100 110
....*....|....*....|....*....|...
gi 2664202365 86 LLTVHT-MVAHAIVRWGSRSLKEYWLPRLARGE 117
Cdd:pfam02771 81 ALSVHSsLGAPPILRFGTEEQKERYLPKLASGE 113
|
|
| PLN02526 |
PLN02526 |
acyl-coenzyme A oxidase |
5-365 |
1.02e-37 |
|
acyl-coenzyme A oxidase
Pssm-ID: 178141 [Multi-domain] Cd Length: 412 Bit Score: 140.76 E-value: 1.02e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2664202365 5 LTPAQARAQKEFRAFAERHIAPYADEYHRAQRTPPEAVKQLAAEGLLGLSVpEEYGGGGCDAVTLGLLAGELGRACSSLR 84
Cdd:PLN02526 29 LTPEEQALRKRVRECMEKEVAPIMTEYWEKAEFPFHIIPKLGSLGIAGGTI-KGYGCPGLSITASAIATAEVARVDASCS 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2664202365 85 SLLTVHTMVAHA-IVRWGSRSLKEYWLPRLARGESIGALAVSEPDVGSDAGSVTSRLTRDGDDWVLDGHKKWTTYGETAD 163
Cdd:PLN02526 108 TFILVHSSLAMLtIALCGSEAQKQKYLPSLAQLDTVACWALTEPDYGSDASSLNTTATKVEGGWILNGQKRWIGNSTFAD 187
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2664202365 164 VYLVVGR--SEEGPTAVLVERGTEGLRTELIEDLIGIRASMTANVYFDGCRVPGGNLLarPGLGVSHVVGAALDLGRYTV 241
Cdd:PLN02526 188 VLVIFARntTTNQINGFIVKKGAPGLKATKIENKIGLRMVQNGDIVLKDVFVPDEDRL--PGVNSFQDTNKVLAVSRVMV 265
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2664202365 242 GWGCVGILDACVEASVDYAAERHQFGSAIKDHQLVRRLITNMYTDARAARL----LC--LEAGRLrdrrDPGAlagTSTA 315
Cdd:PLN02526 266 AWQPIGISMGVYDMCHRYLKERKQFGAPLAAFQINQEKLVRMLGNIQAMFLvgwrLCklYESGKM----TPGH---ASLG 338
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|
gi 2664202365 316 KYFASSAATRAAADAVQIHGANGCSSDFPVQRYLGDSRVMEIIEGSSQIH 365
Cdd:PLN02526 339 KAWITKKARETVALGRELLGGNGILADFLVAKAFCDLEPIYTYEGTYDIN 388
|
|
| ACAD_fadE6_17_26 |
cd01152 |
Putative acyl-CoA dehydrogenases similar to fadE6, fadE17, and fadE26; Putative acyl-CoA ... |
7-375 |
4.92e-37 |
|
Putative acyl-CoA dehydrogenases similar to fadE6, fadE17, and fadE26; Putative acyl-CoA dehydrogenases (ACAD). Mitochondrial acyl-CoA dehydrogenases (ACAD) catalyze the alpha, beta dehydrogenation of the corresponding trans-enoyl-CoA by FAD, which becomes reduced. The reduced form of ACAD is reoxidized in the oxidative half-reaction by electron-transferring flavoprotein (ETF), from which the electrons are transferred to the mitochondrial respiratory chain coupled with ATP synthesis. The ACD family includes the eukaryotic beta-oxidation, as well as amino acid catabolism enzymes. These enzymes share high sequence similarity, but differ in their substrate specificities. The mitochondrial ACD's are generally homotetramers and have an active site glutamate at a conserved position.
Pssm-ID: 173841 [Multi-domain] Cd Length: 380 Bit Score: 138.25 E-value: 4.92e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2664202365 7 PAQARAQKEFRAFAERHIAPYADEYHRAQRTPPEAV-----KQLAAEGLLGLSVPEEYGGGGCDAVTLGLLAGELGRACS 81
Cdd:cd01152 1 PSEEAFRAEVRAWLAAHLPPELREESALGYREGREDrrrwqRALAAAGWAAPGWPKEYGGRGASLMEQLIFREEMAAAGA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2664202365 82 SLRSLLTVHTMVAHAIVRWGSRSLKEYWLPRLARGESIGALAVSEPDVGSDAGSVTSRLTRDGDDWVLDGHKKWTTYGET 161
Cdd:cd01152 81 PVPFNQIGIDLAGPTILAYGTDEQKRRFLPPILSGEEIWCQGFSEPGAGSDLAGLRTRAVRDGDDWVVNGQKIWTSGAHY 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2664202365 162 AD-VYLVV-----GRSEEGPTAVLVERGTEGLRTELIEDLIGirASMTANVYFDGCRVPGGNLLARPGLGVsHVVGAALD 235
Cdd:cd01152 161 ADwAWLLVrtdpeAPKHRGISILLVDMDSPGVTVRPIRSING--GEFFNEVFLDDVRVPDANRVGEVNDGW-KVAMTTLN 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2664202365 236 LGRYTVG----WGCVGILDACveasvdyAAERHQFGSAIKDHQLVRRLiTNMYTDARAARLLCLE-AGRLRDRRDPGALA 310
Cdd:cd01152 238 FERVSIGgsaaTFFELLLARL-------LLLTRDGRPLIDDPLVRQRL-ARLEAEAEALRLLVFRlASALAAGKPPGAEA 309
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2664202365 311 gtSTAKYFASSAATRAAADAVQIHGANGCSSDFP--------VQRYLGDSRVMEIIEGSSQIHQVGLAEYAFQ 375
Cdd:cd01152 310 --SIAKLFGSELAQELAELALELLGTAALLRDPApgaelagrWEADYLRSRATTIYGGTSEIQRNIIAERLLG 380
|
|
| ACAD_FadE2 |
cd01155 |
Acyl-CoA dehydrogenases similar to fadE2; FadE2-like Acyl-CoA dehydrogenase (ACAD). Acyl-CoA ... |
10-371 |
2.09e-32 |
|
Acyl-CoA dehydrogenases similar to fadE2; FadE2-like Acyl-CoA dehydrogenase (ACAD). Acyl-CoA dehydrogenases (ACAD) catalyze the alpha,beta dehydrogenation of the corresponding trans-enoyl-CoA by FAD, which becomes reduced. The reduced form of ACAD is reoxidized in the oxidative half-reaction by electron-transferring flavoprotein (ETF), from which the electrons are transferred to the mitochondrial respiratory chain coupled with ATP synthesis. The ACAD family includes the eukaryotic beta-oxidation, as well as amino acid catabolism enzymes. These enzymes share high sequence similarity, but differ in their substrate specificities. ACAD's are generally homotetramers and have an active site glutamate at a conserved position.
Pssm-ID: 173844 [Multi-domain] Cd Length: 394 Bit Score: 125.97 E-value: 2.09e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2664202365 10 ARAQK---EFRAFAERHIAPYADEY--------HRAQRTPP--EAVKQLA-AEGLLGLSVPEEYGGGGCDAVTLGLLAGE 75
Cdd:cd01155 1 RKAQElraRVKAFMEEHVYPAEQEFleyyaeggDRWWTPPPiiEKLKAKAkAEGLWNLFLPEVSGLSGLTNLEYAYLAEE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2664202365 76 LGRA--------CSSlrslltVHTMVAHAIVRWGSRSLKEYWLPRLARGESIGALAVSEPDVGS-DAGSVTSRLTRDGDD 146
Cdd:cd01155 81 TGRSffapevfnCQA------PDTGNMEVLHRYGSEEQKKQWLEPLLDGKIRSAFAMTEPDVASsDATNIECSIERDGDD 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2664202365 147 WVLDGhKKWTTYGET---ADVYLVVGRSEEGP-------TAVLVERGTEGlrteliedlIGIRASMT-----------AN 205
Cdd:cd01155 155 YVING-RKWWSSGAGdprCKIAIVMGRTDPDGaprhrqqSMILVPMDTPG---------VTIIRPLSvfgyddaphghAE 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2664202365 206 VYFDGCRVPGGNLLARPGLGVShVVGAALDLGRYTVGWGCVGILDACVEASVDYAAERHQFGSAIKDHQLVRRLITNMYT 285
Cdd:cd01155 225 ITFDNVRVPASNLILGEGRGFE-IAQGRLGPGRIHHCMRLIGAAERALELMCQRAVSREAFGKKLAQHGVVAHWIAKSRI 303
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2664202365 286 DARAARLLCLEAGRLRDRRDP-GALAGTSTAKYFASSAATRAAADAVQIHGANGCSSDFPVQRYLGDSRVMEIIEGSSQI 364
Cdd:cd01155 304 EIEQARLLVLKAAHMIDTVGNkAARKEIAMIKVAAPRMALKIIDRAIQVHGAAGVSQDTPLANMYAWARTLRIADGPDEV 383
|
....*....
gi 2664202365 365 H--QVGLAE 371
Cdd:cd01155 384 HlrSIARME 392
|
|
| PRK12341 |
PRK12341 |
acyl-CoA dehydrogenase; |
29-364 |
8.04e-31 |
|
acyl-CoA dehydrogenase;
Pssm-ID: 183454 [Multi-domain] Cd Length: 381 Bit Score: 121.37 E-value: 8.04e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2664202365 29 DEYHRaqrTPPEAVKQLAAEGLLGLSVPEEYGGGGCDAVTLGLLAGELGRACSSLrsLLTVHTMVAHAIVRWGS-RSLKE 107
Cdd:PRK12341 33 DENGT---YPREFMRALADNGISMLGVPEEFGGTPADYVTQMLVLEEVSKCGAPA--FLITNGQCIHSMRRFGSaEQLRK 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2664202365 108 YWLPRLARGESIGALAVSEPDVGSDAGSVTSRLTRDGDDWVLDGHKKWTTYGETADVYLVVGRSEEGP------TAVLVE 181
Cdd:PRK12341 108 TAESTLETGDPAYALALTEPGAGSDNNSATTTYTRKNGKVYLNGQKTFITGAKEYPYMLVLARDPQPKdpkkafTLWWVD 187
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2664202365 182 RGTEGLRTELIEDlIGIRASMTANVYFDGCRVPGGNLLARPGLGVSHVVGaALDLGRYTVGWGCVGILDACVEASVDYAA 261
Cdd:PRK12341 188 SSKPGIKINPLHK-IGWHMLSTCEVYLDNVEVEESDLVGEEGMGFLNVMY-NFEMERLINAARSLGFAECAFEDAARYAN 265
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2664202365 262 ERHQFGSAIKDHQLVRRLITNMYTDARAARLLCLEAGRLRDRRDPGALAgTSTAKYFASSAATRAAADAVQIHGANGCSS 341
Cdd:PRK12341 266 QRIQFGKPIGHNQLIQEKLTLMAIKIENMRNMVYKVAWQADNGQSLRTS-AALAKLYCARTAMEVIDDAIQIMGGLGYTD 344
|
330 340
....*....|....*....|...
gi 2664202365 342 DFPVQRYLGDSRVMEIIEGSSQI 364
Cdd:PRK12341 345 EARVSRFWRDVRCERIGGGTDEI 367
|
|
| Acyl-CoA_dh_1 |
pfam00441 |
Acyl-CoA dehydrogenase, C-terminal domain; C-terminal domain of Acyl-CoA dehydrogenase is an ... |
228-365 |
4.49e-29 |
|
Acyl-CoA dehydrogenase, C-terminal domain; C-terminal domain of Acyl-CoA dehydrogenase is an all-alpha, four helical up-and-down bundle.
Pssm-ID: 395354 [Multi-domain] Cd Length: 149 Bit Score: 110.42 E-value: 4.49e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2664202365 228 HVVGAALDLGRYTVGWGCVGILDACVEASVDYAAERHQFGSAIKDHQLVRRLITNMYTDARAARLLCLEAGRLRDRRDPg 307
Cdd:pfam00441 5 RVAMETLNHERLAIAAMALGLARRALDEALAYARRRKAFGRPLIDFQLVRHKLAEMAAEIEAARLLVYRAAEALDAGGP- 83
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*...
gi 2664202365 308 ALAGTSTAKYFASSAATRAAADAVQIHGANGCSSDFPVQRYLGDSRVMEIIEGSSQIH 365
Cdd:pfam00441 84 DGAEASMAKLYASEAAVEVADLAMQLHGGYGYLREYPVERLYRDARVLRIGEGTSEIQ 141
|
|
| AidB |
cd01154 |
Proteins involved in DNA damage response, similar to the AidB gene product; AidB is one of ... |
30-364 |
2.68e-26 |
|
Proteins involved in DNA damage response, similar to the AidB gene product; AidB is one of several genes involved in the SOS adaptive response to DNA alkylation damage, whose expression is activated by the Ada protein. Its function has not been entirely elucidated; however, it is similar in sequence and function to acyl-CoA dehydrogenases. It has been proposed that aidB directly destroys DNA alkylating agents such as nitrosoguanidines (nitrosated amides) or their reaction intermediates.
Pssm-ID: 173843 [Multi-domain] Cd Length: 418 Bit Score: 109.00 E-value: 2.68e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2664202365 30 EYHRAQRtppEAVKQLAAEGLLGlSVPEEYGGGGC-DAVTLGLL--AGELGRACSslrslLTVHTMVAHAIVRWGSRSLK 106
Cdd:cd01154 62 WVHPAWH---ALMRRLIEEGVIN-IEDGPAGEGRRhVHFAAGYLlsDAAAGLLCP-----LTMTDAAVYALRKYGPEELK 132
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2664202365 107 EYWLPRLARGES---IGALAVSEPDVGSDAGSVTSRLTRDGDD-WVLDGHKkWTTYGETADVYLVVGRSEEGPTAV---- 178
Cdd:cd01154 133 QYLPGLLSDRYKtglLGGTWMTEKQGGSDLGANETTAERSGGGvYRLNGHK-WFASAPLADAALVLARPEGAPAGArgls 211
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2664202365 179 --LVER----GT-EGLRTELIEDLIGIRASMTANVYFDGCRvpgGNLLARPGLGVSHVVgAALDLGRYTVGWGCVGILDA 251
Cdd:cd01154 212 lfLVPRlledGTrNGYRIRRLKDKLGTRSVATGEVEFDDAE---AYLIGDEGKGIYYIL-EMLNISRLDNAVAALGIMRR 287
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2664202365 252 CVEASVDYAAERHQFGSAIKDHQLVRRLITNMYTDARAARLLCLEAGRLRDRRDPG-------ALAGTSTAKYFASSAAT 324
Cdd:cd01154 288 ALSEAYHYARHRRAFGKPLIDHPLMRRDLAEMEVDVEAATALTFRAARAFDRAAADkpveahmARLATPVAKLIACKRAA 367
|
330 340 350 360
....*....|....*....|....*....|....*....|
gi 2664202365 325 RAAADAVQIHGANGCSSDFPVQRYLGDSRVMEIIEGSSQI 364
Cdd:cd01154 368 PVTSEAMEVFGGNGYLEEWPVARLHREAQVTPIWEGTGNI 407
|
|
| PRK03354 |
PRK03354 |
crotonobetainyl-CoA dehydrogenase; Validated |
27-364 |
1.02e-25 |
|
crotonobetainyl-CoA dehydrogenase; Validated
Pssm-ID: 179566 [Multi-domain] Cd Length: 380 Bit Score: 106.84 E-value: 1.02e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2664202365 27 YADEYHRAQRTPPEAVKQLAAEGLLGLSVPEEYGGGGCDAVTLGLLAGELGRACSSLRSLLTVHTMVaHAIVRWGSRSLK 106
Cdd:PRK03354 28 YFAECDRDSVYPERFVKALADMGIDSLLIPEEHGGLDAGFVTLAAVWMELGRLGAPTYVLYQLPGGF-NTFLREGTQEQI 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2664202365 107 EYWLPRLARGESIGALAVSEPDVGSDAGSVTSRLTRDGDDWVLDGHKKWTTYGETADvYLVV----GRSEEGP--TAVLV 180
Cdd:PRK03354 107 DKIMAFRGTGKQMWNSAITEPGAGSDVGSLKTTYTRRNGKVYLNGSKCFITSSAYTP-YIVVmardGASPDKPvyTEWFV 185
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2664202365 181 ERGTEGLRTELIEDLiGIRASMTANVYFDGCRVPGGNLLARPGLGVSHVVgAALDLGRYTVGWGCVGILDACVEASVDYA 260
Cdd:PRK03354 186 DMSKPGIKVTKLEKL-GLRMDSCCEITFDDVELDEKDMFGREGNGFNRVK-EEFDHERFLVALTNYGTAMCAFEDAARYA 263
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2664202365 261 AERHQFGSAIKDHQLVRRLITNMYTDARAARLLCLEAGRLRDRRDPGAlAGTSTAKYFASSAATRAAADAVQIHGANGCS 340
Cdd:PRK03354 264 NQRVQFGEAIGRFQLIQEKFAHMAIKLNSMKNMLYEAAWKADNGTITS-GDAAMCKYFCANAAFEVVDSAMQVLGGVGIA 342
|
330 340
....*....|....*....|....
gi 2664202365 341 SDFPVQRYLGDSRVMEIIEGSSQI 364
Cdd:PRK03354 343 GNHRISRFWRDLRVDRVSGGSDEM 366
|
|
| DszC |
cd01163 |
Dibenzothiophene (DBT) desulfurization enzyme C; DszC is a flavin reductase dependent enzyme, ... |
16-303 |
8.22e-23 |
|
Dibenzothiophene (DBT) desulfurization enzyme C; DszC is a flavin reductase dependent enzyme, which catalyzes the first two steps of DBT desulfurization in mesophilic bacteria. DszC converts DBT to DBT-sulfoxide, which is then converted to DBT-sulfone. Bacteria with this enzyme are candidates for the removal of organic sulfur compounds from fossil fuels, which pollute the environment. An equivalent enzyme tdsC, is found in thermophilic bacteria. This alignment also contains a closely related uncharacterized subgroup.
Pssm-ID: 173852 [Multi-domain] Cd Length: 377 Bit Score: 98.55 E-value: 8.22e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2664202365 16 FRAFAERhIAPYADEYHRAQRTPPEAVKQLAAEGLLGLSVPEEYGGGGCDAVTLGLLAGELGRACSSLRSLLTVHTMVAH 95
Cdd:cd01163 3 ARPLAAR-IAEGAAERDRQRGLPYEEVALLRQSGLGTLRVPKEYGGLGASLPDLYEVVRELAAADSNIAQALRAHFGFVE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2664202365 96 AIVRWGSRSLKEYWLPRLARGESIGAlAVSEPDvGSDAGSVTSRLTRDGDDWVLDGHKKWTTYGETADVYLVVGRSEEGP 175
Cdd:cd01163 82 ALLLAGPEQFRKRWFGRVLNGWIFGN-AVSERG-SVRPGTFLTATVRDGGGYVLNGKKFYSTGALFSDWVTVSALDEEGK 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2664202365 176 -TAVLVERGTEGLRteLIEDLIGIRASMTAN--VYFDGCRVPGGNLLARPGLG--------VSHVVGAALDlgrytvgwg 244
Cdd:cd01163 160 lVFAAVPTDRPGIT--VVDDWDGFGQRLTASgtVTFDNVRVEPDEVLPRPNAPdrgtlltaIYQLVLAAVL--------- 228
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2664202365 245 cVGILDACVEASVDYAAER-----HQFGSAIKDHQLVRRLITNMYTDARAARLLCLEAGRLRDR 303
Cdd:cd01163 229 -AGIARAALDDAVAYVRSRtrpwiHSGAESARDDPYVQQVVGDLAARLHAAEALVLQAARALDA 291
|
|
| Acyl-CoA_dh_M |
pfam02770 |
Acyl-CoA dehydrogenase, middle domain; Central domain of Acyl-CoA dehydrogenase has a ... |
121-209 |
5.34e-21 |
|
Acyl-CoA dehydrogenase, middle domain; Central domain of Acyl-CoA dehydrogenase has a beta-barrel fold.
Pssm-ID: 460685 [Multi-domain] Cd Length: 95 Bit Score: 86.57 E-value: 5.34e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2664202365 121 ALAVSEPDVGSDAGSVTSRL-TRDGDDWVLDGHKKWTTYGETADVYLVVGRSE-----EGPTAVLVERGTEGLRTELIED 194
Cdd:pfam02770 1 AFALTEPGAGSDVASLKTTAaDGDGGGWVLNGTKWWITNAGIADLFLVLARTGgddrhGGISLFLVPKDAPGVSVRRIET 80
|
90
....*....|....*
gi 2664202365 195 LIGIRASMTANVYFD 209
Cdd:pfam02770 81 KLGVRGLPTGELVFD 95
|
|
| PLN02876 |
PLN02876 |
acyl-CoA dehydrogenase |
19-365 |
2.65e-17 |
|
acyl-CoA dehydrogenase
Pssm-ID: 215473 [Multi-domain] Cd Length: 822 Bit Score: 84.08 E-value: 2.65e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2664202365 19 FAERHIAPYADE-YHRAQRT-------PPEAVKQLA-AEGLLGLSVP--------------EEYGGGGCDAVTL---GLL 72
Cdd:PLN02876 416 FMEDHIYPMENEfYKLAQSSsrwtvhpEEERLKELAkKEGLWNLWIPldsaararkllfedNKHMVSGDSADQLlgaGLS 495
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2664202365 73 AGELGRACSSL-RSLLTVHTMVAHA--------IVRWGSRSLKEYWLPRLARGESIGALAVSEPDVGS-DAGSVTSRLTR 142
Cdd:PLN02876 496 NLEYGYLCEIMgRSVWAPQVFNCGApdtgnmevLLRYGNKEQQLEWLIPLLEGKIRSGFAMTEPQVASsDATNIECSIRR 575
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2664202365 143 DGDDWVLDGHKKWTT--YGETADVYLVVGRSEegPTA--------VLVERGTEGlrteliedlIGIRASMT--------- 203
Cdd:PLN02876 576 QGDSYVINGTKWWTSgaMDPRCRVLIVMGKTD--FNApkhkqqsmILVDIQTPG---------VQIKRPLLvfgfddaph 644
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2664202365 204 --ANVYFDGCRVPGGNLLARPGLGVSHVVGAaLDLGRYTVGWGCVGILDACVEASVDYAAERHQFGSAIKDHQLVRRLIT 281
Cdd:PLN02876 645 ghAEISFENVRVPAKNILLGEGRGFEIAQGR-LGPGRLHHCMRLIGAAERGMQLMVQRALSRKAFGKLIAQHGSFLSDLA 723
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2664202365 282 NMYTDARAARLLCLEAG----RLRDRRDPGALAgtsTAKYFASSAATRAAADAVQIHGANGCSSDFPVQRYLGDSRVMEI 357
Cdd:PLN02876 724 KCRVELEQTRLLVLEAAdqldRLGNKKARGIIA---MAKVAAPNMALKVLDMAMQVHGAAGVSSDTVLAHLWATARTLRI 800
|
....*...
gi 2664202365 358 IEGSSQIH 365
Cdd:PLN02876 801 ADGPDEVH 808
|
|
| PTZ00456 |
PTZ00456 |
acyl-CoA dehydrogenase; Provisional |
37-367 |
2.61e-16 |
|
acyl-CoA dehydrogenase; Provisional
Pssm-ID: 185635 [Multi-domain] Cd Length: 622 Bit Score: 80.68 E-value: 2.61e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2664202365 37 TPP---EAVKQLAAEGLLGLSVPEEYGGGGCdAVTLGLLAGEL-GRACSSLRSLLTVHTMVAHAIVRWGSRSLKEYWLPR 112
Cdd:PTZ00456 97 TPKgfkEAYQALKAGGWTGISEPEEYGGQAL-PLSVGFITRELmATANWGFSMYPGLSIGAANTLMAWGSEEQKEQYLTK 175
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2664202365 113 LARGESIGALAVSEPDVGSDAGSVTSRLTRDGD-DWVLDGHKKWTTYGE---TAD-VYLVVGRSEEGPTAV------LVE 181
Cdd:PTZ00456 176 LVSGEWSGTMCLTEPQCGTDLGQVKTKAEPSADgSYKITGTKIFISAGDhdlTENiVHIVLARLPNSLPTTkglslfLVP 255
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2664202365 182 RGTE----GLRTEL------IEDLIGIRASMTANVYFDGCRvpgGNLLARPGLGVSHV--------VGAALDlgrytvgw 243
Cdd:PTZ00456 256 RHVVkpdgSLETAKnvkcigLEKKMGIKGSSTCQLSFENSV---GYLIGEPNAGMKQMftfmntarVGTALE-------- 324
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2664202365 244 gCVGILDACVEASVDYAAERHQF------------GSAIKDHQLVRRLITNMYTDARAARLLCLEAGRLRD----RRDPG 307
Cdd:PTZ00456 325 -GVCHAELAFQNALRYARERRSMralsgtkepekpADRIICHANVRQNILFAKAVAEGGRALLLDVGRLLDihaaAKDAA 403
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2664202365 308 ALAG--------TSTAKYFASSAATRAAADAVQIHGANGCSSDFPVQRYLGDSRVMEIIEGSSQIHQV 367
Cdd:PTZ00456 404 TREAldheigfyTPIAKGCLTEWGVEAASRCLQVWGGHGYIKGNGMEQILRDARIGTLYEGTTGIQAL 471
|
|
| PRK13026 |
PRK13026 |
acyl-CoA dehydrogenase; Reviewed |
38-187 |
2.96e-11 |
|
acyl-CoA dehydrogenase; Reviewed
Pssm-ID: 237277 [Multi-domain] Cd Length: 774 Bit Score: 64.98 E-value: 2.96e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2664202365 38 PPEAVKQLAAEGLLGLSVPEEYGGGGCDAvtlgllagelgRACS------SLRSLLT-VHTMV------AHAIVRWGSRS 104
Cdd:PRK13026 110 PPEVWDYLKKEGFFALIIPKEYGGKGFSA-----------YANStivskiATRSVSAaVTVMVpnslgpGELLTHYGTQE 178
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2664202365 105 LKEYWLPRLARGESIGALAVSEPDVGSDAGSVTS-----RLTRDGDDWV---LDGHKKWTTYGETADVY----------- 165
Cdd:PRK13026 179 QKDYWLPRLADGTEIPCFALTGPEAGSDAGAIPDtgivcRGEFEGEEVLglrLTWDKRYITLAPVATVLglafklrdpdg 258
|
170 180
....*....|....*....|..
gi 2664202365 166 LVVGRSEEGPTAVLVERGTEGL 187
Cdd:PRK13026 259 LLGDKKELGITCALIPTDHPGV 280
|
|
| fadE |
PRK09463 |
acyl-CoA dehydrogenase; Reviewed |
32-137 |
5.59e-10 |
|
acyl-CoA dehydrogenase; Reviewed
Pssm-ID: 236528 [Multi-domain] Cd Length: 777 Bit Score: 60.99 E-value: 5.59e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2664202365 32 HRAQRTPPEAVKQLAAEGLLGLSVPEEYGGggcdavtLGLLAgeLGRAC-----SSLRSLLTVHTMV------AHAIVRW 100
Cdd:PRK09463 105 HELADLPPEVWQFIKEHGFFGMIIPKEYGG-------LEFSA--YAHSRvlqklASRSGTLAVTVMVpnslgpGELLLHY 175
|
90 100 110
....*....|....*....|....*....|....*..
gi 2664202365 101 GSRSLKEYWLPRLARGESIGALAVSEPDVGSDAGSVT 137
Cdd:PRK09463 176 GTDEQKDHYLPRLARGEEIPCFALTSPEAGSDAGSIP 212
|
|
| NcnH |
cd01159 |
Naphthocyclinone hydroxylase; Naphthocyclinone is an aromatic polyketide and an antibiotic, ... |
24-355 |
6.43e-09 |
|
Naphthocyclinone hydroxylase; Naphthocyclinone is an aromatic polyketide and an antibiotic, which is active against Gram-positive bacteria. Polyketides are secondary metabolites, which have important biological functions such as antitumor, immunosupressive or antibiotic activities. NcnH is a hydroxylase involved in the biosynthesis of naphthocyclinone and possibly other polyketides.
Pssm-ID: 173848 [Multi-domain] Cd Length: 370 Bit Score: 56.97 E-value: 6.43e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2664202365 24 IAPYADEYHRAQRTPPEAVKQLAAEGLLGLSVPEEYGGGGCDAVTLGLLAGELGRACSSLRSLLTVHTMVAHAIVRWGSR 103
Cdd:cd01159 10 IRERAPEAERARRLPDEVVRALREIGFFRMFVPKRYGGLEGDFAEFAEAIATLAEACGSAAWVASIVATHSRMLAAFPPE 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2664202365 104 SLKEYWlprlarGESIGALAVSepdvgsdAGSVTSRLTRDGDDWVLDGHKKWTTYGETADVYLVVGRSEEG-----PTAV 178
Cdd:cd01159 90 AQEEVW------GDGPDTLLAG-------SYAPGGRAERVDGGYRVSGTWPFASGCDHADWILVGAIVEDDdggplPRAF 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2664202365 179 LVERgtEGLRTELIEDLIGIRASMTANVYFDGCRVPGGNLLARPGLGVSHVVGAALDLGRYTVGWG--------CVGILD 250
Cdd:cd01159 157 VVPR--AEYEIVDTWHVVGLRGTGSNTVVVDDVFVPEHRTLTAGDMMAGDGPGGSTPVYRMPLRQVfplsfaavSLGAAE 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2664202365 251 ACVEASVDYAAERHQ---FGSAIKDHQLVRRLITNMYTDARAARLLCLEAG-----------------RLRDRRDPGALA 310
Cdd:cd01159 235 GALAEFLELAGKRVRqygAAVKMAEAPITQLRLAEAAAELDAARAFLERATrdlwahalaggpidveeRARIRRDAAYAA 314
|
330 340 350 360
....*....|....*....|....*....|....*....|....*....
gi 2664202365 311 GTSTAkyfassaatraaadAVQI----HGANGCSSDFPVQRYLGDSRVM 355
Cdd:cd01159 315 KLSAE--------------AVDRlfhaAGGSALYTASPLQRIWRDIHAA 349
|
|
| PTZ00457 |
PTZ00457 |
acyl-CoA dehydrogenase; Provisional |
50-190 |
1.55e-05 |
|
acyl-CoA dehydrogenase; Provisional
Pssm-ID: 185636 [Multi-domain] Cd Length: 520 Bit Score: 46.80 E-value: 1.55e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2664202365 50 LLGLSVPEEYGGGGCDAVTLGLLAGELGRAC-SSLRSLLTVHTMVAHAIVRWGSRSLKEYWLPRLARGESIGALAVSEpD 128
Cdd:PTZ00457 65 LYGARIATEYGGLGLGHTAHALIYEEVGTNCdSKLLSTIQHSGFCTYLLSTVGSKELKGKYLTAMSDGTIMMGWATEE-G 143
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2664202365 129 VGSDAGSVTSRLT-RDGDDWVLDGHKKwTTYGETADVYLVVGR------SEEGPTAV------LVERGTEGLRTE 190
Cdd:PTZ00457 144 CGSDISMNTTKASlTDDGSYVLTGQKR-CEFAASATHFLVLAKtltqtaAEEGATEVsrnsffICAKDAKGVSVN 217
|
|
| Acyl-CoA_dh_2 |
pfam08028 |
Acyl-CoA dehydrogenase, C-terminal domain; |
245-354 |
5.54e-05 |
|
Acyl-CoA dehydrogenase, C-terminal domain;
Pssm-ID: 429790 [Multi-domain] Cd Length: 133 Bit Score: 42.72 E-value: 5.54e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2664202365 245 CVGILDACVEASVDYAAER--HQFGSAIKDHQLVRRLITNMYTDARAARLLCLEAG----RLRDRRDPGALAGT---STA 315
Cdd:pfam08028 6 ALGAARAALAEFTERARGRvrAYFGVPLAEDPATQLALAEAAARIDAARLLLERAAarieAAAAAGKPVTPALRaeaRRA 85
|
90 100 110
....*....|....*....|....*....|....*....
gi 2664202365 316 KYFASSAATRAAADAVQIHGANGCSSDFPVQRYLGDSRV 354
Cdd:pfam08028 86 AAFATELAVAAVDALFRAAGGSALFQDSPLQRIWRDIHA 124
|
|
| |
