|
Name |
Accession |
Description |
Interval |
E-value |
| CaiA |
COG1960 |
Acyl-CoA dehydrogenase related to the alkylation response protein AidB [Lipid transport and ... |
25-398 |
1.84e-121 |
|
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: 357.61 E-value: 1.84e-121
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2762263583 25 LELTDEQRTAQAGFADFARREILPHADRWDREEHLPGEVVRALADEGHLGAWAPREHGGAGLDPVTFGLLNEALGHACSS 104
Cdd:COG1960 3 FELTEEQRALRDEVREFAEEEIAPEAREWDREGEFPRELWRKLAELGLLGLTIPEEYGGLGLSLVELALVLEELARADAS 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2762263583 105 VRSLLTVHSMVIRAVTRWGGSRLRSRWLPPLASGTAVGAFALTEPEAGSDVASLRTAAEKTADGYRLTGGKRWITFGQAA 184
Cdd:COG1960 83 LALPVGVHNGAAEALLRFGTEEQKERYLPRLASGEWIGAFALTEPGAGSDAAALRTTAVRDGDGYVLNGQKTFITNAPVA 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2762263583 185 DVFLVFARCDD-----GPAAFLVERDAPGCTVEPVTGMLGTRAAMTAHLHFDGCAVPAEALVGRAGFGLnAVAADALETG 259
Cdd:COG1960 163 DVILVLARTDPaaghrGISLFLVPKDTPGVTVGRIEDKMGLRGSDTGELFFDDVRVPAENLLGEEGKGF-KIAMSTLNAG 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2762263583 260 RYSVAWGSAGLARACVEASARHAAAREQFGRPLAQHELVQRLITEMAVNTSAARLLCLRAGRLLHSADPQAVEAVwSAKY 339
Cdd:COG1960 242 RLGLAAQALGIAEAALELAVAYAREREQFGRPIADFQAVQHRLADMAAELEAARALVYRAAWLLDAGEDAALEAA-MAKL 320
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*....
gi 2762263583 340 FAARSAFRAAADAVQVHGARGCGPDTPVQRLLRDAKIMEIIEGTTEIQQTVIAQSVVRE 398
Cdd:COG1960 321 FATEAALEVADEALQIHGGYGYTREYPLERLYRDARILTIYEGTNEIQRLIIARRLLGR 379
|
|
| SCAD_SBCAD |
cd01158 |
Short chain acyl-CoA dehydrogenases and eukaryotic short/branched chain acyl-CoA ... |
29-397 |
8.85e-100 |
|
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: 301.88 E-value: 8.85e-100
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2762263583 29 DEQRTAQAGFADFARREILPHADRWDREEHLPGEVVRALADEGHLGAWAPREHGGAGLDPVTFGLLNEALGHACSSVRSL 108
Cdd:cd01158 1 EEHQMIRKTVRDFAEKEIAPLAAEMDEKGEFPREVIKEMAELGLMGIPIPEEYGGAGLDFLAYAIAIEELAKVDASVAVI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2762263583 109 LTVH-SMVIRAVTRWGGSRLRSRWLPPLASGTAVGAFALTEPEAGSDVASLRTAAEKTADGYRLTGGKRWITFGQAADVF 187
Cdd:cd01158 81 VSVHnSLGANPIIKFGTEEQKKKYLPPLATGEKIGAFALSEPGAGSDAAALKTTAKKDGDDYVLNGSKMWITNGGEADFY 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2762263583 188 LVFARCD-----DGPAAFLVERDAPGCTVEPVTGMLGTRAAMTAHLHFDGCAVPAEALVGRAGFGLnAVAADALETGRYS 262
Cdd:cd01158 161 IVFAVTDpskgyRGITAFIVERDTPGLSVGKKEDKLGIRGSSTTELIFEDVRVPKENILGEEGEGF-KIAMQTLDGGRIG 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2762263583 263 VAWGSAGLARACVEASARHAAAREQFGRPLAQHELVQRLITEMAVNTSAARLLCLRAGRLLHSADPQAVEAVwSAKYFAA 342
Cdd:cd01158 240 IAAQALGIAQAALDAAVDYAKERKQFGKPIADFQGIQFKLADMATEIEAARLLTYKAARLKDNGEPFIKEAA-MAKLFAS 318
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*
gi 2762263583 343 RSAFRAAADAVQVHGARGCGPDTPVQRLLRDAKIMEIIEGTTEIQQTVIAQSVVR 397
Cdd:cd01158 319 EVAMRVTTDAVQIFGGYGYTKDYPVERYYRDAKITEIYEGTSEIQRLVIAKHLLK 373
|
|
| IBD |
cd01162 |
Isobutyryl-CoA dehydrogenase; Isobutyryl-CoA dehydrogenase (IBD) catalyzes the alpha, beta- ... |
27-398 |
1.78e-85 |
|
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: 265.46 E-value: 1.78e-85
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2762263583 27 LTDEQRTAQAGFADFARREILPHADRWDREEHLPGEVVRALADEGHLGAWAPREHGGAGLDPVTFGLLNEALGHACSSVR 106
Cdd:cd01162 1 LNEEQRAIQEVARAFAAKEMAPHAADWDQKKHFPVDVLRKAAELGFGGIYIRDDVGGSGLSRLDASIIFEALSTGCVSTA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2762263583 107 SLLTVHSMVIRAVTRWGGSRLRSRWLPPLASGTAVGAFALTEPEAGSDVASLRTAAEKTADGYRLTGGKRWITFGQAADV 186
Cdd:cd01162 81 AYISIHNMCAWMIDSFGNDEQRERFLPDLCTMEKLASYCLTEPGSGSDAAALRTRAVREGDHYVLNGSKAFISGAGDSDV 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2762263583 187 FLVFARCD-DGP---AAFLVERDAPGCTVEPVTGMLGTRAAMTAHLHFDGCAVPAEALVGRAGFGLNaVAADALETGRYS 262
Cdd:cd01162 161 YVVMARTGgEGPkgiSCFVVEKGTPGLSFGANEKKMGWNAQPTRAVIFEDCRVPVENRLGGEGQGFG-IAMAGLNGGRLN 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2762263583 263 VAWGSAGLARACVEASARHAAAREQFGRPLAQHELVQRLITEMAVNTSAARLLCLRAGRLLHSADPQAVEAVWSAKYFAA 342
Cdd:cd01162 240 IASCSLGAAQAALDLARAYLEERKQFGKPLADFQALQFKLADMATELVASRLMVRRAASALDRGDPDAVKLCAMAKRFAT 319
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*.
gi 2762263583 343 RSAFRAAADAVQVHGARGCGPDTPVQRLLRDAKIMEIIEGTTEIQQTVIAQSVVRE 398
Cdd:cd01162 320 DECFDVANQALQLHGGYGYLKDYPVEQYVRDLRVHQILEGTNEIMRLIIARALLTR 375
|
|
| ACAD |
cd00567 |
Acyl-CoA dehydrogenase; Both mitochondrial acyl-CoA dehydrogenases (ACAD) and peroxisomal ... |
29-393 |
7.59e-81 |
|
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: 251.82 E-value: 7.59e-81
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2762263583 29 DEQRTAQAGFADFARREILPHADRWDREEHLPGEVVRALadeghlgawaprehggagldpvtfGLLnealghacssvrsl 108
Cdd:cd00567 1 EEQRELRDSAREFAAEELEPYARERRETPEEPWELLAEL------------------------GLL-------------- 42
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2762263583 109 ltvhsMVIRAVTRWGGSRLRSRWLPPLASGTAVGAFALTEPEAGSDVASLRTAAEKTADGYRLTGGKRWITFGQAADVFL 188
Cdd:cd00567 43 -----LGAALLLAYGTEEQKERYLPPLASGEAIAAFALTEPGAGSDLAGIRTTARKDGDGYVLNGRKIFISNGGDADLFI 117
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2762263583 189 VFARCDD------GPAAFLVERDAPGCTVEPVTGMLGTRAAMTAHLHFDGCAVPAEALVGRAGFGLNaVAADALETGRYS 262
Cdd:cd00567 118 VLARTDEegpghrGISAFLVPADTPGVTVGRIWDKMGMRGSGTGELVFDDVRVPEDNLLGEEGGGFE-LAMKGLNVGRLL 196
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2762263583 263 VAWGSAGLARACVEASARHAAAREQFGRPLAQHELVQRLITEMAVNTSAARLLCLRAGRLLHSADPQAVEAVWSAKYFAA 342
Cdd:cd00567 197 LAAVALGAARAALDEAVEYAKQRKQFGKPLAEFQAVQFKLADMAAELEAARLLLYRAAWLLDQGPDEARLEAAMAKLFAT 276
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|.
gi 2762263583 343 RSAFRAAADAVQVHGARGCGPDTPVQRLLRDAKIMEIIEGTTEIQQTVIAQ 393
Cdd:cd00567 277 EAAREVADLAMQIHGGRGYSREYPVERYLRDARAARIAEGTAEIQRLIIAR 327
|
|
| GCD |
cd01151 |
Glutaryl-CoA dehydrogenase; Glutaryl-CoA dehydrogenase (GCD). GCD is an acyl-CoA dehydrogenase, ... |
27-395 |
1.41e-79 |
|
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: 250.74 E-value: 1.41e-79
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2762263583 27 LTDEQRTAQAGFADFARREILPHADRWDREEHLPGEVVRALADEGHLGAwAPREHGGAGLDPVTFGLLNEALGHACSSVR 106
Cdd:cd01151 13 LTEEERAIRDTAREFCQEELAPRVLEAYREEKFDRKIIEEMGELGLLGA-TIKGYGCAGLSSVAYGLIAREVERVDSGYR 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2762263583 107 SLLTVH-SMVIRAVTRWGGSRLRSRWLPPLASGTAVGAFALTEPEAGSDVASLRTAAEKTADGYRLTGGKRWITFGQAAD 185
Cdd:cd01151 92 SFMSVQsSLVMLPIYDFGSEEQKQKYLPKLASGELIGCFGLTEPNHGSDPGGMETRARKDGGGYKLNGSKTWITNSPIAD 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2762263583 186 VFLVFARCD--DGPAAFLVERDAPGCTVEPVTGMLGTRAAMTAHLHFDGCAVPAEALVGRAGfGLNAVAAdALETGRYSV 263
Cdd:cd01151 172 VFVVWARNDetGKIRGFILERGMKGLSAPKIQGKFSLRASITGEIVMDNVFVPEENLLPGAE-GLRGPFK-CLNNARYGI 249
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2762263583 264 AWGSAGLARACVEASARHAAAREQFGRPLAQHELVQRLITEMAVNTSAARLLCLRAGRLLhSADPQAVEAVWSAKYFAAR 343
Cdd:cd01151 250 AWGALGAAEDCYHTARQYVLDRKQFGRPLAAFQLVQKKLADMLTEIALGLLACLRVGRLK-DQGKATPEQISLLKRNNCG 328
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|..
gi 2762263583 344 SAFRAAADAVQVHGARGCGPDTPVQRLLRDAKIMEIIEGTTEIQQTVIAQSV 395
Cdd:cd01151 329 KALEIARTAREMLGGNGISDEYHIIRHMVNLESVNTYEGTHDIHALILGRAI 380
|
|
| IVD |
cd01156 |
Isovaleryl-CoA dehydrogenase; Isovaleryl-CoA dehydrogenase (IVD) is an is an acyl-CoA ... |
27-397 |
1.59e-78 |
|
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: 247.71 E-value: 1.59e-78
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2762263583 27 LTDEQRTAQAGFADFARREILPHADRWDREEHLPGEVVRALADEGHLGAWAPREHGGAGLDPVTFGLLNEALGHACSSVR 106
Cdd:cd01156 2 LDDEIEMLRQSVREFAQKEIAPLAAKIDRDNEFPRDLWRKMGKLGLLGITAPEEYGGSGMGYLAHVIIMEEISRASGSVA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2762263583 107 SLLTVHS-MVIRAVTRWGGSRLRSRWLPPLASGTAVGAFALTEPEAGSDVASLRTAAEKTADGYRLTGGKRWITFGQAAD 185
Cdd:cd01156 82 LSYGAHSnLCINQIYRNGSAAQKEKYLPKLISGEHIGALAMSEPNAGSDVVSMKLRAEKKGDRYVLNGSKMWITNGPDAD 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2762263583 186 VFLVFARCD-----DGPAAFLVERDAPGCTVEPVTGMLGTRAAMTAHLHFDGCAVPAEALVGRAGFGLNaVAADALETGR 260
Cdd:cd01156 162 TLVVYAKTDpsagaHGITAFIVEKGMPGFSRAQKLDKLGMRGSNTCELVFEDCEVPEENILGGENKGVY-VLMSGLDYER 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2762263583 261 YSVAWGSAGLARACVEASARHAAAREQFGRPLAQHELVQRLITEMAVNTSAARLLCLRAGRLLHSADPQAVEAVWSAKYf 340
Cdd:cd01156 241 LVLAGGPIGIMQAALDVAIPYAHQRKQFGQPIGEFQLVQGKLADMYTRLNASRSYLYTVAKACDRGNMDPKDAAGVILY- 319
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*..
gi 2762263583 341 AARSAFRAAADAVQVHGARGCGPDTPVQRLLRDAKIMEIIEGTTEIQQTVIAQSVVR 397
Cdd:cd01156 320 AAEKATQVALDAIQILGGNGYINDYPTGRLLRDAKLYEIGAGTSEIRRMVIGRELFK 376
|
|
| VLCAD |
cd01161 |
Very long chain acyl-CoA dehydrogenase; VLCAD is an acyl-CoA dehydrogenase (ACAD), which is ... |
26-397 |
5.06e-68 |
|
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: 221.57 E-value: 5.06e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2762263583 26 ELTDEQRTAQAGFADFARREILPHadRWDREEHLPGEVVRALADEGHLGAWAPREHGGAGLDPVTFGLLNEALGHAcSSV 105
Cdd:cd01161 26 EQTEELNMLVGPVEKFFEEVNDPA--KNDQLEKIPRKTLTQLKELGLFGLQVPEEYGGLGLNNTQYARLAEIVGMD-LGF 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2762263583 106 RSLLTVHSMV-IRAVTRWGGSRLRSRWLPPLASGTAVGAFALTEPEAGSDVASLRTAAEKTADG--YRLTGGKRWITFGQ 182
Cdd:cd01161 103 SVTLGAHQSIgFKGILLFGTEAQKEKYLPKLASGEWIAAFALTEPSSGSDAASIRTTAVLSEDGkhYVLNGSKIWITNGG 182
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2762263583 183 AADVFLVFARCD---------DGPAAFLVERDAPGCTVEPVTGMLGTRAAMTAHLHFDGCAVPAEALVGRAGFGLNaVAA 253
Cdd:cd01161 183 IADIFTVFAKTEvkdatgsvkDKITAFIVERSFGGVTNGPPEKKMGIKGSNTAEVYFEDVKIPVENVLGEVGDGFK-VAM 261
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2762263583 254 DALETGRYSVAWGSAGLARACVEASARHAAAREQFGRPLAQHELVQRLITEMAVNTSAARLLCLRAGRLLHS---ADPQa 330
Cdd:cd01161 262 NILNNGRFGMGAALIGTMKRCIEKAVDYANNRKQFGKKIHEFGLIQEKLANMAILQYATESMAYMTSGNMDRglkAEYQ- 340
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2762263583 331 VEAVWSaKYFAARSAFRAAADAVQVHGARGCGPDTPVQRLLRDAKIMEIIEGTTEIQQTVIAQSVVR 397
Cdd:cd01161 341 IEAAIS-KVFASEAAWLVVDEAIQIHGGMGFMREYGVERVLRDLRIFRIFEGTNEILRLFIALTGLQ 406
|
|
| LCAD |
cd01160 |
Long chain acyl-CoA dehydrogenase; LCAD is an acyl-CoA dehydrogenases (ACAD), which is found ... |
41-396 |
6.87e-65 |
|
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: 211.98 E-value: 6.87e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2762263583 41 FARREILPHADRWDREEHLPGEVVRALADEGHLGAWAPREHGGAGLDPVTFGLLNEALGHACSSVRSLLTVHSMVIRAVT 120
Cdd:cd01160 13 FFAKEVAPFHHEWEKAGEVPREVWRKAGEQGLLGVGFPEEYGGIGGDLLSAAVLWEELARAGGSGPGLSLHTDIVSPYIT 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2762263583 121 RWGGSRLRSRWLPPLASGTAVGAFALTEPEAGSDVASLRTAAEKTADGYRLTGGKRWITFGQAADVFLVFARCD------ 194
Cdd:cd01160 93 RAGSPEQKERVLPQMVAGKKIGAIAMTEPGAGSDLQGIRTTARKDGDHYVLNGSKTFITNGMLADVVIVVARTGgearga 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2762263583 195 DGPAAFLVERDAPGCTVEPVTGMLGTRAAMTAHLHFDGCAVPAEALVGRAGFGLNAVAADaLETGRYSVAWGSAGLARAC 274
Cdd:cd01160 173 GGISLFLVERGTPGFSRGRKLKKMGWKAQDTAELFFDDCRVPAENLLGEENKGFYYLMQN-LPQERLLIAAGALAAAEFM 251
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2762263583 275 VEASARHAAAREQFGRPLAQHELVQRLITEMAVNTSAARLLCLRAGRlLHSADPQAVEAVWSAKYFAARSAFRAAADAVQ 354
Cdd:cd01160 252 LEETRNYVKQRKAFGKTLAQLQVVRHKIAELATKVAVTRAFLDNCAW-RHEQGRLDVAEASMAKYWATELQNRVAYECVQ 330
|
330 340 350 360
....*....|....*....|....*....|....*....|..
gi 2762263583 355 VHGARGCGPDTPVQRLLRDAKIMEIIEGTTEIQQTVIAQSVV 396
Cdd:cd01160 331 LHGGWGYMREYPIARAYRDARVQPIYGGTTEIMKELISRQMV 372
|
|
| MCAD |
cd01157 |
Medium chain acyl-CoA dehydrogenase; MCADs are mitochondrial beta-oxidation enzymes, which ... |
27-396 |
1.95e-64 |
|
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: 211.29 E-value: 1.95e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2762263583 27 LTDEQRTAQAGFADFARREILPHADRWDREEHLPGEVVRALADEGHLGAWAPREHGGAGLDPVTFGLLNEALGHACSSVR 106
Cdd:cd01157 1 LTEQQKEFQETARKFAREEIIPVAAEYDKSGEYPWPLIKRAWELGLMNTHIPEDCGGLGLGTFDTCLITEELAYGCTGVQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2762263583 107 SLLTVHSMVIRAVTRWGGSRLRSRWLPPLASGTAVGAFALTEPEAGSDVASLRTAAEKTADGYRLTGGKRWITFGQAADV 186
Cdd:cd01157 81 TAIEANSLGQMPVIISGNDEQKKKYLGRMTEEPLMCAYCVTEPGAGSDVAGIKTKAEKKGDEYIINGQKMWITNGGKANW 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2762263583 187 FLVFARCDDGP--------AAFLVERDAPGCTVEPVTGMLGTRAAMTAHLHFDGCAVPAEALVGRAGFGLNaVAADALET 258
Cdd:cd01157 161 YFLLARSDPDPkcpaskafTGFIVEADTPGIQPGRKELNMGQRCSDTRGITFEDVRVPKENVLIGEGAGFK-IAMGAFDK 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2762263583 259 GRYSVAWGSAGLARACVEASARHAAAREQFGRPLAQHELVQRLITEMAVNTSAARLLCLRAGRLLHSADPQAVEAVwSAK 338
Cdd:cd01157 240 TRPPVAAGAVGLAQRALDEATKYALERKTFGKLIAEHQAVSFMLADMAMKVELARLAYQRAAWEVDSGRRNTYYAS-IAK 318
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*...
gi 2762263583 339 YFAARSAFRAAADAVQVHGARGCGPDTPVQRLLRDAKIMEIIEGTTEIQQTVIAQSVV 396
Cdd:cd01157 319 AFAADIANQLATDAVQIFGGNGFNSEYPVEKLMRDAKIYQIYEGTSQIQRLIISREHL 376
|
|
| PTZ00461 |
PTZ00461 |
isovaleryl-CoA dehydrogenase; Provisional |
28-399 |
3.00e-62 |
|
isovaleryl-CoA dehydrogenase; Provisional
Pssm-ID: 185640 [Multi-domain] Cd Length: 410 Bit Score: 206.33 E-value: 3.00e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2762263583 28 TDEQRTAQAGFADFARREILPHADRWDREEHLPGEVVRALADEGHLGAWAPREHGGAGLDPVTFGLLNEALGHACSSVRS 107
Cdd:PTZ00461 38 TPEHAALRETVAKFSREVVDKHAREDDINMHFNRDLFKQLGDLGVMGVTVPEADGGAGMDAVAAVIIHHELSKYDPGFCL 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2762263583 108 LLTVHSMVIRAVTRWGGSRL-RSRWLPPLASGTAVGAFALTEPEAGSDVASLRTAAEKTADG-YRLTGGKRWITFGQAAD 185
Cdd:PTZ00461 118 AYLAHSMLFVNNFYYSASPAqRARWLPKVLTGEHVGAMGMSEPGAGTDVLGMRTTAKKDSNGnYVLNGSKIWITNGTVAD 197
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2762263583 186 VFLVFARCDDGPAAFLVERDAPGCTVEPVTGMLGTRAAMTAHLHFDGCAVPAEALVGRAGFGLNAVAADaLETGRYSVAW 265
Cdd:PTZ00461 198 VFLIYAKVDGKITAFVVERGTKGFTQGPKIDKCGMRASHMCQLFFEDVVVPAENLLGEEGKGMVGMMRN-LELERVTLAA 276
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2762263583 266 GSAGLARACVEASARHAAAREQFGRPLAQHELVQRLITEMAVNTSAARLLCLRAGRLLHSADPQAVEAVwSAKYFAARSA 345
Cdd:PTZ00461 277 MAVGIAERSVELMTSYASERKAFGKPISNFGQIQRYIAEGYADTEAAKALVYSVSHNVHPGNKNRLGSD-AAKLFATPIA 355
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....
gi 2762263583 346 FRAAADAVQVHGARGCGPDTPVQRLLRDAKIMEIIEGTTEIQQTVIAQSVVREL 399
Cdd:PTZ00461 356 KKVADSAIQVMGGMGYSRDMPVERLWRDAKLLEIGGGTIEAHHKNITKDLLKGL 409
|
|
| PLN02519 |
PLN02519 |
isovaleryl-CoA dehydrogenase |
22-398 |
3.79e-56 |
|
isovaleryl-CoA dehydrogenase
Pssm-ID: 215284 [Multi-domain] Cd Length: 404 Bit Score: 190.09 E-value: 3.79e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2762263583 22 TEGLELTDEQRTAQAGFADFARREILPHADRWDREEHLPGEV--VRALADEGHLGAWAPREHGGAGLDPVTFGLLNEALG 99
Cdd:PLN02519 21 SSSLLFDDTQLQFKESVQQFAQENIAPHAAAIDATNSFPKDVnlWKLMGDFNLHGITAPEEYGGLGLGYLYHCIAMEEIS 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2762263583 100 HACSSVRSLLTVHS-MVIRAVTRWGGSRLRSRWLPPLASGTAVGAFALTEPEAGSDVASLRTAAEKTADGYRLTGGKRWI 178
Cdd:PLN02519 101 RASGSVGLSYGAHSnLCINQLVRNGTPAQKEKYLPKLISGEHVGALAMSEPNSGSDVVSMKCKAERVDGGYVLNGNKMWC 180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2762263583 179 TFGQAADVFLVFARCD-----DGPAAFLVERDAPGCTVEPVTGMLGTRAAMTAHLHFDGCAVPAEALVGRAGFGLnAVAA 253
Cdd:PLN02519 181 TNGPVAQTLVVYAKTDvaagsKGITAFIIEKGMPGFSTAQKLDKLGMRGSDTCELVFENCFVPEENVLGQEGKGV-YVMM 259
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2762263583 254 DALETGRYSVAWGSAGLARACVEASARHAAAREQFGRPLAQHELVQRLITEMAVNTSAARLLCLRAGRLLHS--ADPQAV 331
Cdd:PLN02519 260 SGLDLERLVLAAGPLGLMQACLDVVLPYVRQREQFGRPIGEFQFIQGKLADMYTSLQSSRSYVYSVARDCDNgkVDRKDC 339
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2762263583 332 EAV--WSAKyfaarSAFRAAADAVQVHGARGCGPDTPVQRLLRDAKIMEIIEGTTEIQQTVIAQSVVRE 398
Cdd:PLN02519 340 AGVilCAAE-----RATQVALQAIQCLGGNGYINEYPTGRLLRDAKLYEIGAGTSEIRRMLIGRELFKE 403
|
|
| PRK12341 |
PRK12341 |
acyl-CoA dehydrogenase; |
27-386 |
7.79e-38 |
|
acyl-CoA dehydrogenase;
Pssm-ID: 183454 [Multi-domain] Cd Length: 381 Bit Score: 141.02 E-value: 7.79e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2762263583 27 LTDEQRTAQAGFADFARREIlPHAD--RWDREEHLPGEVVRALADEGH--LGAwaPREHGGAGLDPVTFGLLNEALGHAC 102
Cdd:PRK12341 5 LTEEQELLLASIRELITRNF-PEEYfrTCDENGTYPREFMRALADNGIsmLGV--PEEFGGTPADYVTQMLVLEEVSKCG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2762263583 103 SSVrsLLTVHSMVIRAVTRWGGSR-LRSRWLPPLASGTAVGAFALTEPEAGSDVASLRTAAEKTADGYRLTGGKRWITFG 181
Cdd:PRK12341 82 APA--FLITNGQCIHSMRRFGSAEqLRKTAESTLETGDPAYALALTEPGAGSDNNSATTTYTRKNGKVYLNGQKTFITGA 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2762263583 182 QAADVFLVFARCDDGPA---AF---LVERDAPGCTVEPVtGMLGTRAAMTAHLHFDGCAVPAEALVGRAGFGLNAVAADa 255
Cdd:PRK12341 160 KEYPYMLVLARDPQPKDpkkAFtlwWVDSSKPGIKINPL-HKIGWHMLSTCEVYLDNVEVEESDLVGEEGMGFLNVMYN- 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2762263583 256 LETGRYSVAWGSAGLARACVEASARHAAAREQFGRPLAQHELVQRLITEMAVNTSAARLLCLRAGRLLHSADPQAVEAVw 335
Cdd:PRK12341 238 FEMERLINAARSLGFAECAFEDAARYANQRIQFGKPIGHNQLIQEKLTLMAIKIENMRNMVYKVAWQADNGQSLRTSAA- 316
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|.
gi 2762263583 336 SAKYFAARSAFRAAADAVQVHGARGCGPDTPVQRLLRDAKIMEIIEGTTEI 386
Cdd:PRK12341 317 LAKLYCARTAMEVIDDAIQIMGGLGYTDEARVSRFWRDVRCERIGGGTDEI 367
|
|
| AidB |
cd01154 |
Proteins involved in DNA damage response, similar to the AidB gene product; AidB is one of ... |
39-387 |
1.47e-37 |
|
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: 140.97 E-value: 1.47e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2762263583 39 ADFARRE--ILPHADRW----DREEHLPG--EVVRALADEG-HLGAWAPREHGGAGLDPVTFGLLNEAL-GHACSsvrsl 108
Cdd:cd01154 38 ARLADRNppVLEMWDRWgrrvDRVWVHPAwhALMRRLIEEGvINIEDGPAGEGRRHVHFAAGYLLSDAAaGLLCP----- 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2762263583 109 LTVHSMVIRAVTRWGGSRLRsRWLPPLASGTA----VGAFALTEPEAGSDVASLRTAAEKTADG-YRLTGGKrWITFGQA 183
Cdd:cd01154 113 LTMTDAAVYALRKYGPEELK-QYLPGLLSDRYktglLGGTWMTEKQGGSDLGANETTAERSGGGvYRLNGHK-WFASAPL 190
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2762263583 184 ADVFLVFARCDDGPAA------FLVERDAPGCT-----VEPVTGMLGTRAAMTAHLHFDGcavpAEA-LVGRAGFGLnAV 251
Cdd:cd01154 191 ADAALVLARPEGAPAGarglslFLVPRLLEDGTrngyrIRRLKDKLGTRSVATGEVEFDD----AEAyLIGDEGKGI-YY 265
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2762263583 252 AADALETGRYSVAWGSAGLARACVEASARHAAAREQFGRPLAQHELVQRLITEMAVNTSAARLLCLRAGRLLH-SADPQA 330
Cdd:cd01154 266 ILEMLNISRLDNAVAALGIMRRALSEAYHYARHRRAFGKPLIDHPLMRRDLAEMEVDVEAATALTFRAARAFDrAAADKP 345
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2762263583 331 VEAVWS------AKYFAARSAFRAAADAVQVHGARGCGPDTPVQRLLRDAKIMEIIEGTTEIQ 387
Cdd:cd01154 346 VEAHMArlatpvAKLIACKRAAPVTSEAMEVFGGNGYLEEWPVARLHREAQVTPIWEGTGNIQ 408
|
|
| ACAD_fadE5 |
cd01153 |
Putative acyl-CoA dehydrogenases similar to fadE5; Putative acyl-CoA dehydrogenase (ACAD). ... |
39-387 |
2.00e-37 |
|
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: 140.22 E-value: 2.00e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2762263583 39 ADFARREILPHADRWDREE--------HLPGEV---VRALADEGHLGAWAPREHGGAGLDPVTFGLLNEALGHACSSVRS 107
Cdd:cd01153 6 ARLAENVLAPLNADGDREGpvfddgrvVVPPPFkeaLDAFAEAGWMALGVPEEYGGQGLPITVYSALAEIFSRGDAPLMY 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2762263583 108 LLTVHSmVIRAVTRWGGSRLRSRWLPPLASGTAVGAFALTEPEAGSDVASLRTAAEKTADG-YRLTGGKRWITFGQAAD- 185
Cdd:cd01153 86 ASGTQG-AAATLLAHGTEAQREKWIPRLAEGEWTGTMCLTEPDAGSDLGALRTKAVYQADGsWRINGVKRFISAGEHDMs 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2762263583 186 ---VFLVFARCDDGPAA-----------FLVERDAPGCTVEPVTGMLGTRAAMTAHLHFDGCAVPaeaLVGRAGFGLNAV 251
Cdd:cd01153 165 eniVHLVLARSEGAPPGvkglslflvpkFLDDGERNGVTVARIEEKMGLHGSPTCELVFDNAKGE---LIGEEGMGLAQM 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2762263583 252 AAdALETGRYSVAWGSAGLARACVEASARHAAAREQFGRPL--------AQHELVQRLITEMAVNTSAARLLCLRAGRLL 323
Cdd:cd01153 242 FA-MMNGARLGVGTQGTGLAEAAYLNALAYAKERKQGGDLIkaapavtiIHHPDVRRSLMTQKAYAEGSRALDLYTATVQ 320
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2762263583 324 HSADPQAVE----AVWSA---------KYFAARSAFRAAADAVQVHGARGCGPDTPVQRLLRDAKIMEIIEGTTEIQ 387
Cdd:cd01153 321 DLAERKATEgedrKALSAladlltpvvKGFGSEAALEAVSDAIQVHGGSGYTREYPIEQYYRDARITTIYEGTTGIQ 397
|
|
| PRK03354 |
PRK03354 |
crotonobetainyl-CoA dehydrogenase; Validated |
27-398 |
1.76e-34 |
|
crotonobetainyl-CoA dehydrogenase; Validated
Pssm-ID: 179566 [Multi-domain] Cd Length: 380 Bit Score: 131.88 E-value: 1.76e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2762263583 27 LTDEQRTAQAGFADFARREilphadRW-------DREEHLPGEVVRALADEGHLGAWAPREHGGAGLDPVTFGLLNEALG 99
Cdd:PRK03354 5 LNDEQELFVAGIRELMASE------NWeayfaecDRDSVYPERFVKALADMGIDSLLIPEEHGGLDAGFVTLAAVWMELG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2762263583 100 HACSSVRSLLTVhSMVIRAVTRWGGSRLRSRWLPPLASGTAVGAFALTEPEAGSDVASLRTAAEKTADGYRLTGGKRWIT 179
Cdd:PRK03354 79 RLGAPTYVLYQL-PGGFNTFLREGTQEQIDKIMAFRGTGKQMWNSAITEPGAGSDVGSLKTTYTRRNGKVYLNGSKCFIT 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2762263583 180 FGQAADVFLVFARCDDGP-----AAFLVERDAPGCTVEPVTgMLGTRAAMTAHLHFDGCAVPAEALVGRAGFGLNAVAAD 254
Cdd:PRK03354 158 SSAYTPYIVVMARDGASPdkpvyTEWFVDMSKPGIKVTKLE-KLGLRMDSCCEITFDDVELDEKDMFGREGNGFNRVKEE 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2762263583 255 aLETGRYSVAWGSAGLARACVEASARHAAAREQFGRPLAQHELVQRLITEMAVNTSAARLLCLRAG-----RLLHSADPQ 329
Cdd:PRK03354 237 -FDHERFLVALTNYGTAMCAFEDAARYANQRVQFGEAIGRFQLIQEKFAHMAIKLNSMKNMLYEAAwkadnGTITSGDAA 315
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2762263583 330 AveavwsAKYFAARSAFRAAADAVQVHGARGCGPDTPVQRLLRDAKIMEIIEGTTEIQQTVIAQSVVRE 398
Cdd:PRK03354 316 M------CKYFCANAAFEVVDSAMQVLGGVGIAGNHRISRFWRDLRVDRVSGGSDEMQILTLGRAVLKQ 378
|
|
| ACAD_FadE2 |
cd01155 |
Acyl-CoA dehydrogenases similar to fadE2; FadE2-like Acyl-CoA dehydrogenase (ACAD). Acyl-CoA ... |
39-392 |
2.62e-33 |
|
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: 128.66 E-value: 2.62e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2762263583 39 ADFARREILP----------HADRWDREEHLPGEVVRALA-DEGHLGAWAPREHGGAGLDPVTFGLLNEALGHA------ 101
Cdd:cd01155 11 KAFMEEHVYPaeqefleyyaEGGDRWWTPPPIIEKLKAKAkAEGLWNLFLPEVSGLSGLTNLEYAYLAEETGRSffapev 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2762263583 102 --CSSVRSlltvHSMVIRAvtRWGGSRLRSRWLPPLASGTAVGAFALTEPE-AGSDVASLRTAAEKTADGYRLTGGKRWI 178
Cdd:cd01155 91 fnCQAPDT----GNMEVLH--RYGSEEQKKQWLEPLLDGKIRSAFAMTEPDvASSDATNIECSIERDGDDYVINGRKWWS 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2762263583 179 TfgQAAD----VFLVFARCDDGPAA-------FLVERDAPGCTVEPVTGMLGTRAAMTAH--LHFDGCAVPAEALVGRAG 245
Cdd:cd01155 165 S--GAGDprckIAIVMGRTDPDGAPrhrqqsmILVPMDTPGVTIIRPLSVFGYDDAPHGHaeITFDNVRVPASNLILGEG 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2762263583 246 FGLnAVAADALETGRYSVAWGSAGLARACVEASARHAAAREQFGRPLAQHELVQRLITEMAVNTSAARLLCLRAGRLLHS 325
Cdd:cd01155 243 RGF-EIAQGRLGPGRIHHCMRLIGAAERALELMCQRAVSREAFGKKLAQHGVVAHWIAKSRIEIEQARLLVLKAAHMIDT 321
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2762263583 326 ADPQAVEA-VWSAKYFAARSAFRAAADAVQVHGARGCGPDTPVQRLLRDAKIMEIIEGTTEIQQTVIA 392
Cdd:cd01155 322 VGNKAARKeIAMIKVAAPRMALKIIDRAIQVHGAAGVSQDTPLANMYAWARTLRIADGPDEVHLRSIA 389
|
|
| PLN02526 |
PLN02526 |
acyl-coenzyme A oxidase |
27-412 |
4.05e-33 |
|
acyl-coenzyme A oxidase
Pssm-ID: 178141 [Multi-domain] Cd Length: 412 Bit Score: 128.82 E-value: 4.05e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2762263583 27 LTDEQRTAQAGFADFARREILP-HADRWDREEhLPGEVVRALADEGHLGAwAPREHGGAGLDPVTFGLLNEALGHACSSV 105
Cdd:PLN02526 29 LTPEEQALRKRVRECMEKEVAPiMTEYWEKAE-FPFHIIPKLGSLGIAGG-TIKGYGCPGLSITASAIATAEVARVDASC 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2762263583 106 RSLLTVHS-MVIRAVTRWGGSRLRSRWLPPLASGTAVGAFALTEPEAGSDVASLRTAAEKTADGYRLTGGKRWITFGQAA 184
Cdd:PLN02526 107 STFILVHSsLAMLTIALCGSEAQKQKYLPSLAQLDTVACWALTEPDYGSDASSLNTTATKVEGGWILNGQKRWIGNSTFA 186
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2762263583 185 DVFLVFARCDDGPA--AFLVERDAPGCTVEPVTGMLGTRAAMTAHLHFDGCAVPAEALVGragfGLNAVA--ADALETGR 260
Cdd:PLN02526 187 DVLVIFARNTTTNQinGFIVKKGAPGLKATKIENKIGLRMVQNGDIVLKDVFVPDEDRLP----GVNSFQdtNKVLAVSR 262
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2762263583 261 YSVAWGSAGLARACVEASARHAAAREQFGRPLAQHELVQRLITEMAVNTSAARLLCLRAGRLLHSADPQAVEAVWsAKYF 340
Cdd:PLN02526 263 VMVAWQPIGISMGVYDMCHRYLKERKQFGAPLAAFQINQEKLVRMLGNIQAMFLVGWRLCKLYESGKMTPGHASL-GKAW 341
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2762263583 341 AARSAFRAAADAVQVHGARGCGPDTPVQRLLRDAKIMEIIEGTTEIQQTVIAqsvvRELAGPAGLSAPAQNR 412
Cdd:PLN02526 342 ITKKARETVALGRELLGGNGILADFLVAKAFCDLEPIYTYEGTYDINALVTG----REITGIASFKPAASTR 409
|
|
| ACAD_fadE6_17_26 |
cd01152 |
Putative acyl-CoA dehydrogenases similar to fadE6, fadE17, and fadE26; Putative acyl-CoA ... |
43-395 |
1.94e-31 |
|
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: 123.23 E-value: 1.94e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2762263583 43 RREILPHADRWDREEHLPGEvvRALADEGHLGAWAPREHGGAGLDPVTFGLLNEALGHACSSVRSLLTVHSMVIRAVTRW 122
Cdd:cd01152 22 LREESALGYREGREDRRRWQ--RALAAAGWAAPGWPKEYGGRGASLMEQLIFREEMAAAGAPVPFNQIGIDLAGPTILAY 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2762263583 123 GGSRLRSRWLPPLASGTAVGAFALTEPEAGSDVASLRTAAEKTADGYRLTGGKRWITFGQAADVFLVFARCD------DG 196
Cdd:cd01152 100 GTDEQKRRFLPPILSGEEIWCQGFSEPGAGSDLAGLRTRAVRDGDDWVVNGQKIWTSGAHYADWAWLLVRTDpeapkhRG 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2762263583 197 PAAFLVERDAPGCTVEPVTGMLGtrAAMTAHLHFDGCAVPAEALVGRAGFGLnAVAADALETGRYSVAWGSAGLARACVE 276
Cdd:cd01152 180 ISILLVDMDSPGVTVRPIRSING--GEFFNEVFLDDVRVPDANRVGEVNDGW-KVAMTTLNFERVSIGGSAATFFELLLA 256
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2762263583 277 ASARHAAAreqfGRPLAQHELVQRLITEMAVNTSAARLLCLRAGRLLHSADPQAVEAVwSAKYFAARSAFRAAADAVQVH 356
Cdd:cd01152 257 RLLLLTRD----GRPLIDDPLVRQRLARLEAEAEALRLLVFRLASALAAGKPPGAEAS-IAKLFGSELAQELAELALELL 331
|
330 340 350 360
....*....|....*....|....*....|....*....|....*..
gi 2762263583 357 GARGCGPDTP--------VQRLLRDAKIMEIIEGTTEIQQTVIAQSV 395
Cdd:cd01152 332 GTAALLRDPApgaelagrWEADYLRSRATTIYGGTSEIQRNIIAERL 378
|
|
| Acyl-CoA_dh_1 |
pfam00441 |
Acyl-CoA dehydrogenase, C-terminal domain; C-terminal domain of Acyl-CoA dehydrogenase is an ... |
250-395 |
3.16e-30 |
|
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: 113.89 E-value: 3.16e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2762263583 250 AVAADALETGRYSVAWGSAGLARACVEASARHAAAREQFGRPLAQHELVQRLITEMAVNTSAARLLCLRAGRLLHSADPQ 329
Cdd:pfam00441 5 RVAMETLNHERLAIAAMALGLARRALDEALAYARRRKAFGRPLIDFQLVRHKLAEMAAEIEAARLLVYRAAEALDAGGPD 84
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2762263583 330 AVEAVwSAKYFAARSAFRAAADAVQVHGARGCGPDTPVQRLLRDAKIMEIIEGTTEIQQTVIAQSV 395
Cdd:pfam00441 85 GAEAS-MAKLYASEAAVEVADLAMQLHGGYGYLREYPVERLYRDARVLRIGEGTSEIQRNIIARRL 149
|
|
| Acyl-CoA_dh_N |
pfam02771 |
Acyl-CoA dehydrogenase, N-terminal domain; The N-terminal domain of Acyl-CoA dehydrogenase is ... |
28-138 |
7.43e-30 |
|
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: 111.79 E-value: 7.43e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2762263583 28 TDEQRTAQAGFADFARREILPHADRWDREEHLPGEVVRALADEGHLGAWAPREHGGAGLDPVTFGLLNEALGHACSSVRS 107
Cdd:pfam02771 1 TEEQEALRDTVREFAEEEIAPHAAEWDEEGEFPRELWKKLGELGLLGITIPEEYGGAGLDYLAYALVAEELARADASVAL 80
|
90 100 110
....*....|....*....|....*....|..
gi 2762263583 108 LLTVHS-MVIRAVTRWGGSRLRSRWLPPLASG 138
Cdd:pfam02771 81 ALSVHSsLGAPPILRFGTEEQKERYLPKLASG 112
|
|
| Acyl-CoA_dh_M |
pfam02770 |
Acyl-CoA dehydrogenase, middle domain; Central domain of Acyl-CoA dehydrogenase has a ... |
143-231 |
1.36e-22 |
|
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: 91.19 E-value: 1.36e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2762263583 143 AFALTEPEAGSDVASLRT-AAEKTADGYRLTGGKRWITFGQAADVFLVFAR-----CDDGPAAFLVERDAPGCTVEPVTG 216
Cdd:pfam02770 1 AFALTEPGAGSDVASLKTtAADGDGGGWVLNGTKWWITNAGIADLFLVLARtggddRHGGISLFLVPKDAPGVSVRRIET 80
|
90
....*....|....*
gi 2762263583 217 MLGTRAAMTAHLHFD 231
Cdd:pfam02770 81 KLGVRGLPTGELVFD 95
|
|
| PTZ00456 |
PTZ00456 |
acyl-CoA dehydrogenase; Provisional |
62-387 |
1.12e-16 |
|
acyl-CoA dehydrogenase; Provisional
Pssm-ID: 185635 [Multi-domain] Cd Length: 622 Bit Score: 82.22 E-value: 1.12e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2762263583 62 EVVRALADEGHLGAWAPREHGGAGLdPVTFGLLNEALGHACSSVRSLLTVHSM-VIRAVTRWGGSRLRSRWLPPLASGTA 140
Cdd:PTZ00456 103 EAYQALKAGGWTGISEPEEYGGQAL-PLSVGFITRELMATANWGFSMYPGLSIgAANTLMAWGSEEQKEQYLTKLVSGEW 181
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2762263583 141 VGAFALTEPEAGSDVASLRTAAEKTADG-YRLTGGKRWITFGQ----AADVFLVFARCDDGPAA------FLVERDAPG- 208
Cdd:PTZ00456 182 SGTMCLTEPQCGTDLGQVKTKAEPSADGsYKITGTKIFISAGDhdltENIVHIVLARLPNSLPTtkglslFLVPRHVVKp 261
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2762263583 209 -----------CT-VEPVTGMLGTRaamTAHLHFDGcavPAEALVGRAGFGLNAVAAdALETGRYSVAWGSAGLARACVE 276
Cdd:PTZ00456 262 dgsletaknvkCIgLEKKMGIKGSS---TCQLSFEN---SVGYLIGEPNAGMKQMFT-FMNTARVGTALEGVCHAELAFQ 334
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2762263583 277 ASARHAAAR------------EQFGRPLAQHELVQRLITEMAVNTSAARLLCLRAGRLL---HSA-DPQAVEAVWS---- 336
Cdd:PTZ00456 335 NALRYARERrsmralsgtkepEKPADRIICHANVRQNILFAKAVAEGGRALLLDVGRLLdihAAAkDAATREALDHeigf 414
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*
gi 2762263583 337 ----AKYFAARSAFRAAADAVQVHGARGCGPDTPVQRLLRDAKIMEIIEGTTEIQ 387
Cdd:PTZ00456 415 ytpiAKGCLTEWGVEAASRCLQVWGGHGYIKGNGMEQILRDARIGTLYEGTTGIQ 469
|
|
| PRK13026 |
PRK13026 |
acyl-CoA dehydrogenase; Reviewed |
26-339 |
1.67e-16 |
|
acyl-CoA dehydrogenase; Reviewed
Pssm-ID: 237277 [Multi-domain] Cd Length: 774 Bit Score: 81.54 E-value: 1.67e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2762263583 26 ELTDEQrtaQAgFADFARREILPHADRWD---REEHLPGEVVRALADEGHLGAWAPREHGGAGLDPvtfgllnealgHAC 102
Cdd:PRK13026 77 TLTAEE---QA-FIDNEVETLLTMLDDWDivqNRKDLPPEVWDYLKKEGFFALIIPKEYGGKGFSA-----------YAN 141
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2762263583 103 SSVRSLLTVHSMVIrAVT--------------RWGGSRLRSRWLPPLASGTAVGAFALTEPEAGSDVASLRTAA---EKT 165
Cdd:PRK13026 142 STIVSKIATRSVSA-AVTvmvpnslgpgelltHYGTQEQKDYWLPRLADGTEIPCFALTGPEAGSDAGAIPDTGivcRGE 220
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2762263583 166 AD-----GYRLTGGKRWITFGQAADVF-LVF----------ARCDDGPAAFLVERDAPGctVEpvtgmLGTR------AA 223
Cdd:PRK13026 221 FEgeevlGLRLTWDKRYITLAPVATVLgLAFklrdpdgllgDKKELGITCALIPTDHPG--VE-----IGRRhnplgmAF 293
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2762263583 224 MTAHLHFDGCAVPAEALVG---RAGFGLNAVaADALETGR-YSVAWGSAGLARACVEASARHAAAREQFGRPLAQHELVQ 299
Cdd:PRK13026 294 MNGTTRGKDVFIPLDWIIGgpdYAGRGWRML-VECLSAGRgISLPALGTASGHMATRTTGAYAYVRRQFGMPIGQFEGVQ 372
|
330 340 350 360
....*....|....*....|....*....|....*....|...
gi 2762263583 300 RLITEMAVNT---SAARLLCLRAGRLLHSadPQAVEAVwsAKY 339
Cdd:PRK13026 373 EALARIAGNTyllEAARRLTTTGLDLGVK--PSVVTAI--AKY 411
|
|
| PRK11561 |
PRK11561 |
isovaleryl CoA dehydrogenase; Provisional |
131-412 |
2.31e-15 |
|
isovaleryl CoA dehydrogenase; Provisional
Pssm-ID: 183199 [Multi-domain] Cd Length: 538 Bit Score: 77.87 E-value: 2.31e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2762263583 131 WLPPLAS--------------GTAVGaFALTEPEAGSDVASLRTAAEKTADG-YRLTGGKRWITFGQaADVFLVFARCDD 195
Cdd:PRK11561 156 WLTPLLSdrydshllpggqkrGLLIG-MGMTEKQGGSDVLSNTTRAERLADGsYRLVGHKWFFSVPQ-SDAHLVLAQAKG 233
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2762263583 196 GPAAFLVERDAPGCT-----VEPVTGMLGTRAAMTAHLHFDgcavpaEA---LVGRAGFGLNAVaadaLETG---RYSVA 264
Cdd:PRK11561 234 GLSCFFVPRFLPDGQrnairLERLKDKLGNRSNASSEVEFQ------DAigwLLGEEGEGIRLI----LKMGgmtRFDCA 303
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2762263583 265 WGSAGLARACVEASARHAAAREQFGRPLAQHELVQRLITEMAVNTSAARLLCLRAGRLL-HSADPQavEAVWS------A 337
Cdd:PRK11561 304 LGSHGLMRRAFSVAIYHAHQRQVFGKPLIEQPLMRQVLSRMALQLEGQTALLFRLARAWdRRADAK--EALWArlftpaA 381
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2762263583 338 KYFAARSAFRAAADAVQVHGARGCGPDTPVQRLLRDAKIMEIIEGTTEIQ-----QTVIAQSVVRELAGPAGLSAPAQNR 412
Cdd:PRK11561 382 KFVICKRGIPFVAEAMEVLGGIGYCEESELPRLYREMPVNSIWEGSGNIMcldvlRVLNKQPGVYDLLSEAFVEVKGQDR 461
|
|
| DszC |
cd01163 |
Dibenzothiophene (DBT) desulfurization enzyme C; DszC is a flavin reductase dependent enzyme, ... |
38-326 |
4.54e-14 |
|
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: 73.13 E-value: 4.54e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2762263583 38 FADFARReILPHADRWDREEHLPGEVVRALADEGHLGAWAPREHGGAGLDPVTFGLLNEALGHACSSVRSLLTVHSMVIR 117
Cdd:cd01163 3 ARPLAAR-IAEGAAERDRQRGLPYEEVALLRQSGLGTLRVPKEYGGLGASLPDLYEVVRELAAADSNIAQALRAHFGFVE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2762263583 118 AVTRWGGSRLRSRWLPPLASGTAVGAfALTEpEAGSDVASLRTAAEKTADGYRLTGGKRWITFGQAADVFLVFARCDDGP 197
Cdd:cd01163 82 ALLLAGPEQFRKRWFGRVLNGWIFGN-AVSE-RGSVRPGTFLTATVRDGGGYVLNGKKFYSTGALFSDWVTVSALDEEGK 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2762263583 198 AAF-LVERDAPGCTVEPVTGMLGTRAAMTAHLHFDGCAVPAEALVGRAgfglNAVAADALETGRYSVAWGS--AGLARAC 274
Cdd:cd01163 160 LVFaAVPTDRPGITVVDDWDGFGQRLTASGTVTFDNVRVEPDEVLPRP----NAPDRGTLLTAIYQLVLAAvlAGIARAA 235
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*..
gi 2762263583 275 VEASARHAAAREQ-FGRPLAQHE----LVQRLITEMAVNTSAARLLCLRAGRLLHSA 326
Cdd:cd01163 236 LDDAVAYVRSRTRpWIHSGAESArddpYVQQVVGDLAARLHAAEALVLQAARALDAA 292
|
|
| fadE |
PRK09463 |
acyl-CoA dehydrogenase; Reviewed |
50-319 |
6.88e-14 |
|
acyl-CoA dehydrogenase; Reviewed
Pssm-ID: 236528 [Multi-domain] Cd Length: 777 Bit Score: 73.70 E-value: 6.88e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2762263583 50 ADRWD---REEHLPGEVVRALADEGHLGAWAPREHGGAGLdpvtfgllnEALGHAC-----SSVRSLLTVHSMVIRAV-- 119
Cdd:PRK09463 98 VNDWQithELADLPPEVWQFIKEHGFFGMIIPKEYGGLEF---------SAYAHSRvlqklASRSGTLAVTVMVPNSLgp 168
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2762263583 120 ----TRWGGSRLRSRWLPPLASGTAVGAFALTEPEAGSDVASLRTAAE--------KTADGYRLTGGKRWITFGQAADVF 187
Cdd:PRK09463 169 gellLHYGTDEQKDHYLPRLARGEEIPCFALTSPEAGSDAGSIPDTGVvckgewqgEEVLGMRLTWNKRYITLAPIATVL 248
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2762263583 188 -LVFaRCDD-----------GPAAFLVERDAPGctVEpvtgmLGTRaamtahlHFD-GCA------------VPAEALVG 242
Cdd:PRK09463 249 gLAF-KLYDpdgllgdkedlGITCALIPTDTPG--VE-----IGRR-------HFPlNVPfqngptrgkdvfIPLDYIIG 313
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2762263583 243 ---RAGFG----LNAVAAdaletGR-YSVAWGSAGLARACVEASARHAAAREQFGRPLAQHELVQRLITEMAVNT---SA 311
Cdd:PRK09463 314 gpkMAGQGwrmlMECLSV-----GRgISLPSNSTGGAKLAALATGAYARIRRQFKLPIGKFEGIEEPLARIAGNAylmDA 388
|
....*...
gi 2762263583 312 ARLLCLRA 319
Cdd:PRK09463 389 ARTLTTAA 396
|
|
| PLN02876 |
PLN02876 |
acyl-CoA dehydrogenase |
83-393 |
1.43e-13 |
|
acyl-CoA dehydrogenase
Pssm-ID: 215473 [Multi-domain] Cd Length: 822 Bit Score: 72.52 E-value: 1.43e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2762263583 83 GAGLDPVTFGLLNEALGhacssvRSLLTVHSMVIRA--------VTRWGGSRLRSRWLPPLASGTAVGAFALTEPE-AGS 153
Cdd:PLN02876 491 GAGLSNLEYGYLCEIMG------RSVWAPQVFNCGApdtgnmevLLRYGNKEQQLEWLIPLLEGKIRSGFAMTEPQvASS 564
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2762263583 154 DVASLRTAAEKTADGYrLTGGKRWITFGqAAD----VFLVFARCDDGPA------AFLVERDAPGCTVEPVTGMLGTRAA 223
Cdd:PLN02876 565 DATNIECSIRRQGDSY-VINGTKWWTSG-AMDprcrVLIVMGKTDFNAPkhkqqsMILVDIQTPGVQIKRPLLVFGFDDA 642
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2762263583 224 MTAH--LHFDGCAVPAEALVGRAGFGLNaVAADALETGRYSVAWGSAGLARACVEASARHAAAREQFGRPLAQHELVQRL 301
Cdd:PLN02876 643 PHGHaeISFENVRVPAKNILLGEGRGFE-IAQGRLGPGRLHHCMRLIGAAERGMQLMVQRALSRKAFGKLIAQHGSFLSD 721
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2762263583 302 ITEMAVNTSAARLLCLRAG-RLLHSADPQAVEAVWSAKYFAARSAFRAAADAVQVHGARGCGPDTPVQRLLRDAKIMEII 380
Cdd:PLN02876 722 LAKCRVELEQTRLLVLEAAdQLDRLGNKKARGIIAMAKVAAPNMALKVLDMAMQVHGAAGVSSDTVLAHLWATARTLRIA 801
|
330
....*....|...
gi 2762263583 381 EGTTEIQQTVIAQ 393
Cdd:PLN02876 802 DGPDEVHLGTIAK 814
|
|
| AXO |
cd01150 |
Peroxisomal acyl-CoA oxidase; Peroxisomal acyl-CoA oxidases (AXO) catalyze the first set in ... |
40-296 |
2.56e-08 |
|
Peroxisomal acyl-CoA oxidase; Peroxisomal acyl-CoA oxidases (AXO) catalyze the first set in the peroxisomal fatty acid beta-oxidation, the alpha,beta dehydrogenation of the corresponding trans-enoyl-CoA by FAD, which becomes reduced. In a second oxidative half-reaction, the reduced FAD is reoxidized by molecular oxygen. AXO is generally a homodimer, but it has been reported to form a different type of oligomer in yeast. There are several subtypes of AXO's, based on substrate specificity. Palmitoyl-CoA oxidase acts on straight-chain fatty acids and prostanoids; whereas, the closely related Trihydroxycoprostanoly-CoA oxidase has the greatest activity for 2-methyl branched side chains of bile precursors. Pristanoyl-CoA oxidase, acts on 2-methyl branched fatty acids. AXO has an additional domain, C-terminal to the region with similarity to acyl-CoA dehydrogenases, which is included in this alignment.
Pssm-ID: 173839 [Multi-domain] Cd Length: 610 Bit Score: 55.80 E-value: 2.56e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2762263583 40 DFARREILPHADRWDREEHLPGEVVRALADEGHLGAWAPREhggagldpvtFGLLNEALGHACSSVRSLLTVH-SMVIRA 118
Cdd:cd01150 43 LFQRELPSKHLSREELYEELKRKAKTDVERMGELMADDPEK----------MLALTNSLGGYDLSLGAKLGLHlGLFGNA 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2762263583 119 VTRWGGSRLRSRWLPPLASGTAVGAFALTEPEAGSDVASLRTAAekTADGYR---------LTGGKRWI-TFGQAADVFL 188
Cdd:cd01150 113 IKNLGTDEHQDYWLQGANNLEIIGCFAQTELGHGSNLQGLETTA--TYDPLTqefvintpdFTATKWWPgNLGKTATHAV 190
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2762263583 189 VFARC-----DDGPAAFLVE-RDA------PGCTVEPVTGMLGTRAAMTAHLHFDGCAVPAEALVGRAGfglnAVAAD-- 254
Cdd:cd01150 191 VFAQLitpgkNHGLHAFIVPiRDPkthqplPGVTVGDIGPKMGLNGVDNGFLQFRNVRIPRENLLNRFG----DVSPDgt 266
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|
gi 2762263583 255 -----------------ALETGRYSVAWGSAG-LARACVEAsARHAAAREQFGRPLAQHE 296
Cdd:cd01150 267 yvspfkdpnkrygamlgTRSGGRVGLIYDAAMsLKKAATIA-IRYSAVRRQFGPKPSDPE 325
|
|
| PTZ00457 |
PTZ00457 |
acyl-CoA dehydrogenase; Provisional |
74-212 |
6.51e-07 |
|
acyl-CoA dehydrogenase; Provisional
Pssm-ID: 185636 [Multi-domain] Cd Length: 520 Bit Score: 51.42 E-value: 6.51e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2762263583 74 GAWAPREHGGAGLDPVTFGLLNEALGHACSSVRSLLTVHSMVIRAVTRWGGSR-LRSRWLPPLASGTAVGAFAlTEPEAG 152
Cdd:PTZ00457 67 GARIATEYGGLGLGHTAHALIYEEVGTNCDSKLLSTIQHSGFCTYLLSTVGSKeLKGKYLTAMSDGTIMMGWA-TEEGCG 145
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2762263583 153 SDVASLRTAAEKTADG-YRLTGGKRWItFGQAADVFLVFAR------CDDGPAA------FLVERDAPGCTVE 212
Cdd:PTZ00457 146 SDISMNTTKASLTDDGsYVLTGQKRCE-FAASATHFLVLAKtltqtaAEEGATEvsrnsfFICAKDAKGVSVN 217
|
|
| NcnH |
cd01159 |
Naphthocyclinone hydroxylase; Naphthocyclinone is an aromatic polyketide and an antibiotic, ... |
43-374 |
7.24e-06 |
|
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: 47.73 E-value: 7.24e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2762263583 43 RREILPHADRWDREEHLPGEVVRALADEGHLGAWAPREHGGAGLDPVTFGLLNEALGHACSS---VRSLLTVHSMVIRAV 119
Cdd:cd01159 7 APLIRERAPEAERARRLPDEVVRALREIGFFRMFVPKRYGGLEGDFAEFAEAIATLAEACGSaawVASIVATHSRMLAAF 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2762263583 120 trwgGSRLRSRWLPPLASGTAVGAFALTEPeagsdvaslrtaAEKTADGYRLTGGKRWITFGQAAD-VFLVFARCDDG-- 196
Cdd:cd01159 87 ----PPEAQEEVWGDGPDTLLAGSYAPGGR------------AERVDGGYRVSGTWPFASGCDHADwILVGAIVEDDDgg 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2762263583 197 --PAAFLVERDapGCTVEP---VTGMLGT-------------------RAAMTAHlHFDGCAVPAEALVGRAGFGLnAVA 252
Cdd:cd01159 151 plPRAFVVPRA--EYEIVDtwhVVGLRGTgsntvvvddvfvpehrtltAGDMMAG-DGPGGSTPVYRMPLRQVFPL-SFA 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2762263583 253 ADAL-------------ETGRYSVAWGSAGLARACV------EASARHAAAREQFGRPLAQHELVQRLITEMAVNTsaaR 313
Cdd:cd01159 227 AVSLgaaegalaeflelAGKRVRQYGAAVKMAEAPItqlrlaEAAAELDAARAFLERATRDLWAHALAGGPIDVEE---R 303
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2762263583 314 LLCLRAGRLLHSADPQAVEAVWSAKyfaarsafraaadavqvhGARGCGPDTPVQRLLRDA 374
Cdd:cd01159 304 ARIRRDAAYAAKLSAEAVDRLFHAA------------------GGSALYTASPLQRIWRDI 346
|
|
| Acyl-CoA_dh_2 |
pfam08028 |
Acyl-CoA dehydrogenase, C-terminal domain; |
269-385 |
7.21e-05 |
|
Acyl-CoA dehydrogenase, C-terminal domain;
Pssm-ID: 429790 [Multi-domain] Cd Length: 133 Bit Score: 42.33 E-value: 7.21e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2762263583 269 GLARACVEASARHAAAREQ--FGRPLAQHELVQRLITEMAVNTSAARLLCLRAG----RLLHSADPQAVEAVWS---AKY 339
Cdd:pfam08028 8 GAARAALAEFTERARGRVRayFGVPLAEDPATQLALAEAAARIDAARLLLERAAarieAAAAAGKPVTPALRAEarrAAA 87
|
90 100 110 120
....*....|....*....|....*....|....*....|....*.
gi 2762263583 340 FAARSAFRAAADAVQVHGARGCGPDTPVQRLLRDAKIMEIIEGTTE 385
Cdd:pfam08028 88 FATELAVAAVDALFRAAGGSALFQDSPLQRIWRDIHAAAQHAAVNP 133
|
|
| PTZ00460 |
PTZ00460 |
acyl-CoA dehydrogenase; Provisional |
110-243 |
7.94e-05 |
|
acyl-CoA dehydrogenase; Provisional
Pssm-ID: 185639 [Multi-domain] Cd Length: 646 Bit Score: 44.84 E-value: 7.94e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2762263583 110 TVH-SMVIRAVTRWGGSRLRSRWLPPLASGTAVGAFALTEPEAGSDVASLRTAA--EKTADGYRL-----TGGKRWI-TF 180
Cdd:PTZ00460 96 TVHfAMVIPAFQVLGTDEQINLWMPSLLNFEIVGCYAQTELGHGSDVQNLETTAtyDKQTNEFVIhtpsvEAVKFWPgEL 175
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2762263583 181 GQAADVFLVFARC-----DDGPAAFLVE-RDA------PGCTVEPVTGMLGTRAAMTAHLHFDGCAVPAEALVGR 243
Cdd:PTZ00460 176 GFLCNFALVYAKLivngkNKGVHPFMVRiRDKethkplQGVEVGDIGPKMGYAVKDNGFLSFDHYRIPLDSLLAR 250
|
|
| PLN02636 |
PLN02636 |
acyl-coenzyme A oxidase |
87-291 |
1.19e-04 |
|
acyl-coenzyme A oxidase
Pssm-ID: 215342 [Multi-domain] Cd Length: 686 Bit Score: 44.46 E-value: 1.19e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2762263583 87 DPVTFGLLNEALGHACSSVRSLLTVHsmviraVTRWGGSRL-------RSRWLPPLASGTAVGAFALTEPEAGSDVASLR 159
Cdd:PLN02636 119 DPAKYFAITEAVGSVDMSLGIKLGVQ------YSLWGGSVInlgtkkhRDKYFDGIDNLDYPGCFAMTELHHGSNVQGLQ 192
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2762263583 160 TAA--EKTADGYRLT-----GGKRWItfGQAA---DVFLVFAR-----------CDDGPAAFLVE-RDA------PGCTV 211
Cdd:PLN02636 193 TTAtfDPLTDEFVINtpndgAIKWWI--GNAAvhgKFATVFARlklpthdskgvSDMGVHAFIVPiRDMkthqvlPGVEI 270
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2762263583 212 EPVTGMLGTRAAMTAHLHFDGCAVPAEALVGRagFG--------------LN---AVAADALETGRYSVAWGSAGLARAC 274
Cdd:PLN02636 271 RDCGHKVGLNGVDNGALRFRSVRIPRDNLLNR--FGdvsrdgkytsslptINkrfAATLGELVGGRVGLAYGSVGVLKAS 348
|
250
....*....|....*..
gi 2762263583 275 VEASARHAAAREQFGRP 291
Cdd:PLN02636 349 NTIAIRYSLLRQQFGPP 365
|
|
| PLN02443 |
PLN02443 |
acyl-coenzyme A oxidase |
114-289 |
1.89e-04 |
|
acyl-coenzyme A oxidase
Pssm-ID: 178062 [Multi-domain] Cd Length: 664 Bit Score: 43.67 E-value: 1.89e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2762263583 114 MVIRAVTRWGGSRLRSRWLPPLASGTAVGAFALTEPEAGSDVASLRTAA--EKTADGY-----RLTGGKRWI-TFGQAAD 185
Cdd:PLN02443 105 MFVPAIKGQGTEEQQKKWLPLAYKMQIIGCYAQTELGHGSNVQGLETTAtfDPKTDEFvihspTLTSSKWWPgGLGKVST 184
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2762263583 186 VFLVFARC-----DDGPAAFLVERDA-------PGCTVEPVTGMLGTRAAMT---AHLHFDGCAVPAE------ALVGRA 244
Cdd:PLN02443 185 HAVVYARLitngkDHGIHGFIVQLRSlddhsplPGVTVGDIGMKFGNGAYNTmdnGFLRFDHVRIPRDqmlmrlSKVTRE 264
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 2762263583 245 GFGLNAVAADALETG-----RYS-VAWGSAGLARAcVEASARHAAAREQFG 289
Cdd:PLN02443 265 GKYVQSDVPRQLVYGtmvyvRQTiVADASTALSRA-VCIATRYSAVRRQFG 314
|
|
| |
