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Conserved domains on  [gi|896565479|ref|WP_049461848|]
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MULTISPECIES: acyl-CoA dehydrogenase family protein [Stenotrophomonas]

Protein Classification

acyl-CoA dehydrogenase family protein( domain architecture ID 550)

acyl-CoA dehydrogenase (ACAD) family protein similar to acyl-CoA dehydrogenase that catalyzes the alpha,beta dehydrogenation of an acyl-CoA to form 2,3-dehydroacyl-CoA; requires an acceptor such as FAD, which becomes reduced

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
ACAD super family cl09933
Acyl-CoA dehydrogenase; Both mitochondrial acyl-CoA dehydrogenases (ACAD) and peroxisomal ...
 7-387 0e+00

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)


The actual alignment was detected with superfamily member cd01151:

Pssm-ID: 447864 [Multi-domain]  Cd Length: 386  Bit Score: 543.10  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896565479   7 DLFDVRSLLNEEERAVQESVARFTNERVLPIIGDAFDQARFPSELVPEIAALGLLGATlPAEYGGGDLGAVSYGLICQEL 86
Cdd:cd01151    5 DPLNLDDLLTEEERAIRDTAREFCQEELAPRVLEAYREEKFDRKIIEEMGELGLLGAT-IKGYGCAGLSSVAYGLIAREV 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896565479  87 ERGDSGLRSFVSVQSSLCMYPIYAYGSEEQRQQWLPAMARGELIGCFGLTEAHGGSDPASMKTRAVRDGSDWRISGSKMW 166
Cdd:cd01151   84 ERVDSGYRSFMSVQSSLVMLPIYDFGSEEQKQKYLPKLASGELIGCFGLTEPNHGSDPGGMETRARKDGGGYKLNGSKTW 163

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896565479 167 ITSGPVADLAIVWA--QTEDGIQGFVLEKGMAGFTTQEIKHKMSLRASLTGALFFDDVRVPDSHRLPNVKGLKGPLGCLT 244
Cdd:cd01151  164 ITNSPIADVFVVWArnDETGKIRGFILERGMKGLSAPKIQGKFSLRASITGEIVMDNVFVPEENLLPGAEGLRGPFKCLN 243

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896565479 245 QARYGISWGPIGAAIACLDEALGYAKERVLFGRPLAATQSAQMKLAEMARRITTAQLLALQLGRLKEAGQLQPQQVSLAK 324
Cdd:cd01151  244 NARYGIAWGALGAAEDCYHTARQYVLDRKQFGRPLAAFQLVQKKLADMLTEIALGLLACLRVGRLKDQGKATPEQISLLK 323

                        330       340       350       360       370       380
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 896565479 325 WNNCRMAIDIARECRDLLGGAGITTEHVAIRHALNLESVITYEGTETVHQLVIGRELTGISAF 387
Cdd:cd01151  324 RNNCGKALEIARTAREMLGGNGISDEYHIIRHMVNLESVNTYEGTHDIHALILGRAITGIQAF 386
 
Name Accession Description Interval E-value
GCD cd01151
Glutaryl-CoA dehydrogenase; Glutaryl-CoA dehydrogenase (GCD). GCD is an acyl-CoA dehydrogenase, ...
 7-387 0e+00

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: 543.10  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896565479   7 DLFDVRSLLNEEERAVQESVARFTNERVLPIIGDAFDQARFPSELVPEIAALGLLGATlPAEYGGGDLGAVSYGLICQEL 86
Cdd:cd01151    5 DPLNLDDLLTEEERAIRDTAREFCQEELAPRVLEAYREEKFDRKIIEEMGELGLLGAT-IKGYGCAGLSSVAYGLIAREV 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896565479  87 ERGDSGLRSFVSVQSSLCMYPIYAYGSEEQRQQWLPAMARGELIGCFGLTEAHGGSDPASMKTRAVRDGSDWRISGSKMW 166
Cdd:cd01151   84 ERVDSGYRSFMSVQSSLVMLPIYDFGSEEQKQKYLPKLASGELIGCFGLTEPNHGSDPGGMETRARKDGGGYKLNGSKTW 163

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896565479 167 ITSGPVADLAIVWA--QTEDGIQGFVLEKGMAGFTTQEIKHKMSLRASLTGALFFDDVRVPDSHRLPNVKGLKGPLGCLT 244
Cdd:cd01151  164 ITNSPIADVFVVWArnDETGKIRGFILERGMKGLSAPKIQGKFSLRASITGEIVMDNVFVPEENLLPGAEGLRGPFKCLN 243

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896565479 245 QARYGISWGPIGAAIACLDEALGYAKERVLFGRPLAATQSAQMKLAEMARRITTAQLLALQLGRLKEAGQLQPQQVSLAK 324
Cdd:cd01151  244 NARYGIAWGALGAAEDCYHTARQYVLDRKQFGRPLAAFQLVQKKLADMLTEIALGLLACLRVGRLKDQGKATPEQISLLK 323

                        330       340       350       360       370       380
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 896565479 325 WNNCRMAIDIARECRDLLGGAGITTEHVAIRHALNLESVITYEGTETVHQLVIGRELTGISAF 387
Cdd:cd01151  324 RNNCGKALEIARTAREMLGGNGISDEYHIIRHMVNLESVNTYEGTHDIHALILGRAITGIQAF 386
CaiA COG1960
Acyl-CoA dehydrogenase related to the alkylation response protein AidB [Lipid transport and ...
 15-383 2.65e-139

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: 401.91  E-value: 2.65e-139
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896565479  15 LNEEERAVQESVARFTNERVLPIIGDAFDQARFPSELVPEIAALGLLGATLPAEYGGGDLGAVSYGLICQELERGDSGLR 94
Cdd:COG1960    5 LTEEQRALRDEVREFAEEEIAPEAREWDREGEFPRELWRKLAELGLLGLTIPEEYGGLGLSLVELALVLEELARADASLA 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896565479  95 SFVSVQSSlCMYPIYAYGSEEQRQQWLPAMARGELIGCFGLTEAHGGSDPASMKTRAVRDGSDWRISGSKMWITSGPVAD 174
Cdd:COG1960   85 LPVGVHNG-AAEALLRFGTEEQKERYLPRLASGEWIGAFALTEPGAGSDAAALRTTAVRDGDGYVLNGQKTFITNAPVAD 163

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896565479 175 LAIVWAQTED-----GIQGFVLEKGMAGFTTQEIKHKMSLRASLTGALFFDDVRVPDSHRLPNV-KGLKGPLGCLTQARY 248
Cdd:COG1960  164 VILVLARTDPaaghrGISLFLVPKDTPGVTVGRIEDKMGLRGSDTGELFFDDVRVPAENLLGEEgKGFKIAMSTLNAGRL 243

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896565479 249 GISWGPIGAAIACLDEALGYAKERVLFGRPLAATQSAQMKLAEMARRITTAQLLALQLGRLKEAGQLQPQQVSLAKWNNC 328
Cdd:COG1960  244 GLAAQALGIAEAALELAVAYAREREQFGRPIADFQAVQHRLADMAAELEAARALVYRAAWLLDAGEDAALEAAMAKLFAT 323

                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 896565479 329 RMAIDIARECRDLLGGAGITTEHVAIRHALNLESVITYEGTETVHQLVIGRELTG 383
Cdd:COG1960  324 EAALEVADEALQIHGGYGYTREYPLERLYRDARILTIYEGTNEIQRLIIARRLLG 378
PLN02526 PLN02526
acyl-coenzyme A oxidase
 7-387 1.79e-89

acyl-coenzyme A oxidase


Pssm-ID: 178141 [Multi-domain]  Cd Length: 412  Bit Score: 275.96  E-value: 1.79e-89
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896565479   7 DLFDVRSLLNEEERAVQESVARFTNERVLPIIGDAFDQARFPSELVPEIAALGLLGATLPAeYGGGDLGAVSYGLICQEL 86
Cdd:PLN02526  21 DYYQFDDLLTPEEQALRKRVRECMEKEVAPIMTEYWEKAEFPFHIIPKLGSLGIAGGTIKG-YGCPGLSITASAIATAEV 99

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896565479  87 ERGDSGLRSFVSVQSSLCMYPIYAYGSEEQRQQWLPAMARGELIGCFGLTEAHGGSDPASMKTRAVRDGSDWRISGSKMW 166
Cdd:PLN02526 100 ARVDASCSTFILVHSSLAMLTIALCGSEAQKQKYLPSLAQLDTVACWALTEPDYGSDASSLNTTATKVEGGWILNGQKRW 179

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896565479 167 ITSGPVADLAIVWAQ--TEDGIQGFVLEKGMAGFTTQEIKHKMSLRASLTGALFFDDVRVPDSHRLPNVKGLKGPLGCLT 244
Cdd:PLN02526 180 IGNSTFADVLVIFARntTTNQINGFIVKKGAPGLKATKIENKIGLRMVQNGDIVLKDVFVPDEDRLPGVNSFQDTNKVLA 259

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896565479 245 QARYGISWGPIGAAIACLDEALGYAKERVLFGRPLAATQSAQMKLAEMARRITTAQLLALQLGRLKEAGQLQPQQVSLAK 324
Cdd:PLN02526 260 VSRVMVAWQPIGISMGVYDMCHRYLKERKQFGAPLAAFQINQEKLVRMLGNIQAMFLVGWRLCKLYESGKMTPGHASLGK 339

                        330       340       350       360       370       380
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 896565479 325 WNNCRMAIDIARECRDLLGGAGITTEHVAIRHALNLESVITYEGTETVHQLVIGRELTGISAF 387
Cdd:PLN02526 340 AWITKKARETVALGRELLGGNGILADFLVAKAFCDLEPIYTYEGTYDINALVTGREITGIASF 402
Acyl-CoA_dh_N pfam02771
Acyl-CoA dehydrogenase, N-terminal domain; The N-terminal domain of Acyl-CoA dehydrogenase is ...
 16-128 8.24e-45

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: 150.31  E-value: 8.24e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896565479   16 NEEERAVQESVARFTNERVLPIIGDAFDQARFPSELVPEIAALGLLGATLPAEYGGGDLGAVSYGLICQELERGDSGLRS 95
Cdd:pfam02771   1 TEEQEALRDTVREFAEEEIAPHAAEWDEEGEFPRELWKKLGELGLLGITIPEEYGGAGLDYLAYALVAEELARADASVAL 80

                          90       100       110
                  ....*....|....*....|....*....|...
gi 896565479   96 FVSVQSSLCMYPIYAYGSEEQRQQWLPAMARGE 128
Cdd:pfam02771  81 ALSVHSSLGAPPILRFGTEEQKERYLPKLASGE 113
 
Name Accession Description Interval E-value
GCD cd01151
Glutaryl-CoA dehydrogenase; Glutaryl-CoA dehydrogenase (GCD). GCD is an acyl-CoA dehydrogenase, ...
 7-387 0e+00

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: 543.10  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896565479   7 DLFDVRSLLNEEERAVQESVARFTNERVLPIIGDAFDQARFPSELVPEIAALGLLGATlPAEYGGGDLGAVSYGLICQEL 86
Cdd:cd01151    5 DPLNLDDLLTEEERAIRDTAREFCQEELAPRVLEAYREEKFDRKIIEEMGELGLLGAT-IKGYGCAGLSSVAYGLIAREV 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896565479  87 ERGDSGLRSFVSVQSSLCMYPIYAYGSEEQRQQWLPAMARGELIGCFGLTEAHGGSDPASMKTRAVRDGSDWRISGSKMW 166
Cdd:cd01151   84 ERVDSGYRSFMSVQSSLVMLPIYDFGSEEQKQKYLPKLASGELIGCFGLTEPNHGSDPGGMETRARKDGGGYKLNGSKTW 163

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896565479 167 ITSGPVADLAIVWA--QTEDGIQGFVLEKGMAGFTTQEIKHKMSLRASLTGALFFDDVRVPDSHRLPNVKGLKGPLGCLT 244
Cdd:cd01151  164 ITNSPIADVFVVWArnDETGKIRGFILERGMKGLSAPKIQGKFSLRASITGEIVMDNVFVPEENLLPGAEGLRGPFKCLN 243

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896565479 245 QARYGISWGPIGAAIACLDEALGYAKERVLFGRPLAATQSAQMKLAEMARRITTAQLLALQLGRLKEAGQLQPQQVSLAK 324
Cdd:cd01151  244 NARYGIAWGALGAAEDCYHTARQYVLDRKQFGRPLAAFQLVQKKLADMLTEIALGLLACLRVGRLKDQGKATPEQISLLK 323

                        330       340       350       360       370       380
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 896565479 325 WNNCRMAIDIARECRDLLGGAGITTEHVAIRHALNLESVITYEGTETVHQLVIGRELTGISAF 387
Cdd:cd01151  324 RNNCGKALEIARTAREMLGGNGISDEYHIIRHMVNLESVNTYEGTHDIHALILGRAITGIQAF 386
CaiA COG1960
Acyl-CoA dehydrogenase related to the alkylation response protein AidB [Lipid transport and ...
 15-383 2.65e-139

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: 401.91  E-value: 2.65e-139
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896565479  15 LNEEERAVQESVARFTNERVLPIIGDAFDQARFPSELVPEIAALGLLGATLPAEYGGGDLGAVSYGLICQELERGDSGLR 94
Cdd:COG1960    5 LTEEQRALRDEVREFAEEEIAPEAREWDREGEFPRELWRKLAELGLLGLTIPEEYGGLGLSLVELALVLEELARADASLA 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896565479  95 SFVSVQSSlCMYPIYAYGSEEQRQQWLPAMARGELIGCFGLTEAHGGSDPASMKTRAVRDGSDWRISGSKMWITSGPVAD 174
Cdd:COG1960   85 LPVGVHNG-AAEALLRFGTEEQKERYLPRLASGEWIGAFALTEPGAGSDAAALRTTAVRDGDGYVLNGQKTFITNAPVAD 163

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896565479 175 LAIVWAQTED-----GIQGFVLEKGMAGFTTQEIKHKMSLRASLTGALFFDDVRVPDSHRLPNV-KGLKGPLGCLTQARY 248
Cdd:COG1960  164 VILVLARTDPaaghrGISLFLVPKDTPGVTVGRIEDKMGLRGSDTGELFFDDVRVPAENLLGEEgKGFKIAMSTLNAGRL 243

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896565479 249 GISWGPIGAAIACLDEALGYAKERVLFGRPLAATQSAQMKLAEMARRITTAQLLALQLGRLKEAGQLQPQQVSLAKWNNC 328
Cdd:COG1960  244 GLAAQALGIAEAALELAVAYAREREQFGRPIADFQAVQHRLADMAAELEAARALVYRAAWLLDAGEDAALEAAMAKLFAT 323

                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 896565479 329 RMAIDIARECRDLLGGAGITTEHVAIRHALNLESVITYEGTETVHQLVIGRELTG 383
Cdd:COG1960  324 EAALEVADEALQIHGGYGYTREYPLERLYRDARILTIYEGTNEIQRLIIARRLLG 378
SCAD_SBCAD cd01158
Short chain acyl-CoA dehydrogenases and eukaryotic short/branched chain acyl-CoA ...
 17-381 1.02e-111

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: 331.15  E-value: 1.02e-111
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896565479  17 EEERAVQESVARFTNERVLPIIGDAFDQARFPSELVPEIAALGLLGATLPAEYGGGDLGAVSYGLICQELERGDSGLRSF 96
Cdd:cd01158    1 EEHQMIRKTVRDFAEKEIAPLAAEMDEKGEFPREVIKEMAELGLMGIPIPEEYGGAGLDFLAYAIAIEELAKVDASVAVI 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896565479  97 VSVQSSLCMYPIYAYGSEEQRQQWLPAMARGELIGCFGLTEAHGGSDPASMKTRAVRDGSDWRISGSKMWITSGPVADLA 176
Cdd:cd01158   81 VSVHNSLGANPIIKFGTEEQKKKYLPPLATGEKIGAFALSEPGAGSDAAALKTTAKKDGDDYVLNGSKMWITNGGEADFY 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896565479 177 IVWAQTE-----DGIQGFVLEKGMAGFTTQEIKHKMSLRASLTGALFFDDVRVPDSHRLPNV-KGLKGPLGCLTQARYGI 250
Cdd:cd01158  161 IVFAVTDpskgyRGITAFIVERDTPGLSVGKKEDKLGIRGSSTTELIFEDVRVPKENILGEEgEGFKIAMQTLDGGRIGI 240

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896565479 251 SWGPIGAAIACLDEALGYAKERVLFGRPLAATQSAQMKLAEMARRITTAQLLALQLGRLKEAGQLQPQQVSLAKWNNCRM 330
Cdd:cd01158  241 AAQALGIAQAALDAAVDYAKERKQFGKPIADFQGIQFKLADMATEIEAARLLTYKAARLKDNGEPFIKEAAMAKLFASEV 320

                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|...
gi 896565479 331 AIDIARECRDLLGGAGITTEHVAIRHAlnLESVIT--YEGTETVHQLVIGREL 381
Cdd:cd01158  321 AMRVTTDAVQIFGGYGYTKDYPVERYY--RDAKITeiYEGTSEIQRLVIAKHL 371
PLN02526 PLN02526
acyl-coenzyme A oxidase
 7-387 1.79e-89

acyl-coenzyme A oxidase


Pssm-ID: 178141 [Multi-domain]  Cd Length: 412  Bit Score: 275.96  E-value: 1.79e-89
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896565479   7 DLFDVRSLLNEEERAVQESVARFTNERVLPIIGDAFDQARFPSELVPEIAALGLLGATLPAeYGGGDLGAVSYGLICQEL 86
Cdd:PLN02526  21 DYYQFDDLLTPEEQALRKRVRECMEKEVAPIMTEYWEKAEFPFHIIPKLGSLGIAGGTIKG-YGCPGLSITASAIATAEV 99

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896565479  87 ERGDSGLRSFVSVQSSLCMYPIYAYGSEEQRQQWLPAMARGELIGCFGLTEAHGGSDPASMKTRAVRDGSDWRISGSKMW 166
Cdd:PLN02526 100 ARVDASCSTFILVHSSLAMLTIALCGSEAQKQKYLPSLAQLDTVACWALTEPDYGSDASSLNTTATKVEGGWILNGQKRW 179

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896565479 167 ITSGPVADLAIVWAQ--TEDGIQGFVLEKGMAGFTTQEIKHKMSLRASLTGALFFDDVRVPDSHRLPNVKGLKGPLGCLT 244
Cdd:PLN02526 180 IGNSTFADVLVIFARntTTNQINGFIVKKGAPGLKATKIENKIGLRMVQNGDIVLKDVFVPDEDRLPGVNSFQDTNKVLA 259

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896565479 245 QARYGISWGPIGAAIACLDEALGYAKERVLFGRPLAATQSAQMKLAEMARRITTAQLLALQLGRLKEAGQLQPQQVSLAK 324
Cdd:PLN02526 260 VSRVMVAWQPIGISMGVYDMCHRYLKERKQFGAPLAAFQINQEKLVRMLGNIQAMFLVGWRLCKLYESGKMTPGHASLGK 339

                        330       340       350       360       370       380
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 896565479 325 WNNCRMAIDIARECRDLLGGAGITTEHVAIRHALNLESVITYEGTETVHQLVIGRELTGISAF 387
Cdd:PLN02526 340 AWITKKARETVALGRELLGGNGILADFLVAKAFCDLEPIYTYEGTYDINALVTGREITGIASF 402
ACAD cd00567
Acyl-CoA dehydrogenase; Both mitochondrial acyl-CoA dehydrogenases (ACAD) and peroxisomal ...
 17-379 3.84e-87

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: 266.84  E-value: 3.84e-87
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896565479  17 EEERAVQESVARFTNERVLPiigDAFDQARFPSELVPEIAALGLLGAtlpaeygggdlgavsyglicqelergdsglrsf 96
Cdd:cd00567    1 EEQRELRDSAREFAAEELEP---YARERRETPEEPWELLAELGLLLG--------------------------------- 44

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896565479  97 vsvqsslcMYPIYAYGSEEQRQQWLPAMARGELIGCFGLTEAHGGSDPASMKTRAVRDGSDWRISGSKMWITSGPVADLA 176
Cdd:cd00567   45 --------AALLLAYGTEEQKERYLPPLASGEAIAAFALTEPGAGSDLAGIRTTARKDGDGYVLNGRKIFISNGGDADLF 116

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896565479 177 IVWAQTED------GIQGFVLEKGMAGFTTQEIKHKMSLRASLTGALFFDDVRVPDSHRLPNV-KGLKGPLGCLTQARYG 249
Cdd:cd00567  117 IVLARTDEegpghrGISAFLVPADTPGVTVGRIWDKMGMRGSGTGELVFDDVRVPEDNLLGEEgGGFELAMKGLNVGRLL 196

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896565479 250 ISWGPIGAAIACLDEALGYAKERVLFGRPLAATQSAQMKLAEMARRITTAQLLALQLGRLKEAGQLQP-QQVSLAKWNNC 328
Cdd:cd00567  197 LAAVALGAARAALDEAVEYAKQRKQFGKPLAEFQAVQFKLADMAAELEAARLLLYRAAWLLDQGPDEArLEAAMAKLFAT 276

                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|.
gi 896565479 329 RMAIDIARECRDLLGGAGITTEHVAIRHALNLESVITYEGTETVHQLVIGR 379
Cdd:cd00567  277 EAAREVADLAMQIHGGRGYSREYPVERYLRDARAARIAEGTAEIQRLIIAR 327
IVD cd01156
Isovaleryl-CoA dehydrogenase; Isovaleryl-CoA dehydrogenase (IVD) is an is an acyl-CoA ...
 15-381 2.55e-80

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: 251.18  E-value: 2.55e-80
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896565479  15 LNEEERAVQESVARFTNERVLPIIGDAFDQARFPSELVPEIAALGLLGATLPAEYGGGDLGAVSYGLICQELERGDSGLR 94
Cdd:cd01156    2 LDDEIEMLRQSVREFAQKEIAPLAAKIDRDNEFPRDLWRKMGKLGLLGITAPEEYGGSGMGYLAHVIIMEEISRASGSVA 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896565479  95 SFVSVQSSLCMYPIYAYGSEEQRQQWLPAMARGELIGCFGLTEAHGGSDPASMKTRAVRDGSDWRISGSKMWITSGPVAD 174
Cdd:cd01156   82 LSYGAHSNLCINQIYRNGSAAQKEKYLPKLISGEHIGALAMSEPNAGSDVVSMKLRAEKKGDRYVLNGSKMWITNGPDAD 161

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896565479 175 LAIVWAQTE-----DGIQGFVLEKGMAGFTTQEIKHKMSLRASLTGALFFDDVRVPDSHRLPNV-KGLKGPLGCLTQARY 248
Cdd:cd01156  162 TLVVYAKTDpsagaHGITAFIVEKGMPGFSRAQKLDKLGMRGSNTCELVFEDCEVPEENILGGEnKGVYVLMSGLDYERL 241

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896565479 249 GISWGPIGAAIACLDEALGYAKERVLFGRPLAATQSAQMKLAEMARRITTAQLLALQLGRLKEAGQLQPQQVSLAKWNNC 328
Cdd:cd01156  242 VLAGGPIGIMQAALDVAIPYAHQRKQFGQPIGEFQLVQGKLADMYTRLNASRSYLYTVAKACDRGNMDPKDAAGVILYAA 321

                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 896565479 329 RMAIDIARECRDLLGGAGITTEHVAIRHalnLESVITYE---GTETVHQLVIGREL 381
Cdd:cd01156  322 EKATQVALDAIQILGGNGYINDYPTGRL---LRDAKLYEigaGTSEIRRMVIGREL 374
LCAD cd01160
Long chain acyl-CoA dehydrogenase; LCAD is an acyl-CoA dehydrogenases (ACAD), which is found ...
 17-381 3.94e-73

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: 232.39  E-value: 3.94e-73
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896565479  17 EEERAVQESVARFTNERVLPIIGDAFDQARFPSELVPEIAALGLLGATLPAEYGGGDLGAVSYGLICQELER-GDSGLRs 95
Cdd:cd01160    1 EEHDAFRDVVRRFFAKEVAPFHHEWEKAGEVPREVWRKAGEQGLLGVGFPEEYGGIGGDLLSAAVLWEELARaGGSGPG- 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896565479  96 fVSVQSSLCMYPIYAYGSEEQRQQWLPAMARGELIGCFGLTEAHGGSDPASMKTRAVRDGSDWRISGSKMWITSGPVADL 175
Cdd:cd01160   80 -LSLHTDIVSPYITRAGSPEQKERVLPQMVAGKKIGAIAMTEPGAGSDLQGIRTTARKDGDHYVLNGSKTFITNGMLADV 158

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896565479 176 AIVWAQT------EDGIQGFVLEKGMAGFTTQEIKHKMSLRASLTGALFFDDVRVPDSHRLPNV-KGLKGPLGCLTQARY 248
Cdd:cd01160  159 VIVVARTggeargAGGISLFLVERGTPGFSRGRKLKKMGWKAQDTAELFFDDCRVPAENLLGEEnKGFYYLMQNLPQERL 238

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896565479 249 GISWGPIGAAIACLDEALGYAKERVLFGRPLAATQSAQMKLAEMARRITTAQLLALQLGRLKEAGQLQPQQVSLAKWNNC 328
Cdd:cd01160  239 LIAAGALAAAEFMLEETRNYVKQRKAFGKTLAQLQVVRHKIAELATKVAVTRAFLDNCAWRHEQGRLDVAEASMAKYWAT 318

                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|...
gi 896565479 329 RMAIDIARECRDLLGGAGITTEHVAIRHALNLESVITYEGTETVHQLVIGREL 381
Cdd:cd01160  319 ELQNRVAYECVQLHGGWGYMREYPIARAYRDARVQPIYGGTTEIMKELISRQM 371
VLCAD cd01161
Very long chain acyl-CoA dehydrogenase; VLCAD is an acyl-CoA dehydrogenase (ACAD), which is ...
 5-384 1.01e-63

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: 209.25  E-value: 1.01e-63
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896565479   5 PYDlFDVRSLLNEEERAVQESVARFTNERVLPIIGDAFDqaRFPSELVPEIAALGLLGATLPAEYGGGDLGAVSYGLICQ 84
Cdd:cd01161   18 PYP-SVLTEEQTEELNMLVGPVEKFFEEVNDPAKNDQLE--KIPRKTLTQLKELGLFGLQVPEEYGGLGLNNTQYARLAE 94

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896565479  85 ELERgDSGLRSFVSVQSSLCMYPIYAYGSEEQRQQWLPAMARGELIGCFGLTEAHGGSDPASMKTRAVR--DGSDWRISG 162
Cdd:cd01161   95 IVGM-DLGFSVTLGAHQSIGFKGILLFGTEAQKEKYLPKLASGEWIAAFALTEPSSGSDAASIRTTAVLseDGKHYVLNG 173

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896565479 163 SKMWITSGPVADLAIVWAQTE---------DGIQGFVLEKGMAGFTTQEIKHKMSLRASLTGALFFDDVRVPDSHRLPNV 233
Cdd:cd01161  174 SKIWITNGGIADIFTVFAKTEvkdatgsvkDKITAFIVERSFGGVTNGPPEKKMGIKGSNTAEVYFEDVKIPVENVLGEV 253

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896565479 234 -KGLKGPLGCLTQARYGISWGPIGAAIACLDEALGYAKERVLFGRPLAATQSAQMKLAEMARRITTAQLLALQLGRLKEA 312
Cdd:cd01161  254 gDGFKVAMNILNNGRFGMGAALIGTMKRCIEKAVDYANNRKQFGKKIHEFGLIQEKLANMAILQYATESMAYMTSGNMDR 333

                        330       340       350       360       370       380       390
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 896565479 313 GQLQPQQV--SLAKWNNCRMAIDIARECRDLLGGAGITTEHVAIRHALNLESVITYEGTETVHQLVIGreLTGI 384
Cdd:cd01161  334 GLKAEYQIeaAISKVFASEAAWLVVDEAIQIHGGMGFMREYGVERVLRDLRIFRIFEGTNEILRLFIA--LTGL 405
IBD cd01162
Isobutyryl-CoA dehydrogenase; Isobutyryl-CoA dehydrogenase (IBD) catalyzes the alpha, beta- ...
 15-383 4.50e-62

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: 203.83  E-value: 4.50e-62
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896565479  15 LNEEERAVQESVARFTNERVLPIIGDAFDQARFPSELVPEIAALGLLGATLPAEYGGGDLGAVSYGLICQELERGDSGLR 94
Cdd:cd01162    1 LNEEQRAIQEVARAFAAKEMAPHAADWDQKKHFPVDVLRKAAELGFGGIYIRDDVGGSGLSRLDASIIFEALSTGCVSTA 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896565479  95 SFVSVQSsLCMYPIYAYGSEEQRQQWLPAMARGELIGCFGLTEAHGGSDPASMKTRAVRDGSDWRISGSKMWITSGPVAD 174
Cdd:cd01162   81 AYISIHN-MCAWMIDSFGNDEQRERFLPDLCTMEKLASYCLTEPGSGSDAAALRTRAVREGDHYVLNGSKAFISGAGDSD 159

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896565479 175 LAIVWAQT-EDGIQG---FVLEKGMAGFTTQEIKHKMSLRASLTGALFFDDVRVPDSHRL-PNVKGLKGPLGCLTQARYG 249
Cdd:cd01162  160 VYVVMARTgGEGPKGiscFVVEKGTPGLSFGANEKKMGWNAQPTRAVIFEDCRVPVENRLgGEGQGFGIAMAGLNGGRLN 239

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896565479 250 ISWGPIGAAIACLDEALGYAKERVLFGRPLAATQSAQMKLAEMARRITTAQLL------ALQLGRlKEAGQLqpqqVSLA 323
Cdd:cd01162  240 IASCSLGAAQAALDLARAYLEERKQFGKPLADFQALQFKLADMATELVASRLMvrraasALDRGD-PDAVKL----CAMA 314

                        330       340       350       360       370       380
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 896565479 324 KWNNCRMAIDIARECRDLLGGAGITTEHVAIRHALNLESVITYEGTETVHQLVIGRELTG 383
Cdd:cd01162  315 KRFATDECFDVANQALQLHGGYGYLKDYPVEQYVRDLRVHQILEGTNEIMRLIIARALLT 374
MCAD cd01157
Medium chain acyl-CoA dehydrogenase; MCADs are mitochondrial beta-oxidation enzymes, which ...
 15-383 7.81e-60

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: 198.19  E-value: 7.81e-60
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896565479  15 LNEEERAVQESVARFTNERVLPIIGDAFDQARFPSELVPEIAALGLLGATLPAEYGGGDLGAVSYGLICQELERGDSGLR 94
Cdd:cd01157    1 LTEQQKEFQETARKFAREEIIPVAAEYDKSGEYPWPLIKRAWELGLMNTHIPEDCGGLGLGTFDTCLITEELAYGCTGVQ 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896565479  95 SFVSVqSSLCMYPIYAYGSEEQRQQWLPAMARGELIGCFGLTEAHGGSDPASMKTRAVRDGSDWRISGSKMWITSGPVAD 174
Cdd:cd01157   81 TAIEA-NSLGQMPVIISGNDEQKKKYLGRMTEEPLMCAYCVTEPGAGSDVAGIKTKAEKKGDEYIINGQKMWITNGGKAN 159

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896565479 175 LAIVWAQTE--------DGIQGFVLEKGMAGFTTQEIKHKMSLRASLTGALFFDDVRVPDSHRL-PNVKGLKGPLGCLTQ 245
Cdd:cd01157  160 WYFLLARSDpdpkcpasKAFTGFIVEADTPGIQPGRKELNMGQRCSDTRGITFEDVRVPKENVLiGEGAGFKIAMGAFDK 239

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896565479 246 ARYGISWGPIGAAIACLDEALGYAKERVLFGRPLAATQSAQMKLAEMARRITTAQLLALQLGRLKEAGQLQPQQVSLAKW 325
Cdd:cd01157  240 TRPPVAAGAVGLAQRALDEATKYALERKTFGKLIAEHQAVSFMLADMAMKVELARLAYQRAAWEVDSGRRNTYYASIAKA 319

                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 896565479 326 NNCRMAIDIARECRDLLGGAGITTEHVAIRHALNLESVITYEGTETVHQLVIGRELTG 383
Cdd:cd01157  320 FAADIANQLATDAVQIFGGNGFNSEYPVEKLMRDAKIYQIYEGTSQIQRLIISREHLG 377
PLN02519 PLN02519
isovaleryl-CoA dehydrogenase
 13-381 5.27e-57

isovaleryl-CoA dehydrogenase


Pssm-ID: 215284 [Multi-domain]  Cd Length: 404  Bit Score: 191.63  E-value: 5.27e-57
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896565479  13 SLLNEEERAVQESVARFTNERVLPIiGDAFDQAR-FPSE--LVPEIAALGLLGATLPAEYGGGDLGAVSYGLICQELERG 89
Cdd:PLN02519  24 LLFDDTQLQFKESVQQFAQENIAPH-AAAIDATNsFPKDvnLWKLMGDFNLHGITAPEEYGGLGLGYLYHCIAMEEISRA 102

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896565479  90 DSGLRSFVSVQSSLCMYPIYAYGSEEQRQQWLPAMARGELIGCFGLTEAHGGSDPASMKTRAVRDGSDWRISGSKMWITS 169
Cdd:PLN02519 103 SGSVGLSYGAHSNLCINQLVRNGTPAQKEKYLPKLISGEHVGALAMSEPNSGSDVVSMKCKAERVDGGYVLNGNKMWCTN 182

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896565479 170 GPVADLAIVWAQTE-----DGIQGFVLEKGMAGFTTQEIKHKMSLRASLTGALFFDDVRVPDSHRLPNV-KGLKGPLGCL 243
Cdd:PLN02519 183 GPVAQTLVVYAKTDvaagsKGITAFIIEKGMPGFSTAQKLDKLGMRGSDTCELVFENCFVPEENVLGQEgKGVYVMMSGL 262

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896565479 244 TQARYGISWGPIGAAIACLDEALGYAKERVLFGRPLAATQSAQMKLAEMARRITTAQLLALQLGRLKEAGQLQPQQVSLA 323
Cdd:PLN02519 263 DLERLVLAAGPLGLMQACLDVVLPYVRQREQFGRPIGEFQFIQGKLADMYTSLQSSRSYVYSVARDCDNGKVDRKDCAGV 342

                        330       340       350       360       370       380
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 896565479 324 KWNNCRMAIDIARECRDLLGGAGITTEHVAIRHalnLESVITYE---GTETVHQLVIGREL 381
Cdd:PLN02519 343 ILCAAERATQVALQAIQCLGGNGYINEYPTGRL---LRDAKLYEigaGTSEIRRMLIGREL 400
PTZ00461 PTZ00461
isovaleryl-CoA dehydrogenase; Provisional
 10-350 3.60e-46

isovaleryl-CoA dehydrogenase; Provisional


Pssm-ID: 185640 [Multi-domain]  Cd Length: 410  Bit Score: 163.18  E-value: 3.60e-46
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896565479  10 DVRSLLNE--EERAVQESVARFTNERVLPIIGDAFDQARFPSELVPEIAALGLLGATLPAEYGGGDLGAVSYGLICQELE 87
Cdd:PTZ00461  30 AFMDLYNPtpEHAALRETVAKFSREVVDKHAREDDINMHFNRDLFKQLGDLGVMGVTVPEADGGAGMDAVAAVIIHHELS 109

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896565479  88 RGDSGLRSFVSVQSSLCMYPIYAYGSEEQRQQWLPAMARGELIGCFGLTEAHGGSDPASMKTRAVRDGS-DWRISGSKMW 166
Cdd:PTZ00461 110 KYDPGFCLAYLAHSMLFVNNFYYSASPAQRARWLPKVLTGEHVGAMGMSEPGAGTDVLGMRTTAKKDSNgNYVLNGSKIW 189

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896565479 167 ITSGPVADLAIVWAQTEDGIQGFVLEKGMAGFTTQEIKHKMSLRASLTGALFFDDVRVPDSHRL-PNVKGLKGPLGCLTQ 245
Cdd:PTZ00461 190 ITNGTVADVFLIYAKVDGKITAFVVERGTKGFTQGPKIDKCGMRASHMCQLFFEDVVVPAENLLgEEGKGMVGMMRNLEL 269

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896565479 246 ARYGISWGPIGAAIACLDEALGYAKERVLFGRPLAATQSAQMKLAEMARRITTAQLLALQLGRLKEAGQLQPQQVSLAKW 325
Cdd:PTZ00461 270 ERVTLAAMAVGIAERSVELMTSYASERKAFGKPISNFGQIQRYIAEGYADTEAAKALVYSVSHNVHPGNKNRLGSDAAKL 349

                        330       340
                 ....*....|....*....|....*
gi 896565479 326 NNCRMAIDIARECRDLLGGAGITTE 350
Cdd:PTZ00461 350 FATPIAKKVADSAIQVMGGMGYSRD 374
Acyl-CoA_dh_N pfam02771
Acyl-CoA dehydrogenase, N-terminal domain; The N-terminal domain of Acyl-CoA dehydrogenase is ...
 16-128 8.24e-45

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: 150.31  E-value: 8.24e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896565479   16 NEEERAVQESVARFTNERVLPIIGDAFDQARFPSELVPEIAALGLLGATLPAEYGGGDLGAVSYGLICQELERGDSGLRS 95
Cdd:pfam02771   1 TEEQEALRDTVREFAEEEIAPHAAEWDEEGEFPRELWKKLGELGLLGITIPEEYGGAGLDYLAYALVAEELARADASVAL 80

                          90       100       110
                  ....*....|....*....|....*....|...
gi 896565479   96 FVSVQSSLCMYPIYAYGSEEQRQQWLPAMARGE 128
Cdd:pfam02771  81 ALSVHSSLGAPPILRFGTEEQKERYLPKLASGE 113
ACAD_fadE6_17_26 cd01152
Putative acyl-CoA dehydrogenases similar to fadE6, fadE17, and fadE26; Putative acyl-CoA ...
 55-346 6.92e-41

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: 148.26  E-value: 6.92e-41
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896565479  55 IAALGLLGATLPAEYGGGDLGAVSYGLICQELERGDsGLRSFVSVQSSLCMYPIYAYGSEEQRQQWLPAMARGELIGCFG 134
Cdd:cd01152   44 LAAAGWAAPGWPKEYGGRGASLMEQLIFREEMAAAG-APVPFNQIGIDLAGPTILAYGTDEQKRRFLPPILSGEEIWCQG 122

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896565479 135 LTEAHGGSDPASMKTRAVRDGSDWRISGSKMWITSGPVADLAIVWAQTE------DGIQGFVLEKGMAGFTTQEIKHKMS 208
Cdd:cd01152  123 FSEPGAGSDLAGLRTRAVRDGDDWVVNGQKIWTSGAHYADWAWLLVRTDpeapkhRGISILLVDMDSPGVTVRPIRSING 202

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896565479 209 lrASLTGALFFDDVRVPDSHRLPNV-KGLKgplgcLTQARYGISWGPIGAAIACLDE-ALGYAKERVLFGRPLAATQSAQ 286
Cdd:cd01152  203 --GEFFNEVFLDDVRVPDANRVGEVnDGWK-----VAMTTLNFERVSIGGSAATFFElLLARLLLLTRDGRPLIDDPLVR 275

                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 896565479 287 MKLAEMARRITTAQLLALQLGRLKEAGQLQPQQVSLAKWNNCRMAIDIARECRDLLGGAG 346
Cdd:cd01152  276 QRLARLEAEAEALRLLVFRLASALAAGKPPGAEASIAKLFGSELAQELAELALELLGTAA 335
ACAD_fadE5 cd01153
Putative acyl-CoA dehydrogenases similar to fadE5; Putative acyl-CoA dehydrogenase (ACAD). ...
 50-382 3.06e-34

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: 130.97  E-value: 3.06e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896565479  50 ELVPEIAALGLLGATLPAEYGGGDLGAVSYGLICQELERGDSGLRSFVSVQSslCMYPIYAYGSEEQRQQWLPAMARGEL 129
Cdd:cd01153   40 EALDAFAEAGWMALGVPEEYGGQGLPITVYSALAEIFSRGDAPLMYASGTQG--AAATLLAHGTEAQREKWIPRLAEGEW 117

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896565479 130 IGCFGLTEAHGGSDPASMKTRAVRDGS-DWRISGSKMWITSGPvADLA-----IVWAQTEDGIQG-----------FVLE 192
Cdd:cd01153  118 TGTMCLTEPDAGSDLGALRTKAVYQADgSWRINGVKRFISAGE-HDMSenivhLVLARSEGAPPGvkglslflvpkFLDD 196

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896565479 193 KGMAGFTTQEIKHKMSLRASLTGALFFDDVRVP---DSHRlpnvkGLKGPLGCLTQARYGISWGPIGAAIACLDEALGYA 269
Cdd:cd01153  197 GERNGVTVARIEEKMGLHGSPTCELVFDNAKGEligEEGM-----GLAQMFAMMNGARLGVGTQGTGLAEAAYLNALAYA 271

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896565479 270 KERVLFGRPLAA--------------TQSAQMKLAEMARRITTAQLLALQLGRLKEAGQLQPQQVS--------LAKWNN 327
Cdd:cd01153  272 KERKQGGDLIKAapavtiihhpdvrrSLMTQKAYAEGSRALDLYTATVQDLAERKATEGEDRKALSaladlltpVVKGFG 351

                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 896565479 328 CRMAIDIARECRDLLGGAGITTEHVAIRHALNLESVITYEGTETVH-QLVIGRELT 382
Cdd:cd01153  352 SEAALEAVSDAIQVHGGSGYTREYPIEQYYRDARITTIYEGTTGIQaLDLIGRKIV 407
Acyl-CoA_dh_1 pfam00441
Acyl-CoA dehydrogenase, C-terminal domain; C-terminal domain of Acyl-CoA dehydrogenase is an ...
 234-381 1.62e-32

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: 119.28  E-value: 1.62e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896565479  234 KGLKGPLGCLTQARYGISWGPIGAAIACLDEALGYAKERVLFGRPLAATQSAQMKLAEMARRITTAQLLALQLGRLKEAG 313
Cdd:pfam00441   2 RGFRVAMETLNHERLAIAAMALGLARRALDEALAYARRRKAFGRPLIDFQLVRHKLAEMAAEIEAARLLVYRAAEALDAG 81

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 896565479  314 QLQPQQVSLAKWNNCRMAIDIARECRDLLGGAGITTEHVAIRHALNLESVITYEGTETVHQLVIGREL 381
Cdd:pfam00441  82 GPDGAEASMAKLYASEAAVEVADLAMQLHGGYGYLREYPVERLYRDARVLRIGEGTSEIQRNIIARRL 149
Acyl-CoA_dh_M pfam02770
Acyl-CoA dehydrogenase, middle domain; Central domain of Acyl-CoA dehydrogenase has a ...
 132-220 7.20e-27

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: 102.36  E-value: 7.20e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896565479  132 CFGLTEAHGGSDPASMKTRAV-RDGSDWRISGSKMWITSGPVADLAIVWAQTE-----DGIQGFVLEKGMAGFTTQEIKH 205
Cdd:pfam02770   1 AFALTEPGAGSDVASLKTTAAdGDGGGWVLNGTKWWITNAGIADLFLVLARTGgddrhGGISLFLVPKDAPGVSVRRIET 80

                          90
                  ....*....|....*
gi 896565479  206 KMSLRASLTGALFFD 220
Cdd:pfam02770  81 KLGVRGLPTGELVFD 95
PRK12341 PRK12341
acyl-CoA dehydrogenase;
43-351 1.27e-26

acyl-CoA dehydrogenase;


Pssm-ID: 183454 [Multi-domain]  Cd Length: 381  Bit Score: 109.43  E-value: 1.27e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896565479  43 DQARFPSELVPEIA--ALGLLGatLPAEYGGGDLGAVSYGLICQELERgdSGLRSFVSVQSsLCMYPIYAYGSEEQ-RQQ 119
Cdd:PRK12341  34 ENGTYPREFMRALAdnGISMLG--VPEEFGGTPADYVTQMLVLEEVSK--CGAPAFLITNG-QCIHSMRRFGSAEQlRKT 108

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896565479 120 WLPAMARGELIGCFGLTEAHGGSDPASMKTRAVRDGSDWRISGSKMWITSGPVADLAIVWA---QTEDGIQGFVL---EK 193
Cdd:PRK12341 109 AESTLETGDPAYALALTEPGAGSDNNSATTTYTRKNGKVYLNGQKTFITGAKEYPYMLVLArdpQPKDPKKAFTLwwvDS 188

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896565479 194 GMAGFTTQEIkHKMSLRASLTGALFFDDVRVPDSHRLpnvkGLKGP-----LGCLTQARYGISWGPIGAAIACLDEALGY 268
Cdd:PRK12341 189 SKPGIKINPL-HKIGWHMLSTCEVYLDNVEVEESDLV----GEEGMgflnvMYNFEMERLINAARSLGFAECAFEDAARY 263

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896565479 269 AKERVLFGRPLAATQSAQMKLAEMARRITTAQLLALQLGRLKEAGQLQPQQVSLAKWNNCRMAIDIARECRDLLGGAGIT 348
Cdd:PRK12341 264 ANQRIQFGKPIGHNQLIQEKLTLMAIKIENMRNMVYKVAWQADNGQSLRTSAALAKLYCARTAMEVIDDAIQIMGGLGYT 343


                 ...
gi 896565479 349 TEH 351
Cdd:PRK12341 344 DEA 346
PRK03354 PRK03354
crotonobetainyl-CoA dehydrogenase; Validated
 47-380 1.73e-25

crotonobetainyl-CoA dehydrogenase; Validated


Pssm-ID: 179566 [Multi-domain]  Cd Length: 380  Bit Score: 106.07  E-value: 1.73e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896565479  47 FPSELVPEIAALGLLGATLPAEYGGGDLGAVSYGLICQELerGDSGLRSFVSVQSSLCMYPIYAYGSEEQRQQWLPAMAR 126
Cdd:PRK03354  38 YPERFVKALADMGIDSLLIPEEHGGLDAGFVTLAAVWMEL--GRLGAPTYVLYQLPGGFNTFLREGTQEQIDKIMAFRGT 115

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896565479 127 GELIGCFGLTEAHGGSDPASMKTRAVRDGSDWRISGSKMWITSGPVADLAIVWAQTEDG-----IQGFVLEKGMAGFTTQ 201
Cdd:PRK03354 116 GKQMWNSAITEPGAGSDVGSLKTTYTRRNGKVYLNGSKCFITSSAYTPYIVVMARDGASpdkpvYTEWFVDMSKPGIKVT 195

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896565479 202 EIkHKMSLRASLTGALFFDDVRVPDSHRL-PNVKGLKGPLGCLTQARYGISWGPIGAAIACLDEALGYAKERVLFGRPLA 280
Cdd:PRK03354 196 KL-EKLGLRMDSCCEITFDDVELDEKDMFgREGNGFNRVKEEFDHERFLVALTNYGTAMCAFEDAARYANQRVQFGEAIG 274

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896565479 281 ATQSAQMKLAEMARRITTAQLLALQLGRLKEAGQLQPQQVSLAKWNNCRMAIDIARECRDLLGGAGITTEHVAIRHALNL 360
Cdd:PRK03354 275 RFQLIQEKFAHMAIKLNSMKNMLYEAAWKADNGTITSGDAAMCKYFCANAAFEVVDSAMQVLGGVGIAGNHRISRFWRDL 354

                        330       340
                 ....*....|....*....|
gi 896565479 361 ESVITYEGTETVHQLVIGRE 380
Cdd:PRK03354 355 RVDRVSGGSDEMQILTLGRA 374
AidB cd01154
Proteins involved in DNA damage response, similar to the AidB gene product; AidB is one of ...
 106-375 1.87e-25

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: 106.69  E-value: 1.87e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896565479 106 YPIYAYGSEEQrQQWLPAMA----RGELIGCFGLTEAHGGSDPASMKTRAVRDGSD-WRISGSKmWITSGPVADLAIVWA 180
Cdd:cd01154  121 YALRKYGPEEL-KQYLPGLLsdryKTGLLGGTWMTEKQGGSDLGANETTAERSGGGvYRLNGHK-WFASAPLADAALVLA 198

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896565479 181 QTED------GIQGF----VLEKG-MAGFTTQEIKHKMSLRASLTGALFFDDVrvpDSHRL-PNVKGLKGPLGCLTQARY 248
Cdd:cd01154  199 RPEGapagarGLSLFlvprLLEDGtRNGYRIRRLKDKLGTRSVATGEVEFDDA---EAYLIgDEGKGIYYILEMLNISRL 275

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896565479 249 GISWGPIGAAIACLDEALGYAKERVLFGRPLAATQSAQMKLAEMARRITTAQLLALQLGRL-KEAGQLQPQQ-------V 320
Cdd:cd01154  276 DNAVAALGIMRRALSEAYHYARHRRAFGKPLIDHPLMRRDLAEMEVDVEAATALTFRAARAfDRAAADKPVEahmarlaT 355

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 896565479 321 SLAKWNNCRMAIDIARECRDLLGGAGITTEHVAIRhaLNLESVIT--YEGTETVHQL 375
Cdd:cd01154  356 PVAKLIACKRAAPVTSEAMEVFGGNGYLEEWPVAR--LHREAQVTpiWEGTGNIQAL 410
ACAD_FadE2 cd01155
Acyl-CoA dehydrogenases similar to fadE2; FadE2-like Acyl-CoA dehydrogenase (ACAD). Acyl-CoA ...
 21-379 1.10e-22

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: 98.23  E-value: 1.10e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896565479  21 AVQESVARFTNERVLPIIGDAFDQARF---PSELVPEI--------AALGLLGATLPAEYGGGDLGAVSYGLICQELERg 89
Cdd:cd01155    5 ELRARVKAFMEEHVYPAEQEFLEYYAEggdRWWTPPPIieklkakaKAEGLWNLFLPEVSGLSGLTNLEYAYLAEETGR- 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896565479  90 dsglrSFVSVQSSLCMYP-------IYAYGSEEQRQQWLPAMARGELIGCFGLTEAH-GGSDPASMKTRAVRDGSDWRIS 161
Cdd:cd01155   84 -----SFFAPEVFNCQAPdtgnmevLHRYGSEEQKKQWLEPLLDGKIRSAFAMTEPDvASSDATNIECSIERDGDDYVIN 158

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896565479 162 GSKmWITSG---PVADLAIVWAQTE-DG---------------IQGFVLEKGMAGFTTQEIKHKMslrasltGALFFDDV 222
Cdd:cd01155  159 GRK-WWSSGagdPRCKIAIVMGRTDpDGaprhrqqsmilvpmdTPGVTIIRPLSVFGYDDAPHGH-------AEITFDNV 230

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896565479 223 RVPDShrlpNVKGLKGPLGCLTQARYgiswGP---------IGAAIACLDEALGYAKERVLFGRPLAATQSAQMKLAEMA 293
Cdd:cd01155  231 RVPAS----NLILGEGRGFEIAQGRL----GPgrihhcmrlIGAAERALELMCQRAVSREAFGKKLAQHGVVAHWIAKSR 302

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896565479 294 RRITTAQLLALQLGRL------KEAgqlqPQQVSLAKWNNCRMAIDIARECRDLLGGAGITTEHVAIRHALNLESVITYE 367
Cdd:cd01155  303 IEIEQARLLVLKAAHMidtvgnKAA----RKEIAMIKVAAPRMALKIIDRAIQVHGAAGVSQDTPLANMYAWARTLRIAD 378

                        410
                 ....*....|..
gi 896565479 368 GTETVHQLVIGR 379
Cdd:cd01155  379 GPDEVHLRSIAR 390
NcnH cd01159
Naphthocyclinone hydroxylase; Naphthocyclinone is an aromatic polyketide and an antibiotic, ...
 32-360 1.09e-14

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: 74.69  E-value: 1.09e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896565479  32 ERVLPIIGDA---FDQAR-FPSELVPEIAALGLLGATLPAEYGGGDLGAVSYGLICQELERGDSglrSFVSVQSSLCMYP 107
Cdd:cd01159    4 EDLAPLIRERapeAERARrLPDEVVRALREIGFFRMFVPKRYGGLEGDFAEFAEAIATLAEACG---SAAWVASIVATHS 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896565479 108 IYAygseeqrqQWLPAMARGELIGCFGLTEAHGGSDPasmKTRAVRDGSDWRISGSKMWITSGPVADLAIVWAQTEDG-- 185
Cdd:cd01159   81 RML--------AAFPPEAQEEVWGDGPDTLLAGSYAP---GGRAERVDGGYRVSGTWPFASGCDHADWILVGAIVEDDdg 149

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896565479 186 ---IQGFVLEKgmAGFTTQEIKHKMSLRASLTGALFFDDVRVPDSHRLPNVKGLKGPLGCLTQARYGISWGP-------- 254
Cdd:cd01159  150 gplPRAFVVPR--AEYEIVDTWHVVGLRGTGSNTVVVDDVFVPEHRTLTAGDMMAGDGPGGSTPVYRMPLRQvfplsfaa 227

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896565479 255 --IGAAIACLDEALGYAKERVL---FGRPLAATQSAQMKLAEMARRITTAQLLALQLGRLKEAGQLQPQQVSLAKWNNCR 329
Cdd:cd01159  228 vsLGAAEGALAEFLELAGKRVRqygAAVKMAEAPITQLRLAEAAAELDAARAFLERATRDLWAHALAGGPIDVEERARIR 307

                        330       340       350       360
                 ....*....|....*....|....*....|....*....|....*....
gi 896565479 330 --------MAIDIARECRDLLGGAGITTE----------HVAIRHALNL 360
Cdd:cd01159  308 rdaayaakLSAEAVDRLFHAAGGSALYTAsplqriwrdiHAAAQHAALN 356
PTZ00456 PTZ00456
acyl-CoA dehydrogenase; Provisional
 59-272 1.21e-14

acyl-CoA dehydrogenase; Provisional


Pssm-ID: 185635 [Multi-domain]  Cd Length: 622  Bit Score: 75.29  E-value: 1.21e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896565479  59 GLLGATLPAEYGGGDLgAVSYGLICQELERGDSGLRSFVSVQSSLCMYPIYAYGSEEQRQQWLPAMARGELIGCFGLTEA 138
Cdd:PTZ00456 112 GWTGISEPEEYGGQAL-PLSVGFITRELMATANWGFSMYPGLSIGAANTLMAWGSEEQKEQYLTKLVSGEWSGTMCLTEP 190

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896565479 139 HGGSDPASMKTRAVR--DGSdWRISGSKMWITSGPvADLA-----IVWAQTEDGIQGfvlEKGMAGF------------- 198
Cdd:PTZ00456 191 QCGTDLGQVKTKAEPsaDGS-YKITGTKIFISAGD-HDLTenivhIVLARLPNSLPT---TKGLSLFlvprhvvkpdgsl 265

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896565479 199 -TTQEIK-----HKMSLRASLTGALFFDD-----VRVPDshrlpnvKGLKGPLGCLTQARYGISWGPIGAAIACLDEALG 267
Cdd:PTZ00456 266 eTAKNVKcigleKKMGIKGSSTCQLSFENsvgylIGEPN-------AGMKQMFTFMNTARVGTALEGVCHAELAFQNALR 338


                 ....*
gi 896565479 268 YAKER 272
Cdd:PTZ00456 339 YARER 343
PRK13026 PRK13026
acyl-CoA dehydrogenase; Reviewed
 111-347 2.22e-14

acyl-CoA dehydrogenase; Reviewed


Pssm-ID: 237277 [Multi-domain]  Cd Length: 774  Bit Score: 74.61  E-value: 2.22e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896565479 111 YGSEEQRQQWLPAMARGELIGCFGLTEAHGGSDPASMK-----TRAVRDGSD---WRISGSKMWITSGPVAD---LAiVW 179
Cdd:PRK13026 174 YGTQEQKDYWLPRLADGTEIPCFALTGPEAGSDAGAIPdtgivCRGEFEGEEvlgLRLTWDKRYITLAPVATvlgLA-FK 252

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896565479 180 AQTEDGIQGfvlEKGMAGFTTQEI-----------KHKMSLRASLTGALFFDDVRVPdshrLPNVKGlkGP--------- 239
Cdd:PRK13026 253 LRDPDGLLG---DKKELGITCALIptdhpgveigrRHNPLGMAFMNGTTRGKDVFIP----LDWIIG--GPdyagrgwrm 323

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896565479 240 -LGCLTQARyGISWGPIGAAIA--CLDEALGYAKERVLFGRPLAATQSAQMKLAEMA---------RRITTAqllALQLG 307
Cdd:PRK13026 324 lVECLSAGR-GISLPALGTASGhmATRTTGAYAYVRRQFGMPIGQFEGVQEALARIAgntylleaaRRLTTT---GLDLG 399

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|.
gi 896565479 308 rlkeagqLQPQQVS-LAKWNNCRMAIDIARECRDLLGGAGI 347
Cdd:PRK13026 400 -------VKPSVVTaIAKYHMTELARDVVNDAMDIHAGKGI 433
AXO cd01150
Peroxisomal acyl-CoA oxidase; Peroxisomal acyl-CoA oxidases (AXO) catalyze the first set in ...
 86-372 9.53e-14

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: 72.75  E-value: 9.53e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896565479  86 LERGDSGLRSFVSVQSSLCMYPIYAYGSEEQRQQWLPAMARGELIGCFGLTEAHGGSDPASMKTRAVRDGSDWR------ 159
Cdd:cd01150   91 LGGYDLSLGAKLGLHLGLFGNAIKNLGTDEHQDYWLQGANNLEIIGCFAQTELGHGSNLQGLETTATYDPLTQEfvintp 170

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896565479 160 -ISGSKMWITS-GPVADLAIVWAQ--TED---GIQGFVLE-------KGMAGFTTQEIKHKMSLRASLTGALFFDDVRVP 225
Cdd:cd01150  171 dFTATKWWPGNlGKTATHAVVFAQliTPGknhGLHAFIVPirdpkthQPLPGVTVGDIGPKMGLNGVDNGFLQFRNVRIP 250

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896565479 226 DSHRL-----------------PNVKGLKGPLGCLTQARYGISWGPIGAAIACLDEALGYAKERVLFGRP---------- 278
Cdd:cd01150  251 RENLLnrfgdvspdgtyvspfkDPNKRYGAMLGTRSGGRVGLIYDAAMSLKKAATIAIRYSAVRRQFGPKpsdpevqild 330

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896565479 279 -----------LAAT---QSAQMKLAEMARRITTaQLLALQLGRLKEAGQLQPQQVSLAKWnNCRMAIDiarECRDLLGG 344
Cdd:cd01150  331 yqlqqyrlfpqLAAAyafHFAAKSLVEMYHEIIK-ELLQGNSELLAELHALSAGLKAVATW-TAAQGIQ---ECREACGG 405

                        330       340       350
                 ....*....|....*....|....*....|....*..
gi 896565479 345 AG---------ITTEHVAirhalnlesVITYEGTETV 372
Cdd:cd01150  406 HGylamnrlptLRDDNDP---------FCTYEGDNTV 433
fadE PRK09463
acyl-CoA dehydrogenase; Reviewed
 59-173 1.74e-12

acyl-CoA dehydrogenase; Reviewed


Pssm-ID: 236528 [Multi-domain]  Cd Length: 777  Bit Score: 69.07  E-value: 1.74e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896565479  59 GLLGATLPAEYGGGDLGAVSYGLICQELERGDSGLRSFVSVQSSL-----CMYpiyaYGSEEQRQQWLPAMARGELIGCF 133
Cdd:PRK09463 122 GFFGMIIPKEYGGLEFSAYAHSRVLQKLASRSGTLAVTVMVPNSLgpgelLLH----YGTDEQKDHYLPRLARGEEIPCF 197

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*...
gi 896565479 134 GLTEAHGGSDPASMKTRAVRDGSDW--------RISGSKMWITSGPVA 173
Cdd:PRK09463 198 ALTSPEAGSDAGSIPDTGVVCKGEWqgeevlgmRLTWNKRYITLAPIA 245
DszC cd01163
Dibenzothiophene (DBT) desulfurization enzyme C; DszC is a flavin reductase dependent enzyme, ...
 43-309 5.03e-12

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: 66.58  E-value: 5.03e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896565479  43 DQAR-FPSELVPEIAALGLLGATLPAEYGGgdLGA---VSYGLIcQELERGDSGLR-------SFVSVqsslcmypIYAY 111
Cdd:cd01163   18 DRQRgLPYEEVALLRQSGLGTLRVPKEYGG--LGAslpDLYEVV-RELAAADSNIAqalrahfGFVEA--------LLLA 86

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896565479 112 GSEEQRQQWLPAMARGELIGCfGLTEaHGGSDPASMKTRAVRDGSDWRISGSKMWITSGPVADLAIVWAQTEDGIQ-GFV 190
Cdd:cd01163   87 GPEQFRKRWFGRVLNGWIFGN-AVSE-RGSVRPGTFLTATVRDGGGYVLNGKKFYSTGALFSDWVTVSALDEEGKLvFAA 164

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896565479 191 LEKGMAGFTTQEIKHKMSLRASLTGALFFDDVRVPDSHRLPNVKGLKGPLGCLTQARYGISWGPIGAAIACLDEALGYAK 270
Cdd:cd01163  165 VPTDRPGITVVDDWDGFGQRLTASGTVTFDNVRVEPDEVLPRPNAPDRGTLLTAIYQLVLAAVLAGIARAALDDAVAYVR 244

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*..
gi 896565479 271 ERvlfGRP---LAATQSA-----QMKLAEMARRITTAQLLALQLGRL 309
Cdd:cd01163  245 SR---TRPwihSGAESARddpyvQQVVGDLAARLHAAEALVLQAARA 288
PRK11561 PRK11561
isovaleryl CoA dehydrogenase; Provisional
 126-346 2.77e-09

isovaleryl CoA dehydrogenase; Provisional


Pssm-ID: 183199 [Multi-domain]  Cd Length: 538  Bit Score: 58.61  E-value: 2.77e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896565479 126 RGELIGcFGLTEAHGGSDPASMKTRAVR-DGSDWRISGSKmWITSGPVADLAIVWAQTEDGIQGFVLEKGMAGFTTQEI- 203
Cdd:PRK11561 176 RGLLIG-MGMTEKQGGSDVLSNTTRAERlADGSYRLVGHK-WFFSVPQSDAHLVLAQAKGGLSCFFVPRFLPDGQRNAIr 253

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896565479 204 ----KHKMSLRASLTGALFFDDVrvpdSHRLPNVKG------LKgpLGCLTqaRYGISWGPIGAAIACLDEALGYAKERV 273
Cdd:PRK11561 254 lerlKDKLGNRSNASSEVEFQDA----IGWLLGEEGegirliLK--MGGMT--RFDCALGSHGLMRRAFSVAIYHAHQRQ 325

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896565479 274 LFGRPLAATQSAQMKLAEMARRITTAQLLALQLGRLKEAgQLQPQQVSL-------AKWNNCRMAIDIARECRDLLGGAG 346
Cdd:PRK11561 326 VFGKPLIEQPLMRQVLSRMALQLEGQTALLFRLARAWDR-RADAKEALWarlftpaAKFVICKRGIPFVAEAMEVLGGIG 404
Acyl-CoA_dh_2 pfam08028
Acyl-CoA dehydrogenase, C-terminal domain;
255-356 1.26e-08

Acyl-CoA dehydrogenase, C-terminal domain;


Pssm-ID: 429790 [Multi-domain]  Cd Length: 133  Bit Score: 53.12  E-value: 1.26e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896565479  255 IGAAIACLDEALGYAKERVL--FGRPLAATQSAQMKLAEMARRITTAQLLALQLGRLKEAGQLQPQQVSLAKWNNCRMA- 331
Cdd:pfam08028   7 LGAARAALAEFTERARGRVRayFGVPLAEDPATQLALAEAAARIDAARLLLERAAARIEAAAAAGKPVTPALRAEARRAa 86

                          90       100       110
                  ....*....|....*....|....*....|..
gi 896565479  332 -------IDIARECRDLLGGAGITTEHVAIRH 356
Cdd:pfam08028  87 afatelaVAAVDALFRAAGGSALFQDSPLQRI 118
PLN02636 PLN02636
acyl-coenzyme A oxidase
 99-292 2.64e-08

acyl-coenzyme A oxidase


Pssm-ID: 215342 [Multi-domain]  Cd Length: 686  Bit Score: 55.63  E-value: 2.64e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896565479  99 VQSSLCMYPIYAYGSEEQRQQWLPAMARGELIGCFGLTEAHGGSDPASMKTRAVRD--GSDWRIS-----GSKMWITSGP 171
Cdd:PLN02636 143 VQYSLWGGSVINLGTKKHRDKYFDGIDNLDYPGCFAMTELHHGSNVQGLQTTATFDplTDEFVINtpndgAIKWWIGNAA 222

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896565479 172 V-ADLAIVWAQ-----------TEDGIQGFVL-------EKGMAGFTTQEIKHKMSLRASLTGALFFDDVRVP------- 225
Cdd:PLN02636 223 VhGKFATVFARlklpthdskgvSDMGVHAFIVpirdmktHQVLPGVEIRDCGHKVGLNGVDNGALRFRSVRIPrdnllnr 302

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896565479 226 --DSHR-------LPNV-KGLKGPLGCLTQARYGISWGPIGAAIACLDEALGYAKERVLFGRP------LAATQSAQMKL 289
Cdd:PLN02636 303 fgDVSRdgkytssLPTInKRFAATLGELVGGRVGLAYGSVGVLKASNTIAIRYSLLRQQFGPPkqpeisILDYQSQQHKL 382


                 ...
gi 896565479 290 AEM 292
Cdd:PLN02636 383 MPM 385
PLN02443 PLN02443
acyl-coenzyme A oxidase
 108-230 5.35e-08

acyl-coenzyme A oxidase


Pssm-ID: 178062 [Multi-domain]  Cd Length: 664  Bit Score: 54.84  E-value: 5.35e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896565479 108 IYAYGSEEQRQQWLPAMARGELIGCFGLTEAHGGSDPASMKTRAVRD-GSDWRI------SGSKMWITS-GPVADLAIVW 179
Cdd:PLN02443 110 IKGQGTEEQQKKWLPLAYKMQIIGCYAQTELGHGSNVQGLETTATFDpKTDEFVihsptlTSSKWWPGGlGKVSTHAVVY 189

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 896565479 180 AQ-----TEDGIQGFVLE-------KGMAGFTTQEIKHKMSLRASLT---GALFFDDVRVPDSHRL 230
Cdd:PLN02443 190 ARlitngKDHGIHGFIVQlrslddhSPLPGVTVGDIGMKFGNGAYNTmdnGFLRFDHVRIPRDQML 255
PTZ00457 PTZ00457
acyl-CoA dehydrogenase; Provisional
 60-164 3.11e-07

acyl-CoA dehydrogenase; Provisional


Pssm-ID: 185636 [Multi-domain]  Cd Length: 520  Bit Score: 52.19  E-value: 3.11e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896565479  60 LLGATLPAEYGGGDLGAVSYGLICQEL-ERGDSGLRSFVSvQSSLCMYPIYAYGSEEQRQQWLPAMARGELIGCFGLTEA 138
Cdd:PTZ00457  65 LYGARIATEYGGLGLGHTAHALIYEEVgTNCDSKLLSTIQ-HSGFCTYLLSTVGSKELKGKYLTAMSDGTIMMGWATEEG 143

                         90       100
                 ....*....|....*....|....*..
gi 896565479 139 HgGSDPASMKTRAV-RDGSDWRISGSK 164
Cdd:PTZ00457 144 C-GSDISMNTTKASlTDDGSYVLTGQK 169
PTZ00460 PTZ00460
acyl-CoA dehydrogenase; Provisional
 112-225 2.23e-06

acyl-CoA dehydrogenase; Provisional


Pssm-ID: 185639 [Multi-domain]  Cd Length: 646  Bit Score: 49.46  E-value: 2.23e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896565479 112 GSEEQRQQWLPAMARGELIGCFGLTEAHGGSDPASMKTRAVRD--GSDW-----RISGSKMWITS-GPVADLAIVWAQ-- 181
Cdd:PTZ00460 110 GTDEQINLWMPSLLNFEIVGCYAQTELGHGSDVQNLETTATYDkqTNEFvihtpSVEAVKFWPGElGFLCNFALVYAKli 189

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....
gi 896565479 182 ---TEDGIQGFVLE-------KGMAGFTTQEIKHKMSLRASLTGALFFDDVRVP 225
Cdd:PTZ00460 190 vngKNKGVHPFMVRirdkethKPLQGVEVGDIGPKMGYAVKDNGFLSFDHYRIP 243
PLN02876 PLN02876
acyl-CoA dehydrogenase
 42-352 5.90e-06

acyl-CoA dehydrogenase


Pssm-ID: 215473 [Multi-domain]  Cd Length: 822  Bit Score: 48.25  E-value: 5.90e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896565479  42 FDQARFPSELVPEIAALGLLGATLPAEYGGGdLGAVSYGLICQELERgdsglrSFVSVQSSLC-------MYPIYAYGSE 114
Cdd:PLN02876 463 LDSAARARKLLFEDNKHMVSGDSADQLLGAG-LSNLEYGYLCEIMGR------SVWAPQVFNCgapdtgnMEVLLRYGNK 535

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896565479 115 EQRQQWLPAMARGELIGCFGLTEAH-GGSDPASMKTRAVRDGSDWRISGSKMWiTSG---PVADLAIVWAQTEDGI---- 186
Cdd:PLN02876 536 EQQLEWLIPLLEGKIRSGFAMTEPQvASSDATNIECSIRRQGDSYVINGTKWW-TSGamdPRCRVLIVMGKTDFNApkhk 614

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896565479 187 -QGFVLekgmAGFTTQEIKHKMSL-----------RASLTgalfFDDVRVPDSH-RLPNVKGLKGPLGCLTQARYGISWG 253
Cdd:PLN02876 615 qQSMIL----VDIQTPGVQIKRPLlvfgfddaphgHAEIS----FENVRVPAKNiLLGEGRGFEIAQGRLGPGRLHHCMR 686

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896565479 254 PIGAAIACLDEALGYAKERVLFGRPLAATQSAQMKLAEMARRITTAQLLAL----QLGRL---KEAGQLqpqqvSLAKWN 326
Cdd:PLN02876 687 LIGAAERGMQLMVQRALSRKAFGKLIAQHGSFLSDLAKCRVELEQTRLLVLeaadQLDRLgnkKARGII-----AMAKVA 761

                        330       340
                 ....*....|....*....|....*.
gi 896565479 327 NCRMAIDIARECRDLLGGAGITTEHV 352
Cdd:PLN02876 762 APNMALKVLDMAMQVHGAAGVSSDTV 787
PLN02312 PLN02312
acyl-CoA oxidase
 112-233 2.75e-04

acyl-CoA oxidase


Pssm-ID: 215178 [Multi-domain]  Cd Length: 680  Bit Score: 42.84  E-value: 2.75e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896565479 112 GSEEQRQQWLPAMARGELIGCFGLTEAHGGSDPASMKTRAVRDGS--DWRI-----SGSKMWItsGPVADLA---IVWAQ 181
Cdd:PLN02312 168 GTKRHHDKWLKDTEDYVVKGCFAMTELGHGSNVRGIETVTTYDPKteEFVIntpceSAQKYWI--GGAANHAthtIVFSQ 245

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 896565479 182 -----TEDGIQGFVLE------KGMAGFTTQEIKHKMSLRASLTGALFFDDVRVPDSHRLPNV 233
Cdd:PLN02312 246 lhingKNEGVHAFIAQirdqdgNICPNIRIADCGHKIGLNGVDNGRIWFDNLRIPRENLLNSV 308
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
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