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Conserved domains on  [gi|394025723|ref|NP_001257376|]
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very long-chain specific acyl-CoA dehydrogenase, mitochondrial isoform 3 [Homo sapiens]

Protein Classification

acyl-CoA dehydrogenase family protein( domain architecture ID 10100190)

acyl-CoA dehydrogenase (ACAD) family protein similar to mitochondrial very long-chain specific acyl-CoA dehydrogenase (VLCAD), which is one of the acyl-CoA dehydrogenases that catalyze the first step of mitochondrial fatty acid beta-oxidation, an aerobic process breaking down fatty acids into acetyl-CoA and allowing the production of energy from fats

CATH:  1.10.540.10
EC:  1.3.8.-
Gene Ontology:  GO:0016627|GO:0006631|GO:0050660
PubMed:  10760462|12504675
SCOP:  3001580|3001701

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
VLCAD cd01161
Very long chain acyl-CoA dehydrogenase; VLCAD is an acyl-CoA dehydrogenase (ACAD), which is ...
 95-504 0e+00

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: 750.07  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 394025723  95 SFAVGMFKGQLTTDQVFPYPSVLNEEQTQFLKELVEPVSRFFEEVNDPAKNDALEMVEETTWQGLKELGAFGLQVPSELG 174
Cdd:cd01161    1 SFALNMFLGDIVTKQVFPYPSVLTEEQTEELNMLVGPVEKFFEEVNDPAKNDQLEKIPRKTLTQLKELGLFGLQVPEEYG 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 394025723 175 GVGLCNTQYARLVEIVGMhDLGVGITLGAHQSIGFKGILLFGTKAQKEKYLPKLASGETVAAFCLTEPSSGSDAASIRTS 254
Cdd:cd01161   81 GLGLNNTQYARLAEIVGM-DLGFSVTLGAHQSIGFKGILLFGTEAQKEKYLPKLASGEWIAAFALTEPSSGSDAASIRTT 159

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 394025723 255 AVPSPCGKYYTLNGSKLWISNGGLADIFTVFAKTPVTDPaTGAVKEKITAFVVERGFGGITHGPPEKKMGIKASNTAEVF 334
Cdd:cd01161  160 AVLSEDGKHYVLNGSKIWITNGGIADIFTVFAKTEVKDA-TGSVKDKITAFIVERSFGGVTNGPPEKKMGIKGSNTAEVY 238

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 394025723 335 FDGVRVPSENVLGEVGSGFKVAMHILNNGRFGMAAALAGTMRGIIAKAVDHATNRTQFGEKIHNFGLIQEKLARMVMLQY 414
Cdd:cd01161  239 FEDVKIPVENVLGEVGDGFKVAMNILNNGRFGMGAALIGTMKRCIEKAVDYANNRKQFGKKIHEFGLIQEKLANMAILQY 318

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 394025723 415 VTESMAYMVSANMDQGAT-DFQIEAAISKIFGSEAAWKVTDECIQIMGGMGFMKEPGVERVLRDLRIFRIFEGTNDILRL 493
Cdd:cd01161  319 ATESMAYMTSGNMDRGLKaEYQIEAAISKVFASEAAWLVVDEAIQIHGGMGFMREYGVERVLRDLRIFRIFEGTNEILRL 398

                        410
                 ....*....|.
gi 394025723 494 FVALQGCMDKG 504
Cdd:cd01161  399 FIALTGLQHAG 409
 
Name Accession Description Interval E-value
VLCAD cd01161
Very long chain acyl-CoA dehydrogenase; VLCAD is an acyl-CoA dehydrogenase (ACAD), which is ...
 95-504 0e+00

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: 750.07  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 394025723  95 SFAVGMFKGQLTTDQVFPYPSVLNEEQTQFLKELVEPVSRFFEEVNDPAKNDALEMVEETTWQGLKELGAFGLQVPSELG 174
Cdd:cd01161    1 SFALNMFLGDIVTKQVFPYPSVLTEEQTEELNMLVGPVEKFFEEVNDPAKNDQLEKIPRKTLTQLKELGLFGLQVPEEYG 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 394025723 175 GVGLCNTQYARLVEIVGMhDLGVGITLGAHQSIGFKGILLFGTKAQKEKYLPKLASGETVAAFCLTEPSSGSDAASIRTS 254
Cdd:cd01161   81 GLGLNNTQYARLAEIVGM-DLGFSVTLGAHQSIGFKGILLFGTEAQKEKYLPKLASGEWIAAFALTEPSSGSDAASIRTT 159

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 394025723 255 AVPSPCGKYYTLNGSKLWISNGGLADIFTVFAKTPVTDPaTGAVKEKITAFVVERGFGGITHGPPEKKMGIKASNTAEVF 334
Cdd:cd01161  160 AVLSEDGKHYVLNGSKIWITNGGIADIFTVFAKTEVKDA-TGSVKDKITAFIVERSFGGVTNGPPEKKMGIKGSNTAEVY 238

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 394025723 335 FDGVRVPSENVLGEVGSGFKVAMHILNNGRFGMAAALAGTMRGIIAKAVDHATNRTQFGEKIHNFGLIQEKLARMVMLQY 414
Cdd:cd01161  239 FEDVKIPVENVLGEVGDGFKVAMNILNNGRFGMGAALIGTMKRCIEKAVDYANNRKQFGKKIHEFGLIQEKLANMAILQY 318

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 394025723 415 VTESMAYMVSANMDQGAT-DFQIEAAISKIFGSEAAWKVTDECIQIMGGMGFMKEPGVERVLRDLRIFRIFEGTNDILRL 493
Cdd:cd01161  319 ATESMAYMTSGNMDRGLKaEYQIEAAISKVFASEAAWLVVDEAIQIHGGMGFMREYGVERVLRDLRIFRIFEGTNEILRL 398

                        410
                 ....*....|.
gi 394025723 494 FVALQGCMDKG 504
Cdd:cd01161  399 FIALTGLQHAG 409
CaiA COG1960
Acyl-CoA dehydrogenase related to the alkylation response protein AidB [Lipid transport and ...
 117-496 3.60e-135

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: 3.60e-135
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 394025723 117 LNEEQTQFLKElvepVSRFFEEVNDP--AKNDALEMVEETTWQGLKELGAFGLQVPSELGGVGLCNTQYARLVEIVGMHD 194
Cdd:COG1960    5 LTEEQRALRDE----VREFAEEEIAPeaREWDREGEFPRELWRKLAELGLLGLTIPEEYGGLGLSLVELALVLEELARAD 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 394025723 195 LGVGITLGAHQSIGfKGILLFGTKAQKEKYLPKLASGETVAAFCLTEPSSGSDAASIRTSAVPSpcGKYYTLNGSKLWIS 274
Cdd:COG1960   81 ASLALPVGVHNGAA-EALLRFGTEEQKERYLPRLASGEWIGAFALTEPGAGSDAAALRTTAVRD--GDGYVLNGQKTFIT 157

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 394025723 275 NGGLADIFTVFAKTpvtDPATGAvkEKITAFVVERGFGGITHGPPEKKMGIKASNTAEVFFDGVRVPSENVLGEVGSGFK 354
Cdd:COG1960  158 NAPVADVILVLART---DPAAGH--RGISLFLVPKDTPGVTVGRIEDKMGLRGSDTGELFFDDVRVPAENLLGEEGKGFK 232

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 394025723 355 VAMHILNNGRFGMAAALAGTMRGIIAKAVDHATNRTQFGEKIHNFGLIQEKLARMVMLQYVTESMAYMVSANMDQGAtDF 434
Cdd:COG1960  233 IAMSTLNAGRLGLAAQALGIAEAALELAVAYAREREQFGRPIADFQAVQHRLADMAAELEAARALVYRAAWLLDAGE-DA 311

                        330       340       350       360       370       380
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 394025723 435 QIEAAISKIFGSEAAWKVTDECIQIMGGMGFMKEPGVERVLRDLRIFRIFEGTNDILRLFVA 496
Cdd:COG1960  312 ALEAAMAKLFATEAALEVADEALQIHGGYGYTREYPLERLYRDARILTIYEGTNEIQRLIIA 373
PLN02519 PLN02519
isovaleryl-CoA dehydrogenase
 119-495 1.70e-65

isovaleryl-CoA dehydrogenase


Pssm-ID: 215284 [Multi-domain]  Cd Length: 404  Bit Score: 221.67  E-value: 1.70e-65
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 394025723 119 EEQTQFLKELVEPVSRFFEEVNDPAKNDALemveettWQGLKELGAFGLQVPSELGGVGLCNTQYARLVEIVGMHDLGVG 198
Cdd:PLN02519  35 ESVQQFAQENIAPHAAAIDATNSFPKDVNL-------WKLMGDFNLHGITAPEEYGGLGLGYLYHCIAMEEISRASGSVG 107

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 394025723 199 ITLGAHQSIGFKGILLFGTKAQKEKYLPKLASGETVAAFCLTEPSSGSDAASIRTSAVPSPCGkyYTLNGSKLWISNGGL 278
Cdd:PLN02519 108 LSYGAHSNLCINQLVRNGTPAQKEKYLPKLISGEHVGALAMSEPNSGSDVVSMKCKAERVDGG--YVLNGNKMWCTNGPV 185

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 394025723 279 ADIFTVFAKTpvtDPATGAvkEKITAFVVERGFGGITHGPPEKKMGIKASNTAEVFFDGVRVPSENVLGEVGSGFKVAMH 358
Cdd:PLN02519 186 AQTLVVYAKT---DVAAGS--KGITAFIIEKGMPGFSTAQKLDKLGMRGSDTCELVFENCFVPEENVLGQEGKGVYVMMS 260

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 394025723 359 ILNNGRFGMAAALAGTMRGIIAKAVDHATNRTQFGEKIHNFGLIQEKLARMVMLQYVTESMAYMVSANMDQGATDFQiEA 438
Cdd:PLN02519 261 GLDLERLVLAAGPLGLMQACLDVVLPYVRQREQFGRPIGEFQFIQGKLADMYTSLQSSRSYVYSVARDCDNGKVDRK-DC 339

                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 394025723 439 AISKIFGSEAAWKVTDECIQIMGGMGFMKEPGVERVLRDLRIFRIFEGTNDILRLFV 495
Cdd:PLN02519 340 AGVILCAAERATQVALQAIQCLGGNGYINEYPTGRLLRDAKLYEIGAGTSEIRRMLI 396
Acyl-CoA_dh_1 pfam00441
Acyl-CoA dehydrogenase, C-terminal domain; C-terminal domain of Acyl-CoA dehydrogenase is an ...
 350-496 8.09e-40

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: 143.16  E-value: 8.09e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 394025723  350 GSGFKVAMHILNNGRFGMAAALAGTMRGIIAKAVDHATNRTQFGEKIHNFGLIQEKLARMVMLQYVTESMAYMVSANMDQ 429
Cdd:pfam00441   1 GRGFRVAMETLNHERLAIAAMALGLARRALDEALAYARRRKAFGRPLIDFQLVRHKLAEMAAEIEAARLLVYRAAEALDA 80

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 394025723  430 GATDfQIEAAISKIFGSEAAWKVTDECIQIMGGMGFMKEPGVERVLRDLRIFRIFEGTNDILRLFVA 496
Cdd:pfam00441  81 GGPD-GAEASMAKLYASEAAVEVADLAMQLHGGYGYLREYPVERLYRDARVLRIGEGTSEIQRNIIA 146
 
Name Accession Description Interval E-value
VLCAD cd01161
Very long chain acyl-CoA dehydrogenase; VLCAD is an acyl-CoA dehydrogenase (ACAD), which is ...
 95-504 0e+00

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: 750.07  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 394025723  95 SFAVGMFKGQLTTDQVFPYPSVLNEEQTQFLKELVEPVSRFFEEVNDPAKNDALEMVEETTWQGLKELGAFGLQVPSELG 174
Cdd:cd01161    1 SFALNMFLGDIVTKQVFPYPSVLTEEQTEELNMLVGPVEKFFEEVNDPAKNDQLEKIPRKTLTQLKELGLFGLQVPEEYG 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 394025723 175 GVGLCNTQYARLVEIVGMhDLGVGITLGAHQSIGFKGILLFGTKAQKEKYLPKLASGETVAAFCLTEPSSGSDAASIRTS 254
Cdd:cd01161   81 GLGLNNTQYARLAEIVGM-DLGFSVTLGAHQSIGFKGILLFGTEAQKEKYLPKLASGEWIAAFALTEPSSGSDAASIRTT 159

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 394025723 255 AVPSPCGKYYTLNGSKLWISNGGLADIFTVFAKTPVTDPaTGAVKEKITAFVVERGFGGITHGPPEKKMGIKASNTAEVF 334
Cdd:cd01161  160 AVLSEDGKHYVLNGSKIWITNGGIADIFTVFAKTEVKDA-TGSVKDKITAFIVERSFGGVTNGPPEKKMGIKGSNTAEVY 238

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 394025723 335 FDGVRVPSENVLGEVGSGFKVAMHILNNGRFGMAAALAGTMRGIIAKAVDHATNRTQFGEKIHNFGLIQEKLARMVMLQY 414
Cdd:cd01161  239 FEDVKIPVENVLGEVGDGFKVAMNILNNGRFGMGAALIGTMKRCIEKAVDYANNRKQFGKKIHEFGLIQEKLANMAILQY 318

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 394025723 415 VTESMAYMVSANMDQGAT-DFQIEAAISKIFGSEAAWKVTDECIQIMGGMGFMKEPGVERVLRDLRIFRIFEGTNDILRL 493
Cdd:cd01161  319 ATESMAYMTSGNMDRGLKaEYQIEAAISKVFASEAAWLVVDEAIQIHGGMGFMREYGVERVLRDLRIFRIFEGTNEILRL 398

                        410
                 ....*....|.
gi 394025723 494 FVALQGCMDKG 504
Cdd:cd01161  399 FIALTGLQHAG 409
CaiA COG1960
Acyl-CoA dehydrogenase related to the alkylation response protein AidB [Lipid transport and ...
 117-496 3.60e-135

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: 3.60e-135
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 394025723 117 LNEEQTQFLKElvepVSRFFEEVNDP--AKNDALEMVEETTWQGLKELGAFGLQVPSELGGVGLCNTQYARLVEIVGMHD 194
Cdd:COG1960    5 LTEEQRALRDE----VREFAEEEIAPeaREWDREGEFPRELWRKLAELGLLGLTIPEEYGGLGLSLVELALVLEELARAD 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 394025723 195 LGVGITLGAHQSIGfKGILLFGTKAQKEKYLPKLASGETVAAFCLTEPSSGSDAASIRTSAVPSpcGKYYTLNGSKLWIS 274
Cdd:COG1960   81 ASLALPVGVHNGAA-EALLRFGTEEQKERYLPRLASGEWIGAFALTEPGAGSDAAALRTTAVRD--GDGYVLNGQKTFIT 157

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 394025723 275 NGGLADIFTVFAKTpvtDPATGAvkEKITAFVVERGFGGITHGPPEKKMGIKASNTAEVFFDGVRVPSENVLGEVGSGFK 354
Cdd:COG1960  158 NAPVADVILVLART---DPAAGH--RGISLFLVPKDTPGVTVGRIEDKMGLRGSDTGELFFDDVRVPAENLLGEEGKGFK 232

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 394025723 355 VAMHILNNGRFGMAAALAGTMRGIIAKAVDHATNRTQFGEKIHNFGLIQEKLARMVMLQYVTESMAYMVSANMDQGAtDF 434
Cdd:COG1960  233 IAMSTLNAGRLGLAAQALGIAEAALELAVAYAREREQFGRPIADFQAVQHRLADMAAELEAARALVYRAAWLLDAGE-DA 311

                        330       340       350       360       370       380
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 394025723 435 QIEAAISKIFGSEAAWKVTDECIQIMGGMGFMKEPGVERVLRDLRIFRIFEGTNDILRLFVA 496
Cdd:COG1960  312 ALEAAMAKLFATEAALEVADEALQIHGGYGYTREYPLERLYRDARILTIYEGTNEIQRLIIA 373
SCAD_SBCAD cd01158
Short chain acyl-CoA dehydrogenases and eukaryotic short/branched chain acyl-CoA ...
 119-496 8.25e-120

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: 362.36  E-value: 8.25e-120
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 394025723 119 EEQTQFLKElvepVSRFFEEVNDP--AKNDALEMVEETTWQGLKELGAFGLQVPSELGGVGLCNTQYARLVEIVGMHDLG 196
Cdd:cd01158    1 EEHQMIRKT----VRDFAEKEIAPlaAEMDEKGEFPREVIKEMAELGLMGIPIPEEYGGAGLDFLAYAIAIEELAKVDAS 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 394025723 197 VGITLGAHQSIGFKGILLFGTKAQKEKYLPKLASGETVAAFCLTEPSSGSDAASIRTSAVPSpcGKYYTLNGSKLWISNG 276
Cdd:cd01158   77 VAVIVSVHNSLGANPIIKFGTEEQKKKYLPPLATGEKIGAFALSEPGAGSDAAALKTTAKKD--GDDYVLNGSKMWITNG 154

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 394025723 277 GLADIFTVFAktpVTDPATGavKEKITAFVVERGFGGITHGPPEKKMGIKASNTAEVFFDGVRVPSENVLGEVGSGFKVA 356
Cdd:cd01158  155 GEADFYIVFA---VTDPSKG--YRGITAFIVERDTPGLSVGKKEDKLGIRGSSTTELIFEDVRVPKENILGEEGEGFKIA 229

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 394025723 357 MHILNNGRFGMAAALAGTMRGIIAKAVDHATNRTQFGEKIHNFGLIQEKLARMVMLQYVTESMAYMVSANMDQGaTDFQI 436
Cdd:cd01158  230 MQTLDGGRIGIAAQALGIAQAALDAAVDYAKERKQFGKPIADFQGIQFKLADMATEIEAARLLTYKAARLKDNG-EPFIK 308

                        330       340       350       360       370       380
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 394025723 437 EAAISKIFGSEAAWKVTDECIQIMGGMGFMKEPGVERVLRDLRIFRIFEGTNDILRLFVA 496
Cdd:cd01158  309 EAAMAKLFASEVAMRVTTDAVQIFGGYGYTKDYPVERYYRDAKITEIYEGTSEIQRLVIA 368
ACAD cd00567
Acyl-CoA dehydrogenase; Both mitochondrial acyl-CoA dehydrogenases (ACAD) and peroxisomal ...
 212-496 5.09e-103

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: 317.30  E-value: 5.09e-103
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 394025723 212 ILLFGTKAQKEKYLPKLASGETVAAFCLTEPSSGSDAASIRTSAVPSpcGKYYTLNGSKLWISNGGLADIFTVFAKTPVT 291
Cdd:cd00567   48 LLAYGTEEQKERYLPPLASGEAIAAFALTEPGAGSDLAGIRTTARKD--GDGYVLNGRKIFISNGGDADLFIVLARTDEE 125

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 394025723 292 DPATGAvkekITAFVVERGFGGITHGPPEKKMGIKASNTAEVFFDGVRVPSENVLGEVGSGFKVAMHILNNGRFGMAAAL 371
Cdd:cd00567  126 GPGHRG----ISAFLVPADTPGVTVGRIWDKMGMRGSGTGELVFDDVRVPEDNLLGEEGGGFELAMKGLNVGRLLLAAVA 201

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 394025723 372 AGTMRGIIAKAVDHATNRTQFGEKIHNFGLIQEKLARMVMLQYVTESMAYMVSANMDQGATDFQIEAAISKIFGSEAAWK 451
Cdd:cd00567  202 LGAARAALDEAVEYAKQRKQFGKPLAEFQAVQFKLADMAAELEAARLLLYRAAWLLDQGPDEARLEAAMAKLFATEAARE 281

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*
gi 394025723 452 VTDECIQIMGGMGFMKEPGVERVLRDLRIFRIFEGTNDILRLFVA 496
Cdd:cd00567  282 VADLAMQIHGGRGYSREYPVERYLRDARAARIAEGTAEIQRLIIA 326
IVD cd01156
Isovaleryl-CoA dehydrogenase; Isovaleryl-CoA dehydrogenase (IVD) is an is an acyl-CoA ...
 117-496 1.27e-90

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: 286.61  E-value: 1.27e-90
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 394025723 117 LNEEQTQflkeLVEPVSRFFEEVNDP--AKNDALEMVEETTWQGLKELGAFGLQVPSELGGVGLCNTQYARLVEIVGMHD 194
Cdd:cd01156    2 LDDEIEM----LRQSVREFAQKEIAPlaAKIDRDNEFPRDLWRKMGKLGLLGITAPEEYGGSGMGYLAHVIIMEEISRAS 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 394025723 195 LGVGITLGAHQSIGFKGILLFGTKAQKEKYLPKLASGETVAAFCLTEPSSGSDAASIRTSAvpSPCGKYYTLNGSKLWIS 274
Cdd:cd01156   78 GSVALSYGAHSNLCINQIYRNGSAAQKEKYLPKLISGEHIGALAMSEPNAGSDVVSMKLRA--EKKGDRYVLNGSKMWIT 155

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 394025723 275 NGGLADIFTVFAKTpvtDPATGAvkEKITAFVVERGFGGITHGPPEKKMGIKASNTAEVFFDGVRVPSENVLGEVGSGFK 354
Cdd:cd01156  156 NGPDADTLVVYAKT---DPSAGA--HGITAFIVEKGMPGFSRAQKLDKLGMRGSNTCELVFEDCEVPEENILGGENKGVY 230

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 394025723 355 VAMHILNNGRFGMAAALAGTMRGIIAKAVDHATNRTQFGEKIHNFGLIQEKLARMVMLQYVTESMAYMVSANMDQGATDf 434
Cdd:cd01156  231 VLMSGLDYERLVLAGGPIGIMQAALDVAIPYAHQRKQFGQPIGEFQLVQGKLADMYTRLNASRSYLYTVAKACDRGNMD- 309

                        330       340       350       360       370       380
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 394025723 435 QIEAAISKIFGSEAAWKVTDECIQIMGGMGFMKEPGVERVLRDLRIFRIFEGTNDILRLFVA 496
Cdd:cd01156  310 PKDAAGVILYAAEKATQVALDAIQILGGNGYINDYPTGRLLRDAKLYEIGAGTSEIRRMVIG 371
IBD cd01162
Isobutyryl-CoA dehydrogenase; Isobutyryl-CoA dehydrogenase (IBD) catalyzes the alpha, beta- ...
 161-496 8.51e-78

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: 253.13  E-value: 8.51e-78
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 394025723 161 ELGAFGLQVPSELGGVGLCNTQYARLVEIVGMHDLGVGITLGAHQSIGFKgILLFGTKAQKEKYLPKLASGETVAAFCLT 240
Cdd:cd01162   43 ELGFGGIYIRDDVGGSGLSRLDASIIFEALSTGCVSTAAYISIHNMCAWM-IDSFGNDEQRERFLPDLCTMEKLASYCLT 121

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 394025723 241 EPSSGSDAASIRTSAVPSpcGKYYTLNGSKLWISNGGLADIFTVFAKTpvtdpaTGAVKEKITAFVVERGFGGITHGPPE 320
Cdd:cd01162  122 EPGSGSDAAALRTRAVRE--GDHYVLNGSKAFISGAGDSDVYVVMART------GGEGPKGISCFVVEKGTPGLSFGANE 193

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 394025723 321 KKMGIKASNTAEVFFDGVRVPSENVLGEVGSGFKVAMHILNNGRFGMAAALAGTMRGIIAKAVDHATNRTQFGEKIHNFG 400
Cdd:cd01162  194 KKMGWNAQPTRAVIFEDCRVPVENRLGGEGQGFGIAMAGLNGGRLNIASCSLGAAQAALDLARAYLEERKQFGKPLADFQ 273

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 394025723 401 LIQEKLARMVMLQYVTESMAYMVSANMDQGATDFQIEAAISKIFGSEAAWKVTDECIQIMGGMGFMKEPGVERVLRDLRI 480
Cdd:cd01162  274 ALQFKLADMATELVASRLMVRRAASALDRGDPDAVKLCAMAKRFATDECFDVANQALQLHGGYGYLKDYPVEQYVRDLRV 353

                        330
                 ....*....|....*.
gi 394025723 481 FRIFEGTNDILRLFVA 496
Cdd:cd01162  354 HQILEGTNEIMRLIIA 369
LCAD cd01160
Long chain acyl-CoA dehydrogenase; LCAD is an acyl-CoA dehydrogenases (ACAD), which is found ...
 132-498 1.90e-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: 241.64  E-value: 1.90e-73
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 394025723 132 VSRFFEEVNDP--AKNDALEMVEETTWQGLKELGAFGLQVPSELGGVGLcNTQYARLVEIVGMHDLGVGITLGAHQSIGF 209
Cdd:cd01160   10 VRRFFAKEVAPfhHEWEKAGEVPREVWRKAGEQGLLGVGFPEEYGGIGG-DLLSAAVLWEELARAGGSGPGLSLHTDIVS 88

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 394025723 210 KGILLFGTKAQKEKYLPKLASGETVAAFCLTEPSSGSDAASIRTSAVPSpcGKYYTLNGSKLWISNGGLADIFTVFAKTp 289
Cdd:cd01160   89 PYITRAGSPEQKERVLPQMVAGKKIGAIAMTEPGAGSDLQGIRTTARKD--GDHYVLNGSKTFITNGMLADVVIVVART- 165

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 394025723 290 vTDPATGAvkEKITAFVVERGFGGITHGPPEKKMGIKASNTAEVFFDGVRVPSENVLGEVGSGFKVAMHILNNGRFGMAA 369
Cdd:cd01160  166 -GGEARGA--GGISLFLVERGTPGFSRGRKLKKMGWKAQDTAELFFDDCRVPAENLLGEENKGFYYLMQNLPQERLLIAA 242

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 394025723 370 ALAGTMRGIIAKAVDHATNRTQFGEKIHNFGLIQEKLARMVMLQYVTESMAYMVSANMDQGATDfQIEAAISKIFGSEAA 449
Cdd:cd01160  243 GALAAAEFMLEETRNYVKQRKAFGKTLAQLQVVRHKIAELATKVAVTRAFLDNCAWRHEQGRLD-VAEASMAKYWATELQ 321

                        330       340       350       360
                 ....*....|....*....|....*....|....*....|....*....
gi 394025723 450 WKVTDECIQIMGGMGFMKEPGVERVLRDLRIFRIFEGTNDILRLFVALQ 498
Cdd:cd01160  322 NRVAYECVQLHGGWGYMREYPIARAYRDARVQPIYGGTTEIMKELISRQ 370
PLN02519 PLN02519
isovaleryl-CoA dehydrogenase
 119-495 1.70e-65

isovaleryl-CoA dehydrogenase


Pssm-ID: 215284 [Multi-domain]  Cd Length: 404  Bit Score: 221.67  E-value: 1.70e-65
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 394025723 119 EEQTQFLKELVEPVSRFFEEVNDPAKNDALemveettWQGLKELGAFGLQVPSELGGVGLCNTQYARLVEIVGMHDLGVG 198
Cdd:PLN02519  35 ESVQQFAQENIAPHAAAIDATNSFPKDVNL-------WKLMGDFNLHGITAPEEYGGLGLGYLYHCIAMEEISRASGSVG 107

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 394025723 199 ITLGAHQSIGFKGILLFGTKAQKEKYLPKLASGETVAAFCLTEPSSGSDAASIRTSAVPSPCGkyYTLNGSKLWISNGGL 278
Cdd:PLN02519 108 LSYGAHSNLCINQLVRNGTPAQKEKYLPKLISGEHVGALAMSEPNSGSDVVSMKCKAERVDGG--YVLNGNKMWCTNGPV 185

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 394025723 279 ADIFTVFAKTpvtDPATGAvkEKITAFVVERGFGGITHGPPEKKMGIKASNTAEVFFDGVRVPSENVLGEVGSGFKVAMH 358
Cdd:PLN02519 186 AQTLVVYAKT---DVAAGS--KGITAFIIEKGMPGFSTAQKLDKLGMRGSDTCELVFENCFVPEENVLGQEGKGVYVMMS 260

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 394025723 359 ILNNGRFGMAAALAGTMRGIIAKAVDHATNRTQFGEKIHNFGLIQEKLARMVMLQYVTESMAYMVSANMDQGATDFQiEA 438
Cdd:PLN02519 261 GLDLERLVLAAGPLGLMQACLDVVLPYVRQREQFGRPIGEFQFIQGKLADMYTSLQSSRSYVYSVARDCDNGKVDRK-DC 339

                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 394025723 439 AISKIFGSEAAWKVTDECIQIMGGMGFMKEPGVERVLRDLRIFRIFEGTNDILRLFV 495
Cdd:PLN02519 340 AGVILCAAERATQVALQAIQCLGGNGYINEYPTGRLLRDAKLYEIGAGTSEIRRMLI 396
GCD cd01151
Glutaryl-CoA dehydrogenase; Glutaryl-CoA dehydrogenase (GCD). GCD is an acyl-CoA dehydrogenase, ...
 101-510 1.33e-63

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: 216.07  E-value: 1.33e-63
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 394025723 101 FKGQLTTDQVfpypsVLNEEQTQFLKELVEP--VSRFFEEVNDPakndalEMVEEttwqgLKELGAFGLQvPSELGGVGL 178
Cdd:cd01151    9 LDDLLTEEER-----AIRDTAREFCQEELAPrvLEAYREEKFDR------KIIEE-----MGELGLLGAT-IKGYGCAGL 71

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 394025723 179 CNTQY---ARLVEIVgmhDLGVGITLGAHQSIGFKGILLFGTKAQKEKYLPKLASGETVAAFCLTEPSSGSDAASIRTSA 255
Cdd:cd01151   72 SSVAYgliAREVERV---DSGYRSFMSVQSSLVMLPIYDFGSEEQKQKYLPKLASGELIGCFGLTEPNHGSDPGGMETRA 148

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 394025723 256 vpSPCGKYYTLNGSKLWISNGGLADIFTVFAKTPVTDpatgavkeKITAFVVERGFGGITHGPPEKKMGIKASNTAEVFF 335
Cdd:cd01151  149 --RKDGGGYKLNGSKTWITNSPIADVFVVWARNDETG--------KIRGFILERGMKGLSAPKIQGKFSLRASITGEIVM 218

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 394025723 336 DGVRVPSENVLGEVgSGFKVAMHILNNGRFGMAAALAGTMRGIIAKAVDHATNRTQFGEKIHNFGLIQEKLARM-VMLQY 414
Cdd:cd01151  219 DNVFVPEENLLPGA-EGLRGPFKCLNNARYGIAWGALGAAEDCYHTARQYVLDRKQFGRPLAAFQLVQKKLADMlTEIAL 297

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 394025723 415 VTEsMAYMVSANMDQG-ATDFQIeaAISKIFGSEAAWKVTDECIQIMGGMGFMKEPGVERVLRDLRIFRIFEGTNDILRL 493
Cdd:cd01151  298 GLL-ACLRVGRLKDQGkATPEQI--SLLKRNNCGKALEIARTAREMLGGNGISDEYHIIRHMVNLESVNTYEGTHDIHAL 374

                        410
                 ....*....|....*..
gi 394025723 494 FValqgcmdkGKELSGL 510
Cdd:cd01151  375 IL--------GRAITGI 383
MCAD cd01157
Medium chain acyl-CoA dehydrogenase; MCADs are mitochondrial beta-oxidation enzymes, which ...
 117-496 3.93e-63

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: 214.37  E-value: 3.93e-63
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 394025723 117 LNEEQtqflKELVEPVSRFFEEVNDPAKNDaLEMVEETTWQGLK---ELGAFGLQVPSELGGVGLCNTQYARLVEIVGMH 193
Cdd:cd01157    1 LTEQQ----KEFQETARKFAREEIIPVAAE-YDKSGEYPWPLIKrawELGLMNTHIPEDCGGLGLGTFDTCLITEELAYG 75

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 394025723 194 DLGVGITLGAHqSIGFKGILLFGTKAQKEKYLPKLASGETVAAFCLTEPSSGSDAASIRTSAVPSpcGKYYTLNGSKLWI 273
Cdd:cd01157   76 CTGVQTAIEAN-SLGQMPVIISGNDEQKKKYLGRMTEEPLMCAYCVTEPGAGSDVAGIKTKAEKK--GDEYIINGQKMWI 152

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 394025723 274 SNGGLADIFTVFAKTPvTDPATGAVKeKITAFVVERGFGGITHGPPEKKMGIKASNTAEVFFDGVRVPSENVLGEVGSGF 353
Cdd:cd01157  153 TNGGKANWYFLLARSD-PDPKCPASK-AFTGFIVEADTPGIQPGRKELNMGQRCSDTRGITFEDVRVPKENVLIGEGAGF 230

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 394025723 354 KVAMHILNNGRFGMAAALAGTMRGIIAKAVDHATNRTQFGEKIHNFGLIQEKLARMVMlQYVTESMAYMVSAN-MDQGAT 432
Cdd:cd01157  231 KIAMGAFDKTRPPVAAGAVGLAQRALDEATKYALERKTFGKLIAEHQAVSFMLADMAM-KVELARLAYQRAAWeVDSGRR 309

                        330       340       350       360       370       380
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 394025723 433 DfQIEAAISKIFGSEAAWKVTDECIQIMGGMGFMKEPGVERVLRDLRIFRIFEGTNDILRLFVA 496
Cdd:cd01157  310 N-TYYASIAKAFAADIANQLATDAVQIFGGNGFNSEYPVEKLMRDAKIYQIYEGTSQIQRLIIS 372
PTZ00461 PTZ00461
isovaleryl-CoA dehydrogenase; Provisional
 126-487 1.92e-62

isovaleryl-CoA dehydrogenase; Provisional


Pssm-ID: 185640 [Multi-domain]  Cd Length: 410  Bit Score: 213.65  E-value: 1.92e-62
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 394025723 126 KELVEPVSRFFEEVNDP-AKNDALEM-VEETTWQGLKELGAFGLQVPSELGGVGLCNTQYARLVEIVGMHDLGVGITLGA 203
Cdd:PTZ00461  42 AALRETVAKFSREVVDKhAREDDINMhFNRDLFKQLGDLGVMGVTVPEADGGAGMDAVAAVIIHHELSKYDPGFCLAYLA 121

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 394025723 204 HQSIGFKGILLFGTKAQKEKYLPKLASGETVAAFCLTEPSSGSDAASIRTSAVPSPCGKYyTLNGSKLWISNGGLADIFT 283
Cdd:PTZ00461 122 HSMLFVNNFYYSASPAQRARWLPKVLTGEHVGAMGMSEPGAGTDVLGMRTTAKKDSNGNY-VLNGSKIWITNGTVADVFL 200

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 394025723 284 VFAKtpvtdpatgaVKEKITAFVVERGFGGITHGPPEKKMGIKASNTAEVFFDGVRVPSENVLGEVGSGFKVAMHILNNG 363
Cdd:PTZ00461 201 IYAK----------VDGKITAFVVERGTKGFTQGPKIDKCGMRASHMCQLFFEDVVVPAENLLGEEGKGMVGMMRNLELE 270

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 394025723 364 RFGMAAALAGTMRGIIAKAVDHATNRTQFGEKIHNFGLIQEKLARMVMLQYVTESMAYMVSANMDQGATDfQIEAAISKI 443
Cdd:PTZ00461 271 RVTLAAMAVGIAERSVELMTSYASERKAFGKPISNFGQIQRYIAEGYADTEAAKALVYSVSHNVHPGNKN-RLGSDAAKL 349

                        330       340       350       360
                 ....*....|....*....|....*....|....*....|....
gi 394025723 444 FGSEAAWKVTDECIQIMGGMGFMKEPGVERVLRDLRIFRIFEGT 487
Cdd:PTZ00461 350 FATPIAKKVADSAIQVMGGMGYSRDMPVERLWRDAKLLEIGGGT 393
ACAD_fadE5 cd01153
Putative acyl-CoA dehydrogenases similar to fadE5; Putative acyl-CoA dehydrogenase (ACAD). ...
 161-490 3.56e-53

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: 188.37  E-value: 3.56e-53
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 394025723 161 ELGAFGLQVPSELGGVGLCNTQYARLVEIVGMHDLGVGITLGAHQsiGFKGILLFGTKAQKEKYLPKLASGETVAAFCLT 240
Cdd:cd01153   47 EAGWMALGVPEEYGGQGLPITVYSALAEIFSRGDAPLMYASGTQG--AAATLLAHGTEAQREKWIPRLAEGEWTGTMCLT 124

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 394025723 241 EPSSGSDAASIRTSAVPSPCGKYYtLNGSKLWISNG--GLAD--IFTVFAKTPvtDPATGAvkEKITAFVV-------ER 309
Cdd:cd01153  125 EPDAGSDLGALRTKAVYQADGSWR-INGVKRFISAGehDMSEniVHLVLARSE--GAPPGV--KGLSLFLVpkflddgER 199

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 394025723 310 GfgGITHGPPEKKMGIKASNTAEVFFDGVRVPsenVLGEVGSGFKVAMHILNNGRFGMAAALAGTMRGIIAKAVDHATNR 389
Cdd:cd01153  200 N--GVTVARIEEKMGLHGSPTCELVFDNAKGE---LIGEEGMGLAQMFAMMNGARLGVGTQGTGLAEAAYLNALAYAKER 274

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 394025723 390 TQFGEKIHNFGLIQEKLARMVMLQYVTESMAYMVSANMD-----------QGATDFQIEAA----------ISKIFGSEA 448
Cdd:cd01153  275 KQGGDLIKAAPAVTIIHHPDVRRSLMTQKAYAEGSRALDlytatvqdlaeRKATEGEDRKAlsaladlltpVVKGFGSEA 354

                        330       340       350       360
                 ....*....|....*....|....*....|....*....|..
gi 394025723 449 AWKVTDECIQIMGGMGFMKEPGVERVLRDLRIFRIFEGTNDI 490
Cdd:cd01153  355 ALEAVSDAIQVHGGSGYTREYPIEQYYRDARITTIYEGTTGI 396
PRK12341 PRK12341
acyl-CoA dehydrogenase;
117-491 1.80e-49

acyl-CoA dehydrogenase;


Pssm-ID: 183454 [Multi-domain]  Cd Length: 381  Bit Score: 177.61  E-value: 1.80e-49
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 394025723 117 LNEEQTQFLKELVEPVSRFFEEvNDPAKNDALEMVEETTWQGLKELGAFGLQVPSELGGVGLCNTQYARLVEivGMHDLG 196
Cdd:PRK12341   5 LTEEQELLLASIRELITRNFPE-EYFRTCDENGTYPREFMRALADNGISMLGVPEEFGGTPADYVTQMLVLE--EVSKCG 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 394025723 197 VGITLgAHQSIGFKGILLFGTKAQKEKYLpKLASGETVAAFCL--TEPSSGSDAASIRTSAVPSPcGKYYtLNGSKLWIS 274
Cdd:PRK12341  82 APAFL-ITNGQCIHSMRRFGSAEQLRKTA-ESTLETGDPAYALalTEPGAGSDNNSATTTYTRKN-GKVY-LNGQKTFIT 157

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 394025723 275 NGGLADIFTVFAKtpvtDPATGAVKEKITAFVVERGFGGITHGPPEKkMGIKASNTAEVFFDGVRVPSENVLGEVGSGFK 354
Cdd:PRK12341 158 GAKEYPYMLVLAR----DPQPKDPKKAFTLWWVDSSKPGIKINPLHK-IGWHMLSTCEVYLDNVEVEESDLVGEEGMGFL 232

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 394025723 355 VAMHILNNGRFGMAAALAGTMRGIIAKAVDHATNRTQFGEKIHNFGLIQEKLARMVMLQYVTESMAYMVSANMDQGATdF 434
Cdd:PRK12341 233 NVMYNFEMERLINAARSLGFAECAFEDAARYANQRIQFGKPIGHNQLIQEKLTLMAIKIENMRNMVYKVAWQADNGQS-L 311

                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 394025723 435 QIEAAISKIFGSEAAWKVTDECIQIMGGMGFMKEPGVERVLRDLRIFRIFEGTNDIL 491
Cdd:PRK12341 312 RTSAALAKLYCARTAMEVIDDAIQIMGGLGYTDEARVSRFWRDVRCERIGGGTDEIM 368
PRK03354 PRK03354
crotonobetainyl-CoA dehydrogenase; Validated
 157-493 8.70e-42

crotonobetainyl-CoA dehydrogenase; Validated


Pssm-ID: 179566 [Multi-domain]  Cd Length: 380  Bit Score: 156.14  E-value: 8.70e-42
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 394025723 157 QGLKELGAFGLQVPSELGGVGLCNTQYARLVEIVGMhdLGVGITLGAHQSIGFKGILLFGTKAQKEKYLPKLASGETVAA 236
Cdd:PRK03354  44 KALADMGIDSLLIPEEHGGLDAGFVTLAAVWMELGR--LGAPTYVLYQLPGGFNTFLREGTQEQIDKIMAFRGTGKQMWN 121

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 394025723 237 FCLTEPSSGSDAASIRTSAVPSPcGKYYtLNGSKLWISNGGLADIFTVFAKTPVTDPatgavKEKITAFVVERGFGGITH 316
Cdd:PRK03354 122 SAITEPGAGSDVGSLKTTYTRRN-GKVY-LNGSKCFITSSAYTPYIVVMARDGASPD-----KPVYTEWFVDMSKPGIKV 194

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 394025723 317 GPPEKkMGIKASNTAEVFFDGVRVPSENVLGEVGSGFKVAMHILNNGRFGMAAALAGTMRGIIAKAVDHATNRTQFGEKI 396
Cdd:PRK03354 195 TKLEK-LGLRMDSCCEITFDDVELDEKDMFGREGNGFNRVKEEFDHERFLVALTNYGTAMCAFEDAARYANQRVQFGEAI 273

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 394025723 397 HNFGLIQEKLARMVMLQYVTESMAYMVSANMDQGATDfQIEAAISKIFGSEAAWKVTDECIQIMGGMGFMKEPGVERVLR 476
Cdd:PRK03354 274 GRFQLIQEKFAHMAIKLNSMKNMLYEAAWKADNGTIT-SGDAAMCKYFCANAAFEVVDSAMQVLGGVGIAGNHRISRFWR 352

                        330
                 ....*....|....*..
gi 394025723 477 DLRIFRIFEGTNDILRL 493
Cdd:PRK03354 353 DLRVDRVSGGSDEMQIL 369
Acyl-CoA_dh_1 pfam00441
Acyl-CoA dehydrogenase, C-terminal domain; C-terminal domain of Acyl-CoA dehydrogenase is an ...
 350-496 8.09e-40

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: 143.16  E-value: 8.09e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 394025723  350 GSGFKVAMHILNNGRFGMAAALAGTMRGIIAKAVDHATNRTQFGEKIHNFGLIQEKLARMVMLQYVTESMAYMVSANMDQ 429
Cdd:pfam00441   1 GRGFRVAMETLNHERLAIAAMALGLARRALDEALAYARRRKAFGRPLIDFQLVRHKLAEMAAEIEAARLLVYRAAEALDA 80

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 394025723  430 GATDfQIEAAISKIFGSEAAWKVTDECIQIMGGMGFMKEPGVERVLRDLRIFRIFEGTNDILRLFVA 496
Cdd:pfam00441  81 GGPD-GAEASMAKLYASEAAVEVADLAMQLHGGYGYLREYPVERLYRDARVLRIGEGTSEIQRNIIA 146
ACAD_fadE6_17_26 cd01152
Putative acyl-CoA dehydrogenases similar to fadE6, fadE17, and fadE26; Putative acyl-CoA ...
 155-496 1.14e-37

Putative acyl-CoA dehydrogenases similar to fadE6, fadE17, and fadE26; Putative acyl-CoA dehydrogenases (ACAD). Mitochondrial acyl-CoA dehydrogenases (ACAD) catalyze the alpha, beta dehydrogenation of the corresponding trans-enoyl-CoA by FAD, which becomes reduced. The reduced form of ACAD is reoxidized in the oxidative half-reaction by electron-transferring flavoprotein (ETF), from which the electrons are transferred to the mitochondrial respiratory chain coupled with ATP synthesis. The ACD family includes the eukaryotic beta-oxidation, as well as amino acid catabolism enzymes. These enzymes share high sequence similarity, but differ in their substrate specificities. The mitochondrial ACD's are generally homotetramers and have an active site glutamate at a conserved position.


Pssm-ID: 173841 [Multi-domain]  Cd Length: 380  Bit Score: 144.41  E-value: 1.14e-37
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 394025723 155 TWQG-LKELGAFGLQVPSELGGVGLCNTQYARLVE---IVGM--HDLGVGITLGAHQsigfkgILLFGTKAQKEKYLPKL 228
Cdd:cd01152   39 RWQRaLAAAGWAAPGWPKEYGGRGASLMEQLIFREemaAAGApvPFNQIGIDLAGPT------ILAYGTDEQKRRFLPPI 112

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 394025723 229 ASGETVaaFCL--TEPSSGSDAASIRTSAVPSpcGKYYTLNGSKLWISNGGLADIFTVFAKTpvtDPAtgAVKEK-ITAF 305
Cdd:cd01152  113 LSGEEI--WCQgfSEPGAGSDLAGLRTRAVRD--GDDWVVNGQKIWTSGAHYADWAWLLVRT---DPE--APKHRgISIL 183

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 394025723 306 VVERGFGGITHGPPEKKMGikASNTAEVFFDGVRVPSENVLGEVGSGFKVAMHILNNGRFGMAAALAGTMRGIIAKAvdH 385
Cdd:cd01152  184 LVDMDSPGVTVRPIRSING--GEFFNEVFLDDVRVPDANRVGEVNDGWKVAMTTLNFERVSIGGSAATFFELLLARL--L 259

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 394025723 386 ATNRTQFGEkiHNFGLIQEKLARMVM----LQYVTESMAYMVSANMDQGAtdfqiEAAISKIFGSEAAWKVTDECIQIMG 461
Cdd:cd01152  260 LLTRDGRPL--IDDPLVRQRLARLEAeaeaLRLLVFRLASALAAGKPPGA-----EASIAKLFGSELAQELAELALELLG 332

                        330       340       350       360
                 ....*....|....*....|....*....|....*....|...
gi 394025723 462 GMGFMKEPG--------VERVLRDLRIFRIFEGTNDILRLFVA 496
Cdd:cd01152  333 TAALLRDPApgaelagrWEADYLRSRATTIYGGTSEIQRNIIA 375
ACAD_FadE2 cd01155
Acyl-CoA dehydrogenases similar to fadE2; FadE2-like Acyl-CoA dehydrogenase (ACAD). Acyl-CoA ...
 125-486 6.03e-35

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: 137.14  E-value: 6.03e-35
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 394025723 125 LKELVEPVSRFFEEVNDPAKNDALEMVEE---TTWQ------GLKE----LGAFGLQVPSELGGVGLCNTQYARLVEIVG 191
Cdd:cd01155    3 AQELRARVKAFMEEHVYPAEQEFLEYYAEggdRWWTpppiieKLKAkakaEGLWNLFLPEVSGLSGLTNLEYAYLAEETG 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 394025723 192 MHDLGVGITLGAHQSIGFKGIL-LFGTKAQKEKYLPKLASGETVAAFCLTEPS-SGSDAASIRTSAVPSpcGKYYTLNGS 269
Cdd:cd01155   83 RSFFAPEVFNCQAPDTGNMEVLhRYGSEEQKKQWLEPLLDGKIRSAFAMTEPDvASSDATNIECSIERD--GDDYVINGR 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 394025723 270 KLWISNGGLAD--IFTVFAKTpvtDPATGAVKEKITAFVVERGFGGITHGPPEKKMGIKAS--NTAEVFFDGVRVPSENV 345
Cdd:cd01155  161 KWWSSGAGDPRckIAIVMGRT---DPDGAPRHRQQSMILVPMDTPGVTIIRPLSVFGYDDAphGHAEITFDNVRVPASNL 237

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 394025723 346 LGEVGSGFKVAMHILNNGRFGMAAALAGTMRGIIAKAVDHATNRTQFGEKIHNFGLIQEKLA--RMV--MLQYVTESMAY 421
Cdd:cd01155  238 ILGEGRGFEIAQGRLGPGRIHHCMRLIGAAERALELMCQRAVSREAFGKKLAQHGVVAHWIAksRIEieQARLLVLKAAH 317

                        330       340       350       360       370       380
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 394025723 422 MvsanMDQ-GATDFQIEAAISKIFGSEAAWKVTDECIQIMGGMGFMKEPGVERVLRDLRIFRIFEG 486
Cdd:cd01155  318 M----IDTvGNKAARKEIAMIKVAAPRMALKIIDRAIQVHGAAGVSQDTPLANMYAWARTLRIADG 379
PLN02526 PLN02526
acyl-coenzyme A oxidase
 174-512 1.46e-33

acyl-coenzyme A oxidase


Pssm-ID: 178141 [Multi-domain]  Cd Length: 412  Bit Score: 133.44  E-value: 1.46e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 394025723 174 GGVGLCNTQYARLVEIVGMHDLGVGITLGAHQSIGFKGILLFGTKAQKEKYLPKLASGETVAAFCLTEPSSGSDAASIRT 253
Cdd:PLN02526  83 GCPGLSITASAIATAEVARVDASCSTFILVHSSLAMLTIALCGSEAQKQKYLPSLAQLDTVACWALTEPDYGSDASSLNT 162

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 394025723 254 SAVPSPCGkyYTLNGSKLWISNGGLADIFTVFAKTPVTDpatgavkeKITAFVVERGFGGITHGPPEKKMGIKASNTAEV 333
Cdd:PLN02526 163 TATKVEGG--WILNGQKRWIGNSTFADVLVIFARNTTTN--------QINGFIVKKGAPGLKATKIENKIGLRMVQNGDI 232

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 394025723 334 FFDGVRVPSENVLGEVGSgFKVAMHILNNGRFGMAAALAGTMRGIIAKAVDHATNRTQFGEKIHNFGLIQEKLARMV--- 410
Cdd:PLN02526 233 VLKDVFVPDEDRLPGVNS-FQDTNKVLAVSRVMVAWQPIGISMGVYDMCHRYLKERKQFGAPLAAFQINQEKLVRMLgni 311

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 394025723 411 --MLQYVTESMAYMVSANMDQGatdfqiEAAISKIFGSEAAWKVTDECIQIMGGMGFMKEPGVERVLRDLRIFRIFEGTN 488
Cdd:PLN02526 312 qaMFLVGWRLCKLYESGKMTPG------HASLGKAWITKKARETVALGRELLGGNGILADFLVAKAFCDLEPIYTYEGTY 385

                        330       340
                 ....*....|....*....|....
gi 394025723 489 DILRLFValqgcmdkGKELSGLGS 512
Cdd:PLN02526 386 DINALVT--------GREITGIAS 401
AidB cd01154
Proteins involved in DNA damage response, similar to the AidB gene product; AidB is one of ...
 222-493 2.68e-31

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: 126.72  E-value: 2.68e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 394025723 222 EKYLPKLASGET----VAAFCLTEPSSGSDAASIRTSAVPSPcGKYYTLNGSKlWISNGGLADIFTVFAKTPVTDPATGA 297
Cdd:cd01154  132 KQYLPGLLSDRYktglLGGTWMTEKQGGSDLGANETTAERSG-GGVYRLNGHK-WFASAPLADAALVLARPEGAPAGARG 209

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 394025723 298 vkekITAFVVER-----GFGGITHGPPEKKMGIKASNTAEVFFDGvrvpSEN-VLGEVGSGFKVAMHILNNGRFGMAAAL 371
Cdd:cd01154  210 ----LSLFLVPRlledgTRNGYRIRRLKDKLGTRSVATGEVEFDD----AEAyLIGDEGKGIYYILEMLNISRLDNAVAA 281

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 394025723 372 AGTMRGIIAKAVDHATNRTQFGEKIHNFGLIQEKLARMVMLQYVTESMAYMVSANMDQGATDFQIEA-------AISKIF 444
Cdd:cd01154  282 LGIMRRALSEAYHYARHRRAFGKPLIDHPLMRRDLAEMEVDVEAATALTFRAARAFDRAAADKPVEAhmarlatPVAKLI 361

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*....
gi 394025723 445 GSEAAWKVTDECIQIMGGMGFMKEPGVERVLRDLRIFRIFEGTNDILRL 493
Cdd:cd01154  362 ACKRAAPVTSEAMEVFGGNGYLEEWPVARLHREAQVTPIWEGTGNIQAL 410
PTZ00456 PTZ00456
acyl-CoA dehydrogenase; Provisional
 153-490 2.64e-28

acyl-CoA dehydrogenase; Provisional


Pssm-ID: 185635 [Multi-domain]  Cd Length: 622  Bit Score: 120.36  E-value: 2.64e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 394025723 153 ETTWQGLKELGAFGLQVPSELGGVGLCNTQYARLVEIVGMHDLGVGITLGahQSIG-FKGILLFGTKAQKEKYLPKLASG 231
Cdd:PTZ00456 102 KEAYQALKAGGWTGISEPEEYGGQALPLSVGFITRELMATANWGFSMYPG--LSIGaANTLMAWGSEEQKEQYLTKLVSG 179

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 394025723 232 ETVAAFCLTEPSSGSDAASIRTSAVPSPCGKyYTLNGSKLWISNG--GLAD--IFTVFAKTPVTDPATgavkEKITAFVV 307
Cdd:PTZ00456 180 EWSGTMCLTEPQCGTDLGQVKTKAEPSADGS-YKITGTKIFISAGdhDLTEniVHIVLARLPNSLPTT----KGLSLFLV 254

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 394025723 308 ERGF----------GGITHGPPEKKMGIKASNTAEVFFDGvrvPSENVLGEVGSGFKVAMHILNNGRfgMAAALAGTMRG 377
Cdd:PTZ00456 255 PRHVvkpdgsletaKNVKCIGLEKKMGIKGSSTCQLSFEN---SVGYLIGEPNAGMKQMFTFMNTAR--VGTALEGVCHA 329

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 394025723 378 IIA--KAVDHATNR--------TQFGEKIHNFGLIQEKLARMVML-QYVTE---SMAYMVSANMD--QGATDFQIEAA-- 439
Cdd:PTZ00456 330 ELAfqNALRYARERrsmralsgTKEPEKPADRIICHANVRQNILFaKAVAEggrALLLDVGRLLDihAAAKDAATREAld 409

                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 394025723 440 --------ISKIFGSEAAWKVTDECIQIMGGMGFMKEPGVERVLRDLRIFRIFEGTNDI 490
Cdd:PTZ00456 410 heigfytpIAKGCLTEWGVEAASRCLQVWGGHGYIKGNGMEQILRDARIGTLYEGTTGI 468
Acyl-CoA_dh_M pfam02770
Acyl-CoA dehydrogenase, middle domain; Central domain of Acyl-CoA dehydrogenase has a ...
 236-336 8.40e-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: 104.67  E-value: 8.40e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 394025723  236 AFCLTEPSSGSDAASIRTSAVPSPcGKYYTLNGSKLWISNGGLADIFTVFAKTPVTDPATGavkekITAFVVERGFGGIT 315
Cdd:pfam02770   1 AFALTEPGAGSDVASLKTTAADGD-GGGWVLNGTKWWITNAGIADLFLVLARTGGDDRHGG-----ISLFLVPKDAPGVS 74

                          90       100
                  ....*....|....*....|.
gi 394025723  316 HGPPEKKMGIKASNTAEVFFD 336
Cdd:pfam02770  75 VRRIETKLGVRGLPTGELVFD 95
Acyl-CoA_dh_N pfam02771
Acyl-CoA dehydrogenase, N-terminal domain; The N-terminal domain of Acyl-CoA dehydrogenase is ...
 118-232 2.57e-24

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: 97.92  E-value: 2.57e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 394025723  118 NEEQTQFLKElvepVSRFFEEVNDP--AKNDALEMVEETTWQGLKELGAFGLQVPSELGGVGLCNTQYARLVEIVGMHDL 195
Cdd:pfam02771   1 TEEQEALRDT----VREFAEEEIAPhaAEWDEEGEFPRELWKKLGELGLLGITIPEEYGGAGLDYLAYALVAEELARADA 76

                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 394025723  196 GVGITLGAHQSIGFKGILLFGTKAQKEKYLPKLASGE 232
Cdd:pfam02771  77 SVALALSVHSSLGAPPILRFGTEEQKERYLPKLASGE 113
PTZ00457 PTZ00457
acyl-CoA dehydrogenase; Provisional
 95-638 1.23e-22

acyl-CoA dehydrogenase; Provisional


Pssm-ID: 185636 [Multi-domain]  Cd Length: 520  Bit Score: 102.27  E-value: 1.23e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 394025723  95 SFAVGMFKGQLTTDQVFPYPS-VLNEEQTQFLKELVEPVSrffeevndpaKNDalemveettwqglKELG-AFGLQVPSE 172
Cdd:PTZ00457  17 SYAAGLFNFKIVPEEMFPYPCrKLDGDEAENLQSLLEQIR----------SND-------------KILGnLYGARIATE 73

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 394025723 173 LGGVGLCNTQYARLVEIVGMHdlGVGITLGAHQSIGFKGILL--FGTKAQKEKYLPKLASGETVAAFClTEPSSGSDAAS 250
Cdd:PTZ00457  74 YGGLGLGHTAHALIYEEVGTN--CDSKLLSTIQHSGFCTYLLstVGSKELKGKYLTAMSDGTIMMGWA-TEEGCGSDISM 150

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 394025723 251 IRTSAVPSPCGKYyTLNGSKLWIsNGGLADIFTVFAKTpVTDPATGA---VKEKITAFVVERgfggithgppeKKMGIKA 327
Cdd:PTZ00457 151 NTTKASLTDDGSY-VLTGQKRCE-FAASATHFLVLAKT-LTQTAAEEgatEVSRNSFFICAK-----------DAKGVSV 216

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 394025723 328 SNTAEVFFDgvrVPSENVLGEVGSGFKVAMHILNNGRFGMAAALAGTMRGIIAKAVDhaTNRTQFgekihnfglIQEKLA 407
Cdd:PTZ00457 217 NGDSVVFEN---TPAADVVGVVGEGFKDAMITLFTEQYLYAASLLGIMKRVVQELRG--SNAEEG---------ATDTVA 282

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 394025723 408 RMVMLQYVTESMAYMVSANMDQGATDFQIEAAISKIFGSEAawkvTDECIQIMGGMGFMKEPgVERVLRDLRIFRIFEGT 487
Cdd:PTZ00457 283 SFACAMYAMESTLYALTANLDLPTEDSLLECTLVSAFVQST----TNQLLSILETATPPSTT-LEKCFANARLFLSMMES 357

                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 394025723 488 NDIlrLFVALQGCmdkGKELSGLgsalknPFGNAGLLLGEAGKQLRrraglgsGLSLSGLVHPELSRSGELAVRALEQFA 567
Cdd:PTZ00457 358 RDF--LYSSAVCC---GVEDYGL------FFQRASTLQMMQARTLR-------SLGVRDRVPIKNLPDCSLIDEAVVAFG 419

                        490       500       510       520       530       540       550
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 394025723 568 TVVEAKLIKHKKGIVNEQFLLQRLADGAIDLYAMVVVLSRASRSLSEGHPTAQHEKMLCDTWCIEAAARIR 638
Cdd:PTZ00457 420 NAVEATFVRSGSQVPYQQLLLNRLGEAASLLYAASAVASRASMCVSKGLPSAKVEGELASAFIAMAVSRAR 490
fadE PRK09463
acyl-CoA dehydrogenase; Reviewed
 111-469 1.62e-20

acyl-CoA dehydrogenase; Reviewed


Pssm-ID: 236528 [Multi-domain]  Cd Length: 777  Bit Score: 96.42  E-value: 1.62e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 394025723 111 FPYPSVLNEEQTqFLKELVEPVSRFfeeVNDPAKNDALEMVEETTWQGLKELGAFGLQVPSELGGVGLCNTQYARLVEIV 190
Cdd:PRK09463  74 YPKPTLTAEEQA-FLDGPVEELCRM---VNDWQITHELADLPPEVWQFIKEHGFFGMIIPKEYGGLEFSAYAHSRVLQKL 149

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 394025723 191 GMHDLGVGITLGAHQSIGfKGILL--FGTKAQKEKYLPKLASGETVAAFCLTEPSSGSDAASIRTSAVpsPC-----GK- 262
Cdd:PRK09463 150 ASRSGTLAVTVMVPNSLG-PGELLlhYGTDEQKDHYLPRLARGEEIPCFALTSPEAGSDAGSIPDTGV--VCkgewqGEe 226

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 394025723 263 --YYTLNGSKLWISnggLADIFTVFA---KtpVTDPaTGAVKEK----ITAFVVERGFGGITHGPPEKKMGIkasntaeV 333
Cdd:PRK09463 227 vlGMRLTWNKRYIT---LAPIATVLGlafK--LYDP-DGLLGDKedlgITCALIPTDTPGVEIGRRHFPLNV-------P 293

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 394025723 334 FFDG------VRVPSENVLGE---VGSGFKVAMHILNNGRFGMAAALAGTMRGIIAKAV-DHATNRTQFGEKIHNFGLIQ 403
Cdd:PRK09463 294 FQNGptrgkdVFIPLDYIIGGpkmAGQGWRMLMECLSVGRGISLPSNSTGGAKLAALATgAYARIRRQFKLPIGKFEGIE 373

                        330       340       350       360       370       380
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 394025723 404 EKLARMVMLQYVTESMAYMVSANMDQGATDFQIeAAISKIFGSEAAWKVTDECIQIMGGMGFMKEP 469
Cdd:PRK09463 374 EPLARIAGNAYLMDAARTLTTAAVDLGEKPSVL-SAIAKYHLTERGRQVINDAMDIHGGKGICLGP 438
PRK13026 PRK13026
acyl-CoA dehydrogenase; Reviewed
 156-464 3.84e-20

acyl-CoA dehydrogenase; Reviewed


Pssm-ID: 237277 [Multi-domain]  Cd Length: 774  Bit Score: 95.41  E-value: 3.84e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 394025723 156 WQGLKELGAFGLQVPSELGGVGLcnTQYA--RLVEIVGMHDLGVGITLGAHQSIGfKGILL--FGTKAQKEKYLPKLASG 231
Cdd:PRK13026 114 WDYLKKEGFFALIIPKEYGGKGF--SAYAnsTIVSKIATRSVSAAVTVMVPNSLG-PGELLthYGTQEQKDYWLPRLADG 190

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 394025723 232 ETVAAFCLTEPSSGSDAASIRTSAVpsPC-GKY-------YTLNGSKLWISnggLADIFTVF-----AKTPvtDPATGAV 298
Cdd:PRK13026 191 TEIPCFALTGPEAGSDAGAIPDTGI--VCrGEFegeevlgLRLTWDKRYIT---LAPVATVLglafkLRDP--DGLLGDK 263

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 394025723 299 KE-KITAFVVERGFGGITHGPPEKKMGIkasntaeVFFDG------VRVPSENVLG---EVGSGFKVAMHILNNGRFGMA 368
Cdd:PRK13026 264 KElGITCALIPTDHPGVEIGRRHNPLGM-------AFMNGttrgkdVFIPLDWIIGgpdYAGRGWRMLVECLSAGRGISL 336

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 394025723 369 AALAGTMRGIIAKAVD-HATNRTQFGEKIHNFGLIQEKLARMVMLQYVTESMAYMVSANMDQGATDfQIEAAISKIFGSE 447
Cdd:PRK13026 337 PALGTASGHMATRTTGaYAYVRRQFGMPIGQFEGVQEALARIAGNTYLLEAARRLTTTGLDLGVKP-SVVTAIAKYHMTE 415

                        330
                 ....*....|....*..
gi 394025723 448 AAWKVTDECIQIMGGMG 464
Cdd:PRK13026 416 LARDVVNDAMDIHAGKG 432
AXO cd01150
Peroxisomal acyl-CoA oxidase; Peroxisomal acyl-CoA oxidases (AXO) catalyze the first set in ...
 186-536 1.47e-18

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: 89.70  E-value: 1.47e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 394025723 186 LVEIVGMHDLGVGITLGAHQSIGFKGILLFGTKAQKEKYLPKLASGETVAAFCLTEPSSGSDAASIRTSAVPSPCGKYYT 265
Cdd:cd01150   87 LTNSLGGYDLSLGAKLGLHLGLFGNAIKNLGTDEHQDYWLQGANNLEIIGCFAQTELGHGSNLQGLETTATYDPLTQEFV 166

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 394025723 266 LN-----GSKLWIsnGGLADIFT---VFAKTpvtdpATGAVKEKITAFVVE-------RGFGGITHGPPEKKMGIKASNT 330
Cdd:cd01150  167 INtpdftATKWWP--GNLGKTAThavVFAQL-----ITPGKNHGLHAFIVPirdpkthQPLPGVTVGDIGPKMGLNGVDN 239

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 394025723 331 AEVFFDGVRVPSENVL---GEV-------------GSGFKVAMHILNNGRFGMAAALAGTMRGIIAKAVDHATNRTQFGE 394
Cdd:cd01150  240 GFLQFRNVRIPRENLLnrfGDVspdgtyvspfkdpNKRYGAMLGTRSGGRVGLIYDAAMSLKKAATIAIRYSAVRRQFGP 319

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 394025723 395 K-------IHNFGLIQEK----LARMVMLQYVTESMAYM---VSANMDQGATDFQIE----AAISKIFGSEAAWKVTDEC 456
Cdd:cd01150  320 KpsdpevqILDYQLQQYRlfpqLAAAYAFHFAAKSLVEMyheIIKELLQGNSELLAElhalSAGLKAVATWTAAQGIQEC 399

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 394025723 457 IQIMGGMGFMKEPGVERVLRDLRIFRIFEGTNDILRLFVAlQGCMDKGKELSGLGSALKNPFGNAGLLLGEAGKQLRRRA 536
Cdd:cd01150  400 REACGGHGYLAMNRLPTLRDDNDPFCTYEGDNTVLLQQTA-NYLLKKYAQAFSLADYLEAYEWLAAHLLRHAAAQLEKLK 478
PLN02636 PLN02636
acyl-coenzyme A oxidase
 182-496 2.44e-18

acyl-coenzyme A oxidase


Pssm-ID: 215342 [Multi-domain]  Cd Length: 686  Bit Score: 89.15  E-value: 2.44e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 394025723 182 QYARLVEIVGMHDLGVGITLGAHQSIGFKGILLFGTKAQKEKYLPKLASGETVAAFCLTEPSSGSDAASIRTSAVPSPCG 261
Cdd:PLN02636 122 KYFAITEAVGSVDMSLGIKLGVQYSLWGGSVINLGTKKHRDKYFDGIDNLDYPGCFAMTELHHGSNVQGLQTTATFDPLT 201

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 394025723 262 KYYTLN-----GSKLWISNGGLADIF-TVFAKTPVTDPATGAVKEK-ITAFVV-------ERGFGGITHGPPEKKMGIKA 327
Cdd:PLN02636 202 DEFVINtpndgAIKWWIGNAAVHGKFaTVFARLKLPTHDSKGVSDMgVHAFIVpirdmktHQVLPGVEIRDCGHKVGLNG 281

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 394025723 328 SNTAEVFFDGVRVPSENVLGEVG----------------SGFKVAMHILNNGRFGMAAALAGTMRGIIAKAVDHATNRTQ 391
Cdd:PLN02636 282 VDNGALRFRSVRIPRDNLLNRFGdvsrdgkytsslptinKRFAATLGELVGGRVGLAYGSVGVLKASNTIAIRYSLLRQQ 361

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 394025723 392 FGE------KIHNFGLIQEKLarMVML----------QYVTESMAYMVSANMDQGATDFQIEAAISKIFGSEAAWKVTDE 455
Cdd:PLN02636 362 FGPpkqpeiSILDYQSQQHKL--MPMLastyafhfatEYLVERYSEMKKTHDDQLVADVHALSAGLKAYITSYTAKALST 439

                        330       340       350       360
                 ....*....|....*....|....*....|....*....|....
gi 394025723 456 CIQIMGGMGFmkePGVER--VLR-DLRIFRIFEGTNDILRLFVA 496
Cdd:PLN02636 440 CREACGGHGY---AAVNRfgSLRnDHDIFQTFEGDNTVLLQQVA 480
PLN02876 PLN02876
acyl-CoA dehydrogenase
 171-490 5.90e-18

acyl-CoA dehydrogenase


Pssm-ID: 215473 [Multi-domain]  Cd Length: 822  Bit Score: 88.31  E-value: 5.90e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 394025723 171 SELGGVGLCNTQYARLVEIVGMHDLGVGI-TLGAHQSIGFKGILLFGTKAQKEKYLPKLASGETVAAFCLTEPS-SGSDA 248
Cdd:PLN02876 487 DQLLGAGLSNLEYGYLCEIMGRSVWAPQVfNCGAPDTGNMEVLLRYGNKEQQLEWLIPLLEGKIRSGFAMTEPQvASSDA 566

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 394025723 249 ASIRTSAVPSpcGKYYTLNGSKLWISngGLAD----IFTVFAKTPVTDPA------------TGAVKEKITAFVVerGFG 312
Cdd:PLN02876 567 TNIECSIRRQ--GDSYVINGTKWWTS--GAMDprcrVLIVMGKTDFNAPKhkqqsmilvdiqTPGVQIKRPLLVF--GFD 640

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 394025723 313 GITHGppekkmgikasnTAEVFFDGVRVPSENVLGEVGSGFKVAMHILNNGRFGMAAALAGTMRGIIAKAVDHATNRTQF 392
Cdd:PLN02876 641 DAPHG------------HAEISFENVRVPAKNILLGEGRGFEIAQGRLGPGRLHHCMRLIGAAERGMQLMVQRALSRKAF 708

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 394025723 393 GEKIHNFGLIQEKLARmvmLQYVTESMAYMVSANMDQ----GATDFQIEAAISKIFGSEAAWKVTDECIQIMGGMGFMKE 468
Cdd:PLN02876 709 GKLIAQHGSFLSDLAK---CRVELEQTRLLVLEAADQldrlGNKKARGIIAMAKVAAPNMALKVLDMAMQVHGAAGVSSD 785

                        330       340
                 ....*....|....*....|..
gi 394025723 469 PGVERVLRDLRIFRIFEGTNDI 490
Cdd:PLN02876 786 TVLAHLWATARTLRIADGPDEV 807
DszC cd01163
Dibenzothiophene (DBT) desulfurization enzyme C; DszC is a flavin reductase dependent enzyme, ...
 151-390 1.13e-10

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: 63.88  E-value: 1.13e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 394025723 151 VEETTWqgLKELGAFGLQVPSELGGVGLCNTQYARLVEIVGMHDLGVGITLGAHqsIGF-KGILLFGTKAQKEKYLPKLA 229
Cdd:cd01163   25 YEEVAL--LRQSGLGTLRVPKEYGGLGASLPDLYEVVRELAAADSNIAQALRAH--FGFvEALLLAGPEQFRKRWFGRVL 100

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 394025723 230 SGETVAAfclTEPSSGSDAASIRTSAVPSPCGKYYtLNGSKlWISNGGL-ADIFTVFAktpvTDPAtgavkEKITAFVVE 308
Cdd:cd01163  101 NGWIFGN---AVSERGSVRPGTFLTATVRDGGGYV-LNGKK-FYSTGALfSDWVTVSA----LDEE-----GKLVFAAVP 166

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 394025723 309 RGFGGITHGPPEKKMGIK--ASNTAEvfFDGVRVPSENVLGEvGSGFKVAMHILNNGRFGMAAALAGTMRGIIAKAVDHA 386
Cdd:cd01163  167 TDRPGITVVDDWDGFGQRltASGTVT--FDNVRVEPDEVLPR-PNAPDRGTLLTAIYQLVLAAVLAGIARAALDDAVAYV 243


                 ....
gi 394025723 387 TNRT 390
Cdd:cd01163  244 RSRT 247
PRK11561 PRK11561
isovaleryl CoA dehydrogenase; Provisional
 239-502 5.48e-08

isovaleryl CoA dehydrogenase; Provisional


Pssm-ID: 183199 [Multi-domain]  Cd Length: 538  Bit Score: 55.91  E-value: 5.48e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 394025723 239 LTEPSSGSDAASIRTSAVPSPcGKYYTLNGSKlWISNGGLADIFTVFAKTpvtdpatgavKEKITAFVVERGFGGITHGP 318
Cdd:PRK11561 184 MTEKQGGSDVLSNTTRAERLA-DGSYRLVGHK-WFFSVPQSDAHLVLAQA----------KGGLSCFFVPRFLPDGQRNA 251

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 394025723 319 P-----EKKMGIKASNTAEVFFDGVrvpSENVLGEVGSGFKvamHILNNG---RFGMAAALAGTMRGIIAKAVDHATNRT 390
Cdd:PRK11561 252 IrlerlKDKLGNRSNASSEVEFQDA---IGWLLGEEGEGIR---LILKMGgmtRFDCALGSHGLMRRAFSVAIYHAHQRQ 325

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 394025723 391 QFGEKIHNFGLIQEKLARMVMLQYVTESMAYMVSANMDQGATdfQIEAAISKIFGSEAAWKVTD-------ECIQIMGGM 463
Cdd:PRK11561 326 VFGKPLIEQPLMRQVLSRMALQLEGQTALLFRLARAWDRRAD--AKEALWARLFTPAAKFVICKrgipfvaEAMEVLGGI 403

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....
gi 394025723 464 GFMKEPGVERVLRDLRIFRIFEGTN-----DILRLFVALQGCMD 502
Cdd:PRK11561 404 GYCEESELPRLYREMPVNSIWEGSGnimclDVLRVLNKQPGVYD 447
PLN02312 PLN02312
acyl-CoA oxidase
 184-511 1.93e-07

acyl-CoA oxidase


Pssm-ID: 215178 [Multi-domain]  Cd Length: 680  Bit Score: 54.39  E-value: 1.93e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 394025723 184 ARLVEIVGMHDLGVGITLGAHQSIGFKGILLFGTKAQKEKYLPKLASGETVAAFCLTEPSSGSDAASIRTSAVPSPCGKY 263
Cdd:PLN02312 136 LALLEVIGIYDHSLAIKLGVHFFLWGGAIKFLGTKRHHDKWLKDTEDYVVKGCFAMTELGHGSNVRGIETVTTYDPKTEE 215

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 394025723 264 YTLN-----GSKLWIsnGGLADIFT---VFAKTPVTdpatgAVKEKITAFVVE------RGFGGITHGPPEKKMGIKASN 329
Cdd:PLN02312 216 FVINtpcesAQKYWI--GGAANHAThtiVFSQLHIN-----GKNEGVHAFIAQirdqdgNICPNIRIADCGHKIGLNGVD 288

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 394025723 330 TAEVFFDGVRVPSENVLGEVG----------------SGFKVAMHILNNGRFGMAAALAGTMRGIIAKAVDHATNRTQF- 392
Cdd:PLN02312 289 NGRIWFDNLRIPRENLLNSVAdvspdgkyvsaikdpdQRFGAFLAPLTSGRVTIAVSAIYSSKVGLAIAIRYSLSRRAFs 368

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 394025723 393 ----GEKI-------HNFGLIqEKLARMVMLQYVTESMAYMVSANMDQGATDFQIeaaISKIFGSEAAW---KVTDECIQ 458
Cdd:PLN02312 369 vtpnGPEVllldypsHQRRLL-PLLAKTYAMSFAANDLKMIYVKRTPESNKAIHV---VSSGFKAVLTWhnmRTLQECRE 444

                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 394025723 459 IMGGMGFMKEPGVERVLRDLRIFRIFEGTNDILR------LFVALQGCMDKGKELSGLG 511
Cdd:PLN02312 445 ACGGQGLKTENRVGQLKAEYDVQSTFEGDNNVLMqqvskaLLAEYVSAKKRNKPFKGLG 503
Acyl-CoA_dh_2 pfam08028
Acyl-CoA dehydrogenase, C-terminal domain;
366-488 5.02e-07

Acyl-CoA dehydrogenase, C-terminal domain;


Pssm-ID: 429790 [Multi-domain]  Cd Length: 133  Bit Score: 49.27  E-value: 5.02e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 394025723  366 GMAAALAGTMRGIIAKAVDHATNRTQ--FGEKIHNFGLIQEKLARMV-------MLQYVTESMAYMVSANMDQGATDFQI 436
Cdd:pfam08028   1 GIAAAALGAARAALAEFTERARGRVRayFGVPLAEDPATQLALAEAAaridaarLLLERAAARIEAAAAAGKPVTPALRA 80

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|..
gi 394025723  437 EAAISKIFGSEAAWKVTDECIQIMGGMGFMKEPGVERVLRDLRIFRIFEGTN 488
Cdd:pfam08028  81 EARRAAAFATELAVAAVDALFRAAGGSALFQDSPLQRIWRDIHAAAQHAAVN 132
PTZ00460 PTZ00460
acyl-CoA dehydrogenase; Provisional
 216-496 6.53e-06

acyl-CoA dehydrogenase; Provisional


Pssm-ID: 185639 [Multi-domain]  Cd Length: 646  Bit Score: 49.46  E-value: 6.53e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 394025723 216 GTKAQKEKYLPKLASGETVAAFCLTEPSSGSDAASIRTSAVPSPCGKYYTLN-----GSKLWISN-GGLADIFTVFAKTP 289
Cdd:PTZ00460 110 GTDEQINLWMPSLLNFEIVGCYAQTELGHGSDVQNLETTATYDKQTNEFVIHtpsveAVKFWPGElGFLCNFALVYAKLI 189

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 394025723 290 VTDPATG--AVKEKITAFVVERGFGGITHGPPEKKMGIKASNTAEVFFDGVRVPSENVLG---EVGSGFKVAMHilNNGR 364
Cdd:PTZ00460 190 VNGKNKGvhPFMVRIRDKETHKPLQGVEVGDIGPKMGYAVKDNGFLSFDHYRIPLDSLLAryiKVSEDGQVERQ--GNPK 267

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 394025723 365 FGMAAALagTMRGIIAK------------AVDHATNRTQFGE------KIHNFGLIQEK----LARMVMLQYVTESMAYM 422
Cdd:PTZ00460 268 VSYASMM--YMRNLIIDqyprfaaqaltvAIRYSIYRQQFTNdnkqenSVLEYQTQQQKllplLAEFYACIFGGLKIKEL 345

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 394025723 423 VSANMDQ-GATDFQIEAAISKIFGSEAAW------KVTDECIQIMGGMGFMKEPGVERVLRDLRIFRIFEGTNDILRLFV 495
Cdd:PTZ00460 346 VDDNFNRvQKNDFSLLQLTHAILSAAKANytyfvsNCAEWCRLSCGGHGYAHYSGLPAIYFDMSPNITLEGENQIMYLQL 425


                 .
gi 394025723 496 A 496
Cdd:PTZ00460 426 A 426
PLN02443 PLN02443
acyl-coenzyme A oxidase
 216-524 2.38e-05

acyl-coenzyme A oxidase


Pssm-ID: 178062 [Multi-domain]  Cd Length: 664  Bit Score: 47.52  E-value: 2.38e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 394025723 216 GTKAQKEKYLPKLASGETVAAFCLTEPSSGSDAASIRTSAVPSPCGKYY-----TLNGSKLWisNGGLADIFT---VFAK 287
Cdd:PLN02443 114 GTEEQQKKWLPLAYKMQIIGCYAQTELGHGSNVQGLETTATFDPKTDEFvihspTLTSSKWW--PGGLGKVSThavVYAR 191

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 394025723 288 TpvtdpATGAVKEKITAFVVE-------RGFGGITHGPPEKKMGIKASNTAE---VFFDGVRVPSENVLGEVGSGFKVAM 357
Cdd:PLN02443 192 L-----ITNGKDHGIHGFIVQlrslddhSPLPGVTVGDIGMKFGNGAYNTMDngfLRFDHVRIPRDQMLMRLSKVTREGK 266

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 394025723 358 HILNNgrfgMAAALA-GTM----RGIIAK-----------AVDHATNRTQFGEK-------IHNFGLIQEK----LARMV 410
Cdd:PLN02443 267 YVQSD----VPRQLVyGTMvyvrQTIVADastalsravciATRYSAVRRQFGSQdggpetqVIDYKTQQSRlfplLASAY 342

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 394025723 411 MLQYVTESMAYMVSANMDQ-GATDF----QIEAAIS--KIFGSEAAWKVTDECIQIMGGMGFMKEPGVERVLRDLRIFRI 483
Cdd:PLN02443 343 AFRFVGEWLKWLYTDVTQRlEANDFstlpEAHACTAglKSLTTSATADGIEECRKLCGGHGYLCSSGLPELFAVYVPACT 422

                        330       340       350       360
                 ....*....|....*....|....*....|....*....|.
gi 394025723 484 FEGTNDILRLFVAlQGCMdkgKELSGLGSAlKNPFGNAGLL 524
Cdd:PLN02443 423 YEGDNVVLLLQVA-RFLM---KTVSQLGSG-KKPVGTTAYM 458
 
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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