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Conserved domains on  [gi|4557235|ref|NP_000009|]
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very long-chain specific acyl-CoA dehydrogenase, mitochondrial isoform 1 precursor [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 ...
 72-481 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: 749.30  E-value: 0e+00
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557235   72 SFAVGMFKGQLTTDQVFPYPSVLNEEQTQFLKELVEPVSRFFEEVNDPAKNDALEMVEETTWQGLKELGAFGLQVPSELG 151
Cdd:cd01161   1 SFALNMFLGDIVTKQVFPYPSVLTEEQTEELNMLVGPVEKFFEEVNDPAKNDQLEKIPRKTLTQLKELGLFGLQVPEEYG 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557235  152 GVGLCNTQYARLVEIVGMhDLGVGITLGAHQSIGFKGILLFGTKAQKEKYLPKLASGETVAAFCLTEPSSGSDAASIRTS 231
Cdd:cd01161  81 GLGLNNTQYARLAEIVGM-DLGFSVTLGAHQSIGFKGILLFGTEAQKEKYLPKLASGEWIAAFALTEPSSGSDAASIRTT 159

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557235  232 AVPSPCGKYYTLNGSKLWISNGGLADIFTVFAKTPVTDPaTGAVKEKITAFVVERGFGGITHGPPEKKMGIKASNTAEVF 311
Cdd:cd01161 160 AVLSEDGKHYVLNGSKIWITNGGIADIFTVFAKTEVKDA-TGSVKDKITAFIVERSFGGVTNGPPEKKMGIKGSNTAEVY 238

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557235  312 FDGVRVPSENVLGEVGSGFKVAMHILNNGRFGMAAALAGTMRGIIAKAVDHATNRTQFGEKIHNFGLIQEKLARMVMLQY 391
Cdd:cd01161 239 FEDVKIPVENVLGEVGDGFKVAMNILNNGRFGMGAALIGTMKRCIEKAVDYANNRKQFGKKIHEFGLIQEKLANMAILQY 318

                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557235  392 VTESMAYMVSANMDQGAT-DFQIEAAISKIFGSEAAWKVTDECIQIMGGMGFMKEPGVERVLRDLRIFRIFEGTNDILRL 470
Cdd:cd01161 319 ATESMAYMTSGNMDRGLKaEYQIEAAISKVFASEAAWLVVDEAIQIHGGMGFMREYGVERVLRDLRIFRIFEGTNEILRL 398

                       410
                ....*....|.
gi 4557235  471 FVALQGCMDKG 481
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 ...
 72-481 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: 749.30  E-value: 0e+00
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557235   72 SFAVGMFKGQLTTDQVFPYPSVLNEEQTQFLKELVEPVSRFFEEVNDPAKNDALEMVEETTWQGLKELGAFGLQVPSELG 151
Cdd:cd01161   1 SFALNMFLGDIVTKQVFPYPSVLTEEQTEELNMLVGPVEKFFEEVNDPAKNDQLEKIPRKTLTQLKELGLFGLQVPEEYG 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557235  152 GVGLCNTQYARLVEIVGMhDLGVGITLGAHQSIGFKGILLFGTKAQKEKYLPKLASGETVAAFCLTEPSSGSDAASIRTS 231
Cdd:cd01161  81 GLGLNNTQYARLAEIVGM-DLGFSVTLGAHQSIGFKGILLFGTEAQKEKYLPKLASGEWIAAFALTEPSSGSDAASIRTT 159

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557235  232 AVPSPCGKYYTLNGSKLWISNGGLADIFTVFAKTPVTDPaTGAVKEKITAFVVERGFGGITHGPPEKKMGIKASNTAEVF 311
Cdd:cd01161 160 AVLSEDGKHYVLNGSKIWITNGGIADIFTVFAKTEVKDA-TGSVKDKITAFIVERSFGGVTNGPPEKKMGIKGSNTAEVY 238

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557235  312 FDGVRVPSENVLGEVGSGFKVAMHILNNGRFGMAAALAGTMRGIIAKAVDHATNRTQFGEKIHNFGLIQEKLARMVMLQY 391
Cdd:cd01161 239 FEDVKIPVENVLGEVGDGFKVAMNILNNGRFGMGAALIGTMKRCIEKAVDYANNRKQFGKKIHEFGLIQEKLANMAILQY 318

                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557235  392 VTESMAYMVSANMDQGAT-DFQIEAAISKIFGSEAAWKVTDECIQIMGGMGFMKEPGVERVLRDLRIFRIFEGTNDILRL 470
Cdd:cd01161 319 ATESMAYMTSGNMDRGLKaEYQIEAAISKVFASEAAWLVVDEAIQIHGGMGFMREYGVERVLRDLRIFRIFEGTNEILRL 398

                       410
                ....*....|.
gi 4557235  471 FVALQGCMDKG 481
Cdd:cd01161 399 FIALTGLQHAG 409
CaiA COG1960
Acyl-CoA dehydrogenase related to the alkylation response protein AidB [Lipid transport and ...
 94-473 1.22e-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: 402.30  E-value: 1.22e-135
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557235   94 LNEEQTQFLKElvepVSRFFEEVNDP--AKNDALEMVEETTWQGLKELGAFGLQVPSELGGVGLCNTQYARLVEIVGMHD 171
Cdd:COG1960   5 LTEEQRALRDE----VREFAEEEIAPeaREWDREGEFPRELWRKLAELGLLGLTIPEEYGGLGLSLVELALVLEELARAD 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557235  172 LGVGITLGAHQSIGfKGILLFGTKAQKEKYLPKLASGETVAAFCLTEPSSGSDAASIRTSAVPSpcGKYYTLNGSKLWIS 251
Cdd:COG1960  81 ASLALPVGVHNGAA-EALLRFGTEEQKERYLPRLASGEWIGAFALTEPGAGSDAAALRTTAVRD--GDGYVLNGQKTFIT 157

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557235  252 NGGLADIFTVFAKTpvtDPATGAvkEKITAFVVERGFGGITHGPPEKKMGIKASNTAEVFFDGVRVPSENVLGEVGSGFK 331
Cdd:COG1960 158 NAPVADVILVLART---DPAAGH--RGISLFLVPKDTPGVTVGRIEDKMGLRGSDTGELFFDDVRVPAENLLGEEGKGFK 232

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557235  332 VAMHILNNGRFGMAAALAGTMRGIIAKAVDHATNRTQFGEKIHNFGLIQEKLARMVMLQYVTESMAYMVSANMDQGAtDF 411
Cdd:COG1960 233 IAMSTLNAGRLGLAAQALGIAEAALELAVAYAREREQFGRPIADFQAVQHRLADMAAELEAARALVYRAAWLLDAGE-DA 311

                       330       340       350       360       370       380
                ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 4557235  412 QIEAAISKIFGSEAAWKVTDECIQIMGGMGFMKEPGVERVLRDLRIFRIFEGTNDILRLFVA 473
Cdd:COG1960 312 ALEAAMAKLFATEAALEVADEALQIHGGYGYTREYPLERLYRDARILTIYEGTNEIQRLIIA 373
PLN02519 PLN02519
isovaleryl-CoA dehydrogenase
 96-472 1.81e-65

isovaleryl-CoA dehydrogenase


Pssm-ID: 215284 [Multi-domain]  Cd Length: 404  Bit Score: 220.90  E-value: 1.81e-65
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557235    96 EEQTQFLKELVEPVSRFFEEVNDPAKNDALemveettWQGLKELGAFGLQVPSELGGVGLCNTQYARLVEIVGMHDLGVG 175
Cdd:PLN02519  35 ESVQQFAQENIAPHAAAIDATNSFPKDVNL-------WKLMGDFNLHGITAPEEYGGLGLGYLYHCIAMEEISRASGSVG 107

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557235   176 ITLGAHQSIGFKGILLFGTKAQKEKYLPKLASGETVAAFCLTEPSSGSDAASIRTSAVPSPCGkyYTLNGSKLWISNGGL 255
Cdd:PLN02519 108 LSYGAHSNLCINQLVRNGTPAQKEKYLPKLISGEHVGALAMSEPNSGSDVVSMKCKAERVDGG--YVLNGNKMWCTNGPV 185

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557235   256 ADIFTVFAKTpvtDPATGAvkEKITAFVVERGFGGITHGPPEKKMGIKASNTAEVFFDGVRVPSENVLGEVGSGFKVAMH 335
Cdd:PLN02519 186 AQTLVVYAKT---DVAAGS--KGITAFIIEKGMPGFSTAQKLDKLGMRGSDTCELVFENCFVPEENVLGQEGKGVYVMMS 260

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557235   336 ILNNGRFGMAAALAGTMRGIIAKAVDHATNRTQFGEKIHNFGLIQEKLARMVMLQYVTESMAYMVSANMDQGATDFQiEA 415
Cdd:PLN02519 261 GLDLERLVLAAGPLGLMQACLDVVLPYVRQREQFGRPIGEFQFIQGKLADMYTSLQSSRSYVYSVARDCDNGKVDRK-DC 339

                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 4557235   416 AISKIFGSEAAWKVTDECIQIMGGMGFMKEPGVERVLRDLRIFRIFEGTNDILRLFV 472
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 ...
 327-473 6.56e-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: 6.56e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557235    327 GSGFKVAMHILNNGRFGMAAALAGTMRGIIAKAVDHATNRTQFGEKIHNFGLIQEKLARMVMLQYVTESMAYMVSANMDQ 406
Cdd:pfam00441   1 GRGFRVAMETLNHERLAIAAMALGLARRALDEALAYARRRKAFGRPLIDFQLVRHKLAEMAAEIEAARLLVYRAAEALDA 80

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 4557235    407 GATDfQIEAAISKIFGSEAAWKVTDECIQIMGGMGFMKEPGVERVLRDLRIFRIFEGTNDILRLFVA 473
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 ...
 72-481 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: 749.30  E-value: 0e+00
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557235   72 SFAVGMFKGQLTTDQVFPYPSVLNEEQTQFLKELVEPVSRFFEEVNDPAKNDALEMVEETTWQGLKELGAFGLQVPSELG 151
Cdd:cd01161   1 SFALNMFLGDIVTKQVFPYPSVLTEEQTEELNMLVGPVEKFFEEVNDPAKNDQLEKIPRKTLTQLKELGLFGLQVPEEYG 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557235  152 GVGLCNTQYARLVEIVGMhDLGVGITLGAHQSIGFKGILLFGTKAQKEKYLPKLASGETVAAFCLTEPSSGSDAASIRTS 231
Cdd:cd01161  81 GLGLNNTQYARLAEIVGM-DLGFSVTLGAHQSIGFKGILLFGTEAQKEKYLPKLASGEWIAAFALTEPSSGSDAASIRTT 159

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557235  232 AVPSPCGKYYTLNGSKLWISNGGLADIFTVFAKTPVTDPaTGAVKEKITAFVVERGFGGITHGPPEKKMGIKASNTAEVF 311
Cdd:cd01161 160 AVLSEDGKHYVLNGSKIWITNGGIADIFTVFAKTEVKDA-TGSVKDKITAFIVERSFGGVTNGPPEKKMGIKGSNTAEVY 238

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557235  312 FDGVRVPSENVLGEVGSGFKVAMHILNNGRFGMAAALAGTMRGIIAKAVDHATNRTQFGEKIHNFGLIQEKLARMVMLQY 391
Cdd:cd01161 239 FEDVKIPVENVLGEVGDGFKVAMNILNNGRFGMGAALIGTMKRCIEKAVDYANNRKQFGKKIHEFGLIQEKLANMAILQY 318

                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557235  392 VTESMAYMVSANMDQGAT-DFQIEAAISKIFGSEAAWKVTDECIQIMGGMGFMKEPGVERVLRDLRIFRIFEGTNDILRL 470
Cdd:cd01161 319 ATESMAYMTSGNMDRGLKaEYQIEAAISKVFASEAAWLVVDEAIQIHGGMGFMREYGVERVLRDLRIFRIFEGTNEILRL 398

                       410
                ....*....|.
gi 4557235  471 FVALQGCMDKG 481
Cdd:cd01161 399 FIALTGLQHAG 409
CaiA COG1960
Acyl-CoA dehydrogenase related to the alkylation response protein AidB [Lipid transport and ...
 94-473 1.22e-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: 402.30  E-value: 1.22e-135
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557235   94 LNEEQTQFLKElvepVSRFFEEVNDP--AKNDALEMVEETTWQGLKELGAFGLQVPSELGGVGLCNTQYARLVEIVGMHD 171
Cdd:COG1960   5 LTEEQRALRDE----VREFAEEEIAPeaREWDREGEFPRELWRKLAELGLLGLTIPEEYGGLGLSLVELALVLEELARAD 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557235  172 LGVGITLGAHQSIGfKGILLFGTKAQKEKYLPKLASGETVAAFCLTEPSSGSDAASIRTSAVPSpcGKYYTLNGSKLWIS 251
Cdd:COG1960  81 ASLALPVGVHNGAA-EALLRFGTEEQKERYLPRLASGEWIGAFALTEPGAGSDAAALRTTAVRD--GDGYVLNGQKTFIT 157

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557235  252 NGGLADIFTVFAKTpvtDPATGAvkEKITAFVVERGFGGITHGPPEKKMGIKASNTAEVFFDGVRVPSENVLGEVGSGFK 331
Cdd:COG1960 158 NAPVADVILVLART---DPAAGH--RGISLFLVPKDTPGVTVGRIEDKMGLRGSDTGELFFDDVRVPAENLLGEEGKGFK 232

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557235  332 VAMHILNNGRFGMAAALAGTMRGIIAKAVDHATNRTQFGEKIHNFGLIQEKLARMVMLQYVTESMAYMVSANMDQGAtDF 411
Cdd:COG1960 233 IAMSTLNAGRLGLAAQALGIAEAALELAVAYAREREQFGRPIADFQAVQHRLADMAAELEAARALVYRAAWLLDAGE-DA 311

                       330       340       350       360       370       380
                ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 4557235  412 QIEAAISKIFGSEAAWKVTDECIQIMGGMGFMKEPGVERVLRDLRIFRIFEGTNDILRLFVA 473
Cdd:COG1960 312 ALEAAMAKLFATEAALEVADEALQIHGGYGYTREYPLERLYRDARILTIYEGTNEIQRLIIA 373
SCAD_SBCAD cd01158
Short chain acyl-CoA dehydrogenases and eukaryotic short/branched chain acyl-CoA ...
 96-473 1.99e-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: 363.13  E-value: 1.99e-120
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557235   96 EEQTQFLKElvepVSRFFEEVNDP--AKNDALEMVEETTWQGLKELGAFGLQVPSELGGVGLCNTQYARLVEIVGMHDLG 173
Cdd:cd01158   1 EEHQMIRKT----VRDFAEKEIAPlaAEMDEKGEFPREVIKEMAELGLMGIPIPEEYGGAGLDFLAYAIAIEELAKVDAS 76

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557235  174 VGITLGAHQSIGFKGILLFGTKAQKEKYLPKLASGETVAAFCLTEPSSGSDAASIRTSAVPSpcGKYYTLNGSKLWISNG 253
Cdd:cd01158  77 VAVIVSVHNSLGANPIIKFGTEEQKKKYLPPLATGEKIGAFALSEPGAGSDAAALKTTAKKD--GDDYVLNGSKMWITNG 154

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557235  254 GLADIFTVFAktpVTDPATGavKEKITAFVVERGFGGITHGPPEKKMGIKASNTAEVFFDGVRVPSENVLGEVGSGFKVA 333
Cdd:cd01158 155 GEADFYIVFA---VTDPSKG--YRGITAFIVERDTPGLSVGKKEDKLGIRGSSTTELIFEDVRVPKENILGEEGEGFKIA 229

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557235  334 MHILNNGRFGMAAALAGTMRGIIAKAVDHATNRTQFGEKIHNFGLIQEKLARMVMLQYVTESMAYMVSANMDQGaTDFQI 413
Cdd:cd01158 230 MQTLDGGRIGIAAQALGIAQAALDAAVDYAKERKQFGKPIADFQGIQFKLADMATEIEAARLLTYKAARLKDNG-EPFIK 308

                       330       340       350       360       370       380
                ....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557235  414 EAAISKIFGSEAAWKVTDECIQIMGGMGFMKEPGVERVLRDLRIFRIFEGTNDILRLFVA 473
Cdd:cd01158 309 EAAMAKLFASEVAMRVTTDAVQIFGGYGYTKDYPVERYYRDAKITEIYEGTSEIQRLVIA 368
ACAD cd00567
Acyl-CoA dehydrogenase; Both mitochondrial acyl-CoA dehydrogenases (ACAD) and peroxisomal ...
 189-473 1.88e-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: 317.69  E-value: 1.88e-103
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557235  189 ILLFGTKAQKEKYLPKLASGETVAAFCLTEPSSGSDAASIRTSAVPSpcGKYYTLNGSKLWISNGGLADIFTVFAKTPVT 268
Cdd:cd00567  48 LLAYGTEEQKERYLPPLASGEAIAAFALTEPGAGSDLAGIRTTARKD--GDGYVLNGRKIFISNGGDADLFIVLARTDEE 125

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557235  269 DPATGAvkekITAFVVERGFGGITHGPPEKKMGIKASNTAEVFFDGVRVPSENVLGEVGSGFKVAMHILNNGRFGMAAAL 348
Cdd:cd00567 126 GPGHRG----ISAFLVPADTPGVTVGRIWDKMGMRGSGTGELVFDDVRVPEDNLLGEEGGGFELAMKGLNVGRLLLAAVA 201

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557235  349 AGTMRGIIAKAVDHATNRTQFGEKIHNFGLIQEKLARMVMLQYVTESMAYMVSANMDQGATDFQIEAAISKIFGSEAAWK 428
Cdd:cd00567 202 LGAARAALDEAVEYAKQRKQFGKPLAEFQAVQFKLADMAAELEAARLLLYRAAWLLDQGPDEARLEAAMAKLFATEAARE 281

                       250       260       270       280
                ....*....|....*....|....*....|....*....|....*
gi 4557235  429 VTDECIQIMGGMGFMKEPGVERVLRDLRIFRIFEGTNDILRLFVA 473
Cdd:cd00567 282 VADLAMQIHGGRGYSREYPVERYLRDARAARIAEGTAEIQRLIIA 326
IVD cd01156
Isovaleryl-CoA dehydrogenase; Isovaleryl-CoA dehydrogenase (IVD) is an is an acyl-CoA ...
 94-473 1.21e-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: 286.23  E-value: 1.21e-90
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557235   94 LNEEQTQflkeLVEPVSRFFEEVNDP--AKNDALEMVEETTWQGLKELGAFGLQVPSELGGVGLCNTQYARLVEIVGMHD 171
Cdd:cd01156   2 LDDEIEM----LRQSVREFAQKEIAPlaAKIDRDNEFPRDLWRKMGKLGLLGITAPEEYGGSGMGYLAHVIIMEEISRAS 77

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557235  172 LGVGITLGAHQSIGFKGILLFGTKAQKEKYLPKLASGETVAAFCLTEPSSGSDAASIRTSAvpSPCGKYYTLNGSKLWIS 251
Cdd:cd01156  78 GSVALSYGAHSNLCINQIYRNGSAAQKEKYLPKLISGEHIGALAMSEPNAGSDVVSMKLRA--EKKGDRYVLNGSKMWIT 155

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557235  252 NGGLADIFTVFAKTpvtDPATGAvkEKITAFVVERGFGGITHGPPEKKMGIKASNTAEVFFDGVRVPSENVLGEVGSGFK 331
Cdd:cd01156 156 NGPDADTLVVYAKT---DPSAGA--HGITAFIVEKGMPGFSRAQKLDKLGMRGSNTCELVFEDCEVPEENILGGENKGVY 230

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557235  332 VAMHILNNGRFGMAAALAGTMRGIIAKAVDHATNRTQFGEKIHNFGLIQEKLARMVMLQYVTESMAYMVSANMDQGATDf 411
Cdd:cd01156 231 VLMSGLDYERLVLAGGPIGIMQAALDVAIPYAHQRKQFGQPIGEFQLVQGKLADMYTRLNASRSYLYTVAKACDRGNMD- 309

                       330       340       350       360       370       380
                ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 4557235  412 QIEAAISKIFGSEAAWKVTDECIQIMGGMGFMKEPGVERVLRDLRIFRIFEGTNDILRLFVA 473
Cdd:cd01156 310 PKDAAGVILYAAEKATQVALDAIQILGGNGYINDYPTGRLLRDAKLYEIGAGTSEIRRMVIG 371
IBD cd01162
Isobutyryl-CoA dehydrogenase; Isobutyryl-CoA dehydrogenase (IBD) catalyzes the alpha, beta- ...
 138-473 8.20e-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: 252.75  E-value: 8.20e-78
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557235  138 ELGAFGLQVPSELGGVGLCNTQYARLVEIVGMHDLGVGITLGAHQSIGFKgILLFGTKAQKEKYLPKLASGETVAAFCLT 217
Cdd:cd01162  43 ELGFGGIYIRDDVGGSGLSRLDASIIFEALSTGCVSTAAYISIHNMCAWM-IDSFGNDEQRERFLPDLCTMEKLASYCLT 121

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557235  218 EPSSGSDAASIRTSAVPSpcGKYYTLNGSKLWISNGGLADIFTVFAKTpvtdpaTGAVKEKITAFVVERGFGGITHGPPE 297
Cdd:cd01162 122 EPGSGSDAAALRTRAVRE--GDHYVLNGSKAFISGAGDSDVYVVMART------GGEGPKGISCFVVEKGTPGLSFGANE 193

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557235  298 KKMGIKASNTAEVFFDGVRVPSENVLGEVGSGFKVAMHILNNGRFGMAAALAGTMRGIIAKAVDHATNRTQFGEKIHNFG 377
Cdd:cd01162 194 KKMGWNAQPTRAVIFEDCRVPVENRLGGEGQGFGIAMAGLNGGRLNIASCSLGAAQAALDLARAYLEERKQFGKPLADFQ 273

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557235  378 LIQEKLARMVMLQYVTESMAYMVSANMDQGATDFQIEAAISKIFGSEAAWKVTDECIQIMGGMGFMKEPGVERVLRDLRI 457
Cdd:cd01162 274 ALQFKLADMATELVASRLMVRRAASALDRGDPDAVKLCAMAKRFATDECFDVANQALQLHGGYGYLKDYPVEQYVRDLRV 353

                       330
                ....*....|....*.
gi 4557235  458 FRIFEGTNDILRLFVA 473
Cdd:cd01162 354 HQILEGTNEIMRLIIA 369
LCAD cd01160
Long chain acyl-CoA dehydrogenase; LCAD is an acyl-CoA dehydrogenases (ACAD), which is found ...
 109-475 9.08e-74

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: 242.02  E-value: 9.08e-74
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557235  109 VSRFFEEVNDP--AKNDALEMVEETTWQGLKELGAFGLQVPSELGGVGLcNTQYARLVEIVGMHDLGVGITLGAHQSIGF 186
Cdd:cd01160  10 VRRFFAKEVAPfhHEWEKAGEVPREVWRKAGEQGLLGVGFPEEYGGIGG-DLLSAAVLWEELARAGGSGPGLSLHTDIVS 88

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557235  187 KGILLFGTKAQKEKYLPKLASGETVAAFCLTEPSSGSDAASIRTSAVPSpcGKYYTLNGSKLWISNGGLADIFTVFAKTp 266
Cdd:cd01160  89 PYITRAGSPEQKERVLPQMVAGKKIGAIAMTEPGAGSDLQGIRTTARKD--GDHYVLNGSKTFITNGMLADVVIVVART- 165

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557235  267 vTDPATGAvkEKITAFVVERGFGGITHGPPEKKMGIKASNTAEVFFDGVRVPSENVLGEVGSGFKVAMHILNNGRFGMAA 346
Cdd:cd01160 166 -GGEARGA--GGISLFLVERGTPGFSRGRKLKKMGWKAQDTAELFFDDCRVPAENLLGEENKGFYYLMQNLPQERLLIAA 242

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557235  347 ALAGTMRGIIAKAVDHATNRTQFGEKIHNFGLIQEKLARMVMLQYVTESMAYMVSANMDQGATDfQIEAAISKIFGSEAA 426
Cdd:cd01160 243 GALAAAEFMLEETRNYVKQRKAFGKTLAQLQVVRHKIAELATKVAVTRAFLDNCAWRHEQGRLD-VAEASMAKYWATELQ 321

                       330       340       350       360
                ....*....|....*....|....*....|....*....|....*....
gi 4557235  427 WKVTDECIQIMGGMGFMKEPGVERVLRDLRIFRIFEGTNDILRLFVALQ 475
Cdd:cd01160 322 NRVAYECVQLHGGWGYMREYPIARAYRDARVQPIYGGTTEIMKELISRQ 370
PLN02519 PLN02519
isovaleryl-CoA dehydrogenase
 96-472 1.81e-65

isovaleryl-CoA dehydrogenase


Pssm-ID: 215284 [Multi-domain]  Cd Length: 404  Bit Score: 220.90  E-value: 1.81e-65
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557235    96 EEQTQFLKELVEPVSRFFEEVNDPAKNDALemveettWQGLKELGAFGLQVPSELGGVGLCNTQYARLVEIVGMHDLGVG 175
Cdd:PLN02519  35 ESVQQFAQENIAPHAAAIDATNSFPKDVNL-------WKLMGDFNLHGITAPEEYGGLGLGYLYHCIAMEEISRASGSVG 107

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557235   176 ITLGAHQSIGFKGILLFGTKAQKEKYLPKLASGETVAAFCLTEPSSGSDAASIRTSAVPSPCGkyYTLNGSKLWISNGGL 255
Cdd:PLN02519 108 LSYGAHSNLCINQLVRNGTPAQKEKYLPKLISGEHVGALAMSEPNSGSDVVSMKCKAERVDGG--YVLNGNKMWCTNGPV 185

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557235   256 ADIFTVFAKTpvtDPATGAvkEKITAFVVERGFGGITHGPPEKKMGIKASNTAEVFFDGVRVPSENVLGEVGSGFKVAMH 335
Cdd:PLN02519 186 AQTLVVYAKT---DVAAGS--KGITAFIIEKGMPGFSTAQKLDKLGMRGSDTCELVFENCFVPEENVLGQEGKGVYVMMS 260

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557235   336 ILNNGRFGMAAALAGTMRGIIAKAVDHATNRTQFGEKIHNFGLIQEKLARMVMLQYVTESMAYMVSANMDQGATDFQiEA 415
Cdd:PLN02519 261 GLDLERLVLAAGPLGLMQACLDVVLPYVRQREQFGRPIGEFQFIQGKLADMYTSLQSSRSYVYSVARDCDNGKVDRK-DC 339

                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 4557235   416 AISKIFGSEAAWKVTDECIQIMGGMGFMKEPGVERVLRDLRIFRIFEGTNDILRLFV 472
Cdd:PLN02519 340 AGVILCAAERATQVALQAIQCLGGNGYINEYPTGRLLRDAKLYEIGAGTSEIRRMLI 396
GCD cd01151
Glutaryl-CoA dehydrogenase; Glutaryl-CoA dehydrogenase (GCD). GCD is an acyl-CoA dehydrogenase, ...
 78-487 8.69e-64

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: 8.69e-64
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557235   78 FKGQLTTDQVfpypsVLNEEQTQFLKELVEP--VSRFFEEVNDPakndalEMVEEttwqgLKELGAFGLQvPSELGGVGL 155
Cdd:cd01151   9 LDDLLTEEER-----AIRDTAREFCQEELAPrvLEAYREEKFDR------KIIEE-----MGELGLLGAT-IKGYGCAGL 71

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557235  156 CNTQY---ARLVEIVgmhDLGVGITLGAHQSIGFKGILLFGTKAQKEKYLPKLASGETVAAFCLTEPSSGSDAASIRTSA 232
Cdd:cd01151  72 SSVAYgliAREVERV---DSGYRSFMSVQSSLVMLPIYDFGSEEQKQKYLPKLASGELIGCFGLTEPNHGSDPGGMETRA 148

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557235  233 vpSPCGKYYTLNGSKLWISNGGLADIFTVFAKTPVTDpatgavkeKITAFVVERGFGGITHGPPEKKMGIKASNTAEVFF 312
Cdd:cd01151 149 --RKDGGGYKLNGSKTWITNSPIADVFVVWARNDETG--------KIRGFILERGMKGLSAPKIQGKFSLRASITGEIVM 218

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557235  313 DGVRVPSENVLGEVgSGFKVAMHILNNGRFGMAAALAGTMRGIIAKAVDHATNRTQFGEKIHNFGLIQEKLARM-VMLQY 391
Cdd:cd01151 219 DNVFVPEENLLPGA-EGLRGPFKCLNNARYGIAWGALGAAEDCYHTARQYVLDRKQFGRPLAAFQLVQKKLADMlTEIAL 297

                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557235  392 VTEsMAYMVSANMDQG-ATDFQIeaAISKIFGSEAAWKVTDECIQIMGGMGFMKEPGVERVLRDLRIFRIFEGTNDILRL 470
Cdd:cd01151 298 GLL-ACLRVGRLKDQGkATPEQI--SLLKRNNCGKALEIARTAREMLGGNGISDEYHIIRHMVNLESVNTYEGTHDIHAL 374

                       410
                ....*....|....*..
gi 4557235  471 FValqgcmdkGKELSGL 487
Cdd:cd01151 375 IL--------GRAITGI 383
MCAD cd01157
Medium chain acyl-CoA dehydrogenase; MCADs are mitochondrial beta-oxidation enzymes, which ...
 94-473 1.39e-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: 215.14  E-value: 1.39e-63
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557235   94 LNEEQtqflKELVEPVSRFFEEVNDPAKNDaLEMVEETTWQGLK---ELGAFGLQVPSELGGVGLCNTQYARLVEIVGMH 170
Cdd:cd01157   1 LTEQQ----KEFQETARKFAREEIIPVAAE-YDKSGEYPWPLIKrawELGLMNTHIPEDCGGLGLGTFDTCLITEELAYG 75

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557235  171 DLGVGITLGAHqSIGFKGILLFGTKAQKEKYLPKLASGETVAAFCLTEPSSGSDAASIRTSAVPSpcGKYYTLNGSKLWI 250
Cdd:cd01157  76 CTGVQTAIEAN-SLGQMPVIISGNDEQKKKYLGRMTEEPLMCAYCVTEPGAGSDVAGIKTKAEKK--GDEYIINGQKMWI 152

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557235  251 SNGGLADIFTVFAKTPvTDPATGAVKeKITAFVVERGFGGITHGPPEKKMGIKASNTAEVFFDGVRVPSENVLGEVGSGF 330
Cdd:cd01157 153 TNGGKANWYFLLARSD-PDPKCPASK-AFTGFIVEADTPGIQPGRKELNMGQRCSDTRGITFEDVRVPKENVLIGEGAGF 230

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557235  331 KVAMHILNNGRFGMAAALAGTMRGIIAKAVDHATNRTQFGEKIHNFGLIQEKLARMVMlQYVTESMAYMVSAN-MDQGAT 409
Cdd:cd01157 231 KIAMGAFDKTRPPVAAGAVGLAQRALDEATKYALERKTFGKLIAEHQAVSFMLADMAM-KVELARLAYQRAAWeVDSGRR 309

                       330       340       350       360       370       380
                ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 4557235  410 DfQIEAAISKIFGSEAAWKVTDECIQIMGGMGFMKEPGVERVLRDLRIFRIFEGTNDILRLFVA 473
Cdd:cd01157 310 N-TYYASIAKAFAADIANQLATDAVQIFGGNGFNSEYPVEKLMRDAKIYQIYEGTSQIQRLIIS 372
PTZ00461 PTZ00461
isovaleryl-CoA dehydrogenase; Provisional
 103-464 1.25e-62

isovaleryl-CoA dehydrogenase; Provisional


Pssm-ID: 185640 [Multi-domain]  Cd Length: 410  Bit Score: 213.65  E-value: 1.25e-62
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557235   103 KELVEPVSRFFEEVNDP-AKNDALEM-VEETTWQGLKELGAFGLQVPSELGGVGLCNTQYARLVEIVGMHDLGVGITLGA 180
Cdd:PTZ00461  42 AALRETVAKFSREVVDKhAREDDINMhFNRDLFKQLGDLGVMGVTVPEADGGAGMDAVAAVIIHHELSKYDPGFCLAYLA 121

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557235   181 HQSIGFKGILLFGTKAQKEKYLPKLASGETVAAFCLTEPSSGSDAASIRTSAVPSPCGKYyTLNGSKLWISNGGLADIFT 260
Cdd:PTZ00461 122 HSMLFVNNFYYSASPAQRARWLPKVLTGEHVGAMGMSEPGAGTDVLGMRTTAKKDSNGNY-VLNGSKIWITNGTVADVFL 200

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557235   261 VFAKtpvtdpatgaVKEKITAFVVERGFGGITHGPPEKKMGIKASNTAEVFFDGVRVPSENVLGEVGSGFKVAMHILNNG 340
Cdd:PTZ00461 201 IYAK----------VDGKITAFVVERGTKGFTQGPKIDKCGMRASHMCQLFFEDVVVPAENLLGEEGKGMVGMMRNLELE 270

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557235   341 RFGMAAALAGTMRGIIAKAVDHATNRTQFGEKIHNFGLIQEKLARMVMLQYVTESMAYMVSANMDQGATDfQIEAAISKI 420
Cdd:PTZ00461 271 RVTLAAMAVGIAERSVELMTSYASERKAFGKPISNFGQIQRYIAEGYADTEAAKALVYSVSHNVHPGNKN-RLGSDAAKL 349

                        330       340       350       360
                 ....*....|....*....|....*....|....*....|....
gi 4557235   421 FGSEAAWKVTDECIQIMGGMGFMKEPGVERVLRDLRIFRIFEGT 464
Cdd:PTZ00461 350 FATPIAKKVADSAIQVMGGMGYSRDMPVERLWRDAKLLEIGGGT 393
ACAD_fadE5 cd01153
Putative acyl-CoA dehydrogenases similar to fadE5; Putative acyl-CoA dehydrogenase (ACAD). ...
 138-467 1.79e-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: 188.75  E-value: 1.79e-53
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557235  138 ELGAFGLQVPSELGGVGLCNTQYARLVEIVGMHDLGVGITLGAHQsiGFKGILLFGTKAQKEKYLPKLASGETVAAFCLT 217
Cdd:cd01153  47 EAGWMALGVPEEYGGQGLPITVYSALAEIFSRGDAPLMYASGTQG--AAATLLAHGTEAQREKWIPRLAEGEWTGTMCLT 124

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557235  218 EPSSGSDAASIRTSAVPSPCGKYYtLNGSKLWISNG--GLAD--IFTVFAKTPvtDPATGAvkEKITAFVV-------ER 286
Cdd:cd01153 125 EPDAGSDLGALRTKAVYQADGSWR-INGVKRFISAGehDMSEniVHLVLARSE--GAPPGV--KGLSLFLVpkflddgER 199

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557235  287 GfgGITHGPPEKKMGIKASNTAEVFFDGVRVPsenVLGEVGSGFKVAMHILNNGRFGMAAALAGTMRGIIAKAVDHATNR 366
Cdd:cd01153 200 N--GVTVARIEEKMGLHGSPTCELVFDNAKGE---LIGEEGMGLAQMFAMMNGARLGVGTQGTGLAEAAYLNALAYAKER 274

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557235  367 TQFGEKIHNFGLIQEKLARMVMLQYVTESMAYMVSANMD-----------QGATDFQIEAA----------ISKIFGSEA 425
Cdd:cd01153 275 KQGGDLIKAAPAVTIIHHPDVRRSLMTQKAYAEGSRALDlytatvqdlaeRKATEGEDRKAlsaladlltpVVKGFGSEA 354

                       330       340       350       360
                ....*....|....*....|....*....|....*....|..
gi 4557235  426 AWKVTDECIQIMGGMGFMKEPGVERVLRDLRIFRIFEGTNDI 467
Cdd:cd01153 355 ALEAVSDAIQVHGGSGYTREYPIEQYYRDARITTIYEGTTGI 396
PRK12341 PRK12341
acyl-CoA dehydrogenase;
94-468 7.38e-50

acyl-CoA dehydrogenase;


Pssm-ID: 183454 [Multi-domain]  Cd Length: 381  Bit Score: 178.00  E-value: 7.38e-50
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557235    94 LNEEQTQFLKELVEPVSRFFEEvNDPAKNDALEMVEETTWQGLKELGAFGLQVPSELGGVGLCNTQYARLVEivGMHDLG 173
Cdd:PRK12341   5 LTEEQELLLASIRELITRNFPE-EYFRTCDENGTYPREFMRALADNGISMLGVPEEFGGTPADYVTQMLVLE--EVSKCG 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557235   174 VGITLgAHQSIGFKGILLFGTKAQKEKYLpKLASGETVAAFCL--TEPSSGSDAASIRTSAVPSPcGKYYtLNGSKLWIS 251
Cdd:PRK12341  82 APAFL-ITNGQCIHSMRRFGSAEQLRKTA-ESTLETGDPAYALalTEPGAGSDNNSATTTYTRKN-GKVY-LNGQKTFIT 157

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557235   252 NGGLADIFTVFAKtpvtDPATGAVKEKITAFVVERGFGGITHGPPEKkMGIKASNTAEVFFDGVRVPSENVLGEVGSGFK 331
Cdd:PRK12341 158 GAKEYPYMLVLAR----DPQPKDPKKAFTLWWVDSSKPGIKINPLHK-IGWHMLSTCEVYLDNVEVEESDLVGEEGMGFL 232

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557235   332 VAMHILNNGRFGMAAALAGTMRGIIAKAVDHATNRTQFGEKIHNFGLIQEKLARMVMLQYVTESMAYMVSANMDQGATdF 411
Cdd:PRK12341 233 NVMYNFEMERLINAARSLGFAECAFEDAARYANQRIQFGKPIGHNQLIQEKLTLMAIKIENMRNMVYKVAWQADNGQS-L 311

                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 4557235   412 QIEAAISKIFGSEAAWKVTDECIQIMGGMGFMKEPGVERVLRDLRIFRIFEGTNDIL 468
Cdd:PRK12341 312 RTSAALAKLYCARTAMEVIDDAIQIMGGLGYTDEARVSRFWRDVRCERIGGGTDEIM 368
PRK03354 PRK03354
crotonobetainyl-CoA dehydrogenase; Validated
 134-470 5.88e-42

crotonobetainyl-CoA dehydrogenase; Validated


Pssm-ID: 179566 [Multi-domain]  Cd Length: 380  Bit Score: 156.14  E-value: 5.88e-42
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557235   134 QGLKELGAFGLQVPSELGGVGLCNTQYARLVEIVGMhdLGVGITLGAHQSIGFKGILLFGTKAQKEKYLPKLASGETVAA 213
Cdd:PRK03354  44 KALADMGIDSLLIPEEHGGLDAGFVTLAAVWMELGR--LGAPTYVLYQLPGGFNTFLREGTQEQIDKIMAFRGTGKQMWN 121

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557235   214 FCLTEPSSGSDAASIRTSAVPSPcGKYYtLNGSKLWISNGGLADIFTVFAKTPVTDPatgavKEKITAFVVERGFGGITH 293
Cdd:PRK03354 122 SAITEPGAGSDVGSLKTTYTRRN-GKVY-LNGSKCFITSSAYTPYIVVMARDGASPD-----KPVYTEWFVDMSKPGIKV 194

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557235   294 GPPEKkMGIKASNTAEVFFDGVRVPSENVLGEVGSGFKVAMHILNNGRFGMAAALAGTMRGIIAKAVDHATNRTQFGEKI 373
Cdd:PRK03354 195 TKLEK-LGLRMDSCCEITFDDVELDEKDMFGREGNGFNRVKEEFDHERFLVALTNYGTAMCAFEDAARYANQRVQFGEAI 273

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557235   374 HNFGLIQEKLARMVMLQYVTESMAYMVSANMDQGATDfQIEAAISKIFGSEAAWKVTDECIQIMGGMGFMKEPGVERVLR 453
Cdd:PRK03354 274 GRFQLIQEKFAHMAIKLNSMKNMLYEAAWKADNGTIT-SGDAAMCKYFCANAAFEVVDSAMQVLGGVGIAGNHRISRFWR 352

                        330
                 ....*....|....*..
gi 4557235   454 DLRIFRIFEGTNDILRL 470
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 ...
 327-473 6.56e-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: 6.56e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557235    327 GSGFKVAMHILNNGRFGMAAALAGTMRGIIAKAVDHATNRTQFGEKIHNFGLIQEKLARMVMLQYVTESMAYMVSANMDQ 406
Cdd:pfam00441   1 GRGFRVAMETLNHERLAIAAMALGLARRALDEALAYARRRKAFGRPLIDFQLVRHKLAEMAAEIEAARLLVYRAAEALDA 80

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 4557235    407 GATDfQIEAAISKIFGSEAAWKVTDECIQIMGGMGFMKEPGVERVLRDLRIFRIFEGTNDILRLFVA 473
Cdd:pfam00441  81 GGPD-GAEASMAKLYASEAAVEVADLAMQLHGGYGYLREYPVERLYRDARVLRIGEGTSEIQRNIIA 146
ACAD_fadE6_17_26 cd01152
Putative acyl-CoA dehydrogenases similar to fadE6, fadE17, and fadE26; Putative acyl-CoA ...
 132-473 5.13e-38

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: 145.18  E-value: 5.13e-38
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557235  132 TWQG-LKELGAFGLQVPSELGGVGLCNTQYARLVE---IVGM--HDLGVGITLGAHQsigfkgILLFGTKAQKEKYLPKL 205
Cdd:cd01152  39 RWQRaLAAAGWAAPGWPKEYGGRGASLMEQLIFREemaAAGApvPFNQIGIDLAGPT------ILAYGTDEQKRRFLPPI 112

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557235  206 ASGETVaaFCL--TEPSSGSDAASIRTSAVPSpcGKYYTLNGSKLWISNGGLADIFTVFAKTpvtDPAtgAVKEK-ITAF 282
Cdd:cd01152 113 LSGEEI--WCQgfSEPGAGSDLAGLRTRAVRD--GDDWVVNGQKIWTSGAHYADWAWLLVRT---DPE--APKHRgISIL 183

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557235  283 VVERGFGGITHGPPEKKMGikASNTAEVFFDGVRVPSENVLGEVGSGFKVAMHILNNGRFGMAAALAGTMRGIIAKAvdH 362
Cdd:cd01152 184 LVDMDSPGVTVRPIRSING--GEFFNEVFLDDVRVPDANRVGEVNDGWKVAMTTLNFERVSIGGSAATFFELLLARL--L 259

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557235  363 ATNRTQFGEkiHNFGLIQEKLARMVM----LQYVTESMAYMVSANMDQGAtdfqiEAAISKIFGSEAAWKVTDECIQIMG 438
Cdd:cd01152 260 LLTRDGRPL--IDDPLVRQRLARLEAeaeaLRLLVFRLASALAAGKPPGA-----EASIAKLFGSELAQELAELALELLG 332

                       330       340       350       360
                ....*....|....*....|....*....|....*....|...
gi 4557235  439 GMGFMKEPG--------VERVLRDLRIFRIFEGTNDILRLFVA 473
Cdd:cd01152 333 TAALLRDPApgaelagrWEADYLRSRATTIYGGTSEIQRNIIA 375
ACAD_FadE2 cd01155
Acyl-CoA dehydrogenases similar to fadE2; FadE2-like Acyl-CoA dehydrogenase (ACAD). Acyl-CoA ...
 102-463 3.29e-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: 137.52  E-value: 3.29e-35
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557235  102 LKELVEPVSRFFEEVNDPAKNDALEMVEE---TTWQ------GLKE----LGAFGLQVPSELGGVGLCNTQYARLVEIVG 168
Cdd:cd01155   3 AQELRARVKAFMEEHVYPAEQEFLEYYAEggdRWWTpppiieKLKAkakaEGLWNLFLPEVSGLSGLTNLEYAYLAEETG 82

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557235  169 MHDLGVGITLGAHQSIGFKGIL-LFGTKAQKEKYLPKLASGETVAAFCLTEPS-SGSDAASIRTSAVPSpcGKYYTLNGS 246
Cdd:cd01155  83 RSFFAPEVFNCQAPDTGNMEVLhRYGSEEQKKQWLEPLLDGKIRSAFAMTEPDvASSDATNIECSIERD--GDDYVINGR 160

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557235  247 KLWISNGGLAD--IFTVFAKTpvtDPATGAVKEKITAFVVERGFGGITHGPPEKKMGIKAS--NTAEVFFDGVRVPSENV 322
Cdd:cd01155 161 KWWSSGAGDPRckIAIVMGRT---DPDGAPRHRQQSMILVPMDTPGVTIIRPLSVFGYDDAphGHAEITFDNVRVPASNL 237

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557235  323 LGEVGSGFKVAMHILNNGRFGMAAALAGTMRGIIAKAVDHATNRTQFGEKIHNFGLIQEKLA--RMV--MLQYVTESMAY 398
Cdd:cd01155 238 ILGEGRGFEIAQGRLGPGRIHHCMRLIGAAERALELMCQRAVSREAFGKKLAQHGVVAHWIAksRIEieQARLLVLKAAH 317

                       330       340       350       360       370       380
                ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 4557235  399 MvsanMDQ-GATDFQIEAAISKIFGSEAAWKVTDECIQIMGGMGFMKEPGVERVLRDLRIFRIFEG 463
Cdd:cd01155 318 M----IDTvGNKAARKEIAMIKVAAPRMALKIIDRAIQVHGAAGVSQDTPLANMYAWARTLRIADG 379
PLN02526 PLN02526
acyl-coenzyme A oxidase
 81-489 1.09e-33

acyl-coenzyme A oxidase


Pssm-ID: 178141 [Multi-domain]  Cd Length: 412  Bit Score: 133.44  E-value: 1.09e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557235    81 QLTTDQVFPyPSVLN----------EEQT------QFLKELVEPV-SRFFEEVNDPakndalemveettWQGLKELGAFG 143
Cdd:PLN02526   8 QATPASIFP-PSVSDyyqfddlltpEEQAlrkrvrECMEKEVAPImTEYWEKAEFP-------------FHIIPKLGSLG 73

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557235   144 LqvpseLGGV-------GLCNTQYARLVEIVGMHDLGVGITLGAHQSIGFKGILLFGTKAQKEKYLPKLASGETVAAFCL 216
Cdd:PLN02526  74 I-----AGGTikgygcpGLSITASAIATAEVARVDASCSTFILVHSSLAMLTIALCGSEAQKQKYLPSLAQLDTVACWAL 148

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557235   217 TEPSSGSDAASIRTSAVPSPCGkyYTLNGSKLWISNGGLADIFTVFAKTPVTDpatgavkeKITAFVVERGFGGITHGPP 296
Cdd:PLN02526 149 TEPDYGSDASSLNTTATKVEGG--WILNGQKRWIGNSTFADVLVIFARNTTTN--------QINGFIVKKGAPGLKATKI 218

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557235   297 EKKMGIKASNTAEVFFDGVRVPSENVLGEVGSgFKVAMHILNNGRFGMAAALAGTMRGIIAKAVDHATNRTQFGEKIHNF 376
Cdd:PLN02526 219 ENKIGLRMVQNGDIVLKDVFVPDEDRLPGVNS-FQDTNKVLAVSRVMVAWQPIGISMGVYDMCHRYLKERKQFGAPLAAF 297

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557235   377 GLIQEKLARmvMLQYVtESMAYM--------VSANMDQGatdfqiEAAISKIFGSEAAWKVTDECIQIMGGMGFMKEPGV 448
Cdd:PLN02526 298 QINQEKLVR--MLGNI-QAMFLVgwrlcklyESGKMTPG------HASLGKAWITKKARETVALGRELLGGNGILADFLV 368

                        410       420       430       440
                 ....*....|....*....|....*....|....*....|.
gi 4557235   449 ERVLRDLRIFRIFEGTNDILRLFValqgcmdkGKELSGLGS 489
Cdd:PLN02526 369 AKAFCDLEPIYTYEGTYDINALVT--------GREITGIAS 401
AidB cd01154
Proteins involved in DNA damage response, similar to the AidB gene product; AidB is one of ...
 199-470 2.28e-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: 2.28e-31
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557235  199 EKYLPKLASGET----VAAFCLTEPSSGSDAASIRTSAVPSPcGKYYTLNGSKlWISNGGLADIFTVFAKTPVTDPATGA 274
Cdd:cd01154 132 KQYLPGLLSDRYktglLGGTWMTEKQGGSDLGANETTAERSG-GGVYRLNGHK-WFASAPLADAALVLARPEGAPAGARG 209

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557235  275 vkekITAFVVER-----GFGGITHGPPEKKMGIKASNTAEVFFDGvrvpSEN-VLGEVGSGFKVAMHILNNGRFGMAAAL 348
Cdd:cd01154 210 ----LSLFLVPRlledgTRNGYRIRRLKDKLGTRSVATGEVEFDD----AEAyLIGDEGKGIYYILEMLNISRLDNAVAA 281

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557235  349 AGTMRGIIAKAVDHATNRTQFGEKIHNFGLIQEKLARMVMLQYVTESMAYMVSANMDQGATDFQIEA-------AISKIF 421
Cdd:cd01154 282 LGIMRRALSEAYHYARHRRAFGKPLIDHPLMRRDLAEMEVDVEAATALTFRAARAFDRAAADKPVEAhmarlatPVAKLI 361

                       250       260       270       280
                ....*....|....*....|....*....|....*....|....*....
gi 4557235  422 GSEAAWKVTDECIQIMGGMGFMKEPGVERVLRDLRIFRIFEGTNDILRL 470
Cdd:cd01154 362 ACKRAAPVTSEAMEVFGGNGYLEEWPVARLHREAQVTPIWEGTGNIQAL 410
PTZ00456 PTZ00456
acyl-CoA dehydrogenase; Provisional
 130-467 2.28e-28

acyl-CoA dehydrogenase; Provisional


Pssm-ID: 185635 [Multi-domain]  Cd Length: 622  Bit Score: 120.36  E-value: 2.28e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557235   130 ETTWQGLKELGAFGLQVPSELGGVGLCNTQYARLVEIVGMHDLGVGITLGahQSIG-FKGILLFGTKAQKEKYLPKLASG 208
Cdd:PTZ00456 102 KEAYQALKAGGWTGISEPEEYGGQALPLSVGFITRELMATANWGFSMYPG--LSIGaANTLMAWGSEEQKEQYLTKLVSG 179

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557235   209 ETVAAFCLTEPSSGSDAASIRTSAVPSPCGKyYTLNGSKLWISNG--GLAD--IFTVFAKTPVTDPATgavkEKITAFVV 284
Cdd:PTZ00456 180 EWSGTMCLTEPQCGTDLGQVKTKAEPSADGS-YKITGTKIFISAGdhDLTEniVHIVLARLPNSLPTT----KGLSLFLV 254

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557235   285 ERGF----------GGITHGPPEKKMGIKASNTAEVFFDGvrvPSENVLGEVGSGFKVAMHILNNGRfgMAAALAGTMRG 354
Cdd:PTZ00456 255 PRHVvkpdgsletaKNVKCIGLEKKMGIKGSSTCQLSFEN---SVGYLIGEPNAGMKQMFTFMNTAR--VGTALEGVCHA 329

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557235   355 IIA--KAVDHATNR--------TQFGEKIHNFGLIQEKLARMVML-QYVTE---SMAYMVSANMD--QGATDFQIEAA-- 416
Cdd:PTZ00456 330 ELAfqNALRYARERrsmralsgTKEPEKPADRIICHANVRQNILFaKAVAEggrALLLDVGRLLDihAAAKDAATREAld 409

                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 4557235   417 --------ISKIFGSEAAWKVTDECIQIMGGMGFMKEPGVERVLRDLRIFRIFEGTNDI 467
Cdd:PTZ00456 410 heigfytpIAKGCLTEWGVEAASRCLQVWGGHGYIKGNGMEQILRDARIGTLYEGTTGI 468
Acyl-CoA_dh_M pfam02770
Acyl-CoA dehydrogenase, middle domain; Central domain of Acyl-CoA dehydrogenase has a ...
 213-313 6.86e-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: 6.86e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557235    213 AFCLTEPSSGSDAASIRTSAVPSPcGKYYTLNGSKLWISNGGLADIFTVFAKTPVTDPATGavkekITAFVVERGFGGIT 292
Cdd:pfam02770   1 AFALTEPGAGSDVASLKTTAADGD-GGGWVLNGTKWWITNAGIADLFLVLARTGGDDRHGG-----ISLFLVPKDAPGVS 74

                          90       100
                  ....*....|....*....|.
gi 4557235    293 HGPPEKKMGIKASNTAEVFFD 313
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 ...
 95-209 2.01e-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: 98.30  E-value: 2.01e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557235     95 NEEQTQFLKElvepVSRFFEEVNDP--AKNDALEMVEETTWQGLKELGAFGLQVPSELGGVGLCNTQYARLVEIVGMHDL 172
Cdd:pfam02771   1 TEEQEALRDT----VREFAEEEIAPhaAEWDEEGEFPRELWKKLGELGLLGITIPEEYGGAGLDYLAYALVAEELARADA 76

                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 4557235    173 GVGITLGAHQSIGFKGILLFGTKAQKEKYLPKLASGE 209
Cdd:pfam02771  77 SVALALSVHSSLGAPPILRFGTEEQKERYLPKLASGE 113
PTZ00457 PTZ00457
acyl-CoA dehydrogenase; Provisional
 72-615 1.49e-22

acyl-CoA dehydrogenase; Provisional


Pssm-ID: 185636 [Multi-domain]  Cd Length: 520  Bit Score: 101.88  E-value: 1.49e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557235    72 SFAVGMFKGQLTTDQVFPYPS-VLNEEQTQFLKELVEPVSrffeevndpaKNDalemveettwqglKELG-AFGLQVPSE 149
Cdd:PTZ00457  17 SYAAGLFNFKIVPEEMFPYPCrKLDGDEAENLQSLLEQIR----------SND-------------KILGnLYGARIATE 73

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557235   150 LGGVGLCNTQYARLVEIVGMHdlGVGITLGAHQSIGFKGILL--FGTKAQKEKYLPKLASGETVAAFClTEPSSGSDAAS 227
Cdd:PTZ00457  74 YGGLGLGHTAHALIYEEVGTN--CDSKLLSTIQHSGFCTYLLstVGSKELKGKYLTAMSDGTIMMGWA-TEEGCGSDISM 150

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557235   228 IRTSAVPSPCGKYyTLNGSKLWIsNGGLADIFTVFAKTpVTDPATGA---VKEKITAFVVERgfggithgppeKKMGIKA 304
Cdd:PTZ00457 151 NTTKASLTDDGSY-VLTGQKRCE-FAASATHFLVLAKT-LTQTAAEEgatEVSRNSFFICAK-----------DAKGVSV 216

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557235   305 SNTAEVFFDgvrVPSENVLGEVGSGFKVAMHILNNGRFGMAAALAGTMRGIIAKAVDhaTNRTQFgekihnfglIQEKLA 384
Cdd:PTZ00457 217 NGDSVVFEN---TPAADVVGVVGEGFKDAMITLFTEQYLYAASLLGIMKRVVQELRG--SNAEEG---------ATDTVA 282

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557235   385 RMVMLQYVTESMAYMVSANMDQGATDFQIEAAISKIFGSEAawkvTDECIQIMGGMGFMKEPgVERVLRDLRIFRIFEGT 464
Cdd:PTZ00457 283 SFACAMYAMESTLYALTANLDLPTEDSLLECTLVSAFVQST----TNQLLSILETATPPSTT-LEKCFANARLFLSMMES 357

                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557235   465 NDIlrLFVALQGCmdkGKELSGLgsalknPFGNAGLLLGEAGKQLRrraglgsGLSLSGLVHPELSRSGELAVRALEQFA 544
Cdd:PTZ00457 358 RDF--LYSSAVCC---GVEDYGL------FFQRASTLQMMQARTLR-------SLGVRDRVPIKNLPDCSLIDEAVVAFG 419

                        490       500       510       520       530       540       550
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 4557235   545 TVVEAKLIKHKKGIVNEQFLLQRLADGAIDLYAMVVVLSRASRSLSEGHPTAQHEKMLCDTWCIEAAARIR 615
Cdd:PTZ00457 420 NAVEATFVRSGSQVPYQQLLLNRLGEAASLLYAASAVASRASMCVSKGLPSAKVEGELASAFIAMAVSRAR 490
fadE PRK09463
acyl-CoA dehydrogenase; Reviewed
 88-446 1.20e-20

acyl-CoA dehydrogenase; Reviewed


Pssm-ID: 236528 [Multi-domain]  Cd Length: 777  Bit Score: 96.81  E-value: 1.20e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557235    88 FPYPSVLNEEQTqFLKELVEPVSRFfeeVNDPAKNDALEMVEETTWQGLKELGAFGLQVPSELGGVGLCNTQYARLVEIV 167
Cdd:PRK09463  74 YPKPTLTAEEQA-FLDGPVEELCRM---VNDWQITHELADLPPEVWQFIKEHGFFGMIIPKEYGGLEFSAYAHSRVLQKL 149

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557235   168 GMHDLGVGITLGAHQSIGfKGILL--FGTKAQKEKYLPKLASGETVAAFCLTEPSSGSDAASIRTSAVpsPC-----GK- 239
Cdd:PRK09463 150 ASRSGTLAVTVMVPNSLG-PGELLlhYGTDEQKDHYLPRLARGEEIPCFALTSPEAGSDAGSIPDTGV--VCkgewqGEe 226

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557235   240 --YYTLNGSKLWISnggLADIFTVFA---KtpVTDPaTGAVKEK----ITAFVVERGFGGITHGPPEKKMGIkasntaeV 310
Cdd:PRK09463 227 vlGMRLTWNKRYIT---LAPIATVLGlafK--LYDP-DGLLGDKedlgITCALIPTDTPGVEIGRRHFPLNV-------P 293

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557235   311 FFDG------VRVPSENVLGE---VGSGFKVAMHILNNGRFGMAAALAGTMRGIIAKAV-DHATNRTQFGEKIHNFGLIQ 380
Cdd:PRK09463 294 FQNGptrgkdVFIPLDYIIGGpkmAGQGWRMLMECLSVGRGISLPSNSTGGAKLAALATgAYARIRRQFKLPIGKFEGIE 373

                        330       340       350       360       370       380
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 4557235   381 EKLARMVMLQYVTESMAYMVSANMDQGATDFQIeAAISKIFGSEAAWKVTDECIQIMGGMGFMKEP 446
Cdd:PRK09463 374 EPLARIAGNAYLMDAARTLTTAAVDLGEKPSVL-SAIAKYHLTERGRQVINDAMDIHGGKGICLGP 438
PRK13026 PRK13026
acyl-CoA dehydrogenase; Reviewed
 133-441 2.96e-20

acyl-CoA dehydrogenase; Reviewed


Pssm-ID: 237277 [Multi-domain]  Cd Length: 774  Bit Score: 95.41  E-value: 2.96e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557235   133 WQGLKELGAFGLQVPSELGGVGLcnTQYA--RLVEIVGMHDLGVGITLGAHQSIGfKGILL--FGTKAQKEKYLPKLASG 208
Cdd:PRK13026 114 WDYLKKEGFFALIIPKEYGGKGF--SAYAnsTIVSKIATRSVSAAVTVMVPNSLG-PGELLthYGTQEQKDYWLPRLADG 190

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557235   209 ETVAAFCLTEPSSGSDAASIRTSAVpsPC-GKY-------YTLNGSKLWISnggLADIFTVF-----AKTPvtDPATGAV 275
Cdd:PRK13026 191 TEIPCFALTGPEAGSDAGAIPDTGI--VCrGEFegeevlgLRLTWDKRYIT---LAPVATVLglafkLRDP--DGLLGDK 263

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557235   276 KE-KITAFVVERGFGGITHGPPEKKMGIkasntaeVFFDG------VRVPSENVLG---EVGSGFKVAMHILNNGRFGMA 345
Cdd:PRK13026 264 KElGITCALIPTDHPGVEIGRRHNPLGM-------AFMNGttrgkdVFIPLDWIIGgpdYAGRGWRMLVECLSAGRGISL 336

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557235   346 AALAGTMRGIIAKAVD-HATNRTQFGEKIHNFGLIQEKLARMVMLQYVTESMAYMVSANMDQGATDfQIEAAISKIFGSE 424
Cdd:PRK13026 337 PALGTASGHMATRTTGaYAYVRRQFGMPIGQFEGVQEALARIAGNTYLLEAARRLTTTGLDLGVKP-SVVTAIAKYHMTE 415

                        330
                 ....*....|....*..
gi 4557235   425 AAWKVTDECIQIMGGMG 441
Cdd:PRK13026 416 LARDVVNDAMDIHAGKG 432
AXO cd01150
Peroxisomal acyl-CoA oxidase; Peroxisomal acyl-CoA oxidases (AXO) catalyze the first set in ...
 163-513 1.56e-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: 1.56e-18
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557235  163 LVEIVGMHDLGVGITLGAHQSIGFKGILLFGTKAQKEKYLPKLASGETVAAFCLTEPSSGSDAASIRTSAVPSPCGKYYT 242
Cdd:cd01150  87 LTNSLGGYDLSLGAKLGLHLGLFGNAIKNLGTDEHQDYWLQGANNLEIIGCFAQTELGHGSNLQGLETTATYDPLTQEFV 166

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557235  243 LN-----GSKLWIsnGGLADIFT---VFAKTpvtdpATGAVKEKITAFVVE-------RGFGGITHGPPEKKMGIKASNT 307
Cdd:cd01150 167 INtpdftATKWWP--GNLGKTAThavVFAQL-----ITPGKNHGLHAFIVPirdpkthQPLPGVTVGDIGPKMGLNGVDN 239

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557235  308 AEVFFDGVRVPSENVL---GEV-------------GSGFKVAMHILNNGRFGMAAALAGTMRGIIAKAVDHATNRTQFGE 371
Cdd:cd01150 240 GFLQFRNVRIPRENLLnrfGDVspdgtyvspfkdpNKRYGAMLGTRSGGRVGLIYDAAMSLKKAATIAIRYSAVRRQFGP 319

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557235  372 K-------IHNFGLIQEK----LARMVMLQYVTESMAYM---VSANMDQGATDFQIE----AAISKIFGSEAAWKVTDEC 433
Cdd:cd01150 320 KpsdpevqILDYQLQQYRlfpqLAAAYAFHFAAKSLVEMyheIIKELLQGNSELLAElhalSAGLKAVATWTAAQGIQEC 399

                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557235  434 IQIMGGMGFMKEPGVERVLRDLRIFRIFEGTNDILRLFVAlQGCMDKGKELSGLGSALKNPFGNAGLLLGEAGKQLRRRA 513
Cdd:cd01150 400 REACGGHGYLAMNRLPTLRDDNDPFCTYEGDNTVLLQQTA-NYLLKKYAQAFSLADYLEAYEWLAAHLLRHAAAQLEKLK 478
PLN02636 PLN02636
acyl-coenzyme A oxidase
 159-473 2.43e-18

acyl-coenzyme A oxidase


Pssm-ID: 215342 [Multi-domain]  Cd Length: 686  Bit Score: 89.15  E-value: 2.43e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557235   159 QYARLVEIVGMHDLGVGITLGAHQSIGFKGILLFGTKAQKEKYLPKLASGETVAAFCLTEPSSGSDAASIRTSAVPSPCG 238
Cdd:PLN02636 122 KYFAITEAVGSVDMSLGIKLGVQYSLWGGSVINLGTKKHRDKYFDGIDNLDYPGCFAMTELHHGSNVQGLQTTATFDPLT 201

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557235   239 KYYTLN-----GSKLWISNGGLADIF-TVFAKTPVTDPATGAVKEK-ITAFVV-------ERGFGGITHGPPEKKMGIKA 304
Cdd:PLN02636 202 DEFVINtpndgAIKWWIGNAAVHGKFaTVFARLKLPTHDSKGVSDMgVHAFIVpirdmktHQVLPGVEIRDCGHKVGLNG 281

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557235   305 SNTAEVFFDGVRVPSENVLGEVG----------------SGFKVAMHILNNGRFGMAAALAGTMRGIIAKAVDHATNRTQ 368
Cdd:PLN02636 282 VDNGALRFRSVRIPRDNLLNRFGdvsrdgkytsslptinKRFAATLGELVGGRVGLAYGSVGVLKASNTIAIRYSLLRQQ 361

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557235   369 FGE------KIHNFGLIQEKLarMVML----------QYVTESMAYMVSANMDQGATDFQIEAAISKIFGSEAAWKVTDE 432
Cdd:PLN02636 362 FGPpkqpeiSILDYQSQQHKL--MPMLastyafhfatEYLVERYSEMKKTHDDQLVADVHALSAGLKAYITSYTAKALST 439

                        330       340       350       360
                 ....*....|....*....|....*....|....*....|....
gi 4557235   433 CIQIMGGMGFmkePGVER--VLR-DLRIFRIFEGTNDILRLFVA 473
Cdd:PLN02636 440 CREACGGHGY---AAVNRfgSLRnDHDIFQTFEGDNTVLLQQVA 480
PLN02876 PLN02876
acyl-CoA dehydrogenase
 148-467 5.51e-18

acyl-CoA dehydrogenase


Pssm-ID: 215473 [Multi-domain]  Cd Length: 822  Bit Score: 88.31  E-value: 5.51e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557235   148 SELGGVGLCNTQYARLVEIVGMHDLGVGI-TLGAHQSIGFKGILLFGTKAQKEKYLPKLASGETVAAFCLTEPS-SGSDA 225
Cdd:PLN02876 487 DQLLGAGLSNLEYGYLCEIMGRSVWAPQVfNCGAPDTGNMEVLLRYGNKEQQLEWLIPLLEGKIRSGFAMTEPQvASSDA 566

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557235   226 ASIRTSAVPSpcGKYYTLNGSKLWISngGLAD----IFTVFAKTPVTDPA------------TGAVKEKITAFVVerGFG 289
Cdd:PLN02876 567 TNIECSIRRQ--GDSYVINGTKWWTS--GAMDprcrVLIVMGKTDFNAPKhkqqsmilvdiqTPGVQIKRPLLVF--GFD 640

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557235   290 GITHGppekkmgikasnTAEVFFDGVRVPSENVLGEVGSGFKVAMHILNNGRFGMAAALAGTMRGIIAKAVDHATNRTQF 369
Cdd:PLN02876 641 DAPHG------------HAEISFENVRVPAKNILLGEGRGFEIAQGRLGPGRLHHCMRLIGAAERGMQLMVQRALSRKAF 708

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557235   370 GEKIHNFGLIQEKLARmvmLQYVTESMAYMVSANMDQ----GATDFQIEAAISKIFGSEAAWKVTDECIQIMGGMGFMKE 445
Cdd:PLN02876 709 GKLIAQHGSFLSDLAK---CRVELEQTRLLVLEAADQldrlGNKKARGIIAMAKVAAPNMALKVLDMAMQVHGAAGVSSD 785

                        330       340
                 ....*....|....*....|..
gi 4557235   446 PGVERVLRDLRIFRIFEGTNDI 467
Cdd:PLN02876 786 TVLAHLWATARTLRIADGPDEV 807
DszC cd01163
Dibenzothiophene (DBT) desulfurization enzyme C; DszC is a flavin reductase dependent enzyme, ...
 128-367 1.09e-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: 1.09e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557235  128 VEETTWqgLKELGAFGLQVPSELGGVGLCNTQYARLVEIVGMHDLGVGITLGAHqsIGF-KGILLFGTKAQKEKYLPKLA 206
Cdd:cd01163  25 YEEVAL--LRQSGLGTLRVPKEYGGLGASLPDLYEVVRELAAADSNIAQALRAH--FGFvEALLLAGPEQFRKRWFGRVL 100

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557235  207 SGETVAAfclTEPSSGSDAASIRTSAVPSPCGKYYtLNGSKlWISNGGL-ADIFTVFAktpvTDPAtgavkEKITAFVVE 285
Cdd:cd01163 101 NGWIFGN---AVSERGSVRPGTFLTATVRDGGGYV-LNGKK-FYSTGALfSDWVTVSA----LDEE-----GKLVFAAVP 166

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557235  286 RGFGGITHGPPEKKMGIK--ASNTAEvfFDGVRVPSENVLGEvGSGFKVAMHILNNGRFGMAAALAGTMRGIIAKAVDHA 363
Cdd:cd01163 167 TDRPGITVVDDWDGFGQRltASGTVT--FDNVRVEPDEVLPR-PNAPDRGTLLTAIYQLVLAAVLAGIARAALDDAVAYV 243


                ....
gi 4557235  364 TNRT 367
Cdd:cd01163 244 RSRT 247
PRK11561 PRK11561
isovaleryl CoA dehydrogenase; Provisional
 216-479 5.03e-08

isovaleryl CoA dehydrogenase; Provisional


Pssm-ID: 183199 [Multi-domain]  Cd Length: 538  Bit Score: 55.91  E-value: 5.03e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557235   216 LTEPSSGSDAASIRTSAVPSPcGKYYTLNGSKlWISNGGLADIFTVFAKTpvtdpatgavKEKITAFVVERGFGGITHGP 295
Cdd:PRK11561 184 MTEKQGGSDVLSNTTRAERLA-DGSYRLVGHK-WFFSVPQSDAHLVLAQA----------KGGLSCFFVPRFLPDGQRNA 251

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557235   296 P-----EKKMGIKASNTAEVFFDGVrvpSENVLGEVGSGFKvamHILNNG---RFGMAAALAGTMRGIIAKAVDHATNRT 367
Cdd:PRK11561 252 IrlerlKDKLGNRSNASSEVEFQDA---IGWLLGEEGEGIR---LILKMGgmtRFDCALGSHGLMRRAFSVAIYHAHQRQ 325

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557235   368 QFGEKIHNFGLIQEKLARMVMLQYVTESMAYMVSANMDQGATdfQIEAAISKIFGSEAAWKVTD-------ECIQIMGGM 440
Cdd:PRK11561 326 VFGKPLIEQPLMRQVLSRMALQLEGQTALLFRLARAWDRRAD--AKEALWARLFTPAAKFVICKrgipfvaEAMEVLGGI 403

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....
gi 4557235   441 GFMKEPGVERVLRDLRIFRIFEGTN-----DILRLFVALQGCMD 479
Cdd:PRK11561 404 GYCEESELPRLYREMPVNSIWEGSGnimclDVLRVLNKQPGVYD 447
PLN02312 PLN02312
acyl-CoA oxidase
 161-326 2.09e-07

acyl-CoA oxidase


Pssm-ID: 215178 [Multi-domain]  Cd Length: 680  Bit Score: 54.01  E-value: 2.09e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557235   161 ARLVEIVGMHDLGVGITLGAHQSIGFKGILLFGTKAQKEKYLPKLASGETVAAFCLTEPSSGSDAASIRTSAVPSPCGKY 240
Cdd:PLN02312 136 LALLEVIGIYDHSLAIKLGVHFFLWGGAIKFLGTKRHHDKWLKDTEDYVVKGCFAMTELGHGSNVRGIETVTTYDPKTEE 215

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557235   241 YTLN-----GSKLWIsnGGLADIFT---VFAKTPVTdpatgAVKEKITAFVVE------RGFGGITHGPPEKKMGIKASN 306
Cdd:PLN02312 216 FVINtpcesAQKYWI--GGAANHAThtiVFSQLHIN-----GKNEGVHAFIAQirdqdgNICPNIRIADCGHKIGLNGVD 288

                        170       180
                 ....*....|....*....|
gi 4557235   307 TAEVFFDGVRVPSENVLGEV 326
Cdd:PLN02312 289 NGRIWFDNLRIPRENLLNSV 308
Acyl-CoA_dh_2 pfam08028
Acyl-CoA dehydrogenase, C-terminal domain;
343-465 4.26e-07

Acyl-CoA dehydrogenase, C-terminal domain;


Pssm-ID: 429790 [Multi-domain]  Cd Length: 133  Bit Score: 49.27  E-value: 4.26e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557235    343 GMAAALAGTMRGIIAKAVDHATNRTQ--FGEKIHNFGLIQEKLARMV-------MLQYVTESMAYMVSANMDQGATDFQI 413
Cdd:pfam08028   1 GIAAAALGAARAALAEFTERARGRVRayFGVPLAEDPATQLALAEAAaridaarLLLERAAARIEAAAAAGKPVTPALRA 80

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|..
gi 4557235    414 EAAISKIFGSEAAWKVTDECIQIMGGMGFMKEPGVERVLRDLRIFRIFEGTN 465
Cdd:pfam08028  81 EARRAAAFATELAVAAVDALFRAAGGSALFQDSPLQRIWRDIHAAAQHAAVN 132
PTZ00460 PTZ00460
acyl-CoA dehydrogenase; Provisional
 193-473 6.22e-06

acyl-CoA dehydrogenase; Provisional


Pssm-ID: 185639 [Multi-domain]  Cd Length: 646  Bit Score: 49.46  E-value: 6.22e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557235   193 GTKAQKEKYLPKLASGETVAAFCLTEPSSGSDAASIRTSAVPSPCGKYYTLN-----GSKLWISN-GGLADIFTVFAKTP 266
Cdd:PTZ00460 110 GTDEQINLWMPSLLNFEIVGCYAQTELGHGSDVQNLETTATYDKQTNEFVIHtpsveAVKFWPGElGFLCNFALVYAKLI 189

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557235   267 VTDPATG--AVKEKITAFVVERGFGGITHGPPEKKMGIKASNTAEVFFDGVRVPSENVLG---EVGSGFKVAMHilNNGR 341
Cdd:PTZ00460 190 VNGKNKGvhPFMVRIRDKETHKPLQGVEVGDIGPKMGYAVKDNGFLSFDHYRIPLDSLLAryiKVSEDGQVERQ--GNPK 267

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557235   342 FGMAAALagTMRGIIAK------------AVDHATNRTQFGE------KIHNFGLIQEK----LARMVMLQYVTESMAYM 399
Cdd:PTZ00460 268 VSYASMM--YMRNLIIDqyprfaaqaltvAIRYSIYRQQFTNdnkqenSVLEYQTQQQKllplLAEFYACIFGGLKIKEL 345

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557235   400 VSANMDQ-GATDFQIEAAISKIFGSEAAW------KVTDECIQIMGGMGFMKEPGVERVLRDLRIFRIFEGTNDILRLFV 472
Cdd:PTZ00460 346 VDDNFNRvQKNDFSLLQLTHAILSAAKANytyfvsNCAEWCRLSCGGHGYAHYSGLPAIYFDMSPNITLEGENQIMYLQL 425


                 .
gi 4557235   473 A 473
Cdd:PTZ00460 426 A 426
PLN02443 PLN02443
acyl-coenzyme A oxidase
 193-501 2.25e-05

acyl-coenzyme A oxidase


Pssm-ID: 178062 [Multi-domain]  Cd Length: 664  Bit Score: 47.52  E-value: 2.25e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557235   193 GTKAQKEKYLPKLASGETVAAFCLTEPSSGSDAASIRTSAVPSPCGKYY-----TLNGSKLWisNGGLADIFT---VFAK 264
Cdd:PLN02443 114 GTEEQQKKWLPLAYKMQIIGCYAQTELGHGSNVQGLETTATFDPKTDEFvihspTLTSSKWW--PGGLGKVSThavVYAR 191

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557235   265 TpvtdpATGAVKEKITAFVVE-------RGFGGITHGPPEKKMGIKASNTAE---VFFDGVRVPSENVLGEVGSGFKVAM 334
Cdd:PLN02443 192 L-----ITNGKDHGIHGFIVQlrslddhSPLPGVTVGDIGMKFGNGAYNTMDngfLRFDHVRIPRDQMLMRLSKVTREGK 266

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557235   335 HILNNgrfgMAAALA-GTM----RGIIAK-----------AVDHATNRTQFGEK-------IHNFGLIQEK----LARMV 387
Cdd:PLN02443 267 YVQSD----VPRQLVyGTMvyvrQTIVADastalsravciATRYSAVRRQFGSQdggpetqVIDYKTQQSRlfplLASAY 342

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557235   388 MLQYVTESMAYMVSANMDQ-GATDF----QIEAAIS--KIFGSEAAWKVTDECIQIMGGMGFMKEPGVERVLRDLRIFRI 460
Cdd:PLN02443 343 AFRFVGEWLKWLYTDVTQRlEANDFstlpEAHACTAglKSLTTSATADGIEECRKLCGGHGYLCSSGLPELFAVYVPACT 422

                        330       340       350       360
                 ....*....|....*....|....*....|....*....|.
gi 4557235   461 FEGTNDILRLFVAlQGCMdkgKELSGLGSAlKNPFGNAGLL 501
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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