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Conserved domains on  [gi|394025725|ref|NP_001257377|]
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very long-chain specific acyl-CoA dehydrogenase, mitochondrial isoform 4 [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 ...
 1-405 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: 739.28  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 394025725   1 MFKGQLTTDQVFPYPSVLNEEQTQFLKELVEPVSRFFEEVNDPAKNDALEMVEETTWQGLKELGAFGLQVPSELGGVGLC 80
Cdd:cd01161    6 MFLGDIVTKQVFPYPSVLTEEQTEELNMLVGPVEKFFEEVNDPAKNDQLEKIPRKTLTQLKELGLFGLQVPEEYGGLGLN 85

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 394025725  81 NTQYARLVEIVGMhDLGVGITLGAHQSIGFKGILLFGTKAQKEKYLPKLASGETVAAFCLTEPSSGSDAASIRTSAVPSP 160
Cdd:cd01161   86 NTQYARLAEIVGM-DLGFSVTLGAHQSIGFKGILLFGTEAQKEKYLPKLASGEWIAAFALTEPSSGSDAASIRTTAVLSE 164

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 394025725 161 CGKYYTLNGSKLWISNGGLADIFTVFAKTPVTDPaTGAVKEKITAFVVERGFGGITHGPPEKKMGIKASNTAEVFFDGVR 240
Cdd:cd01161  165 DGKHYVLNGSKIWITNGGIADIFTVFAKTEVKDA-TGSVKDKITAFIVERSFGGVTNGPPEKKMGIKGSNTAEVYFEDVK 243

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 394025725 241 VPSENVLGEVGSGFKVAMHILNNGRFGMAAALAGTMRGIIAKAVDHATNRTQFGEKIHNFGLIQEKLARMVMLQYVTESM 320
Cdd:cd01161  244 IPVENVLGEVGDGFKVAMNILNNGRFGMGAALIGTMKRCIEKAVDYANNRKQFGKKIHEFGLIQEKLANMAILQYATESM 323

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 394025725 321 AYMVSANMDQGAT-DFQIEAAISKIFGSEAAWKVTDECIQIMGGMGFMKEPGVERVLRDLRIFRIFEGTNDILRLFVALQ 399
Cdd:cd01161  324 AYMTSGNMDRGLKaEYQIEAAISKVFASEAAWLVVDEAIQIHGGMGFMREYGVERVLRDLRIFRIFEGTNEILRLFIALT 403


                 ....*.
gi 394025725 400 GCMDKG 405
Cdd:cd01161  404 GLQHAG 409
 
Name Accession Description Interval E-value
VLCAD cd01161
Very long chain acyl-CoA dehydrogenase; VLCAD is an acyl-CoA dehydrogenase (ACAD), which is ...
 1-405 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: 739.28  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 394025725   1 MFKGQLTTDQVFPYPSVLNEEQTQFLKELVEPVSRFFEEVNDPAKNDALEMVEETTWQGLKELGAFGLQVPSELGGVGLC 80
Cdd:cd01161    6 MFLGDIVTKQVFPYPSVLTEEQTEELNMLVGPVEKFFEEVNDPAKNDQLEKIPRKTLTQLKELGLFGLQVPEEYGGLGLN 85

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 394025725  81 NTQYARLVEIVGMhDLGVGITLGAHQSIGFKGILLFGTKAQKEKYLPKLASGETVAAFCLTEPSSGSDAASIRTSAVPSP 160
Cdd:cd01161   86 NTQYARLAEIVGM-DLGFSVTLGAHQSIGFKGILLFGTEAQKEKYLPKLASGEWIAAFALTEPSSGSDAASIRTTAVLSE 164

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 394025725 161 CGKYYTLNGSKLWISNGGLADIFTVFAKTPVTDPaTGAVKEKITAFVVERGFGGITHGPPEKKMGIKASNTAEVFFDGVR 240
Cdd:cd01161  165 DGKHYVLNGSKIWITNGGIADIFTVFAKTEVKDA-TGSVKDKITAFIVERSFGGVTNGPPEKKMGIKGSNTAEVYFEDVK 243

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 394025725 241 VPSENVLGEVGSGFKVAMHILNNGRFGMAAALAGTMRGIIAKAVDHATNRTQFGEKIHNFGLIQEKLARMVMLQYVTESM 320
Cdd:cd01161  244 IPVENVLGEVGDGFKVAMNILNNGRFGMGAALIGTMKRCIEKAVDYANNRKQFGKKIHEFGLIQEKLANMAILQYATESM 323

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 394025725 321 AYMVSANMDQGAT-DFQIEAAISKIFGSEAAWKVTDECIQIMGGMGFMKEPGVERVLRDLRIFRIFEGTNDILRLFVALQ 399
Cdd:cd01161  324 AYMTSGNMDRGLKaEYQIEAAISKVFASEAAWLVVDEAIQIHGGMGFMREYGVERVLRDLRIFRIFEGTNEILRLFIALT 403


                 ....*.
gi 394025725 400 GCMDKG 405
Cdd:cd01161  404 GLQHAG 409
CaiA COG1960
Acyl-CoA dehydrogenase related to the alkylation response protein AidB [Lipid transport and ...
 18-397 3.34e-138

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: 406.15  E-value: 3.34e-138
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 394025725  18 LNEEQTQFLKElvepVSRFFEEVNDP--AKNDALEMVEETTWQGLKELGAFGLQVPSELGGVGLCNTQYARLVEIVGMHD 95
Cdd:COG1960    5 LTEEQRALRDE----VREFAEEEIAPeaREWDREGEFPRELWRKLAELGLLGLTIPEEYGGLGLSLVELALVLEELARAD 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 394025725  96 LGVGITLGAHQSIGfKGILLFGTKAQKEKYLPKLASGETVAAFCLTEPSSGSDAASIRTSAVPSpcGKYYTLNGSKLWIS 175
Cdd:COG1960   81 ASLALPVGVHNGAA-EALLRFGTEEQKERYLPRLASGEWIGAFALTEPGAGSDAAALRTTAVRD--GDGYVLNGQKTFIT 157

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 394025725 176 NGGLADIFTVFAKTpvtDPATGAvkEKITAFVVERGFGGITHGPPEKKMGIKASNTAEVFFDGVRVPSENVLGEVGSGFK 255
Cdd:COG1960  158 NAPVADVILVLART---DPAAGH--RGISLFLVPKDTPGVTVGRIEDKMGLRGSDTGELFFDDVRVPAENLLGEEGKGFK 232

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 394025725 256 VAMHILNNGRFGMAAALAGTMRGIIAKAVDHATNRTQFGEKIHNFGLIQEKLARMVMLQYVTESMAYMVSANMDQGAtDF 335
Cdd:COG1960  233 IAMSTLNAGRLGLAAQALGIAEAALELAVAYAREREQFGRPIADFQAVQHRLADMAAELEAARALVYRAAWLLDAGE-DA 311

                        330       340       350       360       370       380
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 394025725 336 QIEAAISKIFGSEAAWKVTDECIQIMGGMGFMKEPGVERVLRDLRIFRIFEGTNDILRLFVA 397
Cdd:COG1960  312 ALEAAMAKLFATEAALEVADEALQIHGGYGYTREYPLERLYRDARILTIYEGTNEIQRLIIA 373
PLN02519 PLN02519
isovaleryl-CoA dehydrogenase
 20-396 9.21e-67

isovaleryl-CoA dehydrogenase


Pssm-ID: 215284 [Multi-domain]  Cd Length: 404  Bit Score: 222.44  E-value: 9.21e-67
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 394025725  20 EEQTQFLKELVEPVSRFFEEVNDPAKNDALemveettWQGLKELGAFGLQVPSELGGVGLCNTQYARLVEIVGMHDLGVG 99
Cdd:PLN02519  35 ESVQQFAQENIAPHAAAIDATNSFPKDVNL-------WKLMGDFNLHGITAPEEYGGLGLGYLYHCIAMEEISRASGSVG 107

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 394025725 100 ITLGAHQSIGFKGILLFGTKAQKEKYLPKLASGETVAAFCLTEPSSGSDAASIRTSAVPSPCGkyYTLNGSKLWISNGGL 179
Cdd:PLN02519 108 LSYGAHSNLCINQLVRNGTPAQKEKYLPKLISGEHVGALAMSEPNSGSDVVSMKCKAERVDGG--YVLNGNKMWCTNGPV 185

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 394025725 180 ADIFTVFAKTpvtDPATGAvkEKITAFVVERGFGGITHGPPEKKMGIKASNTAEVFFDGVRVPSENVLGEVGSGFKVAMH 259
Cdd:PLN02519 186 AQTLVVYAKT---DVAAGS--KGITAFIIEKGMPGFSTAQKLDKLGMRGSDTCELVFENCFVPEENVLGQEGKGVYVMMS 260

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 394025725 260 ILNNGRFGMAAALAGTMRGIIAKAVDHATNRTQFGEKIHNFGLIQEKLARMVMLQYVTESMAYMVSANMDQGATDFQiEA 339
Cdd:PLN02519 261 GLDLERLVLAAGPLGLMQACLDVVLPYVRQREQFGRPIGEFQFIQGKLADMYTSLQSSRSYVYSVARDCDNGKVDRK-DC 339

                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 394025725 340 AISKIFGSEAAWKVTDECIQIMGGMGFMKEPGVERVLRDLRIFRIFEGTNDILRLFV 396
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 ...
 251-397 5.65e-41

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: 145.09  E-value: 5.65e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 394025725  251 GSGFKVAMHILNNGRFGMAAALAGTMRGIIAKAVDHATNRTQFGEKIHNFGLIQEKLARMVMLQYVTESMAYMVSANMDQ 330
Cdd:pfam00441   1 GRGFRVAMETLNHERLAIAAMALGLARRALDEALAYARRRKAFGRPLIDFQLVRHKLAEMAAEIEAARLLVYRAAEALDA 80

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 394025725  331 GATDfQIEAAISKIFGSEAAWKVTDECIQIMGGMGFMKEPGVERVLRDLRIFRIFEGTNDILRLFVA 397
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 ...
 1-405 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: 739.28  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 394025725   1 MFKGQLTTDQVFPYPSVLNEEQTQFLKELVEPVSRFFEEVNDPAKNDALEMVEETTWQGLKELGAFGLQVPSELGGVGLC 80
Cdd:cd01161    6 MFLGDIVTKQVFPYPSVLTEEQTEELNMLVGPVEKFFEEVNDPAKNDQLEKIPRKTLTQLKELGLFGLQVPEEYGGLGLN 85

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 394025725  81 NTQYARLVEIVGMhDLGVGITLGAHQSIGFKGILLFGTKAQKEKYLPKLASGETVAAFCLTEPSSGSDAASIRTSAVPSP 160
Cdd:cd01161   86 NTQYARLAEIVGM-DLGFSVTLGAHQSIGFKGILLFGTEAQKEKYLPKLASGEWIAAFALTEPSSGSDAASIRTTAVLSE 164

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 394025725 161 CGKYYTLNGSKLWISNGGLADIFTVFAKTPVTDPaTGAVKEKITAFVVERGFGGITHGPPEKKMGIKASNTAEVFFDGVR 240
Cdd:cd01161  165 DGKHYVLNGSKIWITNGGIADIFTVFAKTEVKDA-TGSVKDKITAFIVERSFGGVTNGPPEKKMGIKGSNTAEVYFEDVK 243

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 394025725 241 VPSENVLGEVGSGFKVAMHILNNGRFGMAAALAGTMRGIIAKAVDHATNRTQFGEKIHNFGLIQEKLARMVMLQYVTESM 320
Cdd:cd01161  244 IPVENVLGEVGDGFKVAMNILNNGRFGMGAALIGTMKRCIEKAVDYANNRKQFGKKIHEFGLIQEKLANMAILQYATESM 323

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 394025725 321 AYMVSANMDQGAT-DFQIEAAISKIFGSEAAWKVTDECIQIMGGMGFMKEPGVERVLRDLRIFRIFEGTNDILRLFVALQ 399
Cdd:cd01161  324 AYMTSGNMDRGLKaEYQIEAAISKVFASEAAWLVVDEAIQIHGGMGFMREYGVERVLRDLRIFRIFEGTNEILRLFIALT 403


                 ....*.
gi 394025725 400 GCMDKG 405
Cdd:cd01161  404 GLQHAG 409
CaiA COG1960
Acyl-CoA dehydrogenase related to the alkylation response protein AidB [Lipid transport and ...
 18-397 3.34e-138

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: 406.15  E-value: 3.34e-138
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 394025725  18 LNEEQTQFLKElvepVSRFFEEVNDP--AKNDALEMVEETTWQGLKELGAFGLQVPSELGGVGLCNTQYARLVEIVGMHD 95
Cdd:COG1960    5 LTEEQRALRDE----VREFAEEEIAPeaREWDREGEFPRELWRKLAELGLLGLTIPEEYGGLGLSLVELALVLEELARAD 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 394025725  96 LGVGITLGAHQSIGfKGILLFGTKAQKEKYLPKLASGETVAAFCLTEPSSGSDAASIRTSAVPSpcGKYYTLNGSKLWIS 175
Cdd:COG1960   81 ASLALPVGVHNGAA-EALLRFGTEEQKERYLPRLASGEWIGAFALTEPGAGSDAAALRTTAVRD--GDGYVLNGQKTFIT 157

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 394025725 176 NGGLADIFTVFAKTpvtDPATGAvkEKITAFVVERGFGGITHGPPEKKMGIKASNTAEVFFDGVRVPSENVLGEVGSGFK 255
Cdd:COG1960  158 NAPVADVILVLART---DPAAGH--RGISLFLVPKDTPGVTVGRIEDKMGLRGSDTGELFFDDVRVPAENLLGEEGKGFK 232

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 394025725 256 VAMHILNNGRFGMAAALAGTMRGIIAKAVDHATNRTQFGEKIHNFGLIQEKLARMVMLQYVTESMAYMVSANMDQGAtDF 335
Cdd:COG1960  233 IAMSTLNAGRLGLAAQALGIAEAALELAVAYAREREQFGRPIADFQAVQHRLADMAAELEAARALVYRAAWLLDAGE-DA 311

                        330       340       350       360       370       380
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 394025725 336 QIEAAISKIFGSEAAWKVTDECIQIMGGMGFMKEPGVERVLRDLRIFRIFEGTNDILRLFVA 397
Cdd:COG1960  312 ALEAAMAKLFATEAALEVADEALQIHGGYGYTREYPLERLYRDARILTIYEGTNEIQRLIIA 373
SCAD_SBCAD cd01158
Short chain acyl-CoA dehydrogenases and eukaryotic short/branched chain acyl-CoA ...
 20-397 7.39e-122

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: 364.28  E-value: 7.39e-122
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 394025725  20 EEQTQFLKElvepVSRFFEEVNDP--AKNDALEMVEETTWQGLKELGAFGLQVPSELGGVGLCNTQYARLVEIVGMHDLG 97
Cdd:cd01158    1 EEHQMIRKT----VRDFAEKEIAPlaAEMDEKGEFPREVIKEMAELGLMGIPIPEEYGGAGLDFLAYAIAIEELAKVDAS 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 394025725  98 VGITLGAHQSIGFKGILLFGTKAQKEKYLPKLASGETVAAFCLTEPSSGSDAASIRTSAVPSpcGKYYTLNGSKLWISNG 177
Cdd:cd01158   77 VAVIVSVHNSLGANPIIKFGTEEQKKKYLPPLATGEKIGAFALSEPGAGSDAAALKTTAKKD--GDDYVLNGSKMWITNG 154

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 394025725 178 GLADIFTVFAktpVTDPATGavKEKITAFVVERGFGGITHGPPEKKMGIKASNTAEVFFDGVRVPSENVLGEVGSGFKVA 257
Cdd:cd01158  155 GEADFYIVFA---VTDPSKG--YRGITAFIVERDTPGLSVGKKEDKLGIRGSSTTELIFEDVRVPKENILGEEGEGFKIA 229

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 394025725 258 MHILNNGRFGMAAALAGTMRGIIAKAVDHATNRTQFGEKIHNFGLIQEKLARMVMLQYVTESMAYMVSANMDQGaTDFQI 337
Cdd:cd01158  230 MQTLDGGRIGIAAQALGIAQAALDAAVDYAKERKQFGKPIADFQGIQFKLADMATEIEAARLLTYKAARLKDNG-EPFIK 308

                        330       340       350       360       370       380
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 394025725 338 EAAISKIFGSEAAWKVTDECIQIMGGMGFMKEPGVERVLRDLRIFRIFEGTNDILRLFVA 397
Cdd:cd01158  309 EAAMAKLFASEVAMRVTTDAVQIFGGYGYTKDYPVERYYRDAKITEIYEGTSEIQRLVIA 368
ACAD cd00567
Acyl-CoA dehydrogenase; Both mitochondrial acyl-CoA dehydrogenases (ACAD) and peroxisomal ...
 20-397 7.07e-106

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: 321.54  E-value: 7.07e-106
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 394025725  20 EEQtqflKELVEPVSRFFEEVNDPAKNDAlEMVEETTWQGLKELGafglqvpsELGGVGLcntqyarlveivgmhdlgvg 99
Cdd:cd00567    1 EEQ----RELRDSAREFAAEELEPYARER-RETPEEPWELLAELG--------LLLGAAL-------------------- 47

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 394025725 100 itlgahqsigfkgILLFGTKAQKEKYLPKLASGETVAAFCLTEPSSGSDAASIRTSAVPSpcGKYYTLNGSKLWISNGGL 179
Cdd:cd00567   48 -------------LLAYGTEEQKERYLPPLASGEAIAAFALTEPGAGSDLAGIRTTARKD--GDGYVLNGRKIFISNGGD 112

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 394025725 180 ADIFTVFAKTPVTDPATGAvkekITAFVVERGFGGITHGPPEKKMGIKASNTAEVFFDGVRVPSENVLGEVGSGFKVAMH 259
Cdd:cd00567  113 ADLFIVLARTDEEGPGHRG----ISAFLVPADTPGVTVGRIWDKMGMRGSGTGELVFDDVRVPEDNLLGEEGGGFELAMK 188

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 394025725 260 ILNNGRFGMAAALAGTMRGIIAKAVDHATNRTQFGEKIHNFGLIQEKLARMVMLQYVTESMAYMVSANMDQGATDFQIEA 339
Cdd:cd00567  189 GLNVGRLLLAAVALGAARAALDEAVEYAKQRKQFGKPLAEFQAVQFKLADMAAELEAARLLLYRAAWLLDQGPDEARLEA 268

                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 394025725 340 AISKIFGSEAAWKVTDECIQIMGGMGFMKEPGVERVLRDLRIFRIFEGTNDILRLFVA 397
Cdd:cd00567  269 AMAKLFATEAAREVADLAMQIHGGRGYSREYPVERYLRDARAARIAEGTAEIQRLIIA 326
IVD cd01156
Isovaleryl-CoA dehydrogenase; Isovaleryl-CoA dehydrogenase (IVD) is an is an acyl-CoA ...
 18-397 6.21e-92

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: 287.39  E-value: 6.21e-92
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 394025725  18 LNEEQTQflkeLVEPVSRFFEEVNDP--AKNDALEMVEETTWQGLKELGAFGLQVPSELGGVGLCNTQYARLVEIVGMHD 95
Cdd:cd01156    2 LDDEIEM----LRQSVREFAQKEIAPlaAKIDRDNEFPRDLWRKMGKLGLLGITAPEEYGGSGMGYLAHVIIMEEISRAS 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 394025725  96 LGVGITLGAHQSIGFKGILLFGTKAQKEKYLPKLASGETVAAFCLTEPSSGSDAASIRTSAvpSPCGKYYTLNGSKLWIS 175
Cdd:cd01156   78 GSVALSYGAHSNLCINQIYRNGSAAQKEKYLPKLISGEHIGALAMSEPNAGSDVVSMKLRA--EKKGDRYVLNGSKMWIT 155

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 394025725 176 NGGLADIFTVFAKTpvtDPATGAvkEKITAFVVERGFGGITHGPPEKKMGIKASNTAEVFFDGVRVPSENVLGEVGSGFK 255
Cdd:cd01156  156 NGPDADTLVVYAKT---DPSAGA--HGITAFIVEKGMPGFSRAQKLDKLGMRGSNTCELVFEDCEVPEENILGGENKGVY 230

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 394025725 256 VAMHILNNGRFGMAAALAGTMRGIIAKAVDHATNRTQFGEKIHNFGLIQEKLARMVMLQYVTESMAYMVSANMDQGATDf 335
Cdd:cd01156  231 VLMSGLDYERLVLAGGPIGIMQAALDVAIPYAHQRKQFGQPIGEFQLVQGKLADMYTRLNASRSYLYTVAKACDRGNMD- 309

                        330       340       350       360       370       380
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 394025725 336 QIEAAISKIFGSEAAWKVTDECIQIMGGMGFMKEPGVERVLRDLRIFRIFEGTNDILRLFVA 397
Cdd:cd01156  310 PKDAAGVILYAAEKATQVALDAIQILGGNGYINDYPTGRLLRDAKLYEIGAGTSEIRRMVIG 371
IBD cd01162
Isobutyryl-CoA dehydrogenase; Isobutyryl-CoA dehydrogenase (IBD) catalyzes the alpha, beta- ...
 62-397 2.01e-79

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: 254.68  E-value: 2.01e-79
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 394025725  62 ELGAFGLQVPSELGGVGLCNTQYARLVEIVGMHDLGVGITLGAHQSIGFKgILLFGTKAQKEKYLPKLASGETVAAFCLT 141
Cdd:cd01162   43 ELGFGGIYIRDDVGGSGLSRLDASIIFEALSTGCVSTAAYISIHNMCAWM-IDSFGNDEQRERFLPDLCTMEKLASYCLT 121

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 394025725 142 EPSSGSDAASIRTSAVPSpcGKYYTLNGSKLWISNGGLADIFTVFAKTpvtdpaTGAVKEKITAFVVERGFGGITHGPPE 221
Cdd:cd01162  122 EPGSGSDAAALRTRAVRE--GDHYVLNGSKAFISGAGDSDVYVVMART------GGEGPKGISCFVVEKGTPGLSFGANE 193

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 394025725 222 KKMGIKASNTAEVFFDGVRVPSENVLGEVGSGFKVAMHILNNGRFGMAAALAGTMRGIIAKAVDHATNRTQFGEKIHNFG 301
Cdd:cd01162  194 KKMGWNAQPTRAVIFEDCRVPVENRLGGEGQGFGIAMAGLNGGRLNIASCSLGAAQAALDLARAYLEERKQFGKPLADFQ 273

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 394025725 302 LIQEKLARMVMLQYVTESMAYMVSANMDQGATDFQIEAAISKIFGSEAAWKVTDECIQIMGGMGFMKEPGVERVLRDLRI 381
Cdd:cd01162  274 ALQFKLADMATELVASRLMVRRAASALDRGDPDAVKLCAMAKRFATDECFDVANQALQLHGGYGYLKDYPVEQYVRDLRV 353

                        330
                 ....*....|....*.
gi 394025725 382 FRIFEGTNDILRLFVA 397
Cdd:cd01162  354 HQILEGTNEIMRLIIA 369
LCAD cd01160
Long chain acyl-CoA dehydrogenase; LCAD is an acyl-CoA dehydrogenases (ACAD), which is found ...
 33-399 6.71e-75

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: 242.79  E-value: 6.71e-75
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 394025725  33 VSRFFEEVNDP--AKNDALEMVEETTWQGLKELGAFGLQVPSELGGVGLcNTQYARLVEIVGMHDLGVGITLGAHQSIGF 110
Cdd:cd01160   10 VRRFFAKEVAPfhHEWEKAGEVPREVWRKAGEQGLLGVGFPEEYGGIGG-DLLSAAVLWEELARAGGSGPGLSLHTDIVS 88

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 394025725 111 KGILLFGTKAQKEKYLPKLASGETVAAFCLTEPSSGSDAASIRTSAVPSpcGKYYTLNGSKLWISNGGLADIFTVFAKTp 190
Cdd:cd01160   89 PYITRAGSPEQKERVLPQMVAGKKIGAIAMTEPGAGSDLQGIRTTARKD--GDHYVLNGSKTFITNGMLADVVIVVART- 165

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 394025725 191 vTDPATGAvkEKITAFVVERGFGGITHGPPEKKMGIKASNTAEVFFDGVRVPSENVLGEVGSGFKVAMHILNNGRFGMAA 270
Cdd:cd01160  166 -GGEARGA--GGISLFLVERGTPGFSRGRKLKKMGWKAQDTAELFFDDCRVPAENLLGEENKGFYYLMQNLPQERLLIAA 242

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 394025725 271 ALAGTMRGIIAKAVDHATNRTQFGEKIHNFGLIQEKLARMVMLQYVTESMAYMVSANMDQGATDfQIEAAISKIFGSEAA 350
Cdd:cd01160  243 GALAAAEFMLEETRNYVKQRKAFGKTLAQLQVVRHKIAELATKVAVTRAFLDNCAWRHEQGRLD-VAEASMAKYWATELQ 321

                        330       340       350       360
                 ....*....|....*....|....*....|....*....|....*....
gi 394025725 351 WKVTDECIQIMGGMGFMKEPGVERVLRDLRIFRIFEGTNDILRLFVALQ 399
Cdd:cd01160  322 NRVAYECVQLHGGWGYMREYPIARAYRDARVQPIYGGTTEIMKELISRQ 370
PLN02519 PLN02519
isovaleryl-CoA dehydrogenase
 20-396 9.21e-67

isovaleryl-CoA dehydrogenase


Pssm-ID: 215284 [Multi-domain]  Cd Length: 404  Bit Score: 222.44  E-value: 9.21e-67
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 394025725  20 EEQTQFLKELVEPVSRFFEEVNDPAKNDALemveettWQGLKELGAFGLQVPSELGGVGLCNTQYARLVEIVGMHDLGVG 99
Cdd:PLN02519  35 ESVQQFAQENIAPHAAAIDATNSFPKDVNL-------WKLMGDFNLHGITAPEEYGGLGLGYLYHCIAMEEISRASGSVG 107

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 394025725 100 ITLGAHQSIGFKGILLFGTKAQKEKYLPKLASGETVAAFCLTEPSSGSDAASIRTSAVPSPCGkyYTLNGSKLWISNGGL 179
Cdd:PLN02519 108 LSYGAHSNLCINQLVRNGTPAQKEKYLPKLISGEHVGALAMSEPNSGSDVVSMKCKAERVDGG--YVLNGNKMWCTNGPV 185

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 394025725 180 ADIFTVFAKTpvtDPATGAvkEKITAFVVERGFGGITHGPPEKKMGIKASNTAEVFFDGVRVPSENVLGEVGSGFKVAMH 259
Cdd:PLN02519 186 AQTLVVYAKT---DVAAGS--KGITAFIIEKGMPGFSTAQKLDKLGMRGSDTCELVFENCFVPEENVLGQEGKGVYVMMS 260

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 394025725 260 ILNNGRFGMAAALAGTMRGIIAKAVDHATNRTQFGEKIHNFGLIQEKLARMVMLQYVTESMAYMVSANMDQGATDFQiEA 339
Cdd:PLN02519 261 GLDLERLVLAAGPLGLMQACLDVVLPYVRQREQFGRPIGEFQFIQGKLADMYTSLQSSRSYVYSVARDCDNGKVDRK-DC 339

                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 394025725 340 AISKIFGSEAAWKVTDECIQIMGGMGFMKEPGVERVLRDLRIFRIFEGTNDILRLFV 396
Cdd:PLN02519 340 AGVILCAAERATQVALQAIQCLGGNGYINEYPTGRLLRDAKLYEIGAGTSEIRRMLI 396
GCD cd01151
Glutaryl-CoA dehydrogenase; Glutaryl-CoA dehydrogenase (GCD). GCD is an acyl-CoA dehydrogenase, ...
 2-411 6.94e-65

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: 217.23  E-value: 6.94e-65
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 394025725   2 FKGQLTTDQVfpypsVLNEEQTQFLKELVEP--VSRFFEEVNDPakndalEMVEEttwqgLKELGAFGLQvPSELGGVGL 79
Cdd:cd01151    9 LDDLLTEEER-----AIRDTAREFCQEELAPrvLEAYREEKFDR------KIIEE-----MGELGLLGAT-IKGYGCAGL 71

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 394025725  80 CNTQY---ARLVEIVgmhDLGVGITLGAHQSIGFKGILLFGTKAQKEKYLPKLASGETVAAFCLTEPSSGSDAASIRTSA 156
Cdd:cd01151   72 SSVAYgliAREVERV---DSGYRSFMSVQSSLVMLPIYDFGSEEQKQKYLPKLASGELIGCFGLTEPNHGSDPGGMETRA 148

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 394025725 157 vpSPCGKYYTLNGSKLWISNGGLADIFTVFAKTPVTDpatgavkeKITAFVVERGFGGITHGPPEKKMGIKASNTAEVFF 236
Cdd:cd01151  149 --RKDGGGYKLNGSKTWITNSPIADVFVVWARNDETG--------KIRGFILERGMKGLSAPKIQGKFSLRASITGEIVM 218

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 394025725 237 DGVRVPSENVLGEVgSGFKVAMHILNNGRFGMAAALAGTMRGIIAKAVDHATNRTQFGEKIHNFGLIQEKLARM-VMLQY 315
Cdd:cd01151  219 DNVFVPEENLLPGA-EGLRGPFKCLNNARYGIAWGALGAAEDCYHTARQYVLDRKQFGRPLAAFQLVQKKLADMlTEIAL 297

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 394025725 316 VTEsMAYMVSANMDQG-ATDFQIeaAISKIFGSEAAWKVTDECIQIMGGMGFMKEPGVERVLRDLRIFRIFEGTNDILRL 394
Cdd:cd01151  298 GLL-ACLRVGRLKDQGkATPEQI--SLLKRNNCGKALEIARTAREMLGGNGISDEYHIIRHMVNLESVNTYEGTHDIHAL 374

                        410
                 ....*....|....*..
gi 394025725 395 FValqgcmdkGKELSGL 411
Cdd:cd01151  375 IL--------GRAITGI 383
MCAD cd01157
Medium chain acyl-CoA dehydrogenase; MCADs are mitochondrial beta-oxidation enzymes, which ...
 18-397 8.49e-65

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: 216.68  E-value: 8.49e-65
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 394025725  18 LNEEQtqflKELVEPVSRFFEEVNDPAKNDaLEMVEETTWQGLK---ELGAFGLQVPSELGGVGLCNTQYARLVEIVGMH 94
Cdd:cd01157    1 LTEQQ----KEFQETARKFAREEIIPVAAE-YDKSGEYPWPLIKrawELGLMNTHIPEDCGGLGLGTFDTCLITEELAYG 75

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 394025725  95 DLGVGITLGAHqSIGFKGILLFGTKAQKEKYLPKLASGETVAAFCLTEPSSGSDAASIRTSAVPSpcGKYYTLNGSKLWI 174
Cdd:cd01157   76 CTGVQTAIEAN-SLGQMPVIISGNDEQKKKYLGRMTEEPLMCAYCVTEPGAGSDVAGIKTKAEKK--GDEYIINGQKMWI 152

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 394025725 175 SNGGLADIFTVFAKTPvTDPATGAVKeKITAFVVERGFGGITHGPPEKKMGIKASNTAEVFFDGVRVPSENVLGEVGSGF 254
Cdd:cd01157  153 TNGGKANWYFLLARSD-PDPKCPASK-AFTGFIVEADTPGIQPGRKELNMGQRCSDTRGITFEDVRVPKENVLIGEGAGF 230

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 394025725 255 KVAMHILNNGRFGMAAALAGTMRGIIAKAVDHATNRTQFGEKIHNFGLIQEKLARMVMlQYVTESMAYMVSAN-MDQGAT 333
Cdd:cd01157  231 KIAMGAFDKTRPPVAAGAVGLAQRALDEATKYALERKTFGKLIAEHQAVSFMLADMAM-KVELARLAYQRAAWeVDSGRR 309

                        330       340       350       360       370       380
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 394025725 334 DfQIEAAISKIFGSEAAWKVTDECIQIMGGMGFMKEPGVERVLRDLRIFRIFEGTNDILRLFVA 397
Cdd:cd01157  310 N-TYYASIAKAFAADIANQLATDAVQIFGGNGFNSEYPVEKLMRDAKIYQIYEGTSQIQRLIIS 372
PTZ00461 PTZ00461
isovaleryl-CoA dehydrogenase; Provisional
 27-388 1.01e-63

isovaleryl-CoA dehydrogenase; Provisional


Pssm-ID: 185640 [Multi-domain]  Cd Length: 410  Bit Score: 214.80  E-value: 1.01e-63
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 394025725  27 KELVEPVSRFFEEVNDP-AKNDALEM-VEETTWQGLKELGAFGLQVPSELGGVGLCNTQYARLVEIVGMHDLGVGITLGA 104
Cdd:PTZ00461  42 AALRETVAKFSREVVDKhAREDDINMhFNRDLFKQLGDLGVMGVTVPEADGGAGMDAVAAVIIHHELSKYDPGFCLAYLA 121

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 394025725 105 HQSIGFKGILLFGTKAQKEKYLPKLASGETVAAFCLTEPSSGSDAASIRTSAVPSPCGKYyTLNGSKLWISNGGLADIFT 184
Cdd:PTZ00461 122 HSMLFVNNFYYSASPAQRARWLPKVLTGEHVGAMGMSEPGAGTDVLGMRTTAKKDSNGNY-VLNGSKIWITNGTVADVFL 200

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 394025725 185 VFAKtpvtdpatgaVKEKITAFVVERGFGGITHGPPEKKMGIKASNTAEVFFDGVRVPSENVLGEVGSGFKVAMHILNNG 264
Cdd:PTZ00461 201 IYAK----------VDGKITAFVVERGTKGFTQGPKIDKCGMRASHMCQLFFEDVVVPAENLLGEEGKGMVGMMRNLELE 270

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 394025725 265 RFGMAAALAGTMRGIIAKAVDHATNRTQFGEKIHNFGLIQEKLARMVMLQYVTESMAYMVSANMDQGATDfQIEAAISKI 344
Cdd:PTZ00461 271 RVTLAAMAVGIAERSVELMTSYASERKAFGKPISNFGQIQRYIAEGYADTEAAKALVYSVSHNVHPGNKN-RLGSDAAKL 349

                        330       340       350       360
                 ....*....|....*....|....*....|....*....|....
gi 394025725 345 FGSEAAWKVTDECIQIMGGMGFMKEPGVERVLRDLRIFRIFEGT 388
Cdd:PTZ00461 350 FATPIAKKVADSAIQVMGGMGYSRDMPVERLWRDAKLLEIGGGT 393
ACAD_fadE5 cd01153
Putative acyl-CoA dehydrogenases similar to fadE5; Putative acyl-CoA dehydrogenase (ACAD). ...
 62-391 1.60e-54

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: 189.91  E-value: 1.60e-54
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 394025725  62 ELGAFGLQVPSELGGVGLCNTQYARLVEIVGMHDLGVGITLGAHQsiGFKGILLFGTKAQKEKYLPKLASGETVAAFCLT 141
Cdd:cd01153   47 EAGWMALGVPEEYGGQGLPITVYSALAEIFSRGDAPLMYASGTQG--AAATLLAHGTEAQREKWIPRLAEGEWTGTMCLT 124

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 394025725 142 EPSSGSDAASIRTSAVPSPCGKYYtLNGSKLWISNG--GLAD--IFTVFAKTPvtDPATGAvkEKITAFVV-------ER 210
Cdd:cd01153  125 EPDAGSDLGALRTKAVYQADGSWR-INGVKRFISAGehDMSEniVHLVLARSE--GAPPGV--KGLSLFLVpkflddgER 199

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 394025725 211 GfgGITHGPPEKKMGIKASNTAEVFFDGVRVPsenVLGEVGSGFKVAMHILNNGRFGMAAALAGTMRGIIAKAVDHATNR 290
Cdd:cd01153  200 N--GVTVARIEEKMGLHGSPTCELVFDNAKGE---LIGEEGMGLAQMFAMMNGARLGVGTQGTGLAEAAYLNALAYAKER 274

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 394025725 291 TQFGEKIHNFGLIQEKLARMVMLQYVTESMAYMVSANMD-----------QGATDFQIEAA----------ISKIFGSEA 349
Cdd:cd01153  275 KQGGDLIKAAPAVTIIHHPDVRRSLMTQKAYAEGSRALDlytatvqdlaeRKATEGEDRKAlsaladlltpVVKGFGSEA 354

                        330       340       350       360
                 ....*....|....*....|....*....|....*....|..
gi 394025725 350 AWKVTDECIQIMGGMGFMKEPGVERVLRDLRIFRIFEGTNDI 391
Cdd:cd01153  355 ALEAVSDAIQVHGGSGYTREYPIEQYYRDARITTIYEGTTGI 396
PRK12341 PRK12341
acyl-CoA dehydrogenase;
18-392 5.94e-50

acyl-CoA dehydrogenase;


Pssm-ID: 183454 [Multi-domain]  Cd Length: 381  Bit Score: 177.23  E-value: 5.94e-50
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 394025725  18 LNEEQTQFLKELVEPVSRFFEEvNDPAKNDALEMVEETTWQGLKELGAFGLQVPSELGGVGLCNTQYARLVEivGMHDLG 97
Cdd:PRK12341   5 LTEEQELLLASIRELITRNFPE-EYFRTCDENGTYPREFMRALADNGISMLGVPEEFGGTPADYVTQMLVLE--EVSKCG 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 394025725  98 VGITLgAHQSIGFKGILLFGTKAQKEKYLpKLASGETVAAFCL--TEPSSGSDAASIRTSAVPSPcGKYYtLNGSKLWIS 175
Cdd:PRK12341  82 APAFL-ITNGQCIHSMRRFGSAEQLRKTA-ESTLETGDPAYALalTEPGAGSDNNSATTTYTRKN-GKVY-LNGQKTFIT 157

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 394025725 176 NGGLADIFTVFAKtpvtDPATGAVKEKITAFVVERGFGGITHGPPEKkMGIKASNTAEVFFDGVRVPSENVLGEVGSGFK 255
Cdd:PRK12341 158 GAKEYPYMLVLAR----DPQPKDPKKAFTLWWVDSSKPGIKINPLHK-IGWHMLSTCEVYLDNVEVEESDLVGEEGMGFL 232

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 394025725 256 VAMHILNNGRFGMAAALAGTMRGIIAKAVDHATNRTQFGEKIHNFGLIQEKLARMVMLQYVTESMAYMVSANMDQGATdF 335
Cdd:PRK12341 233 NVMYNFEMERLINAARSLGFAECAFEDAARYANQRIQFGKPIGHNQLIQEKLTLMAIKIENMRNMVYKVAWQADNGQS-L 311

                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 394025725 336 QIEAAISKIFGSEAAWKVTDECIQIMGGMGFMKEPGVERVLRDLRIFRIFEGTNDIL 392
Cdd:PRK12341 312 RTSAALAKLYCARTAMEVIDDAIQIMGGLGYTDEARVSRFWRDVRCERIGGGTDEIM 368
PRK03354 PRK03354
crotonobetainyl-CoA dehydrogenase; Validated
 58-394 2.86e-42

crotonobetainyl-CoA dehydrogenase; Validated


Pssm-ID: 179566 [Multi-domain]  Cd Length: 380  Bit Score: 156.14  E-value: 2.86e-42
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 394025725  58 QGLKELGAFGLQVPSELGGVGLCNTQYARLVEIVGMhdLGVGITLGAHQSIGFKGILLFGTKAQKEKYLPKLASGETVAA 137
Cdd:PRK03354  44 KALADMGIDSLLIPEEHGGLDAGFVTLAAVWMELGR--LGAPTYVLYQLPGGFNTFLREGTQEQIDKIMAFRGTGKQMWN 121

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 394025725 138 FCLTEPSSGSDAASIRTSAVPSPcGKYYtLNGSKLWISNGGLADIFTVFAKTPVTDPatgavKEKITAFVVERGFGGITH 217
Cdd:PRK03354 122 SAITEPGAGSDVGSLKTTYTRRN-GKVY-LNGSKCFITSSAYTPYIVVMARDGASPD-----KPVYTEWFVDMSKPGIKV 194

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 394025725 218 GPPEKkMGIKASNTAEVFFDGVRVPSENVLGEVGSGFKVAMHILNNGRFGMAAALAGTMRGIIAKAVDHATNRTQFGEKI 297
Cdd:PRK03354 195 TKLEK-LGLRMDSCCEITFDDVELDEKDMFGREGNGFNRVKEEFDHERFLVALTNYGTAMCAFEDAARYANQRVQFGEAI 273

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 394025725 298 HNFGLIQEKLARMVMLQYVTESMAYMVSANMDQGATDfQIEAAISKIFGSEAAWKVTDECIQIMGGMGFMKEPGVERVLR 377
Cdd:PRK03354 274 GRFQLIQEKFAHMAIKLNSMKNMLYEAAWKADNGTIT-SGDAAMCKYFCANAAFEVVDSAMQVLGGVGIAGNHRISRFWR 352

                        330
                 ....*....|....*..
gi 394025725 378 DLRIFRIFEGTNDILRL 394
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 ...
 251-397 5.65e-41

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: 145.09  E-value: 5.65e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 394025725  251 GSGFKVAMHILNNGRFGMAAALAGTMRGIIAKAVDHATNRTQFGEKIHNFGLIQEKLARMVMLQYVTESMAYMVSANMDQ 330
Cdd:pfam00441   1 GRGFRVAMETLNHERLAIAAMALGLARRALDEALAYARRRKAFGRPLIDFQLVRHKLAEMAAEIEAARLLVYRAAEALDA 80

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 394025725  331 GATDfQIEAAISKIFGSEAAWKVTDECIQIMGGMGFMKEPGVERVLRDLRIFRIFEGTNDILRLFVA 397
Cdd:pfam00441  81 GGPD-GAEASMAKLYASEAAVEVADLAMQLHGGYGYLREYPVERLYRDARVLRIGEGTSEIQRNIIA 146
ACAD_fadE6_17_26 cd01152
Putative acyl-CoA dehydrogenases similar to fadE6, fadE17, and fadE26; Putative acyl-CoA ...
 56-397 2.25e-39

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


Pssm-ID: 173841 [Multi-domain]  Cd Length: 380  Bit Score: 148.26  E-value: 2.25e-39
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 394025725  56 TWQG-LKELGAFGLQVPSELGGVGLCNTQYARLVE---IVGM--HDLGVGITLGAHQsigfkgILLFGTKAQKEKYLPKL 129
Cdd:cd01152   39 RWQRaLAAAGWAAPGWPKEYGGRGASLMEQLIFREemaAAGApvPFNQIGIDLAGPT------ILAYGTDEQKRRFLPPI 112

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 394025725 130 ASGETVaaFCL--TEPSSGSDAASIRTSAVPSpcGKYYTLNGSKLWISNGGLADIFTVFAKTpvtDPAtgAVKEK-ITAF 206
Cdd:cd01152  113 LSGEEI--WCQgfSEPGAGSDLAGLRTRAVRD--GDDWVVNGQKIWTSGAHYADWAWLLVRT---DPE--APKHRgISIL 183

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 394025725 207 VVERGFGGITHGPPEKKMGikASNTAEVFFDGVRVPSENVLGEVGSGFKVAMHILNNGRFGMAAALAGTMRGIIAKAvdH 286
Cdd:cd01152  184 LVDMDSPGVTVRPIRSING--GEFFNEVFLDDVRVPDANRVGEVNDGWKVAMTTLNFERVSIGGSAATFFELLLARL--L 259

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 394025725 287 ATNRTQFGEkiHNFGLIQEKLARMVM----LQYVTESMAYMVSANMDQGAtdfqiEAAISKIFGSEAAWKVTDECIQIMG 362
Cdd:cd01152  260 LLTRDGRPL--IDDPLVRQRLARLEAeaeaLRLLVFRLASALAAGKPPGA-----EASIAKLFGSELAQELAELALELLG 332

                        330       340       350       360
                 ....*....|....*....|....*....|....*....|...
gi 394025725 363 GMGFMKEPG--------VERVLRDLRIFRIFEGTNDILRLFVA 397
Cdd:cd01152  333 TAALLRDPApgaelagrWEADYLRSRATTIYGGTSEIQRNIIA 375
ACAD_FadE2 cd01155
Acyl-CoA dehydrogenases similar to fadE2; FadE2-like Acyl-CoA dehydrogenase (ACAD). Acyl-CoA ...
 26-387 6.79e-36

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: 138.68  E-value: 6.79e-36
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 394025725  26 LKELVEPVSRFFEEVNDPAKNDALEMVEE---TTWQ------GLKE----LGAFGLQVPSELGGVGLCNTQYARLVEIVG 92
Cdd:cd01155    3 AQELRARVKAFMEEHVYPAEQEFLEYYAEggdRWWTpppiieKLKAkakaEGLWNLFLPEVSGLSGLTNLEYAYLAEETG 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 394025725  93 MHDLGVGITLGAHQSIGFKGIL-LFGTKAQKEKYLPKLASGETVAAFCLTEPS-SGSDAASIRTSAVPSpcGKYYTLNGS 170
Cdd:cd01155   83 RSFFAPEVFNCQAPDTGNMEVLhRYGSEEQKKQWLEPLLDGKIRSAFAMTEPDvASSDATNIECSIERD--GDDYVINGR 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 394025725 171 KLWISNGGLAD--IFTVFAKTpvtDPATGAVKEKITAFVVERGFGGITHGPPEKKMGIKAS--NTAEVFFDGVRVPSENV 246
Cdd:cd01155  161 KWWSSGAGDPRckIAIVMGRT---DPDGAPRHRQQSMILVPMDTPGVTIIRPLSVFGYDDAphGHAEITFDNVRVPASNL 237

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 394025725 247 LGEVGSGFKVAMHILNNGRFGMAAALAGTMRGIIAKAVDHATNRTQFGEKIHNFGLIQEKLA--RMV--MLQYVTESMAY 322
Cdd:cd01155  238 ILGEGRGFEIAQGRLGPGRIHHCMRLIGAAERALELMCQRAVSREAFGKKLAQHGVVAHWIAksRIEieQARLLVLKAAH 317

                        330       340       350       360       370       380
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 394025725 323 MvsanMDQ-GATDFQIEAAISKIFGSEAAWKVTDECIQIMGGMGFMKEPGVERVLRDLRIFRIFEG 387
Cdd:cd01155  318 M----IDTvGNKAARKEIAMIKVAAPRMALKIIDRAIQVHGAAGVSQDTPLANMYAWARTLRIADG 379
PLN02526 PLN02526
acyl-coenzyme A oxidase
 5-413 3.32e-34

acyl-coenzyme A oxidase


Pssm-ID: 178141 [Multi-domain]  Cd Length: 412  Bit Score: 134.21  E-value: 3.32e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 394025725   5 QLTTDQVFPyPSVLN----------EEQT------QFLKELVEPV-SRFFEEVNDPakndalemveettWQGLKELGAFG 67
Cdd:PLN02526   8 QATPASIFP-PSVSDyyqfddlltpEEQAlrkrvrECMEKEVAPImTEYWEKAEFP-------------FHIIPKLGSLG 73

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 394025725  68 LqvpseLGGV-------GLCNTQYARLVEIVGMHDLGVGITLGAHQSIGFKGILLFGTKAQKEKYLPKLASGETVAAFCL 140
Cdd:PLN02526  74 I-----AGGTikgygcpGLSITASAIATAEVARVDASCSTFILVHSSLAMLTIALCGSEAQKQKYLPSLAQLDTVACWAL 148

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 394025725 141 TEPSSGSDAASIRTSAVPSPCGkyYTLNGSKLWISNGGLADIFTVFAKTPVTDpatgavkeKITAFVVERGFGGITHGPP 220
Cdd:PLN02526 149 TEPDYGSDASSLNTTATKVEGG--WILNGQKRWIGNSTFADVLVIFARNTTTN--------QINGFIVKKGAPGLKATKI 218

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 394025725 221 EKKMGIKASNTAEVFFDGVRVPSENVLGEVGSgFKVAMHILNNGRFGMAAALAGTMRGIIAKAVDHATNRTQFGEKIHNF 300
Cdd:PLN02526 219 ENKIGLRMVQNGDIVLKDVFVPDEDRLPGVNS-FQDTNKVLAVSRVMVAWQPIGISMGVYDMCHRYLKERKQFGAPLAAF 297

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 394025725 301 GLIQEKLARmvMLQYVtESMAYM--------VSANMDQGatdfqiEAAISKIFGSEAAWKVTDECIQIMGGMGFMKEPGV 372
Cdd:PLN02526 298 QINQEKLVR--MLGNI-QAMFLVgwrlcklyESGKMTPG------HASLGKAWITKKARETVALGRELLGGNGILADFLV 368

                        410       420       430       440
                 ....*....|....*....|....*....|....*....|.
gi 394025725 373 ERVLRDLRIFRIFEGTNDILRLFValqgcmdkGKELSGLGS 413
Cdd:PLN02526 369 AKAFCDLEPIYTYEGTYDINALVT--------GREITGIAS 401
AidB cd01154
Proteins involved in DNA damage response, similar to the AidB gene product; AidB is one of ...
 123-394 3.23e-32

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: 128.64  E-value: 3.23e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 394025725 123 EKYLPKLASGET----VAAFCLTEPSSGSDAASIRTSAVPSPcGKYYTLNGSKlWISNGGLADIFTVFAKTPVTDPATGA 198
Cdd:cd01154  132 KQYLPGLLSDRYktglLGGTWMTEKQGGSDLGANETTAERSG-GGVYRLNGHK-WFASAPLADAALVLARPEGAPAGARG 209

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 394025725 199 vkekITAFVVER-----GFGGITHGPPEKKMGIKASNTAEVFFDGvrvpSEN-VLGEVGSGFKVAMHILNNGRFGMAAAL 272
Cdd:cd01154  210 ----LSLFLVPRlledgTRNGYRIRRLKDKLGTRSVATGEVEFDD----AEAyLIGDEGKGIYYILEMLNISRLDNAVAA 281

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 394025725 273 AGTMRGIIAKAVDHATNRTQFGEKIHNFGLIQEKLARMVMLQYVTESMAYMVSANMDQGATDFQIEA-------AISKIF 345
Cdd:cd01154  282 LGIMRRALSEAYHYARHRRAFGKPLIDHPLMRRDLAEMEVDVEAATALTFRAARAFDRAAADKPVEAhmarlatPVAKLI 361

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*....
gi 394025725 346 GSEAAWKVTDECIQIMGGMGFMKEPGVERVLRDLRIFRIFEGTNDILRL 394
Cdd:cd01154  362 ACKRAAPVTSEAMEVFGGNGYLEEWPVARLHREAQVTPIWEGTGNIQAL 410
PTZ00456 PTZ00456
acyl-CoA dehydrogenase; Provisional
 54-391 5.96e-29

acyl-CoA dehydrogenase; Provisional


Pssm-ID: 185635 [Multi-domain]  Cd Length: 622  Bit Score: 121.51  E-value: 5.96e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 394025725  54 ETTWQGLKELGAFGLQVPSELGGVGLCNTQYARLVEIVGMHDLGVGITLGahQSIG-FKGILLFGTKAQKEKYLPKLASG 132
Cdd:PTZ00456 102 KEAYQALKAGGWTGISEPEEYGGQALPLSVGFITRELMATANWGFSMYPG--LSIGaANTLMAWGSEEQKEQYLTKLVSG 179

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 394025725 133 ETVAAFCLTEPSSGSDAASIRTSAVPSPCGKyYTLNGSKLWISNG--GLAD--IFTVFAKTPVTDPATgavkEKITAFVV 208
Cdd:PTZ00456 180 EWSGTMCLTEPQCGTDLGQVKTKAEPSADGS-YKITGTKIFISAGdhDLTEniVHIVLARLPNSLPTT----KGLSLFLV 254

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 394025725 209 ERGF----------GGITHGPPEKKMGIKASNTAEVFFDGvrvPSENVLGEVGSGFKVAMHILNNGRfgMAAALAGTMRG 278
Cdd:PTZ00456 255 PRHVvkpdgsletaKNVKCIGLEKKMGIKGSSTCQLSFEN---SVGYLIGEPNAGMKQMFTFMNTAR--VGTALEGVCHA 329

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 394025725 279 IIA--KAVDHATNR--------TQFGEKIHNFGLIQEKLARMVML-QYVTE---SMAYMVSANMD--QGATDFQIEAA-- 340
Cdd:PTZ00456 330 ELAfqNALRYARERrsmralsgTKEPEKPADRIICHANVRQNILFaKAVAEggrALLLDVGRLLDihAAAKDAATREAld 409

                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 394025725 341 --------ISKIFGSEAAWKVTDECIQIMGGMGFMKEPGVERVLRDLRIFRIFEGTNDI 391
Cdd:PTZ00456 410 heigfytpIAKGCLTEWGVEAASRCLQVWGGHGYIKGNGMEQILRDARIGTLYEGTTGI 468
Acyl-CoA_dh_M pfam02770
Acyl-CoA dehydrogenase, middle domain; Central domain of Acyl-CoA dehydrogenase has a ...
 137-237 5.01e-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: 5.01e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 394025725  137 AFCLTEPSSGSDAASIRTSAVPSPcGKYYTLNGSKLWISNGGLADIFTVFAKTPVTDPATGavkekITAFVVERGFGGIT 216
Cdd:pfam02770   1 AFALTEPGAGSDVASLKTTAADGD-GGGWVLNGTKWWITNAGIADLFLVLARTGGDDRHGG-----ISLFLVPKDAPGVS 74

                          90       100
                  ....*....|....*....|.
gi 394025725  217 HGPPEKKMGIKASNTAEVFFD 237
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 ...
 19-133 1.18e-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: 98.69  E-value: 1.18e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 394025725   19 NEEQTQFLKElvepVSRFFEEVNDP--AKNDALEMVEETTWQGLKELGAFGLQVPSELGGVGLCNTQYARLVEIVGMHDL 96
Cdd:pfam02771   1 TEEQEALRDT----VREFAEEEIAPhaAEWDEEGEFPRELWKKLGELGLLGITIPEEYGGAGLDYLAYALVAEELARADA 76

                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 394025725   97 GVGITLGAHQSIGFKGILLFGTKAQKEKYLPKLASGE 133
Cdd:pfam02771  77 SVALALSVHSSLGAPPILRFGTEEQKERYLPKLASGE 113
fadE PRK09463
acyl-CoA dehydrogenase; Reviewed
 12-370 3.50e-21

acyl-CoA dehydrogenase; Reviewed


Pssm-ID: 236528 [Multi-domain]  Cd Length: 777  Bit Score: 97.96  E-value: 3.50e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 394025725  12 FPYPSVLNEEQTqFLKELVEPVSRFfeeVNDPAKNDALEMVEETTWQGLKELGAFGLQVPSELGGVGLCNTQYARLVEIV 91
Cdd:PRK09463  74 YPKPTLTAEEQA-FLDGPVEELCRM---VNDWQITHELADLPPEVWQFIKEHGFFGMIIPKEYGGLEFSAYAHSRVLQKL 149

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 394025725  92 GMHDLGVGITLGAHQSIGfKGILL--FGTKAQKEKYLPKLASGETVAAFCLTEPSSGSDAASIRTSAVpsPC-----GK- 163
Cdd:PRK09463 150 ASRSGTLAVTVMVPNSLG-PGELLlhYGTDEQKDHYLPRLARGEEIPCFALTSPEAGSDAGSIPDTGV--VCkgewqGEe 226

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 394025725 164 --YYTLNGSKLWISnggLADIFTVFA---KtpVTDPaTGAVKEK----ITAFVVERGFGGITHGPPEKKMGIkasntaeV 234
Cdd:PRK09463 227 vlGMRLTWNKRYIT---LAPIATVLGlafK--LYDP-DGLLGDKedlgITCALIPTDTPGVEIGRRHFPLNV-------P 293

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 394025725 235 FFDG------VRVPSENVLGE---VGSGFKVAMHILNNGRFGMAAALAGTMRGIIAKAV-DHATNRTQFGEKIHNFGLIQ 304
Cdd:PRK09463 294 FQNGptrgkdVFIPLDYIIGGpkmAGQGWRMLMECLSVGRGISLPSNSTGGAKLAALATgAYARIRRQFKLPIGKFEGIE 373

                        330       340       350       360       370       380
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 394025725 305 EKLARMVMLQYVTESMAYMVSANMDQGATDFQIeAAISKIFGSEAAWKVTDECIQIMGGMGFMKEP 370
Cdd:PRK09463 374 EPLARIAGNAYLMDAARTLTTAAVDLGEKPSVL-SAIAKYHLTERGRQVINDAMDIHGGKGICLGP 438
PTZ00457 PTZ00457
acyl-CoA dehydrogenase; Provisional
 1-539 7.26e-21

acyl-CoA dehydrogenase; Provisional


Pssm-ID: 185636 [Multi-domain]  Cd Length: 520  Bit Score: 96.10  E-value: 7.26e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 394025725   1 MFKGQLTTDQVFPYPS-VLNEEQTQFLKELVEPVSrffeevndpaKNDalemveettwqglKELG-AFGLQVPSELGGVG 78
Cdd:PTZ00457  22 LFNFKIVPEEMFPYPCrKLDGDEAENLQSLLEQIR----------SND-------------KILGnLYGARIATEYGGLG 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 394025725  79 LCNTQYARLVEIVGMHdlGVGITLGAHQSIGFKGILL--FGTKAQKEKYLPKLASGETVAAFClTEPSSGSDAASIRTSA 156
Cdd:PTZ00457  79 LGHTAHALIYEEVGTN--CDSKLLSTIQHSGFCTYLLstVGSKELKGKYLTAMSDGTIMMGWA-TEEGCGSDISMNTTKA 155

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 394025725 157 VPSPCGKYyTLNGSKLWIsNGGLADIFTVFAKTpVTDPATGA---VKEKITAFVVERgfggithgppeKKMGIKASNTAE 233
Cdd:PTZ00457 156 SLTDDGSY-VLTGQKRCE-FAASATHFLVLAKT-LTQTAAEEgatEVSRNSFFICAK-----------DAKGVSVNGDSV 221

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 394025725 234 VFFDgvrVPSENVLGEVGSGFKVAMHILNNGRFGMAAALAGTMRGIIAKAVDhaTNRTQFgekihnfglIQEKLARMVML 313
Cdd:PTZ00457 222 VFEN---TPAADVVGVVGEGFKDAMITLFTEQYLYAASLLGIMKRVVQELRG--SNAEEG---------ATDTVASFACA 287

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 394025725 314 QYVTESMAYMVSANMDQGATDFQIEAAISKIFGSEAawkvTDECIQIMGGMGFMKEPgVERVLRDLRIFRIFEGTNDIlr 393
Cdd:PTZ00457 288 MYAMESTLYALTANLDLPTEDSLLECTLVSAFVQST----TNQLLSILETATPPSTT-LEKCFANARLFLSMMESRDF-- 360

                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 394025725 394 LFVALQGCmdkGKELSGLgsalknPFGNAGLLLGEAGKQLRrraglgsGLSLSGLVHPELSRSGELAVRALEQFATVVEA 473
Cdd:PTZ00457 361 LYSSAVCC---GVEDYGL------FFQRASTLQMMQARTLR-------SLGVRDRVPIKNLPDCSLIDEAVVAFGNAVEA 424

                        490       500       510       520       530       540
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 394025725 474 KLIKHKKGIVNEQFLLQRLADGAIDLYAMVVVLSRASRSLSEGHPTAQHEKMLCDTWCIEAAARIR 539
Cdd:PTZ00457 425 TFVRSGSQVPYQQLLLNRLGEAASLLYAASAVASRASMCVSKGLPSAKVEGELASAFIAMAVSRAR 490
PRK13026 PRK13026
acyl-CoA dehydrogenase; Reviewed
 57-365 9.74e-21

acyl-CoA dehydrogenase; Reviewed


Pssm-ID: 237277 [Multi-domain]  Cd Length: 774  Bit Score: 96.56  E-value: 9.74e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 394025725  57 WQGLKELGAFGLQVPSELGGVGLcnTQYA--RLVEIVGMHDLGVGITLGAHQSIGfKGILL--FGTKAQKEKYLPKLASG 132
Cdd:PRK13026 114 WDYLKKEGFFALIIPKEYGGKGF--SAYAnsTIVSKIATRSVSAAVTVMVPNSLG-PGELLthYGTQEQKDYWLPRLADG 190

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 394025725 133 ETVAAFCLTEPSSGSDAASIRTSAVpsPC-GKY-------YTLNGSKLWISnggLADIFTVF-----AKTPvtDPATGAV 199
Cdd:PRK13026 191 TEIPCFALTGPEAGSDAGAIPDTGI--VCrGEFegeevlgLRLTWDKRYIT---LAPVATVLglafkLRDP--DGLLGDK 263

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 394025725 200 KE-KITAFVVERGFGGITHGPPEKKMGIkasntaeVFFDG------VRVPSENVLG---EVGSGFKVAMHILNNGRFGMA 269
Cdd:PRK13026 264 KElGITCALIPTDHPGVEIGRRHNPLGM-------AFMNGttrgkdVFIPLDWIIGgpdYAGRGWRMLVECLSAGRGISL 336

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 394025725 270 AALAGTMRGIIAKAVD-HATNRTQFGEKIHNFGLIQEKLARMVMLQYVTESMAYMVSANMDQGATDfQIEAAISKIFGSE 348
Cdd:PRK13026 337 PALGTASGHMATRTTGaYAYVRRQFGMPIGQFEGVQEALARIAGNTYLLEAARRLTTTGLDLGVKP-SVVTAIAKYHMTE 415

                        330
                 ....*....|....*..
gi 394025725 349 AAWKVTDECIQIMGGMG 365
Cdd:PRK13026 416 LARDVVNDAMDIHAGKG 432
AXO cd01150
Peroxisomal acyl-CoA oxidase; Peroxisomal acyl-CoA oxidases (AXO) catalyze the first set in ...
 87-437 9.51e-19

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: 90.08  E-value: 9.51e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 394025725  87 LVEIVGMHDLGVGITLGAHQSIGFKGILLFGTKAQKEKYLPKLASGETVAAFCLTEPSSGSDAASIRTSAVPSPCGKYYT 166
Cdd:cd01150   87 LTNSLGGYDLSLGAKLGLHLGLFGNAIKNLGTDEHQDYWLQGANNLEIIGCFAQTELGHGSNLQGLETTATYDPLTQEFV 166

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 394025725 167 LN-----GSKLWIsnGGLADIFT---VFAKTpvtdpATGAVKEKITAFVVE-------RGFGGITHGPPEKKMGIKASNT 231
Cdd:cd01150  167 INtpdftATKWWP--GNLGKTAThavVFAQL-----ITPGKNHGLHAFIVPirdpkthQPLPGVTVGDIGPKMGLNGVDN 239

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 394025725 232 AEVFFDGVRVPSENVL---GEV-------------GSGFKVAMHILNNGRFGMAAALAGTMRGIIAKAVDHATNRTQFGE 295
Cdd:cd01150  240 GFLQFRNVRIPRENLLnrfGDVspdgtyvspfkdpNKRYGAMLGTRSGGRVGLIYDAAMSLKKAATIAIRYSAVRRQFGP 319

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 394025725 296 K-------IHNFGLIQEK----LARMVMLQYVTESMAYM---VSANMDQGATDFQIE----AAISKIFGSEAAWKVTDEC 357
Cdd:cd01150  320 KpsdpevqILDYQLQQYRlfpqLAAAYAFHFAAKSLVEMyheIIKELLQGNSELLAElhalSAGLKAVATWTAAQGIQEC 399

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 394025725 358 IQIMGGMGFMKEPGVERVLRDLRIFRIFEGTNDILRLFVAlQGCMDKGKELSGLGSALKNPFGNAGLLLGEAGKQLRRRA 437
Cdd:cd01150  400 REACGGHGYLAMNRLPTLRDDNDPFCTYEGDNTVLLQQTA-NYLLKKYAQAFSLADYLEAYEWLAAHLLRHAAAQLEKLK 478
PLN02636 PLN02636
acyl-coenzyme A oxidase
 83-397 1.45e-18

acyl-coenzyme A oxidase


Pssm-ID: 215342 [Multi-domain]  Cd Length: 686  Bit Score: 89.53  E-value: 1.45e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 394025725  83 QYARLVEIVGMHDLGVGITLGAHQSIGFKGILLFGTKAQKEKYLPKLASGETVAAFCLTEPSSGSDAASIRTSAVPSPCG 162
Cdd:PLN02636 122 KYFAITEAVGSVDMSLGIKLGVQYSLWGGSVINLGTKKHRDKYFDGIDNLDYPGCFAMTELHHGSNVQGLQTTATFDPLT 201

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 394025725 163 KYYTLN-----GSKLWISNGGLADIF-TVFAKTPVTDPATGAVKEK-ITAFVV-------ERGFGGITHGPPEKKMGIKA 228
Cdd:PLN02636 202 DEFVINtpndgAIKWWIGNAAVHGKFaTVFARLKLPTHDSKGVSDMgVHAFIVpirdmktHQVLPGVEIRDCGHKVGLNG 281

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 394025725 229 SNTAEVFFDGVRVPSENVLGEVG----------------SGFKVAMHILNNGRFGMAAALAGTMRGIIAKAVDHATNRTQ 292
Cdd:PLN02636 282 VDNGALRFRSVRIPRDNLLNRFGdvsrdgkytsslptinKRFAATLGELVGGRVGLAYGSVGVLKASNTIAIRYSLLRQQ 361

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 394025725 293 FGE------KIHNFGLIQEKLarMVML----------QYVTESMAYMVSANMDQGATDFQIEAAISKIFGSEAAWKVTDE 356
Cdd:PLN02636 362 FGPpkqpeiSILDYQSQQHKL--MPMLastyafhfatEYLVERYSEMKKTHDDQLVADVHALSAGLKAYITSYTAKALST 439

                        330       340       350       360
                 ....*....|....*....|....*....|....*....|....
gi 394025725 357 CIQIMGGMGFmkePGVER--VLR-DLRIFRIFEGTNDILRLFVA 397
Cdd:PLN02636 440 CREACGGHGY---AAVNRfgSLRnDHDIFQTFEGDNTVLLQQVA 480
PLN02876 PLN02876
acyl-CoA dehydrogenase
 72-391 1.75e-18

acyl-CoA dehydrogenase


Pssm-ID: 215473 [Multi-domain]  Cd Length: 822  Bit Score: 89.47  E-value: 1.75e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 394025725  72 SELGGVGLCNTQYARLVEIVGMHDLGVGI-TLGAHQSIGFKGILLFGTKAQKEKYLPKLASGETVAAFCLTEPS-SGSDA 149
Cdd:PLN02876 487 DQLLGAGLSNLEYGYLCEIMGRSVWAPQVfNCGAPDTGNMEVLLRYGNKEQQLEWLIPLLEGKIRSGFAMTEPQvASSDA 566

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 394025725 150 ASIRTSAVPSpcGKYYTLNGSKLWISngGLAD----IFTVFAKTPVTDPA------------TGAVKEKITAFVVerGFG 213
Cdd:PLN02876 567 TNIECSIRRQ--GDSYVINGTKWWTS--GAMDprcrVLIVMGKTDFNAPKhkqqsmilvdiqTPGVQIKRPLLVF--GFD 640

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 394025725 214 GITHGppekkmgikasnTAEVFFDGVRVPSENVLGEVGSGFKVAMHILNNGRFGMAAALAGTMRGIIAKAVDHATNRTQF 293
Cdd:PLN02876 641 DAPHG------------HAEISFENVRVPAKNILLGEGRGFEIAQGRLGPGRLHHCMRLIGAAERGMQLMVQRALSRKAF 708

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 394025725 294 GEKIHNFGLIQEKLARmvmLQYVTESMAYMVSANMDQ----GATDFQIEAAISKIFGSEAAWKVTDECIQIMGGMGFMKE 369
Cdd:PLN02876 709 GKLIAQHGSFLSDLAK---CRVELEQTRLLVLEAADQldrlGNKKARGIIAMAKVAAPNMALKVLDMAMQVHGAAGVSSD 785

                        330       340
                 ....*....|....*....|..
gi 394025725 370 PGVERVLRDLRIFRIFEGTNDI 391
Cdd:PLN02876 786 TVLAHLWATARTLRIADGPDEV 807
DszC cd01163
Dibenzothiophene (DBT) desulfurization enzyme C; DszC is a flavin reductase dependent enzyme, ...
 52-291 2.77e-11

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: 65.42  E-value: 2.77e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 394025725  52 VEETTWqgLKELGAFGLQVPSELGGVGLCNTQYARLVEIVGMHDLGVGITLGAHqsIGF-KGILLFGTKAQKEKYLPKLA 130
Cdd:cd01163   25 YEEVAL--LRQSGLGTLRVPKEYGGLGASLPDLYEVVRELAAADSNIAQALRAH--FGFvEALLLAGPEQFRKRWFGRVL 100

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 394025725 131 SGETVAAfclTEPSSGSDAASIRTSAVPSPCGKYYtLNGSKlWISNGGL-ADIFTVFAktpvTDPAtgavkEKITAFVVE 209
Cdd:cd01163  101 NGWIFGN---AVSERGSVRPGTFLTATVRDGGGYV-LNGKK-FYSTGALfSDWVTVSA----LDEE-----GKLVFAAVP 166

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 394025725 210 RGFGGITHGPPEKKMGIK--ASNTAEvfFDGVRVPSENVLGEvGSGFKVAMHILNNGRFGMAAALAGTMRGIIAKAVDHA 287
Cdd:cd01163  167 TDRPGITVVDDWDGFGQRltASGTVT--FDNVRVEPDEVLPR-PNAPDRGTLLTAIYQLVLAAVLAGIARAALDDAVAYV 243


                 ....
gi 394025725 288 TNRT 291
Cdd:cd01163  244 RSRT 247
PRK11561 PRK11561
isovaleryl CoA dehydrogenase; Provisional
 140-403 1.81e-08

isovaleryl CoA dehydrogenase; Provisional


Pssm-ID: 183199 [Multi-domain]  Cd Length: 538  Bit Score: 57.07  E-value: 1.81e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 394025725 140 LTEPSSGSDAASIRTSAVPSPcGKYYTLNGSKlWISNGGLADIFTVFAKTpvtdpatgavKEKITAFVVERGFGGITHGP 219
Cdd:PRK11561 184 MTEKQGGSDVLSNTTRAERLA-DGSYRLVGHK-WFFSVPQSDAHLVLAQA----------KGGLSCFFVPRFLPDGQRNA 251

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 394025725 220 P-----EKKMGIKASNTAEVFFDGVrvpSENVLGEVGSGFKvamHILNNG---RFGMAAALAGTMRGIIAKAVDHATNRT 291
Cdd:PRK11561 252 IrlerlKDKLGNRSNASSEVEFQDA---IGWLLGEEGEGIR---LILKMGgmtRFDCALGSHGLMRRAFSVAIYHAHQRQ 325

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 394025725 292 QFGEKIHNFGLIQEKLARMVM-LQYVTESMAYMVSANMDQGATDfqiEAAISKIFGSEAAWKVTD-------ECIQIMGG 363
Cdd:PRK11561 326 VFGKPLIEQPLMRQVLSRMALqLEGQTALLFRLARAWDRRADAK---EALWARLFTPAAKFVICKrgipfvaEAMEVLGG 402

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*
gi 394025725 364 MGFMKEPGVERVLRDLRIFRIFEGTN-----DILRLFVALQGCMD 403
Cdd:PRK11561 403 IGYCEESELPRLYREMPVNSIWEGSGnimclDVLRVLNKQPGVYD 447
Acyl-CoA_dh_2 pfam08028
Acyl-CoA dehydrogenase, C-terminal domain;
267-389 1.05e-07

Acyl-CoA dehydrogenase, C-terminal domain;


Pssm-ID: 429790 [Multi-domain]  Cd Length: 133  Bit Score: 51.19  E-value: 1.05e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 394025725  267 GMAAALAGTMRGIIAKAVDHATNRTQ--FGEKIHNFGLIQEKLARMV-------MLQYVTESMAYMVSANMDQGATDFQI 337
Cdd:pfam08028   1 GIAAAALGAARAALAEFTERARGRVRayFGVPLAEDPATQLALAEAAaridaarLLLERAAARIEAAAAAGKPVTPALRA 80

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|..
gi 394025725  338 EAAISKIFGSEAAWKVTDECIQIMGGMGFMKEPGVERVLRDLRIFRIFEGTN 389
Cdd:pfam08028  81 EARRAAAFATELAVAAVDALFRAAGGSALFQDSPLQRIWRDIHAAAQHAAVN 132
PLN02312 PLN02312
acyl-CoA oxidase
 85-412 1.39e-07

acyl-CoA oxidase


Pssm-ID: 215178 [Multi-domain]  Cd Length: 680  Bit Score: 54.39  E-value: 1.39e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 394025725  85 ARLVEIVGMHDLGVGITLGAHQSIGFKGILLFGTKAQKEKYLPKLASGETVAAFCLTEPSSGSDAASIRTSAVPSPCGKY 164
Cdd:PLN02312 136 LALLEVIGIYDHSLAIKLGVHFFLWGGAIKFLGTKRHHDKWLKDTEDYVVKGCFAMTELGHGSNVRGIETVTTYDPKTEE 215

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 394025725 165 YTLN-----GSKLWIsnGGLADIFT---VFAKTPVTdpatgAVKEKITAFVVE------RGFGGITHGPPEKKMGIKASN 230
Cdd:PLN02312 216 FVINtpcesAQKYWI--GGAANHAThtiVFSQLHIN-----GKNEGVHAFIAQirdqdgNICPNIRIADCGHKIGLNGVD 288

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 394025725 231 TAEVFFDGVRVPSENVLGEVG----------------SGFKVAMHILNNGRFGMAAALAGTMRGIIAKAVDHATNRTQF- 293
Cdd:PLN02312 289 NGRIWFDNLRIPRENLLNSVAdvspdgkyvsaikdpdQRFGAFLAPLTSGRVTIAVSAIYSSKVGLAIAIRYSLSRRAFs 368

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 394025725 294 ----GEKI-------HNFGLIqEKLARMVMLQYVTESMAYMVSANMDQGATDFQIeaaISKIFGSEAAW---KVTDECIQ 359
Cdd:PLN02312 369 vtpnGPEVllldypsHQRRLL-PLLAKTYAMSFAANDLKMIYVKRTPESNKAIHV---VSSGFKAVLTWhnmRTLQECRE 444

                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 394025725 360 IMGGMGFMKEPGVERVLRDLRIFRIFEGTNDILR------LFVALQGCMDKGKELSGLG 412
Cdd:PLN02312 445 ACGGQGLKTENRVGQLKAEYDVQSTFEGDNNVLMqqvskaLLAEYVSAKKRNKPFKGLG 503
PTZ00460 PTZ00460
acyl-CoA dehydrogenase; Provisional
 117-397 5.21e-06

acyl-CoA dehydrogenase; Provisional


Pssm-ID: 185639 [Multi-domain]  Cd Length: 646  Bit Score: 49.46  E-value: 5.21e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 394025725 117 GTKAQKEKYLPKLASGETVAAFCLTEPSSGSDAASIRTSAVPSPCGKYYTLN-----GSKLWISN-GGLADIFTVFAKTP 190
Cdd:PTZ00460 110 GTDEQINLWMPSLLNFEIVGCYAQTELGHGSDVQNLETTATYDKQTNEFVIHtpsveAVKFWPGElGFLCNFALVYAKLI 189

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 394025725 191 VTDPATG--AVKEKITAFVVERGFGGITHGPPEKKMGIKASNTAEVFFDGVRVPSENVLG---EVGSGFKVAMHilNNGR 265
Cdd:PTZ00460 190 VNGKNKGvhPFMVRIRDKETHKPLQGVEVGDIGPKMGYAVKDNGFLSFDHYRIPLDSLLAryiKVSEDGQVERQ--GNPK 267

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 394025725 266 FGMAAALagTMRGIIAK------------AVDHATNRTQFGE------KIHNFGLIQEK----LARMVMLQYVTESMAYM 323
Cdd:PTZ00460 268 VSYASMM--YMRNLIIDqyprfaaqaltvAIRYSIYRQQFTNdnkqenSVLEYQTQQQKllplLAEFYACIFGGLKIKEL 345

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 394025725 324 VSANMDQ-GATDFQIEAAISKIFGSEAAW------KVTDECIQIMGGMGFMKEPGVERVLRDLRIFRIFEGTNDILRLFV 396
Cdd:PTZ00460 346 VDDNFNRvQKNDFSLLQLTHAILSAAKANytyfvsNCAEWCRLSCGGHGYAHYSGLPAIYFDMSPNITLEGENQIMYLQL 425


                 .
gi 394025725 397 A 397
Cdd:PTZ00460 426 A 426
PLN02443 PLN02443
acyl-coenzyme A oxidase
 117-425 1.65e-05

acyl-coenzyme A oxidase


Pssm-ID: 178062 [Multi-domain]  Cd Length: 664  Bit Score: 47.91  E-value: 1.65e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 394025725 117 GTKAQKEKYLPKLASGETVAAFCLTEPSSGSDAASIRTSAVPSPCGKYY-----TLNGSKLWisNGGLADIFT---VFAK 188
Cdd:PLN02443 114 GTEEQQKKWLPLAYKMQIIGCYAQTELGHGSNVQGLETTATFDPKTDEFvihspTLTSSKWW--PGGLGKVSThavVYAR 191

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 394025725 189 TpvtdpATGAVKEKITAFVVE-------RGFGGITHGPPEKKMGIKASNTAE---VFFDGVRVPSENVLGEVGSGFKVAM 258
Cdd:PLN02443 192 L-----ITNGKDHGIHGFIVQlrslddhSPLPGVTVGDIGMKFGNGAYNTMDngfLRFDHVRIPRDQMLMRLSKVTREGK 266

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 394025725 259 HILNNgrfgMAAALA-GTM----RGIIAK-----------AVDHATNRTQFGEK-------IHNFGLIQEK----LARMV 311
Cdd:PLN02443 267 YVQSD----VPRQLVyGTMvyvrQTIVADastalsravciATRYSAVRRQFGSQdggpetqVIDYKTQQSRlfplLASAY 342

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 394025725 312 MLQYVTESMAYMVSANMDQ-GATDF----QIEAAIS--KIFGSEAAWKVTDECIQIMGGMGFMKEPGVERVLRDLRIFRI 384
Cdd:PLN02443 343 AFRFVGEWLKWLYTDVTQRlEANDFstlpEAHACTAglKSLTTSATADGIEECRKLCGGHGYLCSSGLPELFAVYVPACT 422

                        330       340       350       360
                 ....*....|....*....|....*....|....*....|.
gi 394025725 385 FEGTNDILRLFVAlQGCMdkgKELSGLGSAlKNPFGNAGLL 425
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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