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Conserved domains on  [gi|767992071|ref|XP_011522131|]
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very long-chain specific acyl-CoA dehydrogenase, mitochondrial isoform X2 [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 ...
72-478 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: 751.22  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767992071  72 SFAVGMFKGQLTTDQVFPYPSVLNEEQTQFLKELVEPVSRFFEEVNDPAKNDALEMVEETTWQGLKELGAFGLQVPSELG 151
Cdd:cd01161    1 SFALNMFLGDIVTKQVFPYPSVLTEEQTEELNMLVGPVEKFFEEVNDPAKNDQLEKIPRKTLTQLKELGLFGLQVPEEYG 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767992071 152 GVGLCNTQYARLVEIVGMhDLGVGITLGAHQSIGFKGILLFGTKAQKEKYLPKLASGETVAAFCLTEPSSGSDAASIRTS 231
Cdd:cd01161   81 GLGLNNTQYARLAEIVGM-DLGFSVTLGAHQSIGFKGILLFGTEAQKEKYLPKLASGEWIAAFALTEPSSGSDAASIRTT 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767992071 232 AVPSPCGKYYTLNGSKLWISNGGLADIFTVFAKTPVTDPaTGAVKEKITAFVVERGFGGITHGPPEKKMGIKASNTAEVF 311
Cdd:cd01161  160 AVLSEDGKHYVLNGSKIWITNGGIADIFTVFAKTEVKDA-TGSVKDKITAFIVERSFGGVTNGPPEKKMGIKGSNTAEVY 238
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767992071 312 FDGVRVPSENVLGEVGSGFKVAMHILNNGRFGMAAALAGTMRGIIAKAVDHATNRTQFGEKIHNFGLIQEKLARMVMLQY 391
Cdd:cd01161  239 FEDVKIPVENVLGEVGDGFKVAMNILNNGRFGMGAALIGTMKRCIEKAVDYANNRKQFGKKIHEFGLIQEKLANMAILQY 318
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767992071 392 VTESMAYMVSANMDQGAT-DFQIEAAISKIFGSEAAWKVTDECIQIMGGMGFMKEPGVERVLRDLRIFRIFEGTNDILRL 470
Cdd:cd01161  319 ATESMAYMTSGNMDRGLKaEYQIEAAISKVFASEAAWLVVDEAIQIHGGMGFMREYGVERVLRDLRIFRIFEGTNEILRL 398

                 ....*...
gi 767992071 471 FVALQGCM 478
Cdd:cd01161  399 FIALTGLQ 406
 
Name Accession Description Interval E-value
VLCAD cd01161
Very long chain acyl-CoA dehydrogenase; VLCAD is an acyl-CoA dehydrogenase (ACAD), which is ...
72-478 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: 751.22  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767992071  72 SFAVGMFKGQLTTDQVFPYPSVLNEEQTQFLKELVEPVSRFFEEVNDPAKNDALEMVEETTWQGLKELGAFGLQVPSELG 151
Cdd:cd01161    1 SFALNMFLGDIVTKQVFPYPSVLTEEQTEELNMLVGPVEKFFEEVNDPAKNDQLEKIPRKTLTQLKELGLFGLQVPEEYG 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767992071 152 GVGLCNTQYARLVEIVGMhDLGVGITLGAHQSIGFKGILLFGTKAQKEKYLPKLASGETVAAFCLTEPSSGSDAASIRTS 231
Cdd:cd01161   81 GLGLNNTQYARLAEIVGM-DLGFSVTLGAHQSIGFKGILLFGTEAQKEKYLPKLASGEWIAAFALTEPSSGSDAASIRTT 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767992071 232 AVPSPCGKYYTLNGSKLWISNGGLADIFTVFAKTPVTDPaTGAVKEKITAFVVERGFGGITHGPPEKKMGIKASNTAEVF 311
Cdd:cd01161  160 AVLSEDGKHYVLNGSKIWITNGGIADIFTVFAKTEVKDA-TGSVKDKITAFIVERSFGGVTNGPPEKKMGIKGSNTAEVY 238
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767992071 312 FDGVRVPSENVLGEVGSGFKVAMHILNNGRFGMAAALAGTMRGIIAKAVDHATNRTQFGEKIHNFGLIQEKLARMVMLQY 391
Cdd:cd01161  239 FEDVKIPVENVLGEVGDGFKVAMNILNNGRFGMGAALIGTMKRCIEKAVDYANNRKQFGKKIHEFGLIQEKLANMAILQY 318
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767992071 392 VTESMAYMVSANMDQGAT-DFQIEAAISKIFGSEAAWKVTDECIQIMGGMGFMKEPGVERVLRDLRIFRIFEGTNDILRL 470
Cdd:cd01161  319 ATESMAYMTSGNMDRGLKaEYQIEAAISKVFASEAAWLVVDEAIQIHGGMGFMREYGVERVLRDLRIFRIFEGTNEILRL 398

                 ....*...
gi 767992071 471 FVALQGCM 478
Cdd:cd01161  399 FIALTGLQ 406
CaiA COG1960
Acyl-CoA dehydrogenase related to the alkylation response protein AidB [Lipid transport and ...
102-473 2.58e-108

Acyl-CoA dehydrogenase related to the alkylation response protein AidB [Lipid transport and metabolism];


Pssm-ID: 224871 [Multi-domain]  Cd Length: 393  Bit Score: 331.77  E-value: 2.58e-108
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767992071 102 LKELVEPVSRFFEEVNDPAKNDALEMVEETT-----WQGLKELGAFGLQVPSELGGVGLCNTQYARLVEIVGMHDLGVGI 176
Cdd:COG1960    9 QEALRAEVREFAEEELAPEAAEIDRRIEDERfprelLRALAEAGLLGLTIPEEYGGLGLSPLEQAAVLEELARADAGGAL 88
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767992071 177 TLGAHQSIGF---KGILLFGTKAQKEKYLPKLASGETVAAFCLTEPSSGSDAASIRTSAVPSPCGKYYtLNGSKLWISNG 253
Cdd:COG1960   89 ALGLTHGGLGalaPTILRFGTEEQKRRYLPRLASGELIGAFALTEPGAGSDLASLRTTAAVRDDGDYV-LNGQKIWISNA 167
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767992071 254 GLADIFTVFAKTpvtDPATGAVKEkITAFVVERGFG-GITHGPPEKKMGIKASNTAEVFFDGVRVPSENVLGEVGSGFKV 332
Cdd:COG1960  168 PVADWLLVLART---DPAPGKHKG-ISLFLVPKDLTpGVSVGPILKKMGLRGSATGEVFFDDVRVPAENLLGEEGDGFKI 243
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767992071 333 AMHILNNGRFGMAAALAGTMRGIIAKAVDHATNRTQFGEKIHNFGLIQEKLARMVMLQYVTESMAYMVSANMDQGAtDFQ 412
Cdd:COG1960  244 AMETLNVERLGIAAQALGIAEAALEEAVAYARERKQFGRPIADFQLVQFKLADMAAELEAARLLVLRAAELADAGD-DAG 322
                        330       340       350       360       370       380
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 767992071 413 IEAAISKIFGSEAAWKVTDECIQIMGGMGFMKEPGVERVLRDLRIFRIFEGTNDILRLFVA 473
Cdd:COG1960  323 AEAAMAKLFATEAALEVADEAVQVHGGYGYTEEYPVERYYRDARILRIYEGTSEIQRLIIA 383
PLN02519 PLN02519
isovaleryl-CoA dehydrogenase
96-472 6.60e-66

isovaleryl-CoA dehydrogenase


Pssm-ID: 215284 [Multi-domain]  Cd Length: 404  Bit Score: 221.67  E-value: 6.60e-66
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767992071  96 EEQTQFLKELVEPVSRFFEEVNDPAKNDALemveettWQGLKELGAFGLQVPSELGGVGLCNTQYARLVEIVGMHDLGVG 175
Cdd:PLN02519  35 ESVQQFAQENIAPHAAAIDATNSFPKDVNL-------WKLMGDFNLHGITAPEEYGGLGLGYLYHCIAMEEISRASGSVG 107
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767992071 176 ITLGAHQSIGFKGILLFGTKAQKEKYLPKLASGETVAAFCLTEPSSGSDAASIRTSAVPSPCGkyYTLNGSKLWISNGGL 255
Cdd:PLN02519 108 LSYGAHSNLCINQLVRNGTPAQKEKYLPKLISGEHVGALAMSEPNSGSDVVSMKCKAERVDGG--YVLNGNKMWCTNGPV 185
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767992071 256 ADIFTVFAKTpvtDPATGAvkEKITAFVVERGFGGITHGPPEKKMGIKASNTAEVFFDGVRVPSENVLGEVGSGFKVAMH 335
Cdd:PLN02519 186 AQTLVVYAKT---DVAAGS--KGITAFIIEKGMPGFSTAQKLDKLGMRGSDTCELVFENCFVPEENVLGQEGKGVYVMMS 260
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767992071 336 ILNNGRFGMAAALAGTMRGIIAKAVDHATNRTQFGEKIHNFGLIQEKLARMVMLQYVTESMAYMVSANMDQGATDFQiEA 415
Cdd:PLN02519 261 GLDLERLVLAAGPLGLMQACLDVVLPYVRQREQFGRPIGEFQFIQGKLADMYTSLQSSRSYVYSVARDCDNGKVDRK-DC 339
                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 767992071 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 2.85e-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: 143.93  E-value: 2.85e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767992071  327 GSGFKVAMHILNNGRFGMAAALAGTMRGIIAKAVDHATNRTQFGEKIHNFGLIQEKLARMVMLQYVTESMAYMVSANMDQ 406
Cdd:pfam00441   1 GRGFRVAMETLNHERLAIAAMALGLARRALDEALAYARRRKAFGRPLIDFQLVRHKLAEMAAEIEAARLLVYRAAEALDA 80
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 767992071  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 ...
72-478 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: 751.22  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767992071  72 SFAVGMFKGQLTTDQVFPYPSVLNEEQTQFLKELVEPVSRFFEEVNDPAKNDALEMVEETTWQGLKELGAFGLQVPSELG 151
Cdd:cd01161    1 SFALNMFLGDIVTKQVFPYPSVLTEEQTEELNMLVGPVEKFFEEVNDPAKNDQLEKIPRKTLTQLKELGLFGLQVPEEYG 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767992071 152 GVGLCNTQYARLVEIVGMhDLGVGITLGAHQSIGFKGILLFGTKAQKEKYLPKLASGETVAAFCLTEPSSGSDAASIRTS 231
Cdd:cd01161   81 GLGLNNTQYARLAEIVGM-DLGFSVTLGAHQSIGFKGILLFGTEAQKEKYLPKLASGEWIAAFALTEPSSGSDAASIRTT 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767992071 232 AVPSPCGKYYTLNGSKLWISNGGLADIFTVFAKTPVTDPaTGAVKEKITAFVVERGFGGITHGPPEKKMGIKASNTAEVF 311
Cdd:cd01161  160 AVLSEDGKHYVLNGSKIWITNGGIADIFTVFAKTEVKDA-TGSVKDKITAFIVERSFGGVTNGPPEKKMGIKGSNTAEVY 238
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767992071 312 FDGVRVPSENVLGEVGSGFKVAMHILNNGRFGMAAALAGTMRGIIAKAVDHATNRTQFGEKIHNFGLIQEKLARMVMLQY 391
Cdd:cd01161  239 FEDVKIPVENVLGEVGDGFKVAMNILNNGRFGMGAALIGTMKRCIEKAVDYANNRKQFGKKIHEFGLIQEKLANMAILQY 318
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767992071 392 VTESMAYMVSANMDQGAT-DFQIEAAISKIFGSEAAWKVTDECIQIMGGMGFMKEPGVERVLRDLRIFRIFEGTNDILRL 470
Cdd:cd01161  319 ATESMAYMTSGNMDRGLKaEYQIEAAISKVFASEAAWLVVDEAIQIHGGMGFMREYGVERVLRDLRIFRIFEGTNEILRL 398

                 ....*...
gi 767992071 471 FVALQGCM 478
Cdd:cd01161  399 FIALTGLQ 406
SCAD_SBCAD cd01158
Short chain acyl-CoA dehydrogenases and eukaryotic short/branched chain acyl-CoA ...
96-473 3.93e-121

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: 363.90  E-value: 3.93e-121
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767992071  96 EEQTQFLKElvepVSRFFEEVNDP--AKNDALEMVEETTWQGLKELGAFGLQVPSELGGVGLCNTQYARLVEIVGMHDLG 173
Cdd:cd01158    1 EEHQMIRKT----VRDFAEKEIAPlaAEMDEKGEFPREVIKEMAELGLMGIPIPEEYGGAGLDFLAYAIAIEELAKVDAS 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767992071 174 VGITLGAHQSIGFKGILLFGTKAQKEKYLPKLASGETVAAFCLTEPSSGSDAASIRTSAVPSpcGKYYTLNGSKLWISNG 253
Cdd:cd01158   77 VAVIVSVHNSLGANPIIKFGTEEQKKKYLPPLATGEKIGAFALSEPGAGSDAAALKTTAKKD--GDDYVLNGSKMWITNG 154
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767992071 254 GLADIFTVFAktpVTDPATGavKEKITAFVVERGFGGITHGPPEKKMGIKASNTAEVFFDGVRVPSENVLGEVGSGFKVA 333
Cdd:cd01158  155 GEADFYIVFA---VTDPSKG--YRGITAFIVERDTPGLSVGKKEDKLGIRGSSTTELIFEDVRVPKENILGEEGEGFKIA 229
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767992071 334 MHILNNGRFGMAAALAGTMRGIIAKAVDHATNRTQFGEKIHNFGLIQEKLARMVMLQYVTESMAYMVSANMDQGaTDFQI 413
Cdd:cd01158  230 MQTLDGGRIGIAAQALGIAQAALDAAVDYAKERKQFGKPIADFQGIQFKLADMATEIEAARLLTYKAARLKDNG-EPFIK 308
                        330       340       350       360       370       380
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 767992071 414 EAAISKIFGSEAAWKVTDECIQIMGGMGFMKEPGVERVLRDLRIFRIFEGTNDILRLFVA 473
Cdd:cd01158  309 EAAMAKLFASEVAMRVTTDAVQIFGGYGYTKDYPVERYYRDAKITEIYEGTSEIQRLVIA 368
CaiA COG1960
Acyl-CoA dehydrogenase related to the alkylation response protein AidB [Lipid transport and ...
102-473 2.58e-108

Acyl-CoA dehydrogenase related to the alkylation response protein AidB [Lipid transport and metabolism];


Pssm-ID: 224871 [Multi-domain]  Cd Length: 393  Bit Score: 331.77  E-value: 2.58e-108
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767992071 102 LKELVEPVSRFFEEVNDPAKNDALEMVEETT-----WQGLKELGAFGLQVPSELGGVGLCNTQYARLVEIVGMHDLGVGI 176
Cdd:COG1960    9 QEALRAEVREFAEEELAPEAAEIDRRIEDERfprelLRALAEAGLLGLTIPEEYGGLGLSPLEQAAVLEELARADAGGAL 88
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767992071 177 TLGAHQSIGF---KGILLFGTKAQKEKYLPKLASGETVAAFCLTEPSSGSDAASIRTSAVPSPCGKYYtLNGSKLWISNG 253
Cdd:COG1960   89 ALGLTHGGLGalaPTILRFGTEEQKRRYLPRLASGELIGAFALTEPGAGSDLASLRTTAAVRDDGDYV-LNGQKIWISNA 167
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767992071 254 GLADIFTVFAKTpvtDPATGAVKEkITAFVVERGFG-GITHGPPEKKMGIKASNTAEVFFDGVRVPSENVLGEVGSGFKV 332
Cdd:COG1960  168 PVADWLLVLART---DPAPGKHKG-ISLFLVPKDLTpGVSVGPILKKMGLRGSATGEVFFDDVRVPAENLLGEEGDGFKI 243
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767992071 333 AMHILNNGRFGMAAALAGTMRGIIAKAVDHATNRTQFGEKIHNFGLIQEKLARMVMLQYVTESMAYMVSANMDQGAtDFQ 412
Cdd:COG1960  244 AMETLNVERLGIAAQALGIAEAALEEAVAYARERKQFGRPIADFQLVQFKLADMAAELEAARLLVLRAAELADAGD-DAG 322
                        330       340       350       360       370       380
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 767992071 413 IEAAISKIFGSEAAWKVTDECIQIMGGMGFMKEPGVERVLRDLRIFRIFEGTNDILRLFVA 473
Cdd:COG1960  323 AEAAMAKLFATEAALEVADEAVQVHGGYGYTEEYPVERYYRDARILRIYEGTSEIQRLIIA 383
ACAD cd00567
Acyl-CoA dehydrogenase; Both mitochondrial acyl-CoA dehydrogenases (ACAD) and peroxisomal ...
96-473 4.56e-104

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: 318.46  E-value: 4.56e-104
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767992071  96 EEQtqflKELVEPVSRFFEEVNDPAKNDAlEMVEETTWQGLKELGafglqvpsELGGVGLcntqyarlveivgmhdlgvg 175
Cdd:cd00567    1 EEQ----RELRDSAREFAAEELEPYARER-RETPEEPWELLAELG--------LLLGAAL-------------------- 47
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767992071 176 itlgahqsigfkgILLFGTKAQKEKYLPKLASGETVAAFCLTEPSSGSDAASIRTSAVPSpcGKYYTLNGSKLWISNGGL 255
Cdd:cd00567   48 -------------LLAYGTEEQKERYLPPLASGEAIAAFALTEPGAGSDLAGIRTTARKD--GDGYVLNGRKIFISNGGD 112
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767992071 256 ADIFTVFAKTPVTDPATGAvkekITAFVVERGFGGITHGPPEKKMGIKASNTAEVFFDGVRVPSENVLGEVGSGFKVAMH 335
Cdd:cd00567  113 ADLFIVLARTDEEGPGHRG----ISAFLVPADTPGVTVGRIWDKMGMRGSGTGELVFDDVRVPEDNLLGEEGGGFELAMK 188
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767992071 336 ILNNGRFGMAAALAGTMRGIIAKAVDHATNRTQFGEKIHNFGLIQEKLARMVMLQYVTESMAYMVSANMDQGATDFQIEA 415
Cdd:cd00567  189 GLNVGRLLLAAVALGAARAALDEAVEYAKQRKQFGKPLAEFQAVQFKLADMAAELEAARLLLYRAAWLLDQGPDEARLEA 268
                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 767992071 416 AISKIFGSEAAWKVTDECIQIMGGMGFMKEPGVERVLRDLRIFRIFEGTNDILRLFVA 473
Cdd:cd00567  269 AMAKLFATEAAREVADLAMQIHGGRGYSREYPVERYLRDARAARIAEGTAEIQRLIIA 326
IVD cd01156
Isovaleryl-CoA dehydrogenase; Isovaleryl-CoA dehydrogenase (IVD) is an is an acyl-CoA ...
94-473 1.74e-91

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: 287.77  E-value: 1.74e-91
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767992071  94 LNEEQTQflkeLVEPVSRFFEEVNDP--AKNDALEMVEETTWQGLKELGAFGLQVPSELGGVGLCNTQYARLVEIVGMHD 171
Cdd:cd01156    2 LDDEIEM----LRQSVREFAQKEIAPlaAKIDRDNEFPRDLWRKMGKLGLLGITAPEEYGGSGMGYLAHVIIMEEISRAS 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767992071 172 LGVGITLGAHQSIGFKGILLFGTKAQKEKYLPKLASGETVAAFCLTEPSSGSDAASIRTSAvpSPCGKYYTLNGSKLWIS 251
Cdd:cd01156   78 GSVALSYGAHSNLCINQIYRNGSAAQKEKYLPKLISGEHIGALAMSEPNAGSDVVSMKLRA--EKKGDRYVLNGSKMWIT 155
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767992071 252 NGGLADIFTVFAKTpvtDPATGAvkEKITAFVVERGFGGITHGPPEKKMGIKASNTAEVFFDGVRVPSENVLGEVGSGFK 331
Cdd:cd01156  156 NGPDADTLVVYAKT---DPSAGA--HGITAFIVEKGMPGFSRAQKLDKLGMRGSNTCELVFEDCEVPEENILGGENKGVY 230
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767992071 332 VAMHILNNGRFGMAAALAGTMRGIIAKAVDHATNRTQFGEKIHNFGLIQEKLARMVMLQYVTESMAYMVSANMDQGATDf 411
Cdd:cd01156  231 VLMSGLDYERLVLAGGPIGIMQAALDVAIPYAHQRKQFGQPIGEFQLVQGKLADMYTRLNASRSYLYTVAKACDRGNMD- 309
                        330       340       350       360       370       380
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 767992071 412 QIEAAISKIFGSEAAWKVTDECIQIMGGMGFMKEPGVERVLRDLRIFRIFEGTNDILRLFVA 473
Cdd:cd01156  310 PKDAAGVILYAAEKATQVALDAIQILGGNGYINDYPTGRLLRDAKLYEIGAGTSEIRRMVIG 371
IBD cd01162
Isobutyryl-CoA dehydrogenase; Isobutyryl-CoA dehydrogenase (IBD) catalyzes the alpha, beta- ...
138-473 1.99e-78

Isobutyryl-CoA dehydrogenase; Isobutyryl-CoA dehydrogenase (IBD) catalyzes the alpha, beta- dehydrogenation of short branched chain acyl-CoA intermediates in valine catabolism. It is predicted to be a homotetramer.


Pssm-ID: 173851 [Multi-domain]  Cd Length: 375  Bit Score: 253.52  E-value: 1.99e-78
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767992071 138 ELGAFGLQVPSELGGVGLCNTQYARLVEIVGMHDLGVGITLGAHQSIGFKgILLFGTKAQKEKYLPKLASGETVAAFCLT 217
Cdd:cd01162   43 ELGFGGIYIRDDVGGSGLSRLDASIIFEALSTGCVSTAAYISIHNMCAWM-IDSFGNDEQRERFLPDLCTMEKLASYCLT 121
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767992071 218 EPSSGSDAASIRTSAVPSpcGKYYTLNGSKLWISNGGLADIFTVFAKTpvtdpaTGAVKEKITAFVVERGFGGITHGPPE 297
Cdd:cd01162  122 EPGSGSDAAALRTRAVRE--GDHYVLNGSKAFISGAGDSDVYVVMART------GGEGPKGISCFVVEKGTPGLSFGANE 193
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767992071 298 KKMGIKASNTAEVFFDGVRVPSENVLGEVGSGFKVAMHILNNGRFGMAAALAGTMRGIIAKAVDHATNRTQFGEKIHNFG 377
Cdd:cd01162  194 KKMGWNAQPTRAVIFEDCRVPVENRLGGEGQGFGIAMAGLNGGRLNIASCSLGAAQAALDLARAYLEERKQFGKPLADFQ 273
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767992071 378 LIQEKLARMVMLQYVTESMAYMVSANMDQGATDFQIEAAISKIFGSEAAWKVTDECIQIMGGMGFMKEPGVERVLRDLRI 457
Cdd:cd01162  274 ALQFKLADMATELVASRLMVRRAASALDRGDPDAVKLCAMAKRFATDECFDVANQALQLHGGYGYLKDYPVEQYVRDLRV 353
                        330
                 ....*....|....*.
gi 767992071 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 4.85e-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: 4.85e-74
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767992071 109 VSRFFEEVNDP--AKNDALEMVEETTWQGLKELGAFGLQVPSELGGVGLcNTQYARLVEIVGMHDLGVGITLGAHQSIGF 186
Cdd:cd01160   10 VRRFFAKEVAPfhHEWEKAGEVPREVWRKAGEQGLLGVGFPEEYGGIGG-DLLSAAVLWEELARAGGSGPGLSLHTDIVS 88
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767992071 187 KGILLFGTKAQKEKYLPKLASGETVAAFCLTEPSSGSDAASIRTSAVPSpcGKYYTLNGSKLWISNGGLADIFTVFAKTp 266
Cdd:cd01160   89 PYITRAGSPEQKERVLPQMVAGKKIGAIAMTEPGAGSDLQGIRTTARKD--GDHYVLNGSKTFITNGMLADVVIVVART- 165
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767992071 267 vTDPATGAvkEKITAFVVERGFGGITHGPPEKKMGIKASNTAEVFFDGVRVPSENVLGEVGSGFKVAMHILNNGRFGMAA 346
Cdd:cd01160  166 -GGEARGA--GGISLFLVERGTPGFSRGRKLKKMGWKAQDTAELFFDDCRVPAENLLGEENKGFYYLMQNLPQERLLIAA 242
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767992071 347 ALAGTMRGIIAKAVDHATNRTQFGEKIHNFGLIQEKLARMVMLQYVTESMAYMVSANMDQGATDfQIEAAISKIFGSEAA 426
Cdd:cd01160  243 GALAAAEFMLEETRNYVKQRKAFGKTLAQLQVVRHKIAELATKVAVTRAFLDNCAWRHEQGRLD-VAEASMAKYWATELQ 321
                        330       340       350       360
                 ....*....|....*....|....*....|....*....|....*....
gi 767992071 427 WKVTDECIQIMGGMGFMKEPGVERVLRDLRIFRIFEGTNDILRLFVALQ 475
Cdd:cd01160  322 NRVAYECVQLHGGWGYMREYPIARAYRDARVQPIYGGTTEIMKELISRQ 370
PLN02519 PLN02519
isovaleryl-CoA dehydrogenase
96-472 6.60e-66

isovaleryl-CoA dehydrogenase


Pssm-ID: 215284 [Multi-domain]  Cd Length: 404  Bit Score: 221.67  E-value: 6.60e-66
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767992071  96 EEQTQFLKELVEPVSRFFEEVNDPAKNDALemveettWQGLKELGAFGLQVPSELGGVGLCNTQYARLVEIVGMHDLGVG 175
Cdd:PLN02519  35 ESVQQFAQENIAPHAAAIDATNSFPKDVNL-------WKLMGDFNLHGITAPEEYGGLGLGYLYHCIAMEEISRASGSVG 107
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767992071 176 ITLGAHQSIGFKGILLFGTKAQKEKYLPKLASGETVAAFCLTEPSSGSDAASIRTSAVPSPCGkyYTLNGSKLWISNGGL 255
Cdd:PLN02519 108 LSYGAHSNLCINQLVRNGTPAQKEKYLPKLISGEHVGALAMSEPNSGSDVVSMKCKAERVDGG--YVLNGNKMWCTNGPV 185
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767992071 256 ADIFTVFAKTpvtDPATGAvkEKITAFVVERGFGGITHGPPEKKMGIKASNTAEVFFDGVRVPSENVLGEVGSGFKVAMH 335
Cdd:PLN02519 186 AQTLVVYAKT---DVAAGS--KGITAFIIEKGMPGFSTAQKLDKLGMRGSDTCELVFENCFVPEENVLGQEGKGVYVMMS 260
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767992071 336 ILNNGRFGMAAALAGTMRGIIAKAVDHATNRTQFGEKIHNFGLIQEKLARMVMLQYVTESMAYMVSANMDQGATDFQiEA 415
Cdd:PLN02519 261 GLDLERLVLAAGPLGLMQACLDVVLPYVRQREQFGRPIGEFQFIQGKLADMYTSLQSSRSYVYSVARDCDNGKVDRK-DC 339
                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 767992071 416 AISKIFGSEAAWKVTDECIQIMGGMGFMKEPGVERVLRDLRIFRIFEGTNDILRLFV 472
Cdd:PLN02519 340 AGVILCAAERATQVALQAIQCLGGNGYINEYPTGRLLRDAKLYEIGAGTSEIRRMLI 396
GCD cd01151
Glutaryl-CoA dehydrogenase; Glutaryl-CoA dehydrogenase (GCD). GCD is an acyl-CoA dehydrogenase, ...
78-482 2.87e-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: 216.46  E-value: 2.87e-64
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767992071  78 FKGQLTTDQVfpypsVLNEEQTQFLKELVEP--VSRFFEEVNDPakndalEMVEEttwqgLKELGAFGLQvPSELGGVGL 155
Cdd:cd01151    9 LDDLLTEEER-----AIRDTAREFCQEELAPrvLEAYREEKFDR------KIIEE-----MGELGLLGAT-IKGYGCAGL 71
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767992071 156 CNTQY---ARLVEIVgmhDLGVGITLGAHQSIGFKGILLFGTKAQKEKYLPKLASGETVAAFCLTEPSSGSDAASIRTSA 232
Cdd:cd01151   72 SSVAYgliAREVERV---DSGYRSFMSVQSSLVMLPIYDFGSEEQKQKYLPKLASGELIGCFGLTEPNHGSDPGGMETRA 148
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767992071 233 vpSPCGKYYTLNGSKLWISNGGLADIFTVFAKTPVTDpatgavkeKITAFVVERGFGGITHGPPEKKMGIKASNTAEVFF 312
Cdd:cd01151  149 --RKDGGGYKLNGSKTWITNSPIADVFVVWARNDETG--------KIRGFILERGMKGLSAPKIQGKFSLRASITGEIVM 218
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767992071 313 DGVRVPSENVLGEVgSGFKVAMHILNNGRFGMAAALAGTMRGIIAKAVDHATNRTQFGEKIHNFGLIQEKLARM-VMLQY 391
Cdd:cd01151  219 DNVFVPEENLLPGA-EGLRGPFKCLNNARYGIAWGALGAAEDCYHTARQYVLDRKQFGRPLAAFQLVQKKLADMlTEIAL 297
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767992071 392 VTEsMAYMVSANMDQG-ATDFQIeaAISKIFGSEAAWKVTDECIQIMGGMGFMKEPGVERVLRDLRIFRIFEGTNDILRL 470
Cdd:cd01151  298 GLL-ACLRVGRLKDQGkATPEQI--SLLKRNNCGKALEIARTAREMLGGNGISDEYHIIRHMVNLESVNTYEGTHDIHAL 374
                        410
                 ....*....|..
gi 767992071 471 fvalqgcMAGRA 482
Cdd:cd01151  375 -------ILGRA 379
MCAD cd01157
Medium chain acyl-CoA dehydrogenase; MCADs are mitochondrial beta-oxidation enzymes, which ...
94-473 1.41e-63

Medium chain acyl-CoA dehydrogenase; MCADs are mitochondrial beta-oxidation enzymes, which catalyze the alpha,beta dehydrogenation of the corresponding medium chain acyl-CoA by FAD, which becomes reduced. The reduced form of MCAD is reoxidized in the oxidative half-reaction by electron-transferring flavoprotein (ETF), from which the electrons are transferred to the mitochondrial respiratory chain coupled with ATP synthesis. MCAD is a homotetramer.


Pssm-ID: 173846 [Multi-domain]  Cd Length: 378  Bit Score: 214.37  E-value: 1.41e-63
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767992071  94 LNEEQtqflKELVEPVSRFFEEVNDPAKNDaLEMVEETTWQGLK---ELGAFGLQVPSELGGVGLCNTQYARLVEIVGMH 170
Cdd:cd01157    1 LTEQQ----KEFQETARKFAREEIIPVAAE-YDKSGEYPWPLIKrawELGLMNTHIPEDCGGLGLGTFDTCLITEELAYG 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767992071 171 DLGVGITLGAHqSIGFKGILLFGTKAQKEKYLPKLASGETVAAFCLTEPSSGSDAASIRTSAVPSpcGKYYTLNGSKLWI 250
Cdd:cd01157   76 CTGVQTAIEAN-SLGQMPVIISGNDEQKKKYLGRMTEEPLMCAYCVTEPGAGSDVAGIKTKAEKK--GDEYIINGQKMWI 152
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767992071 251 SNGGLADIFTVFAKTPvTDPATGAVKeKITAFVVERGFGGITHGPPEKKMGIKASNTAEVFFDGVRVPSENVLGEVGSGF 330
Cdd:cd01157  153 TNGGKANWYFLLARSD-PDPKCPASK-AFTGFIVEADTPGIQPGRKELNMGQRCSDTRGITFEDVRVPKENVLIGEGAGF 230
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767992071 331 KVAMHILNNGRFGMAAALAGTMRGIIAKAVDHATNRTQFGEKIHNFGLIQEKLARMVMlQYVTESMAYMVSAN-MDQGAT 409
Cdd:cd01157  231 KIAMGAFDKTRPPVAAGAVGLAQRALDEATKYALERKTFGKLIAEHQAVSFMLADMAM-KVELARLAYQRAAWeVDSGRR 309
                        330       340       350       360       370       380
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 767992071 410 DfQIEAAISKIFGSEAAWKVTDECIQIMGGMGFMKEPGVERVLRDLRIFRIFEGTNDILRLFVA 473
Cdd:cd01157  310 N-TYYASIAKAFAADIANQLATDAVQIFGGNGFNSEYPVEKLMRDAKIYQIYEGTSQIQRLIIS 372
PTZ00461 PTZ00461
isovaleryl-CoA dehydrogenase; Provisional
103-464 2.84e-63

isovaleryl-CoA dehydrogenase; Provisional


Pssm-ID: 185640 [Multi-domain]  Cd Length: 410  Bit Score: 214.80  E-value: 2.84e-63
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767992071 103 KELVEPVSRFFEEVNDP-AKNDALEM-VEETTWQGLKELGAFGLQVPSELGGVGLCNTQYARLVEIVGMHDLGVGITLGA 180
Cdd:PTZ00461  42 AALRETVAKFSREVVDKhAREDDINMhFNRDLFKQLGDLGVMGVTVPEADGGAGMDAVAAVIIHHELSKYDPGFCLAYLA 121
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767992071 181 HQSIGFKGILLFGTKAQKEKYLPKLASGETVAAFCLTEPSSGSDAASIRTSAVPSPCGKYyTLNGSKLWISNGGLADIFT 260
Cdd:PTZ00461 122 HSMLFVNNFYYSASPAQRARWLPKVLTGEHVGAMGMSEPGAGTDVLGMRTTAKKDSNGNY-VLNGSKIWITNGTVADVFL 200
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767992071 261 VFAKtpvtdpatgaVKEKITAFVVERGFGGITHGPPEKKMGIKASNTAEVFFDGVRVPSENVLGEVGSGFKVAMHILNNG 340
Cdd:PTZ00461 201 IYAK----------VDGKITAFVVERGTKGFTQGPKIDKCGMRASHMCQLFFEDVVVPAENLLGEEGKGMVGMMRNLELE 270
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767992071 341 RFGMAAALAGTMRGIIAKAVDHATNRTQFGEKIHNFGLIQEKLARMVMLQYVTESMAYMVSANMDQGATDfQIEAAISKI 420
Cdd:PTZ00461 271 RVTLAAMAVGIAERSVELMTSYASERKAFGKPISNFGQIQRYIAEGYADTEAAKALVYSVSHNVHPGNKN-RLGSDAAKL 349
                        330       340       350       360
                 ....*....|....*....|....*....|....*....|....
gi 767992071 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 9.37e-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: 189.14  E-value: 9.37e-54
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767992071 138 ELGAFGLQVPSELGGVGLCNTQYARLVEIVGMHDLGVGITLGAHQsiGFKGILLFGTKAQKEKYLPKLASGETVAAFCLT 217
Cdd:cd01153   47 EAGWMALGVPEEYGGQGLPITVYSALAEIFSRGDAPLMYASGTQG--AAATLLAHGTEAQREKWIPRLAEGEWTGTMCLT 124
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767992071 218 EPSSGSDAASIRTSAVPSPCGKYYtLNGSKLWISNG--GLAD--IFTVFAKTPvtDPATGAvkEKITAFVV-------ER 286
Cdd:cd01153  125 EPDAGSDLGALRTKAVYQADGSWR-INGVKRFISAGehDMSEniVHLVLARSE--GAPPGV--KGLSLFLVpkflddgER 199
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767992071 287 GfgGITHGPPEKKMGIKASNTAEVFFDGVRVPsenVLGEVGSGFKVAMHILNNGRFGMAAALAGTMRGIIAKAVDHATNR 366
Cdd:cd01153  200 N--GVTVARIEEKMGLHGSPTCELVFDNAKGE---LIGEEGMGLAQMFAMMNGARLGVGTQGTGLAEAAYLNALAYAKER 274
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767992071 367 TQFGEKIHNFGLIQEKLARMVMLQYVTESMAYMVSANMD-----------QGATDFQIEAA----------ISKIFGSEA 425
Cdd:cd01153  275 KQGGDLIKAAPAVTIIHHPDVRRSLMTQKAYAEGSRALDlytatvqdlaeRKATEGEDRKAlsaladlltpVVKGFGSEA 354
                        330       340       350       360
                 ....*....|....*....|....*....|....*....|..
gi 767992071 426 AWKVTDECIQIMGGMGFMKEPGVERVLRDLRIFRIFEGTNDI 467
Cdd:cd01153  355 ALEAVSDAIQVHGGSGYTREYPIEQYYRDARITTIYEGTTGI 396
PRK12341 PRK12341
acyl-CoA dehydrogenase;
94-468 4.75e-50

acyl-CoA dehydrogenase;


Pssm-ID: 183454 [Multi-domain]  Cd Length: 381  Bit Score: 178.00  E-value: 4.75e-50
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767992071  94 LNEEQTQFLKELVEPVSRFFEEvNDPAKNDALEMVEETTWQGLKELGAFGLQVPSELGGVGLCNTQYARLVEivGMHDLG 173
Cdd:PRK12341   5 LTEEQELLLASIRELITRNFPE-EYFRTCDENGTYPREFMRALADNGISMLGVPEEFGGTPADYVTQMLVLE--EVSKCG 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767992071 174 VGITLgAHQSIGFKGILLFGTKAQKEKYLpKLASGETVAAFCL--TEPSSGSDAASIRTSAVPSPcGKYYtLNGSKLWIS 251
Cdd:PRK12341  82 APAFL-ITNGQCIHSMRRFGSAEQLRKTA-ESTLETGDPAYALalTEPGAGSDNNSATTTYTRKN-GKVY-LNGQKTFIT 157
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767992071 252 NGGLADIFTVFAKtpvtDPATGAVKEKITAFVVERGFGGITHGPPEKkMGIKASNTAEVFFDGVRVPSENVLGEVGSGFK 331
Cdd:PRK12341 158 GAKEYPYMLVLAR----DPQPKDPKKAFTLWWVDSSKPGIKINPLHK-IGWHMLSTCEVYLDNVEVEESDLVGEEGMGFL 232
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767992071 332 VAMHILNNGRFGMAAALAGTMRGIIAKAVDHATNRTQFGEKIHNFGLIQEKLARMVMLQYVTESMAYMVSANMDQGATdF 411
Cdd:PRK12341 233 NVMYNFEMERLINAARSLGFAECAFEDAARYANQRIQFGKPIGHNQLIQEKLTLMAIKIENMRNMVYKVAWQADNGQS-L 311
                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 767992071 412 QIEAAISKIFGSEAAWKVTDECIQIMGGMGFMKEPGVERVLRDLRIFRIFEGTNDIL 468
Cdd:PRK12341 312 RTSAALAKLYCARTAMEVIDDAIQIMGGLGYTDEARVSRFWRDVRCERIGGGTDEIM 368
PRK03354 PRK03354
crotonobetainyl-CoA dehydrogenase; Validated
134-470 3.21e-42

crotonobetainyl-CoA dehydrogenase; Validated


Pssm-ID: 179566 [Multi-domain]  Cd Length: 380  Bit Score: 156.53  E-value: 3.21e-42
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767992071 134 QGLKELGAFGLQVPSELGGVGLCNTQYARLVEIVGMhdLGVGITLGAHQSIGFKGILLFGTKAQKEKYLPKLASGETVAA 213
Cdd:PRK03354  44 KALADMGIDSLLIPEEHGGLDAGFVTLAAVWMELGR--LGAPTYVLYQLPGGFNTFLREGTQEQIDKIMAFRGTGKQMWN 121
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767992071 214 FCLTEPSSGSDAASIRTSAVPSPcGKYYtLNGSKLWISNGGLADIFTVFAKTPVTDPatgavKEKITAFVVERGFGGITH 293
Cdd:PRK03354 122 SAITEPGAGSDVGSLKTTYTRRN-GKVY-LNGSKCFITSSAYTPYIVVMARDGASPD-----KPVYTEWFVDMSKPGIKV 194
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767992071 294 GPPEKkMGIKASNTAEVFFDGVRVPSENVLGEVGSGFKVAMHILNNGRFGMAAALAGTMRGIIAKAVDHATNRTQFGEKI 373
Cdd:PRK03354 195 TKLEK-LGLRMDSCCEITFDDVELDEKDMFGREGNGFNRVKEEFDHERFLVALTNYGTAMCAFEDAARYANQRVQFGEAI 273
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767992071 374 HNFGLIQEKLARMVMLQYVTESMAYMVSANMDQGATDfQIEAAISKIFGSEAAWKVTDECIQIMGGMGFMKEPGVERVLR 453
Cdd:PRK03354 274 GRFQLIQEKFAHMAIKLNSMKNMLYEAAWKADNGTIT-SGDAAMCKYFCANAAFEVVDSAMQVLGGVGIAGNHRISRFWR 352
                        330
                 ....*....|....*..
gi 767992071 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 2.85e-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: 143.93  E-value: 2.85e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767992071  327 GSGFKVAMHILNNGRFGMAAALAGTMRGIIAKAVDHATNRTQFGEKIHNFGLIQEKLARMVMLQYVTESMAYMVSANMDQ 406
Cdd:pfam00441   1 GRGFRVAMETLNHERLAIAAMALGLARRALDEALAYARRRKAFGRPLIDFQLVRHKLAEMAAEIEAARLLVYRAAEALDA 80
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 767992071  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 9.93e-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: 144.03  E-value: 9.93e-38
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767992071 132 TWQG-LKELGAFGLQVPSELGGVGLCNTQYARLVE---IVGM--HDLGVGITLGAHQsigfkgILLFGTKAQKEKYLPKL 205
Cdd:cd01152   39 RWQRaLAAAGWAAPGWPKEYGGRGASLMEQLIFREemaAAGApvPFNQIGIDLAGPT------ILAYGTDEQKRRFLPPI 112
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767992071 206 ASGETVaaFCL--TEPSSGSDAASIRTSAVPSpcGKYYTLNGSKLWISNGGLADIFTVFAKTpvtDPAtgAVKEK-ITAF 282
Cdd:cd01152  113 LSGEEI--WCQgfSEPGAGSDLAGLRTRAVRD--GDDWVVNGQKIWTSGAHYADWAWLLVRT---DPE--APKHRgISIL 183
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767992071 283 VVERGFGGITHGPPEKKMGikASNTAEVFFDGVRVPSENVLGEVGSGFKVAMHILNNGRFGMAAALAGTMRGIIAKAvdH 362
Cdd:cd01152  184 LVDMDSPGVTVRPIRSING--GEFFNEVFLDDVRVPDANRVGEVNDGWKVAMTTLNFERVSIGGSAATFFELLLARL--L 259
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767992071 363 ATNRTQFGEkiHNFGLIQEKLARMVM----LQYVTESMAYMVSANMDQGAtdfqiEAAISKIFGSEAAWKVTDECIQIMG 438
Cdd:cd01152  260 LLTRDGRPL--IDDPLVRQRLARLEAeaeaLRLLVFRLASALAAGKPPGA-----EASIAKLFGSELAQELAELALELLG 332
                        330       340       350       360
                 ....*....|....*....|....*....|....*....|...
gi 767992071 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 4.46e-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: 136.75  E-value: 4.46e-35
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767992071 102 LKELVEPVSRFFEEVNDPAKNDALEMVEE---TTWQ------GLKE----LGAFGLQVPSELGGVGLCNTQYARLVEIVG 168
Cdd:cd01155    3 AQELRARVKAFMEEHVYPAEQEFLEYYAEggdRWWTpppiieKLKAkakaEGLWNLFLPEVSGLSGLTNLEYAYLAEETG 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767992071 169 MHDLGVGITLGAHQSIGFKGIL-LFGTKAQKEKYLPKLASGETVAAFCLTEPS-SGSDAASIRTSAVPSpcGKYYTLNGS 246
Cdd:cd01155   83 RSFFAPEVFNCQAPDTGNMEVLhRYGSEEQKKQWLEPLLDGKIRSAFAMTEPDvASSDATNIECSIERD--GDDYVINGR 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767992071 247 KLWISNGGLAD--IFTVFAKTpvtDPATGAVKEKITAFVVERGFGGITHGPPEKKMGIKAS--NTAEVFFDGVRVPSENV 322
Cdd:cd01155  161 KWWSSGAGDPRckIAIVMGRT---DPDGAPRHRQQSMILVPMDTPGVTIIRPLSVFGYDDAphGHAEITFDNVRVPASNL 237
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767992071 323 LGEVGSGFKVAMHILNNGRFGMAAALAGTMRGIIAKAVDHATNRTQFGEKIHNFGLIQEKLA--RMV--MLQYVTESMAY 398
Cdd:cd01155  238 ILGEGRGFEIAQGRLGPGRIHHCMRLIGAAERALELMCQRAVSREAFGKKLAQHGVVAHWIAksRIEieQARLLVLKAAH 317
                        330       340       350       360       370       380
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 767992071 399 MvsanMDQ-GATDFQIEAAISKIFGSEAAWKVTDECIQIMGGMGFMKEPGVERVLRDLRIFRIFEG 463
Cdd:cd01155  318 M----IDTvGNKAARKEIAMIKVAAPRMALKIIDRAIQVHGAAGVSQDTPLANMYAWARTLRIADG 379
PLN02526 PLN02526
acyl-coenzyme A oxidase
151-491 7.56e-33

acyl-coenzyme A oxidase


Pssm-ID: 178141 [Multi-domain]  Cd Length: 412  Bit Score: 130.74  E-value: 7.56e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767992071 151 GGVGLCNTQYARLVEIVGMHDLGVGITLGAHQSIGFKGILLFGTKAQKEKYLPKLASGETVAAFCLTEPSSGSDAASIRT 230
Cdd:PLN02526  83 GCPGLSITASAIATAEVARVDASCSTFILVHSSLAMLTIALCGSEAQKQKYLPSLAQLDTVACWALTEPDYGSDASSLNT 162
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767992071 231 SAVPSPCGkyYTLNGSKLWISNGGLADIFTVFAKTPVTDpatgavkeKITAFVVERGFGGITHGPPEKKMGIKASNTAEV 310
Cdd:PLN02526 163 TATKVEGG--WILNGQKRWIGNSTFADVLVIFARNTTTN--------QINGFIVKKGAPGLKATKIENKIGLRMVQNGDI 232
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767992071 311 FFDGVRVPSENVLGEVGSgFKVAMHILNNGRFGMAAALAGTMRGIIAKAVDHATNRTQFGEKIHNFGLIQEKLARmvMLQ 390
Cdd:PLN02526 233 VLKDVFVPDEDRLPGVNS-FQDTNKVLAVSRVMVAWQPIGISMGVYDMCHRYLKERKQFGAPLAAFQINQEKLVR--MLG 309
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767992071 391 YVtESMAYM--------VSANMDQGatdfqiEAAISKIFGSEAAWKVTDECIQIMGGMGFMKEPGVERVLRDLRIFRIFE 462
Cdd:PLN02526 310 NI-QAMFLVgwrlcklyESGKMTPG------HASLGKAWITKKARETVALGRELLGGNGILADFLVAKAFCDLEPIYTYE 382
                        330       340
                 ....*....|....*....|....*....
gi 767992071 463 GTNDILRLFVALQgcMAGRAGQRPESQRT 491
Cdd:PLN02526 383 GTYDINALVTGRE--ITGIASFKPAASTR 409
AidB cd01154
Proteins involved in DNA damage response, similar to the AidB gene product; AidB is one of ...
199-470 1.40e-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: 127.10  E-value: 1.40e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767992071 199 EKYLPKLASGET----VAAFCLTEPSSGSDAASIRTSAVPSPcGKYYTLNGSKlWISNGGLADIFTVFAKTPVTDPATGA 274
Cdd:cd01154  132 KQYLPGLLSDRYktglLGGTWMTEKQGGSDLGANETTAERSG-GGVYRLNGHK-WFASAPLADAALVLARPEGAPAGARG 209
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767992071 275 vkekITAFVVER-----GFGGITHGPPEKKMGIKASNTAEVFFDGvrvpSEN-VLGEVGSGFKVAMHILNNGRFGMAAAL 348
Cdd:cd01154  210 ----LSLFLVPRlledgTRNGYRIRRLKDKLGTRSVATGEVEFDD----AEAyLIGDEGKGIYYILEMLNISRLDNAVAA 281
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767992071 349 AGTMRGIIAKAVDHATNRTQFGEKIHNFGLIQEKLARMVMLQYVTESMAYMVSANMDQGATDFQIEA-------AISKIF 421
Cdd:cd01154  282 LGIMRRALSEAYHYARHRRAFGKPLIDHPLMRRDLAEMEVDVEAATALTFRAARAFDRAAADKPVEAhmarlatPVAKLI 361
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*....
gi 767992071 422 GSEAAWKVTDECIQIMGGMGFMKEPGVERVLRDLRIFRIFEGTNDILRL 470
Cdd:cd01154  362 ACKRAAPVTSEAMEVFGGNGYLEEWPVARLHREAQVTPIWEGTGNIQAL 410
PTZ00456 PTZ00456
acyl-CoA dehydrogenase; Provisional
130-467 1.54e-28

acyl-CoA dehydrogenase; Provisional


Pssm-ID: 185635 [Multi-domain]  Cd Length: 622  Bit Score: 120.74  E-value: 1.54e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767992071 130 ETTWQGLKELGAFGLQVPSELGGVGLCNTQYARLVEIVGMHDLGVGITLGahQSIG-FKGILLFGTKAQKEKYLPKLASG 208
Cdd:PTZ00456 102 KEAYQALKAGGWTGISEPEEYGGQALPLSVGFITRELMATANWGFSMYPG--LSIGaANTLMAWGSEEQKEQYLTKLVSG 179
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767992071 209 ETVAAFCLTEPSSGSDAASIRTSAVPSPCGKyYTLNGSKLWISNG--GLAD--IFTVFAKTPVTDPATgavkEKITAFVV 284
Cdd:PTZ00456 180 EWSGTMCLTEPQCGTDLGQVKTKAEPSADGS-YKITGTKIFISAGdhDLTEniVHIVLARLPNSLPTT----KGLSLFLV 254
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767992071 285 ERGF----------GGITHGPPEKKMGIKASNTAEVFFDGvrvPSENVLGEVGSGFKVAMHILNNGRfgMAAALAGTMRG 354
Cdd:PTZ00456 255 PRHVvkpdgsletaKNVKCIGLEKKMGIKGSSTCQLSFEN---SVGYLIGEPNAGMKQMFTFMNTAR--VGTALEGVCHA 329
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767992071 355 IIA--KAVDHATNR--------TQFGEKIHNFGLIQEKLARMVML-QYVTE---SMAYMVSANMD--QGATDFQIEAA-- 416
Cdd:PTZ00456 330 ELAfqNALRYARERrsmralsgTKEPEKPADRIICHANVRQNILFaKAVAEggrALLLDVGRLLDihAAAKDAATREAld 409
                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 767992071 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 6.11e-27

Acyl-CoA dehydrogenase, middle domain; Central domain of Acyl-CoA dehydrogenase has a beta-barrel fold.


Pssm-ID: 426970 [Multi-domain]  Cd Length: 95  Bit Score: 104.66  E-value: 6.11e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767992071  213 AFCLTEPSSGSDAASIRTSAVPSPcGKYYTLNGSKLWISNGGLADIFTVFAKTPVTDPATGavkekITAFVVERGFGGIT 292
Cdd:pfam02770   1 AFALTEPGAGSDVASLKTTAADGD-GGGWVLNGTKWWITNAGIADLFLVLARTGGDDRHGG-----ISLFLVPKDAPGVT 74
                          90       100
                  ....*....|....*....|.
gi 767992071  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 2.18e-24

Acyl-CoA dehydrogenase, N-terminal domain; The N-terminal domain of Acyl-CoA dehydrogenase is an all-alpha domain.


Pssm-ID: 426971 [Multi-domain]  Cd Length: 113  Bit Score: 97.92  E-value: 2.18e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767992071   95 NEEQTQFLKElvepVSRFFEEVNDP--AKNDALEMVEETTWQGLKELGAFGLQVPSELGGVGLCNTQYARLVEIVGMHDL 172
Cdd:pfam02771   1 TEEQEALRDT----VREFAEEEIAPhaAEWDEEGEFPRELWKKLGELGLLGITIPEEYGGAGLDYLAYALVAEELARADA 76
                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 767992071  173 GVGITLGAHQSIGFKGILLFGTKAQKEKYLPKLASGE 209
Cdd:pfam02771  77 SVALALSVHSSLGAPPILRFGTEEQKERYLPKLASGE 113
fadE PRK09463
acyl-CoA dehydrogenase; Reviewed
88-446 9.69e-21

acyl-CoA dehydrogenase; Reviewed


Pssm-ID: 236528 [Multi-domain]  Cd Length: 777  Bit Score: 96.81  E-value: 9.69e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767992071  88 FPYPSVLNEEQTqFLKELVEPVSRFfeeVNDPAKNDALEMVEETTWQGLKELGAFGLQVPSELGGVGLCNTQYARLVEIV 167
Cdd:PRK09463  74 YPKPTLTAEEQA-FLDGPVEELCRM---VNDWQITHELADLPPEVWQFIKEHGFFGMIIPKEYGGLEFSAYAHSRVLQKL 149
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767992071 168 GMHDLGVGITLGAHQSIGfKGILL--FGTKAQKEKYLPKLASGETVAAFCLTEPSSGSDAASIRTSAVpsPC-----GK- 239
Cdd:PRK09463 150 ASRSGTLAVTVMVPNSLG-PGELLlhYGTDEQKDHYLPRLARGEEIPCFALTSPEAGSDAGSIPDTGV--VCkgewqGEe 226
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767992071 240 --YYTLNGSKLWISnggLADIFTVFA---KtpVTDPaTGAVKEK----ITAFVVERGFGGITHGPPEKKMGIkasntaeV 310
Cdd:PRK09463 227 vlGMRLTWNKRYIT---LAPIATVLGlafK--LYDP-DGLLGDKedlgITCALIPTDTPGVEIGRRHFPLNV-------P 293
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767992071 311 FFDG------VRVPSENVLGE---VGSGFKVAMHILNNGRFGMAAALAGTMRGIIAKAV-DHATNRTQFGEKIHNFGLIQ 380
Cdd:PRK09463 294 FQNGptrgkdVFIPLDYIIGGpkmAGQGWRMLMECLSVGRGISLPSNSTGGAKLAALATgAYARIRRQFKLPIGKFEGIE 373
                        330       340       350       360       370       380
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 767992071 381 EKLARMVMLQYVTESMAYMVSANMDQGATDFQIeAAISKIFGSEAAWKVTDECIQIMGGMGFMKEP 446
Cdd:PRK09463 374 EPLARIAGNAYLMDAARTLTTAAVDLGEKPSVL-SAIAKYHLTERGRQVINDAMDIHGGKGICLGP 438
PRK13026 PRK13026
acyl-CoA dehydrogenase; Reviewed
133-563 1.87e-20

acyl-CoA dehydrogenase; Reviewed


Pssm-ID: 237277 [Multi-domain]  Cd Length: 774  Bit Score: 95.79  E-value: 1.87e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767992071 133 WQGLKELGAFGLQVPSELGGVGLcnTQYA--RLVEIVGMHDLGVGITLGAHQSIGfKGILL--FGTKAQKEKYLPKLASG 208
Cdd:PRK13026 114 WDYLKKEGFFALIIPKEYGGKGF--SAYAnsTIVSKIATRSVSAAVTVMVPNSLG-PGELLthYGTQEQKDYWLPRLADG 190
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767992071 209 ETVAAFCLTEPSSGSDAASIRTSAVpsPC-GKY-------YTLNGSKLWISnggLADIFTVF-----AKTPvtDPATGAV 275
Cdd:PRK13026 191 TEIPCFALTGPEAGSDAGAIPDTGI--VCrGEFegeevlgLRLTWDKRYIT---LAPVATVLglafkLRDP--DGLLGDK 263
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767992071 276 KE-KITAFVVERGFGGITHGPPEKKMGIkasntaeVFFDG------VRVPSENVLG---EVGSGFKVAMHILNNGRFGMA 345
Cdd:PRK13026 264 KElGITCALIPTDHPGVEIGRRHNPLGM-------AFMNGttrgkdVFIPLDWIIGgpdYAGRGWRMLVECLSAGRGISL 336
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767992071 346 AALAGTMRGIIAKAVD-HATNRTQFGEKIHNFGLIQEKLARMVMLQYVTESMAYMVSANMDQGATDfQIEAAISKIFGSE 424
Cdd:PRK13026 337 PALGTASGHMATRTTGaYAYVRRQFGMPIGQFEGVQEALARIAGNTYLLEAARRLTTTGLDLGVKP-SVVTAIAKYHMTE 415
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767992071 425 AAWKVTDECIQIMGGMGFMKEPG--VERVLRDLRIFRIFEGTNDILR-LFVALQGCMAgragqrpesqrtCPPGVESEWR 501
Cdd:PRK13026 416 LARDVVNDAMDIHAGKGIQLGPKnyLGHAYMAVPIAITVEGANILTRnLMIFGQGATR------------CHPYVLAEME 483
                        410       420       430       440       450       460       470
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 767992071 502 AV------RALEQFATVveakLIKHKKGIVSEEAGRECL----SRRGPGPGSQPAQIYFHLLlpARASRSLS 563
Cdd:PRK13026 484 AAamedehEGLEAFDSL----LFKHIGYAARNAFRALFSaltgSRFISAPVSGETAQYYKDM--SRLSAALA 549
AXO cd01150
Peroxisomal acyl-CoA oxidase; Peroxisomal acyl-CoA oxidases (AXO) catalyze the first set in ...
163-577 4.12e-20

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: 94.32  E-value: 4.12e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767992071 163 LVEIVGMHDLGVGITLGAHQSIGFKGILLFGTKAQKEKYLPKLASGETVAAFCLTEPSSGSDAASIRTSAVPSPCGKYYT 242
Cdd:cd01150   87 LTNSLGGYDLSLGAKLGLHLGLFGNAIKNLGTDEHQDYWLQGANNLEIIGCFAQTELGHGSNLQGLETTATYDPLTQEFV 166
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767992071 243 LN-----GSKLWIsnGGLADIFT---VFAKTpvtdpATGAVKEKITAFVVE-------RGFGGITHGPPEKKMGIKASNT 307
Cdd:cd01150  167 INtpdftATKWWP--GNLGKTAThavVFAQL-----ITPGKNHGLHAFIVPirdpkthQPLPGVTVGDIGPKMGLNGVDN 239
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767992071 308 AEVFFDGVRVPSENVL---GEV-------------GSGFKVAMHILNNGRFGMAAALAGTMRGIIAKAVDHATNRTQFGE 371
Cdd:cd01150  240 GFLQFRNVRIPRENLLnrfGDVspdgtyvspfkdpNKRYGAMLGTRSGGRVGLIYDAAMSLKKAATIAIRYSAVRRQFGP 319
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767992071 372 K-------IHNFGLIQEK----LARMVMLQYVTESMAYM---VSANMDQGATDFQIE----AAISKIFGSEAAWKVTDEC 433
Cdd:cd01150  320 KpsdpevqILDYQLQQYRlfpqLAAAYAFHFAAKSLVEMyheIIKELLQGNSELLAElhalSAGLKAVATWTAAQGIQEC 399
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767992071 434 IQIMGGMGFMKEPGVERVLRDLRIFRIFEGTNDILRLFVALQGCMAGRAGQRPESQRTCppgveSEWRAVRALEQFAtvv 513
Cdd:cd01150  400 REACGGHGYLAMNRLPTLRDDNDPFCTYEGDNTVLLQQTANYLLKKYAQAFSLADYLEA-----YEWLAAHLLRHAA--- 471
                        410       420       430       440       450       460
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 767992071 514 eAKLIKHKK-GIVSEEAGRECLSRrgpgpGSQPAQIYFHLLLPARASRSLSEGHPTAQHE--KMLCD 577
Cdd:cd01150  472 -AQLEKLKKsGSGSFEARNNSQVH-----LRCAAKAHTEYTVLQRFHESVEEIVDPSVRAvlKRLCD 532
PLN02636 PLN02636
acyl-coenzyme A oxidase
159-473 1.87e-18

acyl-coenzyme A oxidase


Pssm-ID: 215342 [Multi-domain]  Cd Length: 686  Bit Score: 89.53  E-value: 1.87e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767992071 159 QYARLVEIVGMHDLGVGITLGAHQSIGFKGILLFGTKAQKEKYLPKLASGETVAAFCLTEPSSGSDAASIRTSAVPSPCG 238
Cdd:PLN02636 122 KYFAITEAVGSVDMSLGIKLGVQYSLWGGSVINLGTKKHRDKYFDGIDNLDYPGCFAMTELHHGSNVQGLQTTATFDPLT 201
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767992071 239 KYYTLN-----GSKLWISNGGLADIF-TVFAKTPVTDPATGAVKEK-ITAFVV-------ERGFGGITHGPPEKKMGIKA 304
Cdd:PLN02636 202 DEFVINtpndgAIKWWIGNAAVHGKFaTVFARLKLPTHDSKGVSDMgVHAFIVpirdmktHQVLPGVEIRDCGHKVGLNG 281
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767992071 305 SNTAEVFFDGVRVPSENVLGEVG----------------SGFKVAMHILNNGRFGMAAALAGTMRGIIAKAVDHATNRTQ 368
Cdd:PLN02636 282 VDNGALRFRSVRIPRDNLLNRFGdvsrdgkytsslptinKRFAATLGELVGGRVGLAYGSVGVLKASNTIAIRYSLLRQQ 361
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767992071 369 FGE------KIHNFGLIQEKLarMVML----------QYVTESMAYMVSANMDQGATDFQIEAAISKIFGSEAAWKVTDE 432
Cdd:PLN02636 362 FGPpkqpeiSILDYQSQQHKL--MPMLastyafhfatEYLVERYSEMKKTHDDQLVADVHALSAGLKAYITSYTAKALST 439
                        330       340       350       360
                 ....*....|....*....|....*....|....*....|....
gi 767992071 433 CIQIMGGMGFmkePGVER--VLR-DLRIFRIFEGTNDILRLFVA 473
Cdd:PLN02636 440 CREACGGHGY---AAVNRfgSLRnDHDIFQTFEGDNTVLLQQVA 480
PTZ00457 PTZ00457
acyl-CoA dehydrogenase; Provisional
72-421 4.97e-18

acyl-CoA dehydrogenase; Provisional


Pssm-ID: 185636 [Multi-domain]  Cd Length: 520  Bit Score: 87.63  E-value: 4.97e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767992071  72 SFAVGMFKGQLTTDQVFPYPS-VLNEEQTQFLKELVEPVSrffeevndpaKNDalemveettwqglKELG-AFGLQVPSE 149
Cdd:PTZ00457  17 SYAAGLFNFKIVPEEMFPYPCrKLDGDEAENLQSLLEQIR----------SND-------------KILGnLYGARIATE 73
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767992071 150 LGGVGLCNTQYARLVEIVGMHdlGVGITLGAHQSIGFKGILL--FGTKAQKEKYLPKLASGETVAAFClTEPSSGSDAAS 227
Cdd:PTZ00457  74 YGGLGLGHTAHALIYEEVGTN--CDSKLLSTIQHSGFCTYLLstVGSKELKGKYLTAMSDGTIMMGWA-TEEGCGSDISM 150
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767992071 228 IRTSAVPSPCGKYyTLNGSKLWIsNGGLADIFTVFAKTpVTDPATGA---VKEKITAFVVERgfggithgppeKKMGIKA 304
Cdd:PTZ00457 151 NTTKASLTDDGSY-VLTGQKRCE-FAASATHFLVLAKT-LTQTAAEEgatEVSRNSFFICAK-----------DAKGVSV 216
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767992071 305 SNTAEVFFDgvrVPSENVLGEVGSGFKVAMHILNNGRFGMAAALAGTMRGIIAKAVDhaTNRTQFgekihnfglIQEKLA 384
Cdd:PTZ00457 217 NGDSVVFEN---TPAADVVGVVGEGFKDAMITLFTEQYLYAASLLGIMKRVVQELRG--SNAEEG---------ATDTVA 282
                        330       340       350
                 ....*....|....*....|....*....|....*..
gi 767992071 385 RMVMLQYVTESMAYMVSANMDQGATDFQIEAAISKIF 421
Cdd:PTZ00457 283 SFACAMYAMESTLYALTANLDLPTEDSLLECTLVSAF 319
PLN02876 PLN02876
acyl-CoA dehydrogenase
148-467 5.13e-18

acyl-CoA dehydrogenase


Pssm-ID: 215473 [Multi-domain]  Cd Length: 822  Bit Score: 88.31  E-value: 5.13e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767992071 148 SELGGVGLCNTQYARLVEIVGMHDLGVGI-TLGAHQSIGFKGILLFGTKAQKEKYLPKLASGETVAAFCLTEPS-SGSDA 225
Cdd:PLN02876 487 DQLLGAGLSNLEYGYLCEIMGRSVWAPQVfNCGAPDTGNMEVLLRYGNKEQQLEWLIPLLEGKIRSGFAMTEPQvASSDA 566
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767992071 226 ASIRTSAVPSpcGKYYTLNGSKLWISngGLAD----IFTVFAKTPVTDPA------------TGAVKEKITAFVVerGFG 289
Cdd:PLN02876 567 TNIECSIRRQ--GDSYVINGTKWWTS--GAMDprcrVLIVMGKTDFNAPKhkqqsmilvdiqTPGVQIKRPLLVF--GFD 640
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767992071 290 GITHGppekkmgikasnTAEVFFDGVRVPSENVLGEVGSGFKVAMHILNNGRFGMAAALAGTMRGIIAKAVDHATNRTQF 369
Cdd:PLN02876 641 DAPHG------------HAEISFENVRVPAKNILLGEGRGFEIAQGRLGPGRLHHCMRLIGAAERGMQLMVQRALSRKAF 708
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767992071 370 GEKIHNFGLIQEKLARmvmLQYVTESMAYMVSANMDQ----GATDFQIEAAISKIFGSEAAWKVTDECIQIMGGMGFMKE 445
Cdd:PLN02876 709 GKLIAQHGSFLSDLAK---CRVELEQTRLLVLEAADQldrlGNKKARGIIAMAKVAAPNMALKVLDMAMQVHGAAGVSSD 785
                        330       340
                 ....*....|....*....|..
gi 767992071 446 PGVERVLRDLRIFRIFEGTNDI 467
Cdd:PLN02876 786 TVLAHLWATARTLRIADGPDEV 807
DszC cd01163
Dibenzothiophene (DBT) desulfurization enzyme C; DszC is a flavin reductase dependent enzyme, ...
128-367 9.80e-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: 63.88  E-value: 9.80e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767992071 128 VEETTWqgLKELGAFGLQVPSELGGVGLCNTQYARLVEIVGMHDLGVGITLGAHqsIGF-KGILLFGTKAQKEKYLPKLA 206
Cdd:cd01163   25 YEEVAL--LRQSGLGTLRVPKEYGGLGASLPDLYEVVRELAAADSNIAQALRAH--FGFvEALLLAGPEQFRKRWFGRVL 100
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767992071 207 SGETVAAfclTEPSSGSDAASIRTSAVPSPCGKYYtLNGSKlWISNGGL-ADIFTVFAktpvTDPAtgavkEKITAFVVE 285
Cdd:cd01163  101 NGWIFGN---AVSERGSVRPGTFLTATVRDGGGYV-LNGKK-FYSTGALfSDWVTVSA----LDEE-----GKLVFAAVP 166
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767992071 286 RGFGGITHGPPEKKMGIK--ASNTAEvfFDGVRVPSENVLGEvGSGFKVAMHILNNGRFGMAAALAGTMRGIIAKAVDHA 363
Cdd:cd01163  167 TDRPGITVVDDWDGFGQRltASGTVT--FDNVRVEPDEVLPR-PNAPDRGTLLTAIYQLVLAAVLAGIARAALDDAVAYV 243

                 ....
gi 767992071 364 TNRT 367
Cdd:cd01163  244 RSRT 247
PRK11561 PRK11561
isovaleryl CoA dehydrogenase; Provisional
216-472 1.32e-07

isovaleryl CoA dehydrogenase; Provisional


Pssm-ID: 183199 [Multi-domain]  Cd Length: 538  Bit Score: 54.37  E-value: 1.32e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767992071 216 LTEPSSGSDAASIRTSAVPSPcGKYYTLNGSKlWISNGGLADIFTVFAKTpvtdpatgavKEKITAFVVERGFGGITHGP 295
Cdd:PRK11561 184 MTEKQGGSDVLSNTTRAERLA-DGSYRLVGHK-WFFSVPQSDAHLVLAQA----------KGGLSCFFVPRFLPDGQRNA 251
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767992071 296 P-----EKKMGIKASNTAEVFFDGVrvpSENVLGEVGSGFKvamHILNNG---RFGMAAALAGTMRGIIAKAVDHATNRT 367
Cdd:PRK11561 252 IrlerlKDKLGNRSNASSEVEFQDA---IGWLLGEEGEGIR---LILKMGgmtRFDCALGSHGLMRRAFSVAIYHAHQRQ 325
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767992071 368 QFGEKIHNFGLIQEKLARMVMLQYVTESMAYMVSANMDQGATdfQIEAAISKIFGSEAAWKVTD-------ECIQIMGGM 440
Cdd:PRK11561 326 VFGKPLIEQPLMRQVLSRMALQLEGQTALLFRLARAWDRRAD--AKEALWARLFTPAAKFVICKrgipfvaEAMEVLGGI 403
                        250       260       270
                 ....*....|....*....|....*....|..
gi 767992071 441 GFMKEPGVERVLRDLRIFRIFEGTNDILRLFV 472
Cdd:PRK11561 404 GYCEESELPRLYREMPVNSIWEGSGNIMCLDV 435
PLN02312 PLN02312
acyl-CoA oxidase
161-326 1.71e-07

acyl-CoA oxidase


Pssm-ID: 215178 [Multi-domain]  Cd Length: 680  Bit Score: 54.39  E-value: 1.71e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767992071 161 ARLVEIVGMHDLGVGITLGAHQSIGFKGILLFGTKAQKEKYLPKLASGETVAAFCLTEPSSGSDAASIRTSAVPSPCGKY 240
Cdd:PLN02312 136 LALLEVIGIYDHSLAIKLGVHFFLWGGAIKFLGTKRHHDKWLKDTEDYVVKGCFAMTELGHGSNVRGIETVTTYDPKTEE 215
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767992071 241 YTLN-----GSKLWIsnGGLADIFT---VFAKTPVTdpatgAVKEKITAFVVE------RGFGGITHGPPEKKMGIKASN 306
Cdd:PLN02312 216 FVINtpcesAQKYWI--GGAANHAThtiVFSQLHIN-----GKNEGVHAFIAQirdqdgNICPNIRIADCGHKIGLNGVD 288
                        170       180
                 ....*....|....*....|
gi 767992071 307 TAEVFFDGVRVPSENVLGEV 326
Cdd:PLN02312 289 NGRIWFDNLRIPRENLLNSV 308
Acyl-CoA_dh_2 pfam08028
Acyl-CoA dehydrogenase, C-terminal domain;
343-465 4.37e-07

Acyl-CoA dehydrogenase, C-terminal domain;


Pssm-ID: 429790 [Multi-domain]  Cd Length: 133  Bit Score: 49.27  E-value: 4.37e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767992071  343 GMAAALAGTMRGIIAKAVDHATNRTQ--FGEKIHNFGLIQEKLARMV-------MLQYVTESMAYMVSANMDQGATDFQI 413
Cdd:pfam08028   1 GIAAAALGAARAALAEFTERARGRVRayFGVPLAEDPATQLALAEAAaridaarLLLERAAARIEAAAAAGKPVTPALRA 80
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|..
gi 767992071  414 EAAISKIFGSEAAWKVTDECIQIMGGMGFMKEPGVERVLRDLRIFRIFEGTN 465
Cdd:pfam08028  81 EARRAAAFATELAVAAVDALFRAAGGSALFQDSPLQRIWRDIHAAAQHAAVN 132
PTZ00460 PTZ00460
acyl-CoA dehydrogenase; Provisional
193-473 5.62e-06

acyl-CoA dehydrogenase; Provisional


Pssm-ID: 185639 [Multi-domain]  Cd Length: 646  Bit Score: 49.46  E-value: 5.62e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767992071 193 GTKAQKEKYLPKLASGETVAAFCLTEPSSGSDAASIRTSAVPSPCGKYYTLN-----GSKLWISN-GGLADIFTVFAKTP 266
Cdd:PTZ00460 110 GTDEQINLWMPSLLNFEIVGCYAQTELGHGSDVQNLETTATYDKQTNEFVIHtpsveAVKFWPGElGFLCNFALVYAKLI 189
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767992071 267 VTDPATG--AVKEKITAFVVERGFGGITHGPPEKKMGIKASNTAEVFFDGVRVPSENVLG---EVGSGFKVAMHilNNGR 341
Cdd:PTZ00460 190 VNGKNKGvhPFMVRIRDKETHKPLQGVEVGDIGPKMGYAVKDNGFLSFDHYRIPLDSLLAryiKVSEDGQVERQ--GNPK 267
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767992071 342 FGMAAALagTMRGIIAK------------AVDHATNRTQFGE------KIHNFGLIQEK----LARMVMLQYVTESMAYM 399
Cdd:PTZ00460 268 VSYASMM--YMRNLIIDqyprfaaqaltvAIRYSIYRQQFTNdnkqenSVLEYQTQQQKllplLAEFYACIFGGLKIKEL 345
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767992071 400 VSANMDQ-GATDFQIEAAISKIFGSEAAW------KVTDECIQIMGGMGFMKEPGVERVLRDLRIFRIFEGTNDILRLFV 472
Cdd:PTZ00460 346 VDDNFNRvQKNDFSLLQLTHAILSAAKANytyfvsNCAEWCRLSCGGHGYAHYSGLPAIYFDMSPNITLEGENQIMYLQL 425

                 .
gi 767992071 473 A 473
Cdd:PTZ00460 426 A 426
PLN02443 PLN02443
acyl-coenzyme A oxidase
193-473 1.85e-04

acyl-coenzyme A oxidase


Pssm-ID: 178062 [Multi-domain]  Cd Length: 664  Bit Score: 44.44  E-value: 1.85e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767992071 193 GTKAQKEKYLPKLASGETVAAFCLTEPSSGSDAASIRTSAVPSPCGKYY-----TLNGSKLWisNGGLADIFT---VFAK 264
Cdd:PLN02443 114 GTEEQQKKWLPLAYKMQIIGCYAQTELGHGSNVQGLETTATFDPKTDEFvihspTLTSSKWW--PGGLGKVSThavVYAR 191
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767992071 265 TpvtdpATGAVKEKITAFVVE-------RGFGGITHGPPEKKMGIKASNTAE---VFFDGVRVPSENVLGEVGSGFKVAM 334
Cdd:PLN02443 192 L-----ITNGKDHGIHGFIVQlrslddhSPLPGVTVGDIGMKFGNGAYNTMDngfLRFDHVRIPRDQMLMRLSKVTREGK 266
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767992071 335 HILNNgrfgMAAALA-GTM----RGIIAK-----------AVDHATNRTQFGEK-------IHNFGLIQEK----LARMV 387
Cdd:PLN02443 267 YVQSD----VPRQLVyGTMvyvrQTIVADastalsravciATRYSAVRRQFGSQdggpetqVIDYKTQQSRlfplLASAY 342
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767992071 388 MLQYVTESMAYMVSANMDQ-GATDF----QIEAAIS--KIFGSEAAWKVTDECIQIMGGMGFMKEPGVERVLRDLRIFRI 460
Cdd:PLN02443 343 AFRFVGEWLKWLYTDVTQRlEANDFstlpEAHACTAglKSLTTSATADGIEECRKLCGGHGYLCSSGLPELFAVYVPACT 422
                        330
                 ....*....|...
gi 767992071 461 FEGTNDILRLFVA 473
Cdd:PLN02443 423 YEGDNVVLLLQVA 435
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.20
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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