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Conserved domains on  [gi|21361497|ref|NP_054768|]
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complex I assembly factor ACAD9, mitochondrial isoform 1 [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 ...
 38-445 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: 747.37  E-value: 0e+00
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21361497  38 AFAKELFLGKIKKKEVFPFPEVSQDELNE-INQFLGPVEKFFTEEVDSRKIDQEGKIPDETLEKLKSLGLFGLQVPEEYG 116
Cdd:cd01161   1 SFALNMFLGDIVTKQVFPYPSVLTEEQTEeLNMLVGPVEKFFEEVNDPAKNDQLEKIPRKTLTQLKELGLFGLQVPEEYG 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21361497 117 GLGFSNTMYSRLGEIISMDGSITVTLAAHQAIGLKGIILAGTEEQKAKYLPKLASGEHIAAFCLTEPASGSDAASIRSRA 196
Cdd:cd01161  81 GLGLNNTQYARLAEIVGMDLGFSVTLGAHQSIGFKGILLFGTEAQKEKYLPKLASGEWIAAFALTEPSSGSDAASIRTTA 160

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21361497 197 TLSEDKKHYILNGSKVWITNGGLANIFTVFAKTEVVDSDGSVKDKITAFIVERDFGGVTNGKPEDKLGIRGSNTCEVHFE 276
Cdd:cd01161 161 VLSEDGKHYVLNGSKIWITNGGIADIFTVFAKTEVKDATGSVKDKITAFIVERSFGGVTNGPPEKKMGIKGSNTAEVYFE 240

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21361497 277 NTKIPVENILGEVGDGFKVAMNILNSGRFSMGSVVAGLLKRLIEMTAEYACTRKQFNKRLSEFGLIQEKFALMAQKAYVM 356
Cdd:cd01161 241 DVKIPVENVLGEVGDGFKVAMNILNNGRFGMGAALIGTMKRCIEKAVDYANNRKQFGKKIHEFGLIQEKLANMAILQYAT 320

                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21361497 357 ESMTYLTAGMLDQPGFPDCSIEAAMVKVFSSEAAWQCVSEALQILGGLGYTRDYPYERILRDTRILLIFEGTNEILRMYI 436
Cdd:cd01161 321 ESMAYMTSGNMDRGLKAEYQIEAAISKVFASEAAWLVVDEAIQIHGGMGFMREYGVERVLRDLRIFRIFEGTNEILRLFI 400


                ....*....
gi 21361497 437 ALTGLQHAG 445
Cdd:cd01161 401 ALTGLQHAG 409
 
Name Accession Description Interval E-value
VLCAD cd01161
Very long chain acyl-CoA dehydrogenase; VLCAD is an acyl-CoA dehydrogenase (ACAD), which is ...
 38-445 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: 747.37  E-value: 0e+00
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21361497  38 AFAKELFLGKIKKKEVFPFPEVSQDELNE-INQFLGPVEKFFTEEVDSRKIDQEGKIPDETLEKLKSLGLFGLQVPEEYG 116
Cdd:cd01161   1 SFALNMFLGDIVTKQVFPYPSVLTEEQTEeLNMLVGPVEKFFEEVNDPAKNDQLEKIPRKTLTQLKELGLFGLQVPEEYG 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21361497 117 GLGFSNTMYSRLGEIISMDGSITVTLAAHQAIGLKGIILAGTEEQKAKYLPKLASGEHIAAFCLTEPASGSDAASIRSRA 196
Cdd:cd01161  81 GLGLNNTQYARLAEIVGMDLGFSVTLGAHQSIGFKGILLFGTEAQKEKYLPKLASGEWIAAFALTEPSSGSDAASIRTTA 160

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21361497 197 TLSEDKKHYILNGSKVWITNGGLANIFTVFAKTEVVDSDGSVKDKITAFIVERDFGGVTNGKPEDKLGIRGSNTCEVHFE 276
Cdd:cd01161 161 VLSEDGKHYVLNGSKIWITNGGIADIFTVFAKTEVKDATGSVKDKITAFIVERSFGGVTNGPPEKKMGIKGSNTAEVYFE 240

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21361497 277 NTKIPVENILGEVGDGFKVAMNILNSGRFSMGSVVAGLLKRLIEMTAEYACTRKQFNKRLSEFGLIQEKFALMAQKAYVM 356
Cdd:cd01161 241 DVKIPVENVLGEVGDGFKVAMNILNNGRFGMGAALIGTMKRCIEKAVDYANNRKQFGKKIHEFGLIQEKLANMAILQYAT 320

                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21361497 357 ESMTYLTAGMLDQPGFPDCSIEAAMVKVFSSEAAWQCVSEALQILGGLGYTRDYPYERILRDTRILLIFEGTNEILRMYI 436
Cdd:cd01161 321 ESMAYMTSGNMDRGLKAEYQIEAAISKVFASEAAWLVVDEAIQIHGGMGFMREYGVERVLRDLRIFRIFEGTNEILRLFI 400


                ....*....
gi 21361497 437 ALTGLQHAG 445
Cdd:cd01161 401 ALTGLQHAG 409
CaiA COG1960
Acyl-CoA dehydrogenase related to the alkylation response protein AidB [Lipid transport and ...
 66-437 7.92e-149

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: 435.04  E-value: 7.92e-149
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21361497  66 EINQFLGPVEKFFTEEVD--SRKIDQEGKIPDETLEKLKSLGLFGLQVPEEYGGLGFSNTMYSRLGEIISM-DGSITVTL 142
Cdd:COG1960   8 EQRALRDEVREFAEEEIApeAREWDREGEFPRELWRKLAELGLLGLTIPEEYGGLGLSLVELALVLEELARaDASLALPV 87

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21361497 143 AAHqAIGLKGIILAGTEEQKAKYLPKLASGEHIAAFCLTEPASGSDAASIRSRATLSEDkkHYILNGSKVWITNGGLANI 222
Cdd:COG1960  88 GVH-NGAAEALLRFGTEEQKERYLPRLASGEWIGAFALTEPGAGSDAAALRTTAVRDGD--GYVLNGQKTFITNAPVADV 164

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21361497 223 FTVFAKTEvvDSDGSvkDKITAFIVERDFGGVTNGKPEDKLGIRGSNTCEVHFENTKIPVENILGEVGDGFKVAMNILNS 302
Cdd:COG1960 165 ILVLARTD--PAAGH--RGISLFLVPKDTPGVTVGRIEDKMGLRGSDTGELFFDDVRVPAENLLGEEGKGFKIAMSTLNA 240

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21361497 303 GRFSMGSVVAGLLKRLIEMTAEYACTRKQFNKRLSEFGLIQEKFALMAQKAYVMESMTYLTAGMLDQPGfpDCSIEAAMV 382
Cdd:COG1960 241 GRLGLAAQALGIAEAALELAVAYAREREQFGRPIADFQAVQHRLADMAAELEAARALVYRAAWLLDAGE--DAALEAAMA 318

                       330       340       350       360       370
                ....*....|....*....|....*....|....*....|....*....|....*
gi 21361497 383 KVFSSEAAWQCVSEALQILGGLGYTRDYPYERILRDTRILLIFEGTNEILRMYIA 437
Cdd:COG1960 319 KLFATEAALEVADEALQIHGGYGYTREYPLERLYRDARILTIYEGTNEIQRLIIA 373
PLN02519 PLN02519
isovaleryl-CoA dehydrogenase
 57-436 3.65e-80

isovaleryl-CoA dehydrogenase


Pssm-ID: 215284 [Multi-domain]  Cd Length: 404  Bit Score: 259.04  E-value: 3.65e-80
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21361497   57 PEVSQDELNEinQFLGPVEKFFTEEV--DSRKIDQEGKIPDE-TLEKLK-SLGLFGLQVPEEYGGLGFSNTMYS-RLGEI 131
Cdd:PLN02519  22 SSLLFDDTQL--QFKESVQQFAQENIapHAAAIDATNSFPKDvNLWKLMgDFNLHGITAPEEYGGLGLGYLYHCiAMEEI 99

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21361497  132 ISMDGSITVTLAAHQAIGLKGIILAGTEEQKAKYLPKLASGEHIAAFCLTEPASGSDAASIRSRATLSEdkKHYILNGSK 211
Cdd:PLN02519 100 SRASGSVGLSYGAHSNLCINQLVRNGTPAQKEKYLPKLISGEHVGALAMSEPNSGSDVVSMKCKAERVD--GGYVLNGNK 177

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21361497  212 VWITNGGLANIFTVFAKTEVvdSDGSvkDKITAFIVERDFGGVTNGKPEDKLGIRGSNTCEVHFENTKIPVENILGEVGD 291
Cdd:PLN02519 178 MWCTNGPVAQTLVVYAKTDV--AAGS--KGITAFIIEKGMPGFSTAQKLDKLGMRGSDTCELVFENCFVPEENVLGQEGK 253

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21361497  292 GFKVAMNILNSGRFSMGSVVAGLLKRLIEMTAEYACTRKQFNKRLSEFGLIQEKFA-----LMAQKAYVMESMTYLTAGM 366
Cdd:PLN02519 254 GVYVMMSGLDLERLVLAAGPLGLMQACLDVVLPYVRQREQFGRPIGEFQFIQGKLAdmytsLQSSRSYVYSVARDCDNGK 333

                        330       340       350       360       370       380       390
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21361497  367 LDQpgfPDCsieaAMVKVFSSEAAWQCVSEALQILGGLGYTRDYPYERILRDTRILLIFEGTNEILRMYI 436
Cdd:PLN02519 334 VDR---KDC----AGVILCAAERATQVALQAIQCLGGNGYINEYPTGRLLRDAKLYEIGAGTSEIRRMLI 396
Acyl-CoA_dh_1 pfam00441
Acyl-CoA dehydrogenase, C-terminal domain; C-terminal domain of Acyl-CoA dehydrogenase is an ...
 290-437 5.13e-44

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: 153.95  E-value: 5.13e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21361497   290 GDGFKVAMNILNSGRFSMGSVVAGLLKRLIEMTAEYACTRKQFNKRLSEFGLIQEKFALMAQKAYVMESMTYLTAGMLDQ 369
Cdd:pfam00441   1 GRGFRVAMETLNHERLAIAAMALGLARRALDEALAYARRRKAFGRPLIDFQLVRHKLAEMAAEIEAARLLVYRAAEALDA 80

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 21361497   370 pGFPDcSIEAAMVKVFSSEAAWQCVSEALQILGGLGYTRDYPYERILRDTRILLIFEGTNEILRMYIA 437
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 ...
 38-445 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: 747.37  E-value: 0e+00
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21361497  38 AFAKELFLGKIKKKEVFPFPEVSQDELNE-INQFLGPVEKFFTEEVDSRKIDQEGKIPDETLEKLKSLGLFGLQVPEEYG 116
Cdd:cd01161   1 SFALNMFLGDIVTKQVFPYPSVLTEEQTEeLNMLVGPVEKFFEEVNDPAKNDQLEKIPRKTLTQLKELGLFGLQVPEEYG 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21361497 117 GLGFSNTMYSRLGEIISMDGSITVTLAAHQAIGLKGIILAGTEEQKAKYLPKLASGEHIAAFCLTEPASGSDAASIRSRA 196
Cdd:cd01161  81 GLGLNNTQYARLAEIVGMDLGFSVTLGAHQSIGFKGILLFGTEAQKEKYLPKLASGEWIAAFALTEPSSGSDAASIRTTA 160

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21361497 197 TLSEDKKHYILNGSKVWITNGGLANIFTVFAKTEVVDSDGSVKDKITAFIVERDFGGVTNGKPEDKLGIRGSNTCEVHFE 276
Cdd:cd01161 161 VLSEDGKHYVLNGSKIWITNGGIADIFTVFAKTEVKDATGSVKDKITAFIVERSFGGVTNGPPEKKMGIKGSNTAEVYFE 240

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21361497 277 NTKIPVENILGEVGDGFKVAMNILNSGRFSMGSVVAGLLKRLIEMTAEYACTRKQFNKRLSEFGLIQEKFALMAQKAYVM 356
Cdd:cd01161 241 DVKIPVENVLGEVGDGFKVAMNILNNGRFGMGAALIGTMKRCIEKAVDYANNRKQFGKKIHEFGLIQEKLANMAILQYAT 320

                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21361497 357 ESMTYLTAGMLDQPGFPDCSIEAAMVKVFSSEAAWQCVSEALQILGGLGYTRDYPYERILRDTRILLIFEGTNEILRMYI 436
Cdd:cd01161 321 ESMAYMTSGNMDRGLKAEYQIEAAISKVFASEAAWLVVDEAIQIHGGMGFMREYGVERVLRDLRIFRIFEGTNEILRLFI 400


                ....*....
gi 21361497 437 ALTGLQHAG 445
Cdd:cd01161 401 ALTGLQHAG 409
CaiA COG1960
Acyl-CoA dehydrogenase related to the alkylation response protein AidB [Lipid transport and ...
 66-437 7.92e-149

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: 435.04  E-value: 7.92e-149
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21361497  66 EINQFLGPVEKFFTEEVD--SRKIDQEGKIPDETLEKLKSLGLFGLQVPEEYGGLGFSNTMYSRLGEIISM-DGSITVTL 142
Cdd:COG1960   8 EQRALRDEVREFAEEEIApeAREWDREGEFPRELWRKLAELGLLGLTIPEEYGGLGLSLVELALVLEELARaDASLALPV 87

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21361497 143 AAHqAIGLKGIILAGTEEQKAKYLPKLASGEHIAAFCLTEPASGSDAASIRSRATLSEDkkHYILNGSKVWITNGGLANI 222
Cdd:COG1960  88 GVH-NGAAEALLRFGTEEQKERYLPRLASGEWIGAFALTEPGAGSDAAALRTTAVRDGD--GYVLNGQKTFITNAPVADV 164

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21361497 223 FTVFAKTEvvDSDGSvkDKITAFIVERDFGGVTNGKPEDKLGIRGSNTCEVHFENTKIPVENILGEVGDGFKVAMNILNS 302
Cdd:COG1960 165 ILVLARTD--PAAGH--RGISLFLVPKDTPGVTVGRIEDKMGLRGSDTGELFFDDVRVPAENLLGEEGKGFKIAMSTLNA 240

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21361497 303 GRFSMGSVVAGLLKRLIEMTAEYACTRKQFNKRLSEFGLIQEKFALMAQKAYVMESMTYLTAGMLDQPGfpDCSIEAAMV 382
Cdd:COG1960 241 GRLGLAAQALGIAEAALELAVAYAREREQFGRPIADFQAVQHRLADMAAELEAARALVYRAAWLLDAGE--DAALEAAMA 318

                       330       340       350       360       370
                ....*....|....*....|....*....|....*....|....*....|....*
gi 21361497 383 KVFSSEAAWQCVSEALQILGGLGYTRDYPYERILRDTRILLIFEGTNEILRMYIA 437
Cdd:COG1960 319 KLFATEAALEVADEALQIHGGYGYTREYPLERLYRDARILTIYEGTNEIQRLIIA 373
SCAD_SBCAD cd01158
Short chain acyl-CoA dehydrogenases and eukaryotic short/branched chain acyl-CoA ...
 69-437 5.49e-135

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: 399.34  E-value: 5.49e-135
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21361497  69 QFLGPVEKFFTEEVD--SRKIDQEGKIPDETLEKLKSLGLFGLQVPEEYGGLGFSNTMYSR-LGEIISMDGSITVTLAAH 145
Cdd:cd01158   5 MIRKTVRDFAEKEIAplAAEMDEKGEFPREVIKEMAELGLMGIPIPEEYGGAGLDFLAYAIaIEELAKVDASVAVIVSVH 84

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21361497 146 QAIGLKGIILAGTEEQKAKYLPKLASGEHIAAFCLTEPASGSDAASIRSRATLSEDkkHYILNGSKVWITNGGLANIFTV 225
Cdd:cd01158  85 NSLGANPIIKFGTEEQKKKYLPPLATGEKIGAFALSEPGAGSDAAALKTTAKKDGD--DYVLNGSKMWITNGGEADFYIV 162

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21361497 226 FAKTevvdsDGSVKDK-ITAFIVERDFGGVTNGKPEDKLGIRGSNTCEVHFENTKIPVENILGEVGDGFKVAMNILNSGR 304
Cdd:cd01158 163 FAVT-----DPSKGYRgITAFIVERDTPGLSVGKKEDKLGIRGSSTTELIFEDVRVPKENILGEEGEGFKIAMQTLDGGR 237

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21361497 305 FSMGSVVAGLLKRLIEMTAEYACTRKQFNKRLSEFGLIQEKFALMAQKAYVMESMTYlTAGMLDQPGFPdCSIEAAMVKV 384
Cdd:cd01158 238 IGIAAQALGIAQAALDAAVDYAKERKQFGKPIADFQGIQFKLADMATEIEAARLLTY-KAARLKDNGEP-FIKEAAMAKL 315

                       330       340       350       360       370
                ....*....|....*....|....*....|....*....|....*....|...
gi 21361497 385 FSSEAAWQCVSEALQILGGLGYTRDYPYERILRDTRILLIFEGTNEILRMYIA 437
Cdd:cd01158 316 FASEVAMRVTTDAVQIFGGYGYTKDYPVERYYRDAKITEIYEGTSEIQRLVIA 368
ACAD cd00567
Acyl-CoA dehydrogenase; Both mitochondrial acyl-CoA dehydrogenases (ACAD) and peroxisomal ...
 148-437 7.02e-121

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: 361.22  E-value: 7.02e-121
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21361497 148 IGLKGIILAGTEEQKAKYLPKLASGEHIAAFCLTEPASGSDAASIRSRATLSEDkkHYILNGSKVWITNGGLANIFTVFA 227
Cdd:cd00567  43 LGAALLLAYGTEEQKERYLPPLASGEAIAAFALTEPGAGSDLAGIRTTARKDGD--GYVLNGRKIFISNGGDADLFIVLA 120

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21361497 228 KTevvDSDGSVKDKITAFIVERDFGGVTNGKPEDKLGIRGSNTCEVHFENTKIPVENILGEVGDGFKVAMNILNSGRFSM 307
Cdd:cd00567 121 RT---DEEGPGHRGISAFLVPADTPGVTVGRIWDKMGMRGSGTGELVFDDVRVPEDNLLGEEGGGFELAMKGLNVGRLLL 197

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21361497 308 GSVVAGLLKRLIEMTAEYACTRKQFNKRLSEFGLIQEKFALMAQKAYVMESMTYLTAGMLDQpGFPDCSIEAAMVKVFSS 387
Cdd:cd00567 198 AAVALGAARAALDEAVEYAKQRKQFGKPLAEFQAVQFKLADMAAELEAARLLLYRAAWLLDQ-GPDEARLEAAMAKLFAT 276

                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|
gi 21361497 388 EAAWQCVSEALQILGGLGYTRDYPYERILRDTRILLIFEGTNEILRMYIA 437
Cdd:cd00567 277 EAAREVADLAMQIHGGRGYSREYPVERYLRDARAARIAEGTAEIQRLIIA 326
IVD cd01156
Isovaleryl-CoA dehydrogenase; Isovaleryl-CoA dehydrogenase (IVD) is an is an acyl-CoA ...
 66-437 8.43e-106

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: 324.36  E-value: 8.43e-106
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21361497  66 EINQFLGPVEKFFTEEVDSR--KIDQEGKIPDETLEKLKSLGLFGLQVPEEYGGLGFSntmYsrLGEIISMD------GS 137
Cdd:cd01156   5 EIEMLRQSVREFAQKEIAPLaaKIDRDNEFPRDLWRKMGKLGLLGITAPEEYGGSGMG---Y--LAHVIIMEeisrasGS 79

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21361497 138 ITVTLAAHQAIGLKGIILAGTEEQKAKYLPKLASGEHIAAFCLTEPASGSDAASIRSRATlsEDKKHYILNGSKVWITNG 217
Cdd:cd01156  80 VALSYGAHSNLCINQIYRNGSAAQKEKYLPKLISGEHIGALAMSEPNAGSDVVSMKLRAE--KKGDRYVLNGSKMWITNG 157

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21361497 218 GLANIFTVFAKTEVvdsdGSVKDKITAFIVERDFGGVTNGKPEDKLGIRGSNTCEVHFENTKIPVENILGEVGDGFKVAM 297
Cdd:cd01156 158 PDADTLVVYAKTDP----SAGAHGITAFIVEKGMPGFSRAQKLDKLGMRGSNTCELVFEDCEVPEENILGGENKGVYVLM 233

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21361497 298 NILNSGRFSMGSVVAGLLKRLIEMTAEYACTRKQFNKRLSEFGLIQEKFA-----LMAQKAYVMESMTYLTAGMLDqpgf 372
Cdd:cd01156 234 SGLDYERLVLAGGPIGIMQAALDVAIPYAHQRKQFGQPIGEFQLVQGKLAdmytrLNASRSYLYTVAKACDRGNMD---- 309

                       330       340       350       360       370       380
                ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 21361497 373 pdcSIEAAMVKVFSSEAAWQCVSEALQILGGLGYTRDYPYERILRDTRILLIFEGTNEILRMYIA 437
Cdd:cd01156 310 ---PKDAAGVILYAAEKATQVALDAIQILGGNGYINDYPTGRLLRDAKLYEIGAGTSEIRRMVIG 371
LCAD cd01160
Long chain acyl-CoA dehydrogenase; LCAD is an acyl-CoA dehydrogenases (ACAD), which is found ...
 74-437 1.69e-87

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: 277.07  E-value: 1.69e-87
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21361497  74 VEKFFTEEVD--SRKIDQEGKIPDETLEKLKSLGLFGLQVPEEYGGLGFSNTMYSRLGEIISMDGSITVTLAAHQAIGLK 151
Cdd:cd01160  10 VRRFFAKEVApfHHEWEKAGEVPREVWRKAGEQGLLGVGFPEEYGGIGGDLLSAAVLWEELARAGGSGPGLSLHTDIVSP 89

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21361497 152 GIILAGTEEQKAKYLPKLASGEHIAAFCLTEPASGSDAASIRSRATLseDKKHYILNGSKVWITNGGLANIFTVFAKTev 231
Cdd:cd01160  90 YITRAGSPEQKERVLPQMVAGKKIGAIAMTEPGAGSDLQGIRTTARK--DGDHYVLNGSKTFITNGMLADVVIVVART-- 165

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21361497 232 vDSDGSVKDKITAFIVERDFGGVTNGKPEDKLGIRGSNTCEVHFENTKIPVENILGEVGDGFKVAMNILNSGRFSMGSVV 311
Cdd:cd01160 166 -GGEARGAGGISLFLVERGTPGFSRGRKLKKMGWKAQDTAELFFDDCRVPAENLLGEENKGFYYLMQNLPQERLLIAAGA 244

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21361497 312 AGLLKRLIEMTAEYACTRKQFNKRLSEFGLIQEKFALMAQKAYVMESMTYLTAGMLDQPGFPdcSIEAAMVKVFSSEAAW 391
Cdd:cd01160 245 LAAAEFMLEETRNYVKQRKAFGKTLAQLQVVRHKIAELATKVAVTRAFLDNCAWRHEQGRLD--VAEASMAKYWATELQN 322

                       330       340       350       360
                ....*....|....*....|....*....|....*....|....*.
gi 21361497 392 QCVSEALQILGGLGYTRDYPYERILRDTRILLIFEGTNEILRMYIA 437
Cdd:cd01160 323 RVAYECVQLHGGWGYMREYPIARAYRDARVQPIYGGTTEIMKELIS 368
IBD cd01162
Isobutyryl-CoA dehydrogenase; Isobutyryl-CoA dehydrogenase (IBD) catalyzes the alpha, beta- ...
 88-437 9.14e-87

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: 275.09  E-value: 9.14e-87
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21361497  88 DQEGKIPDETLEKLKSLGLFGLQVPEEYGGLGFSNTMYSRLGEIISM-DGSITVTLAAHQAIGLKgIILAGTEEQKAKYL 166
Cdd:cd01162  28 DQKKHFPVDVLRKAAELGFGGIYIRDDVGGSGLSRLDASIIFEALSTgCVSTAAYISIHNMCAWM-IDSFGNDEQRERFL 106

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21361497 167 PKLASGEHIAAFCLTEPASGSDAASIRSRATLSEDkkHYILNGSKVWITNGGLANIFTVFAKTevvdsDGSVKDKITAFI 246
Cdd:cd01162 107 PDLCTMEKLASYCLTEPGSGSDAAALRTRAVREGD--HYVLNGSKAFISGAGDSDVYVVMART-----GGEGPKGISCFV 179

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21361497 247 VERDFGGVTNGKPEDKLGIRGSNTCEVHFENTKIPVENILGEVGDGFKVAMNILNSGRFSMGSVVAGLLKRLIEMTAEYA 326
Cdd:cd01162 180 VEKGTPGLSFGANEKKMGWNAQPTRAVIFEDCRVPVENRLGGEGQGFGIAMAGLNGGRLNIASCSLGAAQAALDLARAYL 259

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21361497 327 CTRKQFNKRLSEFGLIQEKFALMAQKAYVMESMTYLTAGMLDQpGFPDCSIEAAMVKVFSSEAAWQCVSEALQILGGLGY 406
Cdd:cd01162 260 EERKQFGKPLADFQALQFKLADMATELVASRLMVRRAASALDR-GDPDAVKLCAMAKRFATDECFDVANQALQLHGGYGY 338

                       330       340       350
                ....*....|....*....|....*....|.
gi 21361497 407 TRDYPYERILRDTRILLIFEGTNEILRMYIA 437
Cdd:cd01162 339 LKDYPVEQYVRDLRVHQILEGTNEIMRLIIA 369
PLN02519 PLN02519
isovaleryl-CoA dehydrogenase
 57-436 3.65e-80

isovaleryl-CoA dehydrogenase


Pssm-ID: 215284 [Multi-domain]  Cd Length: 404  Bit Score: 259.04  E-value: 3.65e-80
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21361497   57 PEVSQDELNEinQFLGPVEKFFTEEV--DSRKIDQEGKIPDE-TLEKLK-SLGLFGLQVPEEYGGLGFSNTMYS-RLGEI 131
Cdd:PLN02519  22 SSLLFDDTQL--QFKESVQQFAQENIapHAAAIDATNSFPKDvNLWKLMgDFNLHGITAPEEYGGLGLGYLYHCiAMEEI 99

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21361497  132 ISMDGSITVTLAAHQAIGLKGIILAGTEEQKAKYLPKLASGEHIAAFCLTEPASGSDAASIRSRATLSEdkKHYILNGSK 211
Cdd:PLN02519 100 SRASGSVGLSYGAHSNLCINQLVRNGTPAQKEKYLPKLISGEHVGALAMSEPNSGSDVVSMKCKAERVD--GGYVLNGNK 177

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21361497  212 VWITNGGLANIFTVFAKTEVvdSDGSvkDKITAFIVERDFGGVTNGKPEDKLGIRGSNTCEVHFENTKIPVENILGEVGD 291
Cdd:PLN02519 178 MWCTNGPVAQTLVVYAKTDV--AAGS--KGITAFIIEKGMPGFSTAQKLDKLGMRGSDTCELVFENCFVPEENVLGQEGK 253

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21361497  292 GFKVAMNILNSGRFSMGSVVAGLLKRLIEMTAEYACTRKQFNKRLSEFGLIQEKFA-----LMAQKAYVMESMTYLTAGM 366
Cdd:PLN02519 254 GVYVMMSGLDLERLVLAAGPLGLMQACLDVVLPYVRQREQFGRPIGEFQFIQGKLAdmytsLQSSRSYVYSVARDCDNGK 333

                        330       340       350       360       370       380       390
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21361497  367 LDQpgfPDCsieaAMVKVFSSEAAWQCVSEALQILGGLGYTRDYPYERILRDTRILLIFEGTNEILRMYI 436
Cdd:PLN02519 334 VDR---KDC----AGVILCAAERATQVALQAIQCLGGNGYINEYPTGRLLRDAKLYEIGAGTSEIRRMLI 396
MCAD cd01157
Medium chain acyl-CoA dehydrogenase; MCADs are mitochondrial beta-oxidation enzymes, which ...
 69-443 1.67e-74

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: 243.26  E-value: 1.67e-74
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21361497  69 QFLGPVEKFFTEEV--DSRKIDQEGKIPDETLEKLKSLGLFGLQVPEEYGGLGFSNTMYSRLGEIISMDGSITVTLAAHQ 146
Cdd:cd01157   7 EFQETARKFAREEIipVAAEYDKSGEYPWPLIKRAWELGLMNTHIPEDCGGLGLGTFDTCLITEELAYGCTGVQTAIEAN 86

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21361497 147 AIGLKGIILAGTEEQKAKYLPKLASGEHIAAFCLTEPASGSDAASIRSRATLSEDKkhYILNGSKVWITNGGLANIFTVF 226
Cdd:cd01157  87 SLGQMPVIISGNDEQKKKYLGRMTEEPLMCAYCVTEPGAGSDVAGIKTKAEKKGDE--YIINGQKMWITNGGKANWYFLL 164

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21361497 227 AKTEVvDSDGSVKDKITAFIVERDFGGVTNGKPEDKLGIRGSNTCEVHFENTKIPVENILGEVGDGFKVAMNILNSGRFS 306
Cdd:cd01157 165 ARSDP-DPKCPASKAFTGFIVEADTPGIQPGRKELNMGQRCSDTRGITFEDVRVPKENVLIGEGAGFKIAMGAFDKTRPP 243

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21361497 307 MGSVVAGLLKRLIEMTAEYACTRKQFNKRLSEFGLIQEKFALMAQKAYVMESMTYLTAGMLDQPgfPDCSIEAAMVKVFS 386
Cdd:cd01157 244 VAAGAVGLAQRALDEATKYALERKTFGKLIAEHQAVSFMLADMAMKVELARLAYQRAAWEVDSG--RRNTYYASIAKAFA 321

                       330       340       350       360       370
                ....*....|....*....|....*....|....*....|....*....|....*..
gi 21361497 387 SEAAWQCVSEALQILGGLGYTRDYPYERILRDTRILLIFEGTNEILRMYIALTGLQH 443
Cdd:cd01157 322 ADIANQLATDAVQIFGGNGFNSEYPVEKLMRDAKIYQIYEGTSQIQRLIISREHLGK 378
PTZ00461 PTZ00461
isovaleryl-CoA dehydrogenase; Provisional
 74-430 2.18e-68

isovaleryl-CoA dehydrogenase; Provisional


Pssm-ID: 185640 [Multi-domain]  Cd Length: 410  Bit Score: 228.28  E-value: 2.18e-68
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21361497   74 VEKFFTEEVD--SRKIDQEGKIPDETLEKLKSLGLFGLQVPEEYGGLGFSNTMYSRLG-EIISMDGSITVTLAAHQAIGL 150
Cdd:PTZ00461  48 VAKFSREVVDkhAREDDINMHFNRDLFKQLGDLGVMGVTVPEADGGAGMDAVAAVIIHhELSKYDPGFCLAYLAHSMLFV 127

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21361497  151 KGIILAGTEEQKAKYLPKLASGEHIAAFCLTEPASGSDAASIRSRATLSEDKKhYILNGSKVWITNGGLANIFTVFAKte 230
Cdd:PTZ00461 128 NNFYYSASPAQRARWLPKVLTGEHVGAMGMSEPGAGTDVLGMRTTAKKDSNGN-YVLNGSKIWITNGTVADVFLIYAK-- 204

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21361497  231 vvdsdgsVKDKITAFIVERDFGGVTNGKPEDKLGIRGSNTCEVHFENTKIPVENILGEVGDGFKVAMNILNSGRFSMGSV 310
Cdd:PTZ00461 205 -------VDGKITAFVVERGTKGFTQGPKIDKCGMRASHMCQLFFEDVVVPAENLLGEEGKGMVGMMRNLELERVTLAAM 277

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21361497  311 VAGLLKRLIEMTAEYACTRKQFNKRLSEFGLIQEKFALMAQKAYVMESMTYLTAGMLdQPGFPDcSIEAAMVKVFSSEAA 390
Cdd:PTZ00461 278 AVGIAERSVELMTSYASERKAFGKPISNFGQIQRYIAEGYADTEAAKALVYSVSHNV-HPGNKN-RLGSDAAKLFATPIA 355

                        330       340       350       360
                 ....*....|....*....|....*....|....*....|
gi 21361497  391 WQCVSEALQILGGLGYTRDYPYERILRDTRILLIFEGTNE 430
Cdd:PTZ00461 356 KKVADSAIQVMGGMGYSRDMPVERLWRDAKLLEIGGGTIE 395
GCD cd01151
Glutaryl-CoA dehydrogenase; Glutaryl-CoA dehydrogenase (GCD). GCD is an acyl-CoA dehydrogenase, ...
 74-442 2.56e-68

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: 227.24  E-value: 2.56e-68
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21361497  74 VEKFFTEEVDSRKID--QEGKIPDETLEKLKSLGLFGLQvPEEYGGLGFSNTMYSRLG-EIISMDGSITVTLAAHQAIGL 150
Cdd:cd01151  24 AREFCQEELAPRVLEayREEKFDRKIIEEMGELGLLGAT-IKGYGCAGLSSVAYGLIArEVERVDSGYRSFMSVQSSLVM 102

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21361497 151 KGIILAGTEEQKAKYLPKLASGEHIAAFCLTEPASGSDAASIRSRATlsEDKKHYILNGSKVWITNGGLANIFTVFAKTE 230
Cdd:cd01151 103 LPIYDFGSEEQKQKYLPKLASGELIGCFGLTEPNHGSDPGGMETRAR--KDGGGYKLNGSKTWITNSPIADVFVVWARND 180

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21361497 231 vvdsdgsVKDKITAFIVERDFGGVTNGKPEDKLGIRGSNTCEVHFENTKIPVENILGEVgDGFKVAMNILNSGRFSMGSV 310
Cdd:cd01151 181 -------ETGKIRGFILERGMKGLSAPKIQGKFSLRASITGEIVMDNVFVPEENLLPGA-EGLRGPFKCLNNARYGIAWG 252

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21361497 311 VAGLLKRLIEMTAEYACTRKQFNKRLSEFGLIQEKFALMAQKAYVMESMTYLTAGMLDQPGF-PDcsiEAAMVKVFSSEA 389
Cdd:cd01151 253 ALGAAEDCYHTARQYVLDRKQFGRPLAAFQLVQKKLADMLTEIALGLLACLRVGRLKDQGKAtPE---QISLLKRNNCGK 329

                       330       340       350       360       370
                ....*....|....*....|....*....|....*....|....*....|....*
gi 21361497 390 AWQCVSEALQILGGLGYTRDYPYERILRDTRILLIFEGTNEI--LRMYIALTGLQ 442
Cdd:cd01151 330 ALEIARTAREMLGGNGISDEYHIIRHMVNLESVNTYEGTHDIhaLILGRAITGIQ 384
ACAD_fadE5 cd01153
Putative acyl-CoA dehydrogenases similar to fadE5; Putative acyl-CoA dehydrogenase (ACAD). ...
 85-431 1.23e-63

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: 215.33  E-value: 1.23e-63
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21361497  85 RKIDQEG--------KIPDETLEKLKSL---GLFGLQVPEEYGGLGFSNTMYSRLGEIISM-DGSITVTLAAHQAIglKG 152
Cdd:cd01153  18 ADGDREGpvfddgrvVVPPPFKEALDAFaeaGWMALGVPEEYGGQGLPITVYSALAEIFSRgDAPLMYASGTQGAA--AT 95

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21361497 153 IILAGTEEQKAKYLPKLASGEHIAAFCLTEPASGSDAASIRSRATLSEDKKHYIlNGSKVWITNG---GLANIF-TVFAK 228
Cdd:cd01153  96 LLAHGTEAQREKWIPRLAEGEWTGTMCLTEPDAGSDLGALRTKAVYQADGSWRI-NGVKRFISAGehdMSENIVhLVLAR 174

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21361497 229 TEVVDSDgsVKDkITAFIV-ERDFGGVTNG----KPEDKLGIRGSNTCEVHFENTKIPvenILGEVGDGFKVAMNILNSG 303
Cdd:cd01153 175 SEGAPPG--VKG-LSLFLVpKFLDDGERNGvtvaRIEEKMGLHGSPTCELVFDNAKGE---LIGEEGMGLAQMFAMMNGA 248

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21361497 304 RFSMGSVVAGLLKRLIEMTAEYACTRKQFNKRLSEFGLIQE------KFALMAQKAYVMES--MTYLTAGMLDQPGFPDC 375
Cdd:cd01153 249 RLGVGTQGTGLAEAAYLNALAYAKERKQGGDLIKAAPAVTIihhpdvRRSLMTQKAYAEGSraLDLYTATVQDLAERKAT 328

                       330       340       350       360       370       380
                ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 21361497 376 SIEAA------------MVKVFSSEAAWQCVSEALQILGGLGYTRDYPYERILRDTRILLIFEGTNEI 431
Cdd:cd01153 329 EGEDRkalsaladlltpVVKGFGSEAALEAVSDAIQVHGGSGYTREYPIEQYYRDARITTIYEGTTGI 396
PRK12341 PRK12341
acyl-CoA dehydrogenase;
74-437 1.77e-53

acyl-CoA dehydrogenase;


Pssm-ID: 183454 [Multi-domain]  Cd Length: 381  Bit Score: 187.24  E-value: 1.77e-53
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21361497   74 VEKFFTEEvDSRKIDQEGKIPDETLEKLKSLGLFGLQVPEEYGGLGFSN-TMYSRLGEIISMDGSITVTlaaHQAIGLKG 152
Cdd:PRK12341  20 ITRNFPEE-YFRTCDENGTYPREFMRALADNGISMLGVPEEFGGTPADYvTQMLVLEEVSKCGAPAFLI---TNGQCIHS 95

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21361497  153 IILAGTEEQKAK-YLPKLASGEhiAAFCL--TEPASGSDAASIRSRATlSEDKKHYiLNGSKVWITNGGLANIFTVFAKt 229
Cdd:PRK12341  96 MRRFGSAEQLRKtAESTLETGD--PAYALalTEPGAGSDNNSATTTYT-RKNGKVY-LNGQKTFITGAKEYPYMLVLAR- 170

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21361497  230 evvDSDGSVKDK-ITAFIVERDFGGVTNgKPEDKLGIRGSNTCEVHFENTKIPVENILGEVGDGFKVAMNILNSGRFSMG 308
Cdd:PRK12341 171 ---DPQPKDPKKaFTLWWVDSSKPGIKI-NPLHKIGWHMLSTCEVYLDNVEVEESDLVGEEGMGFLNVMYNFEMERLINA 246

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21361497  309 SVVAGLLKRLIEMTAEYACTRKQFNKRLSEFGLIQEKFALMAQKAYVMESMTYLTAGMLDQpGFPdCSIEAAMVKVFSSE 388
Cdd:PRK12341 247 ARSLGFAECAFEDAARYANQRIQFGKPIGHNQLIQEKLTLMAIKIENMRNMVYKVAWQADN-GQS-LRTSAALAKLYCAR 324

                        330       340       350       360
                 ....*....|....*....|....*....|....*....|....*....
gi 21361497  389 AAWQCVSEALQILGGLGYTRDYPYERILRDTRILLIFEGTNEILrMYIA 437
Cdd:PRK12341 325 TAMEVIDDAIQIMGGLGYTDEARVSRFWRDVRCERIGGGTDEIM-IYIA 372
ACAD_fadE6_17_26 cd01152
Putative acyl-CoA dehydrogenases similar to fadE6, fadE17, and fadE26; Putative acyl-CoA ...
 100-442 2.03e-50

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: 179.08  E-value: 2.03e-50
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21361497 100 KLKSLGLFGLQVPEEYGGLGFS-------NTMYSRLGEIISMdGSITVTLAAHqaiglkgIILA-GTEEQKAKYLPKLAS 171
Cdd:cd01152  43 ALAAAGWAAPGWPKEYGGRGASlmeqlifREEMAAAGAPVPF-NQIGIDLAGP-------TILAyGTDEQKRRFLPPILS 114

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21361497 172 GEHIaaFCL--TEPASGSDAASIRSRATLSEDkkHYILNGSKVWITNGGLANIFTVFAKTevvdsDGSVK--DKITAFIV 247
Cdd:cd01152 115 GEEI--WCQgfSEPGAGSDLAGLRTRAVRDGD--DWVVNGQKIWTSGAHYADWAWLLVRT-----DPEAPkhRGISILLV 185

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21361497 248 ERDFGGVT-------NGKPEdklgirgsnTCEVHFENTKIPVENILGEVGDGFKVAMNILNSGRFSMGSVVAGLLKRLIe 320
Cdd:cd01152 186 DMDSPGVTvrpirsiNGGEF---------FNEVFLDDVRVPDANRVGEVNDGWKVAMTTLNFERVSIGGSAATFFELLL- 255

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21361497 321 mtaEYACTRKQFNKRLSEFGLIQEKFALMAQKAYVMESMTYLTAGMLDQPGFPDcsIEAAMVKVFSSEAAwQCVSE-ALQ 399
Cdd:cd01152 256 ---ARLLLLTRDGRPLIDDPLVRQRLARLEAEAEALRLLVFRLASALAAGKPPG--AEASIAKLFGSELA-QELAElALE 329

                       330       340       350       360       370
                ....*....|....*....|....*....|....*....|....*....|.
gi 21361497 400 ILGGLGYTRDYP--------YERILRDTRILLIFEGTNEILRMYIALTGLQ 442
Cdd:cd01152 330 LLGTAALLRDPApgaelagrWEADYLRSRATTIYGGTSEIQRNIIAERLLG 380
PRK03354 PRK03354
crotonobetainyl-CoA dehydrogenase; Validated
 75-442 1.27e-49

crotonobetainyl-CoA dehydrogenase; Validated


Pssm-ID: 179566 [Multi-domain]  Cd Length: 380  Bit Score: 176.95  E-value: 1.27e-49
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21361497   75 EKFFTEevdsrkIDQEGKIPDETLEKLKSLGLFGLQVPEEYGGLGFSNTMYSRLGEIISMDGSITVTLaaHQ-AIGLKGI 153
Cdd:PRK03354  26 EAYFAE------CDRDSVYPERFVKALADMGIDSLLIPEEHGGLDAGFVTLAAVWMELGRLGAPTYVL--YQlPGGFNTF 97

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21361497  154 ILAGTEEQKAKYLPKLASGEHIAAFCLTEPASGSDAASIRSRATlSEDKKHYiLNGSKVWITNGGLANIFTVFAKtevvD 233
Cdd:PRK03354  98 LREGTQEQIDKIMAFRGTGKQMWNSAITEPGAGSDVGSLKTTYT-RRNGKVY-LNGSKCFITSSAYTPYIVVMAR----D 171

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21361497  234 SDGSVKDKITAFIVERDFGGVTNGKPEdKLGIRGSNTCEVHFENTKIPVENILGEVGDGFKVAMNILNSGRFSMGSVVAG 313
Cdd:PRK03354 172 GASPDKPVYTEWFVDMSKPGIKVTKLE-KLGLRMDSCCEITFDDVELDEKDMFGREGNGFNRVKEEFDHERFLVALTNYG 250

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21361497  314 LLKRLIEMTAEYACTRKQFNKRLSEFGLIQEKFALMAQKAYVMESMTYLTAGMLDQPGFPdcSIEAAMVKVFSSEAAWQC 393
Cdd:PRK03354 251 TAMCAFEDAARYANQRVQFGEAIGRFQLIQEKFAHMAIKLNSMKNMLYEAAWKADNGTIT--SGDAAMCKYFCANAAFEV 328

                        330       340       350       360
                 ....*....|....*....|....*....|....*....|....*....
gi 21361497  394 VSEALQILGGLGYTRDYPYERILRDTRILLIFEGTNEilrMYIALTGLQ 442
Cdd:PRK03354 329 VDSAMQVLGGVGIAGNHRISRFWRDLRVDRVSGGSDE---MQILTLGRA 374
ACAD_FadE2 cd01155
Acyl-CoA dehydrogenases similar to fadE2; FadE2-like Acyl-CoA dehydrogenase (ACAD). Acyl-CoA ...
 73-442 6.85e-46

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: 167.18  E-value: 6.85e-46
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21361497  73 PVEKFFTEEVdsRKIDQEGKIPDETLEKLK----SLGLFGLQVPEEYGGLGFSNTMYSRLGEII--SMDGSITVTLAAHQ 146
Cdd:cd01155  20 PAEQEFLEYY--AEGGDRWWTPPPIIEKLKakakAEGLWNLFLPEVSGLSGLTNLEYAYLAEETgrSFFAPEVFNCQAPD 97

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21361497 147 AIGLKGIILAGTEEQKAKYLPKLASGEHIAAFCLTEPA-SGSDAASIRsrATLSEDKKHYILNGSKVWITNGG--LANIF 223
Cdd:cd01155  98 TGNMEVLHRYGSEEQKKQWLEPLLDGKIRSAFAMTEPDvASSDATNIE--CSIERDGDDYVINGRKWWSSGAGdpRCKIA 175

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21361497 224 TVFAKTevvDSDGSVKDKITAFI-VERDFGGVTNGKPedkLGIRGSNT-----CEVHFENTKIPVENILGEVGDGFKVAM 297
Cdd:cd01155 176 IVMGRT---DPDGAPRHRQQSMIlVPMDTPGVTIIRP---LSVFGYDDaphghAEITFDNVRVPASNLILGEGRGFEIAQ 249

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21361497 298 NILNSGRF--SMGSVvaGLLKRLIEMTAEYACTRKQFNKRLSEFGLIQEKFAlmaqKAYVMESMTYL----TAGMLDQPG 371
Cdd:cd01155 250 GRLGPGRIhhCMRLI--GAAERALELMCQRAVSREAFGKKLAQHGVVAHWIA----KSRIEIEQARLlvlkAAHMIDTVG 323

                       330       340       350       360       370       380       390
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 21361497 372 FPDCSIEAAMVKVFSSEAAWQCVSEALQILGGLGYTRDYPYERILRDTRILLIFEGTNEILRMYIALTGLQ 442
Cdd:cd01155 324 NKAARKEIAMIKVAAPRMALKIIDRAIQVHGAAGVSQDTPLANMYAWARTLRIADGPDEVHLRSIARMELK 394
Acyl-CoA_dh_1 pfam00441
Acyl-CoA dehydrogenase, C-terminal domain; C-terminal domain of Acyl-CoA dehydrogenase is an ...
 290-437 5.13e-44

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: 153.95  E-value: 5.13e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21361497   290 GDGFKVAMNILNSGRFSMGSVVAGLLKRLIEMTAEYACTRKQFNKRLSEFGLIQEKFALMAQKAYVMESMTYLTAGMLDQ 369
Cdd:pfam00441   1 GRGFRVAMETLNHERLAIAAMALGLARRALDEALAYARRRKAFGRPLIDFQLVRHKLAEMAAEIEAARLLVYRAAEALDA 80

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 21361497   370 pGFPDcSIEAAMVKVFSSEAAWQCVSEALQILGGLGYTRDYPYERILRDTRILLIFEGTNEILRMYIA 437
Cdd:pfam00441  81 -GGPD-GAEASMAKLYASEAAVEVADLAMQLHGGYGYLREYPVERLYRDARVLRIGEGTSEIQRNIIA 146
fadE PRK09463
acyl-CoA dehydrogenase; Reviewed
 41-405 2.56e-43

acyl-CoA dehydrogenase; Reviewed


Pssm-ID: 236528 [Multi-domain]  Cd Length: 777  Bit Score: 166.15  E-value: 2.56e-43
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21361497   41 KELFLGK--IKKKEVFPFPEVSQDElneinQ-FL-GPVEKFfTEEVDSRKIDQE-GKIPDETLEKLKSLGLFGLQVPEEY 115
Cdd:PRK09463  59 GELFSGKpdWKKLLNYPKPTLTAEE-----QaFLdGPVEEL-CRMVNDWQITHElADLPPEVWQFIKEHGFFGMIIPKEY 132

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21361497  116 GGLGFSNTMYSR-LGEIISMDGSITVTLAAHQAIGlKGIILA--GTEEQKAKYLPKLASGEHIAAFCLTEPASGSDAASI 192
Cdd:PRK09463 133 GGLEFSAYAHSRvLQKLASRSGTLAVTVMVPNSLG-PGELLLhyGTDEQKDHYLPRLARGEEIPCFALTSPEAGSDAGSI 211

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21361497  193 RS-----RATLSEDKKHYI-LNGSKVWITnggLANIFTVFA---KteVVDSDGSVKDK----ITAFIVERDFGGVTNGKP 259
Cdd:PRK09463 212 PDtgvvcKGEWQGEEVLGMrLTWNKRYIT---LAPIATVLGlafK--LYDPDGLLGDKedlgITCALIPTDTPGVEIGRR 286

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21361497  260 EDKLGirgsntceVHFEN--TK-----IPVENILGE---VGDGFKVAMNILNSGR-FSMGSVVAGLLKRLIEMTAEYACT 328
Cdd:PRK09463 287 HFPLN--------VPFQNgpTRgkdvfIPLDYIIGGpkmAGQGWRMLMECLSVGRgISLPSNSTGGAKLAALATGAYARI 358

                        330       340       350       360       370       380       390
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 21361497  329 RKQFNKRLSEFGLIQEKFALMAQKAYVMESMTYLTAGMLDQPGFPdcSIEAAMVKVFSSEAAWQCVSEALQILGGLG 405
Cdd:PRK09463 359 RRQFKLPIGKFEGIEEPLARIAGNAYLMDAARTLTTAAVDLGEKP--SVLSAIAKYHLTERGRQVINDAMDIHGGKG 433
PRK13026 PRK13026
acyl-CoA dehydrogenase; Reviewed
 20-405 1.70e-39

acyl-CoA dehydrogenase; Reviewed


Pssm-ID: 237277 [Multi-domain]  Cd Length: 774  Bit Score: 154.73  E-value: 1.70e-39
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21361497   20 LVVSTANRRLLRTSPPVRAFAK-----------------------ELFLGK--IKKKEVFPFPEVSQDElneiNQFL-GP 73
Cdd:PRK13026  14 LVFAVKPLRRQFITRPVFKFFKkvlpplsdtereameagdvwwegELFSGKpdWQKLHSYPKPTLTAEE----QAFIdNE 89

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21361497   74 VEKFFTEeVDSRKIDQEGK-IPDETLEKLKSLGLFGLQVPEEYGGLGFSNTMYSRL-GEIISMDGSITVTLAAHQAIGlK 151
Cdd:PRK13026  90 VETLLTM-LDDWDIVQNRKdLPPEVWDYLKKEGFFALIIPKEYGGKGFSAYANSTIvSKIATRSVSAAVTVMVPNSLG-P 167

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21361497  152 GIILA--GTEEQKAKYLPKLASGEHIAAFCLTEPASGSDAASIRSRATLSE---DKKHYI---LNGSKVWITnggLANIF 223
Cdd:PRK13026 168 GELLThyGTQEQKDYWLPRLADGTEIPCFALTGPEAGSDAGAIPDTGIVCRgefEGEEVLglrLTWDKRYIT---LAPVA 244

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21361497  224 TV----FaktEVVDSDGSVKDK----ITAFIVERDFGGVTNGKPEDKLGIR---GSNTCEVHFentkIPVENILG---EV 289
Cdd:PRK13026 245 TVlglaF---KLRDPDGLLGDKkelgITCALIPTDHPGVEIGRRHNPLGMAfmnGTTRGKDVF----IPLDWIIGgpdYA 317

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21361497  290 GDGFKVAMNILNSGR-FSMGSVVAGLLKRLIEMTAEYACTRKQFNKRLSEFGLIQEKFALMAQKAYVMESMTYLTAGMLD 368
Cdd:PRK13026 318 GRGWRMLVECLSAGRgISLPALGTASGHMATRTTGAYAYVRRQFGMPIGQFEGVQEALARIAGNTYLLEAARRLTTTGLD 397

                        410       420       430
                 ....*....|....*....|....*....|....*..
gi 21361497  369 QPGFPdcSIEAAMVKVFSSEAAWQCVSEALQILGGLG 405
Cdd:PRK13026 398 LGVKP--SVVTAIAKYHMTELARDVVNDAMDIHAGKG 432
PLN02526 PLN02526
acyl-coenzyme A oxidase
 89-431 2.71e-37

acyl-coenzyme A oxidase


Pssm-ID: 178141 [Multi-domain]  Cd Length: 412  Bit Score: 143.45  E-value: 2.71e-37
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21361497   89 QEGKIPDETLEKLKSLGLFGLQVpEEYGGLGFSNTMYS-RLGEIISMDGSITVTLAAHQAIGLKGIILAGTEEQKAKYLP 167
Cdd:PLN02526  57 EKAEFPFHIIPKLGSLGIAGGTI-KGYGCPGLSITASAiATAEVARVDASCSTFILVHSSLAMLTIALCGSEAQKQKYLP 135

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21361497  168 KLASGEHIAAFCLTEPASGSDAASIRSRATLSEDKkhYILNGSKVWITNGGLANIFTVFAKTevvdsdgSVKDKITAFIV 247
Cdd:PLN02526 136 SLAQLDTVACWALTEPDYGSDASSLNTTATKVEGG--WILNGQKRWIGNSTFADVLVIFARN-------TTTNQINGFIV 206

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21361497  248 ERDFGGVTNGKPEDKLGIRGSNTCEVHFENTKIPVENILGEVgDGFKVAMNILNSGRFSMGSVVAGLLKRLIEMTAEYAC 327
Cdd:PLN02526 207 KKGAPGLKATKIENKIGLRMVQNGDIVLKDVFVPDEDRLPGV-NSFQDTNKVLAVSRVMVAWQPIGISMGVYDMCHRYLK 285

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21361497  328 TRKQFNKRLSEFGLIQEKFALMAQKAYVMESM------TYLTAGMldQPGfpdcsiEAAMVKVFSSEAAWQCVSEALQIL 401
Cdd:PLN02526 286 ERKQFGAPLAAFQINQEKLVRMLGNIQAMFLVgwrlckLYESGKM--TPG------HASLGKAWITKKARETVALGRELL 357

                        330       340       350
                 ....*....|....*....|....*....|
gi 21361497  402 GGLGYTRDYPYERILRDTRILLIFEGTNEI 431
Cdd:PLN02526 358 GGNGILADFLVAKAFCDLEPIYTYEGTYDI 387
AidB cd01154
Proteins involved in DNA damage response, similar to the AidB gene product; AidB is one of ...
 138-432 1.00e-33

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: 133.65  E-value: 1.00e-33
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21361497 138 ITVTLAAhqaigLKGIILAGTEEQKaKYLPKLASGEH----IAAFCLTEPASGSDAASIRSRATLSEDKKhYILNGSKvW 213
Cdd:cd01154 113 LTMTDAA-----VYALRKYGPEELK-QYLPGLLSDRYktglLGGTWMTEKQGGSDLGANETTAERSGGGV-YRLNGHK-W 184

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21361497 214 ITNGGLANIFTVFAKTEvvDSDGSVKDkITAFIVER-DFGGVTNG----KPEDKLGIRGSNTCEVHFENTkipVENILGE 288
Cdd:cd01154 185 FASAPLADAALVLARPE--GAPAGARG-LSLFLVPRlLEDGTRNGyrirRLKDKLGTRSVATGEVEFDDA---EAYLIGD 258

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21361497 289 VGDGFKVAMNILNSGRFSMGSVVAGLLKRLIEMTAEYACTRKQFNKRLSEFGLIQEKFALMAQKAYVMESMTYLTAGMLD 368
Cdd:cd01154 259 EGKGIYYILEMLNISRLDNAVAALGIMRRALSEAYHYARHRRAFGKPLIDHPLMRRDLAEMEVDVEAATALTFRAARAFD 338

                       250       260       270       280       290       300       310
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 21361497 369 QPGfPDCSIEAAMVKVFS-------SEAAWQCVSEALQILGGLGYTRDYPYERILRDTRILLIFEGTNEIL 432
Cdd:cd01154 339 RAA-ADKPVEAHMARLATpvakliaCKRAAPVTSEAMEVFGGNGYLEEWPVARLHREAQVTPIWEGTGNIQ 408
PTZ00456 PTZ00456
acyl-CoA dehydrogenase; Provisional
 8-431 2.05e-31

acyl-CoA dehydrogenase; Provisional


Pssm-ID: 185635 [Multi-domain]  Cd Length: 622  Bit Score: 129.60  E-value: 2.05e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21361497    8 LRTTAAARACRGLVVSTANRRLLRTSPPVR--AFAKELFLGKIKKKEVFPFPEVSQDELNEInqfLGPVEKFFTE----- 80
Cdd:PTZ00456   2 FRRVCSSAAASHAAAVSASARSLQYQPRIRdvQFLVEEVFNMYDHYEKLGKTDVTKELMDSL---LEEASKLATQtllpl 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21361497   81 ----EVDSRKIDQEGKIP-----DETLEKLKSLGLFGLQVPEEYGGLGFSNTMYSRLGEIISMdGSITVTLAAHQAIG-L 150
Cdd:PTZ00456  79 yessDSEGCVLLKDGNVTtpkgfKEAYQALKAGGWTGISEPEEYGGQALPLSVGFITRELMAT-ANWGFSMYPGLSIGaA 157

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21361497  151 KGIILAGTEEQKAKYLPKLASGEHIAAFCLTEPASGSDAASIRSRATLSEDKKhYILNGSKVWITNGG---LANI-FTVF 226
Cdd:PTZ00456 158 NTLMAWGSEEQKEQYLTKLVSGEWSGTMCLTEPQCGTDLGQVKTKAEPSADGS-YKITGTKIFISAGDhdlTENIvHIVL 236

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21361497  227 AKTEvvDSDGSVKDkITAFIVER----DFGGVTNGKP------EDKLGIRGSNTCEVHFENTkipVENILGEVGDGFKVA 296
Cdd:PTZ00456 237 ARLP--NSLPTTKG-LSLFLVPRhvvkPDGSLETAKNvkciglEKKMGIKGSSTCQLSFENS---VGYLIGEPNAGMKQM 310

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21361497  297 MNILNSGRfsMGSVVAGLLKRLIEMTAEYACTRKQFNKRLSEFGLIQEKFA------------LMAQKAyVME---SMTY 361
Cdd:PTZ00456 311 FTFMNTAR--VGTALEGVCHAELAFQNALRYARERRSMRALSGTKEPEKPAdriichanvrqnILFAKA-VAEggrALLL 387

                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21361497  362 LTAGMLD-QPGFPDCSIEAAM----------VKVFSSEAAWQCVSEALQILGGLGYTRDYPYERILRDTRILLIFEGTNE 430
Cdd:PTZ00456 388 DVGRLLDiHAAAKDAATREALdheigfytpiAKGCLTEWGVEAASRCLQVWGGHGYIKGNGMEQILRDARIGTLYEGTTG 467


                 .
gi 21361497  431 I 431
Cdd:PTZ00456 468 I 468
Acyl-CoA_dh_N pfam02771
Acyl-CoA dehydrogenase, N-terminal domain; The N-terminal domain of Acyl-CoA dehydrogenase is ...
 74-173 3.68e-29

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: 111.79  E-value: 3.68e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21361497    74 VEKFFTEEV--DSRKIDQEGKIPDETLEKLKSLGLFGLQVPEEYGGLGFSNTMYSRLGEIISM-DGSITVTLAAHQAIGL 150
Cdd:pfam02771  11 VREFAEEEIapHAAEWDEEGEFPRELWKKLGELGLLGITIPEEYGGAGLDYLAYALVAEELARaDASVALALSVHSSLGA 90

                          90       100
                  ....*....|....*....|...
gi 21361497   151 KGIILAGTEEQKAKYLPKLASGE 173
Cdd:pfam02771  91 PPILRFGTEEQKERYLPKLASGE 113
Acyl-CoA_dh_M pfam02770
Acyl-CoA dehydrogenase, middle domain; Central domain of Acyl-CoA dehydrogenase has a ...
 177-276 5.10e-28

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: 107.75  E-value: 5.10e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21361497   177 AFCLTEPASGSDAASIRSRAtLSEDKKHYILNGSKVWITNGGLANIFTVFAKTEvvdsDGSVKDKITAFIVERDFGGVTN 256
Cdd:pfam02770   1 AFALTEPGAGSDVASLKTTA-ADGDGGGWVLNGTKWWITNAGIADLFLVLARTG----GDDRHGGISLFLVPKDAPGVSV 75

                          90       100
                  ....*....|....*....|
gi 21361497   257 GKPEDKLGIRGSNTCEVHFE 276
Cdd:pfam02770  76 RRIETKLGVRGLPTGELVFD 95
PTZ00457 PTZ00457
acyl-CoA dehydrogenase; Provisional
 27-571 2.17e-27

acyl-CoA dehydrogenase; Provisional


Pssm-ID: 185636 [Multi-domain]  Cd Length: 520  Bit Score: 116.52  E-value: 2.17e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21361497   27 RRLLRTSP--PVR--AFAKELFLGKIKKKEVFPFPevsqdelneinqflgpvekffteevdSRKID-QEGKIPDETLEKL 101
Cdd:PTZ00457   2 RRRFSSAPrqYVRhaSYAAGLFNFKIVPEEMFPYP--------------------------CRKLDgDEAENLQSLLEQI 55

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21361497  102 KSLG-----LFGLQVPEEYGGLGFSNTMYSRLGEIISMDGsITVTLAAHQAIGLKGIILA--GTEEQKAKYLPKLASGEH 174
Cdd:PTZ00457  56 RSNDkilgnLYGARIATEYGGLGLGHTAHALIYEEVGTNC-DSKLLSTIQHSGFCTYLLStvGSKELKGKYLTAMSDGTI 134

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21361497  175 IAAFClTEPASGSDAASIRSRATLSEDKKhYILNGSKvWITNGGLANIFTVFAKT---EVVDSDGSVKDKITAFIVERDF 251
Cdd:PTZ00457 135 MMGWA-TEEGCGSDISMNTTKASLTDDGS-YVLTGQK-RCEFAASATHFLVLAKTltqTAAEEGATEVSRNSFFICAKDA 211

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21361497  252 GGVTngkpedklgIRGSNtceVHFENTkiPVENILGEVGDGFKVAMNILNSGRFSMGSVVAGLLKRLIEmtaeyactrkQ 331
Cdd:PTZ00457 212 KGVS---------VNGDS---VVFENT--PAADVVGVVGEGFKDAMITLFTEQYLYAASLLGIMKRVVQ----------E 267

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21361497  332 FNKRLSEFGlIQEKFALMAQKAYVMESMTYLTAGMLDQPGfPDCSIEAAMVKVFSSEAawqcVSEALQILgGLGYTRDYP 411
Cdd:PTZ00457 268 LRGSNAEEG-ATDTVASFACAMYAMESTLYALTANLDLPT-EDSLLECTLVSAFVQST----TNQLLSIL-ETATPPSTT 340

                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21361497  412 YERILRDTRILLIFEGTNEILRMYIALTGLQHAG----RILTTRIHELKQAKVSTVMDTVG-RRLRDSlgrtvdlgltgn 486
Cdd:PTZ00457 341 LEKCFANARLFLSMMESRDFLYSSAVCCGVEDYGlffqRASTLQMMQARTLRSLGVRDRVPiKNLPDC------------ 408

                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21361497  487 hgvvhpSLADSAnkfeenTYCFGRTVETLLLRFGKTIMEEQLVLKRVANILINLYGMTAVLSRASRSIRIGLRNHDHEVL 566
Cdd:PTZ00457 409 ------SLIDEA------VVAFGNAVEATFVRSGSQVPYQQLLLNRLGEAASLLYAASAVASRASMCVSKGLPSAKVEGE 476


                 ....*
gi 21361497  567 LANTF 571
Cdd:PTZ00457 477 LASAF 481
PLN02876 PLN02876
acyl-CoA dehydrogenase
 117-444 2.87e-20

acyl-CoA dehydrogenase


Pssm-ID: 215473 [Multi-domain]  Cd Length: 822  Bit Score: 95.25  E-value: 2.87e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21361497  117 GLGFSNTMYSRLGEII--SMDGSITVTLAAHQAIGLKGIILAGTEEQKAKYLPKLASGEHIAAFCLTEP-ASGSDAASIR 193
Cdd:PLN02876 491 GAGLSNLEYGYLCEIMgrSVWAPQVFNCGAPDTGNMEVLLRYGNKEQQLEWLIPLLEGKIRSGFAMTEPqVASSDATNIE 570

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21361497  194 srATLSEDKKHYILNGSKvWITNGGL---ANIFTVFAKTevvDSDGSVKDKITAFIVERDFGGVTNGKPEDKLGIRGS-- 268
Cdd:PLN02876 571 --CSIRRQGDSYVINGTK-WWTSGAMdprCRVLIVMGKT---DFNAPKHKQQSMILVDIQTPGVQIKRPLLVFGFDDAph 644

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21361497  269 NTCEVHFENTKIPVENI-LGEvGDGFKVAMNILNSGRFSMGSVVAGLLKRLIEMTAEYACTRKQFNKRLSEFGliqeKFA 347
Cdd:PLN02876 645 GHAEISFENVRVPAKNIlLGE-GRGFEIAQGRLGPGRLHHCMRLIGAAERGMQLMVQRALSRKAFGKLIAQHG----SFL 719

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21361497  348 LMAQKAYVMESMTYL----TAGMLDQPGFPDCSIEAAMVKVFSSEAAWQCVSEALQILGGLGYTRDYPYERILRDTRILL 423
Cdd:PLN02876 720 SDLAKCRVELEQTRLlvleAADQLDRLGNKKARGIIAMAKVAAPNMALKVLDMAMQVHGAAGVSSDTVLAHLWATARTLR 799

                        330       340
                 ....*....|....*....|.
gi 21361497  424 IFEGTNEILRMYIALTGLQHA 444
Cdd:PLN02876 800 IADGPDEVHLGTIAKLELQRA 820
AXO cd01150
Peroxisomal acyl-CoA oxidase; Peroxisomal acyl-CoA oxidases (AXO) catalyze the first set in ...
 99-462 1.67e-16

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: 83.15  E-value: 1.67e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21361497  99 EKLKSLGLFGLQVPEEYGGLGFSNTMYsrlgeiismDGSITVTLAAHQAIGLKGIILAGTEEQKAKYLPKLASGEHIAAF 178
Cdd:cd01150  68 TDVERMGELMADDPEKMLALTNSLGGY---------DLSLGAKLGLHLGLFGNAIKNLGTDEHQDYWLQGANNLEIIGCF 138

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21361497 179 CLTEPASGSDAASIRSRATLSEDKKHYILN-----GSKVWItnGGL---ANIFTVFAKTEVVDSDGSVKdkitAFIVE-R 249
Cdd:cd01150 139 AQTELGHGSNLQGLETTATYDPLTQEFVINtpdftATKWWP--GNLgktATHAVVFAQLITPGKNHGLH----AFIVPiR 212

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21361497 250 DFG------GVTNGKPEDKLGIRGSNTCEVHFENTKIPVENILGEVGD----------------GFKVAMNILNSGRFSM 307
Cdd:cd01150 213 DPKthqplpGVTVGDIGPKMGLNGVDNGFLQFRNVRIPRENLLNRFGDvspdgtyvspfkdpnkRYGAMLGTRSGGRVGL 292

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21361497 308 GSVVAGLLKRLIEMTAEYACTRKQFNKRLS-------EFGLIQEKFALMAQKAYV------------MESMTYLTAGMLD 368
Cdd:cd01150 293 IYDAAMSLKKAATIAIRYSAVRRQFGPKPSdpevqilDYQLQQYRLFPQLAAAYAfhfaakslvemyHEIIKELLQGNSE 372

                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21361497 369 QpgFPDCSIEAAMVKVFSSEAAWQCVSEALQILGGLGYTrDYPYERILR-DTRILLIFEGTNEILrmyialtgLQHAGRI 447
Cdd:cd01150 373 L--LAELHALSAGLKAVATWTAAQGIQECREACGGHGYL-AMNRLPTLRdDNDPFCTYEGDNTVL--------LQQTANY 441

                       410
                ....*....|....*
gi 21361497 448 LTTRIHELKQAKVST 462
Cdd:cd01150 442 LLKKYAQAFSLADYL 456
DszC cd01163
Dibenzothiophene (DBT) desulfurization enzyme C; DszC is a flavin reductase dependent enzyme, ...
 88-287 5.50e-15

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: 76.98  E-value: 5.50e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21361497  88 DQEGKIPDETLEKLKSLGLFGLQVPEEYGGLGFS-NTMYSRLGEIISMDGSITVTLAAHQAIgLKGIILAGTEEQKAKYL 166
Cdd:cd01163  18 DRQRGLPYEEVALLRQSGLGTLRVPKEYGGLGASlPDLYEVVRELAAADSNIAQALRAHFGF-VEALLLAGPEQFRKRWF 96

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21361497 167 PKLASGeHIAAFCLTEpaSGSDAASIRSRATLSEDkKHYILNGSKvWITNGGLaniFTVFAKTEVVDSDGsvkdKITAFI 246
Cdd:cd01163  97 GRVLNG-WIFGNAVSE--RGSVRPGTFLTATVRDG-GGYVLNGKK-FYSTGAL---FSDWVTVSALDEEG----KLVFAA 164

                       170       180       190       200
                ....*....|....*....|....*....|....*....|...
gi 21361497 247 VERDFGGVTNGKPEDKLGIR--GSNTceVHFENTKIPVENILG 287
Cdd:cd01163 165 VPTDRPGITVVDDWDGFGQRltASGT--VTFDNVRVEPDEVLP 205
PLN02636 PLN02636
acyl-coenzyme A oxidase
 133-437 1.47e-11

acyl-coenzyme A oxidase


Pssm-ID: 215342 [Multi-domain]  Cd Length: 686  Bit Score: 67.58  E-value: 1.47e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21361497  133 SMDGSITVTLAAHQAIGLKGIILAGTEEQKAKYLPKLASGEHIAAFCLTEPASGSDAASIRSRATLSEDKKHYILN---- 208
Cdd:PLN02636 132 SVDMSLGIKLGVQYSLWGGSVINLGTKKHRDKYFDGIDNLDYPGCFAMTELHHGSNVQGLQTTATFDPLTDEFVINtpnd 211

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21361497  209 -GSKVWITNGGLANIF-TVFAKTEVV--DSDGSVKDKITAFIVE-RDFG------GVTNGKPEDKLGIRGSNTCEVHFEN 277
Cdd:PLN02636 212 gAIKWWIGNAAVHGKFaTVFARLKLPthDSKGVSDMGVHAFIVPiRDMKthqvlpGVEIRDCGHKVGLNGVDNGALRFRS 291

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21361497  278 TKIPVENILGEVGD----------------GFKVAMNILNSGRFSMGSVVAGLLKRLIEMTAEYACTRKQFN-KRLSEFG 340
Cdd:PLN02636 292 VRIPRDNLLNRFGDvsrdgkytsslptinkRFAATLGELVGGRVGLAYGSVGVLKASNTIAIRYSLLRQQFGpPKQPEIS 371

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21361497  341 LI-----QEKFALMAQKAYVMESMT-YLT---AGML---DQPGFPDCSIEAAMVKVFSSEAAWQCVSEALQILGGLGYTR 408
Cdd:PLN02636 372 ILdyqsqQHKLMPMLASTYAFHFATeYLVerySEMKkthDDQLVADVHALSAGLKAYITSYTAKALSTCREACGGHGYAA 451

                        330       340
                 ....*....|....*....|....*....
gi 21361497  409 DYPYERILRDTRILLIFEGTNEILRMYIA 437
Cdd:PLN02636 452 VNRFGSLRNDHDIFQTFEGDNTVLLQQVA 480
PRK11561 PRK11561
isovaleryl CoA dehydrogenase; Provisional
 180-432 1.80e-11

isovaleryl CoA dehydrogenase; Provisional


Pssm-ID: 183199 [Multi-domain]  Cd Length: 538  Bit Score: 66.70  E-value: 1.80e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21361497  180 LTEPASGSDAASIRSRATLSEDKKhYILNGSKvWITNGGLANIFTVFAKTevvdsdgsvKDKITAFIVERDF-GGVTNG- 257
Cdd:PRK11561 184 MTEKQGGSDVLSNTTRAERLADGS-YRLVGHK-WFFSVPQSDAHLVLAQA---------KGGLSCFFVPRFLpDGQRNAi 252

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21361497  258 ---KPEDKLGIRGSNTCEVHFENTkipVENILGEVGDGFKvamNILNSG---RF--SMGSvvAGLLKRLIEMTAEYACTR 329
Cdd:PRK11561 253 rleRLKDKLGNRSNASSEVEFQDA---IGWLLGEEGEGIR---LILKMGgmtRFdcALGS--HGLMRRAFSVAIYHAHQR 324

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21361497  330 KQFNKRLSEFGLIQEkfaLMAQKAYVMESMTYLT---AGMLDQPGFPDcsiEAAMVKVFSSEAAWQ-C------VSEALQ 399
Cdd:PRK11561 325 QVFGKPLIEQPLMRQ---VLSRMALQLEGQTALLfrlARAWDRRADAK---EALWARLFTPAAKFViCkrgipfVAEAME 398

                        250       260       270
                 ....*....|....*....|....*....|...
gi 21361497  400 ILGGLGYTRDYPYERILRDTRILLIFEGTNEIL 432
Cdd:PRK11561 399 VLGGIGYCEESELPRLYREMPVNSIWEGSGNIM 431
Acyl-CoA_dh_2 pfam08028
Acyl-CoA dehydrogenase, C-terminal domain;
306-430 4.42e-09

Acyl-CoA dehydrogenase, C-terminal domain;


Pssm-ID: 429790 [Multi-domain]  Cd Length: 133  Bit Score: 55.04  E-value: 4.42e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21361497   306 SMGSVVAGLLKRLIEMTAEYACTRKQ--FNKRLSEFGLIQEKFALMA----QKAYVMESMTYLTAGMLDQ--PGFPDCSI 377
Cdd:pfam08028   1 GIAAAALGAARAALAEFTERARGRVRayFGVPLAEDPATQLALAEAAaridAARLLLERAAARIEAAAAAgkPVTPALRA 80

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|...
gi 21361497   378 EAAMVKVFSSEAAWQCVSEALQILGGLGYTRDYPYERILRDTRILLIFEGTNE 430
Cdd:pfam08028  81 EARRAAAFATELAVAAVDALFRAAGGSALFQDSPLQRIWRDIHAAAQHAAVNP 133
PTZ00460 PTZ00460
acyl-CoA dehydrogenase; Provisional
 143-547 3.67e-07

acyl-CoA dehydrogenase; Provisional


Pssm-ID: 185639 [Multi-domain]  Cd Length: 646  Bit Score: 53.31  E-value: 3.67e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21361497  143 AAHQAIGLKGIILAGTEEQKAKYLPKLASGEHIAAFCLTEPASGSDAASIRSRATLSEDKKHYILN-----GSKVWITN- 216
Cdd:PTZ00460  96 TVHFAMVIPAFQVLGTDEQINLWMPSLLNFEIVGCYAQTELGHGSDVQNLETTATYDKQTNEFVIHtpsveAVKFWPGEl 175

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21361497  217 GGLANIFTVFAKTEVvdsDGSVKDkITAFIVE-RDFG------GVTNGKPEDKLGIRGSNTCEVHFENTKIPVENIL--- 286
Cdd:PTZ00460 176 GFLCNFALVYAKLIV---NGKNKG-VHPFMVRiRDKEthkplqGVEVGDIGPKMGYAVKDNGFLSFDHYRIPLDSLLary 251

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21361497  287 ------GEV---GDGfKVAMNILNSGRFSMGSVVAGLLKRLIEMTAEYACTRKQFNK------RLSEFGLIQEK-FALMA 350
Cdd:PTZ00460 252 ikvsedGQVerqGNP-KVSYASMMYMRNLIIDQYPRFAAQALTVAIRYSIYRQQFTNdnkqenSVLEYQTQQQKlLPLLA 330

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21361497  351 QkAYVMeSMTYLTAGMLDQPGF-----PDCSIEAAMVKVFSSEAAW--QCVSEALQ----ILGGLGYTRDYPYERILRDT 419
Cdd:PTZ00460 331 E-FYAC-IFGGLKIKELVDDNFnrvqkNDFSLLQLTHAILSAAKANytYFVSNCAEwcrlSCGGHGYAHYSGLPAIYFDM 408

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21361497  420 RILLIFEGTNEILRMYIA---LTGLQHA-----------GRILT-----------TRIHELKQAKVSTVMDTVGRRLRDS 474
Cdd:PTZ00460 409 SPNITLEGENQIMYLQLArylLKQLQHAvqkpekvpeyfNFLSHitekladqttiESLGQLLGLNCTILTIYAAKKIMDH 488

                        410       420       430       440       450       460       470
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 21361497  475 LGRTVDLGLTGNHgVVHPSLADSANKFEEN-TYcfgrtvetllLRFGKTIMEEQLVLKRVANILINLYGMTAVL 547
Cdd:PTZ00460 489 INTGKDFQQSWDT-KSGIALASAASRFIEYfNY----------LCFLDTINNANKSTKEILTQLADLYGITMLL 551
PLN02443 PLN02443
acyl-coenzyme A oxidase
 157-406 9.33e-06

acyl-coenzyme A oxidase


Pssm-ID: 178062 [Multi-domain]  Cd Length: 664  Bit Score: 48.68  E-value: 9.33e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21361497  157 GTEEQKAKYLPKLASGEHIAAFCLTEPASGSDAASIRSRATLSEDKKHYILN-----GSKVWitNGGLANIFT---VFAK 228
Cdd:PLN02443 114 GTEEQQKKWLPLAYKMQIIGCYAQTELGHGSNVQGLETTATFDPKTDEFVIHsptltSSKWW--PGGLGKVSThavVYAR 191

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21361497  229 tevVDSDGsvKDK-ITAFIVE-------RDFGGVTNGKPEDKLGIRGSNTCE---VHFENTKIPVENILGEVG----DGF 293
Cdd:PLN02443 192 ---LITNG--KDHgIHGFIVQlrslddhSPLPGVTVGDIGMKFGNGAYNTMDngfLRFDHVRIPRDQMLMRLSkvtrEGK 266

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21361497  294 KVAMNI---LNSGR--FSMGSVVAG---LLKRLIEMTAEYACTRKQFNKRLS--EFGLIQEK------FALMAQkAY--- 354
Cdd:PLN02443 267 YVQSDVprqLVYGTmvYVRQTIVADastALSRAVCIATRYSAVRRQFGSQDGgpETQVIDYKtqqsrlFPLLAS-AYafr 345

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 21361497  355 -VMESMTYLTAGML------DQPGFPDCSIEAAMVKVFSSEAAWQCVSEALQILGGLGY 406
Cdd:PLN02443 346 fVGEWLKWLYTDVTqrleanDFSTLPEAHACTAGLKSLTTSATADGIEECRKLCGGHGY 404
PLN02312 PLN02312
acyl-CoA oxidase
 128-332 2.98e-05

acyl-CoA oxidase


Pssm-ID: 215178 [Multi-domain]  Cd Length: 680  Bit Score: 47.07  E-value: 2.98e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21361497  128 LGEIISM-DGSITVTLAAHQAIGLKGIILAGTEEQKAKYLPKLASGEHIAAFCLTEPASGSDAASIRSRATLSEDKKHYI 206
Cdd:PLN02312 138 LLEVIGIyDHSLAIKLGVHFFLWGGAIKFLGTKRHHDKWLKDTEDYVVKGCFAMTELGHGSNVRGIETVTTYDPKTEEFV 217

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21361497  207 LN-----GSKVWItnGGLANIFT---VFAKTEVvdsDGsVKDKITAFIVE-RDFGGVT--NGKPED---KLGIRGSNTCE 272
Cdd:PLN02312 218 INtpcesAQKYWI--GGAANHAThtiVFSQLHI---NG-KNEGVHAFIAQiRDQDGNIcpNIRIADcghKIGLNGVDNGR 291

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 21361497  273 VHFENTKIPVENILGEVGD----------------GFKVAMNILNSGRFSMGSVVAGLLKRLIEMTAEYACTRKQF 332
Cdd:PLN02312 292 IWFDNLRIPRENLLNSVADvspdgkyvsaikdpdqRFGAFLAPLTSGRVTIAVSAIYSSKVGLAIAIRYSLSRRAF 367
 
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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