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Conserved domains on  [gi|197313734|ref|NP_861433|]
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complex I assembly factor ACAD9, mitochondrial [Rattus norvegicus]

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

 Zoom to residue level

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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 ...
 42-449 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: 718.87  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 197313734  42 SFAKELFLGHIQQKGVFPFPEVSQEELSE-INQFVGPLEKFFNEEVDSRKIDQEGKIPADTLAKLKSLGLFGIQVPEEYG 120
Cdd:cd01161    1 SFALNMFLGDIVTKQVFPYPSVLTEEQTEeLNMLVGPVEKFFEEVNDPAKNDQLEKIPRKTLTQLKELGLFGLQVPEEYG 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 197313734 121 GLGLSNTMYARLGEIISMDASITVTLAAHQAIGLKGIILVGNEEQKAKYLPKLSSGEHIAAFCLTEPASGSDAASIQTRA 200
Cdd:cd01161   81 GLGLNNTQYARLAEIVGMDLGFSVTLGAHQSIGFKGILLFGTEAQKEKYLPKLASGEWIAAFALTEPSSGSDAASIRTTA 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 197313734 201 TLSEDKKYFVLNGSKVWITNGGLANIFTVFAKTEVVDSDGSIKDKMTAFIVERDFGGITNGKPEDKLGIRGSNTCEVHFE 280
Cdd:cd01161  161 VLSEDGKHYVLNGSKIWITNGGIADIFTVFAKTEVKDATGSVKDKITAFIVERSFGGVTNGPPEKKMGIKGSNTAEVYFE 240

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 197313734 281 NTRVPVENVLGEVGGGFKVAMNILNSGRFSMGSAVAGMLKKLIEQTAEYACTRKQFNRNLSEFGLIQEKFALMAQKAYVM 360
Cdd:cd01161  241 DVKIPVENVLGEVGDGFKVAMNILNNGRFGMGAALIGTMKRCIEKAVDYANNRKQFGKKIHEFGLIQEKLANMAILQYAT 320

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 197313734 361 ESMAYLTSGMLDQPGFPDCSIEAAMVKVFSSEAAWQCVSEALQILGGSGYMKDYPYERMLRDARILLIFEGTNEILRLFI 440
Cdd:cd01161  321 ESMAYMTSGNMDRGLKAEYQIEAAISKVFASEAAWLVVDEAIQIHGGMGFMREYGVERVLRDLRIFRIFEGTNEILRLFI 400


                 ....*....
gi 197313734 441 ALTGLQHAG 449
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 ...
 42-449 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: 718.87  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 197313734  42 SFAKELFLGHIQQKGVFPFPEVSQEELSE-INQFVGPLEKFFNEEVDSRKIDQEGKIPADTLAKLKSLGLFGIQVPEEYG 120
Cdd:cd01161    1 SFALNMFLGDIVTKQVFPYPSVLTEEQTEeLNMLVGPVEKFFEEVNDPAKNDQLEKIPRKTLTQLKELGLFGLQVPEEYG 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 197313734 121 GLGLSNTMYARLGEIISMDASITVTLAAHQAIGLKGIILVGNEEQKAKYLPKLSSGEHIAAFCLTEPASGSDAASIQTRA 200
Cdd:cd01161   81 GLGLNNTQYARLAEIVGMDLGFSVTLGAHQSIGFKGILLFGTEAQKEKYLPKLASGEWIAAFALTEPSSGSDAASIRTTA 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 197313734 201 TLSEDKKYFVLNGSKVWITNGGLANIFTVFAKTEVVDSDGSIKDKMTAFIVERDFGGITNGKPEDKLGIRGSNTCEVHFE 280
Cdd:cd01161  161 VLSEDGKHYVLNGSKIWITNGGIADIFTVFAKTEVKDATGSVKDKITAFIVERSFGGVTNGPPEKKMGIKGSNTAEVYFE 240

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 197313734 281 NTRVPVENVLGEVGGGFKVAMNILNSGRFSMGSAVAGMLKKLIEQTAEYACTRKQFNRNLSEFGLIQEKFALMAQKAYVM 360
Cdd:cd01161  241 DVKIPVENVLGEVGDGFKVAMNILNNGRFGMGAALIGTMKRCIEKAVDYANNRKQFGKKIHEFGLIQEKLANMAILQYAT 320

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 197313734 361 ESMAYLTSGMLDQPGFPDCSIEAAMVKVFSSEAAWQCVSEALQILGGSGYMKDYPYERMLRDARILLIFEGTNEILRLFI 440
Cdd:cd01161  321 ESMAYMTSGNMDRGLKAEYQIEAAISKVFASEAAWLVVDEAIQIHGGMGFMREYGVERVLRDLRIFRIFEGTNEILRLFI 400


                 ....*....
gi 197313734 441 ALTGLQHAG 449
Cdd:cd01161  401 ALTGLQHAG 409
CaiA COG1960
Acyl-CoA dehydrogenase related to the alkylation response protein AidB [Lipid transport and ...
 70-441 4.62e-146

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: 428.10  E-value: 4.62e-146
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 197313734  70 EINQFVGPLEKFFNEEVD--SRKIDQEGKIPADTLAKLKSLGLFGIQVPEEYGGLGLSNTMYARLGEIISM-DASITVTL 146
Cdd:COG1960    8 EQRALRDEVREFAEEEIApeAREWDREGEFPRELWRKLAELGLLGLTIPEEYGGLGLSLVELALVLEELARaDASLALPV 87

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 197313734 147 AAHqAIGLKGIILVGNEEQKAKYLPKLSSGEHIAAFCLTEPASGSDAASIQTRATLSEDKkyFVLNGSKVWITNGGLANI 226
Cdd:COG1960   88 GVH-NGAAEALLRFGTEEQKERYLPRLASGEWIGAFALTEPGAGSDAAALRTTAVRDGDG--YVLNGQKTFITNAPVADV 164

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 197313734 227 FTVFAKTEvvDSDGSikDKMTAFIVERDFGGITNGKPEDKLGIRGSNTCEVHFENTRVPVENVLGEVGGGFKVAMNILNS 306
Cdd:COG1960  165 ILVLARTD--PAAGH--RGISLFLVPKDTPGVTVGRIEDKMGLRGSDTGELFFDDVRVPAENLLGEEGKGFKIAMSTLNA 240

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 197313734 307 GRFSMGSAVAGMLKKLIEQTAEYACTRKQFNRNLSEFGLIQEKFALMAQKAYVMESMAYLTSGMLDQPGfpDCSIEAAMV 386
Cdd:COG1960  241 GRLGLAAQALGIAEAALELAVAYAREREQFGRPIADFQAVQHRLADMAAELEAARALVYRAAWLLDAGE--DAALEAAMA 318

                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 197313734 387 KVFSSEAAWQCVSEALQILGGSGYMKDYPYERMLRDARILLIFEGTNEILRLFIA 441
Cdd:COG1960  319 KLFATEAALEVADEALQIHGGYGYTREYPLERLYRDARILTIYEGTNEIQRLIIA 373
PLN02519 PLN02519
isovaleryl-CoA dehydrogenase
 73-440 2.86e-80

isovaleryl-CoA dehydrogenase


Pssm-ID: 215284 [Multi-domain]  Cd Length: 404  Bit Score: 259.42  E-value: 2.86e-80
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 197313734  73 QFVGPLEKFFNEEV--DSRKIDQEGKIPAD-TLAKLK-SLGLFGIQVPEEYGGLGLSNTMYA-RLGEIISMDASITVTLA 147
Cdd:PLN02519  32 QFKESVQQFAQENIapHAAAIDATNSFPKDvNLWKLMgDFNLHGITAPEEYGGLGLGYLYHCiAMEEISRASGSVGLSYG 111

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 197313734 148 AHQAIGLKGIILVGNEEQKAKYLPKLSSGEHIAAFCLTEPASGSDAASIQTRATLSEdkKYFVLNGSKVWITNGGLANIF 227
Cdd:PLN02519 112 AHSNLCINQLVRNGTPAQKEKYLPKLISGEHVGALAMSEPNSGSDVVSMKCKAERVD--GGYVLNGNKMWCTNGPVAQTL 189

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 197313734 228 TVFAKTEVVDSDGSIkdkmTAFIVERDFGGITNGKPEDKLGIRGSNTCEVHFENTRVPVENVLGEVGGGFKVAMNILNSG 307
Cdd:PLN02519 190 VVYAKTDVAAGSKGI----TAFIIEKGMPGFSTAQKLDKLGMRGSDTCELVFENCFVPEENVLGQEGKGVYVMMSGLDLE 265

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 197313734 308 RFSMGSAVAGMLKKLIEQTAEYACTRKQFNRNLSEFGLIQEKFA-----LMAQKAYVMESMAYLTSGMLDQpgfPDCsie 382
Cdd:PLN02519 266 RLVLAAGPLGLMQACLDVVLPYVRQREQFGRPIGEFQFIQGKLAdmytsLQSSRSYVYSVARDCDNGKVDR---KDC--- 339

                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 197313734 383 aAMVKVFSSEAAWQCVSEALQILGGSGYMKDYPYERMLRDARILLIFEGTNEILRLFI 440
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 ...
 294-441 8.21e-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: 153.56  E-value: 8.21e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 197313734  294 GGGFKVAMNILNSGRFSMGSAVAGMLKKLIEQTAEYACTRKQFNRNLSEFGLIQEKFALMAQKAYVMESMAYLTSGMLDQ 373
Cdd:pfam00441   1 GRGFRVAMETLNHERLAIAAMALGLARRALDEALAYARRRKAFGRPLIDFQLVRHKLAEMAAEIEAARLLVYRAAEALDA 80

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 197313734  374 pGFPDcSIEAAMVKVFSSEAAWQCVSEALQILGGSGYMKDYPYERMLRDARILLIFEGTNEILRLFIA 441
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 ...
 42-449 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: 718.87  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 197313734  42 SFAKELFLGHIQQKGVFPFPEVSQEELSE-INQFVGPLEKFFNEEVDSRKIDQEGKIPADTLAKLKSLGLFGIQVPEEYG 120
Cdd:cd01161    1 SFALNMFLGDIVTKQVFPYPSVLTEEQTEeLNMLVGPVEKFFEEVNDPAKNDQLEKIPRKTLTQLKELGLFGLQVPEEYG 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 197313734 121 GLGLSNTMYARLGEIISMDASITVTLAAHQAIGLKGIILVGNEEQKAKYLPKLSSGEHIAAFCLTEPASGSDAASIQTRA 200
Cdd:cd01161   81 GLGLNNTQYARLAEIVGMDLGFSVTLGAHQSIGFKGILLFGTEAQKEKYLPKLASGEWIAAFALTEPSSGSDAASIRTTA 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 197313734 201 TLSEDKKYFVLNGSKVWITNGGLANIFTVFAKTEVVDSDGSIKDKMTAFIVERDFGGITNGKPEDKLGIRGSNTCEVHFE 280
Cdd:cd01161  161 VLSEDGKHYVLNGSKIWITNGGIADIFTVFAKTEVKDATGSVKDKITAFIVERSFGGVTNGPPEKKMGIKGSNTAEVYFE 240

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 197313734 281 NTRVPVENVLGEVGGGFKVAMNILNSGRFSMGSAVAGMLKKLIEQTAEYACTRKQFNRNLSEFGLIQEKFALMAQKAYVM 360
Cdd:cd01161  241 DVKIPVENVLGEVGDGFKVAMNILNNGRFGMGAALIGTMKRCIEKAVDYANNRKQFGKKIHEFGLIQEKLANMAILQYAT 320

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 197313734 361 ESMAYLTSGMLDQPGFPDCSIEAAMVKVFSSEAAWQCVSEALQILGGSGYMKDYPYERMLRDARILLIFEGTNEILRLFI 440
Cdd:cd01161  321 ESMAYMTSGNMDRGLKAEYQIEAAISKVFASEAAWLVVDEAIQIHGGMGFMREYGVERVLRDLRIFRIFEGTNEILRLFI 400


                 ....*....
gi 197313734 441 ALTGLQHAG 449
Cdd:cd01161  401 ALTGLQHAG 409
CaiA COG1960
Acyl-CoA dehydrogenase related to the alkylation response protein AidB [Lipid transport and ...
 70-441 4.62e-146

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: 428.10  E-value: 4.62e-146
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 197313734  70 EINQFVGPLEKFFNEEVD--SRKIDQEGKIPADTLAKLKSLGLFGIQVPEEYGGLGLSNTMYARLGEIISM-DASITVTL 146
Cdd:COG1960    8 EQRALRDEVREFAEEEIApeAREWDREGEFPRELWRKLAELGLLGLTIPEEYGGLGLSLVELALVLEELARaDASLALPV 87

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 197313734 147 AAHqAIGLKGIILVGNEEQKAKYLPKLSSGEHIAAFCLTEPASGSDAASIQTRATLSEDKkyFVLNGSKVWITNGGLANI 226
Cdd:COG1960   88 GVH-NGAAEALLRFGTEEQKERYLPRLASGEWIGAFALTEPGAGSDAAALRTTAVRDGDG--YVLNGQKTFITNAPVADV 164

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 197313734 227 FTVFAKTEvvDSDGSikDKMTAFIVERDFGGITNGKPEDKLGIRGSNTCEVHFENTRVPVENVLGEVGGGFKVAMNILNS 306
Cdd:COG1960  165 ILVLARTD--PAAGH--RGISLFLVPKDTPGVTVGRIEDKMGLRGSDTGELFFDDVRVPAENLLGEEGKGFKIAMSTLNA 240

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 197313734 307 GRFSMGSAVAGMLKKLIEQTAEYACTRKQFNRNLSEFGLIQEKFALMAQKAYVMESMAYLTSGMLDQPGfpDCSIEAAMV 386
Cdd:COG1960  241 GRLGLAAQALGIAEAALELAVAYAREREQFGRPIADFQAVQHRLADMAAELEAARALVYRAAWLLDAGE--DAALEAAMA 318

                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 197313734 387 KVFSSEAAWQCVSEALQILGGSGYMKDYPYERMLRDARILLIFEGTNEILRLFIA 441
Cdd:COG1960  319 KLFATEAALEVADEALQIHGGYGYTREYPLERLYRDARILTIYEGTNEIQRLIIA 373
SCAD_SBCAD cd01158
Short chain acyl-CoA dehydrogenases and eukaryotic short/branched chain acyl-CoA ...
 66-441 1.08e-132

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: 393.56  E-value: 1.08e-132
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 197313734  66 EELSEINQFVgplEKFFNEEVD--SRKIDQEGKIPADTLAKLKSLGLFGIQVPEEYGGLGLSNTMYAR-LGEIISMDASI 142
Cdd:cd01158    1 EEHQMIRKTV---RDFAEKEIAplAAEMDEKGEFPREVIKEMAELGLMGIPIPEEYGGAGLDFLAYAIaIEELAKVDASV 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 197313734 143 TVTLAAHQAIGLKGIILVGNEEQKAKYLPKLSSGEHIAAFCLTEPASGSDAASIQTRATLSEDkkYFVLNGSKVWITNGG 222
Cdd:cd01158   78 AVIVSVHNSLGANPIIKFGTEEQKKKYLPPLATGEKIGAFALSEPGAGSDAAALKTTAKKDGD--DYVLNGSKMWITNGG 155

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 197313734 223 LANIFTVFAKTevvdsDGSIKDK-MTAFIVERDFGGITNGKPEDKLGIRGSNTCEVHFENTRVPVENVLGEVGGGFKVAM 301
Cdd:cd01158  156 EADFYIVFAVT-----DPSKGYRgITAFIVERDTPGLSVGKKEDKLGIRGSSTTELIFEDVRVPKENILGEEGEGFKIAM 230

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 197313734 302 NILNSGRFSMGSAVAGMLKKLIEQTAEYACTRKQFNRNLSEFGLIQEKFALMAQKayvMESMAYLT--SGMLDQPGFPdC 379
Cdd:cd01158  231 QTLDGGRIGIAAQALGIAQAALDAAVDYAKERKQFGKPIADFQGIQFKLADMATE---IEAARLLTykAARLKDNGEP-F 306

                        330       340       350       360       370       380
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 197313734 380 SIEAAMVKVFSSEAAWQCVSEALQILGGSGYMKDYPYERMLRDARILLIFEGTNEILRLFIA 441
Cdd:cd01158  307 IKEAAMAKLFASEVAMRVTTDAVQIFGGYGYTKDYPVERYYRDAKITEIYEGTSEIQRLVIA 368
ACAD cd00567
Acyl-CoA dehydrogenase; Both mitochondrial acyl-CoA dehydrogenases (ACAD) and peroxisomal ...
 152-441 3.74e-115

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: 346.96  E-value: 3.74e-115
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 197313734 152 IGLKGIILVGNEEQKAKYLPKLSSGEHIAAFCLTEPASGSDAASIQTRATLSEDKkyFVLNGSKVWITNGGLANIFTVFA 231
Cdd:cd00567   43 LGAALLLAYGTEEQKERYLPPLASGEAIAAFALTEPGAGSDLAGIRTTARKDGDG--YVLNGRKIFISNGGDADLFIVLA 120

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 197313734 232 KTevvDSDGSIKDKMTAFIVERDFGGITNGKPEDKLGIRGSNTCEVHFENTRVPVENVLGEVGGGFKVAMNILNSGRFSM 311
Cdd:cd00567  121 RT---DEEGPGHRGISAFLVPADTPGVTVGRIWDKMGMRGSGTGELVFDDVRVPEDNLLGEEGGGFELAMKGLNVGRLLL 197

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 197313734 312 GSAVAGMLKKLIEQTAEYACTRKQFNRNLSEFGLIQEKFALMAQKAYVMESMAYLTSGMLDQpGFPDCSIEAAMVKVFSS 391
Cdd:cd00567  198 AAVALGAARAALDEAVEYAKQRKQFGKPLAEFQAVQFKLADMAAELEAARLLLYRAAWLLDQ-GPDEARLEAAMAKLFAT 276

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|
gi 197313734 392 EAAWQCVSEALQILGGSGYMKDYPYERMLRDARILLIFEGTNEILRLFIA 441
Cdd:cd00567  277 EAAREVADLAMQIHGGRGYSREYPVERYLRDARAARIAEGTAEIQRLIIA 326
IVD cd01156
Isovaleryl-CoA dehydrogenase; Isovaleryl-CoA dehydrogenase (IVD) is an is an acyl-CoA ...
 70-441 2.19e-107

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: 328.60  E-value: 2.19e-107
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 197313734  70 EINQFVGPLEKFFNEEVDSR--KIDQEGKIPADTLAKLKSLGLFGIQVPEEYGGLGLSNTMYARLGEIIS-MDASITVTL 146
Cdd:cd01156    5 EIEMLRQSVREFAQKEIAPLaaKIDRDNEFPRDLWRKMGKLGLLGITAPEEYGGSGMGYLAHVIIMEEISrASGSVALSY 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 197313734 147 AAHQAIGLKGIILVGNEEQKAKYLPKLSSGEHIAAFCLTEPASGSDAASIQTRATlsEDKKYFVLNGSKVWITNGGLANI 226
Cdd:cd01156   85 GAHSNLCINQIYRNGSAAQKEKYLPKLISGEHIGALAMSEPNAGSDVVSMKLRAE--KKGDRYVLNGSKMWITNGPDADT 162

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 197313734 227 FTVFAKTEV-VDSDGsikdkMTAFIVERDFGGITNGKPEDKLGIRGSNTCEVHFENTRVPVENVLGEVGGGFKVAMNILN 305
Cdd:cd01156  163 LVVYAKTDPsAGAHG-----ITAFIVEKGMPGFSRAQKLDKLGMRGSNTCELVFEDCEVPEENILGGENKGVYVLMSGLD 237

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 197313734 306 SGRFSMGSAVAGMLKKLIEQTAEYACTRKQFNRNLSEFGLIQEKFA-----LMAQKAYVMESMAYLTSGMLDqpgfpdcS 380
Cdd:cd01156  238 YERLVLAGGPIGIMQAALDVAIPYAHQRKQFGQPIGEFQLVQGKLAdmytrLNASRSYLYTVAKACDRGNMD-------P 310

                        330       340       350       360       370       380
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 197313734 381 IEAAMVKVFSSEAAWQCVSEALQILGGSGYMKDYPYERMLRDARILLIFEGTNEILRLFIA 441
Cdd:cd01156  311 KDAAGVILYAAEKATQVALDAIQILGGNGYINDYPTGRLLRDAKLYEIGAGTSEIRRMVIG 371
IBD cd01162
Isobutyryl-CoA dehydrogenase; Isobutyryl-CoA dehydrogenase (IBD) catalyzes the alpha, beta- ...
 92-441 4.74e-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: 275.86  E-value: 4.74e-87
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 197313734  92 DQEGKIPADTLAKLKSLGLFGIQVPEEYGGLGLSNTMYARLGEIISM-DASITVTLAAHQAIGLKgIILVGNEEQKAKYL 170
Cdd:cd01162   28 DQKKHFPVDVLRKAAELGFGGIYIRDDVGGSGLSRLDASIIFEALSTgCVSTAAYISIHNMCAWM-IDSFGNDEQRERFL 106

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 197313734 171 PKLSSGEHIAAFCLTEPASGSDAASIQTRATLSEDkkYFVLNGSKVWITNGGLANIFTVFAKTevvdsDGSIKDKMTAFI 250
Cdd:cd01162  107 PDLCTMEKLASYCLTEPGSGSDAAALRTRAVREGD--HYVLNGSKAFISGAGDSDVYVVMART-----GGEGPKGISCFV 179

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 197313734 251 VERDFGGITNGKPEDKLGIRGSNTCEVHFENTRVPVENVLGEVGGGFKVAMNILNSGRFSMGSAVAGMLKKLIEQTAEYA 330
Cdd:cd01162  180 VEKGTPGLSFGANEKKMGWNAQPTRAVIFEDCRVPVENRLGGEGQGFGIAMAGLNGGRLNIASCSLGAAQAALDLARAYL 259

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 197313734 331 CTRKQFNRNLSEFGLIQEKFALMAQKAYVMESMAYLTSGMLDQpGFPDCSIEAAMVKVFSSEAAWQCVSEALQILGGSGY 410
Cdd:cd01162  260 EERKQFGKPLADFQALQFKLADMATELVASRLMVRRAASALDR-GDPDAVKLCAMAKRFATDECFDVANQALQLHGGYGY 338

                        330       340       350
                 ....*....|....*....|....*....|.
gi 197313734 411 MKDYPYERMLRDARILLIFEGTNEILRLFIA 441
Cdd:cd01162  339 LKDYPVEQYVRDLRVHQILEGTNEIMRLIIA 369
LCAD cd01160
Long chain acyl-CoA dehydrogenase; LCAD is an acyl-CoA dehydrogenases (ACAD), which is found ...
 80-441 8.06e-83

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: 264.75  E-value: 8.06e-83
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 197313734  80 KFFNEEVD--SRKIDQEGKIPADTLAKLKSLGLFGIQVPEEYGGLGLSNTMYARLGEIISMDASITVTLAAHQAIGLKGI 157
Cdd:cd01160   12 RFFAKEVApfHHEWEKAGEVPREVWRKAGEQGLLGVGFPEEYGGIGGDLLSAAVLWEELARAGGSGPGLSLHTDIVSPYI 91

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 197313734 158 ILVGNEEQKAKYLPKLSSGEHIAAFCLTEPASGSDAASIQTRATLseDKKYFVLNGSKVWITNGGLANIFTVFAKTevvD 237
Cdd:cd01160   92 TRAGSPEQKERVLPQMVAGKKIGAIAMTEPGAGSDLQGIRTTARK--DGDHYVLNGSKTFITNGMLADVVIVVART---G 166

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 197313734 238 SDGSIKDKMTAFIVERDFGGITNGKPEDKLGIRGSNTCEVHFENTRVPVENVLGEVGGGFKVAMNILNSGRFSMGSAVAG 317
Cdd:cd01160  167 GEARGAGGISLFLVERGTPGFSRGRKLKKMGWKAQDTAELFFDDCRVPAENLLGEENKGFYYLMQNLPQERLLIAAGALA 246

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 197313734 318 MLKKLIEQTAEYACTRKQFNRNLSEFGLIQEKFALMAQKAYVMESMAYLTSGMLDQPGFPdcSIEAAMVKVFSSEAAWQC 397
Cdd:cd01160  247 AAEFMLEETRNYVKQRKAFGKTLAQLQVVRHKIAELATKVAVTRAFLDNCAWRHEQGRLD--VAEASMAKYWATELQNRV 324

                        330       340       350       360
                 ....*....|....*....|....*....|....*....|....
gi 197313734 398 VSEALQILGGSGYMKDYPYERMLRDARILLIFEGTNEILRLFIA 441
Cdd:cd01160  325 AYECVQLHGGWGYMREYPIARAYRDARVQPIYGGTTEIMKELIS 368
PLN02519 PLN02519
isovaleryl-CoA dehydrogenase
 73-440 2.86e-80

isovaleryl-CoA dehydrogenase


Pssm-ID: 215284 [Multi-domain]  Cd Length: 404  Bit Score: 259.42  E-value: 2.86e-80
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 197313734  73 QFVGPLEKFFNEEV--DSRKIDQEGKIPAD-TLAKLK-SLGLFGIQVPEEYGGLGLSNTMYA-RLGEIISMDASITVTLA 147
Cdd:PLN02519  32 QFKESVQQFAQENIapHAAAIDATNSFPKDvNLWKLMgDFNLHGITAPEEYGGLGLGYLYHCiAMEEISRASGSVGLSYG 111

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 197313734 148 AHQAIGLKGIILVGNEEQKAKYLPKLSSGEHIAAFCLTEPASGSDAASIQTRATLSEdkKYFVLNGSKVWITNGGLANIF 227
Cdd:PLN02519 112 AHSNLCINQLVRNGTPAQKEKYLPKLISGEHVGALAMSEPNSGSDVVSMKCKAERVD--GGYVLNGNKMWCTNGPVAQTL 189

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 197313734 228 TVFAKTEVVDSDGSIkdkmTAFIVERDFGGITNGKPEDKLGIRGSNTCEVHFENTRVPVENVLGEVGGGFKVAMNILNSG 307
Cdd:PLN02519 190 VVYAKTDVAAGSKGI----TAFIIEKGMPGFSTAQKLDKLGMRGSDTCELVFENCFVPEENVLGQEGKGVYVMMSGLDLE 265

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 197313734 308 RFSMGSAVAGMLKKLIEQTAEYACTRKQFNRNLSEFGLIQEKFA-----LMAQKAYVMESMAYLTSGMLDQpgfPDCsie 382
Cdd:PLN02519 266 RLVLAAGPLGLMQACLDVVLPYVRQREQFGRPIGEFQFIQGKLAdmytsLQSSRSYVYSVARDCDNGKVDR---KDC--- 339

                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 197313734 383 aAMVKVFSSEAAWQCVSEALQILGGSGYMKDYPYERMLRDARILLIFEGTNEILRLFI 440
Cdd:PLN02519 340 -AGVILCAAERATQVALQAIQCLGGNGYINEYPTGRLLRDAKLYEIGAGTSEIRRMLI 396
MCAD cd01157
Medium chain acyl-CoA dehydrogenase; MCADs are mitochondrial beta-oxidation enzymes, which ...
 80-447 9.81e-77

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: 249.04  E-value: 9.81e-77
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 197313734  80 KFFNEEV--DSRKIDQEGKIPADTLAKLKSLGLFGIQVPEEYGGLGLSNTMYARLGEIISMDASITVTLAAHQAIGLKGI 157
Cdd:cd01157   14 KFAREEIipVAAEYDKSGEYPWPLIKRAWELGLMNTHIPEDCGGLGLGTFDTCLITEELAYGCTGVQTAIEANSLGQMPV 93

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 197313734 158 ILVGNEEQKAKYLPKLSSGEHIAAFCLTEPASGSDAASIQTRATLSEDKkyFVLNGSKVWITNGGLANIFTVFAKTEVvD 237
Cdd:cd01157   94 IISGNDEQKKKYLGRMTEEPLMCAYCVTEPGAGSDVAGIKTKAEKKGDE--YIINGQKMWITNGGKANWYFLLARSDP-D 170

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 197313734 238 SDGSIKDKMTAFIVERDFGGITNGKPEDKLGIRGSNTCEVHFENTRVPVENVLGEVGGGFKVAMNILNSGRFSMGSAVAG 317
Cdd:cd01157  171 PKCPASKAFTGFIVEADTPGIQPGRKELNMGQRCSDTRGITFEDVRVPKENVLIGEGAGFKIAMGAFDKTRPPVAAGAVG 250

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 197313734 318 MLKKLIEQTAEYACTRKQFNRNLSEFGLIQEKFALMAQKAYVMESMAYLTSGMLDQPgfPDCSIEAAMVKVFSSEAAWQC 397
Cdd:cd01157  251 LAQRALDEATKYALERKTFGKLIAEHQAVSFMLADMAMKVELARLAYQRAAWEVDSG--RRNTYYASIAKAFAADIANQL 328

                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|
gi 197313734 398 VSEALQILGGSGYMKDYPYERMLRDARILLIFEGTNEILRLFIALTGLQH 447
Cdd:cd01157  329 ATDAVQIFGGNGFNSEYPVEKLMRDAKIYQIYEGTSQIQRLIISREHLGK 378
GCD cd01151
Glutaryl-CoA dehydrogenase; Glutaryl-CoA dehydrogenase (GCD). GCD is an acyl-CoA dehydrogenase, ...
 79-446 5.93e-71

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: 234.17  E-value: 5.93e-71
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 197313734  79 EKFFNEEVDSRKID--QEGKIPADTLAKLKSLGLFGIQvPEEYGGLGLSNTMYARLG-EIISMDASITVTLAAHQAIGLK 155
Cdd:cd01151   25 REFCQEELAPRVLEayREEKFDRKIIEEMGELGLLGAT-IKGYGCAGLSSVAYGLIArEVERVDSGYRSFMSVQSSLVML 103

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 197313734 156 GIILVGNEEQKAKYLPKLSSGEHIAAFCLTEPASGSDAASIQTRATlsEDKKYFVLNGSKVWITNGGLANIFTVFAKTev 235
Cdd:cd01151  104 PIYDFGSEEQKQKYLPKLASGELIGCFGLTEPNHGSDPGGMETRAR--KDGGGYKLNGSKTWITNSPIADVFVVWARN-- 179

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 197313734 236 vDSDGSIKdkmtAFIVERDFGGITNGKPEDKLGIRGSNTCEVHFENTRVPVENVLGEV---GGGFKVamniLNSGRFSMG 312
Cdd:cd01151  180 -DETGKIR----GFILERGMKGLSAPKIQGKFSLRASITGEIVMDNVFVPEENLLPGAeglRGPFKC----LNNARYGIA 250

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 197313734 313 SAVAGMLKKLIEQTAEYACTRKQFNRNLSEFGLIQEKFALMAQKAYVMESMAYLTSGMLDQPGF-PDcsiEAAMVKVFSS 391
Cdd:cd01151  251 WGALGAAEDCYHTARQYVLDRKQFGRPLAAFQLVQKKLADMLTEIALGLLACLRVGRLKDQGKAtPE---QISLLKRNNC 327

                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 197313734 392 EAAWQCVSEALQILGGSGYMKDYPYERMLRDARILLIFEGTNEILRLFI--ALTGLQ 446
Cdd:cd01151  328 GKALEIARTAREMLGGNGISDEYHIIRHMVNLESVNTYEGTHDIHALILgrAITGIQ 384
PTZ00461 PTZ00461
isovaleryl-CoA dehydrogenase; Provisional
 78-460 2.27e-64

isovaleryl-CoA dehydrogenase; Provisional


Pssm-ID: 185640 [Multi-domain]  Cd Length: 410  Bit Score: 217.50  E-value: 2.27e-64
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 197313734  78 LEKFFNEEVD--SRKIDQEGKIPADTLAKLKSLGLFGIQVPEEYGGLGLSNTMYARLG-EIISMDASITVTLAAHQAIGL 154
Cdd:PTZ00461  48 VAKFSREVVDkhAREDDINMHFNRDLFKQLGDLGVMGVTVPEADGGAGMDAVAAVIIHhELSKYDPGFCLAYLAHSMLFV 127

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 197313734 155 KGIILVGNEEQKAKYLPKLSSGEHIAAFCLTEPASGSDAASIQTRATLSEDKKYfVLNGSKVWITNGGLANIFTVFAKTe 234
Cdd:PTZ00461 128 NNFYYSASPAQRARWLPKVLTGEHVGAMGMSEPGAGTDVLGMRTTAKKDSNGNY-VLNGSKIWITNGTVADVFLIYAKV- 205

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 197313734 235 vvdsDGsikdKMTAFIVERDFGGITNGKPEDKLGIRGSNTCEVHFENTRVPVENVLGEVGGGFKVAMNILNSGRFSMGSA 314
Cdd:PTZ00461 206 ----DG----KITAFVVERGTKGFTQGPKIDKCGMRASHMCQLFFEDVVVPAENLLGEEGKGMVGMMRNLELERVTLAAM 277

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 197313734 315 VAGMLKKLIEQTAEYACTRKQFNRNLSEFGLIQEKFALMAQKAYVMESMAYLTSGMLdQPGFPDcSIEAAMVKVFSSEAA 394
Cdd:PTZ00461 278 AVGIAERSVELMTSYASERKAFGKPISNFGQIQRYIAEGYADTEAAKALVYSVSHNV-HPGNKN-RLGSDAAKLFATPIA 355

                        330       340       350       360       370       380
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 197313734 395 WQCVSEALQILGGSGYMKDYPYERMLRDARILLIFEGTNEilrlfialtglQHAGRILTSRIKELK 460
Cdd:PTZ00461 356 KKVADSAIQVMGGMGYSRDMPVERLWRDAKLLEIGGGTIE-----------AHHKNITKDLLKGLK 410
ACAD_fadE5 cd01153
Putative acyl-CoA dehydrogenases similar to fadE5; Putative acyl-CoA dehydrogenase (ACAD). ...
 109-435 4.78e-60

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: 206.09  E-value: 4.78e-60
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 197313734 109 GLFGIQVPEEYGGLGLSNTMYARLGEIIS------MDASITVTLAAHqaiglkgIILVGNEEQKAKYLPKLSSGEHIAAF 182
Cdd:cd01153   49 GWMALGVPEEYGGQGLPITVYSALAEIFSrgdaplMYASGTQGAAAT-------LLAHGTEAQREKWIPRLAEGEWTGTM 121

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 197313734 183 CLTEPASGSDAASIQTRATLSEDKKYFvLNGSKVWITNG---GLANIF-TVFAKTEVVDSDGSikdKMTAFIV-ERDFGG 257
Cdd:cd01153  122 CLTEPDAGSDLGALRTKAVYQADGSWR-INGVKRFISAGehdMSENIVhLVLARSEGAPPGVK---GLSLFLVpKFLDDG 197

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 197313734 258 ITNG----KPEDKLGIRGSNTCEVHFENTRVPVenvLGEVGGGFKVAMNILNSGRFSMGSAVAGMLKKLIEQTAEYACTR 333
Cdd:cd01153  198 ERNGvtvaRIEEKMGLHGSPTCELVFDNAKGEL---IGEEGMGLAQMFAMMNGARLGVGTQGTGLAEAAYLNALAYAKER 274

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 197313734 334 KQFNRNLSEFGLIQE------KFALMAQKAYVMES----MAYLTSGMLDQPGFPDCSIEAA----------MVKVFSSEA 393
Cdd:cd01153  275 KQGGDLIKAAPAVTIihhpdvRRSLMTQKAYAEGSraldLYTATVQDLAERKATEGEDRKAlsaladlltpVVKGFGSEA 354

                        330       340       350       360
                 ....*....|....*....|....*....|....*....|..
gi 197313734 394 AWQCVSEALQILGGSGYMKDYPYERMLRDARILLIFEGTNEI 435
Cdd:cd01153  355 ALEAVSDAIQVHGGSGYTREYPIEQYYRDARITTIYEGTTGI 396
PRK12341 PRK12341
acyl-CoA dehydrogenase;
78-436 6.70e-50

acyl-CoA dehydrogenase;


Pssm-ID: 183454 [Multi-domain]  Cd Length: 381  Bit Score: 177.61  E-value: 6.70e-50
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 197313734  78 LEKFFNEEvDSRKIDQEGKIP---ADTLAKlKSLGLFGIqvPEEYGGLGLSN-TMYARLGEIISMDASITVTlaaHQAIG 153
Cdd:PRK12341  20 ITRNFPEE-YFRTCDENGTYPrefMRALAD-NGISMLGV--PEEFGGTPADYvTQMLVLEEVSKCGAPAFLI---TNGQC 92

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 197313734 154 LKGIILVGNEEQKAK-YLPKLSSGEhiAAFCL--TEPASGSDAASIQTRATLSEDKKYfvLNGSKVWITNGGLANIFTVF 230
Cdd:PRK12341  93 IHSMRRFGSAEQLRKtAESTLETGD--PAYALalTEPGAGSDNNSATTTYTRKNGKVY--LNGQKTFITGAKEYPYMLVL 168

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 197313734 231 AKtevvDSDGSIKDK-MTAFIVERDFGGITNgKPEDKLGIRGSNTCEVHFENTRVPVENVLGEVGGGFKVAMNILNSGRF 309
Cdd:PRK12341 169 AR----DPQPKDPKKaFTLWWVDSSKPGIKI-NPLHKIGWHMLSTCEVYLDNVEVEESDLVGEEGMGFLNVMYNFEMERL 243

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 197313734 310 SMGSAVAGMLKKLIEQTAEYACTRKQFNRNLSEFGLIQEKFALMAQKAYVMESMAYLTSGMLDQpGFPdCSIEAAMVKVF 389
Cdd:PRK12341 244 INAARSLGFAECAFEDAARYANQRIQFGKPIGHNQLIQEKLTLMAIKIENMRNMVYKVAWQADN-GQS-LRTSAALAKLY 321

                        330       340       350       360
                 ....*....|....*....|....*....|....*....|....*..
gi 197313734 390 SSEAAWQCVSEALQILGGSGYMKDYPYERMLRDARILLIFEGTNEIL 436
Cdd:PRK12341 322 CARTAMEVIDDAIQIMGGLGYTDEARVSRFWRDVRCERIGGGTDEIM 368
ACAD_fadE6_17_26 cd01152
Putative acyl-CoA dehydrogenases similar to fadE6, fadE17, and fadE26; Putative acyl-CoA ...
 99-446 1.08e-48

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: 174.46  E-value: 1.08e-48
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 197313734  99 ADTLAKLKSLGLFGIQVPEEYGGLGLS-------NTMYARLGEIISMdASITVTLAAHQaiglkgIILVGNEEQKAKYLP 171
Cdd:cd01152   38 RRWQRALAAAGWAAPGWPKEYGGRGASlmeqlifREEMAAAGAPVPF-NQIGIDLAGPT------ILAYGTDEQKRRFLP 110

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 197313734 172 KLSSGEHIaaFCL--TEPASGSDAASIQTRATLSEDKkyFVLNGSKVWITNGGLANIFTVFAKTevvDSDGSIKDKMTAF 249
Cdd:cd01152  111 PILSGEEI--WCQgfSEPGAGSDLAGLRTRAVRDGDD--WVVNGQKIWTSGAHYADWAWLLVRT---DPEAPKHRGISIL 183

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 197313734 250 IVERDFGGIT-------NGKPEdklgirgsnTCEVHFENTRVPVENVLGEVGGGFKVAMNILNSGRFSMGSAVAgmlkKL 322
Cdd:cd01152  184 LVDMDSPGVTvrpirsiNGGEF---------FNEVFLDDVRVPDANRVGEVNDGWKVAMTTLNFERVSIGGSAA----TF 250

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 197313734 323 IEQTAEYACTRKQFNRNLSEFGLIQEKFALMAQKAYVMESMAYLTSGMLDQPGFPDcsIEAAMVKVFSSEAAwQCVSE-A 401
Cdd:cd01152  251 FELLLARLLLLTRDGRPLIDDPLVRQRLARLEAEAEALRLLVFRLASALAAGKPPG--AEASIAKLFGSELA-QELAElA 327

                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|...
gi 197313734 402 LQILGGSGYMKDYP--------YERMLRDARILLIFEGTNEILRLFIALTGLQ 446
Cdd:cd01152  328 LELLGTAALLRDPApgaelagrWEADYLRSRATTIYGGTSEIQRNIIAERLLG 380
PRK03354 PRK03354
crotonobetainyl-CoA dehydrogenase; Validated
 79-438 3.30e-48

crotonobetainyl-CoA dehydrogenase; Validated


Pssm-ID: 179566 [Multi-domain]  Cd Length: 380  Bit Score: 173.09  E-value: 3.30e-48
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 197313734  79 EKFFNEevdsrkIDQEGKIPADTLAKLKSLGLFGIQVPEEYGGLGLSNTMYARLGEIISMDASITVTLaaHQ-AIGLKGI 157
Cdd:PRK03354  26 EAYFAE------CDRDSVYPERFVKALADMGIDSLLIPEEHGGLDAGFVTLAAVWMELGRLGAPTYVL--YQlPGGFNTF 97

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 197313734 158 ILVGNEEQKAKYLPKLSSGEHIAAFCLTEPASGSDAASIQTRATLSEDKKYfvLNGSKVWITNGGLANIFTVFAKtevvD 237
Cdd:PRK03354  98 LREGTQEQIDKIMAFRGTGKQMWNSAITEPGAGSDVGSLKTTYTRRNGKVY--LNGSKCFITSSAYTPYIVVMAR----D 171

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 197313734 238 SDGSIKDKMTAFIVERDFGGITNGKPEdKLGIRGSNTCEVHFENTRVPVENVLGEVGGGFKVAMNILNSGRFSMGSAVAG 317
Cdd:PRK03354 172 GASPDKPVYTEWFVDMSKPGIKVTKLE-KLGLRMDSCCEITFDDVELDEKDMFGREGNGFNRVKEEFDHERFLVALTNYG 250

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 197313734 318 MLKKLIEQTAEYACTRKQFNRNLSEFGLIQEKFALMAQKAYVMESMAYLTSGMLDQPGFPdcSIEAAMVKVFSSEAAWQC 397
Cdd:PRK03354 251 TAMCAFEDAARYANQRVQFGEAIGRFQLIQEKFAHMAIKLNSMKNMLYEAAWKADNGTIT--SGDAAMCKYFCANAAFEV 328

                        330       340       350       360
                 ....*....|....*....|....*....|....*....|.
gi 197313734 398 VSEALQILGGSGYMKDYPYERMLRDARILLIFEGTNEILRL 438
Cdd:PRK03354 329 VDSAMQVLGGVGIAGNHRISRFWRDLRVDRVSGGSDEMQIL 369
ACAD_FadE2 cd01155
Acyl-CoA dehydrogenases similar to fadE2; FadE2-like Acyl-CoA dehydrogenase (ACAD). Acyl-CoA ...
 71-446 3.43e-45

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: 165.26  E-value: 3.43e-45
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 197313734  71 INQFVGPLEKFFNEEV--DSRKIDQEGKIPADTLAKLKSLGLFGIQVPEEYGGLGLSNTMYARLGEII--SMDASITVTL 146
Cdd:cd01155   14 MEEHVYPAEQEFLEYYaeGGDRWWTPPPIIEKLKAKAKAEGLWNLFLPEVSGLSGLTNLEYAYLAEETgrSFFAPEVFNC 93

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 197313734 147 AAHQAIGLKGIILVGNEEQKAKYLPKLSSGEHIAAFCLTEPA-SGSDAASIQTRATlsEDKKYFVLNGSKVWITNGG--L 223
Cdd:cd01155   94 QAPDTGNMEVLHRYGSEEQKKQWLEPLLDGKIRSAFAMTEPDvASSDATNIECSIE--RDGDDYVINGRKWWSSGAGdpR 171

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 197313734 224 ANIFTVFAKTevvDSDGSIKDKMTAFI-VERDFGGITNGKPedkLGIRGSNT-----CEVHFENTRVPVENVLGEVGGGF 297
Cdd:cd01155  172 CKIAIVMGRT---DPDGAPRHRQQSMIlVPMDTPGVTIIRP---LSVFGYDDaphghAEITFDNVRVPASNLILGEGRGF 245

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 197313734 298 KVAMNILNSGRFSMGSAVAGMLKKLIEQTAEYACTRKQFNRNLSEFGLIQEKFAlmaqKAYVMESMAYL----TSGMLDQ 373
Cdd:cd01155  246 EIAQGRLGPGRIHHCMRLIGAAERALELMCQRAVSREAFGKKLAQHGVVAHWIA----KSRIEIEQARLlvlkAAHMIDT 321

                        330       340       350       360       370       380       390
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 197313734 374 PGFPDCSIEAAMVKVFSSEAAWQCVSEALQILGGSGYMKDYPYERMLRDARILLIFEGTNEILRLFIALTGLQ 446
Cdd:cd01155  322 VGNKAARKEIAMIKVAAPRMALKIIDRAIQVHGAAGVSQDTPLANMYAWARTLRIADGPDEVHLRSIARMELK 394
Acyl-CoA_dh_1 pfam00441
Acyl-CoA dehydrogenase, C-terminal domain; C-terminal domain of Acyl-CoA dehydrogenase is an ...
 294-441 8.21e-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: 153.56  E-value: 8.21e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 197313734  294 GGGFKVAMNILNSGRFSMGSAVAGMLKKLIEQTAEYACTRKQFNRNLSEFGLIQEKFALMAQKAYVMESMAYLTSGMLDQ 373
Cdd:pfam00441   1 GRGFRVAMETLNHERLAIAAMALGLARRALDEALAYARRRKAFGRPLIDFQLVRHKLAEMAAEIEAARLLVYRAAEALDA 80

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 197313734  374 pGFPDcSIEAAMVKVFSSEAAWQCVSEALQILGGSGYMKDYPYERMLRDARILLIFEGTNEILRLFIA 441
Cdd:pfam00441  81 -GGPD-GAEASMAKLYASEAAVEVADLAMQLHGGYGYLREYPVERLYRDARVLRIGEGTSEIQRNIIA 146
PLN02526 PLN02526
acyl-coenzyme A oxidase
 93-445 1.01e-38

acyl-coenzyme A oxidase


Pssm-ID: 178141 [Multi-domain]  Cd Length: 412  Bit Score: 147.69  E-value: 1.01e-38
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 197313734  93 QEGKIPADTLAKLKSLGLFGIQVpEEYGGLGLSNTMYA-RLGEIISMDASITVTLAAHQAIGLKGIILVGNEEQKAKYLP 171
Cdd:PLN02526  57 EKAEFPFHIIPKLGSLGIAGGTI-KGYGCPGLSITASAiATAEVARVDASCSTFILVHSSLAMLTIALCGSEAQKQKYLP 135

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 197313734 172 KLSSGEHIAAFCLTEPASGSDAASIQTRATLSEDKkyFVLNGSKVWITNGGLANIFTVFAKTevvdsdgSIKDKMTAFIV 251
Cdd:PLN02526 136 SLAQLDTVACWALTEPDYGSDASSLNTTATKVEGG--WILNGQKRWIGNSTFADVLVIFARN-------TTTNQINGFIV 206

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 197313734 252 ERDFGGITNGKPEDKLGIRGSNTCEVHFENTRVPVENVLGEVgGGFKVAMNILNSGRFSMGSAVAGMLKKLIEQTAEYAC 331
Cdd:PLN02526 207 KKGAPGLKATKIENKIGLRMVQNGDIVLKDVFVPDEDRLPGV-NSFQDTNKVLAVSRVMVAWQPIGISMGVYDMCHRYLK 285

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 197313734 332 TRKQFNRNLSEFGLIQEKFALMAQKAYVMESMA------YLTSGMldQPGfpdcsiEAAMVKVFSSEAAWQCVSEALQIL 405
Cdd:PLN02526 286 ERKQFGAPLAAFQINQEKLVRMLGNIQAMFLVGwrlcklYESGKM--TPG------HASLGKAWITKKARETVALGRELL 357

                        330       340       350       360
                 ....*....|....*....|....*....|....*....|..
gi 197313734 406 GGSGYMKDYPYERMLRDARILLIFEGTNEILRLFIA--LTGL 445
Cdd:PLN02526 358 GGNGILADFLVAKAFCDLEPIYTYEGTYDINALVTGreITGI 399
fadE PRK09463
acyl-CoA dehydrogenase; Reviewed
 58-409 4.63e-37

acyl-CoA dehydrogenase; Reviewed


Pssm-ID: 236528 [Multi-domain]  Cd Length: 777  Bit Score: 147.66  E-value: 4.63e-37
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 197313734  58 FPFPEVSQEELSEINqfvGPLEKFFnEEVDSRKIDQE-GKIPADTLAKLKSLGLFGIQVPEEYGGLGLSNTMYARlgeII 136
Cdd:PRK09463  74 YPKPTLTAEEQAFLD---GPVEELC-RMVNDWQITHElADLPPEVWQFIKEHGFFGMIIPKEYGGLEFSAYAHSR---VL 146

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 197313734 137 ------SMDASITVT---------LAAHqaiglkgiilVGNEEQKAKYLPKLSSGEHIAAFCLTEPASGSDAASI----- 196
Cdd:PRK09463 147 qklasrSGTLAVTVMvpnslgpgeLLLH----------YGTDEQKDHYLPRLARGEEIPCFALTSPEAGSDAGSIpdtgv 216

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 197313734 197 ------QTRATLsedkkYFVLNGSKVWITnggLANIFTVFA---KteVVDSDGSIKDK----MTAFIVERDFGGITNGKP 263
Cdd:PRK09463 217 vckgewQGEEVL-----GMRLTWNKRYIT---LAPIATVLGlafK--LYDPDGLLGDKedlgITCALIPTDTPGVEIGRR 286

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 197313734 264 EDKLGirgsntceVHFEN--TR-----VPVENVLGE---VGGGFKVAMNILNSGR-FSMGSAVAGMLKKLIEQTAEYACT 332
Cdd:PRK09463 287 HFPLN--------VPFQNgpTRgkdvfIPLDYIIGGpkmAGQGWRMLMECLSVGRgISLPSNSTGGAKLAALATGAYARI 358

                        330       340       350       360       370       380       390
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 197313734 333 RKQFNRNLSEFGLIQEKFALMAQKAYVMESMAYLTSGMLDQPGFPdcSIEAAMVKVFSSEAAWQCVSEALQILGGSG 409
Cdd:PRK09463 359 RRQFKLPIGKFEGIEEPLARIAGNAYLMDAARTLTTAAVDLGEKP--SVLSAIAKYHLTERGRQVINDAMDIHGGKG 433
AidB cd01154
Proteins involved in DNA damage response, similar to the AidB gene product; AidB is one of ...
 142-438 3.52e-36

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: 140.58  E-value: 3.52e-36
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 197313734 142 ITVTLAAhqaigLKGIILVGNEEQKAKYLPKLSSGEH---IAAFCLTEPASGSDAASIQTRATLSEDKKYfVLNGSKvWI 218
Cdd:cd01154  113 LTMTDAA-----VYALRKYGPEELKQYLPGLLSDRYKtglLGGTWMTEKQGGSDLGANETTAERSGGGVY-RLNGHK-WF 185

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 197313734 219 TNGGLANIFTVFAKTEvvDSDGSIKDkMTAFIVER-DFGGITNG----KPEDKLGIRGSNTCEVHFENTrvpVENVLGEV 293
Cdd:cd01154  186 ASAPLADAALVLARPE--GAPAGARG-LSLFLVPRlLEDGTRNGyrirRLKDKLGTRSVATGEVEFDDA---EAYLIGDE 259

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 197313734 294 GGGFKVAMNILNSGRFSMGSAVAGMLKKLIEQTAEYACTRKQFNRNLSEFGLIQEKFALMAQKayVMESMAYL--TSGML 371
Cdd:cd01154  260 GKGIYYILEMLNISRLDNAVAALGIMRRALSEAYHYARHRRAFGKPLIDHPLMRRDLAEMEVD--VEAATALTfrAARAF 337

                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 197313734 372 DQPGfPDCSIEAAMVKVFS-------SEAAWQCVSEALQILGGSGYMKDYPYERMLRDARILLIFEGTNEILRL 438
Cdd:cd01154  338 DRAA-ADKPVEAHMARLATpvakliaCKRAAPVTSEAMEVFGGNGYLEEWPVARLHREAQVTPIWEGTGNIQAL 410
PTZ00456 PTZ00456
acyl-CoA dehydrogenase; Provisional
 103-435 1.53e-31

acyl-CoA dehydrogenase; Provisional


Pssm-ID: 185635 [Multi-domain]  Cd Length: 622  Bit Score: 129.99  E-value: 1.53e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 197313734 103 AKLKSLGLFGIQVPEEYGGLGLSNTMYARLGEIISMdASITVTLAAHQAIG-LKGIILVGNEEQKAKYLPKLSSGEHIAA 181
Cdd:PTZ00456 106 QALKAGGWTGISEPEEYGGQALPLSVGFITRELMAT-ANWGFSMYPGLSIGaANTLMAWGSEEQKEQYLTKLVSGEWSGT 184

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 197313734 182 FCLTEPASGSDAASIQTRATLSEDKKYfVLNGSKVWITNGG---LANI-FTVFAKTEvvDSDGSIKDkMTAFIVER---- 253
Cdd:PTZ00456 185 MCLTEPQCGTDLGQVKTKAEPSADGSY-KITGTKIFISAGDhdlTENIvHIVLARLP--NSLPTTKG-LSLFLVPRhvvk 260

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 197313734 254 DFGGITNGKP------EDKLGIRGSNTCEVHFENTrvpVENVLGEVGGGFKVAMNILNSGRfsMGSAVAGML-KKLIEQT 326
Cdd:PTZ00456 261 PDGSLETAKNvkciglEKKMGIKGSSTCQLSFENS---VGYLIGEPNAGMKQMFTFMNTAR--VGTALEGVChAELAFQN 335

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 197313734 327 A-EYacTRKQFNRNLSEFGLIQEKFA------------LMAQKAyVME---SMAYLTSGMLD-QPGFPDCSIEAAM---- 385
Cdd:PTZ00456 336 AlRY--ARERRSMRALSGTKEPEKPAdriichanvrqnILFAKA-VAEggrALLLDVGRLLDiHAAAKDAATREALdhei 412

                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 197313734 386 ------VKVFSSEAAWQCVSEALQILGGSGYMKDYPYERMLRDARILLIFEGTNEI 435
Cdd:PTZ00456 413 gfytpiAKGCLTEWGVEAASRCLQVWGGHGYIKGNGMEQILRDARIGTLYEGTTGI 468
PRK13026 PRK13026
acyl-CoA dehydrogenase; Reviewed
 58-409 1.25e-30

acyl-CoA dehydrogenase; Reviewed


Pssm-ID: 237277 [Multi-domain]  Cd Length: 774  Bit Score: 127.77  E-value: 1.25e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 197313734  58 FPFPEVSQEELSEINqfvGPLEKFFnEEVDSRKIDQEGK-IPADTLAKLKSLGLFGIQVPEEYGGLGLSNtmYARlGEII 136
Cdd:PRK13026  73 YPKPTLTAEEQAFID---NEVETLL-TMLDDWDIVQNRKdLPPEVWDYLKKEGFFALIIPKEYGGKGFSA--YAN-STIV 145

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 197313734 137 SMDA----SITVTLAAHQAIGlKGIILV--GNEEQKAKYLPKLSSGEHIAAFCLTEPASGSDAASIQTRATL------SE 204
Cdd:PRK13026 146 SKIAtrsvSAAVTVMVPNSLG-PGELLThyGTQEQKDYWLPRLADGTEIPCFALTGPEAGSDAGAIPDTGIVcrgefeGE 224

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 197313734 205 DKKYFVLNGSKVWITnggLANIFTV----FaktEVVDSDGSIKDK----MTAFIVERDFGGITNGKPEDKLGIRgsntce 276
Cdd:PRK13026 225 EVLGLRLTWDKRYIT---LAPVATVlglaF---KLRDPDGLLGDKkelgITCALIPTDHPGVEIGRRHNPLGMA------ 292

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 197313734 277 vhFEN--TR-----VPVENVLG---EVGGGFKVAMNILNSGRF----SMGSAVAGMLKKLieqTAEYACTRKQFNRNLSE 342
Cdd:PRK13026 293 --FMNgtTRgkdvfIPLDWIIGgpdYAGRGWRMLVECLSAGRGislpALGTASGHMATRT---TGAYAYVRRQFGMPIGQ 367

                        330       340       350       360       370       380
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 197313734 343 FGLIQEKFALMAQKAYVMESMAYLTSGMLDQPGFPdcSIEAAMVKVFSSEAAWQCVSEALQILGGSG 409
Cdd:PRK13026 368 FEGVQEALARIAGNTYLLEAARRLTTTGLDLGVKP--SVVTAIAKYHMTELARDVVNDAMDIHAGKG 432
Acyl-CoA_dh_M pfam02770
Acyl-CoA dehydrogenase, middle domain; Central domain of Acyl-CoA dehydrogenase has a ...
 181-280 6.91e-29

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: 110.06  E-value: 6.91e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 197313734  181 AFCLTEPASGSDAASIQTRATLSEDKKYfVLNGSKVWITNGGLANIFTVFAKTEvvdsDGSIKDKMTAFIVERDFGGITN 260
Cdd:pfam02770   1 AFALTEPGAGSDVASLKTTAADGDGGGW-VLNGTKWWITNAGIADLFLVLARTG----GDDRHGGISLFLVPKDAPGVSV 75

                          90       100
                  ....*....|....*....|
gi 197313734  261 GKPEDKLGIRGSNTCEVHFE 280
Cdd:pfam02770  76 RRIETKLGVRGLPTGELVFD 95
Acyl-CoA_dh_N pfam02771
Acyl-CoA dehydrogenase, N-terminal domain; The N-terminal domain of Acyl-CoA dehydrogenase is ...
 80-177 2.43e-28

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: 109.47  E-value: 2.43e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 197313734   80 KFFNEEV--DSRKIDQEGKIPADTLAKLKSLGLFGIQVPEEYGGLGLSNTMYARLGEIISM-DASITVTLAAHQAIGLKG 156
Cdd:pfam02771  13 EFAEEEIapHAAEWDEEGEFPRELWKKLGELGLLGITIPEEYGGAGLDYLAYALVAEELARaDASVALALSVHSSLGAPP 92

                          90       100
                  ....*....|....*....|.
gi 197313734  157 IILVGNEEQKAKYLPKLSSGE 177
Cdd:pfam02771  93 ILRFGTEEQKERYLPKLASGE 113
PTZ00457 PTZ00457
acyl-CoA dehydrogenase; Provisional
 88-575 1.55e-26

acyl-CoA dehydrogenase; Provisional


Pssm-ID: 185636 [Multi-domain]  Cd Length: 520  Bit Score: 113.82  E-value: 1.55e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 197313734  88 SRKIDQEgkiPADTLAKL--------KSLG-LFGIQVPEEYGGLGLSNTMYARLGEIISMDA-SITVTLAAHQAIGLKGI 157
Cdd:PTZ00457  37 CRKLDGD---EAENLQSLleqirsndKILGnLYGARIATEYGGLGLGHTAHALIYEEVGTNCdSKLLSTIQHSGFCTYLL 113

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 197313734 158 ILVGNEEQKAKYLPKLSSGEHIAAFClTEPASGSDAASIQTRATLSEDKKYfVLNGSKvWITNGGLANIFTVFAKT--EV 235
Cdd:PTZ00457 114 STVGSKELKGKYLTAMSDGTIMMGWA-TEEGCGSDISMNTTKASLTDDGSY-VLTGQK-RCEFAASATHFLVLAKTltQT 190

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 197313734 236 VDSDGSIK-DKMTAFIVERDFGGITngkpedklgIRGSNtceVHFENTrvPVENVLGEVGGGFKVAMNILNSGRFSMGSA 314
Cdd:PTZ00457 191 AAEEGATEvSRNSFFICAKDAKGVS---------VNGDS---VVFENT--PAADVVGVVGEGFKDAMITLFTEQYLYAAS 256

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 197313734 315 VAGMLKKLIEQTAEyactrkqfnrNLSEFGlIQEKFALMAQKAYVMESMAYLTSGMLDQPGfPDCSIEAAMVKVFSSEAa 394
Cdd:PTZ00457 257 LLGIMKRVVQELRG----------SNAEEG-ATDTVASFACAMYAMESTLYALTANLDLPT-EDSLLECTLVSAFVQST- 323

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 197313734 395 wqcVSEALQILGGSGYMKDYpYERMLRDARILLIFEGTNEILRLFIALTGLQHAGRILTsrikelksgNVTTVMETIGRK 474
Cdd:PTZ00457 324 ---TNQLLSILETATPPSTT-LEKCFANARLFLSMMESRDFLYSSAVCCGVEDYGLFFQ---------RASTLQMMQART 390

                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 197313734 475 LRdslgrtvDLGLSSNIAVvhPSLGDSAnKLEENVHYFGRTVETLLLRFGKTIVEEQLVLKRVANILINLYGMTAVLSRA 554
Cdd:PTZ00457 391 LR-------SLGVRDRVPI--KNLPDCS-LIDEAVVAFGNAVEATFVRSGSQVPYQQLLLNRLGEAASLLYAASAVASRA 460

                        490       500
                 ....*....|....*....|.
gi 197313734 555 SRSIRIGLKNHDHEILLANMF 575
Cdd:PTZ00457 461 SMCVSKGLPSAKVEGELASAF 481
PLN02876 PLN02876
acyl-CoA dehydrogenase
 97-448 4.32e-21

acyl-CoA dehydrogenase


Pssm-ID: 215473 [Multi-domain]  Cd Length: 822  Bit Score: 97.94  E-value: 4.32e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 197313734  97 IPADTLAKLKSLGLFGIQVP------EEYGGLGLSNTMYARLGEII--SMDASITVTLAAHQAIGLKGIILVGNEEQKAK 168
Cdd:PLN02876 461 IPLDSAARARKLLFEDNKHMvsgdsaDQLLGAGLSNLEYGYLCEIMgrSVWAPQVFNCGAPDTGNMEVLLRYGNKEQQLE 540

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 197313734 169 YLPKLSSGEHIAAFCLTEP-ASGSDAASIQtrATLSEDKKYFVLNGSKvWITNGGL---ANIFTVFAKTevvDSDGSIKD 244
Cdd:PLN02876 541 WLIPLLEGKIRSGFAMTEPqVASSDATNIE--CSIRRQGDSYVINGTK-WWTSGAMdprCRVLIVMGKT---DFNAPKHK 614

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 197313734 245 KMTAFIVERDFGGITNGKPEDKLGIRGS--NTCEVHFENTRVPVENVLGEVGGGFKVAMNILNSGRFS-----MGSAVAG 317
Cdd:PLN02876 615 QQSMILVDIQTPGVQIKRPLLVFGFDDAphGHAEISFENVRVPAKNILLGEGRGFEIAQGRLGPGRLHhcmrlIGAAERG 694

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 197313734 318 MlkkliEQTAEYACTRKQFNRNLSEFG-----LIQEKFALMAQKAYVMESmayltSGMLDQPGFPDCSIEAAMVKVFSSE 392
Cdd:PLN02876 695 M-----QLMVQRALSRKAFGKLIAQHGsflsdLAKCRVELEQTRLLVLEA-----ADQLDRLGNKKARGIIAMAKVAAPN 764

                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 197313734 393 AAWQCVSEALQILGGSGYMKDYPYERMLRDARILLIFEGTNEILRLFIALTGLQHA 448
Cdd:PLN02876 765 MALKVLDMAMQVHGAAGVSSDTVLAHLWATARTLRIADGPDEVHLGTIAKLELQRA 820
AXO cd01150
Peroxisomal acyl-CoA oxidase; Peroxisomal acyl-CoA oxidases (AXO) catalyze the first set in ...
 104-458 1.78e-18

Peroxisomal acyl-CoA oxidase; Peroxisomal acyl-CoA oxidases (AXO) catalyze the first set in the peroxisomal fatty acid beta-oxidation, the alpha,beta dehydrogenation of the corresponding trans-enoyl-CoA by FAD, which becomes reduced. In a second oxidative half-reaction, the reduced FAD is reoxidized by molecular oxygen. AXO is generally a homodimer, but it has been reported to form a different type of oligomer in yeast. There are several subtypes of AXO's, based on substrate specificity. Palmitoyl-CoA oxidase acts on straight-chain fatty acids and prostanoids; whereas, the closely related Trihydroxycoprostanoly-CoA oxidase has the greatest activity for 2-methyl branched side chains of bile precursors. Pristanoyl-CoA oxidase, acts on 2-methyl branched fatty acids. AXO has an additional domain, C-terminal to the region with similarity to acyl-CoA dehydrogenases, which is included in this alignment.


Pssm-ID: 173839 [Multi-domain]  Cd Length: 610  Bit Score: 89.31  E-value: 1.78e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 197313734 104 KLKSLGLFGIQVPEEYGGLGLSNTMYarlgeiismDASITVTLAAHQAIGLKGIILVGNEEQKAKYLPKLSSGEHIAAFC 183
Cdd:cd01150   69 DVERMGELMADDPEKMLALTNSLGGY---------DLSLGAKLGLHLGLFGNAIKNLGTDEHQDYWLQGANNLEIIGCFA 139

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 197313734 184 LTEPASGSDAASIQTRATLSEDKKYFVLN-----GSKVWItnGGL---ANIFTVFAKTEVVDSDGSIKdkmtAFIVE-RD 254
Cdd:cd01150  140 QTELGHGSNLQGLETTATYDPLTQEFVINtpdftATKWWP--GNLgktATHAVVFAQLITPGKNHGLH----AFIVPiRD 213

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 197313734 255 FG------GITNGKPEDKLGIRGSNTCEVHFENTRVPVENVL---GEV-------------GGGFKVAMNILNSGRFSMG 312
Cdd:cd01150  214 PKthqplpGVTVGDIGPKMGLNGVDNGFLQFRNVRIPRENLLnrfGDVspdgtyvspfkdpNKRYGAMLGTRSGGRVGLI 293

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 197313734 313 SAVAGMLKKLIEQTAEYACTRKQFNRNLS-------EFGLIQEK--------FAL-MAQKAYVMESMAYLTSGMLDQPGF 376
Cdd:cd01150  294 YDAAMSLKKAATIAIRYSAVRRQFGPKPSdpevqilDYQLQQYRlfpqlaaaYAFhFAAKSLVEMYHEIIKELLQGNSEL 373

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 197313734 377 -PDCSIEAAMVKVFSSEAAWQCVSEALQILGGSGYMKDYPYERMLRDARILLIFEGTNEILrlfialtgLQHAGRILTSR 455
Cdd:cd01150  374 lAELHALSAGLKAVATWTAAQGIQECREACGGHGYLAMNRLPTLRDDNDPFCTYEGDNTVL--------LQQTANYLLKK 445


                 ...
gi 197313734 456 IKE 458
Cdd:cd01150  446 YAQ 448
DszC cd01163
Dibenzothiophene (DBT) desulfurization enzyme C; DszC is a flavin reductase dependent enzyme, ...
 92-424 2.19e-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: 78.13  E-value: 2.19e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 197313734  92 DQEGKIPADTLAKLKSLGLFGIQVPEEYGGLGLS-NTMYARLGEIISMDASITVTLAAHQAIgLKGIILVGNEEQKAKYL 170
Cdd:cd01163   18 DRQRGLPYEEVALLRQSGLGTLRVPKEYGGLGASlPDLYEVVRELAAADSNIAQALRAHFGF-VEALLLAGPEQFRKRWF 96

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 197313734 171 PKLSSGeHIAAFCLTEpaSGSDAASIQTRATLSEDKKYfVLNGSKvWITNGGLaniFTVFAKTEVVDSDGsikdKMTAFI 250
Cdd:cd01163   97 GRVLNG-WIFGNAVSE--RGSVRPGTFLTATVRDGGGY-VLNGKK-FYSTGAL---FSDWVTVSALDEEG----KLVFAA 164

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 197313734 251 VERDFGGITNGKPEDKLGIR--GSNTceVHFENTRVPVENVLGEVGGGFkvamnilnsgRFSMGSAV---------AGML 319
Cdd:cd01163  165 VPTDRPGITVVDDWDGFGQRltASGT--VTFDNVRVEPDEVLPRPNAPD----------RGTLLTAIyqlvlaavlAGIA 232

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 197313734 320 KKLIEQTAEYACTRKqfnRNL--------SEFGLIQEKFALMAQKAYVMESM----------AYLTSGMLDQPGFPDCSI 381
Cdd:cd01163  233 RAALDDAVAYVRSRT---RPWihsgaesaRDDPYVQQVVGDLAARLHAAEALvlqaaraldaAAAAGTALTAEARGEAAL 309

                        330       340       350       360
                 ....*....|....*....|....*....|....*....|...
gi 197313734 382 EAAMVKVFSSEAAWQCVSEALQILGGSGYMKDYPYERMLRDAR 424
Cdd:cd01163  310 AVAAAKVVVTRLALDATSRLFEVGGASATAREHNLDRHWRNAR 352
PLN02636 PLN02636
acyl-coenzyme A oxidase
 137-480 3.79e-14

acyl-coenzyme A oxidase


Pssm-ID: 215342 [Multi-domain]  Cd Length: 686  Bit Score: 75.66  E-value: 3.79e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 197313734 137 SMDASITVTLAAHQAIGLKGIILVGNEEQKAKYLPKLSSGEHIAAFCLTEPASGSDAASIQTRATLSEDKKYFVLN---- 212
Cdd:PLN02636 132 SVDMSLGIKLGVQYSLWGGSVINLGTKKHRDKYFDGIDNLDYPGCFAMTELHHGSNVQGLQTTATFDPLTDEFVINtpnd 211

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 197313734 213 -GSKVWITNGGLANIF-TVFAKTEVVDSDGSIKDKMT--AFIVE-RDFG------GITNGKPEDKLGIRGSNTCEVHFEN 281
Cdd:PLN02636 212 gAIKWWIGNAAVHGKFaTVFARLKLPTHDSKGVSDMGvhAFIVPiRDMKthqvlpGVEIRDCGHKVGLNGVDNGALRFRS 291

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 197313734 282 TRVPVENVLGEVG-----GGFKVAMNILNS-----------GRFSMGSAVAGMLKKLIEQTAEYACTRKQFN-RNLSEFG 344
Cdd:PLN02636 292 VRIPRDNLLNRFGdvsrdGKYTSSLPTINKrfaatlgelvgGRVGLAYGSVGVLKASNTIAIRYSLLRQQFGpPKQPEIS 371

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 197313734 345 LI-----QEKFALMAQKAYVME-SMAYLT---SGML---DQPGFPDCSIEAAMVKVFSSEAAWQCVSEALQILGGSGYMK 412
Cdd:PLN02636 372 ILdyqsqQHKLMPMLASTYAFHfATEYLVerySEMKkthDDQLVADVHALSAGLKAYITSYTAKALSTCREACGGHGYAA 451

                        330       340       350       360       370       380
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 197313734 413 DYPYERMLRDARILLIFEGTNEILrlfialtgLQHAGRILTSRIKELKSGNVTTVMETIgrkLRDSLG 480
Cdd:PLN02636 452 VNRFGSLRNDHDIFQTFEGDNTVL--------LQQVAADLLKQYKEKFQGGTLSVTWNY---LRESMN 508
Acyl-CoA_dh_2 pfam08028
Acyl-CoA dehydrogenase, C-terminal domain;
310-434 2.00e-10

Acyl-CoA dehydrogenase, C-terminal domain;


Pssm-ID: 429790 [Multi-domain]  Cd Length: 133  Bit Score: 58.90  E-value: 2.00e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 197313734  310 SMGSAVAGMLKKLIEQTAEYACTRKQ--FNRNLSEFGLIQEKFALMA----QKAYVMESMAYLTSGMLDQ--PGFPDCSI 381
Cdd:pfam08028   1 GIAAAALGAARAALAEFTERARGRVRayFGVPLAEDPATQLALAEAAaridAARLLLERAAARIEAAAAAgkPVTPALRA 80

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|...
gi 197313734  382 EAAMVKVFSSEAAWQCVSEALQILGGSGYMKDYPYERMLRDARILLIFEGTNE 434
Cdd:pfam08028  81 EARRAAAFATELAVAAVDALFRAAGGSALFQDSPLQRIWRDIHAAAQHAAVNP 133
PRK11561 PRK11561
isovaleryl CoA dehydrogenase; Provisional
 184-438 3.19e-09

isovaleryl CoA dehydrogenase; Provisional


Pssm-ID: 183199 [Multi-domain]  Cd Length: 538  Bit Score: 59.77  E-value: 3.19e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 197313734 184 LTEPASGSDAASIQTRATLSEDKKYfVLNGSKvWITNGGLANIFTVFAKTevvdsdgsiKDKMTAFIVERDF-GGITNG- 261
Cdd:PRK11561 184 MTEKQGGSDVLSNTTRAERLADGSY-RLVGHK-WFFSVPQSDAHLVLAQA---------KGGLSCFFVPRFLpDGQRNAi 252

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 197313734 262 ---KPEDKLGIRGSNTCEVHFENTrvpVENVLGEVGGGFKvamNILNSG---RFSMGSAVAGMLKKLIEQTAEYACTRKQ 335
Cdd:PRK11561 253 rleRLKDKLGNRSNASSEVEFQDA---IGWLLGEEGEGIR---LILKMGgmtRFDCALGSHGLMRRAFSVAIYHAHQRQV 326

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 197313734 336 FNRNLSEFGLIQEKFALMAQKAYVMESMAYLTSGMLDQPGFPDcsiEAAMVKVFSSEAAWQ-C------VSEALQILGGS 408
Cdd:PRK11561 327 FGKPLIEQPLMRQVLSRMALQLEGQTALLFRLARAWDRRADAK---EALWARLFTPAAKFViCkrgipfVAEAMEVLGGI 403

                        250       260       270
                 ....*....|....*....|....*....|
gi 197313734 409 GYMKDYPYERMLRDARILLIFEGTNEILRL 438
Cdd:PRK11561 404 GYCEESELPRLYREMPVNSIWEGSGNIMCL 433
PTZ00460 PTZ00460
acyl-CoA dehydrogenase; Provisional
 136-551 6.56e-09

acyl-CoA dehydrogenase; Provisional


Pssm-ID: 185639 [Multi-domain]  Cd Length: 646  Bit Score: 58.70  E-value: 6.56e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 197313734 136 ISMDASITVTlAAHQAIGLKGIILVGNEEQKAKYLPKLSSGEHIAAFCLTEPASGSDAASIQTRATLSEDKKYFVLN--- 212
Cdd:PTZ00460  86 LLCPQGTFIS-TVHFAMVIPAFQVLGTDEQINLWMPSLLNFEIVGCYAQTELGHGSDVQNLETTATYDKQTNEFVIHtps 164

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 197313734 213 --GSKVWITN-GGLANIFTVFAKTeVVDSDG--------SIKDKMTafivERDFGGITNGKPEDKLGIRGSNTCEVHFEN 281
Cdd:PTZ00460 165 veAVKFWPGElGFLCNFALVYAKL-IVNGKNkgvhpfmvRIRDKET----HKPLQGVEVGDIGPKMGYAVKDNGFLSFDH 239

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 197313734 282 TRVPVENVLGEVgggFKVAMN--ILNSGRFSMGSAVAGMLKKLI----EQTA--------EYACTRKQF-NRNLSE---- 342
Cdd:PTZ00460 240 YRIPLDSLLARY---IKVSEDgqVERQGNPKVSYASMMYMRNLIidqyPRFAaqaltvaiRYSIYRQQFtNDNKQEnsvl 316

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 197313734 343 ---------FGLIQEKFALMAQKAYVME--------------SMAYLTSGMLdqpgfpdCSIEAAMVKVFSSEAAWQCVS 399
Cdd:PTZ00460 317 eyqtqqqklLPLLAEFYACIFGGLKIKElvddnfnrvqkndfSLLQLTHAIL-------SAAKANYTYFVSNCAEWCRLS 389

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 197313734 400 ealqiLGGSGYMKDYPYERMLRDARILLIFEGTNEILRLFIA---LTGLQHAGR-----------------------ILT 453
Cdd:PTZ00460 390 -----CGGHGYAHYSGLPAIYFDMSPNITLEGENQIMYLQLArylLKQLQHAVQkpekvpeyfnflshitekladqtTIE 464

                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 197313734 454 SRIKELKSgNVTTVMETIGRKLRDSLGRTVDLGLSSNiAVVHPSLGDSANKLEEnvhYFgrtvetLLLRFGKTIVEEQLV 533
Cdd:PTZ00460 465 SLGQLLGL-NCTILTIYAAKKIMDHINTGKDFQQSWD-TKSGIALASAASRFIE---YF------NYLCFLDTINNANKS 533

                        490
                 ....*....|....*...
gi 197313734 534 LKRVANILINLYGMTAVL 551
Cdd:PTZ00460 534 TKEILTQLADLYGITMLL 551
PLN02443 PLN02443
acyl-coenzyme A oxidase
 161-462 2.85e-06

acyl-coenzyme A oxidase


Pssm-ID: 178062 [Multi-domain]  Cd Length: 664  Bit Score: 50.22  E-value: 2.85e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 197313734 161 GNEEQKAKYLPKLSSGEHIAAFCLTEPASGSDAASIQTRATLSEDKKYFVLN-----GSKVWitNGGLANIFT---VFAK 232
Cdd:PLN02443 114 GTEEQQKKWLPLAYKMQIIGCYAQTELGHGSNVQGLETTATFDPKTDEFVIHsptltSSKWW--PGGLGKVSThavVYAR 191

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 197313734 233 TEVVDSDGSIKdkmtAFIVE-------RDFGGITNGKPEDKLGIRGSNTCE---VHFENTRVPVENVLGEVGG----GFK 298
Cdd:PLN02443 192 LITNGKDHGIH----GFIVQlrslddhSPLPGVTVGDIGMKFGNGAYNTMDngfLRFDHVRIPRDQMLMRLSKvtreGKY 267

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 197313734 299 VAMNI---LNSG-----RFSMGSAVAGMLKKLIEQTAEYACTRKQF--NRNLSEFGLIQEK------FALMAQkAY---- 358
Cdd:PLN02443 268 VQSDVprqLVYGtmvyvRQTIVADASTALSRAVCIATRYSAVRRQFgsQDGGPETQVIDYKtqqsrlFPLLAS-AYafrf 346

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 197313734 359 VMESMAYLTSGML------DQPGFPDCSIEAAMVKVFSSEAAWQCVSEALQILGGSGYMKDYPYERMLRDARILLIFEGT 432
Cdd:PLN02443 347 VGEWLKWLYTDVTqrleanDFSTLPEAHACTAGLKSLTTSATADGIEECRKLCGGHGYLCSSGLPELFAVYVPACTYEGD 426

                        330       340       350
                 ....*....|....*....|....*....|
gi 197313734 433 NEILRLFIAltglqhagRILTSRIKELKSG 462
Cdd:PLN02443 427 NVVLLLQVA--------RFLMKTVSQLGSG 448
PLN02312 PLN02312
acyl-CoA oxidase
 130-336 1.88e-05

acyl-CoA oxidase


Pssm-ID: 215178 [Multi-domain]  Cd Length: 680  Bit Score: 47.85  E-value: 1.88e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 197313734 130 ARLGEIISM-DASITVTLAAHQAIGLKGIILVGNEEQKAKYLPKLSSGEHIAAFCLTEPASGSDAASIQTRATLSEDKKY 208
Cdd:PLN02312 136 LALLEVIGIyDHSLAIKLGVHFFLWGGAIKFLGTKRHHDKWLKDTEDYVVKGCFAMTELGHGSNVRGIETVTTYDPKTEE 215

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 197313734 209 FVLN-----GSKVWItnGGLANIFT---VFAKTEVvdsDGSiKDKMTAFIVE-RDFGG--ITNGKPED---KLGIRGSNT 274
Cdd:PLN02312 216 FVINtpcesAQKYWI--GGAANHAThtiVFSQLHI---NGK-NEGVHAFIAQiRDQDGniCPNIRIADcghKIGLNGVDN 289

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 197313734 275 CEVHFENTRVPVENVLGEV-----GGGFKVA-----------MNILNSGRFSMGSAVAGMLKKLIEQTAEYACTRKQF 336
Cdd:PLN02312 290 GRIWFDNLRIPRENLLNSVadvspDGKYVSAikdpdqrfgafLAPLTSGRVTIAVSAIYSSKVGLAIAIRYSLSRRAF 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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