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Conserved domains on  [gi|1370483927|ref|XP_024309252|]
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complex I assembly factor ACAD9, mitochondrial isoform X1 [Homo sapiens]

Protein Classification

acyl-CoA dehydrogenase family protein( domain architecture ID 550)

acyl-CoA dehydrogenase (ACAD) family protein similar to acyl-CoA dehydrogenase that catalyzes the alpha,beta dehydrogenation of an acyl-CoA to form 2,3-dehydroacyl-CoA; requires an acceptor such as FAD, which becomes reduced

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
ACAD super family cl09933
Acyl-CoA dehydrogenase; Both mitochondrial acyl-CoA dehydrogenases (ACAD) and peroxisomal ...
 1-322 0e+00

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)


The actual alignment was detected with superfamily member cd01161:

Pssm-ID: 447864 [Multi-domain]  Cd Length: 409  Bit Score: 617.56  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370483927   1 MYSRLGEIISMDGSITVTLAAHQAIGLKGIILAGTEEQKAKYLPKLASGEHIAAFCLTEPASGSDAASIRSRATLSEDKK 80
Cdd:cd01161    88 QYARLAEIVGMDLGFSVTLGAHQSIGFKGILLFGTEAQKEKYLPKLASGEWIAAFALTEPSSGSDAASIRTTAVLSEDGK 167

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370483927  81 HYILNGSKVWITNGGLANIFTVFAKTEVVDSDGSVKDKITAFIVERDFGGVTNGKPEDKLGIRGSNTCEVHFENTKIPVE 160
Cdd:cd01161   168 HYVLNGSKIWITNGGIADIFTVFAKTEVKDATGSVKDKITAFIVERSFGGVTNGPPEKKMGIKGSNTAEVYFEDVKIPVE 247

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370483927 161 NILGEVGDGFKVAMNILNSGRFSMGSVVAGLLKRLIEMTAEYACTRKQFNKRLSEFGLIQEKFALMAQKAYVMESMTYLT 240
Cdd:cd01161   248 NVLGEVGDGFKVAMNILNNGRFGMGAALIGTMKRCIEKAVDYANNRKQFGKKIHEFGLIQEKLANMAILQYATESMAYMT 327

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370483927 241 AGMLDQPGFPDCSIEAAMVKVFSSEAAWQCVSEALQILGGLGYTRDYPYERILRDTRILLIFEGTNEILRMYIALTGLQH 320
Cdd:cd01161   328 SGNMDRGLKAEYQIEAAISKVFASEAAWLVVDEAIQIHGGMGFMREYGVERVLRDLRIFRIFEGTNEILRLFIALTGLQH 407


                  ..
gi 1370483927 321 AG 322
Cdd:cd01161   408 AG 409
 
Name Accession Description Interval E-value
VLCAD cd01161
Very long chain acyl-CoA dehydrogenase; VLCAD is an acyl-CoA dehydrogenase (ACAD), which is ...
 1-322 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: 617.56  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370483927   1 MYSRLGEIISMDGSITVTLAAHQAIGLKGIILAGTEEQKAKYLPKLASGEHIAAFCLTEPASGSDAASIRSRATLSEDKK 80
Cdd:cd01161    88 QYARLAEIVGMDLGFSVTLGAHQSIGFKGILLFGTEAQKEKYLPKLASGEWIAAFALTEPSSGSDAASIRTTAVLSEDGK 167

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370483927  81 HYILNGSKVWITNGGLANIFTVFAKTEVVDSDGSVKDKITAFIVERDFGGVTNGKPEDKLGIRGSNTCEVHFENTKIPVE 160
Cdd:cd01161   168 HYVLNGSKIWITNGGIADIFTVFAKTEVKDATGSVKDKITAFIVERSFGGVTNGPPEKKMGIKGSNTAEVYFEDVKIPVE 247

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370483927 161 NILGEVGDGFKVAMNILNSGRFSMGSVVAGLLKRLIEMTAEYACTRKQFNKRLSEFGLIQEKFALMAQKAYVMESMTYLT 240
Cdd:cd01161   248 NVLGEVGDGFKVAMNILNNGRFGMGAALIGTMKRCIEKAVDYANNRKQFGKKIHEFGLIQEKLANMAILQYATESMAYMT 327

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370483927 241 AGMLDQPGFPDCSIEAAMVKVFSSEAAWQCVSEALQILGGLGYTRDYPYERILRDTRILLIFEGTNEILRMYIALTGLQH 320
Cdd:cd01161   328 SGNMDRGLKAEYQIEAAISKVFASEAAWLVVDEAIQIHGGMGFMREYGVERVLRDLRIFRIFEGTNEILRLFIALTGLQH 407


                  ..
gi 1370483927 321 AG 322
Cdd:cd01161   408 AG 409
CaiA COG1960
Acyl-CoA dehydrogenase related to the alkylation response protein AidB [Lipid transport and ...
 2-314 2.13e-126

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: 373.02  E-value: 2.13e-126
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370483927   2 YSRLGEIISM-DGSITVTLAAHqAIGLKGIILAGTEEQKAKYLPKLASGEHIAAFCLTEPASGSDAASIRSRATLSEDkk 80
Cdd:COG1960    69 LALVLEELARaDASLALPVGVH-NGAAEALLRFGTEEQKERYLPRLASGEWIGAFALTEPGAGSDAAALRTTAVRDGD-- 145

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370483927  81 HYILNGSKVWITNGGLANIFTVFAKTEvvDSDGSvkDKITAFIVERDFGGVTNGKPEDKLGIRGSNTCEVHFENTKIPVE 160
Cdd:COG1960   146 GYVLNGQKTFITNAPVADVILVLARTD--PAAGH--RGISLFLVPKDTPGVTVGRIEDKMGLRGSDTGELFFDDVRVPAE 221

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370483927 161 NILGEVGDGFKVAMNILNSGRFSMGSVVAGLLKRLIEMTAEYACTRKQFNKRLSEFGLIQEKFALMAQKAYVMESMTYLT 240
Cdd:COG1960   222 NLLGEEGKGFKIAMSTLNAGRLGLAAQALGIAEAALELAVAYAREREQFGRPIADFQAVQHRLADMAAELEAARALVYRA 301

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1370483927 241 AGMLDQPGfpDCSIEAAMVKVFSSEAAWQCVSEALQILGGLGYTRDYPYERILRDTRILLIFEGTNEILRMYIA 314
Cdd:COG1960   302 AWLLDAGE--DAALEAAMAKLFATEAALEVADEALQIHGGYGYTREYPLERLYRDARILTIYEGTNEIQRLIIA 373
PLN02519 PLN02519
isovaleryl-CoA dehydrogenase
 7-313 8.94e-72

isovaleryl-CoA dehydrogenase


Pssm-ID: 215284 [Multi-domain]  Cd Length: 404  Bit Score: 233.62  E-value: 8.94e-72
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370483927   7 EIISMDGSITVTLAAHQAIGLKGIILAGTEEQKAKYLPKLASGEHIAAFCLTEPASGSDAASIRSRATLSEdkKHYILNG 86
Cdd:PLN02519   98 EISRASGSVGLSYGAHSNLCINQLVRNGTPAQKEKYLPKLISGEHVGALAMSEPNSGSDVVSMKCKAERVD--GGYVLNG 175

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370483927  87 SKVWITNGGLANIFTVFAKTEVvdSDGSvkDKITAFIVERDFGGVTNGKPEDKLGIRGSNTCEVHFENTKIPVENILGEV 166
Cdd:PLN02519  176 NKMWCTNGPVAQTLVVYAKTDV--AAGS--KGITAFIIEKGMPGFSTAQKLDKLGMRGSDTCELVFENCFVPEENVLGQE 251

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370483927 167 GDGFKVAMNILNSGRFSMGSVVAGLLKRLIEMTAEYACTRKQFNKRLSEFGLIQEKFA-----LMAQKAYVMESMTYLTA 241
Cdd:PLN02519  252 GKGVYVMMSGLDLERLVLAAGPLGLMQACLDVVLPYVRQREQFGRPIGEFQFIQGKLAdmytsLQSSRSYVYSVARDCDN 331

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1370483927 242 GMLDQpgfPDCsieaAMVKVFSSEAAWQCVSEALQILGGLGYTRDYPYERILRDTRILLIFEGTNEILRMYI 313
Cdd:PLN02519  332 GKVDR---KDC----AGVILCAAERATQVALQAIQCLGGNGYINEYPTGRLLRDAKLYEIGAGTSEIRRMLI 396
Acyl-CoA_dh_1 pfam00441
Acyl-CoA dehydrogenase, C-terminal domain; C-terminal domain of Acyl-CoA dehydrogenase is an ...
 167-314 7.80e-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: 151.64  E-value: 7.80e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370483927 167 GDGFKVAMNILNSGRFSMGSVVAGLLKRLIEMTAEYACTRKQFNKRLSEFGLIQEKFALMAQKAYVMESMTYLTAGMLDQ 246
Cdd:pfam00441   1 GRGFRVAMETLNHERLAIAAMALGLARRALDEALAYARRRKAFGRPLIDFQLVRHKLAEMAAEIEAARLLVYRAAEALDA 80

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1370483927 247 pGFPDcSIEAAMVKVFSSEAAWQCVSEALQILGGLGYTRDYPYERILRDTRILLIFEGTNEILRMYIA 314
Cdd:pfam00441  81 -GGPD-GAEASMAKLYASEAAVEVADLAMQLHGGYGYLREYPVERLYRDARVLRIGEGTSEIQRNIIA 146
 
Name Accession Description Interval E-value
VLCAD cd01161
Very long chain acyl-CoA dehydrogenase; VLCAD is an acyl-CoA dehydrogenase (ACAD), which is ...
 1-322 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: 617.56  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370483927   1 MYSRLGEIISMDGSITVTLAAHQAIGLKGIILAGTEEQKAKYLPKLASGEHIAAFCLTEPASGSDAASIRSRATLSEDKK 80
Cdd:cd01161    88 QYARLAEIVGMDLGFSVTLGAHQSIGFKGILLFGTEAQKEKYLPKLASGEWIAAFALTEPSSGSDAASIRTTAVLSEDGK 167

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370483927  81 HYILNGSKVWITNGGLANIFTVFAKTEVVDSDGSVKDKITAFIVERDFGGVTNGKPEDKLGIRGSNTCEVHFENTKIPVE 160
Cdd:cd01161   168 HYVLNGSKIWITNGGIADIFTVFAKTEVKDATGSVKDKITAFIVERSFGGVTNGPPEKKMGIKGSNTAEVYFEDVKIPVE 247

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370483927 161 NILGEVGDGFKVAMNILNSGRFSMGSVVAGLLKRLIEMTAEYACTRKQFNKRLSEFGLIQEKFALMAQKAYVMESMTYLT 240
Cdd:cd01161   248 NVLGEVGDGFKVAMNILNNGRFGMGAALIGTMKRCIEKAVDYANNRKQFGKKIHEFGLIQEKLANMAILQYATESMAYMT 327

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370483927 241 AGMLDQPGFPDCSIEAAMVKVFSSEAAWQCVSEALQILGGLGYTRDYPYERILRDTRILLIFEGTNEILRMYIALTGLQH 320
Cdd:cd01161   328 SGNMDRGLKAEYQIEAAISKVFASEAAWLVVDEAIQIHGGMGFMREYGVERVLRDLRIFRIFEGTNEILRLFIALTGLQH 407


                  ..
gi 1370483927 321 AG 322
Cdd:cd01161   408 AG 409
CaiA COG1960
Acyl-CoA dehydrogenase related to the alkylation response protein AidB [Lipid transport and ...
 2-314 2.13e-126

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: 373.02  E-value: 2.13e-126
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370483927   2 YSRLGEIISM-DGSITVTLAAHqAIGLKGIILAGTEEQKAKYLPKLASGEHIAAFCLTEPASGSDAASIRSRATLSEDkk 80
Cdd:COG1960    69 LALVLEELARaDASLALPVGVH-NGAAEALLRFGTEEQKERYLPRLASGEWIGAFALTEPGAGSDAAALRTTAVRDGD-- 145

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370483927  81 HYILNGSKVWITNGGLANIFTVFAKTEvvDSDGSvkDKITAFIVERDFGGVTNGKPEDKLGIRGSNTCEVHFENTKIPVE 160
Cdd:COG1960   146 GYVLNGQKTFITNAPVADVILVLARTD--PAAGH--RGISLFLVPKDTPGVTVGRIEDKMGLRGSDTGELFFDDVRVPAE 221

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370483927 161 NILGEVGDGFKVAMNILNSGRFSMGSVVAGLLKRLIEMTAEYACTRKQFNKRLSEFGLIQEKFALMAQKAYVMESMTYLT 240
Cdd:COG1960   222 NLLGEEGKGFKIAMSTLNAGRLGLAAQALGIAEAALELAVAYAREREQFGRPIADFQAVQHRLADMAAELEAARALVYRA 301

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1370483927 241 AGMLDQPGfpDCSIEAAMVKVFSSEAAWQCVSEALQILGGLGYTRDYPYERILRDTRILLIFEGTNEILRMYIA 314
Cdd:COG1960   302 AWLLDAGE--DAALEAAMAKLFATEAALEVADEALQIHGGYGYTREYPLERLYRDARILTIYEGTNEIQRLIIA 373
ACAD cd00567
Acyl-CoA dehydrogenase; Both mitochondrial acyl-CoA dehydrogenases (ACAD) and peroxisomal ...
 25-314 1.00e-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: 359.29  E-value: 1.00e-121
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370483927  25 IGLKGIILAGTEEQKAKYLPKLASGEHIAAFCLTEPASGSDAASIRSRATLSEDkkHYILNGSKVWITNGGLANIFTVFA 104
Cdd:cd00567    43 LGAALLLAYGTEEQKERYLPPLASGEAIAAFALTEPGAGSDLAGIRTTARKDGD--GYVLNGRKIFISNGGDADLFIVLA 120

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370483927 105 KTevvDSDGSVKDKITAFIVERDFGGVTNGKPEDKLGIRGSNTCEVHFENTKIPVENILGEVGDGFKVAMNILNSGRFSM 184
Cdd:cd00567   121 RT---DEEGPGHRGISAFLVPADTPGVTVGRIWDKMGMRGSGTGELVFDDVRVPEDNLLGEEGGGFELAMKGLNVGRLLL 197

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370483927 185 GSVVAGLLKRLIEMTAEYACTRKQFNKRLSEFGLIQEKFALMAQKAYVMESMTYLTAGMLDQpGFPDCSIEAAMVKVFSS 264
Cdd:cd00567   198 AAVALGAARAALDEAVEYAKQRKQFGKPLAEFQAVQFKLADMAAELEAARLLLYRAAWLLDQ-GPDEARLEAAMAKLFAT 276

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|
gi 1370483927 265 EAAWQCVSEALQILGGLGYTRDYPYERILRDTRILLIFEGTNEILRMYIA 314
Cdd:cd00567   277 EAAREVADLAMQIHGGRGYSREYPVERYLRDARAARIAEGTAEIQRLIIA 326
SCAD_SBCAD cd01158
Short chain acyl-CoA dehydrogenases and eukaryotic short/branched chain acyl-CoA ...
 7-314 6.16e-120

Short chain acyl-CoA dehydrogenases and eukaryotic short/branched chain acyl-CoA dehydrogenases; Short chain acyl-CoA dehydrogenase (SCAD). SCAD is a mitochondrial beta-oxidation enzyme. It catalyzes the alpha,beta dehydrogenation of the corresponding trans-enoyl-CoA by FAD, which becomes reduced. The reduced form of SCAD is reoxidized in the oxidative half-reaction by electron-transferring flavoprotein (ETF), from which the electrons are transferred to the mitochondrial respiratory chain coupled with ATP synthesis. This subgroup also contains the eukaryotic short/branched chain acyl-CoA dehydrogenase(SBCAD), the bacterial butyryl-CoA dehydorgenase(BCAD) and 2-methylbutyryl-CoA dehydrogenase, which is involved in isoleucine catabolism. These enzymes are homotetramers.


Pssm-ID: 173847 [Multi-domain]  Cd Length: 373  Bit Score: 356.58  E-value: 6.16e-120
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370483927   7 EIISMDGSITVTLAAHQAIGLKGIILAGTEEQKAKYLPKLASGEHIAAFCLTEPASGSDAASIRSRATLSEDkkHYILNG 86
Cdd:cd01158    69 ELAKVDASVAVIVSVHNSLGANPIIKFGTEEQKKKYLPPLATGEKIGAFALSEPGAGSDAAALKTTAKKDGD--DYVLNG 146

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370483927  87 SKVWITNGGLANIFTVFAKTevvdsDGSVKDK-ITAFIVERDFGGVTNGKPEDKLGIRGSNTCEVHFENTKIPVENILGE 165
Cdd:cd01158   147 SKMWITNGGEADFYIVFAVT-----DPSKGYRgITAFIVERDTPGLSVGKKEDKLGIRGSSTTELIFEDVRVPKENILGE 221

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370483927 166 VGDGFKVAMNILNSGRFSMGSVVAGLLKRLIEMTAEYACTRKQFNKRLSEFGLIQEKFALMAQKAYVMESMTYlTAGMLD 245
Cdd:cd01158   222 EGEGFKIAMQTLDGGRIGIAAQALGIAQAALDAAVDYAKERKQFGKPIADFQGIQFKLADMATEIEAARLLTY-KAARLK 300

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1370483927 246 QPGFPdCSIEAAMVKVFSSEAAWQCVSEALQILGGLGYTRDYPYERILRDTRILLIFEGTNEILRMYIA 314
Cdd:cd01158   301 DNGEP-FIKEAAMAKLFASEVAMRVTTDAVQIFGGYGYTKDYPVERYYRDAKITEIYEGTSEIQRLVIA 368
IVD cd01156
Isovaleryl-CoA dehydrogenase; Isovaleryl-CoA dehydrogenase (IVD) is an is an acyl-CoA ...
 7-314 3.06e-94

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: 290.85  E-value: 3.06e-94
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370483927   7 EIISMDGSITVTLAAHQAIGLKGIILAGTEEQKAKYLPKLASGEHIAAFCLTEPASGSDAASIRSRATlsEDKKHYILNG 86
Cdd:cd01156    72 EISRASGSVALSYGAHSNLCINQIYRNGSAAQKEKYLPKLISGEHIGALAMSEPNAGSDVVSMKLRAE--KKGDRYVLNG 149

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370483927  87 SKVWITNGGLANIFTVFAKTEVvdsdGSVKDKITAFIVERDFGGVTNGKPEDKLGIRGSNTCEVHFENTKIPVENILGEV 166
Cdd:cd01156   150 SKMWITNGPDADTLVVYAKTDP----SAGAHGITAFIVEKGMPGFSRAQKLDKLGMRGSNTCELVFEDCEVPEENILGGE 225

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370483927 167 GDGFKVAMNILNSGRFSMGSVVAGLLKRLIEMTAEYACTRKQFNKRLSEFGLIQEKFA-----LMAQKAYVMESMTYLTA 241
Cdd:cd01156   226 NKGVYVLMSGLDYERLVLAGGPIGIMQAALDVAIPYAHQRKQFGQPIGEFQLVQGKLAdmytrLNASRSYLYTVAKACDR 305

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1370483927 242 GMLDqpgfpdcSIEAAMVKVFSSEAAWQCVSEALQILGGLGYTRDYPYERILRDTRILLIFEGTNEILRMYIA 314
Cdd:cd01156   306 GNMD-------PKDAAGVILYAAEKATQVALDAIQILGGNGYINDYPTGRLLRDAKLYEIGAGTSEIRRMVIG 371
IBD cd01162
Isobutyryl-CoA dehydrogenase; Isobutyryl-CoA dehydrogenase (IBD) catalyzes the alpha, beta- ...
 34-314 1.06e-80

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: 255.83  E-value: 1.06e-80
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370483927  34 GTEEQKAKYLPKLASGEHIAAFCLTEPASGSDAASIRSRATLSEDkkHYILNGSKVWITNGGLANIFTVFAKTevvdsDG 113
Cdd:cd01162    97 GNDEQRERFLPDLCTMEKLASYCLTEPGSGSDAAALRTRAVREGD--HYVLNGSKAFISGAGDSDVYVVMART-----GG 169

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370483927 114 SVKDKITAFIVERDFGGVTNGKPEDKLGIRGSNTCEVHFENTKIPVENILGEVGDGFKVAMNILNSGRFSMGSVVAGLLK 193
Cdd:cd01162   170 EGPKGISCFVVEKGTPGLSFGANEKKMGWNAQPTRAVIFEDCRVPVENRLGGEGQGFGIAMAGLNGGRLNIASCSLGAAQ 249

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370483927 194 RLIEMTAEYACTRKQFNKRLSEFGLIQEKFALMAQKAYVMESMTYLTAGMLDQpGFPDCSIEAAMVKVFSSEAAWQCVSE 273
Cdd:cd01162   250 AALDLARAYLEERKQFGKPLADFQALQFKLADMATELVASRLMVRRAASALDR-GDPDAVKLCAMAKRFATDECFDVANQ 328

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|.
gi 1370483927 274 ALQILGGLGYTRDYPYERILRDTRILLIFEGTNEILRMYIA 314
Cdd:cd01162   329 ALQLHGGYGYLKDYPVEQYVRDLRVHQILEGTNEIMRLIIA 369
LCAD cd01160
Long chain acyl-CoA dehydrogenase; LCAD is an acyl-CoA dehydrogenases (ACAD), which is found ...
 13-314 2.70e-76

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: 244.33  E-value: 2.70e-76
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370483927  13 GSITVTLAAHQAIGLKGIILAGTEEQKAKYLPKLASGEHIAAFCLTEPASGSDAASIRSRATLseDKKHYILNGSKVWIT 92
Cdd:cd01160    74 GGSGPGLSLHTDIVSPYITRAGSPEQKERVLPQMVAGKKIGAIAMTEPGAGSDLQGIRTTARK--DGDHYVLNGSKTFIT 151

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370483927  93 NGGLANIFTVFAKTevvDSDGSVKDKITAFIVERDFGGVTNGKPEDKLGIRGSNTCEVHFENTKIPVENILGEVGDGFKV 172
Cdd:cd01160   152 NGMLADVVIVVART---GGEARGAGGISLFLVERGTPGFSRGRKLKKMGWKAQDTAELFFDDCRVPAENLLGEENKGFYY 228

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370483927 173 AMNILNSGRFSMGSVVAGLLKRLIEMTAEYACTRKQFNKRLSEFGLIQEKFALMAQKAYVMESMTYLTAGMLDQPGFPdc 252
Cdd:cd01160   229 LMQNLPQERLLIAAGALAAAEFMLEETRNYVKQRKAFGKTLAQLQVVRHKIAELATKVAVTRAFLDNCAWRHEQGRLD-- 306

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1370483927 253 SIEAAMVKVFSSEAAWQCVSEALQILGGLGYTRDYPYERILRDTRILLIFEGTNEILRMYIA 314
Cdd:cd01160   307 VAEASMAKYWATELQNRVAYECVQLHGGWGYMREYPIARAYRDARVQPIYGGTTEIMKELIS 368
PLN02519 PLN02519
isovaleryl-CoA dehydrogenase
 7-313 8.94e-72

isovaleryl-CoA dehydrogenase


Pssm-ID: 215284 [Multi-domain]  Cd Length: 404  Bit Score: 233.62  E-value: 8.94e-72
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370483927   7 EIISMDGSITVTLAAHQAIGLKGIILAGTEEQKAKYLPKLASGEHIAAFCLTEPASGSDAASIRSRATLSEdkKHYILNG 86
Cdd:PLN02519   98 EISRASGSVGLSYGAHSNLCINQLVRNGTPAQKEKYLPKLISGEHVGALAMSEPNSGSDVVSMKCKAERVD--GGYVLNG 175

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370483927  87 SKVWITNGGLANIFTVFAKTEVvdSDGSvkDKITAFIVERDFGGVTNGKPEDKLGIRGSNTCEVHFENTKIPVENILGEV 166
Cdd:PLN02519  176 NKMWCTNGPVAQTLVVYAKTDV--AAGS--KGITAFIIEKGMPGFSTAQKLDKLGMRGSDTCELVFENCFVPEENVLGQE 251

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370483927 167 GDGFKVAMNILNSGRFSMGSVVAGLLKRLIEMTAEYACTRKQFNKRLSEFGLIQEKFA-----LMAQKAYVMESMTYLTA 241
Cdd:PLN02519  252 GKGVYVMMSGLDLERLVLAAGPLGLMQACLDVVLPYVRQREQFGRPIGEFQFIQGKLAdmytsLQSSRSYVYSVARDCDN 331

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1370483927 242 GMLDQpgfPDCsieaAMVKVFSSEAAWQCVSEALQILGGLGYTRDYPYERILRDTRILLIFEGTNEILRMYI 313
Cdd:PLN02519  332 GKVDR---KDC----AGVILCAAERATQVALQAIQCLGGNGYINEYPTGRLLRDAKLYEIGAGTSEIRRMLI 396
MCAD cd01157
Medium chain acyl-CoA dehydrogenase; MCADs are mitochondrial beta-oxidation enzymes, which ...
 24-320 5.15e-67

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: 220.15  E-value: 5.15e-67
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370483927  24 AIGLKGIILAGTEEQKAKYLPKLASGEHIAAFCLTEPASGSDAASIRSRATLSEDKkhYILNGSKVWITNGGLANIFTVF 103
Cdd:cd01157    87 SLGQMPVIISGNDEQKKKYLGRMTEEPLMCAYCVTEPGAGSDVAGIKTKAEKKGDE--YIINGQKMWITNGGKANWYFLL 164

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370483927 104 AKTEVvDSDGSVKDKITAFIVERDFGGVTNGKPEDKLGIRGSNTCEVHFENTKIPVENILGEVGDGFKVAMNILNSGRFS 183
Cdd:cd01157   165 ARSDP-DPKCPASKAFTGFIVEADTPGIQPGRKELNMGQRCSDTRGITFEDVRVPKENVLIGEGAGFKIAMGAFDKTRPP 243

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370483927 184 MGSVVAGLLKRLIEMTAEYACTRKQFNKRLSEFGLIQEKFALMAQKAYVMESMTYLTAGMLDQPgfPDCSIEAAMVKVFS 263
Cdd:cd01157   244 VAAGAVGLAQRALDEATKYALERKTFGKLIAEHQAVSFMLADMAMKVELARLAYQRAAWEVDSG--RRNTYYASIAKAFA 321

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1370483927 264 SEAAWQCVSEALQILGGLGYTRDYPYERILRDTRILLIFEGTNEILRMYIALTGLQH 320
Cdd:cd01157   322 ADIANQLATDAVQIFGGNGFNSEYPVEKLMRDAKIYQIYEGTSQIQRLIISREHLGK 378
PTZ00461 PTZ00461
isovaleryl-CoA dehydrogenase; Provisional
 7-307 8.29e-61

isovaleryl-CoA dehydrogenase; Provisional


Pssm-ID: 185640 [Multi-domain]  Cd Length: 410  Bit Score: 204.79  E-value: 8.29e-61
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370483927   7 EIISMDGSITVTLAAHQAIGLKGIILAGTEEQKAKYLPKLASGEHIAAFCLTEPASGSDAASIRSRATLSEDKKhYILNG 86
Cdd:PTZ00461  107 ELSKYDPGFCLAYLAHSMLFVNNFYYSASPAQRARWLPKVLTGEHVGAMGMSEPGAGTDVLGMRTTAKKDSNGN-YVLNG 185

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370483927  87 SKVWITNGGLANIFTVFAKtevvdsdgsVKDKITAFIVERDFGGVTNGKPEDKLGIRGSNTCEVHFENTKIPVENILGEV 166
Cdd:PTZ00461  186 SKIWITNGTVADVFLIYAK---------VDGKITAFVVERGTKGFTQGPKIDKCGMRASHMCQLFFEDVVVPAENLLGEE 256

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370483927 167 GDGFKVAMNILNSGRFSMGSVVAGLLKRLIEMTAEYACTRKQFNKRLSEFGLIQEKFALMAQKAYVMESMTYLTAGMLdQ 246
Cdd:PTZ00461  257 GKGMVGMMRNLELERVTLAAMAVGIAERSVELMTSYASERKAFGKPISNFGQIQRYIAEGYADTEAAKALVYSVSHNV-H 335

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1370483927 247 PGFPDcSIEAAMVKVFSSEAAWQCVSEALQILGGLGYTRDYPYERILRDTRILLIFEGTNE 307
Cdd:PTZ00461  336 PGNKN-RLGSDAAKLFATPIAKKVADSAIQVMGGMGYSRDMPVERLWRDAKLLEIGGGTIE 395
GCD cd01151
Glutaryl-CoA dehydrogenase; Glutaryl-CoA dehydrogenase (GCD). GCD is an acyl-CoA dehydrogenase, ...
 7-319 8.89e-59

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: 198.74  E-value: 8.89e-59
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370483927   7 EIISMDGSITVTLAAHQAIGLKGIILAGTEEQKAKYLPKLASGEHIAAFCLTEPASGSDAASIRSRATlsEDKKHYILNG 86
Cdd:cd01151    82 EVERVDSGYRSFMSVQSSLVMLPIYDFGSEEQKQKYLPKLASGELIGCFGLTEPNHGSDPGGMETRAR--KDGGGYKLNG 159

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370483927  87 SKVWITNGGLANIFTVFAKTEvvdsdgsVKDKITAFIVERDFGGVTNGKPEDKLGIRGSNTCEVHFENTKIPVENILGEV 166
Cdd:cd01151   160 SKTWITNSPIADVFVVWARND-------ETGKIRGFILERGMKGLSAPKIQGKFSLRASITGEIVMDNVFVPEENLLPGA 232

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370483927 167 gDGFKVAMNILNSGRFSMGSVVAGLLKRLIEMTAEYACTRKQFNKRLSEFGLIQEKFALMAQKAYVMESMTYLTAGMLDQ 246
Cdd:cd01151   233 -EGLRGPFKCLNNARYGIAWGALGAAEDCYHTARQYVLDRKQFGRPLAAFQLVQKKLADMLTEIALGLLACLRVGRLKDQ 311

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1370483927 247 PGF-PDcsiEAAMVKVFSSEAAWQCVSEALQILGGLGYTRDYPYERILRDTRILLIFEGTNEI--LRMYIALTGLQ 319
Cdd:cd01151   312 GKAtPE---QISLLKRNNCGKALEIARTAREMLGGNGISDEYHIIRHMVNLESVNTYEGTHDIhaLILGRAITGIQ 384
ACAD_fadE5 cd01153
Putative acyl-CoA dehydrogenases similar to fadE5; Putative acyl-CoA dehydrogenase (ACAD). ...
 24-308 2.86e-55

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: 190.29  E-value: 2.86e-55
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370483927  24 AIGLKGIILA-GTEEQKAKYLPKLASGEHIAAFCLTEPASGSDAASIRSRATLSEDKKHYIlNGSKVWITNG---GLANI 99
Cdd:cd01153    89 TQGAAATLLAhGTEAQREKWIPRLAEGEWTGTMCLTEPDAGSDLGALRTKAVYQADGSWRI-NGVKRFISAGehdMSENI 167

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370483927 100 F-TVFAKTEVVDSDgsVKDkITAFIV-ERDFGGVTNG----KPEDKLGIRGSNTCEVHFENTKIPvenILGEVGDGFKVA 173
Cdd:cd01153   168 VhLVLARSEGAPPG--VKG-LSLFLVpKFLDDGERNGvtvaRIEEKMGLHGSPTCELVFDNAKGE---LIGEEGMGLAQM 241

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370483927 174 MNILNSGRFSMGSVVAGLLKRLIEMTAEYACTRKQFNKRLSEFGLIQE------KFALMAQKAYVMES--MTYLTAGMLD 245
Cdd:cd01153   242 FAMMNGARLGVGTQGTGLAEAAYLNALAYAKERKQGGDLIKAAPAVTIihhpdvRRSLMTQKAYAEGSraLDLYTATVQD 321

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1370483927 246 QPGFPDCSIEAA------------MVKVFSSEAAWQCVSEALQILGGLGYTRDYPYERILRDTRILLIFEGTNEI 308
Cdd:cd01153   322 LAERKATEGEDRkalsaladlltpVVKGFGSEAALEAVSDAIQVHGGSGYTREYPIEQYYRDARITTIYEGTTGI 396
PRK12341 PRK12341
acyl-CoA dehydrogenase;
34-314 6.59e-47

acyl-CoA dehydrogenase;


Pssm-ID: 183454 [Multi-domain]  Cd Length: 381  Bit Score: 167.21  E-value: 6.59e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370483927  34 GTEEQKAK-YLPKLASGEhiAAFCL--TEPASGSDAASIRSRATlSEDKKHYiLNGSKVWITNGGLANIFTVFAKtevvD 110
Cdd:PRK12341  100 GSAEQLRKtAESTLETGD--PAYALalTEPGAGSDNNSATTTYT-RKNGKVY-LNGQKTFITGAKEYPYMLVLAR----D 171

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370483927 111 SDGSVKDK-ITAFIVERDFGGVTNgKPEDKLGIRGSNTCEVHFENTKIPVENILGEVGDGFKVAMNILNSGRFSMGSVVA 189
Cdd:PRK12341  172 PQPKDPKKaFTLWWVDSSKPGIKI-NPLHKIGWHMLSTCEVYLDNVEVEESDLVGEEGMGFLNVMYNFEMERLINAARSL 250

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370483927 190 GLLKRLIEMTAEYACTRKQFNKRLSEFGLIQEKFALMAQKAYVMESMTYLTAGMLDQpGFPdCSIEAAMVKVFSSEAAWQ 269
Cdd:PRK12341  251 GFAECAFEDAARYANQRIQFGKPIGHNQLIQEKLTLMAIKIENMRNMVYKVAWQADN-GQS-LRTSAALAKLYCARTAME 328

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*
gi 1370483927 270 CVSEALQILGGLGYTRDYPYERILRDTRILLIFEGTNEILrMYIA 314
Cdd:PRK12341  329 VIDDAIQIMGGLGYTDEARVSRFWRDVRCERIGGGTDEIM-IYIA 372
ACAD_fadE6_17_26 cd01152
Putative acyl-CoA dehydrogenases similar to fadE6, fadE17, and fadE26; Putative acyl-CoA ...
 12-319 1.43e-46

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: 166.37  E-value: 1.43e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370483927  12 DGSITVTLAAHqaiglkgIILA-GTEEQKAKYLPKLASGEHIaaFCL--TEPASGSDAASIRSRATLSEDkkHYILNGSK 88
Cdd:cd01152    84 FNQIGIDLAGP-------TILAyGTDEQKRRFLPPILSGEEI--WCQgfSEPGAGSDLAGLRTRAVRDGD--DWVVNGQK 152

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370483927  89 VWITNGGLANIFTVFAKTevvdsDGSVK--DKITAFIVERDFGGVT-------NGKPEdklgirgsnTCEVHFENTKIPV 159
Cdd:cd01152   153 IWTSGAHYADWAWLLVRT-----DPEAPkhRGISILLVDMDSPGVTvrpirsiNGGEF---------FNEVFLDDVRVPD 218

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370483927 160 ENILGEVGDGFKVAMNILNSGRFSMGSVVAGLLKRLIemtaEYACTRKQFNKRLSEFGLIQEKFALMAQKAYVMESMTYL 239
Cdd:cd01152   219 ANRVGEVNDGWKVAMTTLNFERVSIGGSAATFFELLL----ARLLLLTRDGRPLIDDPLVRQRLARLEAEAEALRLLVFR 294

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370483927 240 TAGMLDQPGFPDcsIEAAMVKVFSSEAAwQCVSE-ALQILGGLGYTRDYP--------YERILRDTRILLIFEGTNEILR 310
Cdd:cd01152   295 LASALAAGKPPG--AEASIAKLFGSELA-QELAElALELLGTAALLRDPApgaelagrWEADYLRSRATTIYGGTSEIQR 371


                  ....*....
gi 1370483927 311 MYIALTGLQ 319
Cdd:cd01152   372 NIIAERLLG 380
PRK03354 PRK03354
crotonobetainyl-CoA dehydrogenase; Validated
 26-319 4.58e-44

crotonobetainyl-CoA dehydrogenase; Validated


Pssm-ID: 179566 [Multi-domain]  Cd Length: 380  Bit Score: 159.61  E-value: 4.58e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370483927  26 GLKGIILAGTEEQKAKYLPKLASGEHIAAFCLTEPASGSDAASIRSRATlSEDKKHYiLNGSKVWITNGGLANIFTVFAK 105
Cdd:PRK03354   93 GFNTFLREGTQEQIDKIMAFRGTGKQMWNSAITEPGAGSDVGSLKTTYT-RRNGKVY-LNGSKCFITSSAYTPYIVVMAR 170

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370483927 106 tevvDSDGSVKDKITAFIVERDFGGVTNGKPEdKLGIRGSNTCEVHFENTKIPVENILGEVGDGFKVAMNILNSGRFSMG 185
Cdd:PRK03354  171 ----DGASPDKPVYTEWFVDMSKPGIKVTKLE-KLGLRMDSCCEITFDDVELDEKDMFGREGNGFNRVKEEFDHERFLVA 245

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370483927 186 SVVAGLLKRLIEMTAEYACTRKQFNKRLSEFGLIQEKFALMAQKAYVMESMTYLTAGMLDQPGFPdcSIEAAMVKVFSSE 265
Cdd:PRK03354  246 LTNYGTAMCAFEDAARYANQRVQFGEAIGRFQLIQEKFAHMAIKLNSMKNMLYEAAWKADNGTIT--SGDAAMCKYFCAN 323

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1370483927 266 AAWQCVSEALQILGGLGYTRDYPYERILRDTRILLIFEGTNEilrMYIALTGLQ 319
Cdd:PRK03354  324 AAFEVVDSAMQVLGGVGIAGNHRISRFWRDLRVDRVSGGSDE---MQILTLGRA 374
Acyl-CoA_dh_1 pfam00441
Acyl-CoA dehydrogenase, C-terminal domain; C-terminal domain of Acyl-CoA dehydrogenase is an ...
 167-314 7.80e-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: 151.64  E-value: 7.80e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370483927 167 GDGFKVAMNILNSGRFSMGSVVAGLLKRLIEMTAEYACTRKQFNKRLSEFGLIQEKFALMAQKAYVMESMTYLTAGMLDQ 246
Cdd:pfam00441   1 GRGFRVAMETLNHERLAIAAMALGLARRALDEALAYARRRKAFGRPLIDFQLVRHKLAEMAAEIEAARLLVYRAAEALDA 80

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1370483927 247 pGFPDcSIEAAMVKVFSSEAAWQCVSEALQILGGLGYTRDYPYERILRDTRILLIFEGTNEILRMYIA 314
Cdd:pfam00441  81 -GGPD-GAEASMAKLYASEAAVEVADLAMQLHGGYGYLREYPVERLYRDARVLRIGEGTSEIQRNIIA 146
ACAD_FadE2 cd01155
Acyl-CoA dehydrogenases similar to fadE2; FadE2-like Acyl-CoA dehydrogenase (ACAD). Acyl-CoA ...
 30-319 2.18e-39

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: 147.15  E-value: 2.18e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370483927  30 IILAGTEEQKAKYLPKLASGEHIAAFCLTEPA-SGSDAASIRsrATLSEDKKHYILNGSKVWITNGG--LANIFTVFAKT 106
Cdd:cd01155   104 LHRYGSEEQKKQWLEPLLDGKIRSAFAMTEPDvASSDATNIE--CSIERDGDDYVINGRKWWSSGAGdpRCKIAIVMGRT 181

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370483927 107 evvDSDGSVKDKITAFI-VERDFGGVTNGKPedkLGIRGSNT-----CEVHFENTKIPVENILGEVGDGFKVAMNILNSG 180
Cdd:cd01155   182 ---DPDGAPRHRQQSMIlVPMDTPGVTIIRP---LSVFGYDDaphghAEITFDNVRVPASNLILGEGRGFEIAQGRLGPG 255

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370483927 181 RF--SMGSVvaGLLKRLIEMTAEYACTRKQFNKRLSEFGLIQEKFAlmaqKAYVMESMTYL----TAGMLDQPGFPDCSI 254
Cdd:cd01155   256 RIhhCMRLI--GAAERALELMCQRAVSREAFGKKLAQHGVVAHWIA----KSRIEIEQARLlvlkAAHMIDTVGNKAARK 329

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1370483927 255 EAAMVKVFSSEAAWQCVSEALQILGGLGYTRDYPYERILRDTRILLIFEGTNEILRMYIALTGLQ 319
Cdd:cd01155   330 EIAMIKVAAPRMALKIIDRAIQVHGAAGVSQDTPLANMYAWARTLRIADGPDEVHLRSIARMELK 394
PLN02526 PLN02526
acyl-coenzyme A oxidase
 7-308 2.62e-34

acyl-coenzyme A oxidase


Pssm-ID: 178141 [Multi-domain]  Cd Length: 412  Bit Score: 133.44  E-value: 2.62e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370483927   7 EIISMDGSITVTLAAHQAIGLKGIILAGTEEQKAKYLPKLASGEHIAAFCLTEPASGSDAASIRSRATLSEDKkhYILNG 86
Cdd:PLN02526   98 EVARVDASCSTFILVHSSLAMLTIALCGSEAQKQKYLPSLAQLDTVACWALTEPDYGSDASSLNTTATKVEGG--WILNG 175

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370483927  87 SKVWITNGGLANIFTVFAKTevvdsdgSVKDKITAFIVERDFGGVTNGKPEDKLGIRGSNTCEVHFENTKIPVENILGEV 166
Cdd:PLN02526  176 QKRWIGNSTFADVLVIFARN-------TTTNQINGFIVKKGAPGLKATKIENKIGLRMVQNGDIVLKDVFVPDEDRLPGV 248

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370483927 167 gDGFKVAMNILNSGRFSMGSVVAGLLKRLIEMTAEYACTRKQFNKRLSEFGLIQEKFALMAQKAYVMESM------TYLT 240
Cdd:PLN02526  249 -NSFQDTNKVLAVSRVMVAWQPIGISMGVYDMCHRYLKERKQFGAPLAAFQINQEKLVRMLGNIQAMFLVgwrlckLYES 327

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1370483927 241 AGMldQPGfpdcsiEAAMVKVFSSEAAWQCVSEALQILGGLGYTRDYPYERILRDTRILLIFEGTNEI 308
Cdd:PLN02526  328 GKM--TPG------HASLGKAWITKKARETVALGRELLGGNGILADFLVAKAFCDLEPIYTYEGTYDI 387
AidB cd01154
Proteins involved in DNA damage response, similar to the AidB gene product; AidB is one of ...
 15-309 4.95e-34

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: 132.88  E-value: 4.95e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370483927  15 ITVTLAAhqaigLKGIILAGTEEQKaKYLPKLASGEH----IAAFCLTEPASGSDAASIRSRATLSEDKKhYILNGSKvW 90
Cdd:cd01154   113 LTMTDAA-----VYALRKYGPEELK-QYLPGLLSDRYktglLGGTWMTEKQGGSDLGANETTAERSGGGV-YRLNGHK-W 184

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370483927  91 ITNGGLANIFTVFAKTEvvDSDGSVKDkITAFIVER-DFGGVTNG----KPEDKLGIRGSNTCEVHFENTkipVENILGE 165
Cdd:cd01154   185 FASAPLADAALVLARPE--GAPAGARG-LSLFLVPRlLEDGTRNGyrirRLKDKLGTRSVATGEVEFDDA---EAYLIGD 258

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370483927 166 VGDGFKVAMNILNSGRFSMGSVVAGLLKRLIEMTAEYACTRKQFNKRLSEFGLIQEKFALMAQKAYVMESMTYLTAGMLD 245
Cdd:cd01154   259 EGKGIYYILEMLNISRLDNAVAALGIMRRALSEAYHYARHRRAFGKPLIDHPLMRRDLAEMEVDVEAATALTFRAARAFD 338

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1370483927 246 QPGfPDCSIEAAMVKVFS-------SEAAWQCVSEALQILGGLGYTRDYPYERILRDTRILLIFEGTNEIL 309
Cdd:cd01154   339 RAA-ADKPVEAHMARLATpvakliaCKRAAPVTSEAMEVFGGNGYLEEWPVARLHREAQVTPIWEGTGNIQ 408
fadE PRK09463
acyl-CoA dehydrogenase; Reviewed
 34-282 1.27e-31

acyl-CoA dehydrogenase; Reviewed


Pssm-ID: 236528 [Multi-domain]  Cd Length: 777  Bit Score: 129.17  E-value: 1.27e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370483927  34 GTEEQKAKYLPKLASGEHIAAFCLTEPASGSDAASIRS-----RATLSEDKKHYI-LNGSKVWITnggLANIFTVFA--- 104
Cdd:PRK09463  176 GTDEQKDHYLPRLARGEEIPCFALTSPEAGSDAGSIPDtgvvcKGEWQGEEVLGMrLTWNKRYIT---LAPIATVLGlaf 252

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370483927 105 KteVVDSDGSVKDK----ITAFIVERDFGGVTNGKPEDKLGirgsntceVHFEN--TK-----IPVENILGE---VGDGF 170
Cdd:PRK09463  253 K--LYDPDGLLGDKedlgITCALIPTDTPGVEIGRRHFPLN--------VPFQNgpTRgkdvfIPLDYIIGGpkmAGQGW 322

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370483927 171 KVAMNILNSGR-FSMGSVVAGLLKRLIEMTAEYACTRKQFNKRLSEFGLIQEKFALMAQKAYVMESMTYLTAGMLDQPGF 249
Cdd:PRK09463  323 RMLMECLSVGRgISLPSNSTGGAKLAALATGAYARIRRQFKLPIGKFEGIEEPLARIAGNAYLMDAARTLTTAAVDLGEK 402

                         250       260       270
                  ....*....|....*....|....*....|...
gi 1370483927 250 PdcSIEAAMVKVFSSEAAWQCVSEALQILGGLG 282
Cdd:PRK09463  403 P--SVLSAIAKYHLTERGRQVINDAMDIHGGKG 433
Acyl-CoA_dh_M pfam02770
Acyl-CoA dehydrogenase, middle domain; Central domain of Acyl-CoA dehydrogenase has a ...
 54-153 3.44e-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: 107.37  E-value: 3.44e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370483927  54 AFCLTEPASGSDAASIRSRAtLSEDKKHYILNGSKVWITNGGLANIFTVFAKTEvvdsDGSVKDKITAFIVERDFGGVTN 133
Cdd:pfam02770   1 AFALTEPGAGSDVASLKTTA-ADGDGGGWVLNGTKWWITNAGIADLFLVLARTG----GDDRHGGISLFLVPKDAPGVSV 75

                          90       100
                  ....*....|....*....|
gi 1370483927 134 GKPEDKLGIRGSNTCEVHFE 153
Cdd:pfam02770  76 RRIETKLGVRGLPTGELVFD 95
PRK13026 PRK13026
acyl-CoA dehydrogenase; Reviewed
 34-282 1.99e-27

acyl-CoA dehydrogenase; Reviewed


Pssm-ID: 237277 [Multi-domain]  Cd Length: 774  Bit Score: 116.21  E-value: 1.99e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370483927  34 GTEEQKAKYLPKLASGEHIAAFCLTEPASGSDAASIRSRATLSE---DKKHYI---LNGSKVWITnggLANIFTV----F 103
Cdd:PRK13026  175 GTQEQKDYWLPRLADGTEIPCFALTGPEAGSDAGAIPDTGIVCRgefEGEEVLglrLTWDKRYIT---LAPVATVlglaF 251

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370483927 104 aktEVVDSDGSVKDK----ITAFIVERDFGGVTNGKPEDKLGIR---GSNTCEVHFentkIPVENILG---EVGDGFKVA 173
Cdd:PRK13026  252 ---KLRDPDGLLGDKkelgITCALIPTDHPGVEIGRRHNPLGMAfmnGTTRGKDVF----IPLDWIIGgpdYAGRGWRML 324

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370483927 174 MNILNSGR-FSMGSVVAGLLKRLIEMTAEYACTRKQFNKRLSEFGLIQEKFALMAQKAYVMESMTYLTAGMLDQPGFPdc 252
Cdd:PRK13026  325 VECLSAGRgISLPALGTASGHMATRTTGAYAYVRRQFGMPIGQFEGVQEALARIAGNTYLLEAARRLTTTGLDLGVKP-- 402

                         250       260       270
                  ....*....|....*....|....*....|
gi 1370483927 253 SIEAAMVKVFSSEAAWQCVSEALQILGGLG 282
Cdd:PRK13026  403 SVVTAIAKYHMTELARDVVNDAMDIHAGKG 432
PTZ00456 PTZ00456
acyl-CoA dehydrogenase; Provisional
 23-308 4.00e-26

acyl-CoA dehydrogenase; Provisional


Pssm-ID: 185635 [Multi-domain]  Cd Length: 622  Bit Score: 111.88  E-value: 4.00e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370483927  23 QAIG-LKGIILAGTEEQKAKYLPKLASGEHIAAFCLTEPASGSDAASIRSRATLSEDKKhYILNGSKVWITNGG---LAN 98
Cdd:PTZ00456  152 LSIGaANTLMAWGSEEQKEQYLTKLVSGEWSGTMCLTEPQCGTDLGQVKTKAEPSADGS-YKITGTKIFISAGDhdlTEN 230

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370483927  99 I-FTVFAKTEvvDSDGSVKDkITAFIVER----DFGGVTNGKP------EDKLGIRGSNTCEVHFENTkipVENILGEVG 167
Cdd:PTZ00456  231 IvHIVLARLP--NSLPTTKG-LSLFLVPRhvvkPDGSLETAKNvkciglEKKMGIKGSSTCQLSFENS---VGYLIGEPN 304

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370483927 168 DGFKVAMNILNSGRfsMGSVVAGLLKRLIEMTAEYACTRKQFNKRLSEFGLIQEKFA------------LMAQKAyVME- 234
Cdd:PTZ00456  305 AGMKQMFTFMNTAR--VGTALEGVCHAELAFQNALRYARERRSMRALSGTKEPEKPAdriichanvrqnILFAKA-VAEg 381

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370483927 235 --SMTYLTAGMLD-QPGFPDCSIEAAM----------VKVFSSEAAWQCVSEALQILGGLGYTRDYPYERILRDTRILLI 301
Cdd:PTZ00456  382 grALLLDVGRLLDiHAAAKDAATREALdheigfytpiAKGCLTEWGVEAASRCLQVWGGHGYIKGNGMEQILRDARIGTL 461


                  ....*..
gi 1370483927 302 FEGTNEI 308
Cdd:PTZ00456  462 YEGTTGI 468
PTZ00457 PTZ00457
acyl-CoA dehydrogenase; Provisional
 34-448 3.67e-20

acyl-CoA dehydrogenase; Provisional


Pssm-ID: 185636 [Multi-domain]  Cd Length: 520  Bit Score: 93.41  E-value: 3.67e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370483927  34 GTEEQKAKYLPKLASGEHIAAFClTEPASGSDAASIRSRATLSEDKKhYILNGSKvWITNGGLANIFTVFAKT---EVVD 110
Cdd:PTZ00457  117 GSKELKGKYLTAMSDGTIMMGWA-TEEGCGSDISMNTTKASLTDDGS-YVLTGQK-RCEFAASATHFLVLAKTltqTAAE 193

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370483927 111 SDGSVKDKITAFIVERDFGGVTngkpedklgIRGSNtceVHFENTkiPVENILGEVGDGFKVAMNILNSGRFSMGSVVAG 190
Cdd:PTZ00457  194 EGATEVSRNSFFICAKDAKGVS---------VNGDS---VVFENT--PAADVVGVVGEGFKDAMITLFTEQYLYAASLLG 259

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370483927 191 LLKRLIEmtaeyactrkQFNKRLSEFGlIQEKFALMAQKAYVMESMTYLTAGMLDQPGfPDCSIEAAMVKVFSSEAawqc 270
Cdd:PTZ00457  260 IMKRVVQ----------ELRGSNAEEG-ATDTVASFACAMYAMESTLYALTANLDLPT-EDSLLECTLVSAFVQST---- 323

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370483927 271 VSEALQILgGLGYTRDYPYERILRDTRILLIFEGTNEILRMYIALTGLQHAG----RILTTRIHELKQAKVSTVMDTVG- 345
Cdd:PTZ00457  324 TNQLLSIL-ETATPPSTTLEKCFANARLFLSMMESRDFLYSSAVCCGVEDYGlffqRASTLQMMQARTLRSLGVRDRVPi 402

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370483927 346 RRLRDSlgrtvdlgltgnhgvvhpSLADSAnkfeenTYCFGRTVETLLLRFGKTIMEEQLVLKRVANILINLYGMTAVLS 425
Cdd:PTZ00457  403 KNLPDC------------------SLIDEA------VVAFGNAVEATFVRSGSQVPYQQLLLNRLGEAASLLYAASAVAS 458

                         410       420
                  ....*....|....*....|...
gi 1370483927 426 RASRSIRIGLRNHDHEVLLANTF 448
Cdd:PTZ00457  459 RASMCVSKGLPSAKVEGELASAF 481
PLN02876 PLN02876
acyl-CoA dehydrogenase
 34-321 1.31e-19

acyl-CoA dehydrogenase


Pssm-ID: 215473 [Multi-domain]  Cd Length: 822  Bit Score: 92.17  E-value: 1.31e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370483927  34 GTEEQKAKYLPKLASGEHIAAFCLTEP-ASGSDAASIRsrATLSEDKKHYILNGSKvWITNGGL---ANIFTVFAKTevv 109
Cdd:PLN02876  533 GNKEQQLEWLIPLLEGKIRSGFAMTEPqVASSDATNIE--CSIRRQGDSYVINGTK-WWTSGAMdprCRVLIVMGKT--- 606

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370483927 110 DSDGSVKDKITAFIVERDFGGVTNGKPEDKLGIRGS--NTCEVHFENTKIPVENI-LGEvGDGFKVAMNILNSGRFSMGS 186
Cdd:PLN02876  607 DFNAPKHKQQSMILVDIQTPGVQIKRPLLVFGFDDAphGHAEISFENVRVPAKNIlLGE-GRGFEIAQGRLGPGRLHHCM 685

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370483927 187 VVAGLLKRLIEMTAEYACTRKQFNKRLSEFGliqeKFALMAQKAYVMESMTYL----TAGMLDQPGFPDCSIEAAMVKVF 262
Cdd:PLN02876  686 RLIGAAERGMQLMVQRALSRKAFGKLIAQHG----SFLSDLAKCRVELEQTRLlvleAADQLDRLGNKKARGIIAMAKVA 761

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1370483927 263 SSEAAWQCVSEALQILGGLGYTRDYPYERILRDTRILLIFEGTNEILRMYIALTGLQHA 321
Cdd:PLN02876  762 APNMALKVLDMAMQVHGAAGVSSDTVLAHLWATARTLRIADGPDEVHLGTIAKLELQRA 820
AXO cd01150
Peroxisomal acyl-CoA oxidase; Peroxisomal acyl-CoA oxidases (AXO) catalyze the first set in ...
 12-339 7.17e-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: 80.45  E-value: 7.17e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370483927  12 DGSITVTLAAHQAIGLKGIILAGTEEQKAKYLPKLASGEHIAAFCLTEPASGSDAASIRSRATLSEDKKHYILN-----G 86
Cdd:cd01150    95 DLSLGAKLGLHLGLFGNAIKNLGTDEHQDYWLQGANNLEIIGCFAQTELGHGSNLQGLETTATYDPLTQEFVINtpdftA 174

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370483927  87 SKVWItnGGL---ANIFTVFAKTEVVDSDGSVKdkitAFIVE-RDFG------GVTNGKPEDKLGIRGSNTCEVHFENTK 156
Cdd:cd01150   175 TKWWP--GNLgktATHAVVFAQLITPGKNHGLH----AFIVPiRDPKthqplpGVTVGDIGPKMGLNGVDNGFLQFRNVR 248

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370483927 157 IPVENILGEVGD----------------GFKVAMNILNSGRFSMGSVVAGLLKRLIEMTAEYACTRKQFNKRLS------ 214
Cdd:cd01150   249 IPRENLLNRFGDvspdgtyvspfkdpnkRYGAMLGTRSGGRVGLIYDAAMSLKKAATIAIRYSAVRRQFGPKPSdpevqi 328

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370483927 215 -EFGLIQEKFALMAQKAYV------------MESMTYLTAGMLDQpgFPDCSIEAAMVKVFSSEAAWQCVSEALQILGGL 281
Cdd:cd01150   329 lDYQLQQYRLFPQLAAAYAfhfaakslvemyHEIIKELLQGNSEL--LAELHALSAGLKAVATWTAAQGIQECREACGGH 406

                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1370483927 282 GYTrDYPYERILR-DTRILLIFEGTNEILrmyialtgLQHAGRILTTRIHELKQAKVST 339
Cdd:cd01150   407 GYL-AMNRLPTLRdDNDPFCTYEGDNTVL--------LQQTANYLLKKYAQAFSLADYL 456
PRK11561 PRK11561
isovaleryl CoA dehydrogenase; Provisional
 57-309 1.05e-11

isovaleryl CoA dehydrogenase; Provisional


Pssm-ID: 183199 [Multi-domain]  Cd Length: 538  Bit Score: 67.08  E-value: 1.05e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370483927  57 LTEPASGSDAASIRSRATLSEDKKhYILNGSKvWITNGGLANIFTVFAKTevvdsdgsvKDKITAFIVERDF-GGVTNG- 134
Cdd:PRK11561  184 MTEKQGGSDVLSNTTRAERLADGS-YRLVGHK-WFFSVPQSDAHLVLAQA---------KGGLSCFFVPRFLpDGQRNAi 252

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370483927 135 ---KPEDKLGIRGSNTCEVHFENTkipVENILGEVGDGFKvamNILNSG---RF--SMGSvvAGLLKRLIEMTAEYACTR 206
Cdd:PRK11561  253 rleRLKDKLGNRSNASSEVEFQDA---IGWLLGEEGEGIR---LILKMGgmtRFdcALGS--HGLMRRAFSVAIYHAHQR 324

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370483927 207 KQFNKRLSEFGLIQEkfaLMAQKAYVMESMTYLT---AGMLDQPGFPDcsiEAAMVKVFSSEAAWQ-C------VSEALQ 276
Cdd:PRK11561  325 QVFGKPLIEQPLMRQ---VLSRMALQLEGQTALLfrlARAWDRRADAK---EALWARLFTPAAKFViCkrgipfVAEAME 398

                         250       260       270
                  ....*....|....*....|....*....|...
gi 1370483927 277 ILGGLGYTRDYPYERILRDTRILLIFEGTNEIL 309
Cdd:PRK11561  399 VLGGIGYCEESELPRLYREMPVNSIWEGSGNIM 431
PLN02636 PLN02636
acyl-coenzyme A oxidase
 10-314 1.18e-11

acyl-coenzyme A oxidase


Pssm-ID: 215342 [Multi-domain]  Cd Length: 686  Bit Score: 67.19  E-value: 1.18e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370483927  10 SMDGSITVTLAAHQAIGLKGIILAGTEEQKAKYLPKLASGEHIAAFCLTEPASGSDAASIRSRATLSEDKKHYILN---- 85
Cdd:PLN02636  132 SVDMSLGIKLGVQYSLWGGSVINLGTKKHRDKYFDGIDNLDYPGCFAMTELHHGSNVQGLQTTATFDPLTDEFVINtpnd 211

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370483927  86 -GSKVWITNGGLANIF-TVFAKTEVV--DSDGSVKDKITAFIVE-RDFG------GVTNGKPEDKLGIRGSNTCEVHFEN 154
Cdd:PLN02636  212 gAIKWWIGNAAVHGKFaTVFARLKLPthDSKGVSDMGVHAFIVPiRDMKthqvlpGVEIRDCGHKVGLNGVDNGALRFRS 291

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370483927 155 TKIPVENILGEVGD----------------GFKVAMNILNSGRFSMGSVVAGLLKRLIEMTAEYACTRKQFN-KRLSEFG 217
Cdd:PLN02636  292 VRIPRDNLLNRFGDvsrdgkytsslptinkRFAATLGELVGGRVGLAYGSVGVLKASNTIAIRYSLLRQQFGpPKQPEIS 371

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370483927 218 LI-----QEKFALMAQKAYVMESMT-YLT---AGML---DQPGFPDCSIEAAMVKVFSSEAAWQCVSEALQILGGLGYTR 285
Cdd:PLN02636  372 ILdyqsqQHKLMPMLASTYAFHFATeYLVerySEMKkthDDQLVADVHALSAGLKAYITSYTAKALSTCREACGGHGYAA 451

                         330       340
                  ....*....|....*....|....*....
gi 1370483927 286 DYPYERILRDTRILLIFEGTNEILRMYIA 314
Cdd:PLN02636  452 VNRFGSLRNDHDIFQTFEGDNTVLLQQVA 480
Acyl-CoA_dh_N pfam02771
Acyl-CoA dehydrogenase, N-terminal domain; The N-terminal domain of Acyl-CoA dehydrogenase is ...
 12-50 1.95e-10

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: 57.86  E-value: 1.95e-10
                          10        20        30
                  ....*....|....*....|....*....|....*....
gi 1370483927  12 DGSITVTLAAHQAIGLKGIILAGTEEQKAKYLPKLASGE 50
Cdd:pfam02771  75 DASVALALSVHSSLGAPPILRFGTEEQKERYLPKLASGE 113
Acyl-CoA_dh_2 pfam08028
Acyl-CoA dehydrogenase, C-terminal domain;
183-307 9.18e-09

Acyl-CoA dehydrogenase, C-terminal domain;


Pssm-ID: 429790 [Multi-domain]  Cd Length: 133  Bit Score: 53.89  E-value: 9.18e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370483927 183 SMGSVVAGLLKRLIEMTAEYACTRKQ--FNKRLSEFGLIQEKFALMA----QKAYVMESMTYLTAGMLDQ--PGFPDCSI 254
Cdd:pfam08028   1 GIAAAALGAARAALAEFTERARGRVRayFGVPLAEDPATQLALAEAAaridAARLLLERAAARIEAAAAAgkPVTPALRA 80

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1370483927 255 EAAMVKVFSSEAAWQCVSEALQILGGLGYTRDYPYERILRDTRILLIFEGTNE 307
Cdd:pfam08028  81 EARRAAAFATELAVAAVDALFRAAGGSALFQDSPLQRIWRDIHAAAQHAAVNP 133
PTZ00460 PTZ00460
acyl-CoA dehydrogenase; Provisional
 20-424 2.58e-07

acyl-CoA dehydrogenase; Provisional


Pssm-ID: 185639 [Multi-domain]  Cd Length: 646  Bit Score: 53.31  E-value: 2.58e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370483927  20 AAHQAIGLKGIILAGTEEQKAKYLPKLASGEHIAAFCLTEPASGSDAASIRSRATLSEDKKHYILN-----GSKVWITN- 93
Cdd:PTZ00460   96 TVHFAMVIPAFQVLGTDEQINLWMPSLLNFEIVGCYAQTELGHGSDVQNLETTATYDKQTNEFVIHtpsveAVKFWPGEl 175

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370483927  94 GGLANIFTVFAKTEVvdsDGSVKDkITAFIVE-RDFG------GVTNGKPEDKLGIRGSNTCEVHFENTKIPVENIL--- 163
Cdd:PTZ00460  176 GFLCNFALVYAKLIV---NGKNKG-VHPFMVRiRDKEthkplqGVEVGDIGPKMGYAVKDNGFLSFDHYRIPLDSLLary 251

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370483927 164 ------GEV---GDGfKVAMNILNSGRFSMGSVVAGLLKRLIEMTAEYACTRKQFNK------RLSEFGLIQEK-FALMA 227
Cdd:PTZ00460  252 ikvsedGQVerqGNP-KVSYASMMYMRNLIIDQYPRFAAQALTVAIRYSIYRQQFTNdnkqenSVLEYQTQQQKlLPLLA 330

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370483927 228 QkAYVMeSMTYLTAGMLDQPGF-----PDCSIEAAMVKVFSSEAAW--QCVSEALQ----ILGGLGYTRDYPYERILRDT 296
Cdd:PTZ00460  331 E-FYAC-IFGGLKIKELVDDNFnrvqkNDFSLLQLTHAILSAAKANytYFVSNCAEwcrlSCGGHGYAHYSGLPAIYFDM 408

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370483927 297 RILLIFEGTNEILRMYIA---LTGLQHA-----------GRILT-----------TRIHELKQAKVSTVMDTVGRRLRDS 351
Cdd:PTZ00460  409 SPNITLEGENQIMYLQLArylLKQLQHAvqkpekvpeyfNFLSHitekladqttiESLGQLLGLNCTILTIYAAKKIMDH 488

                         410       420       430       440       450       460       470
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1370483927 352 LGRTVDLGLTGNHgVVHPSLADSANKFEEN-TYcfgrtvetllLRFGKTIMEEQLVLKRVANILINLYGMTAVL 424
Cdd:PTZ00460  489 INTGKDFQQSWDT-KSGIALASAASRFIEYfNY----------LCFLDTINNANKSTKEILTQLADLYGITMLL 551
PLN02443 PLN02443
acyl-coenzyme A oxidase
 34-283 6.70e-06

acyl-coenzyme A oxidase


Pssm-ID: 178062 [Multi-domain]  Cd Length: 664  Bit Score: 48.68  E-value: 6.70e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370483927  34 GTEEQKAKYLPKLASGEHIAAFCLTEPASGSDAASIRSRATLSEDKKHYILN-----GSKVWitNGGLANIFT---VFAK 105
Cdd:PLN02443  114 GTEEQQKKWLPLAYKMQIIGCYAQTELGHGSNVQGLETTATFDPKTDEFVIHsptltSSKWW--PGGLGKVSThavVYAR 191

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370483927 106 tevVDSDGsvKDK-ITAFIVE-------RDFGGVTNGKPEDKLGIRGSNTCE---VHFENTKIPVENILGEVG----DGF 170
Cdd:PLN02443  192 ---LITNG--KDHgIHGFIVQlrslddhSPLPGVTVGDIGMKFGNGAYNTMDngfLRFDHVRIPRDQMLMRLSkvtrEGK 266

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370483927 171 KVAMNI---LNSGR--FSMGSVVAG---LLKRLIEMTAEYACTRKQFNKRLS--EFGLIQEK------FALMAQkAY--- 231
Cdd:PLN02443  267 YVQSDVprqLVYGTmvYVRQTIVADastALSRAVCIATRYSAVRRQFGSQDGgpETQVIDYKtqqsrlFPLLAS-AYafr 345

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1370483927 232 -VMESMTYLTAGML------DQPGFPDCSIEAAMVKVFSSEAAWQCVSEALQILGGLGY 283
Cdd:PLN02443  346 fVGEWLKWLYTDVTqrleanDFSTLPEAHACTAGLKSLTTSATADGIEECRKLCGGHGY 404
PLN02312 PLN02312
acyl-CoA oxidase
 5-209 1.75e-05

acyl-CoA oxidase


Pssm-ID: 215178 [Multi-domain]  Cd Length: 680  Bit Score: 47.46  E-value: 1.75e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370483927   5 LGEIISM-DGSITVTLAAHQAIGLKGIILAGTEEQKAKYLPKLASGEHIAAFCLTEPASGSDAASIRSRATLSEDKKHYI 83
Cdd:PLN02312  138 LLEVIGIyDHSLAIKLGVHFFLWGGAIKFLGTKRHHDKWLKDTEDYVVKGCFAMTELGHGSNVRGIETVTTYDPKTEEFV 217

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370483927  84 LN-----GSKVWItnGGLANIFT---VFAKTEVvdsDGsVKDKITAFIVE-RDFGGVT--NGKPED---KLGIRGSNTCE 149
Cdd:PLN02312  218 INtpcesAQKYWI--GGAANHAThtiVFSQLHI---NG-KNEGVHAFIAQiRDQDGNIcpNIRIADcghKIGLNGVDNGR 291

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1370483927 150 VHFENTKIPVENILGEVGD----------------GFKVAMNILNSGRFSMGSVVAGLLKRLIEMTAEYACTRKQF 209
Cdd:PLN02312  292 IWFDNLRIPRENLLNSVADvspdgkyvsaikdpdqRFGAFLAPLTSGRVTIAVSAIYSSKVGLAIAIRYSLSRRAF 367
DszC cd01163
Dibenzothiophene (DBT) desulfurization enzyme C; DszC is a flavin reductase dependent enzyme, ...
 7-164 2.32e-05

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: 46.55  E-value: 2.32e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370483927   7 EIISMDGSITVTLAAHQAIgLKGIILAGTEEQKAKYLPKLASGeHIAAFCLTEpaSGSDAASIRSRATLSEDKkHYILNG 86
Cdd:cd01163    61 ELAAADSNIAQALRAHFGF-VEALLLAGPEQFRKRWFGRVLNG-WIFGNAVSE--RGSVRPGTFLTATVRDGG-GYVLNG 135

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370483927  87 SKvWITNGGLaniFTVFAKTEVVDSDGsvkdKITAFIVERDFGGVTNGKPEDKLGIR--GSNTceVHFENTKIPVENILG 164
Cdd:cd01163   136 KK-FYSTGAL---FSDWVTVSALDEEG----KLVFAAVPTDRPGITVVDDWDGFGQRltASGT--VTFDNVRVEPDEVLP 205
 
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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