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Conserved domains on  [gi|1065243|pdb|1BUC|A]
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Chain A, BUTYRYL-COA DEHYDROGENASE

Protein Classification

acyl-CoA dehydrogenase( domain architecture ID 10100181)

acyl-CoA dehydrogenase, with similarity to short- and short/branched-chain CoA dehydrogenases, participates in consecutive cycles of fatty acid beta-oxidation to produce acetyl-CoA and reducing equivalents for generating energy

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
SCAD_SBCAD cd01158
Short chain acyl-CoA dehydrogenases and eukaryotic short/branched chain acyl-CoA ...
7-383 0e+00

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: 588.85  E-value: 0e+00
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1BUC_A        7 DIQQDFLKLAHDFGEKKLAPTVTERDHKGIYDKELIDELLSLGITGAYFEEKYGGSGDDggdVLSYILAVEELAKYDAGV 86
Cdd:cd01158   1 EEHQMIRKTVRDFAEKEIAPLAAEMDEKGEFPREVIKEMAELGLMGIPIPEEYGGAGLD---FLAYAIAIEELAKVDASV 77
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1BUC_A       87 AITLSATVSLCANPIWQFGTEAQKEKFLVPLVEGTKLGAFGLTEPNAGTDASGQQTIATKNDDgTYTLNGSKIFITNGGA 166
Cdd:cd01158  78 AVIVSVHNSLGANPIIKFGTEEQKKKYLPPLATGEKIGAFALSEPGAGSDAAALKTTAKKDGD-DYVLNGSKMWITNGGE 156
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1BUC_A      167 ADIYIVFAMTDKSKGNHGITAFILEDGTPGFTYGKKEDKMGIHTSQTMELVFQDVKVPAENMLGEEGKGFKIAMMTLDGG 246
Cdd:cd01158 157 ADFYIVFAVTDPSKGYRGITAFIVERDTPGLSVGKKEDKLGIRGSSTTELIFEDVRVPKENILGEEGEGFKIAMQTLDGG 236
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1BUC_A      247 RIGVAAQALGIAEAALADAVEYSKQRVQFGKPLCKFQSISFKLADMKMQIEAARNLVYKAACKKQEGKPFTVDAAIAKRV 326
Cdd:cd01158 237 RIGIAAQALGIAQAALDAAVDYAKERKQFGKPIADFQGIQFKLADMATEIEAARLLTYKAARLKDNGEPFIKEAAMAKLF 316
                       330       340       350       360       370
                ....*....|....*....|....*....|....*....|....*....|....*..
1BUC_A      327 ASDVAMRVTTEAVQIFGGYGYSEEYPVARHMRDAKITQIYEGTNEVQLMVTGGALLR 383
Cdd:cd01158 317 ASEVAMRVTTDAVQIFGGYGYTKDYPVERYYRDAKITEIYEGTSEIQRLVIAKHLLK 373
 
Name Accession Description Interval E-value
SCAD_SBCAD cd01158
Short chain acyl-CoA dehydrogenases and eukaryotic short/branched chain acyl-CoA ...
7-383 0e+00

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: 588.85  E-value: 0e+00
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1BUC_A        7 DIQQDFLKLAHDFGEKKLAPTVTERDHKGIYDKELIDELLSLGITGAYFEEKYGGSGDDggdVLSYILAVEELAKYDAGV 86
Cdd:cd01158   1 EEHQMIRKTVRDFAEKEIAPLAAEMDEKGEFPREVIKEMAELGLMGIPIPEEYGGAGLD---FLAYAIAIEELAKVDASV 77
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1BUC_A       87 AITLSATVSLCANPIWQFGTEAQKEKFLVPLVEGTKLGAFGLTEPNAGTDASGQQTIATKNDDgTYTLNGSKIFITNGGA 166
Cdd:cd01158  78 AVIVSVHNSLGANPIIKFGTEEQKKKYLPPLATGEKIGAFALSEPGAGSDAAALKTTAKKDGD-DYVLNGSKMWITNGGE 156
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1BUC_A      167 ADIYIVFAMTDKSKGNHGITAFILEDGTPGFTYGKKEDKMGIHTSQTMELVFQDVKVPAENMLGEEGKGFKIAMMTLDGG 246
Cdd:cd01158 157 ADFYIVFAVTDPSKGYRGITAFIVERDTPGLSVGKKEDKLGIRGSSTTELIFEDVRVPKENILGEEGEGFKIAMQTLDGG 236
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1BUC_A      247 RIGVAAQALGIAEAALADAVEYSKQRVQFGKPLCKFQSISFKLADMKMQIEAARNLVYKAACKKQEGKPFTVDAAIAKRV 326
Cdd:cd01158 237 RIGIAAQALGIAQAALDAAVDYAKERKQFGKPIADFQGIQFKLADMATEIEAARLLTYKAARLKDNGEPFIKEAAMAKLF 316
                       330       340       350       360       370
                ....*....|....*....|....*....|....*....|....*....|....*..
1BUC_A      327 ASDVAMRVTTEAVQIFGGYGYSEEYPVARHMRDAKITQIYEGTNEVQLMVTGGALLR 383
Cdd:cd01158 317 ASEVAMRVTTDAVQIFGGYGYTKDYPVERYYRDAKITEIYEGTSEIQRLVIAKHLLK 373
CaiA COG1960
Acyl-CoA dehydrogenase related to the alkylation response protein AidB [Lipid transport and ...
1-383 1.46e-171

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: 483.57  E-value: 1.46e-171
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1BUC_A        1 MDFNLTDIQQDFLKLAHDFGEKKLAPTVTERDHKGIYDKELIDELLSLGITGAYFEEKYGGSGDDggdVLSYILAVEELA 80
Cdd:COG1960   1 MDFELTEEQRALRDEVREFAEEEIAPEAREWDREGEFPRELWRKLAELGLLGLTIPEEYGGLGLS---LVELALVLEELA 77
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1BUC_A       81 KYDAGVAITLSATVSlCANPIWQFGTEAQKEKFLVPLVEGTKLGAFGLTEPNAGTDASGQQTIATKNDDGtYTLNGSKIF 160
Cdd:COG1960  78 RADASLALPVGVHNG-AAEALLRFGTEEQKERYLPRLASGEWIGAFALTEPGAGSDAAALRTTAVRDGDG-YVLNGQKTF 155
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1BUC_A      161 ITNGGAADIYIVFAMTDKSKGNHGITAFILEDGTPGFTYGKKEDKMGIHTSQTMELVFQDVKVPAENMLGEEGKGFKIAM 240
Cdd:COG1960 156 ITNAPVADVILVLARTDPAAGHRGISLFLVPKDTPGVTVGRIEDKMGLRGSDTGELFFDDVRVPAENLLGEEGKGFKIAM 235
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1BUC_A      241 MTLDGGRIGVAAQALGIAEAALADAVEYSKQRVQFGKPLCKFQSISFKLADMKMQIEAARNLVYKAACKKQEGKPFTVDA 320
Cdd:COG1960 236 STLNAGRLGLAAQALGIAEAALELAVAYAREREQFGRPIADFQAVQHRLADMAAELEAARALVYRAAWLLDAGEDAALEA 315
                       330       340       350       360       370       380
                ....*....|....*....|....*....|....*....|....*....|....*....|...
1BUC_A      321 AIAKRVASDVAMRVTTEAVQIFGGYGYSEEYPVARHMRDAKITQIYEGTNEVQLMVTGGALLR 383
Cdd:COG1960 316 AMAKLFATEAALEVADEALQIHGGYGYTREYPLERLYRDARILTIYEGTNEIQRLIIARRLLG 378
PLN02519 PLN02519
isovaleryl-CoA dehydrogenase
2-383 1.56e-88

isovaleryl-CoA dehydrogenase


Pssm-ID: 215284 [Multi-domain]  Cd Length: 404  Bit Score: 272.91  E-value: 1.56e-88
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1BUC_A         2 DFNLTDIQQDFLKLAHDFGEKKLAPTVTERDHKGIYDKE--LIDELLSLGITGAYFEEKYGGSGDDGgdvLSYILAVEEL 79
Cdd:PLN02519  23 SLLFDDTQLQFKESVQQFAQENIAPHAAAIDATNSFPKDvnLWKLMGDFNLHGITAPEEYGGLGLGY---LYHCIAMEEI 99
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1BUC_A        80 AKYDAGVAITLSATVSLCANPIWQFGTEAQKEKFLVPLVEGTKLGAFGLTEPNAGTDASGQQTIATKNDDGtYTLNGSKI 159
Cdd:PLN02519 100 SRASGSVGLSYGAHSNLCINQLVRNGTPAQKEKYLPKLISGEHVGALAMSEPNSGSDVVSMKCKAERVDGG-YVLNGNKM 178
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1BUC_A       160 FITNGGAADIYIVFAMTDKSKGNHGITAFILEDGTPGFTYGKKEDKMGIHTSQTMELVFQDVKVPAENMLGEEGKGFKIA 239
Cdd:PLN02519 179 WCTNGPVAQTLVVYAKTDVAAGSKGITAFIIEKGMPGFSTAQKLDKLGMRGSDTCELVFENCFVPEENVLGQEGKGVYVM 258
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1BUC_A       240 MMTLDGGRIGVAAQALGIAEAALADAVEYSKQRVQFGKPLCKFQSISFKLADMKMQIEAARNLVYKAACKKQEGKPFTVD 319
Cdd:PLN02519 259 MSGLDLERLVLAAGPLGLMQACLDVVLPYVRQREQFGRPIGEFQFIQGKLADMYTSLQSSRSYVYSVARDCDNGKVDRKD 338
                        330       340       350       360       370       380
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
1BUC_A       320 AAIAKRVASDVAMRVTTEAVQIFGGYGYSEEYPVARHMRDAKITQIYEGTNEVQLMVTGGALLR 383
Cdd:PLN02519 339 CAGVILCAAERATQVALQAIQCLGGNGYINEYPTGRLLRDAKLYEIGAGTSEIRRMLIGRELFK 402
Acyl-CoA_dh_1 pfam00441
Acyl-CoA dehydrogenase, C-terminal domain; C-terminal domain of Acyl-CoA dehydrogenase is an ...
233-376 7.50e-57

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: 182.84  E-value: 7.50e-57
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1BUC_A        233 GKGFKIAMMTLDGGRIGVAAQALGIAEAALADAVEYSKQRVQFGKPLCKFQSISFKLADMKMQIEAARNLVYKAACKKQE 312
Cdd:pfam00441   1 GRGFRVAMETLNHERLAIAAMALGLARRALDEALAYARRRKAFGRPLIDFQLVRHKLAEMAAEIEAARLLVYRAAEALDA 80
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
1BUC_A        313 GKPFTVDAAIAKRVASDVAMRVTTEAVQIFGGYGYSEEYPVARHMRDAKITQIYEGTNEVQLMV 376
Cdd:pfam00441  81 GGPDGAEASMAKLYASEAAVEVADLAMQLHGGYGYLREYPVERLYRDARVLRIGEGTSEIQRNI 144
 
Name Accession Description Interval E-value
SCAD_SBCAD cd01158
Short chain acyl-CoA dehydrogenases and eukaryotic short/branched chain acyl-CoA ...
7-383 0e+00

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: 588.85  E-value: 0e+00
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1BUC_A        7 DIQQDFLKLAHDFGEKKLAPTVTERDHKGIYDKELIDELLSLGITGAYFEEKYGGSGDDggdVLSYILAVEELAKYDAGV 86
Cdd:cd01158   1 EEHQMIRKTVRDFAEKEIAPLAAEMDEKGEFPREVIKEMAELGLMGIPIPEEYGGAGLD---FLAYAIAIEELAKVDASV 77
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1BUC_A       87 AITLSATVSLCANPIWQFGTEAQKEKFLVPLVEGTKLGAFGLTEPNAGTDASGQQTIATKNDDgTYTLNGSKIFITNGGA 166
Cdd:cd01158  78 AVIVSVHNSLGANPIIKFGTEEQKKKYLPPLATGEKIGAFALSEPGAGSDAAALKTTAKKDGD-DYVLNGSKMWITNGGE 156
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1BUC_A      167 ADIYIVFAMTDKSKGNHGITAFILEDGTPGFTYGKKEDKMGIHTSQTMELVFQDVKVPAENMLGEEGKGFKIAMMTLDGG 246
Cdd:cd01158 157 ADFYIVFAVTDPSKGYRGITAFIVERDTPGLSVGKKEDKLGIRGSSTTELIFEDVRVPKENILGEEGEGFKIAMQTLDGG 236
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1BUC_A      247 RIGVAAQALGIAEAALADAVEYSKQRVQFGKPLCKFQSISFKLADMKMQIEAARNLVYKAACKKQEGKPFTVDAAIAKRV 326
Cdd:cd01158 237 RIGIAAQALGIAQAALDAAVDYAKERKQFGKPIADFQGIQFKLADMATEIEAARLLTYKAARLKDNGEPFIKEAAMAKLF 316
                       330       340       350       360       370
                ....*....|....*....|....*....|....*....|....*....|....*..
1BUC_A      327 ASDVAMRVTTEAVQIFGGYGYSEEYPVARHMRDAKITQIYEGTNEVQLMVTGGALLR 383
Cdd:cd01158 317 ASEVAMRVTTDAVQIFGGYGYTKDYPVERYYRDAKITEIYEGTSEIQRLVIAKHLLK 373
CaiA COG1960
Acyl-CoA dehydrogenase related to the alkylation response protein AidB [Lipid transport and ...
1-383 1.46e-171

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: 483.57  E-value: 1.46e-171
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1BUC_A        1 MDFNLTDIQQDFLKLAHDFGEKKLAPTVTERDHKGIYDKELIDELLSLGITGAYFEEKYGGSGDDggdVLSYILAVEELA 80
Cdd:COG1960   1 MDFELTEEQRALRDEVREFAEEEIAPEAREWDREGEFPRELWRKLAELGLLGLTIPEEYGGLGLS---LVELALVLEELA 77
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1BUC_A       81 KYDAGVAITLSATVSlCANPIWQFGTEAQKEKFLVPLVEGTKLGAFGLTEPNAGTDASGQQTIATKNDDGtYTLNGSKIF 160
Cdd:COG1960  78 RADASLALPVGVHNG-AAEALLRFGTEEQKERYLPRLASGEWIGAFALTEPGAGSDAAALRTTAVRDGDG-YVLNGQKTF 155
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1BUC_A      161 ITNGGAADIYIVFAMTDKSKGNHGITAFILEDGTPGFTYGKKEDKMGIHTSQTMELVFQDVKVPAENMLGEEGKGFKIAM 240
Cdd:COG1960 156 ITNAPVADVILVLARTDPAAGHRGISLFLVPKDTPGVTVGRIEDKMGLRGSDTGELFFDDVRVPAENLLGEEGKGFKIAM 235
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1BUC_A      241 MTLDGGRIGVAAQALGIAEAALADAVEYSKQRVQFGKPLCKFQSISFKLADMKMQIEAARNLVYKAACKKQEGKPFTVDA 320
Cdd:COG1960 236 STLNAGRLGLAAQALGIAEAALELAVAYAREREQFGRPIADFQAVQHRLADMAAELEAARALVYRAAWLLDAGEDAALEA 315
                       330       340       350       360       370       380
                ....*....|....*....|....*....|....*....|....*....|....*....|...
1BUC_A      321 AIAKRVASDVAMRVTTEAVQIFGGYGYSEEYPVARHMRDAKITQIYEGTNEVQLMVTGGALLR 383
Cdd:COG1960 316 AMAKLFATEAALEVADEALQIHGGYGYTREYPLERLYRDARILTIYEGTNEIQRLIIARRLLG 378
ACAD cd00567
Acyl-CoA dehydrogenase; Both mitochondrial acyl-CoA dehydrogenases (ACAD) and peroxisomal ...
96-378 5.54e-132

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: 380.86  E-value: 5.54e-132
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1BUC_A       96 LCANPIWQFGTEAQKEKFLVPLVEGTKLGAFGLTEPNAGTDASGQQTIATKNDDGtYTLNGSKIFITNGGAADIYIVFAM 175
Cdd:cd00567  43 LGAALLLAYGTEEQKERYLPPLASGEAIAAFALTEPGAGSDLAGIRTTARKDGDG-YVLNGRKIFISNGGDADLFIVLAR 121
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1BUC_A      176 TDKS-KGNHGITAFILEDGTPGFTYGKKEDKMGIHTSQTMELVFQDVKVPAENMLGEEGKGFKIAMMTLDGGRIGVAAQA 254
Cdd:cd00567 122 TDEEgPGHRGISAFLVPADTPGVTVGRIWDKMGMRGSGTGELVFDDVRVPEDNLLGEEGGGFELAMKGLNVGRLLLAAVA 201
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1BUC_A      255 LGIAEAALADAVEYSKQRVQFGKPLCKFQSISFKLADMKMQIEAARNLVYKAACKKQEGKPF-TVDAAIAKRVASDVAMR 333
Cdd:cd00567 202 LGAARAALDEAVEYAKQRKQFGKPLAEFQAVQFKLADMAAELEAARLLLYRAAWLLDQGPDEaRLEAAMAKLFATEAARE 281
                       250       260       270       280
                ....*....|....*....|....*....|....*....|....*
1BUC_A      334 VTTEAVQIFGGYGYSEEYPVARHMRDAKITQIYEGTNEVQLMVTG 378
Cdd:cd00567 282 VADLAMQIHGGRGYSREYPVERYLRDARAARIAEGTAEIQRLIIA 326
IBD cd01162
Isobutyryl-CoA dehydrogenase; Isobutyryl-CoA dehydrogenase (IBD) catalyzes the alpha, beta- ...
5-383 2.87e-112

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: 332.49  E-value: 2.87e-112
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1BUC_A        5 LTDIQQDFLKLAHDFGEKKLAPTVTERDHKGIYDKELIDELLSLGITGAYFEEKYGGSGDDGgdvLSYILAVEELAKYDA 84
Cdd:cd01162   1 LNEEQRAIQEVARAFAAKEMAPHAADWDQKKHFPVDVLRKAAELGFGGIYIRDDVGGSGLSR---LDASIIFEALSTGCV 77
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1BUC_A       85 GVAITLSATvSLCANPIWQFGTEAQKEKFLVPLVEGTKLGAFGLTEPNAGTDASGQQTIATKNDDgTYTLNGSKIFITNG 164
Cdd:cd01162  78 STAAYISIH-NMCAWMIDSFGNDEQRERFLPDLCTMEKLASYCLTEPGSGSDAAALRTRAVREGD-HYVLNGSKAFISGA 155
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1BUC_A      165 GAADIYIVFAMTDkSKGNHGITAFILEDGTPGFTYGKKEDKMGIHTSQTMELVFQDVKVPAENMLGEEGKGFKIAMMTLD 244
Cdd:cd01162 156 GDSDVYVVMARTG-GEGPKGISCFVVEKGTPGLSFGANEKKMGWNAQPTRAVIFEDCRVPVENRLGGEGQGFGIAMAGLN 234
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1BUC_A      245 GGRIGVAAQALGIAEAALADAVEYSKQRVQFGKPLCKFQSISFKLADMKMQIEAARNLVYKAACKKQEGKPFTVD-AAIA 323
Cdd:cd01162 235 GGRLNIASCSLGAAQAALDLARAYLEERKQFGKPLADFQALQFKLADMATELVASRLMVRRAASALDRGDPDAVKlCAMA 314
                       330       340       350       360       370       380
                ....*....|....*....|....*....|....*....|....*....|....*....|
1BUC_A      324 KRVASDVAMRVTTEAVQIFGGYGYSEEYPVARHMRDAKITQIYEGTNEVQLMVTGGALLR 383
Cdd:cd01162 315 KRFATDECFDVANQALQLHGGYGYLKDYPVEQYVRDLRVHQILEGTNEIMRLIIARALLT 374
IVD cd01156
Isovaleryl-CoA dehydrogenase; Isovaleryl-CoA dehydrogenase (IVD) is an is an acyl-CoA ...
5-381 9.71e-111

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: 9.71e-111
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1BUC_A        5 LTDIQQDFLKLAHDFGEKKLAPTVTERDHKGIYDKELIDELLSLGITGAYFEEKYGGSGDDGgdvLSYILAVEELAKYDA 84
Cdd:cd01156   2 LDDEIEMLRQSVREFAQKEIAPLAAKIDRDNEFPRDLWRKMGKLGLLGITAPEEYGGSGMGY---LAHVIIMEEISRASG 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1BUC_A       85 GVAITLSATVSLCANPIWQFGTEAQKEKFLVPLVEGTKLGAFGLTEPNAGTDASGQQTIATKNDDGtYTLNGSKIFITNG 164
Cdd:cd01156  79 SVALSYGAHSNLCINQIYRNGSAAQKEKYLPKLISGEHIGALAMSEPNAGSDVVSMKLRAEKKGDR-YVLNGSKMWITNG 157
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1BUC_A      165 GAADIYIVFAMTDKSKGNHGITAFILEDGTPGFTYGKKEDKMGIHTSQTMELVFQDVKVPAENMLGEEGKGFKIAMMTLD 244
Cdd:cd01156 158 PDADTLVVYAKTDPSAGAHGITAFIVEKGMPGFSRAQKLDKLGMRGSNTCELVFEDCEVPEENILGGENKGVYVLMSGLD 237
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1BUC_A      245 GGRIGVAAQALGIAEAALADAVEYSKQRVQFGKPLCKFQSISFKLADMKMQIEAARNLVYKAACKKQEGKPFTVDAAIAK 324
Cdd:cd01156 238 YERLVLAGGPIGIMQAALDVAIPYAHQRKQFGQPIGEFQLVQGKLADMYTRLNASRSYLYTVAKACDRGNMDPKDAAGVI 317
                       330       340       350       360       370
                ....*....|....*....|....*....|....*....|....*....|....*..
1BUC_A      325 RVASDVAMRVTTEAVQIFGGYGYSEEYPVARHMRDAKITQIYEGTNEVQLMVTGGAL 381
Cdd:cd01156 318 LYAAEKATQVALDAIQILGGNGYINDYPTGRLLRDAKLYEIGAGTSEIRRMVIGREL 374
VLCAD cd01161
Very long chain acyl-CoA dehydrogenase; VLCAD is an acyl-CoA dehydrogenase (ACAD), which is ...
2-383 2.25e-102

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: 308.63  E-value: 2.25e-102
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1BUC_A        2 DFNLTDIQQDFLKL----AHDFGEKKLAPTVTerDHKGIYDKELIDELLSLGITGAYFEEKYGGSGDDGgdVLSYILAve 77
Cdd:cd01161  20 PSVLTEEQTEELNMlvgpVEKFFEEVNDPAKN--DQLEKIPRKTLTQLKELGLFGLQVPEEYGGLGLNN--TQYARLA-- 93
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1BUC_A       78 ELAKYDAGVAITLSATVSLCANPIWQFGTEAQKEKFLVPLVEGTKLGAFGLTEPNAGTDASGQQTIATKNDDGT-YTLNG 156
Cdd:cd01161  94 EIVGMDLGFSVTLGAHQSIGFKGILLFGTEAQKEKYLPKLASGEWIAAFALTEPSSGSDAASIRTTAVLSEDGKhYVLNG 173
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1BUC_A      157 SKIFITNGGAADIYIVFAMT-----DKSKGNHgITAFILEDGTPGFTYGKKEDKMGIHTSQTMELVFQDVKVPAENMLGE 231
Cdd:cd01161 174 SKIWITNGGIADIFTVFAKTevkdaTGSVKDK-ITAFIVERSFGGVTNGPPEKKMGIKGSNTAEVYFEDVKIPVENVLGE 252
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1BUC_A      232 EGKGFKIAMMTLDGGRIGVAAQALGIAEAALADAVEYSKQRVQFGKPLCKFQSISFKLADMKMQIEAARNLVYK-AACKK 310
Cdd:cd01161 253 VGDGFKVAMNILNNGRFGMGAALIGTMKRCIEKAVDYANNRKQFGKKIHEFGLIQEKLANMAILQYATESMAYMtSGNMD 332
                       330       340       350       360       370       380       390
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
1BUC_A      311 QEGKP-FTVDAAIAKRVASDVAMRVTTEAVQIFGGYGYSEEYPVARHMRDAKITQIYEGTNEVQLMVTGGALLR 383
Cdd:cd01161 333 RGLKAeYQIEAAISKVFASEAAWLVVDEAIQIHGGMGFMREYGVERVLRDLRIFRIFEGTNEILRLFIALTGLQ 406
LCAD cd01160
Long chain acyl-CoA dehydrogenase; LCAD is an acyl-CoA dehydrogenases (ACAD), which is found ...
19-372 3.90e-98

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: 296.33  E-value: 3.90e-98
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1BUC_A       19 FGEKKLAPTVTERDHKGIYDKELIDELLSLGITGAYFEEKYGGSGDDggdVLSYILAVEELAkYDAGVAITLSATVSLCA 98
Cdd:cd01160  13 FFAKEVAPFHHEWEKAGEVPREVWRKAGEQGLLGVGFPEEYGGIGGD---LLSAAVLWEELA-RAGGSGPGLSLHTDIVS 88
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1BUC_A       99 NPIWQFGTEAQKEKFLVPLVEGTKLGAFGLTEPNAGTDASGQQTIATKndDGT-YTLNGSKIFITNGGAADIYIVFAMTD 177
Cdd:cd01160  89 PYITRAGSPEQKERVLPQMVAGKKIGAIAMTEPGAGSDLQGIRTTARK--DGDhYVLNGSKTFITNGMLADVVIVVARTG 166
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1BUC_A      178 -KSKGNHGITAFILEDGTPGFTYGKKEDKMGIHTSQTMELVFQDVKVPAENMLGEEGKGFKIAMMTLDGGRIGVAAQALG 256
Cdd:cd01160 167 gEARGAGGISLFLVERGTPGFSRGRKLKKMGWKAQDTAELFFDDCRVPAENLLGEENKGFYYLMQNLPQERLLIAAGALA 246
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1BUC_A      257 IAEAALADAVEYSKQRVQFGKPLCKFQSISFKLADMKMQIEAARNLVYKAACKKQEGKPFTVDAAIAKRVASDVAMRVTT 336
Cdd:cd01160 247 AAEFMLEETRNYVKQRKAFGKTLAQLQVVRHKIAELATKVAVTRAFLDNCAWRHEQGRLDVAEASMAKYWATELQNRVAY 326
                       330       340       350
                ....*....|....*....|....*....|....*.
1BUC_A      337 EAVQIFGGYGYSEEYPVARHMRDAKITQIYEGTNEV 372
Cdd:cd01160 327 ECVQLHGGWGYMREYPIARAYRDARVQPIYGGTTEI 362
MCAD cd01157
Medium chain acyl-CoA dehydrogenase; MCADs are mitochondrial beta-oxidation enzymes, which ...
5-376 1.08e-95

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: 290.64  E-value: 1.08e-95
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1BUC_A        5 LTDIQQDFLKLAHDFGEKKLAPTVTERDHKGIYDKELIDELLSLGITGAYFEEKYGGSGDDggdVLSYILAVEELAKYDA 84
Cdd:cd01157   1 LTEQQKEFQETARKFAREEIIPVAAEYDKSGEYPWPLIKRAWELGLMNTHIPEDCGGLGLG---TFDTCLITEELAYGCT 77
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1BUC_A       85 GVAITLSATvSLCANPIWQFGTEAQKEKFLVPLVEGTKLGAFGLTEPNAGTDASGQQTIATKNDDgTYTLNGSKIFITNG 164
Cdd:cd01157  78 GVQTAIEAN-SLGQMPVIISGNDEQKKKYLGRMTEEPLMCAYCVTEPGAGSDVAGIKTKAEKKGD-EYIINGQKMWITNG 155
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1BUC_A      165 GAADIYIVFAMTD---KSKGNHGITAFILEDGTPGFTYGKKEDKMGIHTSQTMELVFQDVKVPAENMLGEEGKGFKIAMM 241
Cdd:cd01157 156 GKANWYFLLARSDpdpKCPASKAFTGFIVEADTPGIQPGRKELNMGQRCSDTRGITFEDVRVPKENVLIGEGAGFKIAMG 235
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1BUC_A      242 TLDGGRIGVAAQALGIAEAALADAVEYSKQRVQFGKPLCKFQSISFKLADMKMQIEAARNLVYKAACKKQEGKPFTVDAA 321
Cdd:cd01157 236 AFDKTRPPVAAGAVGLAQRALDEATKYALERKTFGKLIAEHQAVSFMLADMAMKVELARLAYQRAAWEVDSGRRNTYYAS 315
                       330       340       350       360       370
                ....*....|....*....|....*....|....*....|....*....|....*
1BUC_A      322 IAKRVASDVAMRVTTEAVQIFGGYGYSEEYPVARHMRDAKITQIYEGTNEVQLMV 376
Cdd:cd01157 316 IAKAFAADIANQLATDAVQIFGGNGFNSEYPVEKLMRDAKIYQIYEGTSQIQRLI 370
GCD cd01151
Glutaryl-CoA dehydrogenase; Glutaryl-CoA dehydrogenase (GCD). GCD is an acyl-CoA dehydrogenase, ...
5-380 9.93e-93

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: 283.10  E-value: 9.93e-93
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1BUC_A        5 LTDIQQDFLKLAHDFGEKKLAPTVTERDHKGIYDKELIDELLSLGITGAYFEEkYGGSGDDGgdvLSYILAVEELAKYDA 84
Cdd:cd01151  13 LTEEERAIRDTAREFCQEELAPRVLEAYREEKFDRKIIEEMGELGLLGATIKG-YGCAGLSS---VAYGLIAREVERVDS 88
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1BUC_A       85 GVAITLSATVSLCANPIWQFGTEAQKEKFLVPLVEGTKLGAFGLTEPNAGTDASGQQTIATKnDDGTYTLNGSKIFITNG 164
Cdd:cd01151  89 GYRSFMSVQSSLVMLPIYDFGSEEQKQKYLPKLASGELIGCFGLTEPNHGSDPGGMETRARK-DGGGYKLNGSKTWITNS 167
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1BUC_A      165 GAADIYIVFAmtdKSKGNHGITAFILEDGTPGFTYGKKEDKMGIHTSQTMELVFQDVKVPAENMLgEEGKGFKIAMMTLD 244
Cdd:cd01151 168 PIADVFVVWA---RNDETGKIRGFILERGMKGLSAPKIQGKFSLRASITGEIVMDNVFVPEENLL-PGAEGLRGPFKCLN 243
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1BUC_A      245 GGRIGVAAQALGIAEAALADAVEYSKQRVQFGKPLCKFQSISFKLADMKMQIEAARNLVYKAACKKQEGKPFTVDAAIAK 324
Cdd:cd01151 244 NARYGIAWGALGAAEDCYHTARQYVLDRKQFGRPLAAFQLVQKKLADMLTEIALGLLACLRVGRLKDQGKATPEQISLLK 323
                       330       340       350       360       370
                ....*....|....*....|....*....|....*....|....*....|....*.
1BUC_A      325 RVASDVAMRVTTEAVQIFGGYGYSEEYPVARHMRDAKITQIYEGTNEVQLMVTGGA 380
Cdd:cd01151 324 RNNCGKALEIARTAREMLGGNGISDEYHIIRHMVNLESVNTYEGTHDIHALILGRA 379
PLN02519 PLN02519
isovaleryl-CoA dehydrogenase
2-383 1.56e-88

isovaleryl-CoA dehydrogenase


Pssm-ID: 215284 [Multi-domain]  Cd Length: 404  Bit Score: 272.91  E-value: 1.56e-88
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1BUC_A         2 DFNLTDIQQDFLKLAHDFGEKKLAPTVTERDHKGIYDKE--LIDELLSLGITGAYFEEKYGGSGDDGgdvLSYILAVEEL 79
Cdd:PLN02519  23 SLLFDDTQLQFKESVQQFAQENIAPHAAAIDATNSFPKDvnLWKLMGDFNLHGITAPEEYGGLGLGY---LYHCIAMEEI 99
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1BUC_A        80 AKYDAGVAITLSATVSLCANPIWQFGTEAQKEKFLVPLVEGTKLGAFGLTEPNAGTDASGQQTIATKNDDGtYTLNGSKI 159
Cdd:PLN02519 100 SRASGSVGLSYGAHSNLCINQLVRNGTPAQKEKYLPKLISGEHVGALAMSEPNSGSDVVSMKCKAERVDGG-YVLNGNKM 178
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1BUC_A       160 FITNGGAADIYIVFAMTDKSKGNHGITAFILEDGTPGFTYGKKEDKMGIHTSQTMELVFQDVKVPAENMLGEEGKGFKIA 239
Cdd:PLN02519 179 WCTNGPVAQTLVVYAKTDVAAGSKGITAFIIEKGMPGFSTAQKLDKLGMRGSDTCELVFENCFVPEENVLGQEGKGVYVM 258
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1BUC_A       240 MMTLDGGRIGVAAQALGIAEAALADAVEYSKQRVQFGKPLCKFQSISFKLADMKMQIEAARNLVYKAACKKQEGKPFTVD 319
Cdd:PLN02519 259 MSGLDLERLVLAAGPLGLMQACLDVVLPYVRQREQFGRPIGEFQFIQGKLADMYTSLQSSRSYVYSVARDCDNGKVDRKD 338
                        330       340       350       360       370       380
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
1BUC_A       320 AAIAKRVASDVAMRVTTEAVQIFGGYGYSEEYPVARHMRDAKITQIYEGTNEVQLMVTGGALLR 383
Cdd:PLN02519 339 CAGVILCAAERATQVALQAIQCLGGNGYINEYPTGRLLRDAKLYEIGAGTSEIRRMLIGRELFK 402
PRK12341 PRK12341
acyl-CoA dehydrogenase;
1-383 1.94e-77

acyl-CoA dehydrogenase;


Pssm-ID: 183454 [Multi-domain]  Cd Length: 381  Bit Score: 243.87  E-value: 1.94e-77
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1BUC_A         1 MDFNLTDIQQDFLK-----LAHDFGEKKLAptvtERDHKGIYDKELIDELLSLGITGAYFEEKYGGSGDDggdVLSYILA 75
Cdd:PRK12341   1 MDFSLTEEQELLLAsirelITRNFPEEYFR----TCDENGTYPREFMRALADNGISMLGVPEEFGGTPAD---YVTQMLV 73
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1BUC_A        76 VEELAKydAGVAITLsATVSLCANPIWQFGTEAQKEKFLVPLVEGTKLG-AFGLTEPNAGTDASGQQTIATKNDDGTYtL 154
Cdd:PRK12341  74 LEEVSK--CGAPAFL-ITNGQCIHSMRRFGSAEQLRKTAESTLETGDPAyALALTEPGAGSDNNSATTTYTRKNGKVY-L 149
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1BUC_A       155 NGSKIFITNGGAADIYIVFAMTDKSKGNH-GITAFILEDGTPGFTYGKKEdKMGIHTSQTMELVFQDVKVPAENMLGEEG 233
Cdd:PRK12341 150 NGQKTFITGAKEYPYMLVLARDPQPKDPKkAFTLWWVDSSKPGIKINPLH-KIGWHMLSTCEVYLDNVEVEESDLVGEEG 228
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1BUC_A       234 KGFKIAMMTLDGGRIGVAAQALGIAEAALADAVEYSKQRVQFGKPLCKFQSISFKLADMKMQIEAARNLVYKAACKKQEG 313
Cdd:PRK12341 229 MGFLNVMYNFEMERLINAARSLGFAECAFEDAARYANQRIQFGKPIGHNQLIQEKLTLMAIKIENMRNMVYKVAWQADNG 308
                        330       340       350       360       370       380       390
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1BUC_A       314 KPFTVDAAIAKRVASDVAMRVTTEAVQIFGGYGYSEEYPVARHMRDAKITQIYEGTNEVQLMVTGGALLR 383
Cdd:PRK12341 309 QSLRTSAALAKLYCARTAMEVIDDAIQIMGGLGYTDEARVSRFWRDVRCERIGGGTDEIMIYIAGRQILK 378
PTZ00461 PTZ00461
isovaleryl-CoA dehydrogenase; Provisional
19-371 6.04e-76

isovaleryl-CoA dehydrogenase; Provisional


Pssm-ID: 185640 [Multi-domain]  Cd Length: 410  Bit Score: 240.61  E-value: 6.04e-76
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1BUC_A        19 FGEKKLAPTVTERDHKGIYDKELIDELLSLGITGAYFEEkygGSGDDGGDVLSYILAVEELAKYDAGVAITLSATVSLCA 98
Cdd:PTZ00461  51 FSREVVDKHAREDDINMHFNRDLFKQLGDLGVMGVTVPE---ADGGAGMDAVAAVIIHHELSKYDPGFCLAYLAHSMLFV 127
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1BUC_A        99 NPIWQFGTEAQKEKFLVPLVEGTKLGAFGLTEPNAGTDASGQQTIATKNDDGTYTLNGSKIFITNGGAADIYIVFAMTDK 178
Cdd:PTZ00461 128 NNFYYSASPAQRARWLPKVLTGEHVGAMGMSEPGAGTDVLGMRTTAKKDSNGNYVLNGSKIWITNGTVADVFLIYAKVDG 207
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1BUC_A       179 SkgnhgITAFILEDGTPGFTYGKKEDKMGIHTSQTMELVFQDVKVPAENMLGEEGKGFKIAMMTLDGGRIGVAAQALGIA 258
Cdd:PTZ00461 208 K-----ITAFVVERGTKGFTQGPKIDKCGMRASHMCQLFFEDVVVPAENLLGEEGKGMVGMMRNLELERVTLAAMAVGIA 282
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1BUC_A       259 EAALADAVEYSKQRVQFGKPLCKFQSISFKLADMKMQIEAARNLVYKAACKKQEGKPFTVDAAIAKRVASDVAMRVTTEA 338
Cdd:PTZ00461 283 ERSVELMTSYASERKAFGKPISNFGQIQRYIAEGYADTEAAKALVYSVSHNVHPGNKNRLGSDAAKLFATPIAKKVADSA 362
                        330       340       350
                 ....*....|....*....|....*....|...
1BUC_A       339 VQIFGGYGYSEEYPVARHMRDAKITQIYEGTNE 371
Cdd:PTZ00461 363 IQVMGGMGYSRDMPVERLWRDAKLLEIGGGTIE 395
ACAD_fadE5 cd01153
Putative acyl-CoA dehydrogenases similar to fadE5; Putative acyl-CoA dehydrogenase (ACAD). ...
13-373 6.68e-65

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: 211.86  E-value: 6.68e-65
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1BUC_A       13 LKLAHDFGEKKLAPTVTERDHKG-IYD----------KELIDELLSLGITGAYFEEKYGGSGddggdvLSYIL--AVEEL 79
Cdd:cd01153   2 LEEVARLAENVLAPLNADGDREGpVFDdgrvvvpppfKEALDAFAEAGWMALGVPEEYGGQG------LPITVysALAEI 75
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1BUC_A       80 AKYDAGVAITLSATVSlCANPIWQFGTEAQKEKFLVPLVEGTKLGAFGLTEPNAGTDASGQQTIATKNDDGTYTLNGSKI 159
Cdd:cd01153  76 FSRGDAPLMYASGTQG-AAATLLAHGTEAQREKWIPRLAEGEWTGTMCLTEPDAGSDLGALRTKAVYQADGSWRINGVKR 154
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1BUC_A      160 FITNGGAAD----IYIVFAMT-DKSKGNHGITAFI----LEDGTP-GFTYGKKEDKMGIHTSQTMELVFQDVKVPaenML 229
Cdd:cd01153 155 FISAGEHDMseniVHLVLARSeGAPPGVKGLSLFLvpkfLDDGERnGVTVARIEEKMGLHGSPTCELVFDNAKGE---LI 231
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1BUC_A      230 GEEGKGFKIAMMTLDGGRIGVAAQALGIAEAALADAVEYSKQRVQFGKPLCKFQS--------ISFKLADMKMQIEAARN 301
Cdd:cd01153 232 GEEGMGLAQMFAMMNGARLGVGTQGTGLAEAAYLNALAYAKERKQGGDLIKAAPAvtiihhpdVRRSLMTQKAYAEGSRA 311
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1BUC_A      302 LV-YKA-ACKKQEGKPFTVDAA------------IAKRVASDVAMRVTTEAVQIFGGYGYSEEYPVARHMRDAKITQIYE 367
Cdd:cd01153 312 LDlYTAtVQDLAERKATEGEDRkalsaladlltpVVKGFGSEAALEAVSDAIQVHGGSGYTREYPIEQYYRDARITTIYE 391

                ....*.
1BUC_A      368 GTNEVQ 373
Cdd:cd01153 392 GTTGIQ 397
Acyl-CoA_dh_1 pfam00441
Acyl-CoA dehydrogenase, C-terminal domain; C-terminal domain of Acyl-CoA dehydrogenase is an ...
233-376 7.50e-57

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: 182.84  E-value: 7.50e-57
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1BUC_A        233 GKGFKIAMMTLDGGRIGVAAQALGIAEAALADAVEYSKQRVQFGKPLCKFQSISFKLADMKMQIEAARNLVYKAACKKQE 312
Cdd:pfam00441   1 GRGFRVAMETLNHERLAIAAMALGLARRALDEALAYARRRKAFGRPLIDFQLVRHKLAEMAAEIEAARLLVYRAAEALDA 80
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
1BUC_A        313 GKPFTVDAAIAKRVASDVAMRVTTEAVQIFGGYGYSEEYPVARHMRDAKITQIYEGTNEVQLMV 376
Cdd:pfam00441  81 GGPDGAEASMAKLYASEAAVEVADLAMQLHGGYGYLREYPVERLYRDARVLRIGEGTSEIQRNI 144
PRK03354 PRK03354
crotonobetainyl-CoA dehydrogenase; Validated
1-383 7.05e-56

crotonobetainyl-CoA dehydrogenase; Validated


Pssm-ID: 179566 [Multi-domain]  Cd Length: 380  Bit Score: 187.73  E-value: 7.05e-56
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1BUC_A         1 MDFNLTDIQQDFLKLAHDFGEKKLAPT-VTERDHKGIYDKELIDELLSLGITGAYFEEKYGGSGDDGGDVLSyilAVEEL 79
Cdd:PRK03354   1 MDFNLNDEQELFVAGIRELMASENWEAyFAECDRDSVYPERFVKALADMGIDSLLIPEEHGGLDAGFVTLAA---VWMEL 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1BUC_A        80 AKYDAGVAITLSATVSLcaNPIWQFGTEAQKEKFLVPLVEGTKLGAFGLTEPNAGTDASGQQTIATKNDDGTYtLNGSKI 159
Cdd:PRK03354  78 GRLGAPTYVLYQLPGGF--NTFLREGTQEQIDKIMAFRGTGKQMWNSAITEPGAGSDVGSLKTTYTRRNGKVY-LNGSKC 154
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1BUC_A       160 FITNGgAADIYIVFAMTDKSKGNHGI-TAFILEDGTPGFTYGKKEdKMGIHTSQTMELVFQDVKVPAENMLGEEGKGFKI 238
Cdd:PRK03354 155 FITSS-AYTPYIVVMARDGASPDKPVyTEWFVDMSKPGIKVTKLE-KLGLRMDSCCEITFDDVELDEKDMFGREGNGFNR 232
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1BUC_A       239 AMMTLDGGRIGVAAQALGIAEAALADAVEYSKQRVQFGKPLCKFQSISFKLADMKMQIEAARNLVYKAACKKQEGKPFTV 318
Cdd:PRK03354 233 VKEEFDHERFLVALTNYGTAMCAFEDAARYANQRVQFGEAIGRFQLIQEKFAHMAIKLNSMKNMLYEAAWKADNGTITSG 312
                        330       340       350       360       370       380
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
1BUC_A       319 DAAIAKRVASDVAMRVTTEAVQIFGGYGYSEEYPVARHMRDAKITQIYEGTNEVQLMVTGGALLR 383
Cdd:PRK03354 313 DAAMCKYFCANAAFEVVDSAMQVLGGVGIAGNHRISRFWRDLRVDRVSGGSDEMQILTLGRAVLK 377
AidB cd01154
Proteins involved in DNA damage response, similar to the AidB gene product; AidB is one of ...
83-373 5.09e-52

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: 178.72  E-value: 5.09e-52
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1BUC_A       83 DAGVAITLSATvSLCANPIWQFGTEAQKEKFLVPLVEGTK---LGAFGLTEPNAGTDASGQQTIATKNDDGTYTLNGSKI 159
Cdd:cd01154 106 AAGLLCPLTMT-DAAVYALRKYGPEELKQYLPGLLSDRYKtglLGGTWMTEKQGGSDLGANETTAERSGGGVYRLNGHKW 184
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1BUC_A      160 FiTNGGAADIYIVFAMTDKSK-GNHGITAFI----LEDGT-PGFTYGKKEDKMGIHTSQTMELVFQDvkvpAEN-MLGEE 232
Cdd:cd01154 185 F-ASAPLADAALVLARPEGAPaGARGLSLFLvprlLEDGTrNGYRIRRLKDKLGTRSVATGEVEFDD----AEAyLIGDE 259
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1BUC_A      233 GKGFKIAMMTLDGGRIGVAAQALGIAEAALADAVEYSKQRVQFGKPLCKFQSISFKLADMKMQIEAARNLVYKAAC---K 309
Cdd:cd01154 260 GKGIYYILEMLNISRLDNAVAALGIMRRALSEAYHYARHRRAFGKPLIDHPLMRRDLAEMEVDVEAATALTFRAARafdR 339
                       250       260       270       280       290       300       310
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
1BUC_A      310 KQEGKP--------FTvdaAIAKRVASDVAMRVTTEAVQIFGGYGYSEEYPVARHMRDAKITQIYEGTNEVQ 373
Cdd:cd01154 340 AAADKPveahmarlAT---PVAKLIACKRAAPVTSEAMEVFGGNGYLEEWPVARLHREAQVTPIWEGTGNIQ 408
PLN02526 PLN02526
acyl-coenzyme A oxidase
5-378 8.47e-50

acyl-coenzyme A oxidase


Pssm-ID: 178141 [Multi-domain]  Cd Length: 412  Bit Score: 172.73  E-value: 8.47e-50
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1BUC_A         5 LTDIQQDFLKLAHDFGEKKLAPTVTERDHKGIYDKELIDELLSLGITGAYFEekygGSGDDGGDVLSYILAVEELAKYDA 84
Cdd:PLN02526  29 LTPEEQALRKRVRECMEKEVAPIMTEYWEKAEFPFHIIPKLGSLGIAGGTIK----GYGCPGLSITASAIATAEVARVDA 104
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1BUC_A        85 GVAITLSATVSLCANPIWQFGTEAQKEKFLVPLVEGTKLGAFGLTEPNAGTDASGQQTIATKNDDGtYTLNGSKIFITNG 164
Cdd:PLN02526 105 SCSTFILVHSSLAMLTIALCGSEAQKQKYLPSLAQLDTVACWALTEPDYGSDASSLNTTATKVEGG-WILNGQKRWIGNS 183
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1BUC_A       165 GAADIYIVFAmtdKSKGNHGITAFILEDGTPGFTYGKKEDKMGIHTSQTMELVFQDVKVPAENMLgEEGKGFKIAMMTLD 244
Cdd:PLN02526 184 TFADVLVIFA---RNTTTNQINGFIVKKGAPGLKATKIENKIGLRMVQNGDIVLKDVFVPDEDRL-PGVNSFQDTNKVLA 259
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1BUC_A       245 GGRIGVAAQALGIAEAALADAVEYSKQRVQFGKPLCKFQSISFKLADMKMQIEAARnLVYKAACKKQE-GKPFTVDAAIA 323
Cdd:PLN02526 260 VSRVMVAWQPIGISMGVYDMCHRYLKERKQFGAPLAAFQINQEKLVRMLGNIQAMF-LVGWRLCKLYEsGKMTPGHASLG 338
                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|....*
1BUC_A       324 KRVASDVAMRVTTEAVQIFGGYGYSEEYPVARHMRDAKITQIYEGTNEVQLMVTG 378
Cdd:PLN02526 339 KAWITKKARETVALGRELLGGNGILADFLVAKAFCDLEPIYTYEGTYDINALVTG 393
ACAD_FadE2 cd01155
Acyl-CoA dehydrogenases similar to fadE2; FadE2-like Acyl-CoA dehydrogenase (ACAD). Acyl-CoA ...
103-374 2.29e-49

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: 171.03  E-value: 2.29e-49
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1BUC_A      103 QFGTEAQKEKFLVPLVEGTKLGAFGLTEPN-AGTDASGQQTIATKnDDGTYTLNGSKIFITngGAAD----IYIVFAMTD 177
Cdd:cd01155 106 RYGSEEQKKQWLEPLLDGKIRSAFAMTEPDvASSDATNIECSIER-DGDDYVINGRKWWSS--GAGDprckIAIVMGRTD 182
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1BUC_A      178 -KSKGNHGITAFILED-GTPGFT-------YGKkEDKMGIHtsqtMELVFQDVKVPAENMLGEEGKGFKIAMMTLDGGRI 248
Cdd:cd01155 183 pDGAPRHRQQSMILVPmDTPGVTiirplsvFGY-DDAPHGH----AEITFDNVRVPASNLILGEGRGFEIAQGRLGPGRI 257
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1BUC_A      249 GVAAQALGIAEAALADAVEYSKQRVQFGKPLCKFQSISFKLADMKMQIEAARNLVYKAACKKQEGKPFTVDAAIA--KRV 326
Cdd:cd01155 258 HHCMRLIGAAERALELMCQRAVSREAFGKKLAQHGVVAHWIAKSRIEIEQARLLVLKAAHMIDTVGNKAARKEIAmiKVA 337
                       250       260       270       280
                ....*....|....*....|....*....|....*....|....*...
1BUC_A      327 ASDVAMRVTTEAVQIFGGYGYSEEYPVARHMRDAKITQIYEGTNEVQL 374
Cdd:cd01155 338 APRMALKIIDRAIQVHGAAGVSQDTPLANMYAWARTLRIADGPDEVHL 385
ACAD_fadE6_17_26 cd01152
Putative acyl-CoA dehydrogenases similar to fadE6, fadE17, and fadE26; Putative acyl-CoA ...
77-382 7.14e-42

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: 150.96  E-value: 7.14e-42
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1BUC_A       77 EELAKYDAGVAITLSATvSLCANPIWQFGTEAQKEKFLVPLVEGTKLGAFGLTEPNAGTDASGQQTIATKNDDGtYTLNG 156
Cdd:cd01152  73 EEMAAAGAPVPFNQIGI-DLAGPTILAYGTDEQKRRFLPPILSGEEIWCQGFSEPGAGSDLAGLRTRAVRDGDD-WVVNG 150
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1BUC_A      157 SKIFITNGGAADIYIVFAMTDKSKGNH-GITAFILEDGTPGFTYGKKEDKMGiHTSqTMELVFQDVKVPAENMLGEEGKG 235
Cdd:cd01152 151 QKIWTSGAHYADWAWLLVRTDPEAPKHrGISILLVDMDSPGVTVRPIRSING-GEF-FNEVFLDDVRVPDANRVGEVNDG 228
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1BUC_A      236 FKIAMMTLDGGR---IGVAAQALGIAEAALADAVEYskqrvqfGKPLCKFQSISFKLADMKMQIEAARNLVYKAACKKQE 312
Cdd:cd01152 229 WKVAMTTLNFERvsiGGSAATFFELLLARLLLLTRD-------GRPLIDDPLVRQRLARLEAEAEALRLLVFRLASALAA 301
                       250       260       270       280       290       300       310
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
1BUC_A      313 GKPFTVDAAIAKRVASDVAMRVTTEAVQIFGGYGY-SEEYPVA-------RHMRDAKITQIYEGTNEVQLMVTGGALL 382
Cdd:cd01152 302 GKPPGAEASIAKLFGSELAQELAELALELLGTAALlRDPAPGAelagrweADYLRSRATTIYGGTSEIQRNIIAERLL 379
PTZ00456 PTZ00456
acyl-CoA dehydrogenase; Provisional
98-373 4.28e-31

acyl-CoA dehydrogenase; Provisional


Pssm-ID: 185635 [Multi-domain]  Cd Length: 622  Bit Score: 124.60  E-value: 4.28e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1BUC_A        98 ANPIWQFGTEAQKEKFLVPLVEGTKLGAFGLTEPNAGTDASGQQTIATKNDDGTYTLNGSKIFITNGG----AADIYIVF 173
Cdd:PTZ00456 157 ANTLMAWGSEEQKEQYLTKLVSGEWSGTMCLTEPQCGTDLGQVKTKAEPSADGSYKITGTKIFISAGDhdltENIVHIVL 236
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1BUC_A       174 AMTDKSK-GNHGITAFIL------EDGT----PGFTYGKKEDKMGIHTSQTMELVFQDVKvpaENMLGEEGKGFKIAMMT 242
Cdd:PTZ00456 237 ARLPNSLpTTKGLSLFLVprhvvkPDGSletaKNVKCIGLEKKMGIKGSSTCQLSFENSV---GYLIGEPNAGMKQMFTF 313
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1BUC_A       243 LDGGRIGVAAQALGIAEAALADAVEYSKQRVQF------------GKPLCKFQSISFKLADMKMQIEAARNLVYK----- 305
Cdd:PTZ00456 314 MNTARVGTALEGVCHAELAFQNALRYARERRSMralsgtkepekpADRIICHANVRQNILFAKAVAEGGRALLLDvgrll 393
                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
1BUC_A       306 --------AACKKQEGKPFTVDAAIAKRVASDVAMRVTTEAVQIFGGYGYSEEYPVARHMRDAKITQIYEGTNEVQ 373
Cdd:PTZ00456 394 dihaaakdAATREALDHEIGFYTPIAKGCLTEWGVEAASRCLQVWGGHGYIKGNGMEQILRDARIGTLYEGTTGIQ 469
PLN02876 PLN02876
acyl-CoA dehydrogenase
103-374 3.97e-30

acyl-CoA dehydrogenase


Pssm-ID: 215473 [Multi-domain]  Cd Length: 822  Bit Score: 122.21  E-value: 3.97e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1BUC_A       103 QFGTEAQKEKFLVPLVEGTKLGAFGLTEPN-AGTDASGQQ-TIATKNDdgTYTLNGSKIFITngGAAD----IYIVFAMT 176
Cdd:PLN02876 531 RYGNKEQQLEWLIPLLEGKIRSGFAMTEPQvASSDATNIEcSIRRQGD--SYVINGTKWWTS--GAMDprcrVLIVMGKT 606
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1BUC_A       177 DKSKGNHGITAFILED-GTPG-------FTYGKKEDKMGiHTsqtmELVFQDVKVPAENMLGEEGKGFKIAMMTLDGGRI 248
Cdd:PLN02876 607 DFNAPKHKQQSMILVDiQTPGvqikrplLVFGFDDAPHG-HA----EISFENVRVPAKNILLGEGRGFEIAQGRLGPGRL 681
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1BUC_A       249 GVAAQALGIAEAALADAVEYSKQRVQFGKPLCKFQSISFKLADMKMQIEAARNLVYKAA-------CKKQEGKpftvdAA 321
Cdd:PLN02876 682 HHCMRLIGAAERGMQLMVQRALSRKAFGKLIAQHGSFLSDLAKCRVELEQTRLLVLEAAdqldrlgNKKARGI-----IA 756
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|...
1BUC_A       322 IAKRVASDVAMRVTTEAVQIFGGYGYSEEYPVARHMRDAKITQIYEGTNEVQL 374
Cdd:PLN02876 757 MAKVAAPNMALKVLDMAMQVHGAAGVSSDTVLAHLWATARTLRIADGPDEVHL 809
Acyl-CoA_dh_M pfam02770
Acyl-CoA dehydrogenase, middle domain; Central domain of Acyl-CoA dehydrogenase has a ...
125-218 7.82e-30

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: 110.45  E-value: 7.82e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1BUC_A        125 AFGLTEPNAGTDASGQQTIATKNDDGTYTLNGSKIFITNGGAADIYIVFAMTDKSKGNHGITAFILEDGTPGFTYGKKED 204
Cdd:pfam02770   1 AFALTEPGAGSDVASLKTTAADGDGGGWVLNGTKWWITNAGIADLFLVLARTGGDDRHGGISLFLVPKDAPGVSVRRIET 80
                          90
                  ....*....|....
1BUC_A        205 KMGIHTSQTMELVF 218
Cdd:pfam02770  81 KLGVRGLPTGELVF 94
Acyl-CoA_dh_2 pfam08028
Acyl-CoA dehydrogenase, C-terminal domain;
249-371 8.68e-28

Acyl-CoA dehydrogenase, C-terminal domain;


Pssm-ID: 429790 [Multi-domain]  Cd Length: 133  Bit Score: 106.28  E-value: 8.68e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1BUC_A        249 GVAAQALGIAEAALADAVEYSKQRVQ--FGKPLCKFQSISFKLADMKMQIEAARNLVYKAACKKQE----GKPFTV---- 318
Cdd:pfam08028   1 GIAAAALGAARAALAEFTERARGRVRayFGVPLAEDPATQLALAEAAARIDAARLLLERAAARIEAaaaaGKPVTPalra 80
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|...
1BUC_A        319 DAAIAKRVASDVAMRVTTEAVQIFGGYGYSEEYPVARHMRDAKITQIYEGTNE 371
Cdd:pfam08028  81 EARRAAAFATELAVAAVDALFRAAGGSALFQDSPLQRIWRDIHAAAQHAAVNP 133
Acyl-CoA_dh_N pfam02771
Acyl-CoA dehydrogenase, N-terminal domain; The N-terminal domain of Acyl-CoA dehydrogenase is ...
6-120 2.04e-27

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: 104.47  E-value: 2.04e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1BUC_A          6 TDIQQDFLKLAHDFGEKKLAPTVTERDHKGIYDKELIDELLSLGITGAYFEEKYGGSGDDGgdvLSYILAVEELAKYDAG 85
Cdd:pfam02771   1 TEEQEALRDTVREFAEEEIAPHAAEWDEEGEFPRELWKKLGELGLLGITIPEEYGGAGLDY---LAYALVAEELARADAS 77
                          90       100       110
                  ....*....|....*....|....*....|....*
1BUC_A         86 VAITLSATVSLCANPIWQFGTEAQKEKFLVPLVEG 120
Cdd:pfam02771  78 VALALSVHSSLGAPPILRFGTEEQKERYLPKLASG 112
fadE PRK09463
acyl-CoA dehydrogenase; Reviewed
84-346 7.80e-19

acyl-CoA dehydrogenase; Reviewed


Pssm-ID: 236528 [Multi-domain]  Cd Length: 777  Bit Score: 88.33  E-value: 7.80e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1BUC_A        84 AGVAITLSATV----SLCANPIWQ-FGTEAQKEKFLVPLVEGTKLGAFGLTEPNAGTDAS--------------GQQTIA 144
Cdd:PRK09463 150 ASRSGTLAVTVmvpnSLGPGELLLhYGTDEQKDHYLPRLARGEEIPCFALTSPEAGSDAGsipdtgvvckgewqGEEVLG 229
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1BUC_A       145 TKnddgtytLNGSKIFITNG------GAAdiyivFAMTDK-----SKGNHGITAFILEDGTPGFTYGKKEDKMGIhtsqt 213
Cdd:PRK09463 230 MR-------LTWNKRYITLApiatvlGLA-----FKLYDPdgllgDKEDLGITCALIPTDTPGVEIGRRHFPLNV----- 292
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1BUC_A       214 melVFQ-------DVKVPAENMLGEE---GKGFKIAMMTLDGGR-IGVAAQALGIAEAALADAVEYSKQRVQFGKPLCKF 282
Cdd:PRK09463 293 ---PFQngptrgkDVFIPLDYIIGGPkmaGQGWRMLMECLSVGRgISLPSNSTGGAKLAALATGAYARIRRQFKLPIGKF 369
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
1BUC_A       283 QSISFKLADM---KMQIEAARNLVykAACKKQEGKPfTVDAAIAKRVASDVAMRVTTEAVQIFGGYG 346
Cdd:PRK09463 370 EGIEEPLARIagnAYLMDAARTLT--TAAVDLGEKP-SVLSAIAKYHLTERGRQVINDAMDIHGGKG 433
PRK13026 PRK13026
acyl-CoA dehydrogenase; Reviewed
103-346 9.80e-19

acyl-CoA dehydrogenase; Reviewed


Pssm-ID: 237277 [Multi-domain]  Cd Length: 774  Bit Score: 88.09  E-value: 9.80e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1BUC_A       103 QFGTEAQKEKFLVPLVEGTKLGAFGLTEPNAGTDASG--QQTIATKND-DGTYTL----NGSKIFITNGGAADIY-IVFA 174
Cdd:PRK13026 173 HYGTQEQKDYWLPRLADGTEIPCFALTGPEAGSDAGAipDTGIVCRGEfEGEEVLglrlTWDKRYITLAPVATVLgLAFK 252
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1BUC_A       175 MTDK-----SKGNHGIT-AFILEDgTPGFTYGKKEDKMGihtsqtmeLVFQ-------DVKVPAENMLG---EEGKGFKI 238
Cdd:PRK13026 253 LRDPdgllgDKKELGITcALIPTD-HPGVEIGRRHNPLG--------MAFMngttrgkDVFIPLDWIIGgpdYAGRGWRM 323
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1BUC_A       239 AMMTLDGGRiGVAAQALGIAEAALA--DAVEYSKQRVQFGKPLCKFQSISFKLADM---KMQIEAARNLVYKAACKKQeg 313
Cdd:PRK13026 324 LVECLSAGR-GISLPALGTASGHMAtrTTGAYAYVRRQFGMPIGQFEGVQEALARIagnTYLLEAARRLTTTGLDLGV-- 400
                        250       260       270
                 ....*....|....*....|....*....|...
1BUC_A       314 KPfTVDAAIAKRVASDVAMRVTTEAVQIFGGYG 346
Cdd:PRK13026 401 KP-SVVTAIAKYHMTELARDVVNDAMDIHAGKG 432
PRK11561 PRK11561
isovaleryl CoA dehydrogenase; Provisional
74-372 3.08e-15

isovaleryl CoA dehydrogenase; Provisional


Pssm-ID: 183199 [Multi-domain]  Cd Length: 538  Bit Score: 77.10  E-value: 3.08e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1BUC_A        74 LAVEELAKYDAGVA----ITLSATV---SLC-------ANPIWQFGTEAQKEKFLVPLVE----------GTKLG---AF 126
Cdd:PRK11561 103 LAWEEDARSGAFVAraarFMLHAQVeagTLCpitmtfaATPLLLQMLPAPFQDWLTPLLSdrydshllpgGQKRGlliGM 182
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1BUC_A       127 GLTEPNAGTDASGQQTIATKNDDGTYTLNGSKIFITNGgAADIYIVFAMTdksKGnhGITAF----ILEDGT-PGFTYGK 201
Cdd:PRK11561 183 GMTEKQGGSDVLSNTTRAERLADGSYRLVGHKWFFSVP-QSDAHLVLAQA---KG--GLSCFfvprFLPDGQrNAIRLER 256
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1BUC_A       202 KEDKMGIHTSQTMELVFQDVkvpAENMLGEEGKG----FKIAMMTldggRIGVAAQALGIAEAALADAVEYSKQRVQFGK 277
Cdd:PRK11561 257 LKDKLGNRSNASSEVEFQDA---IGWLLGEEGEGirliLKMGGMT----RFDCALGSHGLMRRAFSVAIYHAHQRQVFGK 329
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1BUC_A       278 PLCKFQSISFKLADMKMQIEAARNLVYK-AACKKQEGKP--------FTVDA--AIAKRVASDVAmrvttEAVQIFGGYG 346
Cdd:PRK11561 330 PLIEQPLMRQVLSRMALQLEGQTALLFRlARAWDRRADAkealwarlFTPAAkfVICKRGIPFVA-----EAMEVLGGIG 404
                        330       340
                 ....*....|....*....|....*.
1BUC_A       347 YSEEYPVARHMRDAKITQIYEGTNEV 372
Cdd:PRK11561 405 YCEESELPRLYREMPVNSIWEGSGNI 430
AXO cd01150
Peroxisomal acyl-CoA oxidase; Peroxisomal acyl-CoA oxidases (AXO) catalyze the first set in ...
82-383 6.81e-15

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: 76.21  E-value: 6.81e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1BUC_A       82 YDAGVAITLSATVSLCANPIWQFGTEAQKEKFLVPLVEGTKLGAFGLTEPNAGTDASGQQTIAT--KNDD----GTYTLN 155
Cdd:cd01150  94 YDLSLGAKLGLHLGLFGNAIKNLGTDEHQDYWLQGANNLEIIGCFAQTELGHGSNLQGLETTATydPLTQefviNTPDFT 173
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1BUC_A      156 GSKIFITNGG-AADIYIVFAMTDKSKGNHGITAFIL---EDGT----PGFTYGKKEDKMGIHTSQTMELVFQDVKVPAEN 227
Cdd:cd01150 174 ATKWWPGNLGkTATHAVVFAQLITPGKNHGLHAFIVpirDPKThqplPGVTVGDIGPKMGLNGVDNGFLQFRNVRIPREN 253
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1BUC_A      228 MLG----------------EEGKGFKIAMMTLDGGRIGVAAQALGIAEAALADAVEYSKQRVQFGK-------PLCKFQS 284
Cdd:cd01150 254 LLNrfgdvspdgtyvspfkDPNKRYGAMLGTRSGGRVGLIYDAAMSLKKAATIAIRYSAVRRQFGPkpsdpevQILDYQL 333
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1BUC_A      285 ISFKLADMkmqieAARNLVYKAACKK-----------------QEGKPFTVDAAIAKRVASDVAMRVTTEAVQIFGGYGY 347
Cdd:cd01150 334 QQYRLFPQ-----LAAAYAFHFAAKSlvemyheiikellqgnsELLAELHALSAGLKAVATWTAAQGIQECREACGGHGY 408
                       330       340       350
                ....*....|....*....|....*....|....*...
1BUC_A      348 SEE--YPVARHMRDAKITqiYEGTNEVQLMVTGGALLR 383
Cdd:cd01150 409 LAMnrLPTLRDDNDPFCT--YEGDNTVLLQQTANYLLK 444
DszC cd01163
Dibenzothiophene (DBT) desulfurization enzyme C; DszC is a flavin reductase dependent enzyme, ...
23-361 1.16e-14

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: 74.67  E-value: 1.16e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1BUC_A       23 KLAPTVTERDHKGIYDKELIDELLSLGITGAYFEEKYGGSGDDggdVLSYILAVEELAKYDAGVAITLSATVSLCANpIW 102
Cdd:cd01163   9 RIAEGAAERDRQRGLPYEEVALLRQSGLGTLRVPKEYGGLGAS---LPDLYEVVRELAAADSNIAQALRAHFGFVEA-LL 84
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1BUC_A      103 QFGTEAQKEKFLVPLVEGTKLGAfGLTEpnAGTDASGQQTIATKNDDGTYTLNGSKIFITNGGAADIYIVFAMTDKSKgn 182
Cdd:cd01163  85 LAGPEQFRKRWFGRVLNGWIFGN-AVSE--RGSVRPGTFLTATVRDGGGYVLNGKKFYSTGALFSDWVTVSALDEEGK-- 159
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1BUC_A      183 hgITAFILEDGTPGFTYGKKEDKMGIHTSQTMELVFQDVKVPAENMLGEEGKGFKIAMMTLdGGRIGVAAQALGIAEAAL 262
Cdd:cd01163 160 --LVFAAVPTDRPGITVVDDWDGFGQRLTASGTVTFDNVRVEPDEVLPRPNAPDRGTLLTA-IYQLVLAAVLAGIARAAL 236
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1BUC_A      263 ADAVEYSKQRVQ------FGKPLCKFQSISfKLADMKMQIEAARNLVYKAA------------CKKQEGKPFTVDAAIAK 324
Cdd:cd01163 237 DDAVAYVRSRTRpwihsgAESARDDPYVQQ-VVGDLAARLHAAEALVLQAAraldaaaaagtaLTAEARGEAALAVAAAK 315
                       330       340       350
                ....*....|....*....|....*....|....*..
1BUC_A      325 RVASDVAMRVTTEAVQIFGGYGYSEEYPVARHMRDAK 361
Cdd:cd01163 316 VVVTRLALDATSRLFEVGGASATAREHNLDRHWRNAR 352
PLN02636 PLN02636
acyl-coenzyme A oxidase
71-383 1.41e-14

acyl-coenzyme A oxidase


Pssm-ID: 215342 [Multi-domain]  Cd Length: 686  Bit Score: 75.28  E-value: 1.41e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1BUC_A        71 SYILAVEELAKYDAGVAITLSATVSLCANPIWQFGTEAQKEKFLVPLVEGTKLGAFGLTEPNAGTDASGQQTIATKN--- 147
Cdd:PLN02636 122 KYFAITEAVGSVDMSLGIKLGVQYSLWGGSVINLGTKKHRDKYFDGIDNLDYPGCFAMTELHHGSNVQGLQTTATFDplt 201
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1BUC_A       148 --------DDGtytlnGSKIFITNGGA-ADIYIVFAM----TDKSKG--NHGITAFI-----LEDGT--PGFTYGKKEDK 205
Cdd:PLN02636 202 defvintpNDG-----AIKWWIGNAAVhGKFATVFARlklpTHDSKGvsDMGVHAFIvpirdMKTHQvlPGVEIRDCGHK 276
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1BUC_A       206 MGIHTSQTMELVFQDVKVPAENMLGEEG----------------KGFKIAMMTLDGGRIGVAAQALGIAEAALADAVEYS 269
Cdd:PLN02636 277 VGLNGVDNGALRFRSVRIPRDNLLNRFGdvsrdgkytsslptinKRFAATLGELVGGRVGLAYGSVGVLKASNTIAIRYS 356
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1BUC_A       270 KQRVQFGKP------LCKFQSISFKLADMKMQIE----AARNLVYKAACKKQE------GKPFTVDAAIAKRVASDVAMR 333
Cdd:PLN02636 357 LLRQQFGPPkqpeisILDYQSQQHKLMPMLASTYafhfATEYLVERYSEMKKThddqlvADVHALSAGLKAYITSYTAKA 436
                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|..
1BUC_A       334 VTT--EAVqifGGYGYSEEYPVARHMRDAKITQIYEGTNEVQLMVTGGALLR 383
Cdd:PLN02636 437 LSTcrEAC---GGHGYAAVNRFGSLRNDHDIFQTFEGDNTVLLQQVAADLLK 485
NcnH cd01159
Naphthocyclinone hydroxylase; Naphthocyclinone is an aromatic polyketide and an antibiotic, ...
75-383 1.65e-13

Naphthocyclinone hydroxylase; Naphthocyclinone is an aromatic polyketide and an antibiotic, which is active against Gram-positive bacteria. Polyketides are secondary metabolites, which have important biological functions such as antitumor, immunosupressive or antibiotic activities. NcnH is a hydroxylase involved in the biosynthesis of naphthocyclinone and possibly other polyketides.


Pssm-ID: 173848 [Multi-domain]  Cd Length: 370  Bit Score: 71.23  E-value: 1.65e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1BUC_A       75 AVEELAKYDAGVA--ITLSATVS--LCAnpiwqFGTEAQKEKFLVPlvEGTKLgafgltepnAGTDASGQQtiATKNDDG 150
Cdd:cd01159  58 AIATLAEACGSAAwvASIVATHSrmLAA-----FPPEAQEEVWGDG--PDTLL---------AGSYAPGGR--AERVDGG 119
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1BUC_A      151 tYTLNGSKIFITNGGAADIYIVFAMTDKSKGNHGITAFILedgtPGFTYGKKED--KMGIHTSQTMELVFQDVKVPAENM 228
Cdd:cd01159 120 -YRVSGTWPFASGCDHADWILVGAIVEDDDGGPLPRAFVV----PRAEYEIVDTwhVVGLRGTGSNTVVVDDVFVPEHRT 194
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1BUC_A      229 L-----------GEEGKGFKIAMMTLDGgrIGVAAQALGIAEAALADAVEYSKQRVQ---FGKPLCKFQSISFKLADMKM 294
Cdd:cd01159 195 LtagdmmagdgpGGSTPVYRMPLRQVFP--LSFAAVSLGAAEGALAEFLELAGKRVRqygAAVKMAEAPITQLRLAEAAA 272
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1BUC_A      295 QIEAARNLVYKAA----CKKQEGKPFTVDAAIAKRVASDVAMRVTTEAVQIF----GGYGYSEEYPVARHMRDAKITQIY 366
Cdd:cd01159 273 ELDAARAFLERATrdlwAHALAGGPIDVEERARIRRDAAYAAKLSAEAVDRLfhaaGGSALYTASPLQRIWRDIHAAAQH 352
                       330
                ....*....|....*...
1BUC_A      367 EGTN-EVQLMVTGGALLR 383
Cdd:cd01159 353 AALNpETAAEAYGRALLG 370
PLN02312 PLN02312
acyl-CoA oxidase
77-382 2.01e-11

acyl-CoA oxidase


Pssm-ID: 215178 [Multi-domain]  Cd Length: 680  Bit Score: 65.56  E-value: 2.01e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1BUC_A        77 EELAKYDAGVAITLSATVSLCANPIWQFGTEAQKEKFLVPLVEGTKLGAFGLTEPNAGTDASGQQTIATKN-DDGTYTLN 155
Cdd:PLN02312 140 EVIGIYDHSLAIKLGVHFFLWGGAIKFLGTKRHHDKWLKDTEDYVVKGCFAMTELGHGSNVRGIETVTTYDpKTEEFVIN 219
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1BUC_A       156 -----GSKIFItnGGAAD---IYIVFAMTDKSKGNHGITAFIL----EDGT--PGFTYGKKEDKMGIHTSQTMELVFQDV 221
Cdd:PLN02312 220 tpcesAQKYWI--GGAANhatHTIVFSQLHINGKNEGVHAFIAqirdQDGNicPNIRIADCGHKIGLNGVDNGRIWFDNL 297
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1BUC_A       222 KVPAENMLGE------EGK----------GFKIAMMTLDGGRIGVAAQALGIAEAALADAVEYSKQRVQF----GKP--- 278
Cdd:PLN02312 298 RIPRENLLNSvadvspDGKyvsaikdpdqRFGAFLAPLTSGRVTIAVSAIYSSKVGLAIAIRYSLSRRAFsvtpNGPevl 377
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1BUC_A       279 --------------LCKFQSISFKLADMKMqieaarnLVYKAacKKQEGKPFTVDAAIAKRVASDVAMRVTTEAVQIFGG 344
Cdd:PLN02312 378 lldypshqrrllplLAKTYAMSFAANDLKM-------IYVKR--TPESNKAIHVVSSGFKAVLTWHNMRTLQECREACGG 448
                        330       340       350
                 ....*....|....*....|....*....|....*...
1BUC_A       345 YGYSEEYPVARHMRDAKITQIYEGTNEVQLMVTGGALL 382
Cdd:PLN02312 449 QGLKTENRVGQLKAEYDVQSTFEGDNNVLMQQVSKALL 486
PLN02443 PLN02443
acyl-coenzyme A oxidase
105-276 3.28e-08

acyl-coenzyme A oxidase


Pssm-ID: 178062 [Multi-domain]  Cd Length: 664  Bit Score: 55.23  E-value: 3.28e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1BUC_A       105 GTEAQKEKFLvPLVEGTK-LGAFGLTEPNAGTDASGQQTIAT---KNDD---GTYTLNGSKIFITNGGAADIY-IVFAMT 176
Cdd:PLN02443 114 GTEEQQKKWL-PLAYKMQiIGCYAQTELGHGSNVQGLETTATfdpKTDEfviHSPTLTSSKWWPGGLGKVSTHaVVYARL 192
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1BUC_A       177 DKSKGNHGITAFI-----LEDGTP--GFTYGKKEDKMGIHTSQTME---LVFQDVKVPAENMLgeegkgFKIAMMTLDGG 246
Cdd:PLN02443 193 ITNGKDHGIHGFIvqlrsLDDHSPlpGVTVGDIGMKFGNGAYNTMDngfLRFDHVRIPRDQML------MRLSKVTREGK 266
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*...
1BUC_A       247 ------------------RIGVAAQALGIAEAALADAVEYSKQRVQFG 276
Cdd:PLN02443 267 yvqsdvprqlvygtmvyvRQTIVADASTALSRAVCIATRYSAVRRQFG 314
PTZ00457 PTZ00457
acyl-CoA dehydrogenase; Provisional
105-257 7.72e-05

acyl-CoA dehydrogenase; Provisional


Pssm-ID: 185636 [Multi-domain]  Cd Length: 520  Bit Score: 44.49  E-value: 7.72e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1BUC_A       105 GTEAQKEKFLVPLVEGTKLGAFGLTEPNaGTDASGQQTIATKNDDGTYTLNGSKiFITNGGAADIYIVFAMT-DKSKGNH 183
Cdd:PTZ00457 117 GSKELKGKYLTAMSDGTIMMGWATEEGC-GSDISMNTTKASLTDDGSYVLTGQK-RCEFAASATHFLVLAKTlTQTAAEE 194
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1BUC_A       184 GITA------FILEDGTPGFTYGKKedkmgihtsqtmELVFQDvkVPAENMLGEEGKGFKIAMMTLDGGRIGVAAQALGI 257
Cdd:PTZ00457 195 GATEvsrnsfFICAKDAKGVSVNGD------------SVVFEN--TPAADVVGVVGEGFKDAMITLFTEQYLYAASLLGI 260
 
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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