NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|1959994196|ref|WP_201818501|]
View 

MULTISPECIES: acyl-CoA dehydrogenase family protein [Pseudomonas]

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

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

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 ...
 8-378 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 cd01158:

Pssm-ID: 447864 [Multi-domain]  Cd Length: 373  Bit Score: 531.07  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1959994196   8 EDQVMIRDMARDFARGEIAPHAQAWEKAGWIDDGLVAKMGELGLLGMVVPEEWGGTYVDYVAYALAVEEISAGDGATGAF 87
Cdd:cd01158     1 EEHQMIRKTVRDFAEKEIAPLAAEMDEKGEFPREVIKEMAELGLMGIPIPEEYGGAGLDFLAYAIAIEELAKVDASVAVI 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1959994196  88 MSIHNSVGCGPVLNYGSEEQKQTWLADLASGAVIGCFCLTEPQAGSEAHNLRTRAELRDGQWVINGAKQFVSNGKRAKLA 167
Cdd:cd01158    81 VSVHNSLGANPIIKFGTEEQKKKYLPPLATGEKIGAFALSEPGAGSDAAALKTTAKKDGDDYVLNGSKMWITNGGEADFY 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1959994196 168 IVFAVTDPDLGKRGISAFLVPTDTPGFIVDRTEHKMGIRASDTCAVTLSNCSIPEANLLGERGKGLAIALSNLEGGRIGI 247
Cdd:cd01158   161 IVFAVTDPSKGYRGITAFIVERDTPGLSVGKKEDKLGIRGSSTTELIFEDVRVPKENILGEEGEGFKIAMQTLDGGRIGI 240

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1959994196 248 AAQALGIARAAFEAALGYARDRVQFGKAIVEHQSIANLLADMQMQINAARLMILHAARLRTAGKPCLSEASQAKLFASEM 327
Cdd:cd01158   241 AAQALGIAQAALDAAVDYAKERKQFGKPIADFQGIQFKLADMATEIEAARLLTYKAARLKDNGEPFIKEAAMAKLFASEV 320

                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1959994196 328 AEKVCSSAIQIHGGYGYLEDYPVEKYYRDARITQIYEGSSEIQRMVIAREL 378
Cdd:cd01158   321 AMRVTTDAVQIFGGYGYTKDYPVERYYRDAKITEIYEGTSEIQRLVIAKHL 371
 
Name Accession Description Interval E-value
SCAD_SBCAD cd01158
Short chain acyl-CoA dehydrogenases and eukaryotic short/branched chain acyl-CoA ...
 8-378 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: 531.07  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1959994196   8 EDQVMIRDMARDFARGEIAPHAQAWEKAGWIDDGLVAKMGELGLLGMVVPEEWGGTYVDYVAYALAVEEISAGDGATGAF 87
Cdd:cd01158     1 EEHQMIRKTVRDFAEKEIAPLAAEMDEKGEFPREVIKEMAELGLMGIPIPEEYGGAGLDFLAYAIAIEELAKVDASVAVI 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1959994196  88 MSIHNSVGCGPVLNYGSEEQKQTWLADLASGAVIGCFCLTEPQAGSEAHNLRTRAELRDGQWVINGAKQFVSNGKRAKLA 167
Cdd:cd01158    81 VSVHNSLGANPIIKFGTEEQKKKYLPPLATGEKIGAFALSEPGAGSDAAALKTTAKKDGDDYVLNGSKMWITNGGEADFY 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1959994196 168 IVFAVTDPDLGKRGISAFLVPTDTPGFIVDRTEHKMGIRASDTCAVTLSNCSIPEANLLGERGKGLAIALSNLEGGRIGI 247
Cdd:cd01158   161 IVFAVTDPSKGYRGITAFIVERDTPGLSVGKKEDKLGIRGSSTTELIFEDVRVPKENILGEEGEGFKIAMQTLDGGRIGI 240

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1959994196 248 AAQALGIARAAFEAALGYARDRVQFGKAIVEHQSIANLLADMQMQINAARLMILHAARLRTAGKPCLSEASQAKLFASEM 327
Cdd:cd01158   241 AAQALGIAQAALDAAVDYAKERKQFGKPIADFQGIQFKLADMATEIEAARLLTYKAARLKDNGEPFIKEAAMAKLFASEV 320

                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1959994196 328 AEKVCSSAIQIHGGYGYLEDYPVEKYYRDARITQIYEGSSEIQRMVIAREL 378
Cdd:cd01158   321 AMRVTTDAVQIFGGYGYTKDYPVERYYRDAKITEIYEGTSEIQRLVIAKHL 371
CaiA COG1960
Acyl-CoA dehydrogenase related to the alkylation response protein AidB [Lipid transport and ...
 3-378 6.47e-179

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: 502.06  E-value: 6.47e-179
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1959994196   3 DLELTEDQVMIRDMARDFARGEIAPHAQAWEKAGWIDDGLVAKMGELGLLGMVVPEEWGGTYVDYVAYALAVEEISAGDG 82
Cdd:COG1960     2 DFELTEEQRALRDEVREFAEEEIAPEAREWDREGEFPRELWRKLAELGLLGLTIPEEYGGLGLSLVELALVLEELARADA 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1959994196  83 ATGAFMSIHNSVGcGPVLNYGSEEQKQTWLADLASGAVIGCFCLTEPQAGSEAHNLRTRAELRDGQWVINGAKQFVSNGK 162
Cdd:COG1960    82 SLALPVGVHNGAA-EALLRFGTEEQKERYLPRLASGEWIGAFALTEPGAGSDAAALRTTAVRDGDGYVLNGQKTFITNAP 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1959994196 163 RAKLAIVFAVTDPDLGKRGISAFLVPTDTPGFIVDRTEHKMGIRASDTCAVTLSNCSIPEANLLGERGKGLAIALSNLEG 242
Cdd:COG1960   161 VADVILVLARTDPAAGHRGISLFLVPKDTPGVTVGRIEDKMGLRGSDTGELFFDDVRVPAENLLGEEGKGFKIAMSTLNA 240

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1959994196 243 GRIGIAAQALGIARAAFEAALGYARDRVQFGKAIVEHQSIANLLADMQMQINAARLMILHAARLRTAGKPCLSEASQAKL 322
Cdd:COG1960   241 GRLGLAAQALGIAEAALELAVAYAREREQFGRPIADFQAVQHRLADMAAELEAARALVYRAAWLLDAGEDAALEAAMAKL 320

                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1959994196 323 FASEMAEKVCSSAIQIHGGYGYLEDYPVEKYYRDARITQIYEGSSEIQRMVIAREL 378
Cdd:COG1960   321 FATEAALEVADEALQIHGGYGYTREYPLERLYRDARILTIYEGTNEIQRLIIARRL 376
PLN02519 PLN02519
isovaleryl-CoA dehydrogenase
 3-378 1.65e-90

isovaleryl-CoA dehydrogenase


Pssm-ID: 215284 [Multi-domain]  Cd Length: 404  Bit Score: 277.91  E-value: 1.65e-90
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1959994196   3 DLELTEDQVMIRDMARDFARGEIAPHAQAWEKAGWI--DDGLVAKMGELGLLGMVVPEEWGGTYVDYVAYALAVEEISAG 80
Cdd:PLN02519   23 SLLFDDTQLQFKESVQQFAQENIAPHAAAIDATNSFpkDVNLWKLMGDFNLHGITAPEEYGGLGLGYLYHCIAMEEISRA 102

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1959994196  81 DGATGAFMSIHNSVGCGPVLNYGSEEQKQTWLADLASGAVIGCFCLTEPQAGSEAHNLRTRAELRDGQWVINGAKQFVSN 160
Cdd:PLN02519  103 SGSVGLSYGAHSNLCINQLVRNGTPAQKEKYLPKLISGEHVGALAMSEPNSGSDVVSMKCKAERVDGGYVLNGNKMWCTN 182

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1959994196 161 GKRAKLAIVFAVTDPDLGKRGISAFLVPTDTPGFIVDRTEHKMGIRASDTCAVTLSNCSIPEANLLGERGKGLAIALSNL 240
Cdd:PLN02519  183 GPVAQTLVVYAKTDVAAGSKGITAFIIEKGMPGFSTAQKLDKLGMRGSDTCELVFENCFVPEENVLGQEGKGVYVMMSGL 262

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1959994196 241 EGGRIGIAAQALGIARAAFEAALGYARDRVQFGKAIVEHQSIANLLADMQMQINAARLMILHAARLRTAGKPCLSEASQA 320
Cdd:PLN02519  263 DLERLVLAAGPLGLMQACLDVVLPYVRQREQFGRPIGEFQFIQGKLADMYTSLQSSRSYVYSVARDCDNGKVDRKDCAGV 342

                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1959994196 321 KLFASEMAEKVCSSAIQIHGGYGYLEDYPVEKYYRDARITQIYEGSSEIQRMVIAREL 378
Cdd:PLN02519  343 ILCAAERATQVALQAIQCLGGNGYINEYPTGRLLRDAKLYEIGAGTSEIRRMLIGREL 400
Acyl-CoA_dh_1 pfam00441
Acyl-CoA dehydrogenase, C-terminal domain; C-terminal domain of Acyl-CoA dehydrogenase is an ...
 230-378 1.97e-54

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: 176.29  E-value: 1.97e-54
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1959994196 230 GKGLAIALSNLEGGRIGIAAQALGIARAAFEAALGYARDRVQFGKAIVEHQSIANLLADMQMQINAARLMILHAARLRTA 309
Cdd:pfam00441   1 GRGFRVAMETLNHERLAIAAMALGLARRALDEALAYARRRKAFGRPLIDFQLVRHKLAEMAAEIEAARLLVYRAAEALDA 80

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1959994196 310 GKPCLSEASQAKLFASEMAEKVCSSAIQIHGGYGYLEDYPVEKYYRDARITQIYEGSSEIQRMVIAREL 378
Cdd:pfam00441  81 GGPDGAEASMAKLYASEAAVEVADLAMQLHGGYGYLREYPVERLYRDARVLRIGEGTSEIQRNIIARRL 149
 
Name Accession Description Interval E-value
SCAD_SBCAD cd01158
Short chain acyl-CoA dehydrogenases and eukaryotic short/branched chain acyl-CoA ...
 8-378 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: 531.07  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1959994196   8 EDQVMIRDMARDFARGEIAPHAQAWEKAGWIDDGLVAKMGELGLLGMVVPEEWGGTYVDYVAYALAVEEISAGDGATGAF 87
Cdd:cd01158     1 EEHQMIRKTVRDFAEKEIAPLAAEMDEKGEFPREVIKEMAELGLMGIPIPEEYGGAGLDFLAYAIAIEELAKVDASVAVI 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1959994196  88 MSIHNSVGCGPVLNYGSEEQKQTWLADLASGAVIGCFCLTEPQAGSEAHNLRTRAELRDGQWVINGAKQFVSNGKRAKLA 167
Cdd:cd01158    81 VSVHNSLGANPIIKFGTEEQKKKYLPPLATGEKIGAFALSEPGAGSDAAALKTTAKKDGDDYVLNGSKMWITNGGEADFY 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1959994196 168 IVFAVTDPDLGKRGISAFLVPTDTPGFIVDRTEHKMGIRASDTCAVTLSNCSIPEANLLGERGKGLAIALSNLEGGRIGI 247
Cdd:cd01158   161 IVFAVTDPSKGYRGITAFIVERDTPGLSVGKKEDKLGIRGSSTTELIFEDVRVPKENILGEEGEGFKIAMQTLDGGRIGI 240

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1959994196 248 AAQALGIARAAFEAALGYARDRVQFGKAIVEHQSIANLLADMQMQINAARLMILHAARLRTAGKPCLSEASQAKLFASEM 327
Cdd:cd01158   241 AAQALGIAQAALDAAVDYAKERKQFGKPIADFQGIQFKLADMATEIEAARLLTYKAARLKDNGEPFIKEAAMAKLFASEV 320

                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1959994196 328 AEKVCSSAIQIHGGYGYLEDYPVEKYYRDARITQIYEGSSEIQRMVIAREL 378
Cdd:cd01158   321 AMRVTTDAVQIFGGYGYTKDYPVERYYRDAKITEIYEGTSEIQRLVIAKHL 371
CaiA COG1960
Acyl-CoA dehydrogenase related to the alkylation response protein AidB [Lipid transport and ...
 3-378 6.47e-179

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: 502.06  E-value: 6.47e-179
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1959994196   3 DLELTEDQVMIRDMARDFARGEIAPHAQAWEKAGWIDDGLVAKMGELGLLGMVVPEEWGGTYVDYVAYALAVEEISAGDG 82
Cdd:COG1960     2 DFELTEEQRALRDEVREFAEEEIAPEAREWDREGEFPRELWRKLAELGLLGLTIPEEYGGLGLSLVELALVLEELARADA 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1959994196  83 ATGAFMSIHNSVGcGPVLNYGSEEQKQTWLADLASGAVIGCFCLTEPQAGSEAHNLRTRAELRDGQWVINGAKQFVSNGK 162
Cdd:COG1960    82 SLALPVGVHNGAA-EALLRFGTEEQKERYLPRLASGEWIGAFALTEPGAGSDAAALRTTAVRDGDGYVLNGQKTFITNAP 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1959994196 163 RAKLAIVFAVTDPDLGKRGISAFLVPTDTPGFIVDRTEHKMGIRASDTCAVTLSNCSIPEANLLGERGKGLAIALSNLEG 242
Cdd:COG1960   161 VADVILVLARTDPAAGHRGISLFLVPKDTPGVTVGRIEDKMGLRGSDTGELFFDDVRVPAENLLGEEGKGFKIAMSTLNA 240

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1959994196 243 GRIGIAAQALGIARAAFEAALGYARDRVQFGKAIVEHQSIANLLADMQMQINAARLMILHAARLRTAGKPCLSEASQAKL 322
Cdd:COG1960   241 GRLGLAAQALGIAEAALELAVAYAREREQFGRPIADFQAVQHRLADMAAELEAARALVYRAAWLLDAGEDAALEAAMAKL 320

                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1959994196 323 FASEMAEKVCSSAIQIHGGYGYLEDYPVEKYYRDARITQIYEGSSEIQRMVIAREL 378
Cdd:COG1960   321 FATEAALEVADEALQIHGGYGYTREYPLERLYRDARILTIYEGTNEIQRLIIARRL 376
ACAD cd00567
Acyl-CoA dehydrogenase; Both mitochondrial acyl-CoA dehydrogenases (ACAD) and peroxisomal ...
 8-376 8.81e-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: 352.36  E-value: 8.81e-121
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1959994196   8 EDQVMIRDMARDFARGEIAPHAQAWEKAGWIDDGLVAKMGELGLLGmvvpeewggtyvdyvayalaveeisagdgatgaf 87
Cdd:cd00567     1 EEQRELRDSAREFAAEELEPYARERRETPEEPWELLAELGLLLGAA---------------------------------- 46

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1959994196  88 msihnsvgcgPVLNYGSEEQKQTWLADLASGAVIGCFCLTEPQAGSEAHNLRTRAELRDGQWVINGAKQFVSNGKRAKLA 167
Cdd:cd00567    47 ----------LLLAYGTEEQKERYLPPLASGEAIAAFALTEPGAGSDLAGIRTTARKDGDGYVLNGRKIFISNGGDADLF 116

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1959994196 168 IVFAVTDP-DLGKRGISAFLVPTDTPGFIVDRTEHKMGIRASDTCAVTLSNCSIPEANLLGERGKGLAIALSNLEGGRIG 246
Cdd:cd00567   117 IVLARTDEeGPGHRGISAFLVPADTPGVTVGRIWDKMGMRGSGTGELVFDDVRVPEDNLLGEEGGGFELAMKGLNVGRLL 196

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1959994196 247 IAAQALGIARAAFEAALGYARDRVQFGKAIVEHQSIANLLADMQMQINAARLMILHAARLRTAGKPCLS-EASQAKLFAS 325
Cdd:cd00567   197 LAAVALGAARAALDEAVEYAKQRKQFGKPLAEFQAVQFKLADMAAELEAARLLLYRAAWLLDQGPDEARlEAAMAKLFAT 276

                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1959994196 326 EMAEKVCSSAIQIHGGYGYLEDYPVEKYYRDARITQIYEGSSEIQRMVIAR 376
Cdd:cd00567   277 EAAREVADLAMQIHGGRGYSREYPVERYLRDARAARIAEGTAEIQRLIIAR 327
IBD cd01162
Isobutyryl-CoA dehydrogenase; Isobutyryl-CoA dehydrogenase (IBD) catalyzes the alpha, beta- ...
 6-378 2.37e-117

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: 345.58  E-value: 2.37e-117
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1959994196   6 LTEDQVMIRDMARDFARGEIAPHAQAWEKAGWIDDGLVAKMGELGLLGMVVPEEWGGTYVDYVAYALAVEEISAGDGATG 85
Cdd:cd01162     1 LNEEQRAIQEVARAFAAKEMAPHAADWDQKKHFPVDVLRKAAELGFGGIYIRDDVGGSGLSRLDASIIFEALSTGCVSTA 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1959994196  86 AFMSIHNSvgCGPVLN-YGSEEQKQTWLADLASGAVIGCFCLTEPQAGSEAHNLRTRAELRDGQWVINGAKQFVSNGKRA 164
Cdd:cd01162    81 AYISIHNM--CAWMIDsFGNDEQRERFLPDLCTMEKLASYCLTEPGSGSDAAALRTRAVREGDHYVLNGSKAFISGAGDS 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1959994196 165 KLAIVFAVTDPDlGKRGISAFLVPTDTPGFIVDRTEHKMGIRASDTCAVTLSNCSIPEANLLGERGKGLAIALSNLEGGR 244
Cdd:cd01162   159 DVYVVMARTGGE-GPKGISCFVVEKGTPGLSFGANEKKMGWNAQPTRAVIFEDCRVPVENRLGGEGQGFGIAMAGLNGGR 237

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1959994196 245 IGIAAQALGIARAAFEAALGYARDRVQFGKAIVEHQSIANLLADMQMQINAARLMILHAA-RLRTAGKPCLSEASQAKLF 323
Cdd:cd01162   238 LNIASCSLGAAQAALDLARAYLEERKQFGKPLADFQALQFKLADMATELVASRLMVRRAAsALDRGDPDAVKLCAMAKRF 317

                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1959994196 324 ASEMAEKVCSSAIQIHGGYGYLEDYPVEKYYRDARITQIYEGSSEIQRMVIAREL 378
Cdd:cd01162   318 ATDECFDVANQALQLHGGYGYLKDYPVEQYVRDLRVHQILEGTNEIMRLIIARAL 372
IVD cd01156
Isovaleryl-CoA dehydrogenase; Isovaleryl-CoA dehydrogenase (IVD) is an is an acyl-CoA ...
 6-378 8.98e-116

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: 341.70  E-value: 8.98e-116
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1959994196   6 LTEDQVMIRDMARDFARGEIAPHAQAWEKAGWIDDGLVAKMGELGLLGMVVPEEWGGTYVDYVAYALAVEEISAGDGATG 85
Cdd:cd01156     2 LDDEIEMLRQSVREFAQKEIAPLAAKIDRDNEFPRDLWRKMGKLGLLGITAPEEYGGSGMGYLAHVIIMEEISRASGSVA 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1959994196  86 AFMSIHNSVGCGPVLNYGSEEQKQTWLADLASGAVIGCFCLTEPQAGSEAHNLRTRAELRDGQWVINGAKQFVSNGKRAK 165
Cdd:cd01156    82 LSYGAHSNLCINQIYRNGSAAQKEKYLPKLISGEHIGALAMSEPNAGSDVVSMKLRAEKKGDRYVLNGSKMWITNGPDAD 161

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1959994196 166 LAIVFAVTDPDLGKRGISAFLVPTDTPGFIVDRTEHKMGIRASDTCAVTLSNCSIPEANLLGERGKGLAIALSNLEGGRI 245
Cdd:cd01156   162 TLVVYAKTDPSAGAHGITAFIVEKGMPGFSRAQKLDKLGMRGSNTCELVFEDCEVPEENILGGENKGVYVLMSGLDYERL 241

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1959994196 246 GIAAQALGIARAAFEAALGYARDRVQFGKAIVEHQSIANLLADMQMQINAARLMILHAARLRTAGKPCLSEASQAKLFAS 325
Cdd:cd01156   242 VLAGGPIGIMQAALDVAIPYAHQRKQFGQPIGEFQLVQGKLADMYTRLNASRSYLYTVAKACDRGNMDPKDAAGVILYAA 321

                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1959994196 326 EMAEKVCSSAIQIHGGYGYLEDYPVEKYYRDARITQIYEGSSEIQRMVIAREL 378
Cdd:cd01156   322 EKATQVALDAIQILGGNGYINDYPTGRLLRDAKLYEIGAGTSEIRRMVIGREL 374
LCAD cd01160
Long chain acyl-CoA dehydrogenase; LCAD is an acyl-CoA dehydrogenases (ACAD), which is found ...
 8-378 1.23e-108

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: 323.30  E-value: 1.23e-108
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1959994196   8 EDQVMIRDMARDFARGEIAPHAQAWEKAGWIDDGLVAKMGELGLLGMVVPEEWGGTYVDYVAYALAVEEIsAGDGATGAF 87
Cdd:cd01160     1 EEHDAFRDVVRRFFAKEVAPFHHEWEKAGEVPREVWRKAGEQGLLGVGFPEEYGGIGGDLLSAAVLWEEL-ARAGGSGPG 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1959994196  88 MSIHNSVGCGPVLNYGSEEQKQTWLADLASGAVIGCFCLTEPQAGSEAHNLRTRAELRDGQWVINGAKQFVSNGKRAKLA 167
Cdd:cd01160    80 LSLHTDIVSPYITRAGSPEQKERVLPQMVAGKKIGAIAMTEPGAGSDLQGIRTTARKDGDHYVLNGSKTFITNGMLADVV 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1959994196 168 IVFAVTDPDL-GKRGISAFLVPTDTPGFIVDRTEHKMGIRASDTCAVTLSNCSIPEANLLGERGKGLAIALSNLEGGRIG 246
Cdd:cd01160   160 IVVARTGGEArGAGGISLFLVERGTPGFSRGRKLKKMGWKAQDTAELFFDDCRVPAENLLGEENKGFYYLMQNLPQERLL 239

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1959994196 247 IAAQALGIARAAFEAALGYARDRVQFGKAIVEHQSIANLLADMQMQINAARLMILHAARLRTAGKPCLSEASQAKLFASE 326
Cdd:cd01160   240 IAAGALAAAEFMLEETRNYVKQRKAFGKTLAQLQVVRHKIAELATKVAVTRAFLDNCAWRHEQGRLDVAEASMAKYWATE 319

                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1959994196 327 MAEKVCSSAIQIHGGYGYLEDYPVEKYYRDARITQIYEGSSEIQRMVIAREL 378
Cdd:cd01160   320 LQNRVAYECVQLHGGWGYMREYPIARAYRDARVQPIYGGTTEIMKELISRQM 371
VLCAD cd01161
Very long chain acyl-CoA dehydrogenase; VLCAD is an acyl-CoA dehydrogenase (ACAD), which is ...
 5-375 5.91e-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: 307.47  E-value: 5.91e-102
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1959994196   5 ELTEDQVMIRDMARDFARGEIAPHA-QAWEKagwIDDGLVAKMGELGLLGMVVPEEWGGTYVDYVAYALAVEEISAgDGA 83
Cdd:cd01161    26 EQTEELNMLVGPVEKFFEEVNDPAKnDQLEK---IPRKTLTQLKELGLFGLQVPEEYGGLGLNNTQYARLAEIVGM-DLG 101

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1959994196  84 TGAFMSIHNSVGCGPVLNYGSEEQKQTWLADLASGAVIGCFCLTEPQAGSEAHNLRTRAELR-DGQ-WVINGAKQFVSNG 161
Cdd:cd01161   102 FSVTLGAHQSIGFKGILLFGTEAQKEKYLPKLASGEWIAAFALTEPSSGSDAASIRTTAVLSeDGKhYVLNGSKIWITNG 181

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1959994196 162 KRAKLAIVFA---VTDPDLG-KRGISAFLVPTDTPGFIVDRTEHKMGIRASDTCAVTLSNCSIPEANLLGERGKGLAIAL 237
Cdd:cd01161   182 GIADIFTVFAkteVKDATGSvKDKITAFIVERSFGGVTNGPPEKKMGIKGSNTAEVYFEDVKIPVENVLGEVGDGFKVAM 261

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1959994196 238 SNLEGGRIGIAAQALGIARAAFEAALGYARDRVQFGKAIVEHQSIANLLADMQMQINAARLMILHAARL--RTAGKPCLS 315
Cdd:cd01161   262 NILNNGRFGMGAALIGTMKRCIEKAVDYANNRKQFGKKIHEFGLIQEKLANMAILQYATESMAYMTSGNmdRGLKAEYQI 341

                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1959994196 316 EASQAKLFASEMAEKVCSSAIQIHGGYGYLEDYPVEKYYRDARITQIYEGSSEIQRMVIA 375
Cdd:cd01161   342 EAAISKVFASEAAWLVVDEAIQIHGGMGFMREYGVERVLRDLRIFRIFEGTNEILRLFIA 401
GCD cd01151
Glutaryl-CoA dehydrogenase; Glutaryl-CoA dehydrogenase (GCD). GCD is an acyl-CoA dehydrogenase, ...
 2-382 4.46e-100

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: 301.97  E-value: 4.46e-100
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1959994196   2 HDLELTEDQVMIRDMARDFARGEIAPH-AQAWEKAGWiDDGLVAKMGELGLLGMVvPEEWGGTYVDYVAYALAVEEISAG 80
Cdd:cd01151     9 LDDLLTEEERAIRDTAREFCQEELAPRvLEAYREEKF-DRKIIEEMGELGLLGAT-IKGYGCAGLSSVAYGLIAREVERV 86

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1959994196  81 DGATGAFMSIHNSVGCGPVLNYGSEEQKQTWLADLASGAVIGCFCLTEPQAGSEAHNLRTRAELRDGQWVINGAKQFVSN 160
Cdd:cd01151    87 DSGYRSFMSVQSSLVMLPIYDFGSEEQKQKYLPKLASGELIGCFGLTEPNHGSDPGGMETRARKDGGGYKLNGSKTWITN 166

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1959994196 161 GKRAKLAIVFAVTDPDLGKRGisaFLVPTDTPGFIVDRTEHKMGIRASDTCAVTLSNCSIPEANLLGErGKGLAIALSNL 240
Cdd:cd01151   167 SPIADVFVVWARNDETGKIRG---FILERGMKGLSAPKIQGKFSLRASITGEIVMDNVFVPEENLLPG-AEGLRGPFKCL 242

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1959994196 241 EGGRIGIAAQALGIARAAFEAALGYARDRVQFGKAIVEHQSIANLLADMQMQINAARLMILHAARLRTAGKPCLSEASQA 320
Cdd:cd01151   243 NNARYGIAWGALGAAEDCYHTARQYVLDRKQFGRPLAAFQLVQKKLADMLTEIALGLLACLRVGRLKDQGKATPEQISLL 322

                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1959994196 321 KLFASEMAEKVCSSAIQIHGGYGYLEDYPVEKYYRDARITQIYEGSSEIQRMVIARELKNYQ 382
Cdd:cd01151   323 KRNNCGKALEIARTAREMLGGNGISDEYHIIRHMVNLESVNTYEGTHDIHALILGRAITGIQ 384
MCAD cd01157
Medium chain acyl-CoA dehydrogenase; MCADs are mitochondrial beta-oxidation enzymes, which ...
 6-378 8.98e-96

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: 8.98e-96
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1959994196   6 LTEDQVMIRDMARDFARGEIAPHAQAWEKAGWIDDGLVAKMGELGLLGMVVPEEWGGTYVDYVAYALAVEEISAGdgATG 85
Cdd:cd01157     1 LTEQQKEFQETARKFAREEIIPVAAEYDKSGEYPWPLIKRAWELGLMNTHIPEDCGGLGLGTFDTCLITEELAYG--CTG 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1959994196  86 AFMSIH-NSVGCGPVLNYGSEEQKQTWLADLASGAVIGCFCLTEPQAGSEAHNLRTRAELRDGQWVINGAKQFVSNGKRA 164
Cdd:cd01157    79 VQTAIEaNSLGQMPVIISGNDEQKKKYLGRMTEEPLMCAYCVTEPGAGSDVAGIKTKAEKKGDEYIINGQKMWITNGGKA 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1959994196 165 KLAIVFAVTDPDL---GKRGISAFLVPTDTPGFIVDRTEHKMGIRASDTCAVTLSNCSIPEANLLGERGKGLAIALSNLE 241
Cdd:cd01157   159 NWYFLLARSDPDPkcpASKAFTGFIVEADTPGIQPGRKELNMGQRCSDTRGITFEDVRVPKENVLIGEGAGFKIAMGAFD 238

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1959994196 242 GGRIGIAAQALGIARAAFEAALGYARDRVQFGKAIVEHQSIANLLADMQMQINAARLMILHAARLRTAGKPCLSEASQAK 321
Cdd:cd01157   239 KTRPPVAAGAVGLAQRALDEATKYALERKTFGKLIAEHQAVSFMLADMAMKVELARLAYQRAAWEVDSGRRNTYYASIAK 318

                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1959994196 322 LFASEMAEKVCSSAIQIHGGYGYLEDYPVEKYYRDARITQIYEGSSEIQRMVIAREL 378
Cdd:cd01157   319 AFAADIANQLATDAVQIFGGNGFNSEYPVEKLMRDAKIYQIYEGTSQIQRLIISREH 375
PLN02519 PLN02519
isovaleryl-CoA dehydrogenase
 3-378 1.65e-90

isovaleryl-CoA dehydrogenase


Pssm-ID: 215284 [Multi-domain]  Cd Length: 404  Bit Score: 277.91  E-value: 1.65e-90
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1959994196   3 DLELTEDQVMIRDMARDFARGEIAPHAQAWEKAGWI--DDGLVAKMGELGLLGMVVPEEWGGTYVDYVAYALAVEEISAG 80
Cdd:PLN02519   23 SLLFDDTQLQFKESVQQFAQENIAPHAAAIDATNSFpkDVNLWKLMGDFNLHGITAPEEYGGLGLGYLYHCIAMEEISRA 102

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1959994196  81 DGATGAFMSIHNSVGCGPVLNYGSEEQKQTWLADLASGAVIGCFCLTEPQAGSEAHNLRTRAELRDGQWVINGAKQFVSN 160
Cdd:PLN02519  103 SGSVGLSYGAHSNLCINQLVRNGTPAQKEKYLPKLISGEHVGALAMSEPNSGSDVVSMKCKAERVDGGYVLNGNKMWCTN 182

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1959994196 161 GKRAKLAIVFAVTDPDLGKRGISAFLVPTDTPGFIVDRTEHKMGIRASDTCAVTLSNCSIPEANLLGERGKGLAIALSNL 240
Cdd:PLN02519  183 GPVAQTLVVYAKTDVAAGSKGITAFIIEKGMPGFSTAQKLDKLGMRGSDTCELVFENCFVPEENVLGQEGKGVYVMMSGL 262

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1959994196 241 EGGRIGIAAQALGIARAAFEAALGYARDRVQFGKAIVEHQSIANLLADMQMQINAARLMILHAARLRTAGKPCLSEASQA 320
Cdd:PLN02519  263 DLERLVLAAGPLGLMQACLDVVLPYVRQREQFGRPIGEFQFIQGKLADMYTSLQSSRSYVYSVARDCDNGKVDRKDCAGV 342

                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1959994196 321 KLFASEMAEKVCSSAIQIHGGYGYLEDYPVEKYYRDARITQIYEGSSEIQRMVIAREL 378
Cdd:PLN02519  343 ILCAAERATQVALQAIQCLGGNGYINEYPTGRLLRDAKLYEIGAGTSEIRRMLIGREL 400
ACAD_fadE5 cd01153
Putative acyl-CoA dehydrogenases similar to fadE5; Putative acyl-CoA dehydrogenase (ACAD). ...
 19-370 1.64e-79

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: 250.00  E-value: 1.64e-79
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1959994196  19 DFARGEIAPHAQAWEKAG-WIDDGLVA----------KMGELGLLGMVVPEEWGGTYVDYVAYALAVEEISAGDGAtgaF 87
Cdd:cd01153     7 RLAENVLAPLNADGDREGpVFDDGRVVvpppfkealdAFAEAGWMALGVPEEYGGQGLPITVYSALAEIFSRGDAP---L 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1959994196  88 MSIHNSVGCGPVLNY-GSEEQKQTWLADLASGAVIGCFCLTEPQAGSEAHNLRTRAELR-DGQWVINGAKQFVSNGKRAK 165
Cdd:cd01153    84 MYASGTQGAAATLLAhGTEAQREKWIPRLAEGEWTGTMCLTEPDAGSDLGALRTKAVYQaDGSWRINGVKRFISAGEHDM 163

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1959994196 166 ----LAIVFAVT-DPDLGKRGISAFLVP-----TDTPGFIVDRTEHKMGIRASDTCAVTLSNCsipEANLLGERGKGLAI 235
Cdd:cd01153   164 seniVHLVLARSeGAPPGVKGLSLFLVPkflddGERNGVTVARIEEKMGLHGSPTCELVFDNA---KGELIGEEGMGLAQ 240

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1959994196 236 ALSNLEGGRIGIAAQALGIARAAFEAALGYARDRVQFGK--------AIVEHQSIANLLADMQMQINAARLMILHAARLR 307
Cdd:cd01153   241 MFAMMNGARLGVGTQGTGLAEAAYLNALAYAKERKQGGDlikaapavTIIHHPDVRRSLMTQKAYAEGSRALDLYTATVQ 320

                         330       340       350       360       370       380       390
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1959994196 308 TAGKPCLSEASQAKL--------------FASEMAEKVCSSAIQIHGGYGYLEDYPVEKYYRDARITQIYEGSSEIQ 370
Cdd:cd01153   321 DLAERKATEGEDRKAlsaladlltpvvkgFGSEAALEAVSDAIQVHGGSGYTREYPIEQYYRDARITTIYEGTTGIQ 397
PRK12341 PRK12341
acyl-CoA dehydrogenase;
3-382 1.05e-71

acyl-CoA dehydrogenase;


Pssm-ID: 183454 [Multi-domain]  Cd Length: 381  Bit Score: 228.84  E-value: 1.05e-71
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1959994196   3 DLELTEDQVMIRD-----MARDFARG------EIAPHAQAWEKAgWIDDGLvakmgelGLLGmvVPEEWGGTYVDYVAYA 71
Cdd:PRK12341    2 DFSLTEEQELLLAsirelITRNFPEEyfrtcdENGTYPREFMRA-LADNGI-------SMLG--VPEEFGGTPADYVTQM 71

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1959994196  72 LAVEEIsAGDGATGAFMS----IHNsvgcgpVLNYGSEEQ-KQTWLADLASGAVIGCFCLTEPQAGSEAHNLRTRAELRD 146
Cdd:PRK12341   72 LVLEEV-SKCGAPAFLITngqcIHS------MRRFGSAEQlRKTAESTLETGDPAYALALTEPGAGSDNNSATTTYTRKN 144

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1959994196 147 GQWVINGAKQFVSNGKRAKLAIVFAV-TDPDLGKRGISAFLVPTDTPGFIVDRTeHKMGIRASDTCAVTLSNCSIPEANL 225
Cdd:PRK12341  145 GKVYLNGQKTFITGAKEYPYMLVLARdPQPKDPKKAFTLWWVDSSKPGIKINPL-HKIGWHMLSTCEVYLDNVEVEESDL 223

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1959994196 226 LGERGKGLAIALSNLEGGRIGIAAQALGIARAAFEAALGYARDRVQFGKAIVEHQSIANLLADMQMQINAARLMILHAAR 305
Cdd:PRK12341  224 VGEEGMGFLNVMYNFEMERLINAARSLGFAECAFEDAARYANQRIQFGKPIGHNQLIQEKLTLMAIKIENMRNMVYKVAW 303

                         330       340       350       360       370       380       390
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1959994196 306 LRTAGKPCLSEASQAKLFASEMAEKVCSSAIQIHGGYGYLEDYPVEKYYRDARITQIYEGSSEIQRMVIARE-LKNYQ 382
Cdd:PRK12341  304 QADNGQSLRTSAALAKLYCARTAMEVIDDAIQIMGGLGYTDEARVSRFWRDVRCERIGGGTDEIMIYIAGRQiLKDYQ 381
PTZ00461 PTZ00461
isovaleryl-CoA dehydrogenase; Provisional
 7-380 1.30e-65

isovaleryl-CoA dehydrogenase; Provisional


Pssm-ID: 185640 [Multi-domain]  Cd Length: 410  Bit Score: 214.03  E-value: 1.30e-65
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1959994196   7 TEDQVMIRDMARDFARGEIAPHAQAWEKAGWIDDGLVAKMGELGLLGMVVPEEWGGTYVDYVAYALAVEEISAGD-GATG 85
Cdd:PTZ00461   38 TPEHAALRETVAKFSREVVDKHAREDDINMHFNRDLFKQLGDLGVMGVTVPEADGGAGMDAVAAVIIHHELSKYDpGFCL 117

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1959994196  86 AFMSiHNSVGCGPVLNYGSEEQKQTWLADLASGAVIGCFCLTEPQAGSEAHNLRTRA-ELRDGQWVINGAKQFVSNGKRA 164
Cdd:PTZ00461  118 AYLA-HSMLFVNNFYYSASPAQRARWLPKVLTGEHVGAMGMSEPGAGTDVLGMRTTAkKDSNGNYVLNGSKIWITNGTVA 196

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1959994196 165 KLAIVFAVTDpdlGKrgISAFLVPTDTPGFIVDRTEHKMGIRASDTCAVTLSNCSIPEANLLGERGKGLAIALSNLEGGR 244
Cdd:PTZ00461  197 DVFLIYAKVD---GK--ITAFVVERGTKGFTQGPKIDKCGMRASHMCQLFFEDVVVPAENLLGEEGKGMVGMMRNLELER 271

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1959994196 245 IGIAAQALGIARAAFEAALGYARDRVQFGKAIVEHQSIANLLADMQMQINAARLMILHAARLRTAGKPCLSEASQAKLFA 324
Cdd:PTZ00461  272 VTLAAMAVGIAERSVELMTSYASERKAFGKPISNFGQIQRYIAEGYADTEAAKALVYSVSHNVHPGNKNRLGSDAAKLFA 351

                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1959994196 325 SEMAEKVCSSAIQIHGGYGYLEDYPVEKYYRDARITQIYEGSSEIQRMVIARELKN 380
Cdd:PTZ00461  352 TPIAKKVADSAIQVMGGMGYSRDMPVERLWRDAKLLEIGGGTIEAHHKNITKDLLK 407
ACAD_FadE2 cd01155
Acyl-CoA dehydrogenases similar to fadE2; FadE2-like Acyl-CoA dehydrogenase (ACAD). Acyl-CoA ...
 23-379 5.53e-64

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: 209.17  E-value: 5.53e-64
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1959994196  23 GEIAPHAQAWEKAGWIDDGLVAKMGELGLLGMVVPEEWGGTYVDYVAYALAVEEISAGDGATGAFMSIHNSVGCGPVLN- 101
Cdd:cd01155    27 EYYAEGGDRWWTPPPIIEKLKAKAKAEGLWNLFLPEVSGLSGLTNLEYAYLAEETGRSFFAPEVFNCQAPDTGNMEVLHr 106

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1959994196 102 YGSEEQKQTWLADLASGAVIGCFCLTEPQ-AGSEAHNLRTRAElRDG-QWVINGAKQFVSNG--KRAKLAIVFAVTDPDL 177
Cdd:cd01155   107 YGSEEQKKQWLEPLLDGKIRSAFAMTEPDvASSDATNIECSIE-RDGdDYVINGRKWWSSGAgdPRCKIAIVMGRTDPDG 185

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1959994196 178 GKRGI--SAFLVPTDTPGFIVDRTEHKMGirASDT----CAVTLSNCSIPEANLLGERGKGLAIALSNLEGGRIGIAAQA 251
Cdd:cd01155   186 APRHRqqSMILVPMDTPGVTIIRPLSVFG--YDDAphghAEITFDNVRVPASNLILGEGRGFEIAQGRLGPGRIHHCMRL 263

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1959994196 252 LGIARAAFEAALGYARDRVQFGKAIVEHQSIANLLADMQMQINAARLMILHAA-RLRTAG-KPCLSEASQAKLFASEMAE 329
Cdd:cd01155   264 IGAAERALELMCQRAVSREAFGKKLAQHGVVAHWIAKSRIEIEQARLLVLKAAhMIDTVGnKAARKEIAMIKVAAPRMAL 343

                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1959994196 330 KVCSSAIQIHGGYGYLEDYPVEKYYRDARITQIYEGSSEIQRMVIAR-ELK 379
Cdd:cd01155   344 KIIDRAIQVHGAAGVSQDTPLANMYAWARTLRIADGPDEVHLRSIARmELK 394
ACAD_fadE6_17_26 cd01152
Putative acyl-CoA dehydrogenases similar to fadE6, fadE17, and fadE26; Putative acyl-CoA ...
 13-378 4.64e-57

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: 191.02  E-value: 4.64e-57
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1959994196  13 IRDMARDFARGEIAPHAQAWEKAGWI-----DDGLVAKMGELGLLGMVVPEEWGGTYVDYVAYALAVEEISAGDGATGAF 87
Cdd:cd01152     6 FRAEVRAWLAAHLPPELREESALGYRegredRRRWQRALAAAGWAAPGWPKEYGGRGASLMEQLIFREEMAAAGAPVPFN 85

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1959994196  88 MSIHNSvgCGPVLN-YGSEEQKQTWLADLASGAVIGCFCLTEPQAGSEAHNLRTRAELRDGQWVINGAKQFVSNGKRAKL 166
Cdd:cd01152    86 QIGIDL--AGPTILaYGTDEQKRRFLPPILSGEEIWCQGFSEPGAGSDLAGLRTRAVRDGDDWVVNGQKIWTSGAHYADW 163

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1959994196 167 AIVFAVTDPDLGK-RGISAFLVPTDTPGFIVDRTEHKMGirASDTCAVTLSNCSIPEANLLGERGKGLAIALSNLEGGRI 245
Cdd:cd01152   164 AWLLVRTDPEAPKhRGISILLVDMDSPGVTVRPIRSING--GEFFNEVFLDDVRVPDANRVGEVNDGWKVAMTTLNFERV 241

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1959994196 246 GIAAQALGIARAAFEAALGYARDRVQFGKAIVEHQSIANLLADMQmqinAARLMILHAARLRTAGKPCLSEASQAKLFAS 325
Cdd:cd01152   242 SIGGSAATFFELLLARLLLLTRDGRPLIDDPLVRQRLARLEAEAE----ALRLLVFRLASALAAGKPPGAEASIAKLFGS 317

                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1959994196 326 EMAEKVCSSAIQIHGGYGYLEDYP--------VEKYYRDARITQIYEGSSEIQRMVIAREL 378
Cdd:cd01152   318 ELAQELAELALELLGTAALLRDPApgaelagrWEADYLRSRATTIYGGTSEIQRNIIAERL 378
Acyl-CoA_dh_1 pfam00441
Acyl-CoA dehydrogenase, C-terminal domain; C-terminal domain of Acyl-CoA dehydrogenase is an ...
 230-378 1.97e-54

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: 176.29  E-value: 1.97e-54
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1959994196 230 GKGLAIALSNLEGGRIGIAAQALGIARAAFEAALGYARDRVQFGKAIVEHQSIANLLADMQMQINAARLMILHAARLRTA 309
Cdd:pfam00441   1 GRGFRVAMETLNHERLAIAAMALGLARRALDEALAYARRRKAFGRPLIDFQLVRHKLAEMAAEIEAARLLVYRAAEALDA 80

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1959994196 310 GKPCLSEASQAKLFASEMAEKVCSSAIQIHGGYGYLEDYPVEKYYRDARITQIYEGSSEIQRMVIAREL 378
Cdd:pfam00441  81 GGPDGAEASMAKLYASEAAVEVADLAMQLHGGYGYLREYPVERLYRDARVLRIGEGTSEIQRNIIARRL 149
PLN02526 PLN02526
acyl-coenzyme A oxidase
 1-378 3.39e-53

acyl-coenzyme A oxidase


Pssm-ID: 178141 [Multi-domain]  Cd Length: 412  Bit Score: 181.59  E-value: 3.39e-53
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1959994196   1 MHDLELTEDQVmIRDMARDFARGEIAP-HAQAWEKAGWIDDgLVAKMGELGLLGMVVpEEWGGTYVDYVAYALAVEEISA 79
Cdd:PLN02526   25 FDDLLTPEEQA-LRKRVRECMEKEVAPiMTEYWEKAEFPFH-IIPKLGSLGIAGGTI-KGYGCPGLSITASAIATAEVAR 101

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1959994196  80 GDGATGAFMSIHNSVGCGPVLNYGSEEQKQTWLADLASGAVIGCFCLTEPQAGSEAHNLRTRAELRDGQWVINGAKQFVS 159
Cdd:PLN02526  102 VDASCSTFILVHSSLAMLTIALCGSEAQKQKYLPSLAQLDTVACWALTEPDYGSDASSLNTTATKVEGGWILNGQKRWIG 181

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1959994196 160 NGKRAKLAIVFAvtdPDLGKRGISAFLVPTDTPGFIVDRTEHKMGIRASDTCAVTLSNCSIPE------ANLLGERGKGL 233
Cdd:PLN02526  182 NSTFADVLVIFA---RNTTTNQINGFIVKKGAPGLKATKIENKIGLRMVQNGDIVLKDVFVPDedrlpgVNSFQDTNKVL 258

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1959994196 234 AIAlsnleggRIGIAAQALGIARAAFEAALGYARDRVQFGKAIVEHQSIANLLADMQMQINAARLMILHAARLRTAGKPC 313
Cdd:PLN02526  259 AVS-------RVMVAWQPIGISMGVYDMCHRYLKERKQFGAPLAAFQINQEKLVRMLGNIQAMFLVGWRLCKLYESGKMT 331

                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1959994196 314 LSEASQAKLFASEMAEKVCSSAIQIHGGYGYLEDYPVEKYYRDARITQIYEGSSEIQRMVIAREL 378
Cdd:PLN02526  332 PGHASLGKAWITKKARETVALGRELLGGNGILADFLVAKAFCDLEPIYTYEGTYDINALVTGREI 396
PRK03354 PRK03354
crotonobetainyl-CoA dehydrogenase; Validated
 3-382 2.20e-50

crotonobetainyl-CoA dehydrogenase; Validated


Pssm-ID: 179566 [Multi-domain]  Cd Length: 380  Bit Score: 173.48  E-value: 2.20e-50
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1959994196   3 DLELTEDQVMIRDMARDFARGEiaphaqAWEKAGWIDDG-------LVAKMGELGLLGMVVPEEWGGTYVDYVAYALAVE 75
Cdd:PRK03354    2 DFNLNDEQELFVAGIRELMASE------NWEAYFAECDRdsvyperFVKALADMGIDSLLIPEEHGGLDAGFVTLAAVWM 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1959994196  76 EISAGDGATGAFMSIhnSVGCGPVLNYGSEEQKQTWLADLASGAVIGCFCLTEPQAGSEAHNLRTRAELRDGQWVINGAK 155
Cdd:PRK03354   76 ELGRLGAPTYVLYQL--PGGFNTFLREGTQEQIDKIMAFRGTGKQMWNSAITEPGAGSDVGSLKTTYTRRNGKVYLNGSK 153

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1959994196 156 QFVSNGKRAKLAIVFAVTDPDLGKRGISAFLVPTDTPGFIVDRTeHKMGIRASDTCAVTLSNCSIPEANLLGERGKGLAI 235
Cdd:PRK03354  154 CFITSSAYTPYIVVMARDGASPDKPVYTEWFVDMSKPGIKVTKL-EKLGLRMDSCCEITFDDVELDEKDMFGREGNGFNR 232

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1959994196 236 ALSNLEGGRIGIAAQALGIARAAFEAALGYARDRVQFGKAIVEHQSIANLLADMQMQINAARLMILHAARLRTAGKPCLS 315
Cdd:PRK03354  233 VKEEFDHERFLVALTNYGTAMCAFEDAARYANQRVQFGEAIGRFQLIQEKFAHMAIKLNSMKNMLYEAAWKADNGTITSG 312

                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1959994196 316 EASQAKLFASEMAEKVCSSAIQIHGGYGYLEDYPVEKYYRDARITQIYEGSSEIQRMVIARE-LKNYQ 382
Cdd:PRK03354  313 DAAMCKYFCANAAFEVVDSAMQVLGGVGIAGNHRISRFWRDLRVDRVSGGSDEMQILTLGRAvLKQYR 380
Acyl-CoA_dh_N pfam02771
Acyl-CoA dehydrogenase, N-terminal domain; The N-terminal domain of Acyl-CoA dehydrogenase is ...
 7-118 7.54e-49

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: 160.71  E-value: 7.54e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1959994196   7 TEDQVMIRDMARDFARGEIAPHAQAWEKAGWIDDGLVAKMGELGLLGMVVPEEWGGTYVDYVAYALAVEEISAGDGATGA 86
Cdd:pfam02771   1 TEEQEALRDTVREFAEEEIAPHAAEWDEEGEFPRELWKKLGELGLLGITIPEEYGGAGLDYLAYALVAEELARADASVAL 80

                          90       100       110
                  ....*....|....*....|....*....|..
gi 1959994196  87 FMSIHNSVGCGPVLNYGSEEQKQTWLADLASG 118
Cdd:pfam02771  81 ALSVHSSLGAPPILRFGTEEQKERYLPKLASG 112
AidB cd01154
Proteins involved in DNA damage response, similar to the AidB gene product; AidB is one of ...
 102-370 1.11e-48

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: 169.86  E-value: 1.11e-48
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1959994196 102 YGSEEQKQtWLADLAS-----GAVIGCFcLTEPQAGSEAHNLRTRAE-LRDGQWVINGAKQFVSNGKrAKLAIVFAVT-D 174
Cdd:cd01154   126 YGPEELKQ-YLPGLLSdryktGLLGGTW-MTEKQGGSDLGANETTAErSGGGVYRLNGHKWFASAPL-ADAALVLARPeG 202

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1959994196 175 PDLGKRGISAFLVPTDTP-----GFIVDRTEHKMGIRASDTCAVTLSNCsipEANLLGERGKGLAIALSNLEGGRIGIAA 249
Cdd:cd01154   203 APAGARGLSLFLVPRLLEdgtrnGYRIRRLKDKLGTRSVATGEVEFDDA---EAYLIGDEGKGIYYILEMLNISRLDNAV 279

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1959994196 250 QALGIARAAFEAALGYARDRVQFGKAIVEHQSIANLLADMQMQINAARLMILHAARL---RTAGKPclSEASQAKLF--- 323
Cdd:cd01154   280 AALGIMRRALSEAYHYARHRRAFGKPLIDHPLMRRDLAEMEVDVEAATALTFRAARAfdrAAADKP--VEAHMARLAtpv 357

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1959994196 324 ----ASEMAEKVCSSAIQIHGGYGYLEDYPVEKYYRDARITQIYEGSSEIQ 370
Cdd:cd01154   358 akliACKRAAPVTSEAMEVFGGNGYLEEWPVARLHREAQVTPIWEGTGNIQ 408
PTZ00456 PTZ00456
acyl-CoA dehydrogenase; Provisional
 50-370 4.57e-35

acyl-CoA dehydrogenase; Provisional


Pssm-ID: 185635 [Multi-domain]  Cd Length: 622  Bit Score: 136.15  E-value: 4.57e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1959994196  50 GLLGMVVPEEWGGTYVDYVAYALAVEEISAGDGATGAFMSIhnSVG-CGPVLNYGSEEQKQTWLADLASGAVIGCFCLTE 128
Cdd:PTZ00456  112 GWTGISEPEEYGGQALPLSVGFITRELMATANWGFSMYPGL--SIGaANTLMAWGSEEQKEQYLTKLVSGEWSGTMCLTE 189

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1959994196 129 PQAGSEAHNLRTRAE-LRDGQWVINGAKQFVSNGKRAK----LAIVFAVTDPDL-GKRGISAFLVPTDTP---------- 192
Cdd:PTZ00456  190 PQCGTDLGQVKTKAEpSADGSYKITGTKIFISAGDHDLteniVHIVLARLPNSLpTTKGLSLFLVPRHVVkpdgsletak 269

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1959994196 193 GFIVDRTEHKMGIRASDTCAVTLSNCSipeANLLGERGKGLAIALSNLEGGRIGIAAQALGIARAAFEAALGYARDRVQF 272
Cdd:PTZ00456  270 NVKCIGLEKKMGIKGSSTCQLSFENSV---GYLIGEPNAGMKQMFTFMNTARVGTALEGVCHAELAFQNALRYARERRSM 346

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1959994196 273 ------------GKAIVEHQSIANLLADMQMQINAARLMILHAARL----RTAGKPCLSEASQ---------AKLFASEM 327
Cdd:PTZ00456  347 ralsgtkepekpADRIICHANVRQNILFAKAVAEGGRALLLDVGRLldihAAAKDAATREALDheigfytpiAKGCLTEW 426

                         330       340       350       360
                  ....*....|....*....|....*....|....*....|...
gi 1959994196 328 AEKVCSSAIQIHGGYGYLEDYPVEKYYRDARITQIYEGSSEIQ 370
Cdd:PTZ00456  427 GVEAASRCLQVWGGHGYIKGNGMEQILRDARIGTLYEGTTGIQ 469
PLN02876 PLN02876
acyl-CoA dehydrogenase
 99-383 2.68e-30

acyl-CoA dehydrogenase


Pssm-ID: 215473 [Multi-domain]  Cd Length: 822  Bit Score: 122.60  E-value: 2.68e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1959994196  99 VLNYGSEEQKQTWLADLASGAVIGCFCLTEPQ-AGSEAHNLRTRAELRDGQWVINGAKQFVSNG--KRAKLAIVFAVTDP 175
Cdd:PLN02876  529 LLRYGNKEQQLEWLIPLLEGKIRSGFAMTEPQvASSDATNIECSIRRQGDSYVINGTKWWTSGAmdPRCRVLIVMGKTDF 608

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1959994196 176 DLGK-RGISAFLVPTDTPGFIVDRTEHKMGIRAS--DTCAVTLSNCSIPEANLLGERGKGLAIALSNLEGGRIGIAAQAL 252
Cdd:PLN02876  609 NAPKhKQQSMILVDIQTPGVQIKRPLLVFGFDDAphGHAEISFENVRVPAKNILLGEGRGFEIAQGRLGPGRLHHCMRLI 688

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1959994196 253 GIARAAFEAALGYARDRVQFGKAIVEHQSIANLLADMQMQINAARLMILHAARL--RTAGKPCLSEASQAKLFASEMAEK 330
Cdd:PLN02876  689 GAAERGMQLMVQRALSRKAFGKLIAQHGSFLSDLAKCRVELEQTRLLVLEAADQldRLGNKKARGIIAMAKVAAPNMALK 768

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1959994196 331 VCSSAIQIHGGYGYLEDYPVEKYYRDARITQIYEGSSEIQRMVIAR-ELKNYQL 383
Cdd:PLN02876  769 VLDMAMQVHGAAGVSSDTVLAHLWATARTLRIADGPDEVHLGTIAKlELQRAKL 822
Acyl-CoA_dh_M pfam02770
Acyl-CoA dehydrogenase, middle domain; Central domain of Acyl-CoA dehydrogenase has a ...
 123-215 6.76e-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: 6.76e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1959994196 123 CFCLTEPQAGSEAHNLRTRAELRDG-QWVINGAKQFVSNGKRAKLAIVFAVTDPDLGKRGISAFLVPTDTPGFIVDRTEH 201
Cdd:pfam02770   1 AFALTEPGAGSDVASLKTTAADGDGgGWVLNGTKWWITNAGIADLFLVLARTGGDDRHGGISLFLVPKDAPGVSVRRIET 80

                          90
                  ....*....|....
gi 1959994196 202 KMGIRASDTCAVTL 215
Cdd:pfam02770  81 KLGVRGLPTGELVF 94
PRK13026 PRK13026
acyl-CoA dehydrogenase; Reviewed
 46-343 2.61e-27

acyl-CoA dehydrogenase; Reviewed


Pssm-ID: 237277 [Multi-domain]  Cd Length: 774  Bit Score: 113.90  E-value: 2.61e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1959994196  46 MGELGLLGMVVPEEWGGTyvDYVAYALA--VEEISAGDGATGAFMSIHNSVGCGPVLN-YGSEEQKQTWLADLASGAVIG 122
Cdd:PRK13026  117 LKKEGFFALIIPKEYGGK--GFSAYANStiVSKIATRSVSAAVTVMVPNSLGPGELLThYGTQEQKDYWLPRLADGTEIP 194

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1959994196 123 CFCLTEPQAGSEAHNLR-----TRAELrDGQWV----INGAKQFVSNGKRAK-LAIVFAVTDPD--LGKR---GISAFLV 187
Cdd:PRK13026  195 CFALTGPEAGSDAGAIPdtgivCRGEF-EGEEVlglrLTWDKRYITLAPVATvLGLAFKLRDPDglLGDKkelGITCALI 273

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1959994196 188 PTDTPGFIVDRTEHKMG-------IRASDTcavtlsncSIPEANLLGER---GKGLAIALSNLEGGRiGIAAQALGIARA 257
Cdd:PRK13026  274 PTDHPGVEIGRRHNPLGmafmngtTRGKDV--------FIPLDWIIGGPdyaGRGWRMLVECLSAGR-GISLPALGTASG 344

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1959994196 258 --AFEAALGYARDRVQFGKAIVEHQSIANLLADMqmqinAARLMILHAARLRTAG------KPCLSEASqAKLFASEMAE 329
Cdd:PRK13026  345 hmATRTTGAYAYVRRQFGMPIGQFEGVQEALARI-----AGNTYLLEAARRLTTTgldlgvKPSVVTAI-AKYHMTELAR 418

                         330
                  ....*....|....
gi 1959994196 330 KVCSSAIQIHGGYG 343
Cdd:PRK13026  419 DVVNDAMDIHAGKG 432
fadE PRK09463
acyl-CoA dehydrogenase; Reviewed
 50-343 3.51e-24

acyl-CoA dehydrogenase; Reviewed


Pssm-ID: 236528 [Multi-domain]  Cd Length: 777  Bit Score: 104.51  E-value: 3.51e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1959994196  50 GLLGMVVPEEWGGtyVDYVAYALA--VEEISAGDGATGAFMSIHNSVGCGPVL-NYGSEEQKQTWLADLASGAVIGCFCL 126
Cdd:PRK09463  122 GFFGMIIPKEYGG--LEFSAYAHSrvLQKLASRSGTLAVTVMVPNSLGPGELLlHYGTDEQKDHYLPRLARGEEIPCFAL 199

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1959994196 127 TEPQAGSEAHNLRTRAELRDGQWviNGAKQF---VSNGKR----AKLAIV----FAVTDPD--LGKR---GISAFLVPTD 190
Cdd:PRK09463  200 TSPEAGSDAGSIPDTGVVCKGEW--QGEEVLgmrLTWNKRyitlAPIATVlglaFKLYDPDglLGDKedlGITCALIPTD 277

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1959994196 191 TPGFIVDRTEHKMG-------IRASDTCavtlsncsIPEANLLGER---GKGLAIALSNLEGGR-IGIAAQALGIARAAF 259
Cdd:PRK09463  278 TPGVEIGRRHFPLNvpfqngpTRGKDVF--------IPLDYIIGGPkmaGQGWRMLMECLSVGRgISLPSNSTGGAKLAA 349

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1959994196 260 EAALGYARDRVQFGKAIVEHQSIANLLADMqmqinAARLMILHAARLRTAG------KPCLSEASqAKLFASEMAEKVCS 333
Cdd:PRK09463  350 LATGAYARIRRQFKLPIGKFEGIEEPLARI-----AGNAYLMDAARTLTTAavdlgeKPSVLSAI-AKYHLTERGRQVIN 423

                         330
                  ....*....|
gi 1959994196 334 SAIQIHGGYG 343
Cdd:PRK09463  424 DAMDIHGGKG 433
Acyl-CoA_dh_2 pfam08028
Acyl-CoA dehydrogenase, C-terminal domain;
246-368 4.02e-24

Acyl-CoA dehydrogenase, C-terminal domain;


Pssm-ID: 429790 [Multi-domain]  Cd Length: 133  Bit Score: 96.26  E-value: 4.02e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1959994196 246 GIAAQALGIARAAFEAALGYARDRVQ--FGKAIVEHQSIANLLADMQMQINAARLMILHAA----RLRTAGKPC----LS 315
Cdd:pfam08028   1 GIAAAALGAARAALAEFTERARGRVRayFGVPLAEDPATQLALAEAAARIDAARLLLERAAarieAAAAAGKPVtpalRA 80

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1959994196 316 EASQAKLFASEMAEKVCSSAIQIHGGYGYLEDYPVEKYYRDARITQIYEGSSE 368
Cdd:pfam08028  81 EARRAAAFATELAVAAVDALFRAAGGSALFQDSPLQRIWRDIHAAAQHAAVNP 133
DszC cd01163
Dibenzothiophene (DBT) desulfurization enzyme C; DszC is a flavin reductase dependent enzyme, ...
 17-358 5.50e-21

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: 93.16  E-value: 5.50e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1959994196  17 ARDFARgEIAPHAQAWEKAGWIDDGLVAKMGELGLLGMVVPEEWGGTYVDYVAYALAVEEISAGDGATGAFMSIHNSVgC 96
Cdd:cd01163     3 ARPLAA-RIAEGAAERDRQRGLPYEEVALLRQSGLGTLRVPKEYGGLGASLPDLYEVVRELAAADSNIAQALRAHFGF-V 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1959994196  97 GPVLNYGSEEQKQTWLADLASGAVIGCfcltepqAGSEAHNLRTRAELR-----DGQWVINGAKQFVSNGKRAKLAIVFA 171
Cdd:cd01163    81 EALLLAGPEQFRKRWFGRVLNGWIFGN-------AVSERGSVRPGTFLTatvrdGGGYVLNGKKFYSTGALFSDWVTVSA 153

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1959994196 172 VTDPDlgkRGISAfLVPTDTPGFIVDRTEHKMGIRASDTCAVTLSNCSIPEANLLGERGKGLAIALsNLEGGRIGIAAQA 251
Cdd:cd01163   154 LDEEG---KLVFA-AVPTDRPGITVVDDWDGFGQRLTASGTVTFDNVRVEPDEVLPRPNAPDRGTL-LTAIYQLVLAAVL 228

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1959994196 252 LGIARAAFEAALGYARDRVQ-FGKAIVEHQS----IANLLADMQMQINAARLMILHAARL--RTAGKPCLSEA------- 317
Cdd:cd01163   229 AGIARAALDDAVAYVRSRTRpWIHSGAESARddpyVQQVVGDLAARLHAAEALVLQAARAldAAAAAGTALTAeargeaa 308

                         330       340       350       360
                  ....*....|....*....|....*....|....*....|....
gi 1959994196 318 ---SQAKLFASEMAEKVCSSAIQIHGGYGYLEDYPVEKYYRDAR 358
Cdd:cd01163   309 lavAAAKVVVTRLALDATSRLFEVGGASATAREHNLDRHWRNAR 352
AXO cd01150
Peroxisomal acyl-CoA oxidase; Peroxisomal acyl-CoA oxidases (AXO) catalyze the first set in ...
 42-382 9.13e-21

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: 93.93  E-value: 9.13e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1959994196  42 LVAKMGELGLlgmVVPEEwggtyvdYVAYALAVEeisAGDGATGAFMSIHNSVGCGPVLNYGSEEQKQTWLADLASGAVI 121
Cdd:cd01150    69 DVERMGELMA---DDPEK-------MLALTNSLG---GYDLSLGAKLGLHLGLFGNAIKNLGTDEHQDYWLQGANNLEII 135

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1959994196 122 GCFCLTEPQAGSEAHNLRTRA---ELRDgQWVIN-----GAKQFVSN-GKRAKLAIVFA--VTDpdlGKR-GISAFLVP- 188
Cdd:cd01150   136 GCFAQTELGHGSNLQGLETTAtydPLTQ-EFVINtpdftATKWWPGNlGKTATHAVVFAqlITP---GKNhGLHAFIVPi 211

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1959994196 189 ------TDTPGFIVDRTEHKMGIRASDTCAVTLSNCSIPEANLLGERG----------------KGLAIALSNLEGGRIG 246
Cdd:cd01150   212 rdpkthQPLPGVTVGDIGPKMGLNGVDNGFLQFRNVRIPRENLLNRFGdvspdgtyvspfkdpnKRYGAMLGTRSGGRVG 291

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1959994196 247 IAAQALGIARAAFEAALGYARDRVQFGK-------AIVEHQ---------------------SIANLLADMQMQI---NA 295
Cdd:cd01150   292 LIYDAAMSLKKAATIAIRYSAVRRQFGPkpsdpevQILDYQlqqyrlfpqlaaayafhfaakSLVEMYHEIIKELlqgNS 371

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1959994196 296 ARLMILHAarLRTAGKPCLSEASQAKLfasEMAEKVCssaiqihGGYGYLEDYPVEKYYRDARITQIYEGSSEIQRMVIA 375
Cdd:cd01150   372 ELLAELHA--LSAGLKAVATWTAAQGI---QECREAC-------GGHGYLAMNRLPTLRDDNDPFCTYEGDNTVLLQQTA 439


                  ....*...
gi 1959994196 376 REL-KNYQ 382
Cdd:cd01150   440 NYLlKKYA 447
PRK11561 PRK11561
isovaleryl CoA dehydrogenase; Provisional
 109-378 3.25e-18

isovaleryl CoA dehydrogenase; Provisional


Pssm-ID: 183199 [Multi-domain]  Cd Length: 538  Bit Score: 85.96  E-value: 3.25e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1959994196 109 QTWLADLAS--------------GAVIGcFCLTEPQAGSEAHNLRTRAE-LRDGQWVINGAKQFVSNgKRAKLAIVFAVT 173
Cdd:PRK11561  154 QDWLTPLLSdrydshllpggqkrGLLIG-MGMTEKQGGSDVLSNTTRAErLADGSYRLVGHKWFFSV-PQSDAHLVLAQA 231

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1959994196 174 dpdlgKRGISAFLVPTDTP-----GFIVDRTEHKMGIRASDTCAVTLSNCSipeANLLGERGKGLAIALSnlEGG--RIG 246
Cdd:PRK11561  232 -----KGGLSCFFVPRFLPdgqrnAIRLERLKDKLGNRSNASSEVEFQDAI---GWLLGEEGEGIRLILK--MGGmtRFD 301

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1959994196 247 IAAQALGIARAAFEAALGYARDRVQFGKAIVEHQSIANLLADMQMQINAARLMILHAARLRTA-GKPclSEASQAKLFAS 325
Cdd:PRK11561  302 CALGSHGLMRRAFSVAIYHAHQRQVFGKPLIEQPLMRQVLSRMALQLEGQTALLFRLARAWDRrADA--KEALWARLFTP 379

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1959994196 326 EMAEKVCSS-------AIQIHGGYGYLEDYPVEKYYRDARITQIYEGSSEIQRMVIAREL 378
Cdd:PRK11561  380 AAKFVICKRgipfvaeAMEVLGGIGYCEESELPRLYREMPVNSIWEGSGNIMCLDVLRVL 439
PLN02636 PLN02636
acyl-coenzyme A oxidase
 66-289 1.18e-16

acyl-coenzyme A oxidase


Pssm-ID: 215342 [Multi-domain]  Cd Length: 686  Bit Score: 81.44  E-value: 1.18e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1959994196  66 DYVAYALAVEEISAGDGATGAFMSIHNSVGCGPVLNYGSEEQKQTWLADLASGAVIGCFCLTEPQAGSEAHNLRTRA--- 142
Cdd:PLN02636  119 DPAKYFAITEAVGSVDMSLGIKLGVQYSLWGGSVINLGTKKHRDKYFDGIDNLDYPGCFAMTELHHGSNVQGLQTTAtfd 198

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1959994196 143 ELRDgQWVIN----GA-KQFVSNGK-RAKLAIVFA---VTDPD---LGKRGISAFLVPTDT-------PGFIVDRTEHKM 203
Cdd:PLN02636  199 PLTD-EFVINtpndGAiKWWIGNAAvHGKFATVFArlkLPTHDskgVSDMGVHAFIVPIRDmkthqvlPGVEIRDCGHKV 277

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1959994196 204 GIRASDTCAVTLSNCSIPEANLLGERG----------------KGLAIALSNLEGGRIGIAAQALGIARAAFEAALGYAR 267
Cdd:PLN02636  278 GLNGVDNGALRFRSVRIPRDNLLNRFGdvsrdgkytsslptinKRFAATLGELVGGRVGLAYGSVGVLKASNTIAIRYSL 357

                         250       260
                  ....*....|....*....|....*...
gi 1959994196 268 DRVQFGK------AIVEHQSIANLLADM 289
Cdd:PLN02636  358 LRQQFGPpkqpeiSILDYQSQQHKLMPM 385
NcnH cd01159
Naphthocyclinone hydroxylase; Naphthocyclinone is an aromatic polyketide and an antibiotic, ...
 17-358 2.55e-16

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: 79.32  E-value: 2.55e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1959994196  17 ARDFARgEIAPHAQAWEKAGWIDDGLVAKMGELGLLGMVVPEEWGGTYVDYVAYALAVEEISAGDGATG---AFMSIHNS 93
Cdd:cd01159     3 AEDLAP-LIRERAPEAERARRLPDEVVRALREIGFFRMFVPKRYGGLEGDFAEFAEAIATLAEACGSAAwvaSIVATHSR 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1959994196  94 VGCGpvlnYGSEEQKQTWLAD---LASGAVIgcfcltePQAgseahnlrtRAELRDGQWVINGAKQFVSNGKRAKLAIVF 170
Cdd:cd01159    82 MLAA----FPPEAQEEVWGDGpdtLLAGSYA-------PGG---------RAERVDGGYRVSGTWPFASGCDHADWILVG 141

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1959994196 171 AVTDPDLGKRGISAFLVPTDtpGFIVDRTEHKMGIRASDTCAVTLSNCSIPEANLL------GERGKGLAIALSNLEGGR 244
Cdd:cd01159   142 AIVEDDDGGPLPRAFVVPRA--EYEIVDTWHVVGLRGTGSNTVVVDDVFVPEHRTLtagdmmAGDGPGGSTPVYRMPLRQ 219

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1959994196 245 I---GIAAQALGIARAAFEAALGYARDRVQFGKAIV---EHQSIANLLADMQMQINAARLMILHAAR-----LRTAGKPC 313
Cdd:cd01159   220 VfplSFAAVSLGAAEGALAEFLELAGKRVRQYGAAVkmaEAPITQLRLAEAAAELDAARAFLERATRdlwahALAGGPID 299

                         330       340       350       360
                  ....*....|....*....|....*....|....*....|....*....
gi 1959994196 314 LSEASQAKLFASEmAEKVCSSAIQI----HGGYGYLEDYPVEKYYRDAR 358
Cdd:cd01159   300 VEERARIRRDAAY-AAKLSAEAVDRlfhaAGGSALYTASPLQRIWRDIH 347
PLN02312 PLN02312
acyl-CoA oxidase
 97-272 3.15e-06

acyl-CoA oxidase


Pssm-ID: 215178 [Multi-domain]  Cd Length: 680  Bit Score: 49.00  E-value: 3.15e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1959994196  97 GPVLNYGSEEQKQTWLADLASGAVIGCFCLTEPQAGSEAHNLRTRA--ELRDGQWVIN----GAKQFVSNG--KRAKLAI 168
Cdd:PLN02312  162 GAIKFLGTKRHHDKWLKDTEDYVVKGCFAMTELGHGSNVRGIETVTtyDPKTEEFVINtpceSAQKYWIGGaaNHATHTI 241

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1959994196 169 VFAVTDPDLGKRGISAFLVP------TDTPGFIVDRTEHKMGIRASDTCAVTLSNCSIPEANLLGE------RGKGL--- 233
Cdd:PLN02312  242 VFSQLHINGKNEGVHAFIAQirdqdgNICPNIRIADCGHKIGLNGVDNGRIWFDNLRIPRENLLNSvadvspDGKYVsai 321

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*.
gi 1959994196 234 -------AIALSNLEGGRIGIAAQALGIARAAFEAALGYARDRVQF 272
Cdd:PLN02312  322 kdpdqrfGAFLAPLTSGRVTIAVSAIYSSKVGLAIAIRYSLSRRAF 367
PLN02443 PLN02443
acyl-coenzyme A oxidase
 103-210 7.37e-05

acyl-coenzyme A oxidase


Pssm-ID: 178062 [Multi-domain]  Cd Length: 664  Bit Score: 44.83  E-value: 7.37e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1959994196 103 GSEEQKQTWLADLASGAVIGCFCLTEPQAGSEAHNLRTRA--ELRDGQWVINGAKQFVSN------GKRAKLAIVFAVTD 174
Cdd:PLN02443  114 GTEEQQKKWLPLAYKMQIIGCYAQTELGHGSNVQGLETTAtfDPKTDEFVIHSPTLTSSKwwpgglGKVSTHAVVYARLI 193

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|...
gi 1959994196 175 PDLGKRGISAFLVP-------TDTPGFIVDRTEHKMGIRASDT 210
Cdd:PLN02443  194 TNGKDHGIHGFIVQlrslddhSPLPGVTVGDIGMKFGNGAYNT 236
PTZ00460 PTZ00460
acyl-CoA dehydrogenase; Provisional
 103-226 8.88e-05

acyl-CoA dehydrogenase; Provisional


Pssm-ID: 185639 [Multi-domain]  Cd Length: 646  Bit Score: 44.45  E-value: 8.88e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1959994196 103 GSEEQKQTWLADLASGAVIGCFCLTEPQAGSEAHNLRTRA--ELRDGQWVIN----GAKQFVSN--GKRAKLAIVFAVTD 174
Cdd:PTZ00460  110 GTDEQINLWMPSLLNFEIVGCYAQTELGHGSDVQNLETTAtyDKQTNEFVIHtpsvEAVKFWPGelGFLCNFALVYAKLI 189

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1959994196 175 PDLGKRGISAFLVP---TDT----PGFIVDRTEHKMGIRASDTCAVTLSNCSIPEANLL 226
Cdd:PTZ00460  190 VNGKNKGVHPFMVRirdKEThkplQGVEVGDIGPKMGYAVKDNGFLSFDHYRIPLDSLL 248
 
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.
Help | Disclaimer | Write to the Help Desk
NCBI | NLM | NIH