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Conserved domains on  [gi|754529347|ref|WP_041932463|]
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acyl-CoA dehydrogenase family protein [Cytophaga hutchinsonii]

Protein Classification

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

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

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
ACAD super family cl09933
Acyl-CoA dehydrogenase; Both mitochondrial acyl-CoA dehydrogenases (ACAD) and peroxisomal ...
 7-379 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: 530.30  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754529347   7 ENQRLIASMAKDVAEKYIRPNIMKWDEVQEFPVDLFHKMGEFGLLGVLVPEQYGGAGMGYFEYITALEEISKVCGSIGLS 86
Cdd:cd01158    1 EEHQMIRKTVRDFAEKEIAPLAAEMDEKGEFPREVIKEMAELGLMGIPIPEEYGGAGLDFLAYAIAIEELAKVDASVAVI 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754529347  87 MAAHNSLCTGHILAFGNEEQKAKYLPLLATGKWIGAWALTEANTGSDSGNMKTVARQDGDYWILNGSKNFITHAKSSNVV 166
Cdd:cd01158   81 VSVHNSLGANPIIKFGTEEQKKKYLPPLATGEKIGAFALSEPGAGSDAAALKTTAKKDGDDYVLNGSKMWITNGGEADFY 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754529347 167 VVLARHADSEDKKFSSAFIIEKGTEGLTHGRKENKMGMRASETCELLLDNVRVHKSQLLGNIGDGFKQAMKVLDGGRISI 246
Cdd:cd01158  161 IVFAVTDPSKGYRGITAFIVERDTPGLSVGKKEDKLGIRGSSTTELIFEDVRVPKENILGEEGEGFKIAMQTLDGGRIGI 240

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754529347 247 AALSLGIAQGAYEAALQYSKERQQFNQPIGNFQGISFKLVDMATEIEAARLLTYKAADMKMKGQPMTREAAMAKLYASEV 326
Cdd:cd01158  241 AAQALGIAQAALDAAVDYAKERKQFGKPIADFQGIQFKLADMATEIEAARLLTYKAARLKDNGEPFIKEAAMAKLFASEV 320

                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|...
gi 754529347 327 SVRVANEAVQIFGGYGYTKDYPVEKFYRDAKLCTIGEGTSEIQKIVIAKSLQK 379
Cdd:cd01158  321 AMRVTTDAVQIFGGYGYTKDYPVERYYRDAKITEIYEGTSEIQRLVIAKHLLK 373
 
Name Accession Description Interval E-value
SCAD_SBCAD cd01158
Short chain acyl-CoA dehydrogenases and eukaryotic short/branched chain acyl-CoA ...
 7-379 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: 530.30  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754529347   7 ENQRLIASMAKDVAEKYIRPNIMKWDEVQEFPVDLFHKMGEFGLLGVLVPEQYGGAGMGYFEYITALEEISKVCGSIGLS 86
Cdd:cd01158    1 EEHQMIRKTVRDFAEKEIAPLAAEMDEKGEFPREVIKEMAELGLMGIPIPEEYGGAGLDFLAYAIAIEELAKVDASVAVI 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754529347  87 MAAHNSLCTGHILAFGNEEQKAKYLPLLATGKWIGAWALTEANTGSDSGNMKTVARQDGDYWILNGSKNFITHAKSSNVV 166
Cdd:cd01158   81 VSVHNSLGANPIIKFGTEEQKKKYLPPLATGEKIGAFALSEPGAGSDAAALKTTAKKDGDDYVLNGSKMWITNGGEADFY 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754529347 167 VVLARHADSEDKKFSSAFIIEKGTEGLTHGRKENKMGMRASETCELLLDNVRVHKSQLLGNIGDGFKQAMKVLDGGRISI 246
Cdd:cd01158  161 IVFAVTDPSKGYRGITAFIVERDTPGLSVGKKEDKLGIRGSSTTELIFEDVRVPKENILGEEGEGFKIAMQTLDGGRIGI 240

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754529347 247 AALSLGIAQGAYEAALQYSKERQQFNQPIGNFQGISFKLVDMATEIEAARLLTYKAADMKMKGQPMTREAAMAKLYASEV 326
Cdd:cd01158  241 AAQALGIAQAALDAAVDYAKERKQFGKPIADFQGIQFKLADMATEIEAARLLTYKAARLKDNGEPFIKEAAMAKLFASEV 320

                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|...
gi 754529347 327 SVRVANEAVQIFGGYGYTKDYPVEKFYRDAKLCTIGEGTSEIQKIVIAKSLQK 379
Cdd:cd01158  321 AMRVTTDAVQIFGGYGYTKDYPVERYYRDAKITEIYEGTSEIQRLVIAKHLLK 373
CaiA COG1960
Acyl-CoA dehydrogenase related to the alkylation response protein AidB [Lipid transport and ...
 1-379 2.18e-180

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: 505.53  E-value: 2.18e-180
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754529347   1 MNLEPTENQRLIASMAKDVAEKYIRPNIMKWDEVQEFPVDLFHKMGEFGLLGVLVPEQYGGAGMGYFEYITALEEISKVC 80
Cdd:COG1960    1 MDFELTEEQRALRDEVREFAEEEIAPEAREWDREGEFPRELWRKLAELGLLGLTIPEEYGGLGLSLVELALVLEELARAD 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754529347  81 GSIGLSMAAHNSlCTGHILAFGNEEQKAKYLPLLATGKWIGAWALTEANTGSDSGNMKTVARQDGDYWILNGSKNFITHA 160
Cdd:COG1960   81 ASLALPVGVHNG-AAEALLRFGTEEQKERYLPRLASGEWIGAFALTEPGAGSDAAALRTTAVRDGDGYVLNGQKTFITNA 159

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754529347 161 KSSNVVVVLARHADSEDKKFSSAFIIEKGTEGLTHGRKENKMGMRASETCELLLDNVRVHKSQLLGNIGDGFKQAMKVLD 240
Cdd:COG1960  160 PVADVILVLARTDPAAGHRGISLFLVPKDTPGVTVGRIEDKMGLRGSDTGELFFDDVRVPAENLLGEEGKGFKIAMSTLN 239

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754529347 241 GGRISIAALSLGIAQGAYEAALQYSKERQQFNQPIGNFQGISFKLVDMATEIEAARLLTYKAADMKMKGQPMTREAAMAK 320
Cdd:COG1960  240 AGRLGLAAQALGIAEAALELAVAYAREREQFGRPIADFQAVQHRLADMAAELEAARALVYRAAWLLDAGEDAALEAAMAK 319

                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 754529347 321 LYASEVSVRVANEAVQIFGGYGYTKDYPVEKFYRDAKLCTIGEGTSEIQKIVIAKSLQK 379
Cdd:COG1960  320 LFATEAALEVADEALQIHGGYGYTREYPLERLYRDARILTIYEGTNEIQRLIIARRLLG 378
PLN02519 PLN02519
isovaleryl-CoA dehydrogenase
 7-379 7.64e-102

isovaleryl-CoA dehydrogenase


Pssm-ID: 215284 [Multi-domain]  Cd Length: 404  Bit Score: 306.80  E-value: 7.64e-102
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754529347   7 ENQRLIASMAKDVAEKYIRPNIMKWDEVQEFP--VDLFHKMGEFGLLGVLVPEQYGGAGMGYFEYITALEEISKVCGSIG 84
Cdd:PLN02519  28 DTQLQFKESVQQFAQENIAPHAAAIDATNSFPkdVNLWKLMGDFNLHGITAPEEYGGLGLGYLYHCIAMEEISRASGSVG 107

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754529347  85 LSMAAHNSLCTGHILAFGNEEQKAKYLPLLATGKWIGAWALTEANTGSDSGNMKTVA-RQDGDYwILNGSKNFITHAKSS 163
Cdd:PLN02519 108 LSYGAHSNLCINQLVRNGTPAQKEKYLPKLISGEHVGALAMSEPNSGSDVVSMKCKAeRVDGGY-VLNGNKMWCTNGPVA 186

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754529347 164 NVVVVLARHADSEDKKFSSAFIIEKGTEGLTHGRKENKMGMRASETCELLLDNVRVHKSQLLGNIGDGFKQAMKVLDGGR 243
Cdd:PLN02519 187 QTLVVYAKTDVAAGSKGITAFIIEKGMPGFSTAQKLDKLGMRGSDTCELVFENCFVPEENVLGQEGKGVYVMMSGLDLER 266

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754529347 244 ISIAALSLGIAQGAYEAALQYSKERQQFNQPIGNFQGISFKLVDMATEIEAARLLTYKAADMKMKGQPMTREAAMAKLYA 323
Cdd:PLN02519 267 LVLAAGPLGLMQACLDVVLPYVRQREQFGRPIGEFQFIQGKLADMYTSLQSSRSYVYSVARDCDNGKVDRKDCAGVILCA 346

                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 754529347 324 SEVSVRVANEAVQIFGGYGYTKDYPVEKFYRDAKLCTIGEGTSEIQKIVIAKSLQK 379
Cdd:PLN02519 347 AERATQVALQAIQCLGGNGYINEYPTGRLLRDAKLYEIGAGTSEIRRMLIGRELFK 402
Acyl-CoA_dh_1 pfam00441
Acyl-CoA dehydrogenase, C-terminal domain; C-terminal domain of Acyl-CoA dehydrogenase is an ...
 229-377 8.82e-63

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: 197.86  E-value: 8.82e-63
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754529347  229 GDGFKQAMKVLDGGRISIAALSLGIAQGAYEAALQYSKERQQFNQPIGNFQGISFKLVDMATEIEAARLLTYKAADMKMK 308
Cdd:pfam00441   1 GRGFRVAMETLNHERLAIAAMALGLARRALDEALAYARRRKAFGRPLIDFQLVRHKLAEMAAEIEAARLLVYRAAEALDA 80

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 754529347  309 GQPMTREAAMAKLYASEVSVRVANEAVQIFGGYGYTKDYPVEKFYRDAKLCTIGEGTSEIQKIVIAKSL 377
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 ...
 7-379 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: 530.30  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754529347   7 ENQRLIASMAKDVAEKYIRPNIMKWDEVQEFPVDLFHKMGEFGLLGVLVPEQYGGAGMGYFEYITALEEISKVCGSIGLS 86
Cdd:cd01158    1 EEHQMIRKTVRDFAEKEIAPLAAEMDEKGEFPREVIKEMAELGLMGIPIPEEYGGAGLDFLAYAIAIEELAKVDASVAVI 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754529347  87 MAAHNSLCTGHILAFGNEEQKAKYLPLLATGKWIGAWALTEANTGSDSGNMKTVARQDGDYWILNGSKNFITHAKSSNVV 166
Cdd:cd01158   81 VSVHNSLGANPIIKFGTEEQKKKYLPPLATGEKIGAFALSEPGAGSDAAALKTTAKKDGDDYVLNGSKMWITNGGEADFY 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754529347 167 VVLARHADSEDKKFSSAFIIEKGTEGLTHGRKENKMGMRASETCELLLDNVRVHKSQLLGNIGDGFKQAMKVLDGGRISI 246
Cdd:cd01158  161 IVFAVTDPSKGYRGITAFIVERDTPGLSVGKKEDKLGIRGSSTTELIFEDVRVPKENILGEEGEGFKIAMQTLDGGRIGI 240

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754529347 247 AALSLGIAQGAYEAALQYSKERQQFNQPIGNFQGISFKLVDMATEIEAARLLTYKAADMKMKGQPMTREAAMAKLYASEV 326
Cdd:cd01158  241 AAQALGIAQAALDAAVDYAKERKQFGKPIADFQGIQFKLADMATEIEAARLLTYKAARLKDNGEPFIKEAAMAKLFASEV 320

                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|...
gi 754529347 327 SVRVANEAVQIFGGYGYTKDYPVEKFYRDAKLCTIGEGTSEIQKIVIAKSLQK 379
Cdd:cd01158  321 AMRVTTDAVQIFGGYGYTKDYPVERYYRDAKITEIYEGTSEIQRLVIAKHLLK 373
CaiA COG1960
Acyl-CoA dehydrogenase related to the alkylation response protein AidB [Lipid transport and ...
 1-379 2.18e-180

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: 505.53  E-value: 2.18e-180
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754529347   1 MNLEPTENQRLIASMAKDVAEKYIRPNIMKWDEVQEFPVDLFHKMGEFGLLGVLVPEQYGGAGMGYFEYITALEEISKVC 80
Cdd:COG1960    1 MDFELTEEQRALRDEVREFAEEEIAPEAREWDREGEFPRELWRKLAELGLLGLTIPEEYGGLGLSLVELALVLEELARAD 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754529347  81 GSIGLSMAAHNSlCTGHILAFGNEEQKAKYLPLLATGKWIGAWALTEANTGSDSGNMKTVARQDGDYWILNGSKNFITHA 160
Cdd:COG1960   81 ASLALPVGVHNG-AAEALLRFGTEEQKERYLPRLASGEWIGAFALTEPGAGSDAAALRTTAVRDGDGYVLNGQKTFITNA 159

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754529347 161 KSSNVVVVLARHADSEDKKFSSAFIIEKGTEGLTHGRKENKMGMRASETCELLLDNVRVHKSQLLGNIGDGFKQAMKVLD 240
Cdd:COG1960  160 PVADVILVLARTDPAAGHRGISLFLVPKDTPGVTVGRIEDKMGLRGSDTGELFFDDVRVPAENLLGEEGKGFKIAMSTLN 239

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754529347 241 GGRISIAALSLGIAQGAYEAALQYSKERQQFNQPIGNFQGISFKLVDMATEIEAARLLTYKAADMKMKGQPMTREAAMAK 320
Cdd:COG1960  240 AGRLGLAAQALGIAEAALELAVAYAREREQFGRPIADFQAVQHRLADMAAELEAARALVYRAAWLLDAGEDAALEAAMAK 319

                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 754529347 321 LYASEVSVRVANEAVQIFGGYGYTKDYPVEKFYRDAKLCTIGEGTSEIQKIVIAKSLQK 379
Cdd:COG1960  320 LFATEAALEVADEALQIHGGYGYTREYPLERLYRDARILTIYEGTNEIQRLIIARRLLG 378
IVD cd01156
Isovaleryl-CoA dehydrogenase; Isovaleryl-CoA dehydrogenase (IVD) is an is an acyl-CoA ...
 6-379 1.27e-137

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: 397.17  E-value: 1.27e-137
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754529347   6 TENQRLIASMAKDVAEKYIRPNIMKWDEVQEFPVDLFHKMGEFGLLGVLVPEQYGGAGMGYFEYITALEEISKVCGSIGL 85
Cdd:cd01156    3 DDEIEMLRQSVREFAQKEIAPLAAKIDRDNEFPRDLWRKMGKLGLLGITAPEEYGGSGMGYLAHVIIMEEISRASGSVAL 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754529347  86 SMAAHNSLCTGHILAFGNEEQKAKYLPLLATGKWIGAWALTEANTGSDSGNMKTVARQDGDYWILNGSKNFITHAKSSNV 165
Cdd:cd01156   83 SYGAHSNLCINQIYRNGSAAQKEKYLPKLISGEHIGALAMSEPNAGSDVVSMKLRAEKKGDRYVLNGSKMWITNGPDADT 162

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754529347 166 VVVLARHADSEDKKFSSAFIIEKGTEGLTHGRKENKMGMRASETCELLLDNVRVHKSQLLGNIGDGFKQAMKVLDGGRIS 245
Cdd:cd01156  163 LVVYAKTDPSAGAHGITAFIVEKGMPGFSRAQKLDKLGMRGSNTCELVFEDCEVPEENILGGENKGVYVLMSGLDYERLV 242

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754529347 246 IAALSLGIAQGAYEAALQYSKERQQFNQPIGNFQGISFKLVDMATEIEAARLLTYKAADMKMKGQPMTREAAMAKLYASE 325
Cdd:cd01156  243 LAGGPIGIMQAALDVAIPYAHQRKQFGQPIGEFQLVQGKLADMYTRLNASRSYLYTVAKACDRGNMDPKDAAGVILYAAE 322

                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|....
gi 754529347 326 VSVRVANEAVQIFGGYGYTKDYPVEKFYRDAKLCTIGEGTSEIQKIVIAKSLQK 379
Cdd:cd01156  323 KATQVALDAIQILGGNGYINDYPTGRLLRDAKLYEIGAGTSEIRRMVIGRELFK 376
ACAD cd00567
Acyl-CoA dehydrogenase; Both mitochondrial acyl-CoA dehydrogenases (ACAD) and peroxisomal ...
 7-375 5.46e-128

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: 370.85  E-value: 5.46e-128
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754529347   7 ENQRLIASMAKDVAEKYIRPNIMKWDEVQEFPVDLFHKMGEFGllgvlvpeqyggagmgyfeyitaleeiskvcgsigls 86
Cdd:cd00567    1 EEQRELRDSAREFAAEELEPYARERRETPEEPWELLAELGLLL------------------------------------- 43

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754529347  87 maahnslCTGHILAFGNEEQKAKYLPLLATGKWIGAWALTEANTGSDSGNMKTVARQDGDYWILNGSKNFITHAKSSNVV 166
Cdd:cd00567   44 -------GAALLLAYGTEEQKERYLPPLASGEAIAAFALTEPGAGSDLAGIRTTARKDGDGYVLNGRKIFISNGGDADLF 116

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754529347 167 VVLARHADSEDKKFS-SAFIIEKGTEGLTHGRKENKMGMRASETCELLLDNVRVHKSQLLGNIGDGFKQAMKVLDGGRIS 245
Cdd:cd00567  117 IVLARTDEEGPGHRGiSAFLVPADTPGVTVGRIWDKMGMRGSGTGELVFDDVRVPEDNLLGEEGGGFELAMKGLNVGRLL 196

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754529347 246 IAALSLGIAQGAYEAALQYSKERQQFNQPIGNFQGISFKLVDMATEIEAARLLTYKAADMKMKGQP-MTREAAMAKLYAS 324
Cdd:cd00567  197 LAAVALGAARAALDEAVEYAKQRKQFGKPLAEFQAVQFKLADMAAELEAARLLLYRAAWLLDQGPDeARLEAAMAKLFAT 276

                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|.
gi 754529347 325 EVSVRVANEAVQIFGGYGYTKDYPVEKFYRDAKLCTIGEGTSEIQKIVIAK 375
Cdd:cd00567  277 EAAREVADLAMQIHGGRGYSREYPVERYLRDARAARIAEGTAEIQRLIIAR 327
IBD cd01162
Isobutyryl-CoA dehydrogenase; Isobutyryl-CoA dehydrogenase (IBD) catalyzes the alpha, beta- ...
 6-377 2.17e-123

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: 360.99  E-value: 2.17e-123
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754529347   6 TENQRLIASMAKDVAEKYIRPNIMKWDEVQEFPVDLFHKMGEFGLLGVLVPEQYGGAGMGYFEYITALEEISKVCGSIGL 85
Cdd:cd01162    2 NEEQRAIQEVARAFAAKEMAPHAADWDQKKHFPVDVLRKAAELGFGGIYIRDDVGGSGLSRLDASIIFEALSTGCVSTAA 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754529347  86 SMAAHNsLCTGHILAFGNEEQKAKYLPLLATGKWIGAWALTEANTGSDSGNMKTVARQDGDYWILNGSKNFITHAKSSNV 165
Cdd:cd01162   82 YISIHN-MCAWMIDSFGNDEQRERFLPDLCTMEKLASYCLTEPGSGSDAAALRTRAVREGDHYVLNGSKAFISGAGDSDV 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754529347 166 VVVLARhADSEDKKFSSAFIIEKGTEGLTHGRKENKMGMRASETCELLLDNVRVHKSQLLGNIGDGFKQAMKVLDGGRIS 245
Cdd:cd01162  161 YVVMAR-TGGEGPKGISCFVVEKGTPGLSFGANEKKMGWNAQPTRAVIFEDCRVPVENRLGGEGQGFGIAMAGLNGGRLN 239

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754529347 246 IAALSLGIAQGAYEAALQYSKERQQFNQPIGNFQGISFKLVDMATEIEAARLLTYKAADMKMKGQP-MTREAAMAKLYAS 324
Cdd:cd01162  240 IASCSLGAAQAALDLARAYLEERKQFGKPLADFQALQFKLADMATELVASRLMVRRAASALDRGDPdAVKLCAMAKRFAT 319

                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|...
gi 754529347 325 EVSVRVANEAVQIFGGYGYTKDYPVEKFYRDAKLCTIGEGTSEIQKIVIAKSL 377
Cdd:cd01162  320 DECFDVANQALQLHGGYGYLKDYPVEQYVRDLRVHQILEGTNEIMRLIIARAL 372
VLCAD cd01161
Very long chain acyl-CoA dehydrogenase; VLCAD is an acyl-CoA dehydrogenase (ACAD), which is ...
 1-376 9.87e-108

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: 322.11  E-value: 9.87e-108
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754529347   1 MNLEPTENQRLIASMAKDVAEKYIRPniMKWDEVQEFPVDLFHKMGEFGLLGVLVPEQYGGAGMGYFEYiTALEEISKVC 80
Cdd:cd01161   23 LTEEQTEELNMLVGPVEKFFEEVNDP--AKNDQLEKIPRKTLTQLKELGLFGLQVPEEYGGLGLNNTQY-ARLAEIVGMD 99

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754529347  81 GSIGLSMAAHNSLCTGHILAFGNEEQKAKYLPLLATGKWIGAWALTEANTGSDSGNMKTVAR--QDGDYWILNGSKNFIT 158
Cdd:cd01161  100 LGFSVTLGAHQSIGFKGILLFGTEAQKEKYLPKLASGEWIAAFALTEPSSGSDAASIRTTAVlsEDGKHYVLNGSKIWIT 179

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754529347 159 HAKSSNVVVVLAR----HADSEDKKFSSAFIIEKGTEGLTHGRKENKMGMRASETCELLLDNVRVHKSQLLGNIGDGFKQ 234
Cdd:cd01161  180 NGGIADIFTVFAKtevkDATGSVKDKITAFIVERSFGGVTNGPPEKKMGIKGSNTAEVYFEDVKIPVENVLGEVGDGFKV 259

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754529347 235 AMKVLDGGRISIAALSLGIAQGAYEAALQYSKERQQFNQPIGNFQGISFKLVDMATEIEAARLLTYKAADMkMKGQPMTR 314
Cdd:cd01161  260 AMNILNNGRFGMGAALIGTMKRCIEKAVDYANNRKQFGKKIHEFGLIQEKLANMAILQYATESMAYMTSGN-MDRGLKAE 338

                        330       340       350       360       370       380
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 754529347 315 ---EAAMAKLYASEVSVRVANEAVQIFGGYGYTKDYPVEKFYRDAKLCTIGEGTSEIQKIVIAKS 376
Cdd:cd01161  339 yqiEAAISKVFASEAAWLVVDEAIQIHGGMGFMREYGVERVLRDLRIFRIFEGTNEILRLFIALT 403
LCAD cd01160
Long chain acyl-CoA dehydrogenase; LCAD is an acyl-CoA dehydrogenases (ACAD), which is found ...
 21-377 2.03e-104

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: 312.51  E-value: 2.03e-104
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754529347  21 EKYIRPNIMKWDEVQEFPVDLFHKMGEFGLLGVLVPEQYGGAGMGYFEYITALEEISKVCGSiGLSMAAHNSLCTGHILA 100
Cdd:cd01160   15 AKEVAPFHHEWEKAGEVPREVWRKAGEQGLLGVGFPEEYGGIGGDLLSAAVLWEELARAGGS-GPGLSLHTDIVSPYITR 93

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754529347 101 FGNEEQKAKYLPLLATGKWIGAWALTEANTGSDSGNMKTVARQDGDYWILNGSKNFITHAKSSNVVVVLARhADSEDKKF 180
Cdd:cd01160   94 AGSPEQKERVLPQMVAGKKIGAIAMTEPGAGSDLQGIRTTARKDGDHYVLNGSKTFITNGMLADVVIVVAR-TGGEARGA 172

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754529347 181 S--SAFIIEKGTEGLTHGRKENKMGMRASETCELLLDNVRVHKSQLLGNIGDGFKQAMKVLDGGRISIAALSLGIAQGAY 258
Cdd:cd01160  173 GgiSLFLVERGTPGFSRGRKLKKMGWKAQDTAELFFDDCRVPAENLLGEENKGFYYLMQNLPQERLLIAAGALAAAEFML 252

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754529347 259 EAALQYSKERQQFNQPIGNFQGISFKLVDMATEIEAARLLTYKAADMKMKGQPMTREAAMAKLYASEVSVRVANEAVQIF 338
Cdd:cd01160  253 EETRNYVKQRKAFGKTLAQLQVVRHKIAELATKVAVTRAFLDNCAWRHEQGRLDVAEASMAKYWATELQNRVAYECVQLH 332

                        330       340       350
                 ....*....|....*....|....*....|....*....
gi 754529347 339 GGYGYTKDYPVEKFYRDAKLCTIGEGTSEIQKIVIAKSL 377
Cdd:cd01160  333 GGWGYMREYPIARAYRDARVQPIYGGTTEIMKELISRQM 371
PLN02519 PLN02519
isovaleryl-CoA dehydrogenase
 7-379 7.64e-102

isovaleryl-CoA dehydrogenase


Pssm-ID: 215284 [Multi-domain]  Cd Length: 404  Bit Score: 306.80  E-value: 7.64e-102
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754529347   7 ENQRLIASMAKDVAEKYIRPNIMKWDEVQEFP--VDLFHKMGEFGLLGVLVPEQYGGAGMGYFEYITALEEISKVCGSIG 84
Cdd:PLN02519  28 DTQLQFKESVQQFAQENIAPHAAAIDATNSFPkdVNLWKLMGDFNLHGITAPEEYGGLGLGYLYHCIAMEEISRASGSVG 107

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754529347  85 LSMAAHNSLCTGHILAFGNEEQKAKYLPLLATGKWIGAWALTEANTGSDSGNMKTVA-RQDGDYwILNGSKNFITHAKSS 163
Cdd:PLN02519 108 LSYGAHSNLCINQLVRNGTPAQKEKYLPKLISGEHVGALAMSEPNSGSDVVSMKCKAeRVDGGY-VLNGNKMWCTNGPVA 186

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754529347 164 NVVVVLARHADSEDKKFSSAFIIEKGTEGLTHGRKENKMGMRASETCELLLDNVRVHKSQLLGNIGDGFKQAMKVLDGGR 243
Cdd:PLN02519 187 QTLVVYAKTDVAAGSKGITAFIIEKGMPGFSTAQKLDKLGMRGSDTCELVFENCFVPEENVLGQEGKGVYVMMSGLDLER 266

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754529347 244 ISIAALSLGIAQGAYEAALQYSKERQQFNQPIGNFQGISFKLVDMATEIEAARLLTYKAADMKMKGQPMTREAAMAKLYA 323
Cdd:PLN02519 267 LVLAAGPLGLMQACLDVVLPYVRQREQFGRPIGEFQFIQGKLADMYTSLQSSRSYVYSVARDCDNGKVDRKDCAGVILCA 346

                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 754529347 324 SEVSVRVANEAVQIFGGYGYTKDYPVEKFYRDAKLCTIGEGTSEIQKIVIAKSLQK 379
Cdd:PLN02519 347 AERATQVALQAIQCLGGNGYINEYPTGRLLRDAKLYEIGAGTSEIRRMLIGRELFK 402
GCD cd01151
Glutaryl-CoA dehydrogenase; Glutaryl-CoA dehydrogenase (GCD). GCD is an acyl-CoA dehydrogenase, ...
 6-375 1.15e-97

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: 295.42  E-value: 1.15e-97
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754529347   6 TENQRLIASMAKDVAEKYIRPNIMKWDEVQEFPVDLFHKMGEFGLLGVLvPEQYGGAGMGYFEYITALEEISKVCGSIGL 85
Cdd:cd01151   14 TEEERAIRDTAREFCQEELAPRVLEAYREEKFDRKIIEEMGELGLLGAT-IKGYGCAGLSSVAYGLIAREVERVDSGYRS 92

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754529347  86 SMAAHNSLCTGHILAFGNEEQKAKYLPLLATGKWIGAWALTEANTGSDSGNMKTVARQDGDYWILNGSKNFITHAKSSNV 165
Cdd:cd01151   93 FMSVQSSLVMLPIYDFGSEEQKQKYLPKLASGELIGCFGLTEPNHGSDPGGMETRARKDGGGYKLNGSKTWITNSPIADV 172

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754529347 166 VVVLARHADSEDKKfssAFIIEKGTEGLTHGRKENKMGMRASETCELLLDNVRVHKSQLLGNIgDGFKQAMKVLDGGRIS 245
Cdd:cd01151  173 FVVWARNDETGKIR---GFILERGMKGLSAPKIQGKFSLRASITGEIVMDNVFVPEENLLPGA-EGLRGPFKCLNNARYG 248

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754529347 246 IAALSLGIAQGAYEAALQYSKERQQFNQPIGNFQGISFKLVDMATEIEAARLLTYKAADMKMKGQPMTREAAMAKLYASE 325
Cdd:cd01151  249 IAWGALGAAEDCYHTARQYVLDRKQFGRPLAAFQLVQKKLADMLTEIALGLLACLRVGRLKDQGKATPEQISLLKRNNCG 328

                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|
gi 754529347 326 VSVRVANEAVQIFGGYGYTKDYPVEKFYRDAKLCTIGEGTSEIQKIVIAK 375
Cdd:cd01151  329 KALEIARTAREMLGGNGISDEYHIIRHMVNLESVNTYEGTHDIHALILGR 378
MCAD cd01157
Medium chain acyl-CoA dehydrogenase; MCADs are mitochondrial beta-oxidation enzymes, which ...
 6-377 2.99e-94

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: 286.79  E-value: 2.99e-94
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754529347   6 TENQRLIASMAKDVAEKYIRPNIMKWDEVQEFPVDLFHKMGEFGLLGVLVPEQYGGAGMGYFEYITALEEISKVCGSIGL 85
Cdd:cd01157    2 TEQQKEFQETARKFAREEIIPVAAEYDKSGEYPWPLIKRAWELGLMNTHIPEDCGGLGLGTFDTCLITEELAYGCTGVQT 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754529347  86 SMAAhNSLCTGHILAFGNEEQKAKYLPLLATGKWIGAWALTEANTGSDSGNMKTVARQDGDYWILNGSKNFITHAKSSNV 165
Cdd:cd01157   82 AIEA-NSLGQMPVIISGNDEQKKKYLGRMTEEPLMCAYCVTEPGAGSDVAGIKTKAEKKGDEYIINGQKMWITNGGKANW 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754529347 166 VVVLARhADSEDK----KFSSAFIIEKGTEGLTHGRKENKMGMRASETCELLLDNVRVHKSQLLGNIGDGFKQAMKVLDG 241
Cdd:cd01157  161 YFLLAR-SDPDPKcpasKAFTGFIVEADTPGIQPGRKELNMGQRCSDTRGITFEDVRVPKENVLIGEGAGFKIAMGAFDK 239

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754529347 242 GRISIAALSLGIAQGAYEAALQYSKERQQFNQPIGNFQGISFKLVDMATEIEAARLLTYKAADMKMKGQPMTREAAMAKL 321
Cdd:cd01157  240 TRPPVAAGAVGLAQRALDEATKYALERKTFGKLIAEHQAVSFMLADMAMKVELARLAYQRAAWEVDSGRRNTYYASIAKA 319

                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 754529347 322 YASEVSVRVANEAVQIFGGYGYTKDYPVEKFYRDAKLCTIGEGTSEIQKIVIAKSL 377
Cdd:cd01157  320 FAADIANQLATDAVQIFGGNGFNSEYPVEKLMRDAKIYQIYEGTSQIQRLIISREH 375
PRK12341 PRK12341
acyl-CoA dehydrogenase;
1-379 4.26e-85

acyl-CoA dehydrogenase;


Pssm-ID: 183454 [Multi-domain]  Cd Length: 381  Bit Score: 263.13  E-value: 4.26e-85
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754529347   1 MNLEPTENQRL-IAS----MAKDVAEKYIRpnimKWDEVQEFPVDLFHKMGE--FGLLGVlvPEQYGGAGMGYFEYITAL 73
Cdd:PRK12341   1 MDFSLTEEQELlLASirelITRNFPEEYFR----TCDENGTYPREFMRALADngISMLGV--PEEFGGTPADYVTQMLVL 74

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754529347  74 EEISKVCGSIGLsmaAHNSLCTGHILAFGNEEQKAK-YLPLLATGKWIGAWALTEANTGSDSGNMKTVA-RQDGDYwILN 151
Cdd:PRK12341  75 EEVSKCGAPAFL---ITNGQCIHSMRRFGSAEQLRKtAESTLETGDPAYALALTEPGAGSDNNSATTTYtRKNGKV-YLN 150

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754529347 152 GSKNFITHAKSSNVVVVLARHADSED-KKFSSAFIIEKGTEGLTHGRKEnKMGMRASETCELLLDNVRVHKSQLLGNIGD 230
Cdd:PRK12341 151 GQKTFITGAKEYPYMLVLARDPQPKDpKKAFTLWWVDSSKPGIKINPLH-KIGWHMLSTCEVYLDNVEVEESDLVGEEGM 229

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754529347 231 GFKQAMKVLDGGRISIAALSLGIAQGAYEAALQYSKERQQFNQPIGNFQGISFKLVDMATEIEAARLLTYKAADMKMKGQ 310
Cdd:PRK12341 230 GFLNVMYNFEMERLINAARSLGFAECAFEDAARYANQRIQFGKPIGHNQLIQEKLTLMAIKIENMRNMVYKVAWQADNGQ 309

                        330       340       350       360       370       380
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 754529347 311 PMTREAAMAKLYASEVSVRVANEAVQIFGGYGYTKDYPVEKFYRDAKLCTIGEGTSEIQKIVIAKSLQK 379
Cdd:PRK12341 310 SLRTSAALAKLYCARTAMEVIDDAIQIMGGLGYTDEARVSRFWRDVRCERIGGGTDEIMIYIAGRQILK 378
PTZ00461 PTZ00461
isovaleryl-CoA dehydrogenase; Provisional
 12-379 1.08e-78

isovaleryl-CoA dehydrogenase; Provisional


Pssm-ID: 185640 [Multi-domain]  Cd Length: 410  Bit Score: 247.93  E-value: 1.08e-78
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754529347  12 IASMAKDVAEKYIRPNimkwDEVQEFPVDLFHKMGEFGLLGVLVPEQYGGAGMGYFEYITALEEISKVCGSIGLSMAAHN 91
Cdd:PTZ00461  48 VAKFSREVVDKHARED----DINMHFNRDLFKQLGDLGVMGVTVPEADGGAGMDAVAAVIIHHELSKYDPGFCLAYLAHS 123

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754529347  92 SLCTGHILAFGNEEQKAKYLPLLATGKWIGAWALTEANTGSDSGNMKTVARQDGD-YWILNGSKNFITHAKSSNVVVVLA 170
Cdd:PTZ00461 124 MLFVNNFYYSASPAQRARWLPKVLTGEHVGAMGMSEPGAGTDVLGMRTTAKKDSNgNYVLNGSKIWITNGTVADVFLIYA 203

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754529347 171 RhadsEDKKFSsAFIIEKGTEGLTHGRKENKMGMRASETCELLLDNVRVHKSQLLGNIGDGFKQAMKVLDGGRISIAALS 250
Cdd:PTZ00461 204 K----VDGKIT-AFVVERGTKGFTQGPKIDKCGMRASHMCQLFFEDVVVPAENLLGEEGKGMVGMMRNLELERVTLAAMA 278

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754529347 251 LGIAQGAYEAALQYSKERQQFNQPIGNFQGISFKLVDMATEIEAARLLTYKAADMKMKGQPMTREAAMAKLYASEVSVRV 330
Cdd:PTZ00461 279 VGIAERSVELMTSYASERKAFGKPISNFGQIQRYIAEGYADTEAAKALVYSVSHNVHPGNKNRLGSDAAKLFATPIAKKV 358

                        330       340       350       360
                 ....*....|....*....|....*....|....*....|....*....
gi 754529347 331 ANEAVQIFGGYGYTKDYPVEKFYRDAKLCTIGEGTSEIQKIVIAKSLQK 379
Cdd:PTZ00461 359 ADSAIQVMGGMGYSRDMPVERLWRDAKLLEIGGGTIEAHHKNITKDLLK 407
ACAD_fadE5 cd01153
Putative acyl-CoA dehydrogenases similar to fadE5; Putative acyl-CoA dehydrogenase (ACAD). ...
 39-369 6.77e-72

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: 229.97  E-value: 6.77e-72
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754529347  39 VDLFHKMGEFGLLGVLVPEQYGGAGMGYFEYITALEEISKVCGSIGLSMAAHNSLCtgHILAFGNEEQKAKYLPLLATGK 118
Cdd:cd01153   39 KEALDAFAEAGWMALGVPEEYGGQGLPITVYSALAEIFSRGDAPLMYASGTQGAAA--TLLAHGTEAQREKWIPRLAEGE 116

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754529347 119 WIGAWALTEANTGSDSGNMKTVARQDGD-YWILNGSKNFIT---HAKSSNVV-VVLARHADS-EDKKFSSAFIIEK---G 189
Cdd:cd01153  117 WTGTMCLTEPDAGSDLGALRTKAVYQADgSWRINGVKRFISageHDMSENIVhLVLARSEGApPGVKGLSLFLVPKfldD 196

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754529347 190 TE--GLTHGRKENKMGMRASETCELLLDNvrvHKSQLLGNIGDGFKQAMKVLDGGRISIAALSLGIAQGAYEAALQYSKE 267
Cdd:cd01153  197 GErnGVTVARIEEKMGLHGSPTCELVFDN---AKGELIGEEGMGLAQMFAMMNGARLGVGTQGTGLAEAAYLNALAYAKE 273

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754529347 268 RQQFNQPIGNFQG--------ISFKLVDMATEIEAARLLT-YKAADMKMKGQPMTREAA-------------MAKLYASE 325
Cdd:cd01153  274 RKQGGDLIKAAPAvtiihhpdVRRSLMTQKAYAEGSRALDlYTATVQDLAERKATEGEDrkalsaladlltpVVKGFGSE 353

                        330       340       350       360
                 ....*....|....*....|....*....|....*....|....
gi 754529347 326 VSVRVANEAVQIFGGYGYTKDYPVEKFYRDAKLCTIGEGTSEIQ 369
Cdd:cd01153  354 AALEAVSDAIQVHGGSGYTREYPIEQYYRDARITTIYEGTTGIQ 397
PRK03354 PRK03354
crotonobetainyl-CoA dehydrogenase; Validated
 1-379 3.21e-63

crotonobetainyl-CoA dehydrogenase; Validated


Pssm-ID: 179566 [Multi-domain]  Cd Length: 380  Bit Score: 206.61  E-value: 3.21e-63
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754529347   1 MNLEPTENQRLIAS-----MAKDVAEKYIRpnimKWDEVQEFPVDLFHKMGEFGLLGVLVPEQYGGAGMGYFEYITALEE 75
Cdd:PRK03354   1 MDFNLNDEQELFVAgirelMASENWEAYFA----ECDRDSVYPERFVKALADMGIDSLLIPEEHGGLDAGFVTLAAVWME 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754529347  76 IskvcGSIGLSMAAHNSLCTG--HILAFGNEEQKAKYLPLLATGKWIGAWALTEANTGSDSGNMKTV-ARQDGDYWiLNG 152
Cdd:PRK03354  77 L----GRLGAPTYVLYQLPGGfnTFLREGTQEQIDKIMAFRGTGKQMWNSAITEPGAGSDVGSLKTTyTRRNGKVY-LNG 151

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754529347 153 SKNFITHAKSSNVVVVLARHADSEDKKFSSAFIIEKGTEGLTHGRKEnKMGMRASETCELLLDNVRVHKSQLLGNIGDGF 232
Cdd:PRK03354 152 SKCFITSSAYTPYIVVMARDGASPDKPVYTEWFVDMSKPGIKVTKLE-KLGLRMDSCCEITFDDVELDEKDMFGREGNGF 230

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754529347 233 KQAMKVLDGGRISIAALSLGIAQGAYEAALQYSKERQQFNQPIGNFQGISFKLVDMATEIEAARLLTYKAADMKMKGQPM 312
Cdd:PRK03354 231 NRVKEEFDHERFLVALTNYGTAMCAFEDAARYANQRVQFGEAIGRFQLIQEKFAHMAIKLNSMKNMLYEAAWKADNGTIT 310

                        330       340       350       360       370       380
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 754529347 313 TREAAMAKLYASEVSVRVANEAVQIFGGYGYTKDYPVEKFYRDAKLCTIGEGTSEIQKIVIAKSLQK 379
Cdd:PRK03354 311 SGDAAMCKYFCANAAFEVVDSAMQVLGGVGIAGNHRISRFWRDLRVDRVSGGSDEMQILTLGRAVLK 377
PLN02526 PLN02526
acyl-coenzyme A oxidase
 17-377 4.35e-63

acyl-coenzyme A oxidase


Pssm-ID: 178141 [Multi-domain]  Cd Length: 412  Bit Score: 207.40  E-value: 4.35e-63
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754529347  17 KDVAEKYIRPNIMKWDEVQEFPVDLFHKMGEFGLLGVLVpEQYGGAGMGYFEYITALEEISKVCGSIGLSMAAHNSLCTG 96
Cdd:PLN02526  41 RECMEKEVAPIMTEYWEKAEFPFHIIPKLGSLGIAGGTI-KGYGCPGLSITASAIATAEVARVDASCSTFILVHSSLAML 119

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754529347  97 HILAFGNEEQKAKYLPLLATGKWIGAWALTEANTGSDSGNMKTVARQDGDYWILNGSKNFITHAKSSNVVVVLARHADSE 176
Cdd:PLN02526 120 TIALCGSEAQKQKYLPSLAQLDTVACWALTEPDYGSDASSLNTTATKVEGGWILNGQKRWIGNSTFADVLVIFARNTTTN 199

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754529347 177 DkkfSSAFIIEKGTEGLTHGRKENKMGMRASETCELLLDNVRVHKSQLLGNIgDGFKQAMKVLDGGRISIAALSLGIAQG 256
Cdd:PLN02526 200 Q---INGFIVKKGAPGLKATKIENKIGLRMVQNGDIVLKDVFVPDEDRLPGV-NSFQDTNKVLAVSRVMVAWQPIGISMG 275

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754529347 257 AYEAALQYSKERQQFNQPIGNFQGISFKLVDMATEIEAARLLTYKAADMKMKGQPMTREAAMAKLYASEVSVRVANEAVQ 336
Cdd:PLN02526 276 VYDMCHRYLKERKQFGAPLAAFQINQEKLVRMLGNIQAMFLVGWRLCKLYESGKMTPGHASLGKAWITKKARETVALGRE 355

                        330       340       350       360
                 ....*....|....*....|....*....|....*....|.
gi 754529347 337 IFGGYGYTKDYPVEKFYRDAKLCTIGEGTSEIQKIVIAKSL 377
Cdd:PLN02526 356 LLGGNGILADFLVAKAFCDLEPIYTYEGTYDINALVTGREI 396
Acyl-CoA_dh_1 pfam00441
Acyl-CoA dehydrogenase, C-terminal domain; C-terminal domain of Acyl-CoA dehydrogenase is an ...
 229-377 8.82e-63

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: 197.86  E-value: 8.82e-63
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754529347  229 GDGFKQAMKVLDGGRISIAALSLGIAQGAYEAALQYSKERQQFNQPIGNFQGISFKLVDMATEIEAARLLTYKAADMKMK 308
Cdd:pfam00441   1 GRGFRVAMETLNHERLAIAAMALGLARRALDEALAYARRRKAFGRPLIDFQLVRHKLAEMAAEIEAARLLVYRAAEALDA 80

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 754529347  309 GQPMTREAAMAKLYASEVSVRVANEAVQIFGGYGYTKDYPVEKFYRDAKLCTIGEGTSEIQKIVIAKSL 377
Cdd:pfam00441  81 GGPDGAEASMAKLYASEAAVEVADLAMQLHGGYGYLREYPVERLYRDARVLRIGEGTSEIQRNIIARRL 149
ACAD_fadE6_17_26 cd01152
Putative acyl-CoA dehydrogenases similar to fadE6, fadE17, and fadE26; Putative acyl-CoA ...
 9-377 6.90e-55

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: 184.86  E-value: 6.90e-55
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754529347   9 QRLIASMAKDVAEKYIRPNIMKWDEVQEFPVDLFHKMGEFGLLGVLVPEQYGGAGMGYFEYITALEEISKVC-----GSI 83
Cdd:cd01152    8 AEVRAWLAAHLPPELREESALGYREGREDRRRWQRALAAAGWAAPGWPKEYGGRGASLMEQLIFREEMAAAGapvpfNQI 87

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754529347  84 GLSMAAHNslctghILAFGNEEQKAKYLPLLATGKWIGAWALTEANTGSDSGNMKTVARQDGDYWILNGSKNFITHAKSS 163
Cdd:cd01152   88 GIDLAGPT------ILAYGTDEQKRRFLPPILSGEEIWCQGFSEPGAGSDLAGLRTRAVRDGDDWVVNGQKIWTSGAHYA 161

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754529347 164 NVVVVLARHADSEDK-KFSSAFIIEKGTEGLThgRKENKMGMRASETCELLLDNVRVHKSQLLGNIGDGFKQAMKVLDGG 242
Cdd:cd01152  162 DWAWLLVRTDPEAPKhRGISILLVDMDSPGVT--VRPIRSINGGEFFNEVFLDDVRVPDANRVGEVNDGWKVAMTTLNFE 239

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754529347 243 RISIAalslGIAQGAYEAALQYSKERQQFNQPIGNFQGISFKLVDMATEIEAARLLTYKAADMKMKGQPMTREAAMAKLY 322
Cdd:cd01152  240 RVSIG----GSAATFFELLLARLLLLTRDGRPLIDDPLVRQRLARLEAEAEALRLLVFRLASALAAGKPPGAEASIAKLF 315

                        330       340       350       360       370       380
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 754529347 323 ASEVSVRVANEAVQIFG--------GYGYTKDYPVEKFYRDAKLCTIGEGTSEIQKIVIAKSL 377
Cdd:cd01152  316 GSELAQELAELALELLGtaallrdpAPGAELAGRWEADYLRSRATTIYGGTSEIQRNIIAERL 378
AidB cd01154
Proteins involved in DNA damage response, similar to the AidB gene product; AidB is one of ...
 98-379 6.34e-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: 167.55  E-value: 6.34e-48
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754529347  98 ILAFGNEEQKaKYLPLLATGK----WIGAWALTEANTGSD-SGNMKTVARQDGDYWILNGSKNFiTHAKSSNVVVVLARH 172
Cdd:cd01154  123 LRKYGPEELK-QYLPGLLSDRyktgLLGGTWMTEKQGGSDlGANETTAERSGGGVYRLNGHKWF-ASAPLADAALVLARP 200

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754529347 173 ADSED-KKFSSAFII----EKGT-EGLTHGRKENKMGMRASETCELLLDNVRVHksqLLGNIGDGFKQAMKVLDGGRISI 246
Cdd:cd01154  201 EGAPAgARGLSLFLVprllEDGTrNGYRIRRLKDKLGTRSVATGEVEFDDAEAY---LIGDEGKGIYYILEMLNISRLDN 277

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754529347 247 AALSLGIAQGAYEAALQYSKERQQFNQPIGNFQGISFKLVDMATEIEAARLLTYKAADMKMKGQP-MTREAAMA------ 319
Cdd:cd01154  278 AVAALGIMRRALSEAYHYARHRRAFGKPLIDHPLMRRDLAEMEVDVEAATALTFRAARAFDRAAAdKPVEAHMArlatpv 357

                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 754529347 320 -KLYASEVSVRVANEAVQIFGGYGYTKDYPVEKFYRDAKLCTIGEGTSEIQKIVIAKSLQK 379
Cdd:cd01154  358 aKLIACKRAAPVTSEAMEVFGGNGYLEEWPVARLHREAQVTPIWEGTGNIQALDVLRVLVK 418
Acyl-CoA_dh_N pfam02771
Acyl-CoA dehydrogenase, N-terminal domain; The N-terminal domain of Acyl-CoA dehydrogenase is ...
 6-118 3.79e-47

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: 156.08  E-value: 3.79e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754529347    6 TENQRLIASMAKDVAEKYIRPNIMKWDEVQEFPVDLFHKMGEFGLLGVLVPEQYGGAGMGYFEYITALEEISKVCGSIGL 85
Cdd:pfam02771   1 TEEQEALRDTVREFAEEEIAPHAAEWDEEGEFPRELWKKLGELGLLGITIPEEYGGAGLDYLAYALVAEELARADASVAL 80

                          90       100       110
                  ....*....|....*....|....*....|...
gi 754529347   86 SMAAHNSLCTGHILAFGNEEQKAKYLPLLATGK 118
Cdd:pfam02771  81 ALSVHSSLGAPPILRFGTEEQKERYLPKLASGE 113
ACAD_FadE2 cd01155
Acyl-CoA dehydrogenases similar to fadE2; FadE2-like Acyl-CoA dehydrogenase (ACAD). Acyl-CoA ...
 9-375 9.82e-42

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: 150.62  E-value: 9.82e-42
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754529347   9 QRLIASMAKDV------AEKYIRPNIMKWDEVQEFPVDLFHKMGEFGLLGVLVPEQYGGAGMGYFEYITALEEISK-VCG 81
Cdd:cd01155    8 ARVKAFMEEHVypaeqeFLEYYAEGGDRWWTPPPIIEKLKAKAKAEGLWNLFLPEVSGLSGLTNLEYAYLAEETGRsFFA 87

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754529347  82 SIGLSMAAHNslcTGH---ILAFGNEEQKAKYL-PLLAtGKWIGAWALTEANTGS-DSGNMKTVARQDGDYWILNGSKNF 156
Cdd:cd01155   88 PEVFNCQAPD---TGNmevLHRYGSEEQKKQWLePLLD-GKIRSAFAMTEPDVASsDATNIECSIERDGDDYVINGRKWW 163

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754529347 157 ITHAKSSN--VVVVLAR-HADSEDK-KFSSAFIIEKGTEGLT-------HGRKENKMGMrasetCELLLDNVRVHKSQLL 225
Cdd:cd01155  164 SSGAGDPRckIAIVMGRtDPDGAPRhRQQSMILVPMDTPGVTiirplsvFGYDDAPHGH-----AEITFDNVRVPASNLI 238

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754529347 226 GNIGDGFKQAMKVLDGGRISIAALSLGIAQGAYEAALQYSKERQQFNQPIGNFQGISFKLVDMATEIEAARLLTYKAADM 305
Cdd:cd01155  239 LGEGRGFEIAQGRLGPGRIHHCMRLIGAAERALELMCQRAVSREAFGKKLAQHGVVAHWIAKSRIEIEQARLLVLKAAHM 318

                        330       340       350       360       370       380       390
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 754529347 306 KMKGQPmtREA----AMAKLYASEVSVRVANEAVQIFGGYGYTKDYPVEKFYRDAKLCTIGEGTSEIQKIVIAK 375
Cdd:cd01155  319 IDTVGN--KAArkeiAMIKVAAPRMALKIIDRAIQVHGAAGVSQDTPLANMYAWARTLRIADGPDEVHLRSIAR 390
PTZ00456 PTZ00456
acyl-CoA dehydrogenase; Provisional
 49-371 1.12e-36

acyl-CoA dehydrogenase; Provisional


Pssm-ID: 185635 [Multi-domain]  Cd Length: 622  Bit Score: 140.39  E-value: 1.12e-36
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754529347  49 GLLGVLVPEQYGGAGMGYFEYITALEEISKVCGSI----GLSMAAHNSLctghiLAFGNEEQKAKYLPLLATGKWIGAWA 124
Cdd:PTZ00456 112 GWTGISEPEEYGGQALPLSVGFITRELMATANWGFsmypGLSIGAANTL-----MAWGSEEQKEQYLTKLVSGEWSGTMC 186

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754529347 125 LTEANTGSDSGNMKTVAR--QDGDYWIlNGSKNFIT---HAKSSNVV-VVLARHADSE-DKKFSSAFIIEK---GTEGLT 194
Cdd:PTZ00456 187 LTEPQCGTDLGQVKTKAEpsADGSYKI-TGTKIFISagdHDLTENIVhIVLARLPNSLpTTKGLSLFLVPRhvvKPDGSL 265

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754529347 195 HGRK-------ENKMGMRASETCELLLDNvrvHKSQLLGNIGDGFKQAMKVLDGGRISIAALSLGIAQGAYEAALQYSKE 267
Cdd:PTZ00456 266 ETAKnvkciglEKKMGIKGSSTCQLSFEN---SVGYLIGEPNAGMKQMFTFMNTARVGTALEGVCHAELAFQNALRYARE 342

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754529347 268 R------------QQFNQPIGNFQGISFKLVDMATEIEAARLLTY---KAADMKMKGQPMTREAAM----------AKLY 322
Cdd:PTZ00456 343 RrsmralsgtkepEKPADRIICHANVRQNILFAKAVAEGGRALLLdvgRLLDIHAAAKDAATREALdheigfytpiAKGC 422

                        330       340       350       360
                 ....*....|....*....|....*....|....*....|....*....
gi 754529347 323 ASEVSVRVANEAVQIFGGYGYTKDYPVEKFYRDAKLCTIGEGTSEIQKI 371
Cdd:PTZ00456 423 LTEWGVEAASRCLQVWGGHGYIKGNGMEQILRDARIGTLYEGTTGIQAL 471
PRK13026 PRK13026
acyl-CoA dehydrogenase; Reviewed
 31-342 3.67e-31

acyl-CoA dehydrogenase; Reviewed


Pssm-ID: 237277 [Multi-domain]  Cd Length: 774  Bit Score: 125.07  E-value: 3.67e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754529347  31 WDEVQE---FPVDLFHKMGEFGLLGVLVPEQYGGAGMGYFEYITALEEISKVCGSIGLSMAAHNSLCTGHILA-FGNEEQ 106
Cdd:PRK13026 100 WDIVQNrkdLPPEVWDYLKKEGFFALIIPKEYGGKGFSAYANSTIVSKIATRSVSAAVTVMVPNSLGPGELLThYGTQEQ 179

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754529347 107 KAKYLPLLATGKWIGAWALTEANTGSDSGNMK---TVARQ--DGDYWI---LNGSKNFITHAKSSNVVVVLARHADSE-- 176
Cdd:PRK13026 180 KDYWLPRLADGTEIPCFALTGPEAGSDAGAIPdtgIVCRGefEGEEVLglrLTWDKRYITLAPVATVLGLAFKLRDPDgl 259

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754529347 177 --DKK---FSSAfIIEKGTEGLTHGRKENKMGMRasetcellLDN-------VRVHKSQLLG---NIGDGFKQAMKVLDG 241
Cdd:PRK13026 260 lgDKKelgITCA-LIPTDHPGVEIGRRHNPLGMA--------FMNgttrgkdVFIPLDWIIGgpdYAGRGWRMLVECLSA 330

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754529347 242 GR-ISIAALSLGIAQGAYEAALQYSKERQQFNQPIGNFQGISFKLVDMAT---EIEAARLLTYKAADMKMKGQPMTreaA 317
Cdd:PRK13026 331 GRgISLPALGTASGHMATRTTGAYAYVRRQFGMPIGQFEGVQEALARIAGntyLLEAARRLTTTGLDLGVKPSVVT---A 407

                        330       340
                 ....*....|....*....|....*
gi 754529347 318 MAKLYASEVSVRVANEAVQIFGGYG 342
Cdd:PRK13026 408 IAKYHMTELARDVVNDAMDIHAGKG 432
fadE PRK09463
acyl-CoA dehydrogenase; Reviewed
 33-342 9.70e-30

acyl-CoA dehydrogenase; Reviewed


Pssm-ID: 236528 [Multi-domain]  Cd Length: 777  Bit Score: 121.08  E-value: 9.70e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754529347  33 EVQEFPVDLFHKMGEFGLLGVLVPEQYGGAGMGYFEYITALEEISKVCGSIGLSMAAHNSLCTGHILA-FGNEEQKAKYL 111
Cdd:PRK09463 106 ELADLPPEVWQFIKEHGFFGMIIPKEYGGLEFSAYAHSRVLQKLASRSGTLAVTVMVPNSLGPGELLLhYGTDEQKDHYL 185

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754529347 112 PLLATGKWIGAWALTEANTGSDSGNMK---TVARQD--GDYWI---LNGSKNFITHAKSSNVVVvLARHA--------DS 175
Cdd:PRK09463 186 PRLARGEEIPCFALTSPEAGSDAGSIPdtgVVCKGEwqGEEVLgmrLTWNKRYITLAPIATVLG-LAFKLydpdgllgDK 264

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754529347 176 EDKKFSSAfIIEKGTEGLTHGRKENKMG-------MRAsetcelllDNVRVHKSQLLG---NIGDGFKQAMKVLDGGR-I 244
Cdd:PRK09463 265 EDLGITCA-LIPTDTPGVEIGRRHFPLNvpfqngpTRG--------KDVFIPLDYIIGgpkMAGQGWRMLMECLSVGRgI 335

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754529347 245 SIAALSLGIAQGAYEAALQYSKERQQFNQPIGNFQGISFKLVDMATE---IEAARLLTYKAADMKMKGQPMTreaAMAKL 321
Cdd:PRK09463 336 SLPSNSTGGAKLAALATGAYARIRRQFKLPIGKFEGIEEPLARIAGNaylMDAARTLTTAAVDLGEKPSVLS---AIAKY 412

                        330       340
                 ....*....|....*....|.
gi 754529347 322 YASEVSVRVANEAVQIFGGYG 342
Cdd:PRK09463 413 HLTERGRQVINDAMDIHGGKG 433
Acyl-CoA_dh_2 pfam08028
Acyl-CoA dehydrogenase, C-terminal domain;
245-367 4.44e-28

Acyl-CoA dehydrogenase, C-terminal domain;


Pssm-ID: 429790 [Multi-domain]  Cd Length: 133  Bit Score: 107.05  E-value: 4.44e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754529347  245 SIAALSLGIAQGAYEAALQYSKERQQ--FNQPIGNFQGISFKLVDMATEIEAARLLTYKAADMKMK----GQPMT----R 314
Cdd:pfam08028   1 GIAAAALGAARAALAEFTERARGRVRayFGVPLAEDPATQLALAEAAARIDAARLLLERAAARIEAaaaaGKPVTpalrA 80

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|...
gi 754529347  315 EAAMAKLYASEVSVRVANEAVQIFGGYGYTKDYPVEKFYRDAKLCTIGEGTSE 367
Cdd:pfam08028  81 EARRAAAFATELAVAAVDALFRAAGGSALFQDSPLQRIWRDIHAAAQHAAVNP 133
DszC cd01163
Dibenzothiophene (DBT) desulfurization enzyme C; DszC is a flavin reductase dependent enzyme, ...
 11-357 8.63e-28

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: 112.42  E-value: 8.63e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754529347  11 LIASMAKDVAEKYiRPNIMKWDEVQEFpvdlfhkmGEFGLLGVLVPEQYGGAGMGYFEYITALEEISKVCGSIGLSMAAH 90
Cdd:cd01163    6 LAARIAEGAAERD-RQRGLPYEEVALL--------RQSGLGTLRVPKEYGGLGASLPDLYEVVRELAAADSNIAQALRAH 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754529347  91 NSLcTGHILAFGNEEQKAKYLPLLATGKWIGAwALTEaNTGSDSGNMKTVARQDGDYWILNGSKNFITHAKSSNVVVVLA 170
Cdd:cd01163   77 FGF-VEALLLAGPEQFRKRWFGRVLNGWIFGN-AVSE-RGSVRPGTFLTATVRDGGGYVLNGKKFYSTGALFSDWVTVSA 153

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754529347 171 rhADSEDKKFSsaFIIEKGTEGLTHGRKENKMGMRASETCELLLDNVRVHKSQLLGnIGDGFKQAMKVLDGGRISIAALS 250
Cdd:cd01163  154 --LDEEGKLVF--AAVPTDRPGITVVDDWDGFGQRLTASGTVTFDNVRVEPDEVLP-RPNAPDRGTLLTAIYQLVLAAVL 228

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754529347 251 LGIAQGAYEAALQYSKERQ---------------QFNQPIGnfqgisfklvDMATEIEAARLLTYKAAD----MKMKGQP 311
Cdd:cd01163  229 AGIARAALDDAVAYVRSRTrpwihsgaesarddpYVQQVVG----------DLAARLHAAEALVLQAARaldaAAAAGTA 298

                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|....
gi 754529347 312 MTREA--------AMAKLYASEVSVRVANEAVQIFGGYGYTKDYPVEKFYRDAK 357
Cdd:cd01163  299 LTAEArgeaalavAAAKVVVTRLALDATSRLFEVGGASATAREHNLDRHWRNAR 352
Acyl-CoA_dh_M pfam02770
Acyl-CoA dehydrogenase, middle domain; Central domain of Acyl-CoA dehydrogenase has a ...
 122-215 3.76e-25

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: 97.74  E-value: 3.76e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754529347  122 AWALTEANTGSDSGNMKTVA-RQDGDYWILNGSKNFITHAKSSNVVVVLARHADSEDKKFSSAFIIEKGTEGLTHGRKEN 200
Cdd:pfam02770   1 AFALTEPGAGSDVASLKTTAaDGDGGGWVLNGTKWWITNAGIADLFLVLARTGGDDRHGGISLFLVPKDAPGVSVRRIET 80

                          90
                  ....*....|....*
gi 754529347  201 KMGMRASETCELLLD 215
Cdd:pfam02770  81 KLGVRGLPTGELVFD 95
PLN02876 PLN02876
acyl-CoA dehydrogenase
 57-379 9.40e-20

acyl-CoA dehydrogenase


Pssm-ID: 215473 [Multi-domain]  Cd Length: 822  Bit Score: 91.01  E-value: 9.40e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754529347  57 EQYGGAGMGYFEYitaleeiSKVCGSIGLSMAAHNSL-C----TGH---ILAFGNEEQKAKYLPLLATGKWIGAWALTEA 128
Cdd:PLN02876 487 DQLLGAGLSNLEY-------GYLCEIMGRSVWAPQVFnCgapdTGNmevLLRYGNKEQQLEWLIPLLEGKIRSGFAMTEP 559

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754529347 129 NTGS-DSGNMKTVARQDGDYWILNGSKNFITHAKSS--NVVVVLARHADSEDK-KFSSAFIIEKGTEGLTHGRKENKMGM 204
Cdd:PLN02876 560 QVASsDATNIECSIRRQGDSYVINGTKWWTSGAMDPrcRVLIVMGKTDFNAPKhKQQSMILVDIQTPGVQIKRPLLVFGF 639

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754529347 205 RASET--CELLLDNVRVHKSQLLGNIGDGFKQAMKVLDGGRISIAALSLGIAQGAYEAALQYSKERQQFNQPIGNfQGiS 282
Cdd:PLN02876 640 DDAPHghAEISFENVRVPAKNILLGEGRGFEIAQGRLGPGRLHHCMRLIGAAERGMQLMVQRALSRKAFGKLIAQ-HG-S 717

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754529347 283 FkLVDMA---TEIEAARLLTYKAAD-MKMKGQPMTREA-AMAKLYASEVSVRVANEAVQIFGGYGYTKDYPVEKFYRDAK 357
Cdd:PLN02876 718 F-LSDLAkcrVELEQTRLLVLEAADqLDRLGNKKARGIiAMAKVAAPNMALKVLDMAMQVHGAAGVSSDTVLAHLWATAR 796

                        330       340
                 ....*....|....*....|...
gi 754529347 358 LCTIGEGTSEIQKIVIAK-SLQK 379
Cdd:PLN02876 797 TLRIADGPDEVHLGTIAKlELQR 819
NcnH cd01159
Naphthocyclinone hydroxylase; Naphthocyclinone is an aromatic polyketide and an antibiotic, ...
 16-356 1.11e-14

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: 74.69  E-value: 1.11e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754529347  16 AKDVAEKyIRPNIMKWDEVQEFPVDLFHKMGEFGLLGVLVPEQYGGAGMGYFEYITALEEISKVCGSIG---LSMAAHNs 92
Cdd:cd01159    3 AEDLAPL-IRERAPEAERARRLPDEVVRALREIGFFRMFVPKRYGGLEGDFAEFAEAIATLAEACGSAAwvaSIVATHS- 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754529347  93 lctgHILA-FGNEEQKAkylpLLATGkwigawalTEANTGSDSGNMKTVARQDGDYwILNGSKNFITHAKSSNVVVVLAR 171
Cdd:cd01159   81 ----RMLAaFPPEAQEE----VWGDG--------PDTLLAGSYAPGGRAERVDGGY-RVSGTWPFASGCDHADWILVGAI 143

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754529347 172 HADSEDKKFSSAFIIEKgtEGLTHGRKENKMGMRASETCELLLDNVRV--HKSQLLGNIGDGFKqAMKVLDGGRI----- 244
Cdd:cd01159  144 VEDDDGGPLPRAFVVPR--AEYEIVDTWHVVGLRGTGSNTVVVDDVFVpeHRTLTAGDMMAGDG-PGGSTPVYRMplrqv 220

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754529347 245 ---SIAALSLGIAQGAYEAALQYSKERQQ---FNQPIGNFQGISFKLVDMATEIEAARLLTYKAADMKMKGQ-------P 311
Cdd:cd01159  221 fplSFAAVSLGAAEGALAEFLELAGKRVRqygAAVKMAEAPITQLRLAEAAAELDAARAFLERATRDLWAHAlaggpidV 300

                        330       340       350       360
                 ....*....|....*....|....*....|....*....|....*.
gi 754529347 312 MTR-EAAMAKLYASEVSVRVANEAVQIFGGYGYTKDYPVEKFYRDA 356
Cdd:cd01159  301 EERaRIRRDAAYAAKLSAEAVDRLFHAAGGSALYTASPLQRIWRDI 346
AXO cd01150
Peroxisomal acyl-CoA oxidase; Peroxisomal acyl-CoA oxidases (AXO) catalyze the first set in ...
 82-271 2.78e-12

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: 68.12  E-value: 2.78e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754529347  82 SIGLSMAAHNSLCTGHILAFGNEEQKAKYLPLLATGKWIGAWALTEANTGSDSGNMKTVARQDgdywilNGSKNFITH-- 159
Cdd:cd01150   97 SLGAKLGLHLGLFGNAIKNLGTDEHQDYWLQGANNLEIIGCFAQTELGHGSNLQGLETTATYD------PLTQEFVINtp 170

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754529347 160 ------------AKSSNVVVVLAR-HADSEDKKFsSAFII---EKGTE----GLTHGRKENKMGMRASETCELLLDNVRV 219
Cdd:cd01150  171 dftatkwwpgnlGKTATHAVVFAQlITPGKNHGL-HAFIVpirDPKTHqplpGVTVGDIGPKMGLNGVDNGFLQFRNVRI 249

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 754529347 220 HKSQLLGNIGD----------------GFKQAMKVLDGGRISIAALSLGIAQGAYEAALQYSKERQQF 271
Cdd:cd01150  250 PRENLLNRFGDvspdgtyvspfkdpnkRYGAMLGTRSGGRVGLIYDAAMSLKKAATIAIRYSAVRRQF 317
PTZ00457 PTZ00457
acyl-CoA dehydrogenase; Provisional
 50-253 1.11e-11

acyl-CoA dehydrogenase; Provisional


Pssm-ID: 185636 [Multi-domain]  Cd Length: 520  Bit Score: 66.06  E-value: 1.11e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754529347  50 LLGVLVPEQYGGAGMGYFEYITALEEISKVCGSIGLSMAAHNSLCTGHILAFGNEEQKAKYLPLLATGKWIGAWALTEAN 129
Cdd:PTZ00457  65 LYGARIATEYGGLGLGHTAHALIYEEVGTNCDSKLLSTIQHSGFCTYLLSTVGSKELKGKYLTAMSDGTIMMGWATEEGC 144

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754529347 130 tGSDSG--NMKTVARQDGDYwILNGSKNFITHAKSSNVVVV------LARHADSEDKKFSSAFIIEKGTEGLThgrkenk 201
Cdd:PTZ00457 145 -GSDISmnTTKASLTDDGSY-VLTGQKRCEFAASATHFLVLaktltqTAAEEGATEVSRNSFFICAKDAKGVS------- 215

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|..
gi 754529347 202 mgmraSETCELLLDNVRVhkSQLLGNIGDGFKQAMKVLDGGRISIAALSLGI 253
Cdd:PTZ00457 216 -----VNGDSVVFENTPA--ADVVGVVGEGFKDAMITLFTEQYLYAASLLGI 260
PLN02636 PLN02636
acyl-coenzyme A oxidase
 69-343 7.33e-11

acyl-coenzyme A oxidase


Pssm-ID: 215342 [Multi-domain]  Cd Length: 686  Bit Score: 63.72  E-value: 7.33e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754529347  69 YITALEEISKVCGSIGLSMAAHNSLCTGHILAFGNEEQKAKYLPLLATGKWIGAWALTEANTGSDSGNMKTVARQD--GD 146
Cdd:PLN02636 123 YFAITEAVGSVDMSLGIKLGVQYSLWGGSVINLGTKKHRDKYFDGIDNLDYPGCFAMTELHHGSNVQGLQTTATFDplTD 202

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754529347 147 YWILNGSK---------NFITHAKSSNVVVVLArhADSEDKKFSS-----AFIIE----------KGTEGLTHGrkeNKM 202
Cdd:PLN02636 203 EFVINTPNdgaikwwigNAAVHGKFATVFARLK--LPTHDSKGVSdmgvhAFIVPirdmkthqvlPGVEIRDCG---HKV 277

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754529347 203 GMRASETCELLLDNVRVHKSQLLGNIGD----------------GFKQAMKVLDGGRISIAALSLGIAQGAYEAALQYSK 266
Cdd:PLN02636 278 GLNGVDNGALRFRSVRIPRDNLLNRFGDvsrdgkytsslptinkRFAATLGELVGGRVGLAYGSVGVLKASNTIAIRYSL 357

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754529347 267 ERQQF---NQP---IGNFQGISFKLVDMATEIE----AARLLTYKAADMKMK------GQPMTREAAMaKLYASEVSVRV 330
Cdd:PLN02636 358 LRQQFgppKQPeisILDYQSQQHKLMPMLASTYafhfATEYLVERYSEMKKThddqlvADVHALSAGL-KAYITSYTAKA 436

                        330
                 ....*....|...
gi 754529347 331 ANEAVQIFGGYGY 343
Cdd:PLN02636 437 LSTCREACGGHGY 449
PRK11561 PRK11561
isovaleryl CoA dehydrogenase; Provisional
 125-379 1.28e-09

isovaleryl CoA dehydrogenase; Provisional


Pssm-ID: 183199 [Multi-domain]  Cd Length: 538  Bit Score: 59.77  E-value: 1.28e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754529347 125 LTEANTGSDS-GNMKTVARQDGDYWILNGSKNFIThAKSSNVVVVLARHADSEDKKFSSAFIIEKGTEGLTHGRKENKMG 203
Cdd:PRK11561 184 MTEKQGGSDVlSNTTRAERLADGSYRLVGHKWFFS-VPQSDAHLVLAQAKGGLSCFFVPRFLPDGQRNAIRLERLKDKLG 262

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754529347 204 MRASETCELLLDNVrvhKSQLLGNIGDGFKQAMKVldGG--RISIAALSLGIAQGAYEAALQYSKERQQFNQPIGNFQGI 281
Cdd:PRK11561 263 NRSNASSEVEFQDA---IGWLLGEEGEGIRLILKM--GGmtRFDCALGSHGLMRRAFSVAIYHAHQRQVFGKPLIEQPLM 337

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754529347 282 SFKLVDMATEIEAARLLTYKAADM-KMKGQPmtREAAMAKLYASEVSVRVAN-------EAVQIFGGYGYTKDYPVEKFY 353
Cdd:PRK11561 338 RQVLSRMALQLEGQTALLFRLARAwDRRADA--KEALWARLFTPAAKFVICKrgipfvaEAMEVLGGIGYCEESELPRLY 415

                        250       260
                 ....*....|....*....|....*.
gi 754529347 354 RDAKLCTIGEGTSEIQKIVIAKSLQK 379
Cdd:PRK11561 416 REMPVNSIWEGSGNIMCLDVLRVLNK 441
PLN02443 PLN02443
acyl-coenzyme A oxidase
 102-225 2.47e-03

acyl-coenzyme A oxidase


Pssm-ID: 178062 [Multi-domain]  Cd Length: 664  Bit Score: 39.82  E-value: 2.47e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754529347 102 GNEEQKAKYLPLLATGKWIGAWALTEANTGSDSGNMKTVARQDGDywilngSKNFITHA--------------KSSNVVV 167
Cdd:PLN02443 114 GTEEQQKKWLPLAYKMQIIGCYAQTELGHGSNVQGLETTATFDPK------TDEFVIHSptltsskwwpgglgKVSTHAV 187

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 754529347 168 VLARHADSEDKKFSSAFIIE-------KGTEGLTHGRKENKMGMRASETCE---LLLDNVRVHKSQLL 225
Cdd:PLN02443 188 VYARLITNGKDHGIHGFIVQlrslddhSPLPGVTVGDIGMKFGNGAYNTMDngfLRFDHVRIPRDQML 255
 
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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