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Conserved domains on  [gi|446467688|ref|WP_000545542|]
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MULTISPECIES: acyl-CoA dehydrogenase AcdA [Bacillus]

Protein Classification

acyl-CoA dehydrogenase( domain architecture ID 10100181)

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

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
SCAD_SBCAD cd01158
Short chain acyl-CoA dehydrogenases and eukaryotic short/branched chain acyl-CoA ...
 7-379 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: 655.88  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446467688   7 EEHEMIRKMVRDFAKNEVAPTAAERDEEERFDRELFDQMAELGLTGIPWPEEYGGIGSDYLAYVIAIEELSRVCASTGVT 86
Cdd:cd01158    1 EEHQMIRKTVRDFAEKEIAPLAAEMDEKGEFPREVIKEMAELGLMGIPIPEEYGGAGLDFLAYAIAIEELAKVDASVAVI 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446467688  87 LSAHTSLAGWPIFKFGTEEQKQKFLRPMAEGKKIGAYGLTEPGSGSDAGGMKTIAKRDGDHYILNGSKIFITNGGIADIY 166
Cdd:cd01158   81 VSVHNSLGANPIIKFGTEEQKKKYLPPLATGEKIGAFALSEPGAGSDAAALKTTAKKDGDDYVLNGSKMWITNGGEADFY 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446467688 167 VVFALTDPESKQRGTSAFIVESDTPGFSVGKKESKLGIRSSPTTEIMFEDCRIPVENLLGEEGQGFKVAMQTLDGGRNGI 246
Cdd:cd01158  161 IVFAVTDPSKGYRGITAFIVERDTPGLSVGKKEDKLGIRGSSTTELIFEDVRVPKENILGEEGEGFKIAMQTLDGGRIGI 240

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446467688 247 AAQAVGIAQGALDASVEYARERHQFGKPIAAQQGIGFKLADMATDVEAARLLTYQAAWLESEGLPYGKESAMSKVFAGDA 326
Cdd:cd01158  241 AAQALGIAQAALDAAVDYAKERKQFGKPIADFQGIQFKLADMATEIEAARLLTYKAARLKDNGEPFIKEAAMAKLFASEV 320

                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|...
gi 446467688 327 AMKVTTEAVQVFGGYGYTKDYPVERYMRDAKITQIYEGTQEIQRLVISRMLTK 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: 655.88  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446467688   7 EEHEMIRKMVRDFAKNEVAPTAAERDEEERFDRELFDQMAELGLTGIPWPEEYGGIGSDYLAYVIAIEELSRVCASTGVT 86
Cdd:cd01158    1 EEHQMIRKTVRDFAEKEIAPLAAEMDEKGEFPREVIKEMAELGLMGIPIPEEYGGAGLDFLAYAIAIEELAKVDASVAVI 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446467688  87 LSAHTSLAGWPIFKFGTEEQKQKFLRPMAEGKKIGAYGLTEPGSGSDAGGMKTIAKRDGDHYILNGSKIFITNGGIADIY 166
Cdd:cd01158   81 VSVHNSLGANPIIKFGTEEQKKKYLPPLATGEKIGAFALSEPGAGSDAAALKTTAKKDGDDYVLNGSKMWITNGGEADFY 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446467688 167 VVFALTDPESKQRGTSAFIVESDTPGFSVGKKESKLGIRSSPTTEIMFEDCRIPVENLLGEEGQGFKVAMQTLDGGRNGI 246
Cdd:cd01158  161 IVFAVTDPSKGYRGITAFIVERDTPGLSVGKKEDKLGIRGSSTTELIFEDVRVPKENILGEEGEGFKIAMQTLDGGRIGI 240

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446467688 247 AAQAVGIAQGALDASVEYARERHQFGKPIAAQQGIGFKLADMATDVEAARLLTYQAAWLESEGLPYGKESAMSKVFAGDA 326
Cdd:cd01158  241 AAQALGIAQAALDAAVDYAKERKQFGKPIADFQGIQFKLADMATEIEAARLLTYKAARLKDNGEPFIKEAAMAKLFASEV 320

                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|...
gi 446467688 327 AMKVTTEAVQVFGGYGYTKDYPVERYMRDAKITQIYEGTQEIQRLVISRMLTK 379
Cdd:cd01158  321 AMRVTTDAVQIFGGYGYTKDYPVERYYRDAKITEIYEGTSEIQRLVIAKHLLK 373
CaiA COG1960
Acyl-CoA dehydrogenase related to the alkylation response protein AidB [Lipid transport and ...
 1-379 0e+00

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: 563.31  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446467688   1 MHFKLSEEHEMIRKMVRDFAKNEVAPTAAERDEEERFDRELFDQMAELGLTGIPWPEEYGGIGSDYLAYVIAIEELSRVC 80
Cdd:COG1960    1 MDFELTEEQRALRDEVREFAEEEIAPEAREWDREGEFPRELWRKLAELGLLGLTIPEEYGGLGLSLVELALVLEELARAD 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446467688  81 ASTGVTLSAHTSlAGWPIFKFGTEEQKQKFLRPMAEGKKIGAYGLTEPGSGSDAGGMKTIAKRDGDHYILNGSKIFITNG 160
Cdd:COG1960   81 ASLALPVGVHNG-AAEALLRFGTEEQKERYLPRLASGEWIGAFALTEPGAGSDAAALRTTAVRDGDGYVLNGQKTFITNA 159

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446467688 161 GIADIYVVFALTDPESKQRGTSAFIVESDTPGFSVGKKESKLGIRSSPTTEIMFEDCRIPVENLLGEEGQGFKVAMQTLD 240
Cdd:COG1960  160 PVADVILVLARTDPAAGHRGISLFLVPKDTPGVTVGRIEDKMGLRGSDTGELFFDDVRVPAENLLGEEGKGFKIAMSTLN 239

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446467688 241 GGRNGIAAQAVGIAQGALDASVEYARERHQFGKPIAAQQGIGFKLADMATDVEAARLLTYQAAWLESEGLPYGKESAMSK 320
Cdd:COG1960  240 AGRLGLAAQALGIAEAALELAVAYAREREQFGRPIADFQAVQHRLADMAAELEAARALVYRAAWLLDAGEDAALEAAMAK 319

                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 446467688 321 VFAGDAAMKVTTEAVQVFGGYGYTKDYPVERYMRDAKITQIYEGTQEIQRLVISRMLTK 379
Cdd:COG1960  320 LFATEAALEVADEALQIHGGYGYTREYPLERLYRDARILTIYEGTNEIQRLIIARRLLG 378
PLN02519 PLN02519
isovaleryl-CoA dehydrogenase
 5-379 1.01e-104

isovaleryl-CoA dehydrogenase


Pssm-ID: 215284 [Multi-domain]  Cd Length: 404  Bit Score: 314.12  E-value: 1.01e-104
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446467688   5 LSEEHEMIRKMVRDFAKNEVAPTAAERDEEERF--DRELFDQMAELGLTGIPWPEEYGGIGSDYLAYVIAIEELSRVCAS 82
Cdd:PLN02519  26 FDDTQLQFKESVQQFAQENIAPHAAAIDATNSFpkDVNLWKLMGDFNLHGITAPEEYGGLGLGYLYHCIAMEEISRASGS 105

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446467688  83 TGVTLSAHTSLAGWPIFKFGTEEQKQKFLRPMAEGKKIGAYGLTEPGSGSDAGGMKTIAKRDGDHYILNGSKIFITNGGI 162
Cdd:PLN02519 106 VGLSYGAHSNLCINQLVRNGTPAQKEKYLPKLISGEHVGALAMSEPNSGSDVVSMKCKAERVDGGYVLNGNKMWCTNGPV 185

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446467688 163 ADIYVVFALTDPESKQRGTSAFIVESDTPGFSVGKKESKLGIRSSPTTEIMFEDCRIPVENLLGEEGQGFKVAMQTLDGG 242
Cdd:PLN02519 186 AQTLVVYAKTDVAAGSKGITAFIIEKGMPGFSTAQKLDKLGMRGSDTCELVFENCFVPEENVLGQEGKGVYVMMSGLDLE 265

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446467688 243 RNGIAAQAVGIAQGALDASVEYARERHQFGKPIAAQQGIGFKLADMATDVEAARLLTYQAAWLESEGLPYGKESAMSKVF 322
Cdd:PLN02519 266 RLVLAAGPLGLMQACLDVVLPYVRQREQFGRPIGEFQFIQGKLADMYTSLQSSRSYVYSVARDCDNGKVDRKDCAGVILC 345

                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 446467688 323 AGDAAMKVTTEAVQVFGGYGYTKDYPVERYMRDAKITQIYEGTQEIQRLVISRMLTK 379
Cdd:PLN02519 346 AAERATQVALQAIQCLGGNGYINEYPTGRLLRDAKLYEIGAGTSEIRRMLIGRELFK 402
Acyl-CoA_dh_1 pfam00441
Acyl-CoA dehydrogenase, C-terminal domain; C-terminal domain of Acyl-CoA dehydrogenase is an ...
 229-375 2.95e-61

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: 194.01  E-value: 2.95e-61
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446467688  229 GQGFKVAMQTLDGGRNGIAAQAVGIAQGALDASVEYARERHQFGKPIAAQQGIGFKLADMATDVEAARLLTYQAAWLESE 308
Cdd:pfam00441   1 GRGFRVAMETLNHERLAIAAMALGLARRALDEALAYARRRKAFGRPLIDFQLVRHKLAEMAAEIEAARLLVYRAAEALDA 80

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 446467688  309 GLPYGKESAMSKVFAGDAAMKVTTEAVQVFGGYGYTKDYPVERYMRDAKITQIYEGTQEIQRLVISR 375
Cdd:pfam00441  81 GGPDGAEASMAKLYASEAAVEVADLAMQLHGGYGYLREYPVERLYRDARVLRIGEGTSEIQRNIIAR 147
 
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: 655.88  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446467688   7 EEHEMIRKMVRDFAKNEVAPTAAERDEEERFDRELFDQMAELGLTGIPWPEEYGGIGSDYLAYVIAIEELSRVCASTGVT 86
Cdd:cd01158    1 EEHQMIRKTVRDFAEKEIAPLAAEMDEKGEFPREVIKEMAELGLMGIPIPEEYGGAGLDFLAYAIAIEELAKVDASVAVI 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446467688  87 LSAHTSLAGWPIFKFGTEEQKQKFLRPMAEGKKIGAYGLTEPGSGSDAGGMKTIAKRDGDHYILNGSKIFITNGGIADIY 166
Cdd:cd01158   81 VSVHNSLGANPIIKFGTEEQKKKYLPPLATGEKIGAFALSEPGAGSDAAALKTTAKKDGDDYVLNGSKMWITNGGEADFY 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446467688 167 VVFALTDPESKQRGTSAFIVESDTPGFSVGKKESKLGIRSSPTTEIMFEDCRIPVENLLGEEGQGFKVAMQTLDGGRNGI 246
Cdd:cd01158  161 IVFAVTDPSKGYRGITAFIVERDTPGLSVGKKEDKLGIRGSSTTELIFEDVRVPKENILGEEGEGFKIAMQTLDGGRIGI 240

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446467688 247 AAQAVGIAQGALDASVEYARERHQFGKPIAAQQGIGFKLADMATDVEAARLLTYQAAWLESEGLPYGKESAMSKVFAGDA 326
Cdd:cd01158  241 AAQALGIAQAALDAAVDYAKERKQFGKPIADFQGIQFKLADMATEIEAARLLTYKAARLKDNGEPFIKEAAMAKLFASEV 320

                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|...
gi 446467688 327 AMKVTTEAVQVFGGYGYTKDYPVERYMRDAKITQIYEGTQEIQRLVISRMLTK 379
Cdd:cd01158  321 AMRVTTDAVQIFGGYGYTKDYPVERYYRDAKITEIYEGTSEIQRLVIAKHLLK 373
CaiA COG1960
Acyl-CoA dehydrogenase related to the alkylation response protein AidB [Lipid transport and ...
 1-379 0e+00

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: 563.31  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446467688   1 MHFKLSEEHEMIRKMVRDFAKNEVAPTAAERDEEERFDRELFDQMAELGLTGIPWPEEYGGIGSDYLAYVIAIEELSRVC 80
Cdd:COG1960    1 MDFELTEEQRALRDEVREFAEEEIAPEAREWDREGEFPRELWRKLAELGLLGLTIPEEYGGLGLSLVELALVLEELARAD 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446467688  81 ASTGVTLSAHTSlAGWPIFKFGTEEQKQKFLRPMAEGKKIGAYGLTEPGSGSDAGGMKTIAKRDGDHYILNGSKIFITNG 160
Cdd:COG1960   81 ASLALPVGVHNG-AAEALLRFGTEEQKERYLPRLASGEWIGAFALTEPGAGSDAAALRTTAVRDGDGYVLNGQKTFITNA 159

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446467688 161 GIADIYVVFALTDPESKQRGTSAFIVESDTPGFSVGKKESKLGIRSSPTTEIMFEDCRIPVENLLGEEGQGFKVAMQTLD 240
Cdd:COG1960  160 PVADVILVLARTDPAAGHRGISLFLVPKDTPGVTVGRIEDKMGLRGSDTGELFFDDVRVPAENLLGEEGKGFKIAMSTLN 239

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446467688 241 GGRNGIAAQAVGIAQGALDASVEYARERHQFGKPIAAQQGIGFKLADMATDVEAARLLTYQAAWLESEGLPYGKESAMSK 320
Cdd:COG1960  240 AGRLGLAAQALGIAEAALELAVAYAREREQFGRPIADFQAVQHRLADMAAELEAARALVYRAAWLLDAGEDAALEAAMAK 319

                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 446467688 321 VFAGDAAMKVTTEAVQVFGGYGYTKDYPVERYMRDAKITQIYEGTQEIQRLVISRMLTK 379
Cdd:COG1960  320 LFATEAALEVADEALQIHGGYGYTREYPLERLYRDARILTIYEGTNEIQRLIIARRLLG 378
IVD cd01156
Isovaleryl-CoA dehydrogenase; Isovaleryl-CoA dehydrogenase (IVD) is an is an acyl-CoA ...
 5-379 3.46e-145

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: 416.43  E-value: 3.46e-145
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446467688   5 LSEEHEMIRKMVRDFAKNEVAPTAAERDEEERFDRELFDQMAELGLTGIPWPEEYGGIGSDYLAYVIAIEELSRVCASTG 84
Cdd:cd01156    2 LDDEIEMLRQSVREFAQKEIAPLAAKIDRDNEFPRDLWRKMGKLGLLGITAPEEYGGSGMGYLAHVIIMEEISRASGSVA 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446467688  85 VTLSAHTSLAGWPIFKFGTEEQKQKFLRPMAEGKKIGAYGLTEPGSGSDAGGMKTIAKRDGDHYILNGSKIFITNGGIAD 164
Cdd:cd01156   82 LSYGAHSNLCINQIYRNGSAAQKEKYLPKLISGEHIGALAMSEPNAGSDVVSMKLRAEKKGDRYVLNGSKMWITNGPDAD 161

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446467688 165 IYVVFALTDPESKQRGTSAFIVESDTPGFSVGKKESKLGIRSSPTTEIMFEDCRIPVENLLGEEGQGFKVAMQTLDGGRN 244
Cdd:cd01156  162 TLVVYAKTDPSAGAHGITAFIVEKGMPGFSRAQKLDKLGMRGSNTCELVFEDCEVPEENILGGENKGVYVLMSGLDYERL 241

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446467688 245 GIAAQAVGIAQGALDASVEYARERHQFGKPIAAQQGIGFKLADMATDVEAARLLTYQAAWLESEGLPYGKESAMSKVFAG 324
Cdd:cd01156  242 VLAGGPIGIMQAALDVAIPYAHQRKQFGQPIGEFQLVQGKLADMYTRLNASRSYLYTVAKACDRGNMDPKDAAGVILYAA 321

                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 446467688 325 DAAMKVTTEAVQVFGGYGYTKDYPVERYMRDAKITQIYEGTQEIQRLVISRMLTK 379
Cdd:cd01156  322 EKATQVALDAIQILGGNGYINDYPTGRLLRDAKLYEIGAGTSEIRRMVIGRELFK 376
ACAD cd00567
Acyl-CoA dehydrogenase; Both mitochondrial acyl-CoA dehydrogenases (ACAD) and peroxisomal ...
 7-375 1.39e-143

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: 410.14  E-value: 1.39e-143
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446467688   7 EEHEMIRKMVRDFAKNEVAPTAAERDEEERFDRELFDQMAELGltgipwpeeyggigsdylayviaieelsrvcastgvt 86
Cdd:cd00567    1 EEQRELRDSAREFAAEELEPYARERRETPEEPWELLAELGLLL------------------------------------- 43

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446467688  87 lsahtslAGWPIFKFGTEEQKQKFLRPMAEGKKIGAYGLTEPGSGSDAGGMKTIAKRDGDHYILNGSKIFITNGGIADIY 166
Cdd:cd00567   44 -------GAALLLAYGTEEQKERYLPPLASGEAIAAFALTEPGAGSDLAGIRTTARKDGDGYVLNGRKIFISNGGDADLF 116

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446467688 167 VVFALTDPESKQ-RGTSAFIVESDTPGFSVGKKESKLGIRSSPTTEIMFEDCRIPVENLLGEEGQGFKVAMQTLDGGRNG 245
Cdd:cd00567  117 IVLARTDEEGPGhRGISAFLVPADTPGVTVGRIWDKMGMRGSGTGELVFDDVRVPEDNLLGEEGGGFELAMKGLNVGRLL 196

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446467688 246 IAAQAVGIAQGALDASVEYARERHQFGKPIAAQQGIGFKLADMATDVEAARLLTYQAAWLESEGLP-YGKESAMSKVFAG 324
Cdd:cd00567  197 LAAVALGAARAALDEAVEYAKQRKQFGKPLAEFQAVQFKLADMAAELEAARLLLYRAAWLLDQGPDeARLEAAMAKLFAT 276

                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|.
gi 446467688 325 DAAMKVTTEAVQVFGGYGYTKDYPVERYMRDAKITQIYEGTQEIQRLVISR 375
Cdd:cd00567  277 EAAREVADLAMQIHGGRGYSREYPVERYLRDARAARIAEGTAEIQRLIIAR 327
IBD cd01162
Isobutyryl-CoA dehydrogenase; Isobutyryl-CoA dehydrogenase (IBD) catalyzes the alpha, beta- ...
 5-377 5.65e-143

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: 410.68  E-value: 5.65e-143
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446467688   5 LSEEHEMIRKMVRDFAKNEVAPTAAERDEEERFDRELFDQMAELGLTGIPWPEEYGGIGSDYLAYVIAIEELSRVCASTG 84
Cdd:cd01162    1 LNEEQRAIQEVARAFAAKEMAPHAADWDQKKHFPVDVLRKAAELGFGGIYIRDDVGGSGLSRLDASIIFEALSTGCVSTA 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446467688  85 VTLSAHtSLAGWPIFKFGTEEQKQKFLRPMAEGKKIGAYGLTEPGSGSDAGGMKTIAKRDGDHYILNGSKIFITNGGIAD 164
Cdd:cd01162   81 AYISIH-NMCAWMIDSFGNDEQRERFLPDLCTMEKLASYCLTEPGSGSDAAALRTRAVREGDHYVLNGSKAFISGAGDSD 159

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446467688 165 IYVVFALTDpESKQRGTSAFIVESDTPGFSVGKKESKLGIRSSPTTEIMFEDCRIPVENLLGEEGQGFKVAMQTLDGGRN 244
Cdd:cd01162  160 VYVVMARTG-GEGPKGISCFVVEKGTPGLSFGANEKKMGWNAQPTRAVIFEDCRVPVENRLGGEGQGFGIAMAGLNGGRL 238

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446467688 245 GIAAQAVGIAQGALDASVEYARERHQFGKPIAAQQGIGFKLADMATDVEAARLLTYQAA-WLESEGLPYGKESAMSKVFA 323
Cdd:cd01162  239 NIASCSLGAAQAALDLARAYLEERKQFGKPLADFQALQFKLADMATELVASRLMVRRAAsALDRGDPDAVKLCAMAKRFA 318

                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|....
gi 446467688 324 GDAAMKVTTEAVQVFGGYGYTKDYPVERYMRDAKITQIYEGTQEIQRLVISRML 377
Cdd:cd01162  319 TDECFDVANQALQLHGGYGYLKDYPVEQYVRDLRVHQILEGTNEIMRLIIARAL 372
LCAD cd01160
Long chain acyl-CoA dehydrogenase; LCAD is an acyl-CoA dehydrogenases (ACAD), which is found ...
 7-377 7.44e-132

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: 382.23  E-value: 7.44e-132
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446467688   7 EEHEMIRKMVRDFAKNEVAPTAAERDEEERFDRELFDQMAELGLTGIPWPEEYGGIGSDYLAYVIAIEELSRVCAStGVT 86
Cdd:cd01160    1 EEHDAFRDVVRRFFAKEVAPFHHEWEKAGEVPREVWRKAGEQGLLGVGFPEEYGGIGGDLLSAAVLWEELARAGGS-GPG 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446467688  87 LSAHTSLAGWPIFKFGTEEQKQKFLRPMAEGKKIGAYGLTEPGSGSDAGGMKTIAKRDGDHYILNGSKIFITNGGIADIY 166
Cdd:cd01160   80 LSLHTDIVSPYITRAGSPEQKERVLPQMVAGKKIGAIAMTEPGAGSDLQGIRTTARKDGDHYVLNGSKTFITNGMLADVV 159

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446467688 167 VVFALTDPE-SKQRGTSAFIVESDTPGFSVGKKESKLGIRSSPTTEIMFEDCRIPVENLLGEEGQGFKVAMQTLDGGRNG 245
Cdd:cd01160  160 IVVARTGGEaRGAGGISLFLVERGTPGFSRGRKLKKMGWKAQDTAELFFDDCRVPAENLLGEENKGFYYLMQNLPQERLL 239

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446467688 246 IAAQAVGIAQGALDASVEYARERHQFGKPIAAQQGIGFKLADMATDVEAARLLTYQAAWLESEGLPYGKESAMSKVFAGD 325
Cdd:cd01160  240 IAAGALAAAEFMLEETRNYVKQRKAFGKTLAQLQVVRHKIAELATKVAVTRAFLDNCAWRHEQGRLDVAEASMAKYWATE 319

                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|..
gi 446467688 326 AAMKVTTEAVQVFGGYGYTKDYPVERYMRDAKITQIYEGTQEIQRLVISRML 377
Cdd:cd01160  320 LQNRVAYECVQLHGGWGYMREYPIARAYRDARVQPIYGGTTEIMKELISRQM 371
VLCAD cd01161
Very long chain acyl-CoA dehydrogenase; VLCAD is an acyl-CoA dehydrogenase (ACAD), which is ...
 1-374 3.16e-123

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: 361.79  E-value: 3.16e-123
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446467688   1 MHFKLSEEHEMIRKMVRDFAKNEVAPtaAERDEEERFDRELFDQMAELGLTGIPWPEEYGGIGSDYLAYVIAIEELSRVc 80
Cdd:cd01161   23 LTEEQTEELNMLVGPVEKFFEEVNDP--AKNDQLEKIPRKTLTQLKELGLFGLQVPEEYGGLGLNNTQYARLAEIVGMD- 99

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446467688  81 ASTGVTLSAHTSLAGWPIFKFGTEEQKQKFLRPMAEGKKIGAYGLTEPGSGSDAGGMKTIAKR--DGDHYILNGSKIFIT 158
Cdd:cd01161  100 LGFSVTLGAHQSIGFKGILLFGTEAQKEKYLPKLASGEWIAAFALTEPSSGSDAASIRTTAVLseDGKHYVLNGSKIWIT 179

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446467688 159 NGGIADIYVVFALTDPE----SKQRGTSAFIVESDTPGFSVGKKESKLGIRSSPTTEIMFEDCRIPVENLLGEEGQGFKV 234
Cdd:cd01161  180 NGGIADIFTVFAKTEVKdatgSVKDKITAFIVERSFGGVTNGPPEKKMGIKGSNTAEVYFEDVKIPVENVLGEVGDGFKV 259

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446467688 235 AMQTLDGGRNGIAAQAVGIAQGALDASVEYARERHQFGKPIAAQQGIGFKLADMATDVEAARLLTYQAAWLESEGL--PY 312
Cdd:cd01161  260 AMNILNNGRFGMGAALIGTMKRCIEKAVDYANNRKQFGKKIHEFGLIQEKLANMAILQYATESMAYMTSGNMDRGLkaEY 339

                        330       340       350       360       370       380
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 446467688 313 GKESAMSKVFAGDAAMKVTTEAVQVFGGYGYTKDYPVERYMRDAKITQIYEGTQEIQRLVIS 374
Cdd:cd01161  340 QIEAAISKVFASEAAWLVVDEAIQIHGGMGFMREYGVERVLRDLRIFRIFEGTNEILRLFIA 401
MCAD cd01157
Medium chain acyl-CoA dehydrogenase; MCADs are mitochondrial beta-oxidation enzymes, which ...
 5-377 6.40e-123

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: 359.59  E-value: 6.40e-123
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446467688   5 LSEEHEMIRKMVRDFAKNEVAPTAAERDEEERFDRELFDQMAELGLTGIPWPEEYGGIGSDYLAYVIAIEELSRVCasTG 84
Cdd:cd01157    1 LTEQQKEFQETARKFAREEIIPVAAEYDKSGEYPWPLIKRAWELGLMNTHIPEDCGGLGLGTFDTCLITEELAYGC--TG 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446467688  85 VTLSAH-TSLAGWPIFKFGTEEQKQKFLRPMAEGKKIGAYGLTEPGSGSDAGGMKTIAKRDGDHYILNGSKIFITNGGIA 163
Cdd:cd01157   79 VQTAIEaNSLGQMPVIISGNDEQKKKYLGRMTEEPLMCAYCVTEPGAGSDVAGIKTKAEKKGDEYIINGQKMWITNGGKA 158

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446467688 164 DIYVVFALTDPESK---QRGTSAFIVESDTPGFSVGKKESKLGIRSSPTTEIMFEDCRIPVENLLGEEGQGFKVAMQTLD 240
Cdd:cd01157  159 NWYFLLARSDPDPKcpaSKAFTGFIVEADTPGIQPGRKELNMGQRCSDTRGITFEDVRVPKENVLIGEGAGFKIAMGAFD 238

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446467688 241 GGRNGIAAQAVGIAQGALDASVEYARERHQFGKPIAAQQGIGFKLADMATDVEAARLLTYQAAWLESEGLPYGKESAMSK 320
Cdd:cd01157  239 KTRPPVAAGAVGLAQRALDEATKYALERKTFGKLIAEHQAVSFMLADMAMKVELARLAYQRAAWEVDSGRRNTYYASIAK 318

                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 446467688 321 VFAGDAAMKVTTEAVQVFGGYGYTKDYPVERYMRDAKITQIYEGTQEIQRLVISRML 377
Cdd:cd01157  319 AFAADIANQLATDAVQIFGGNGFNSEYPVEKLMRDAKIYQIYEGTSQIQRLIISREH 375
GCD cd01151
Glutaryl-CoA dehydrogenase; Glutaryl-CoA dehydrogenase (GCD). GCD is an acyl-CoA dehydrogenase, ...
 5-378 1.35e-111

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: 331.25  E-value: 1.35e-111
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446467688   5 LSEEHEMIRKMVRDFAKNEVAPTAAERDEEERFDRELFDQMAELGLTGIPwPEEYGGIGSDYLAYVIAIEELSRVCASTG 84
Cdd:cd01151   13 LTEEERAIRDTAREFCQEELAPRVLEAYREEKFDRKIIEEMGELGLLGAT-IKGYGCAGLSSVAYGLIAREVERVDSGYR 91

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446467688  85 VTLSAHTSLAGWPIFKFGTEEQKQKFLRPMAEGKKIGAYGLTEPGSGSDAGGMKTIAKRDGDHYILNGSKIFITNGGIAD 164
Cdd:cd01151   92 SFMSVQSSLVMLPIYDFGSEEQKQKYLPKLASGELIGCFGLTEPNHGSDPGGMETRARKDGGGYKLNGSKTWITNSPIAD 171

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446467688 165 IYVVFALTDPESKQRGtsaFIVESDTPGFSVGKKESKLGIRSSPTTEIMFEDCRIPVENLLgEEGQGFKVAMQTLDGGRN 244
Cdd:cd01151  172 VFVVWARNDETGKIRG---FILERGMKGLSAPKIQGKFSLRASITGEIVMDNVFVPEENLL-PGAEGLRGPFKCLNNARY 247

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446467688 245 GIAAQAVGIAQGALDASVEYARERHQFGKPIAAQQGIGFKLADMATDVEAARLLTYQAAWLESEGLPYGKESAMSKVFAG 324
Cdd:cd01151  248 GIAWGALGAAEDCYHTARQYVLDRKQFGRPLAAFQLVQKKLADMLTEIALGLLACLRVGRLKDQGKATPEQISLLKRNNC 327

                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|....
gi 446467688 325 DAAMKVTTEAVQVFGGYGYTKDYPVERYMRDAKITQIYEGTQEIQRLVISRMLT 378
Cdd:cd01151  328 GKALEIARTAREMLGGNGISDEYHIIRHMVNLESVNTYEGTHDIHALILGRAIT 381
PLN02519 PLN02519
isovaleryl-CoA dehydrogenase
 5-379 1.01e-104

isovaleryl-CoA dehydrogenase


Pssm-ID: 215284 [Multi-domain]  Cd Length: 404  Bit Score: 314.12  E-value: 1.01e-104
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446467688   5 LSEEHEMIRKMVRDFAKNEVAPTAAERDEEERF--DRELFDQMAELGLTGIPWPEEYGGIGSDYLAYVIAIEELSRVCAS 82
Cdd:PLN02519  26 FDDTQLQFKESVQQFAQENIAPHAAAIDATNSFpkDVNLWKLMGDFNLHGITAPEEYGGLGLGYLYHCIAMEEISRASGS 105

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446467688  83 TGVTLSAHTSLAGWPIFKFGTEEQKQKFLRPMAEGKKIGAYGLTEPGSGSDAGGMKTIAKRDGDHYILNGSKIFITNGGI 162
Cdd:PLN02519 106 VGLSYGAHSNLCINQLVRNGTPAQKEKYLPKLISGEHVGALAMSEPNSGSDVVSMKCKAERVDGGYVLNGNKMWCTNGPV 185

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446467688 163 ADIYVVFALTDPESKQRGTSAFIVESDTPGFSVGKKESKLGIRSSPTTEIMFEDCRIPVENLLGEEGQGFKVAMQTLDGG 242
Cdd:PLN02519 186 AQTLVVYAKTDVAAGSKGITAFIIEKGMPGFSTAQKLDKLGMRGSDTCELVFENCFVPEENVLGQEGKGVYVMMSGLDLE 265

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446467688 243 RNGIAAQAVGIAQGALDASVEYARERHQFGKPIAAQQGIGFKLADMATDVEAARLLTYQAAWLESEGLPYGKESAMSKVF 322
Cdd:PLN02519 266 RLVLAAGPLGLMQACLDVVLPYVRQREQFGRPIGEFQFIQGKLADMYTSLQSSRSYVYSVARDCDNGKVDRKDCAGVILC 345

                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 446467688 323 AGDAAMKVTTEAVQVFGGYGYTKDYPVERYMRDAKITQIYEGTQEIQRLVISRMLTK 379
Cdd:PLN02519 346 AAERATQVALQAIQCLGGNGYINEYPTGRLLRDAKLYEIGAGTSEIRRMLIGRELFK 402
PTZ00461 PTZ00461
isovaleryl-CoA dehydrogenase; Provisional
 3-379 1.34e-88

isovaleryl-CoA dehydrogenase; Provisional


Pssm-ID: 185640 [Multi-domain]  Cd Length: 410  Bit Score: 273.35  E-value: 1.34e-88
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446467688   3 FKLSEEHEMIRKMVRDFAKNEVAPTAAERDEEERFDRELFDQMAELGLTGIPWPEEYGGIGSDYLAYVIAIEELSRVCAS 82
Cdd:PTZ00461  35 YNPTPEHAALRETVAKFSREVVDKHAREDDINMHFNRDLFKQLGDLGVMGVTVPEADGGAGMDAVAAVIIHHELSKYDPG 114

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446467688  83 TGVTLSAHTSLAGWPIFKFGTEEQKQKFLRPMAEGKKIGAYGLTEPGSGSDAGGMKTIAKRDGD-HYILNGSKIFITNGG 161
Cdd:PTZ00461 115 FCLAYLAHSMLFVNNFYYSASPAQRARWLPKVLTGEHVGAMGMSEPGAGTDVLGMRTTAKKDSNgNYVLNGSKIWITNGT 194

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446467688 162 IADIYVVFALTDPEskqrgTSAFIVESDTPGFSVGKKESKLGIRSSPTTEIMFEDCRIPVENLLGEEGQGFKVAMQTLDG 241
Cdd:PTZ00461 195 VADVFLIYAKVDGK-----ITAFVVERGTKGFTQGPKIDKCGMRASHMCQLFFEDVVVPAENLLGEEGKGMVGMMRNLEL 269

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446467688 242 GRNGIAAQAVGIAQGALDASVEYARERHQFGKPIAAQQGIGFKLADMATDVEAARLLTYQAAWLESEGLPYGKESAMSKV 321
Cdd:PTZ00461 270 ERVTLAAMAVGIAERSVELMTSYASERKAFGKPISNFGQIQRYIAEGYADTEAAKALVYSVSHNVHPGNKNRLGSDAAKL 349

                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 446467688 322 FAGDAAMKVTTEAVQVFGGYGYTKDYPVERYMRDAKITQIYEGTQEIQRLVISRMLTK 379
Cdd:PTZ00461 350 FATPIAKKVADSAIQVMGGMGYSRDMPVERLWRDAKLLEIGGGTIEAHHKNITKDLLK 407
PRK12341 PRK12341
acyl-CoA dehydrogenase;
1-379 5.12e-78

acyl-CoA dehydrogenase;


Pssm-ID: 183454 [Multi-domain]  Cd Length: 381  Bit Score: 245.02  E-value: 5.12e-78
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446467688   1 MHFKLSEEHEMIRKMVRDFAKNEVAPT-AAERDEEERFDRELFDQMAE--LGLTGIPwpEEYGGIGSDYLAYVIAIEELS 77
Cdd:PRK12341   1 MDFSLTEEQELLLASIRELITRNFPEEyFRTCDENGTYPREFMRALADngISMLGVP--EEFGGTPADYVTQMLVLEEVS 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446467688  78 RVCASTGVTLSAhtsLAGWPIFKFGTEEQKQKflrPMAEGKKIG--AY--GLTEPGSGSDAGGMKTIAKRDGDHYILNGS 153
Cdd:PRK12341  79 KCGAPAFLITNG---QCIHSMRRFGSAEQLRK---TAESTLETGdpAYalALTEPGAGSDNNSATTTYTRKNGKVYLNGQ 152

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446467688 154 KIFITNGGIADIYVVFAL-TDPESKQRGTSAFIVESDTPGFSVGKKEsKLGIRSSPTTEIMFEDCRIPVENLLGEEGQGF 232
Cdd:PRK12341 153 KTFITGAKEYPYMLVLARdPQPKDPKKAFTLWWVDSSKPGIKINPLH-KIGWHMLSTCEVYLDNVEVEESDLVGEEGMGF 231

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446467688 233 KVAMQTLDGGRNGIAAQAVGIAQGALDASVEYARERHQFGKPIAAQQGIGFKLADMATDVEAARLLTYQAAWLESEGLPY 312
Cdd:PRK12341 232 LNVMYNFEMERLINAARSLGFAECAFEDAARYANQRIQFGKPIGHNQLIQEKLTLMAIKIENMRNMVYKVAWQADNGQSL 311

                        330       340       350       360       370       380
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 446467688 313 GKESAMSKVFAGDAAMKVTTEAVQVFGGYGYTKDYPVERYMRDAKITQIYEGTQEIQRLVISRMLTK 379
Cdd:PRK12341 312 RTSAALAKLYCARTAMEVIDDAIQIMGGLGYTDEARVSRFWRDVRCERIGGGTDEIMIYIAGRQILK 378
ACAD_fadE5 cd01153
Putative acyl-CoA dehydrogenases similar to fadE5; Putative acyl-CoA dehydrogenase (ACAD). ...
 16-369 7.36e-73

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: 232.67  E-value: 7.36e-73
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446467688  16 VRDFAKNEVAPTAAERDEEE-RFD----------RELFDQMAELGLTGIPWPEEYGGIGSDYLAYVIAIEELSRVCASTG 84
Cdd:cd01153    5 VARLAENVLAPLNADGDREGpVFDdgrvvvpppfKEALDAFAEAGWMALGVPEEYGGQGLPITVYSALAEIFSRGDAPLM 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446467688  85 VTLSAHTSLAGwpIFKFGTEEQKQKFLRPMAEGKKIGAYGLTEPGSGSDAGGMKTIAKRDGD-HYILNGSKIFITNG--G 161
Cdd:cd01153   85 YASGTQGAAAT--LLAHGTEAQREKWIPRLAEGEWTGTMCLTEPDAGSDLGALRTKAVYQADgSWRINGVKRFISAGehD 162

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446467688 162 IAD--IYVVFALT-DPESKQRGTSAFIVES-----DTPGFSVGKKESKLGIRSSPTTEIMFEDCRIPvenLLGEEGQGFK 233
Cdd:cd01153  163 MSEniVHLVLARSeGAPPGVKGLSLFLVPKflddgERNGVTVARIEEKMGLHGSPTCELVFDNAKGE---LIGEEGMGLA 239

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446467688 234 VAMQTLDGGRNGIAAQAVGIAQGALDASVEYARERHQFGKPIAAQQG--------IGFKLADMATDVEAARLLTYQAAWL 305
Cdd:cd01153  240 QMFAMMNGARLGVGTQGTGLAEAAYLNALAYAKERKQGGDLIKAAPAvtiihhpdVRRSLMTQKAYAEGSRALDLYTATV 319

                        330       340       350       360       370       380       390
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 446467688 306 -------ESEGLPYGKESA-------MSKVFAGDAAMKVTTEAVQVFGGYGYTKDYPVERYMRDAKITQIYEGTQEIQ 369
Cdd:cd01153  320 qdlaerkATEGEDRKALSAladlltpVVKGFGSEAALEAVSDAIQVHGGSGYTREYPIEQYYRDARITTIYEGTTGIQ 397
ACAD_fadE6_17_26 cd01152
Putative acyl-CoA dehydrogenases similar to fadE6, fadE17, and fadE26; Putative acyl-CoA ...
 7-377 2.29e-72

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: 230.31  E-value: 2.29e-72
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446467688   7 EEHEMIRKMVRDFAKNEVAP-----TAAERDEEERFDRELFDQMAELGLTGIPWPEEYGGIGSDYLAYVIAIEELSRVCA 81
Cdd:cd01152    1 PSEEAFRAEVRAWLAAHLPPelreeSALGYREGREDRRRWQRALAAAGWAAPGWPKEYGGRGASLMEQLIFREEMAAAGA 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446467688  82 STGVTLSAhTSLAGWPIFKFGTEEQKQKFLRPMAEGKKIGAYGLTEPGSGSDAGGMKTIAKRDGDHYILNGSKIFITNGG 161
Cdd:cd01152   81 PVPFNQIG-IDLAGPTILAYGTDEQKRRFLPPILSGEEIWCQGFSEPGAGSDLAGLRTRAVRDGDDWVVNGQKIWTSGAH 159

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446467688 162 IADIYVVFALTDPES-KQRGTSAFIVESDTPGFSVGKKESKLGirSSPTTEIMFEDCRIPVENLLGEEGQGFKVAMQTLD 240
Cdd:cd01152  160 YADWAWLLVRTDPEApKHRGISILLVDMDSPGVTVRPIRSING--GEFFNEVFLDDVRVPDANRVGEVNDGWKVAMTTLN 237

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446467688 241 GGRNGIAAQAVGIAQGALDASVEYARERHQFGKPIAAQQgigfKLADMATDVEAARLLTYQAAWLESEGLPYGKESAMSK 320
Cdd:cd01152  238 FERVSIGGSAATFFELLLARLLLLTRDGRPLIDDPLVRQ----RLARLEAEAEALRLLVFRLASALAAGKPPGAEASIAK 313

                        330       340       350       360       370       380
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 446467688 321 VFAGDAAMKVTTEAVQVFG--------GYGYTKDYPVERYMRDAKITQIYEGTQEIQRLVIS-RML 377
Cdd:cd01152  314 LFGSELAQELAELALELLGtaallrdpAPGAELAGRWEADYLRSRATTIYGGTSEIQRNIIAeRLL 379
PRK03354 PRK03354
crotonobetainyl-CoA dehydrogenase; Validated
 1-379 2.34e-67

crotonobetainyl-CoA dehydrogenase; Validated


Pssm-ID: 179566 [Multi-domain]  Cd Length: 380  Bit Score: 217.39  E-value: 2.34e-67
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446467688   1 MHFKLSEEHEMIRKMVRDFAKNEVAPTA-AERDEEERFDRELFDQMAELGLTGIPWPEEYGGIGSDYLAYVIAIEELSRV 79
Cdd:PRK03354   1 MDFNLNDEQELFVAGIRELMASENWEAYfAECDRDSVYPERFVKALADMGIDSLLIPEEHGGLDAGFVTLAAVWMELGRL 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446467688  80 CASTGVTLSAHTSLAGwpIFKFGTEEQKQKFLRPMAEGKKIGAYGLTEPGSGSDAGGMKTIAKRDGDHYILNGSKIFITN 159
Cdd:PRK03354  81 GAPTYVLYQLPGGFNT--FLREGTQEQIDKIMAFRGTGKQMWNSAITEPGAGSDVGSLKTTYTRRNGKVYLNGSKCFITS 158

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446467688 160 GGIADIYVVFALTDPESKQRGTSAFIVESDTPGFSVGKKEsKLGIRSSPTTEIMFEDCRIPVENLLGEEGQGFKVAMQTL 239
Cdd:PRK03354 159 SAYTPYIVVMARDGASPDKPVYTEWFVDMSKPGIKVTKLE-KLGLRMDSCCEITFDDVELDEKDMFGREGNGFNRVKEEF 237

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446467688 240 DGGRNGIAAQAVGIAQGALDASVEYARERHQFGKPIAAQQGIGFKLADMATDVEAARLLTYQAAWLESEGLPYGKESAMS 319
Cdd:PRK03354 238 DHERFLVALTNYGTAMCAFEDAARYANQRVQFGEAIGRFQLIQEKFAHMAIKLNSMKNMLYEAAWKADNGTITSGDAAMC 317

                        330       340       350       360       370       380
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 446467688 320 KVFAGDAAMKVTTEAVQVFGGYGYTKDYPVERYMRDAKITQIYEGTQEIQRLVISRMLTK 379
Cdd:PRK03354 318 KYFCANAAFEVVDSAMQVLGGVGIAGNHRISRFWRDLRVDRVSGGSDEMQILTLGRAVLK 377
ACAD_FadE2 cd01155
Acyl-CoA dehydrogenases similar to fadE2; FadE2-like Acyl-CoA dehydrogenase (ACAD). Acyl-CoA ...
 12-376 7.38e-62

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: 203.78  E-value: 7.38e-62
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446467688  12 IRKMVRDFAKNEVAPTAAERDEE-ERFDR---------ELFDQMA-ELGLTGIPWPEEYGGIGSDYLAYVIAIEELSR-V 79
Cdd:cd01155    6 LRARVKAFMEEHVYPAEQEFLEYyAEGGDrwwtpppiiEKLKAKAkAEGLWNLFLPEVSGLSGLTNLEYAYLAEETGRsF 85

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446467688  80 CASTGVTLSAHTSLAGWPIFKFGTEEQKQKFLRPMAEGKKIGAYGLTEPG-SGSDAGGMKTIAKRDGDHYILNGSKIFIT 158
Cdd:cd01155   86 FAPEVFNCQAPDTGNMEVLHRYGSEEQKKQWLEPLLDGKIRSAFAMTEPDvASSDATNIECSIERDGDDYVINGRKWWSS 165

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446467688 159 NGGIAD--IYVVFALTDP--ESKQRGTSAFIVESDTPGFSVGKKESKLGIRSSPT--TEIMFEDCRIPVENLLGEEGQGF 232
Cdd:cd01155  166 GAGDPRckIAIVMGRTDPdgAPRHRQQSMILVPMDTPGVTIIRPLSVFGYDDAPHghAEITFDNVRVPASNLILGEGRGF 245

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446467688 233 KVAMQTLDGGRNGIAAQAVGIAQGALDASVEYARERHQFGKPIAAQQGIGFKLADMATDVEAARLLTYQAAWLESEGLPY 312
Cdd:cd01155  246 EIAQGRLGPGRIHHCMRLIGAAERALELMCQRAVSREAFGKKLAQHGVVAHWIAKSRIEIEQARLLVLKAAHMIDTVGNK 325

                        330       340       350       360       370       380
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 446467688 313 G--KESAMSKVFAGDAAMKVTTEAVQVFGGYGYTKDYPVERYMRDAKITQIYEGTQEIQRLVISRM 376
Cdd:cd01155  326 AarKEIAMIKVAAPRMALKIIDRAIQVHGAAGVSQDTPLANMYAWARTLRIADGPDEVHLRSIARM 391
Acyl-CoA_dh_1 pfam00441
Acyl-CoA dehydrogenase, C-terminal domain; C-terminal domain of Acyl-CoA dehydrogenase is an ...
 229-375 2.95e-61

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: 194.01  E-value: 2.95e-61
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446467688  229 GQGFKVAMQTLDGGRNGIAAQAVGIAQGALDASVEYARERHQFGKPIAAQQGIGFKLADMATDVEAARLLTYQAAWLESE 308
Cdd:pfam00441   1 GRGFRVAMETLNHERLAIAAMALGLARRALDEALAYARRRKAFGRPLIDFQLVRHKLAEMAAEIEAARLLVYRAAEALDA 80

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 446467688  309 GLPYGKESAMSKVFAGDAAMKVTTEAVQVFGGYGYTKDYPVERYMRDAKITQIYEGTQEIQRLVISR 375
Cdd:pfam00441  81 GGPDGAEASMAKLYASEAAVEVADLAMQLHGGYGYLREYPVERLYRDARVLRIGEGTSEIQRNIIAR 147
PLN02526 PLN02526
acyl-coenzyme A oxidase
 5-379 1.77e-60

acyl-coenzyme A oxidase


Pssm-ID: 178141 [Multi-domain]  Cd Length: 412  Bit Score: 200.46  E-value: 1.77e-60
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446467688   5 LSEEHEMIRKMVRDFAKNEVAPTAAERDEEERFDRELFDQMAELGLTGiPWPEEYGGIGSDYLAYVIAIEELSRVCASTG 84
Cdd:PLN02526  29 LTPEEQALRKRVRECMEKEVAPIMTEYWEKAEFPFHIIPKLGSLGIAG-GTIKGYGCPGLSITASAIATAEVARVDASCS 107

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446467688  85 VTLSAHTSLAGWPIFKFGTEEQKQKFLRPMAEGKKIGAYGLTEPGSGSDAGGMKTIAKRDGDHYILNGSKIFITNGGIAD 164
Cdd:PLN02526 108 TFILVHSSLAMLTIALCGSEAQKQKYLPSLAQLDTVACWALTEPDYGSDASSLNTTATKVEGGWILNGQKRWIGNSTFAD 187

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446467688 165 IYVVFAlTDPESKQrgTSAFIVESDTPGFSVGKKESKLGIRSSPTTEIMFEDCRIPVENLLgEEGQGFKVAMQTLDGGRN 244
Cdd:PLN02526 188 VLVIFA-RNTTTNQ--INGFIVKKGAPGLKATKIENKIGLRMVQNGDIVLKDVFVPDEDRL-PGVNSFQDTNKVLAVSRV 263

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446467688 245 GIAAQAVGIAQGALDASVEYARERHQFGKPIAAQQGIGFKLADMATDVEAARLLTYQAAWLESEGLPYGKESAMSKVFAG 324
Cdd:PLN02526 264 MVAWQPIGISMGVYDMCHRYLKERKQFGAPLAAFQINQEKLVRMLGNIQAMFLVGWRLCKLYESGKMTPGHASLGKAWIT 343

                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 446467688 325 DAAMKVTTEAVQVFGGYGYTKDYPVERYMRDAKITQIYEGTQEIQRLVISRMLTK 379
Cdd:PLN02526 344 KKARETVALGRELLGGNGILADFLVAKAFCDLEPIYTYEGTYDINALVTGREITG 398
Acyl-CoA_dh_N pfam02771
Acyl-CoA dehydrogenase, N-terminal domain; The N-terminal domain of Acyl-CoA dehydrogenase is ...
 6-118 4.92e-58

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: 184.20  E-value: 4.92e-58
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446467688    6 SEEHEMIRKMVRDFAKNEVAPTAAERDEEERFDRELFDQMAELGLTGIPWPEEYGGIGSDYLAYVIAIEELSRVCASTGV 85
Cdd:pfam02771   1 TEEQEALRDTVREFAEEEIAPHAAEWDEEGEFPRELWKKLGELGLLGITIPEEYGGAGLDYLAYALVAEELARADASVAL 80

                          90       100       110
                  ....*....|....*....|....*....|...
gi 446467688   86 TLSAHTSLAGWPIFKFGTEEQKQKFLRPMAEGK 118
Cdd:pfam02771  81 ALSVHSSLGAPPILRFGTEEQKERYLPKLASGE 113
AidB cd01154
Proteins involved in DNA damage response, similar to the AidB gene product; AidB is one of ...
 98-379 1.08e-47

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: 167.16  E-value: 1.08e-47
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446467688  98 IFKFGTEEQKQKFLRPMAEGKK---IGAYGLTEPGSGSDAGGMKTIAKRD-GDHYILNGSKIFiTNGGIADIYVVFALT- 172
Cdd:cd01154  123 LRKYGPEELKQYLPGLLSDRYKtglLGGTWMTEKQGGSDLGANETTAERSgGGVYRLNGHKWF-ASAPLADAALVLARPe 201

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446467688 173 DPESKQRGTSAFIVESDTP-----GFSVGKKESKLGIRSSPTTEIMFEDCripVENLLGEEGQGFKVAMQTLDGGRNGIA 247
Cdd:cd01154  202 GAPAGARGLSLFLVPRLLEdgtrnGYRIRRLKDKLGTRSVATGEVEFDDA---EAYLIGDEGKGIYYILEMLNISRLDNA 278

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446467688 248 AQAVGIAQGALDASVEYARERHQFGKPIAAQQGIGFKLADMATDVEAARLLTYQAAWL--------ESEGLPYGKESAMS 319
Cdd:cd01154  279 VAALGIMRRALSEAYHYARHRRAFGKPLIDHPLMRRDLAEMEVDVEAATALTFRAARAfdraaadkPVEAHMARLATPVA 358

                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 446467688 320 KVFAGDAAMKVTTEAVQVFGGYGYTKDYPVERYMRDAKITQIYEGTQEIQRLVISRMLTK 379
Cdd:cd01154  359 KLIACKRAAPVTSEAMEVFGGNGYLEEWPVARLHREAQVTPIWEGTGNIQALDVLRVLVK 418
PLN02876 PLN02876
acyl-CoA dehydrogenase
 98-376 2.92e-35

acyl-CoA dehydrogenase


Pssm-ID: 215473 [Multi-domain]  Cd Length: 822  Bit Score: 137.23  E-value: 2.92e-35
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446467688  98 IFKFGTEEQKQKFLRPMAEGKKIGAYGLTEPG-SGSDAGGMKTIAKRDGDHYILNGSKIFiTNGGI---ADIYVVFALTD 173
Cdd:PLN02876 529 LLRYGNKEQQLEWLIPLLEGKIRSGFAMTEPQvASSDATNIECSIRRQGDSYVINGTKWW-TSGAMdprCRVLIVMGKTD 607

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446467688 174 PES-KQRGTSAFIVESDTPGFSVGKKESKLGIRSSPT--TEIMFEDCRIPVENLLGEEGQGFKVAMQTLDGGRNGIAAQA 250
Cdd:PLN02876 608 FNApKHKQQSMILVDIQTPGVQIKRPLLVFGFDDAPHghAEISFENVRVPAKNILLGEGRGFEIAQGRLGPGRLHHCMRL 687

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446467688 251 VGIAQGALDASVEYARERHQFGKPIAAQQGIGFKLADMATDVEAARLLTYQAA-WLESEGLPYGKES-AMSKVFAGDAAM 328
Cdd:PLN02876 688 IGAAERGMQLMVQRALSRKAFGKLIAQHGSFLSDLAKCRVELEQTRLLVLEAAdQLDRLGNKKARGIiAMAKVAAPNMAL 767

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*...
gi 446467688 329 KVTTEAVQVFGGYGYTKDYPVERYMRDAKITQIYEGTQEIQRLVISRM 376
Cdd:PLN02876 768 KVLDMAMQVHGAAGVSSDTVLAHLWATARTLRIADGPDEVHLGTIAKL 815
PTZ00456 PTZ00456
acyl-CoA dehydrogenase; Provisional
 39-371 6.13e-35

acyl-CoA dehydrogenase; Provisional


Pssm-ID: 185635 [Multi-domain]  Cd Length: 622  Bit Score: 135.38  E-value: 6.13e-35
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446467688  39 RELFDQMAELGLTGIPWPEEYGGIGSDYLAYVIAIEELSRVCAS----TGVTLSAHTSLAGWpifkfGTEEQKQKFLRPM 114
Cdd:PTZ00456 102 KEAYQALKAGGWTGISEPEEYGGQALPLSVGFITRELMATANWGfsmyPGLSIGAANTLMAW-----GSEEQKEQYLTKL 176

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446467688 115 AEGKKIGAYGLTEPGSGSDAGGMKTIAKRDGD-HYILNGSKIFITNG--GIAD--IYVVFA-LTDPESKQRGTSAFIVES 188
Cdd:PTZ00456 177 VSGEWSGTMCLTEPQCGTDLGQVKTKAEPSADgSYKITGTKIFISAGdhDLTEniVHIVLArLPNSLPTTKGLSLFLVPR 256

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446467688 189 DTP----------GFSVGKKESKLGIRSSPTTEIMFEDcriPVENLLGEEGQGFKVAMQTLDGGRNGIAAQAVGIAQGAL 258
Cdd:PTZ00456 257 HVVkpdgsletakNVKCIGLEKKMGIKGSSTCQLSFEN---SVGYLIGEPNAGMKQMFTFMNTARVGTALEGVCHAELAF 333

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446467688 259 DASVEYARERHQF------------GKPIA----AQQGIGFKLA------DMATDVeaARLLTYQAAW---LESEGLPY- 312
Cdd:PTZ00456 334 QNALRYARERRSMralsgtkepekpADRIIchanVRQNILFAKAvaeggrALLLDV--GRLLDIHAAAkdaATREALDHe 411

                        330       340       350       360       370       380
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 446467688 313 -GKESAMSKVFAGDAAMKVTTEAVQVFGGYGYTKDYPVERYMRDAKITQIYEGTQEIQRL 371
Cdd:PTZ00456 412 iGFYTPIAKGCLTEWGVEAASRCLQVWGGHGYIKGNGMEQILRDARIGTLYEGTTGIQAL 471
Acyl-CoA_dh_M pfam02770
Acyl-CoA dehydrogenase, middle domain; Central domain of Acyl-CoA dehydrogenase has a ...
 122-215 3.30e-34

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: 122.00  E-value: 3.30e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446467688  122 AYGLTEPGSGSDAGGMKT-IAKRDGDHYILNGSKIFITNGGIADIYVVFALTDPESKQRGTSAFIVESDTPGFSVGKKES 200
Cdd:pfam02770   1 AFALTEPGAGSDVASLKTtAADGDGGGWVLNGTKWWITNAGIADLFLVLARTGGDDRHGGISLFLVPKDAPGVSVRRIET 80

                          90
                  ....*....|....*
gi 446467688  201 KLGIRSSPTTEIMFE 215
Cdd:pfam02770  81 KLGVRGLPTGELVFD 95
DszC cd01163
Dibenzothiophene (DBT) desulfurization enzyme C; DszC is a flavin reductase dependent enzyme, ...
 23-357 3.52e-30

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: 118.96  E-value: 3.52e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446467688  23 EVAPTAAERDEEERFDRELFDQMAELGLTGIPWPEEYGGIGSDYLAYVIAIEELSRVCASTGVTLSAHTSLAgWPIFKFG 102
Cdd:cd01163    9 RIAEGAAERDRQRGLPYEEVALLRQSGLGTLRVPKEYGGLGASLPDLYEVVRELAAADSNIAQALRAHFGFV-EALLLAG 87

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446467688 103 TEEQKQKFLRPMAEGKKIGAyGLTEPGSgSDAGGMKTIAKRDGDHYILNGSKIFITNGGIADIYVVFALtDPESKQrgtS 182
Cdd:cd01163   88 PEQFRKRWFGRVLNGWIFGN-AVSERGS-VRPGTFLTATVRDGGGYVLNGKKFYSTGALFSDWVTVSAL-DEEGKL---V 161

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446467688 183 AFIVESDTPGFSVGKKESKLGIR--SSPTTEimFEDCRIPVENLLG-----EEGQGFKVAMQTLdggrngIAAQAVGIAQ 255
Cdd:cd01163  162 FAAVPTDRPGITVVDDWDGFGQRltASGTVT--FDNVRVEPDEVLPrpnapDRGTLLTAIYQLV------LAAVLAGIAR 233

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446467688 256 GALDASVEYARERhqfGKPIA------------AQQGIGfklaDMATDVEAARLLTYQAAWL---------ESEGLPYGK 314
Cdd:cd01163  234 AALDDAVAYVRSR---TRPWIhsgaesarddpyVQQVVG----DLAARLHAAEALVLQAARAldaaaaagtALTAEARGE 306

                        330       340       350       360
                 ....*....|....*....|....*....|....*....|....*.
gi 446467688 315 ---ESAMSKVFAGDAAMKVTTEAVQVFGGYGYTKDYPVERYMRDAK 357
Cdd:cd01163  307 aalAVAAAKVVVTRLALDATSRLFEVGGASATAREHNLDRHWRNAR 352
Acyl-CoA_dh_2 pfam08028
Acyl-CoA dehydrogenase, C-terminal domain;
245-367 7.24e-30

Acyl-CoA dehydrogenase, C-terminal domain;


Pssm-ID: 429790 [Multi-domain]  Cd Length: 133  Bit Score: 111.67  E-value: 7.24e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446467688  245 GIAAQAVGIAQGALDASVEYARER--HQFGKPIAAQQGIGFKLADMATDVEAARLLTYQAAWLESE----GLPY----GK 314
Cdd:pfam08028   1 GIAAAALGAARAALAEFTERARGRvrAYFGVPLAEDPATQLALAEAAARIDAARLLLERAAARIEAaaaaGKPVtpalRA 80

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|...
gi 446467688  315 ESAMSKVFAGDAAMKVTTEAVQVFGGYGYTKDYPVERYMRDAKITQIYEGTQE 367
Cdd:pfam08028  81 EARRAAAFATELAVAAVDALFRAAGGSALFQDSPLQRIWRDIHAAAQHAAVNP 133
PRK13026 PRK13026
acyl-CoA dehydrogenase; Reviewed
 4-342 9.99e-27

acyl-CoA dehydrogenase; Reviewed


Pssm-ID: 237277 [Multi-domain]  Cd Length: 774  Bit Score: 111.97  E-value: 9.99e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446467688   4 KLSEEHEmirkmvrDFAKNEVAPTAAERDE----EERFD--RELFDQMAELGLTGIPWPEEYGGIGSDYLAYVIAIEELS 77
Cdd:PRK13026  77 TLTAEEQ-------AFIDNEVETLLTMLDDwdivQNRKDlpPEVWDYLKKEGFFALIIPKEYGGKGFSAYANSTIVSKIA 149

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446467688  78 RVCASTGVTLSAHTSLA-GWPIFKFGTEEQKQKFLRPMAEGKKIGAYGLTEPGSGSDAGGMKTIA-----KRDGDHYI-- 149
Cdd:PRK13026 150 TRSVSAAVTVMVPNSLGpGELLTHYGTQEQKDYWLPRLADGTEIPCFALTGPEAGSDAGAIPDTGivcrgEFEGEEVLgl 229

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446467688 150 -LNGSKIFITNGGIADIY-VVFALTDPE-----SKQRGTSAFIVESDTPGFSVGKKESKLGIR--SSPTTEimfEDCRIP 220
Cdd:PRK13026 230 rLTWDKRYITLAPVATVLgLAFKLRDPDgllgdKKELGITCALIPTDHPGVEIGRRHNPLGMAfmNGTTRG---KDVFIP 306

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446467688 221 VENLLG---EEGQGFKVAMQTLDGGRnGIA--AQAVGIAQGALDASVEYARERHQFGKPIAAQQGIGFKLADMATD---V 292
Cdd:PRK13026 307 LDWIIGgpdYAGRGWRMLVECLSAGR-GISlpALGTASGHMATRTTGAYAYVRRQFGMPIGQFEGVQEALARIAGNtylL 385

                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|....
gi 446467688 293 EAARLLTyqaawleSEGLPYGKE----SAMSKVFAGDAAMKVTTEAVQVFGGYG 342
Cdd:PRK13026 386 EAARRLT-------TTGLDLGVKpsvvTAIAKYHMTELARDVVNDAMDIHAGKG 432
fadE PRK09463
acyl-CoA dehydrogenase; Reviewed
 40-342 2.35e-26

acyl-CoA dehydrogenase; Reviewed


Pssm-ID: 236528 [Multi-domain]  Cd Length: 777  Bit Score: 110.68  E-value: 2.35e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446467688  40 ELFDQMAELGLTGIPWPEEYGGIGSDYLAYVIAIEELSRVCASTGVTLSAHTSL-AGWPIFKFGTEEQKQKFLRPMAEGK 118
Cdd:PRK09463 113 EVWQFIKEHGFFGMIIPKEYGGLEFSAYAHSRVLQKLASRSGTLAVTVMVPNSLgPGELLLHYGTDEQKDHYLPRLARGE 192

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446467688 119 KIGAYGLTEPGSGSDAGGMK---TIAKRD--GDHYI---LNGSKIFITNGGIADIY-VVFALTDPE-----SKQRGTSAF 184
Cdd:PRK09463 193 EIPCFALTSPEAGSDAGSIPdtgVVCKGEwqGEEVLgmrLTWNKRYITLAPIATVLgLAFKLYDPDgllgdKEDLGITCA 272

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446467688 185 IVESDTPGFSVGKKESKLGIR--SSPTTEimfEDCRIPVENLLGEE---GQGFKVAMQTLDGGRnGIA--AQAVGIAQGA 257
Cdd:PRK09463 273 LIPTDTPGVEIGRRHFPLNVPfqNGPTRG---KDVFIPLDYIIGGPkmaGQGWRMLMECLSVGR-GISlpSNSTGGAKLA 348

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446467688 258 LDASVEYARERHQFGKPIAAQQGIGFKLADMATD---VEAARLLTyqaawleSEGLPYGKE----SAMSKVFAGDAAMKV 330
Cdd:PRK09463 349 ALATGAYARIRRQFKLPIGKFEGIEEPLARIAGNaylMDAARTLT-------TAAVDLGEKpsvlSAIAKYHLTERGRQV 421

                        330
                 ....*....|..
gi 446467688 331 TTEAVQVFGGYG 342
Cdd:PRK09463 422 INDAMDIHGGKG 433
AXO cd01150
Peroxisomal acyl-CoA oxidase; Peroxisomal acyl-CoA oxidases (AXO) catalyze the first set in ...
 9-379 8.29e-19

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: 88.15  E-value: 8.29e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446467688   9 HEMIRKMVRDFAkNEVAPTAAERDEEERFD------RELFDQMAELGLTGipwPEEYggigsdylaYVIaIEELSRVCAS 82
Cdd:cd01150   32 REVERELESDPL-FQRELPSKHLSREELYEelkrkaKTDVERMGELMADD---PEKM---------LAL-TNSLGGYDLS 97

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446467688  83 TGVTLSAHTSLAGWPIFKFGTEEQKQKFLRPMAEGKKIGAYGLTEPGSGSDAGGMKTIAKRD--GDHYILN-----GSKI 155
Cdd:cd01150   98 LGAKLGLHLGLFGNAIKNLGTDEHQDYWLQGANNLEIIGCFAQTELGHGSNLQGLETTATYDplTQEFVINtpdftATKW 177

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446467688 156 FITNGGI-ADIYVVFALTDPESKQRGTSAFIV---ESDT----PGFSVGKKESKLGIRSSPTTEIMFEDCRIPVENLLGE 227
Cdd:cd01150  178 WPGNLGKtATHAVVFAQLITPGKNHGLHAFIVpirDPKThqplPGVTVGDIGPKMGLNGVDNGFLQFRNVRIPRENLLNR 257

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446467688 228 EGQ----------------GFKVAMQTLDGGRNGIAAQAVGIAQGALDASVEYARERHQFGkPIAAQQGIgfKLADMATd 291
Cdd:cd01150  258 FGDvspdgtyvspfkdpnkRYGAMLGTRSGGRVGLIYDAAMSLKKAATIAIRYSAVRRQFG-PKPSDPEV--QILDYQL- 333

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446467688 292 vEAARLLTYQAA--------------WLE-SEGLPYGKESAMSKVFAGDAAMKVTT---------EAVQVFGGYGYTK-- 345
Cdd:cd01150  334 -QQYRLFPQLAAayafhfaakslvemYHEiIKELLQGNSELLAELHALSAGLKAVAtwtaaqgiqECREACGGHGYLAmn 412

                        410       420       430
                 ....*....|....*....|....*....|....
gi 446467688 346 DYPVERYMRDAKITqiYEGTQEIQRLVISRMLTK 379
Cdd:cd01150  413 RLPTLRDDNDPFCT--YEGDNTVLLQQTANYLLK 444
PRK11561 PRK11561
isovaleryl CoA dehydrogenase; Provisional
 124-379 1.96e-16

isovaleryl CoA dehydrogenase; Provisional


Pssm-ID: 183199 [Multi-domain]  Cd Length: 538  Bit Score: 80.57  E-value: 1.96e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446467688 124 GLTEPGSGSDAGGMKTIAKR-DGDHYILNGSKIFITNGGiADIYVVFALTdpeskQRGTSAFIVESDTP-----GFSVGK 197
Cdd:PRK11561 183 GMTEKQGGSDVLSNTTRAERlADGSYRLVGHKWFFSVPQ-SDAHLVLAQA-----KGGLSCFFVPRFLPdgqrnAIRLER 256

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446467688 198 KESKLGIRSSPTTEIMFEDCripVENLLGEEGQGFKVAMQTldGG--RNGIAAQAVGIAQGALDASVEYARERHQFGKPI 275
Cdd:PRK11561 257 LKDKLGNRSNASSEVEFQDA---IGWLLGEEGEGIRLILKM--GGmtRFDCALGSHGLMRRAFSVAIYHAHQRQVFGKPL 331

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446467688 276 AAQQGIGFKLADMATDVEA--ARLLTYQAAWlESEGLPygKESAMSKVFAGDAAMKV-------TTEAVQVFGGYGYTKD 346
Cdd:PRK11561 332 IEQPLMRQVLSRMALQLEGqtALLFRLARAW-DRRADA--KEALWARLFTPAAKFVIckrgipfVAEAMEVLGGIGYCEE 408

                        250       260       270
                 ....*....|....*....|....*....|...
gi 446467688 347 YPVERYMRDAKITQIYEGTQEIQRLVISRMLTK 379
Cdd:PRK11561 409 SELPRLYREMPVNSIWEGSGNIMCLDVLRVLNK 441
NcnH cd01159
Naphthocyclinone hydroxylase; Naphthocyclinone is an aromatic polyketide and an antibiotic, ...
 22-356 2.42e-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: 79.70  E-value: 2.42e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446467688  22 NEVAPTAAER----DEEERFDRELFDQMAELGLTGIPWPEEYGGIGSDYLAYVIAIEELSRVCASTG-VTLSAHTSlaGW 96
Cdd:cd01159    4 EDLAPLIRERapeaERARRLPDEVVRALREIGFFRMFVPKRYGGLEGDFAEFAEAIATLAEACGSAAwVASIVATH--SR 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446467688  97 PIFKFGTEEQKQKFlrpmaegkkigaygltepGSGSDA--------GGMktiAKRDGDHYILNGSKIFITNGGIAD-IYV 167
Cdd:cd01159   82 MLAAFPPEAQEEVW------------------GDGPDTllagsyapGGR---AERVDGGYRVSGTWPFASGCDHADwILV 140

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446467688 168 VFALTDPESKQRGTSAFIVESDtpgFSVGKKESKLGIRSSPTTEIMFEDCRIPVENLL-----------GEEGQGFKVAM 236
Cdd:cd01159  141 GAIVEDDDGGPLPRAFVVPRAE---YEIVDTWHVVGLRGTGSNTVVVDDVFVPEHRTLtagdmmagdgpGGSTPVYRMPL 217

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446467688 237 QTLDGgrNGIAAQAVGIAQGALDASVEYA--RERHQFGKPIAAQQGIGF-KLADMATDVEAARLLTYQAAWLESEGLPYG 313
Cdd:cd01159  218 RQVFP--LSFAAVSLGAAEGALAEFLELAgkRVRQYGAAVKMAEAPITQlRLAEAAAELDAARAFLERATRDLWAHALAG 295

                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|.
gi 446467688 314 KESAMS---KVFAGDA-AMKVTTEAVQ-VF---GGYGYTKDYPVERYMRDA 356
Cdd:cd01159  296 GPIDVEeraRIRRDAAyAAKLSAEAVDrLFhaaGGSALYTASPLQRIWRDI 346
PLN02636 PLN02636
acyl-coenzyme A oxidase
 5-364 6.72e-16

acyl-coenzyme A oxidase


Pssm-ID: 215342 [Multi-domain]  Cd Length: 686  Bit Score: 79.13  E-value: 6.72e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446467688   5 LSEEHEMIRKMVRDFAKNE---VAPTAAERDEEerfdREL-FDQMAELGLTGIPWPEEYggIGSDYLAYVIAIEELSRVC 80
Cdd:PLN02636  61 MRGKHRDIQEKIYEFFNSRpdlQTPVEISKDEH----RELcMRQLTGLVREAGIRPMKY--LVEDPAKYFAITEAVGSVD 134

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446467688  81 ASTGVTLSAHTSLAGWPIFKFGTEEQKQKFLRPMAEGKKIGAYGLTEPGSGSDAGGMKTIAKRD--GDHYILN-----GS 153
Cdd:PLN02636 135 MSLGIKLGVQYSLWGGSVINLGTKKHRDKYFDGIDNLDYPGCFAMTELHHGSNVQGLQTTATFDplTDEFVINtpndgAI 214

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446467688 154 KIFITN----GGIADIYVVFALTDPESK---QRGTSAFIV-------ESDTPGFSVGKKESKLGIRSSPTTEIMFEDCRI 219
Cdd:PLN02636 215 KWWIGNaavhGKFATVFARLKLPTHDSKgvsDMGVHAFIVpirdmktHQVLPGVEIRDCGHKVGLNGVDNGALRFRSVRI 294

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446467688 220 PVENLLGEEG----------------QGFKVAMQTLDGGRNGIAAQAVGIAQGALDASVEYARERHQFGKP------IAA 277
Cdd:PLN02636 295 PRDNLLNRFGdvsrdgkytsslptinKRFAATLGELVGGRVGLAYGSVGVLKASNTIAIRYSLLRQQFGPPkqpeisILD 374

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446467688 278 QQGIGFKLADMATDVEAARLLTYQAAWLESEGLPYGKESAMSKVFAGDAAMKV-----TTEAVQV----FGGYGYTKdyp 348
Cdd:PLN02636 375 YQSQQHKLMPMLASTYAFHFATEYLVERYSEMKKTHDDQLVADVHALSAGLKAyitsyTAKALSTcreaCGGHGYAA--- 451

                        410
                 ....*....|....*....
gi 446467688 349 VERY--MR-DAKITQIYEG 364
Cdd:PLN02636 452 VNRFgsLRnDHDIFQTFEG 470
PTZ00457 PTZ00457
acyl-CoA dehydrogenase; Provisional
 58-239 5.50e-11

acyl-CoA dehydrogenase; Provisional


Pssm-ID: 185636 [Multi-domain]  Cd Length: 520  Bit Score: 63.75  E-value: 5.50e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446467688  58 EYGGIGSDYLAYVIAIEELSRVCASTGVTLSAHTSLAGWPIFKFGTEEQKQKFLRPMAEGKKIGAYGlTEPGSGSDAGGM 137
Cdd:PTZ00457  73 EYGGLGLGHTAHALIYEEVGTNCDSKLLSTIQHSGFCTYLLSTVGSKELKGKYLTAMSDGTIMMGWA-TEEGCGSDISMN 151

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446467688 138 KTIAK-RDGDHYILNGSKiFITNGGIADIYVVFA--LTDPESKQRGTSA-----FIVESDTPGFSVGKKesklgirsspt 209
Cdd:PTZ00457 152 TTKASlTDDGSYVLTGQK-RCEFAASATHFLVLAktLTQTAAEEGATEVsrnsfFICAKDAKGVSVNGD----------- 219

                        170       180       190
                 ....*....|....*....|....*....|
gi 446467688 210 tEIMFEDcrIPVENLLGEEGQGFKVAMQTL 239
Cdd:PTZ00457 220 -SVVFEN--TPAADVVGVVGEGFKDAMITL 246
PLN02312 PLN02312
acyl-CoA oxidase
 82-271 9.41e-11

acyl-CoA oxidase


Pssm-ID: 215178 [Multi-domain]  Cd Length: 680  Bit Score: 63.25  E-value: 9.41e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446467688  82 STGVTLSAHTSLAGWPIFKFGTEEQKQKFLRPMAEGKKIGAYGLTEPGSGSDAGGMKTIAKRD--GDHYILN-----GSK 154
Cdd:PLN02312 148 SLAIKLGVHFFLWGGAIKFLGTKRHHDKWLKDTEDYVVKGCFAMTELGHGSNVRGIETVTTYDpkTEEFVINtpcesAQK 227

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446467688 155 IFItnGGIAD---IYVVFALTDPESKQRGTSAFIVE------SDTPGFSVGKKESKLGIRSSPTTEIMFEDCRIPVENLL 225
Cdd:PLN02312 228 YWI--GGAANhatHTIVFSQLHINGKNEGVHAFIAQirdqdgNICPNIRIADCGHKIGLNGVDNGRIWFDNLRIPRENLL 305

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 446467688 226 G----------------EEGQGFKVAMQTLDGGRNGIAAQAVGIAQGALDASVEYARERHQF 271
Cdd:PLN02312 306 NsvadvspdgkyvsaikDPDQRFGAFLAPLTSGRVTIAVSAIYSSKVGLAIAIRYSLSRRAF 367
PLN02443 PLN02443
acyl-coenzyme A oxidase
 102-272 1.39e-10

acyl-coenzyme A oxidase


Pssm-ID: 178062 [Multi-domain]  Cd Length: 664  Bit Score: 62.93  E-value: 1.39e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446467688 102 GTEEQKQKFLrPMAEGKK-IGAYGLTEPGSGSDAGGMKTIAKRD--GDHYILNGSKIFITN---GGIADIY---VVFALT 172
Cdd:PLN02443 114 GTEEQQKKWL-PLAYKMQiIGCYAQTELGHGSNVQGLETTATFDpkTDEFVIHSPTLTSSKwwpGGLGKVSthaVVYARL 192

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446467688 173 DPESKQRGTSAFIVE-------SDTPGFSVGKKESKLGIRSSPTTE---IMFEDCRIPVENLL------GEEGQ--GFKV 234
Cdd:PLN02443 193 ITNGKDHGIHGFIVQlrslddhSPLPGVTVGDIGMKFGNGAYNTMDngfLRFDHVRIPRDQMLmrlskvTREGKyvQSDV 272

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|..
gi 446467688 235 AMQTLDGG----RNGIAAQAVGIAQGALDASVEYARERHQFG 272
Cdd:PLN02443 273 PRQLVYGTmvyvRQTIVADASTALSRAVCIATRYSAVRRQFG 314
PTZ00460 PTZ00460
acyl-CoA dehydrogenase; Provisional
 97-271 9.50e-10

acyl-CoA dehydrogenase; Provisional


Pssm-ID: 185639 [Multi-domain]  Cd Length: 646  Bit Score: 60.24  E-value: 9.50e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446467688  97 PIFKF-GTEEQKQKFLRPMAEGKKIGAYGLTEPGSGSDAGGMKTIAKRD--GDHYILNGSKIFITN------GGIADIYV 167
Cdd:PTZ00460 104 PAFQVlGTDEQINLWMPSLLNFEIVGCYAQTELGHGSDVQNLETTATYDkqTNEFVIHTPSVEAVKfwpgelGFLCNFAL 183

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446467688 168 VFALTDPESKQRGTSAFIV---ESDT----PGFSVGKKESKLGIRSSPTTEIMFEDCRIPVENLLG------EEGQ---- 230
Cdd:PTZ00460 184 VYAKLIVNGKNKGVHPFMVrirDKEThkplQGVEVGDIGPKMGYAVKDNGFLSFDHYRIPLDSLLAryikvsEDGQverq 263

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|..
gi 446467688 231 -GFKVAMQTLDGGRNGIAAQAVGIAQGALDASVEYARERHQF 271
Cdd:PTZ00460 264 gNPKVSYASMMYMRNLIIDQYPRFAAQALTVAIRYSIYRQQF 305
 
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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