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Conserved domains on  [gi|1253006504|ref|WP_096901859|]
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MULTISPECIES: acyl-CoA dehydrogenase family protein [Acinetobacter]

Protein Classification

acyl-CoA dehydrogenase family protein( domain architecture ID 11449292)

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

CATH:  1.10.540.10
EC:  1.-.-.-
Gene Ontology:  GO:0003995|GO:0050660
PubMed:  10760462|12504675
SCOP:  3001580|3001701

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
CaiA COG1960
Acyl-CoA dehydrogenase related to the alkylation response protein AidB [Lipid transport and ...
 2-380 1.63e-154

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: 440.05  E-value: 1.63e-154
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1253006504   2 LAYDADLELFRDNFRRFMQEHIAPHYAAWEREGIMPRSVWNLLGENGFLCIDVPEEYGGYGVPTHYSLMLVEESARAGyS 81
Cdd:COG1960     3 FELTEEQRALRDEVREFAEEEIAPEAREWDREGEFPRELWRKLAELGLLGLTIPEEYGGLGLSLVELALVLEELARAD-A 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1253006504  82 ALSTGISCHSeIAAPYILHIGTEEQKQYWLPKMVSGEVVGAIGMTEPGAGSDLQAMRTNAILQDDHYVLNGSKTFISNGQ 161
Cdd:COG1960    82 SLALPVGVHN-GAAEALLRFGTEEQKERYLPRLASGEWIGAFALTEPGAGSDAAALRTTAVRDGDGYVLNGQKTFITNAP 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1253006504 162 HADLVVLAVKTDPQARAKGVSLMLVDTHLEGFKKGTNLEKIGLHSQDTSELFFDNVKVPKNQLLGQAGHGFAYLMQELPR 241
Cdd:COG1960   161 VADVILVLARTDPAAGHRGISLFLVPKDTPGVTVGRIEDKMGLRGSDTGELFFDDVRVPAENLLGEEGKGFKIAMSTLNA 240

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1253006504 242 ERTAIAATALGAIRGSIDVTTQYVQERQAFGQAIGQFQNTRFVLAQAKIDELATAAFYNQNVELYMQGKLDVETAAALKS 321
Cdd:COG1960   241 GRLGLAAQALGIAEAALELAVAYAREREQFGRPIADFQAVQHRLADMAAELEAARALVYRAAWLLDAGEDAALEAAMAKL 320

                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1253006504 322 FATDMQMKIADQLLQLFGGYGYMTEYPISRFFVDARIQRIYGGTNEIMKEIVARGLLGR 380
Cdd:COG1960   321 FATEAALEVADEALQIHGGYGYTREYPLERLYRDARILTIYEGTNEIQRLIIARRLLGR 379
 
Name Accession Description Interval E-value
CaiA COG1960
Acyl-CoA dehydrogenase related to the alkylation response protein AidB [Lipid transport and ...
 2-380 1.63e-154

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: 440.05  E-value: 1.63e-154
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1253006504   2 LAYDADLELFRDNFRRFMQEHIAPHYAAWEREGIMPRSVWNLLGENGFLCIDVPEEYGGYGVPTHYSLMLVEESARAGyS 81
Cdd:COG1960     3 FELTEEQRALRDEVREFAEEEIAPEAREWDREGEFPRELWRKLAELGLLGLTIPEEYGGLGLSLVELALVLEELARAD-A 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1253006504  82 ALSTGISCHSeIAAPYILHIGTEEQKQYWLPKMVSGEVVGAIGMTEPGAGSDLQAMRTNAILQDDHYVLNGSKTFISNGQ 161
Cdd:COG1960    82 SLALPVGVHN-GAAEALLRFGTEEQKERYLPRLASGEWIGAFALTEPGAGSDAAALRTTAVRDGDGYVLNGQKTFITNAP 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1253006504 162 HADLVVLAVKTDPQARAKGVSLMLVDTHLEGFKKGTNLEKIGLHSQDTSELFFDNVKVPKNQLLGQAGHGFAYLMQELPR 241
Cdd:COG1960   161 VADVILVLARTDPAAGHRGISLFLVPKDTPGVTVGRIEDKMGLRGSDTGELFFDDVRVPAENLLGEEGKGFKIAMSTLNA 240

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1253006504 242 ERTAIAATALGAIRGSIDVTTQYVQERQAFGQAIGQFQNTRFVLAQAKIDELATAAFYNQNVELYMQGKLDVETAAALKS 321
Cdd:COG1960   241 GRLGLAAQALGIAEAALELAVAYAREREQFGRPIADFQAVQHRLADMAAELEAARALVYRAAWLLDAGEDAALEAAMAKL 320

                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1253006504 322 FATDMQMKIADQLLQLFGGYGYMTEYPISRFFVDARIQRIYGGTNEIMKEIVARGLLGR 380
Cdd:COG1960   321 FATEAALEVADEALQIHGGYGYTREYPLERLYRDARILTIYEGTNEIQRLIIARRLLGR 379
LCAD cd01160
Long chain acyl-CoA dehydrogenase; LCAD is an acyl-CoA dehydrogenases (ACAD), which is found ...
 6-378 3.98e-154

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: 438.86  E-value: 3.98e-154
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1253006504   6 ADLELFRDNFRRFMQEHIAPHYAAWEREGIMPRSVWNLLGENGFLCIDVPEEYGGYGVPTHYSLMLVEESARAGYSALst 85
Cdd:cd01160     1 EEHDAFRDVVRRFFAKEVAPFHHEWEKAGEVPREVWRKAGEQGLLGVGFPEEYGGIGGDLLSAAVLWEELARAGGSGP-- 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1253006504  86 GISCHSEIAAPYILHIGTEEQKQYWLPKMVSGEVVGAIGMTEPGAGSDLQAMRTNAILQDDHYVLNGSKTFISNGQHADL 165
Cdd:cd01160    79 GLSLHTDIVSPYITRAGSPEQKERVLPQMVAGKKIGAIAMTEPGAGSDLQGIRTTARKDGDHYVLNGSKTFITNGMLADV 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1253006504 166 VVLAVKTDPQAR-AKGVSLMLVDTHLEGFKKGTNLEKIGLHSQDTSELFFDNVKVPKNQLLGQAGHGFAYLMQELPRERT 244
Cdd:cd01160   159 VIVVARTGGEARgAGGISLFLVERGTPGFSRGRKLKKMGWKAQDTAELFFDDCRVPAENLLGEENKGFYYLMQNLPQERL 238

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1253006504 245 AIAATALGAIRGSIDVTTQYVQERQAFGQAIGQFQNTRFVLAQAKIDELATAAFYNQNVELYMQGKLDVETAAALKSFAT 324
Cdd:cd01160   239 LIAAGALAAAEFMLEETRNYVKQRKAFGKTLAQLQVVRHKIAELATKVAVTRAFLDNCAWRHEQGRLDVAEASMAKYWAT 318

                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1253006504 325 DMQMKIADQLLQLFGGYGYMTEYPISRFFVDARIQRIYGGTNEIMKEIVARGLL 378
Cdd:cd01160   319 ELQNRVAYECVQLHGGWGYMREYPIARAYRDARVQPIYGGTTEIMKELISRQMV 372
PLN02519 PLN02519
isovaleryl-CoA dehydrogenase
 2-377 1.08e-87

isovaleryl-CoA dehydrogenase


Pssm-ID: 215284 [Multi-domain]  Cd Length: 404  Bit Score: 270.59  E-value: 1.08e-87
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1253006504   2 LAYDADLELFRDNFRRFMQEHIAPHYAAWEREGIMPRSV--WNLLGENGFLCIDVPEEYGGYGVPTHYSLMLVEESARA- 78
Cdd:PLN02519   24 LLFDDTQLQFKESVQQFAQENIAPHAAAIDATNSFPKDVnlWKLMGDFNLHGITAPEEYGGLGLGYLYHCIAMEEISRAs 103

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1253006504  79 GYSALSTGisCHSEIAAPYILHIGTEEQKQYWLPKMVSGEVVGAIGMTEPGAGSDLQAMRTNAILQDDHYVLNGSKTFIS 158
Cdd:PLN02519  104 GSVGLSYG--AHSNLCINQLVRNGTPAQKEKYLPKLISGEHVGALAMSEPNSGSDVVSMKCKAERVDGGYVLNGNKMWCT 181

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1253006504 159 NGQHADLVVLAVKTDPQARAKGVSLMLVDTHLEGFKKGTNLEKIGLHSQDTSELFFDNVKVPKNQLLGQAGHGFAYLMQE 238
Cdd:PLN02519  182 NGPVAQTLVVYAKTDVAAGSKGITAFIIEKGMPGFSTAQKLDKLGMRGSDTCELVFENCFVPEENVLGQEGKGVYVMMSG 261

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1253006504 239 LPRERTAIAATALGAIRGSIDVTTQYVQERQAFGQAIGQFQntrfvLAQAKIDELATA-----AFYNQNVELYMQGKLDV 313
Cdd:PLN02519  262 LDLERLVLAAGPLGLMQACLDVVLPYVRQREQFGRPIGEFQ-----FIQGKLADMYTSlqssrSYVYSVARDCDNGKVDR 336

                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1253006504 314 ETAAALKSFATDMQMKIADQLLQLFGGYGYMTEYPISRFFVDARIQRIYGGTNEIMKEIVARGL 377
Cdd:PLN02519  337 KDCAGVILCAAERATQVALQAIQCLGGNGYINEYPTGRLLRDAKLYEIGAGTSEIRRMLIGREL 400
Acyl-CoA_dh_N pfam02771
Acyl-CoA dehydrogenase, N-terminal domain; The N-terminal domain of Acyl-CoA dehydrogenase is ...
 5-118 3.69e-42

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: 143.37  E-value: 3.69e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1253006504   5 DADLELFRDNFRRFMQEHIAPHYAAWEREGIMPRSVWNLLGENGFLCIDVPEEYGGYGVPTHYSLMLVEESARAGySALS 84
Cdd:pfam02771   1 TEEQEALRDTVREFAEEEIAPHAAEWDEEGEFPRELWKKLGELGLLGITIPEEYGGAGLDYLAYALVAEELARAD-ASVA 79

                          90       100       110
                  ....*....|....*....|....*....|....
gi 1253006504  85 TGISCHSEIAAPYILHIGTEEQKQYWLPKMVSGE 118
Cdd:pfam02771  80 LALSVHSSLGAPPILRFGTEEQKERYLPKLASGE 113
 
Name Accession Description Interval E-value
CaiA COG1960
Acyl-CoA dehydrogenase related to the alkylation response protein AidB [Lipid transport and ...
 2-380 1.63e-154

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: 440.05  E-value: 1.63e-154
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1253006504   2 LAYDADLELFRDNFRRFMQEHIAPHYAAWEREGIMPRSVWNLLGENGFLCIDVPEEYGGYGVPTHYSLMLVEESARAGyS 81
Cdd:COG1960     3 FELTEEQRALRDEVREFAEEEIAPEAREWDREGEFPRELWRKLAELGLLGLTIPEEYGGLGLSLVELALVLEELARAD-A 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1253006504  82 ALSTGISCHSeIAAPYILHIGTEEQKQYWLPKMVSGEVVGAIGMTEPGAGSDLQAMRTNAILQDDHYVLNGSKTFISNGQ 161
Cdd:COG1960    82 SLALPVGVHN-GAAEALLRFGTEEQKERYLPRLASGEWIGAFALTEPGAGSDAAALRTTAVRDGDGYVLNGQKTFITNAP 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1253006504 162 HADLVVLAVKTDPQARAKGVSLMLVDTHLEGFKKGTNLEKIGLHSQDTSELFFDNVKVPKNQLLGQAGHGFAYLMQELPR 241
Cdd:COG1960   161 VADVILVLARTDPAAGHRGISLFLVPKDTPGVTVGRIEDKMGLRGSDTGELFFDDVRVPAENLLGEEGKGFKIAMSTLNA 240

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1253006504 242 ERTAIAATALGAIRGSIDVTTQYVQERQAFGQAIGQFQNTRFVLAQAKIDELATAAFYNQNVELYMQGKLDVETAAALKS 321
Cdd:COG1960   241 GRLGLAAQALGIAEAALELAVAYAREREQFGRPIADFQAVQHRLADMAAELEAARALVYRAAWLLDAGEDAALEAAMAKL 320

                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1253006504 322 FATDMQMKIADQLLQLFGGYGYMTEYPISRFFVDARIQRIYGGTNEIMKEIVARGLLGR 380
Cdd:COG1960   321 FATEAALEVADEALQIHGGYGYTREYPLERLYRDARILTIYEGTNEIQRLIIARRLLGR 379
LCAD cd01160
Long chain acyl-CoA dehydrogenase; LCAD is an acyl-CoA dehydrogenases (ACAD), which is found ...
 6-378 3.98e-154

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: 438.86  E-value: 3.98e-154
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1253006504   6 ADLELFRDNFRRFMQEHIAPHYAAWEREGIMPRSVWNLLGENGFLCIDVPEEYGGYGVPTHYSLMLVEESARAGYSALst 85
Cdd:cd01160     1 EEHDAFRDVVRRFFAKEVAPFHHEWEKAGEVPREVWRKAGEQGLLGVGFPEEYGGIGGDLLSAAVLWEELARAGGSGP-- 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1253006504  86 GISCHSEIAAPYILHIGTEEQKQYWLPKMVSGEVVGAIGMTEPGAGSDLQAMRTNAILQDDHYVLNGSKTFISNGQHADL 165
Cdd:cd01160    79 GLSLHTDIVSPYITRAGSPEQKERVLPQMVAGKKIGAIAMTEPGAGSDLQGIRTTARKDGDHYVLNGSKTFITNGMLADV 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1253006504 166 VVLAVKTDPQAR-AKGVSLMLVDTHLEGFKKGTNLEKIGLHSQDTSELFFDNVKVPKNQLLGQAGHGFAYLMQELPRERT 244
Cdd:cd01160   159 VIVVARTGGEARgAGGISLFLVERGTPGFSRGRKLKKMGWKAQDTAELFFDDCRVPAENLLGEENKGFYYLMQNLPQERL 238

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1253006504 245 AIAATALGAIRGSIDVTTQYVQERQAFGQAIGQFQNTRFVLAQAKIDELATAAFYNQNVELYMQGKLDVETAAALKSFAT 324
Cdd:cd01160   239 LIAAGALAAAEFMLEETRNYVKQRKAFGKTLAQLQVVRHKIAELATKVAVTRAFLDNCAWRHEQGRLDVAEASMAKYWAT 318

                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1253006504 325 DMQMKIADQLLQLFGGYGYMTEYPISRFFVDARIQRIYGGTNEIMKEIVARGLL 378
Cdd:cd01160   319 ELQNRVAYECVQLHGGWGYMREYPIARAYRDARVQPIYGGTTEIMKELISRQMV 372
SCAD_SBCAD cd01158
Short chain acyl-CoA dehydrogenases and eukaryotic short/branched chain acyl-CoA ...
 9-379 6.23e-116

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: 341.94  E-value: 6.23e-116
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1253006504   9 ELFRDNFRRFMQEHIAPHYAAWEREGIMPRSVWNLLGENGFLCIDVPEEYGGYGVPTHYSLMLVEESARAGYSAlSTGIS 88
Cdd:cd01158     4 QMIRKTVRDFAEKEIAPLAAEMDEKGEFPREVIKEMAELGLMGIPIPEEYGGAGLDFLAYAIAIEELAKVDASV-AVIVS 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1253006504  89 CHSEIAAPYILHIGTEEQKQYWLPKMVSGEVVGAIGMTEPGAGSDLQAMRTNAILQDDHYVLNGSKTFISNGQHADLVVL 168
Cdd:cd01158    83 VHNSLGANPIIKFGTEEQKKKYLPPLATGEKIGAFALSEPGAGSDAAALKTTAKKDGDDYVLNGSKMWITNGGEADFYIV 162

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1253006504 169 AVKTDPQARAKGVSLMLVDTHLEGFKKGTNLEKIGLHSQDTSELFFDNVKVPKNQLLGQAGHGFAYLMQELPRERTAIAA 248
Cdd:cd01158   163 FAVTDPSKGYRGITAFIVERDTPGLSVGKKEDKLGIRGSSTTELIFEDVRVPKENILGEEGEGFKIAMQTLDGGRIGIAA 242

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1253006504 249 TALGAIRGSIDVTTQYVQERQAFGQAIGQFQNTRFVLAQAKIDELATAAFYNQNVELYMQGKLDVETAAALKSFATDMQM 328
Cdd:cd01158   243 QALGIAQAALDAAVDYAKERKQFGKPIADFQGIQFKLADMATEIEAARLLTYKAARLKDNGEPFIKEAAMAKLFASEVAM 322

                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1253006504 329 KIADQLLQLFGGYGYMTEYPISRFFVDARIQRIYGGTNEIMKEIVARGLLG 379
Cdd:cd01158   323 RVTTDAVQIFGGYGYTKDYPVERYYRDAKITEIYEGTSEIQRLVIAKHLLK 373
IVD cd01156
Isovaleryl-CoA dehydrogenase; Isovaleryl-CoA dehydrogenase (IVD) is an is an acyl-CoA ...
 3-377 1.52e-104

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: 312.81  E-value: 1.52e-104
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1253006504   3 AYDADLELFRDNFRRFMQEHIAPHYAAWEREGIMPRSVWNLLGENGFLCIDVPEEYGGYGVPTHYSLMLVEESARAGYS- 81
Cdd:cd01156     1 GLDDEIEMLRQSVREFAQKEIAPLAAKIDRDNEFPRDLWRKMGKLGLLGITAPEEYGGSGMGYLAHVIIMEEISRASGSv 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1253006504  82 ALSTGisCHSEIAAPYILHIGTEEQKQYWLPKMVSGEVVGAIGMTEPGAGSDLQAMRTNAILQDDHYVLNGSKTFISNGQ 161
Cdd:cd01156    81 ALSYG--AHSNLCINQIYRNGSAAQKEKYLPKLISGEHIGALAMSEPNAGSDVVSMKLRAEKKGDRYVLNGSKMWITNGP 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1253006504 162 HADLVVLAVKTDPQARAKGVSLMLVDTHLEGFKKGTNLEKIGLHSQDTSELFFDNVKVPKNQLLGQAGHGFAYLMQELPR 241
Cdd:cd01156   159 DADTLVVYAKTDPSAGAHGITAFIVEKGMPGFSRAQKLDKLGMRGSNTCELVFEDCEVPEENILGGENKGVYVLMSGLDY 238

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1253006504 242 ERTAIAATALGAIRGSIDVTTQYVQERQAFGQAIGQFQntrfvLAQAKIDELATaAFYNQNVELYM------QGKLDVET 315
Cdd:cd01156   239 ERLVLAGGPIGIMQAALDVAIPYAHQRKQFGQPIGEFQ-----LVQGKLADMYT-RLNASRSYLYTvakacdRGNMDPKD 312

                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1253006504 316 AAALKSFATDMQMKIADQLLQLFGGYGYMTEYPISRFFVDARIQRIYGGTNEIMKEIVARGL 377
Cdd:cd01156   313 AAGVILYAAEKATQVALDAIQILGGNGYINDYPTGRLLRDAKLYEIGAGTSEIRRMVIGREL 374
ACAD cd00567
Acyl-CoA dehydrogenase; Both mitochondrial acyl-CoA dehydrogenases (ACAD) and peroxisomal ...
 7-375 2.19e-95

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: 287.64  E-value: 2.19e-95
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1253006504   7 DLELFRDNFRRFMQEHIAPHYAAWEREgimPRSVWNLLGENGFLcidvpeeyggygvpthyslmlveesaragysalstg 86
Cdd:cd00567     2 EQRELRDSAREFAAEELEPYARERRET---PEEPWELLAELGLL------------------------------------ 42

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1253006504  87 ischseIAAPYILHIGTEEQKQYWLPKMVSGEVVGAIGMTEPGAGSDLQAMRTNAILQDDHYVLNGSKTFISNGQHADL- 165
Cdd:cd00567    43 ------LGAALLLAYGTEEQKERYLPPLASGEAIAAFALTEPGAGSDLAGIRTTARKDGDGYVLNGRKIFISNGGDADLf 116

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1253006504 166 VVLAVKTDPQARAKGVSLMLVDTHLEGFKKGTNLEKIGLHSQDTSELFFDNVKVPKNQLLGQAGHGFAYLMQELPRERTA 245
Cdd:cd00567   117 IVLARTDEEGPGHRGISAFLVPADTPGVTVGRIWDKMGMRGSGTGELVFDDVRVPEDNLLGEEGGGFELAMKGLNVGRLL 196

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1253006504 246 IAATALGAIRGSIDVTTQYVQERQAFGQAIGQFQNTRFVLAQAKIDELATAAFYNQNVELYMQGKLDVETAAAL-KSFAT 324
Cdd:cd00567   197 LAAVALGAARAALDEAVEYAKQRKQFGKPLAEFQAVQFKLADMAAELEAARLLLYRAAWLLDQGPDEARLEAAMaKLFAT 276

                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1253006504 325 DMQMKIADQLLQLFGGYGYMTEYPISRFFVDARIQRIYGGTNEIMKEIVAR 375
Cdd:cd00567   277 EAAREVADLAMQIHGGRGYSREYPVERYLRDARAARIAEGTAEIQRLIIAR 327
IBD cd01162
Isobutyryl-CoA dehydrogenase; Isobutyryl-CoA dehydrogenase (IBD) catalyzes the alpha, beta- ...
 7-380 1.02e-89

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: 275.09  E-value: 1.02e-89
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1253006504   7 DLELFRDNFRRFMQEHIAPHYAAWEREGIMPRSVWNLLGENGFLCIDVPEEYGGYGVpTHYSLMLVEESARAGYSALSTG 86
Cdd:cd01162     4 EQRAIQEVARAFAAKEMAPHAADWDQKKHFPVDVLRKAAELGFGGIYIRDDVGGSGL-SRLDASIIFEALSTGCVSTAAY 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1253006504  87 ISCHSeIAAPYILHIGTEEQKQYWLPKMVSGEVVGAIGMTEPGAGSDLQAMRTNAILQDDHYVLNGSKTFISNGQHADLV 166
Cdd:cd01162    83 ISIHN-MCAWMIDSFGNDEQRERFLPDLCTMEKLASYCLTEPGSGSDAAALRTRAVREGDHYVLNGSKAFISGAGDSDVY 161

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1253006504 167 VLAVKTDPQArAKGVSLMLVDTHLEGFKKGTNLEKIGLHSQDTSELFFDNVKVPKNQLLGQAGHGFAYLMQELPRERTAI 246
Cdd:cd01162   162 VVMARTGGEG-PKGISCFVVEKGTPGLSFGANEKKMGWNAQPTRAVIFEDCRVPVENRLGGEGQGFGIAMAGLNGGRLNI 240

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1253006504 247 AATALGAIRGSIDVTTQYVQERQAFGQAIGQFQNTRFVLAQAKIDELATAAFYNQNVELYMQGKLD-VETAAALKSFATD 325
Cdd:cd01162   241 ASCSLGAAQAALDLARAYLEERKQFGKPLADFQALQFKLADMATELVASRLMVRRAASALDRGDPDaVKLCAMAKRFATD 320

                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1253006504 326 MQMKIADQLLQLFGGYGYMTEYPISRFFVDARIQRIYGGTNEIMKEIVARGLLGR 380
Cdd:cd01162   321 ECFDVANQALQLHGGYGYLKDYPVEQYVRDLRVHQILEGTNEIMRLIIARALLTR 375
PLN02519 PLN02519
isovaleryl-CoA dehydrogenase
 2-377 1.08e-87

isovaleryl-CoA dehydrogenase


Pssm-ID: 215284 [Multi-domain]  Cd Length: 404  Bit Score: 270.59  E-value: 1.08e-87
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1253006504   2 LAYDADLELFRDNFRRFMQEHIAPHYAAWEREGIMPRSV--WNLLGENGFLCIDVPEEYGGYGVPTHYSLMLVEESARA- 78
Cdd:PLN02519   24 LLFDDTQLQFKESVQQFAQENIAPHAAAIDATNSFPKDVnlWKLMGDFNLHGITAPEEYGGLGLGYLYHCIAMEEISRAs 103

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1253006504  79 GYSALSTGisCHSEIAAPYILHIGTEEQKQYWLPKMVSGEVVGAIGMTEPGAGSDLQAMRTNAILQDDHYVLNGSKTFIS 158
Cdd:PLN02519  104 GSVGLSYG--AHSNLCINQLVRNGTPAQKEKYLPKLISGEHVGALAMSEPNSGSDVVSMKCKAERVDGGYVLNGNKMWCT 181

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1253006504 159 NGQHADLVVLAVKTDPQARAKGVSLMLVDTHLEGFKKGTNLEKIGLHSQDTSELFFDNVKVPKNQLLGQAGHGFAYLMQE 238
Cdd:PLN02519  182 NGPVAQTLVVYAKTDVAAGSKGITAFIIEKGMPGFSTAQKLDKLGMRGSDTCELVFENCFVPEENVLGQEGKGVYVMMSG 261

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1253006504 239 LPRERTAIAATALGAIRGSIDVTTQYVQERQAFGQAIGQFQntrfvLAQAKIDELATA-----AFYNQNVELYMQGKLDV 313
Cdd:PLN02519  262 LDLERLVLAAGPLGLMQACLDVVLPYVRQREQFGRPIGEFQ-----FIQGKLADMYTSlqssrSYVYSVARDCDNGKVDR 336

                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1253006504 314 ETAAALKSFATDMQMKIADQLLQLFGGYGYMTEYPISRFFVDARIQRIYGGTNEIMKEIVARGL 377
Cdd:PLN02519  337 KDCAGVILCAAERATQVALQAIQCLGGNGYINEYPTGRLLRDAKLYEIGAGTSEIRRMLIGREL 400
VLCAD cd01161
Very long chain acyl-CoA dehydrogenase; VLCAD is an acyl-CoA dehydrogenase (ACAD), which is ...
 7-374 5.52e-75

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: 238.14  E-value: 5.52e-75
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1253006504   7 DLELFRDNFRRFMQEHIAPhyAAWEREGIMPRSVWNLLGENGFLCIDVPEEYGGYGVPTHYSLMLVEESARAGYSALSTG 86
Cdd:cd01161    30 ELNMLVGPVEKFFEEVNDP--AKNDQLEKIPRKTLTQLKELGLFGLQVPEEYGGLGLNNTQYARLAEIVGMDLGFSVTLG 107

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1253006504  87 IscHSEIAAPYILHIGTEEQKQYWLPKMVSGEVVGAIGMTEPGAGSDLQAMRTNAILQDD--HYVLNGSKTFISNGQHAD 164
Cdd:cd01161   108 A--HQSIGFKGILLFGTEAQKEKYLPKLASGEWIAAFALTEPSSGSDAASIRTTAVLSEDgkHYVLNGSKIWITNGGIAD 185

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1253006504 165 LVVLAVKTDPQ----ARAKGVSLMLVDTHLEGFKKGTNLEKIGLHSQDTSELFFDNVKVPKNQLLGQAGHGFAYLMQELP 240
Cdd:cd01161   186 IFTVFAKTEVKdatgSVKDKITAFIVERSFGGVTNGPPEKKMGIKGSNTAEVYFEDVKIPVENVLGEVGDGFKVAMNILN 265

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1253006504 241 RERTAIAATALGAIRGSIDVTTQYVQERQAFGQAIGQFQntrfvLAQAKIDELATAAFYNQNVELYMQGKLD-------- 312
Cdd:cd01161   266 NGRFGMGAALIGTMKRCIEKAVDYANNRKQFGKKIHEFG-----LIQEKLANMAILQYATESMAYMTSGNMDrglkaeyq 340

                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1253006504 313 VEtAAALKSFATDMQMKIADQLLQLFGGYGYMTEYPISRFFVDARIQRIYGGTNEIMKEIVA 374
Cdd:cd01161   341 IE-AAISKVFASEAAWLVVDEAIQIHGGMGFMREYGVERVLRDLRIFRIFEGTNEILRLFIA 401
GCD cd01151
Glutaryl-CoA dehydrogenase; Glutaryl-CoA dehydrogenase (GCD). GCD is an acyl-CoA dehydrogenase, ...
 12-379 2.38e-70

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: 225.32  E-value: 2.38e-70
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1253006504  12 RDNFRRFMQEHIAPHYAAWEREGIMPRSVWNLLGENGFLCIdVPEEYGGYGVP-THYSLmLVEESARAGySALSTGISCH 90
Cdd:cd01151    21 RDTAREFCQEELAPRVLEAYREEKFDRKIIEEMGELGLLGA-TIKGYGCAGLSsVAYGL-IAREVERVD-SGYRSFMSVQ 97

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1253006504  91 SEIAAPYILHIGTEEQKQYWLPKMVSGEVVGAIGMTEPGAGSDLQAMRTNAILQDDHYVLNGSKTFISNGQHADLVVLAV 170
Cdd:cd01151    98 SSLVMLPIYDFGSEEQKQKYLPKLASGELIGCFGLTEPNHGSDPGGMETRARKDGGGYKLNGSKTWITNSPIADVFVVWA 177

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1253006504 171 KTDPQARAKGvslMLVDTHLEGFKKGTNLEKIGLHSQDTSELFFDNVKVPKNQLLGQAgHGFAYLMQELPRERTAIAATA 250
Cdd:cd01151   178 RNDETGKIRG---FILERGMKGLSAPKIQGKFSLRASITGEIVMDNVFVPEENLLPGA-EGLRGPFKCLNNARYGIAWGA 253

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1253006504 251 LGAIRGSIDVTTQYVQERQAFGQAIGQFQntrfvLAQAKIDELATAAFYNQNV-----ELYMQGKLDVETAAALKSFATD 325
Cdd:cd01151   254 LGAAEDCYHTARQYVLDRKQFGRPLAAFQ-----LVQKKLADMLTEIALGLLAclrvgRLKDQGKATPEQISLLKRNNCG 328

                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1253006504 326 MQMKIADQLLQLFGGYGYMTEYPISRFFVDARIQRIYGGTNEIMKEIVARGLLG 379
Cdd:cd01151   329 KALEIARTAREMLGGNGISDEYHIIRHMVNLESVNTYEGTHDIHALILGRAITG 382
PRK12341 PRK12341
acyl-CoA dehydrogenase;
9-378 6.46e-70

acyl-CoA dehydrogenase;


Pssm-ID: 183454 [Multi-domain]  Cd Length: 381  Bit Score: 224.22  E-value: 6.46e-70
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1253006504   9 ELFRDNFRRFMQEHIAPHY-AAWEREGIMPRSVWNLLGENGFLCIDVPEEYGGygVPTHY-SLMLV-EESARAGYSA--L 83
Cdd:PRK12341   10 ELLLASIRELITRNFPEEYfRTCDENGTYPREFMRALADNGISMLGVPEEFGG--TPADYvTQMLVlEEVSKCGAPAflI 87

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1253006504  84 STGISCHSeiaapyILHIGTEEQ-KQYWLPKMVSGEVVGAIGMTEPGAGSDLQAMRTNAILQDDHYVLNGSKTFISNGQH 162
Cdd:PRK12341   88 TNGQCIHS------MRRFGSAEQlRKTAESTLETGDPAYALALTEPGAGSDNNSATTTYTRKNGKVYLNGQKTFITGAKE 161

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1253006504 163 AD-LVVLAVKTDPQARAKGVSLMLVDTHLEGFKKgTNLEKIGLHSQDTSELFFDNVKVPKNQLLGQAGHGFAYLMQELPR 241
Cdd:PRK12341  162 YPyMLVLARDPQPKDPKKAFTLWWVDSSKPGIKI-NPLHKIGWHMLSTCEVYLDNVEVEESDLVGEEGMGFLNVMYNFEM 240

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1253006504 242 ERTAIAATALGAIRGSIDVTTQYVQERQAFGQAIGQFQntrfvLAQAKIDELAtAAFYNQNVELYM------QGkLDVET 315
Cdd:PRK12341  241 ERLINAARSLGFAECAFEDAARYANQRIQFGKPIGHNQ-----LIQEKLTLMA-IKIENMRNMVYKvawqadNG-QSLRT 313

                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1253006504 316 AAAL-KSFATDMQMKIADQLLQLFGGYGYMTEYPISRFFVDARIQRIYGGTNEIMKEIVARGLL 378
Cdd:PRK12341  314 SAALaKLYCARTAMEVIDDAIQIMGGLGYTDEARVSRFWRDVRCERIGGGTDEIMIYIAGRQIL 377
MCAD cd01157
Medium chain acyl-CoA dehydrogenase; MCADs are mitochondrial beta-oxidation enzymes, which ...
 11-380 1.31e-67

Medium chain acyl-CoA dehydrogenase; MCADs are mitochondrial beta-oxidation enzymes, which catalyze the alpha,beta dehydrogenation of the corresponding medium chain acyl-CoA by FAD, which becomes reduced. The reduced form of MCAD is reoxidized in the oxidative half-reaction by electron-transferring flavoprotein (ETF), from which the electrons are transferred to the mitochondrial respiratory chain coupled with ATP synthesis. MCAD is a homotetramer.


Pssm-ID: 173846 [Multi-domain]  Cd Length: 378  Bit Score: 218.22  E-value: 1.31e-67
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1253006504  11 FRDNFRRFMQEHIAPHYAAWEREGIMP----RSVWNLlgenGFLCIDVPEEYGGYGVPTHYSLMLVEESARaGYSALSTG 86
Cdd:cd01157     8 FQETARKFAREEIIPVAAEYDKSGEYPwpliKRAWEL----GLMNTHIPEDCGGLGLGTFDTCLITEELAY-GCTGVQTA 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1253006504  87 ISCHSEIAAPYILHiGTEEQKQYWLPKMVSGEVVGAIGMTEPGAGSDLQAMRTNAILQDDHYVLNGSKTFISNGQHADLV 166
Cdd:cd01157    83 IEANSLGQMPVIIS-GNDEQKKKYLGRMTEEPLMCAYCVTEPGAGSDVAGIKTKAEKKGDEYIINGQKMWITNGGKANWY 161

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1253006504 167 VLAVKTDPQARA---KGVSLMLVDTHLEGFKKGTNLEKIGLHSQDTSELFFDNVKVPKNQLLGQAGHGFAYLMQELPRER 243
Cdd:cd01157   162 FLLARSDPDPKCpasKAFTGFIVEADTPGIQPGRKELNMGQRCSDTRGITFEDVRVPKENVLIGEGAGFKIAMGAFDKTR 241

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1253006504 244 TAIAATALGAIRGSIDVTTQYVQERQAFGQAIGQFQNTRFVLAQAKID-ELATAAFYNQNVELYMqGKLDVETAAALKSF 322
Cdd:cd01157   242 PPVAAGAVGLAQRALDEATKYALERKTFGKLIAEHQAVSFMLADMAMKvELARLAYQRAAWEVDS-GRRNTYYASIAKAF 320

                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1253006504 323 ATDMQMKIADQLLQLFGGYGYMTEYPISRFFVDARIQRIYGGTNEIMKEIVARGLLGR 380
Cdd:cd01157   321 AADIANQLATDAVQIFGGNGFNSEYPVEKLMRDAKIYQIYEGTSQIQRLIISREHLGK 378
ACAD_fadE6_17_26 cd01152
Putative acyl-CoA dehydrogenases similar to fadE6, fadE17, and fadE26; Putative acyl-CoA ...
 7-379 3.70e-65

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: 211.82  E-value: 3.70e-65
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1253006504   7 DLELFRDNFRRFMQEHIAP----HYAAWEREGIMPRSVWN-LLGENGFLCIDVPEEYGGYGVPTHYSLMLVEESARAG-- 79
Cdd:cd01152     2 SEEAFRAEVRAWLAAHLPPelreESALGYREGREDRRRWQrALAAAGWAAPGWPKEYGGRGASLMEQLIFREEMAAAGap 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1253006504  80 YSALSTGIschsEIAAPYILHIGTEEQKQYWLPKMVSGEVVGAIGMTEPGAGSDLQAMRTNAILQDDHYVLNGSKTFISN 159
Cdd:cd01152    82 VPFNQIGI----DLAGPTILAYGTDEQKRRFLPPILSGEEIWCQGFSEPGAGSDLAGLRTRAVRDGDDWVVNGQKIWTSG 157

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1253006504 160 GQHADLVVLAVKTDPQA-RAKGVSLMLVDTHLEGFKKgTNLEKIGLHSqDTSELFFDNVKVPKNQLLGQAGHGFAYLMQE 238
Cdd:cd01152   158 AHYADWAWLLVRTDPEApKHRGISILLVDMDSPGVTV-RPIRSINGGE-FFNEVFLDDVRVPDANRVGEVNDGWKVAMTT 235

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1253006504 239 LPRERTAIAATAlgAIRGSIDVttQYVQERQAFGQAIGQFQNTRFVLAQAKIDELATAAFYNQNVELYMQGKLDVETAAA 318
Cdd:cd01152   236 LNFERVSIGGSA--ATFFELLL--ARLLLLTRDGRPLIDDPLVRQRLARLEAEAEALRLLVFRLASALAAGKPPGAEASI 311

                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1253006504 319 LKSFATDMQMKIADQLLQLFG-----GYGYMTEYPISRFFVD---ARIQRIYGGTNEIMKEIVARGLLG 379
Cdd:cd01152   312 AKLFGSELAQELAELALELLGtaallRDPAPGAELAGRWEADylrSRATTIYGGTSEIQRNIIAERLLG 380
PTZ00461 PTZ00461
isovaleryl-CoA dehydrogenase; Provisional
 10-378 4.47e-65

isovaleryl-CoA dehydrogenase; Provisional


Pssm-ID: 185640 [Multi-domain]  Cd Length: 410  Bit Score: 212.49  E-value: 4.47e-65
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1253006504  10 LFRDNFRRFMQEHIAPHYAAWEREGIMPRSVWNLLGENGFLCIDVPEEYGGYG------VPTHYSLMLVEESARAGYSAl 83
Cdd:PTZ00461   43 ALRETVAKFSREVVDKHAREDDINMHFNRDLFKQLGDLGVMGVTVPEADGGAGmdavaaVIIHHELSKYDPGFCLAYLA- 121

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1253006504  84 stgiscHSEIAAPYILHIGTEEQKQYWLPKMVSGEVVGAIGMTEPGAGSDLQAMRTNAI-LQDDHYVLNGSKTFISNGQH 162
Cdd:PTZ00461  122 ------HSMLFVNNFYYSASPAQRARWLPKVLTGEHVGAMGMSEPGAGTDVLGMRTTAKkDSNGNYVLNGSKIWITNGTV 195

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1253006504 163 ADLVVLAVKTDPQarakgVSLMLVDTHLEGFKKGTNLEKIGLHSQDTSELFFDNVKVPKNQLLGQAGHGFAYLMQELPRE 242
Cdd:PTZ00461  196 ADVFLIYAKVDGK-----ITAFVVERGTKGFTQGPKIDKCGMRASHMCQLFFEDVVVPAENLLGEEGKGMVGMMRNLELE 270

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1253006504 243 RTAIAATALGAIRGSIDVTTQYVQERQAFGQAIGQFQNTRFVLAQAKID-ELATAAFY--NQNVELYMQGKLDVEtaaAL 319
Cdd:PTZ00461  271 RVTLAAMAVGIAERSVELMTSYASERKAFGKPISNFGQIQRYIAEGYADtEAAKALVYsvSHNVHPGNKNRLGSD---AA 347

                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1253006504 320 KSFATDMQMKIADQLLQLFGGYGYMTEYPISRFFVDARIQRIYGGTNEIMKEIVARGLL 378
Cdd:PTZ00461  348 KLFATPIAKKVADSAIQVMGGMGYSRDMPVERLWRDAKLLEIGGGTIEAHHKNITKDLL 406
ACAD_fadE5 cd01153
Putative acyl-CoA dehydrogenases similar to fadE5; Putative acyl-CoA dehydrogenase (ACAD). ...
 17-368 1.70e-58

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: 195.30  E-value: 1.70e-58
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1253006504  17 RFMQEHIAPHYAAWEREG---------IMPRSVWNL--LGENGFLCIDVPEEYGGYGVPTHYSLMLVEESARaGYSALST 85
Cdd:cd01153     7 RLAENVLAPLNADGDREGpvfddgrvvVPPPFKEALdaFAEAGWMALGVPEEYGGQGLPITVYSALAEIFSR-GDAPLMY 85

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1253006504  86 GISCHSeiAAPYILHIGTEEQKQYWLPKMVSGEVVGAIGMTEPGAGSDLQAMRTNAILQDD-HYVLNGSKTFISNGQHAD 164
Cdd:cd01153    86 ASGTQG--AAATLLAHGTEAQREKWIPRLAEGEWTGTMCLTEPDAGSDLGALRTKAVYQADgSWRINGVKRFISAGEHDM 163

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1253006504 165 -----LVVLAVKTDPQARAKGVSLMLVDTHLEGFKKG----TNLE-KIGLHSQDTSELFFDNVKVPknqLLGQAGHGFAY 234
Cdd:cd01153   164 senivHLVLARSEGAPPGVKGLSLFLVPKFLDDGERNgvtvARIEeKMGLHGSPTCELVFDNAKGE---LIGEEGMGLAQ 240

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1253006504 235 LMQELPRERTAIAATALGAIRGSIDVTTQYVQERQAFGQAIGQFQNTRFVLAQAKIDELATAAFYNQN---VELYMQGKL 311
Cdd:cd01153   241 MFAMMNGARLGVGTQGTGLAEAAYLNALAYAKERKQGGDLIKAAPAVTIIHHPDVRRSLMTQKAYAEGsraLDLYTATVQ 320

                         330       340       350       360       370       380       390
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1253006504 312 DVETAAA-------------------LKSFATDMQMKIADQLLQLFGGYGYMTEYPISRFFVDARIQRIYGGTNEI 368
Cdd:cd01153   321 DLAERKAtegedrkalsaladlltpvVKGFGSEAALEAVSDAIQVHGGSGYTREYPIEQYYRDARITTIYEGTTGI 396
PRK03354 PRK03354
crotonobetainyl-CoA dehydrogenase; Validated
 7-378 2.58e-47

crotonobetainyl-CoA dehydrogenase; Validated


Pssm-ID: 179566 [Multi-domain]  Cd Length: 380  Bit Score: 165.39  E-value: 2.58e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1253006504   7 DLELFRDNFRRFM-QEHIAPHYAAWEREGIMPRSVWNLLGENGFLCIDVPEEYGGYGVPTHYSLMLVEESARAGYSA--- 82
Cdd:PRK03354    8 EQELFVAGIRELMaSENWEAYFAECDRDSVYPERFVKALADMGIDSLLIPEEHGGLDAGFVTLAAVWMELGRLGAPTyvl 87

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1253006504  83 --LSTGISChseiaapyILHIGTEEQKQYWLPKMVSGEVVGAIGMTEPGAGSDLQAMRTNAILQDDHYVLNGSKTFISNG 160
Cdd:PRK03354   88 yqLPGGFNT--------FLREGTQEQIDKIMAFRGTGKQMWNSAITEPGAGSDVGSLKTTYTRRNGKVYLNGSKCFITSS 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1253006504 161 QHADLVVLAVKTDPQARAKGVSLMLVDTHLEGFKKgTNLEKIGLHSQDTSELFFDNVKVPKNQLLGQAGHGFAYLMQELP 240
Cdd:PRK03354  160 AYTPYIVVMARDGASPDKPVYTEWFVDMSKPGIKV-TKLEKLGLRMDSCCEITFDDVELDEKDMFGREGNGFNRVKEEFD 238

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1253006504 241 RERTAIAATALGAIRGSIDVTTQYVQERQAFGQAIGQFQntrfvLAQAKIDELATAAFYNQNVeLYM------QGKLDVE 314
Cdd:PRK03354  239 HERFLVALTNYGTAMCAFEDAARYANQRVQFGEAIGRFQ-----LIQEKFAHMAIKLNSMKNM-LYEaawkadNGTITSG 312

                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1253006504 315 TAAALKSFATDMQMKIADQLLQLFGGYGYMTEYPISRFFVDARIQRIYGGTNEIMKEIVARGLL 378
Cdd:PRK03354  313 DAAMCKYFCANAAFEVVDSAMQVLGGVGIAGNHRISRFWRDLRVDRVSGGSDEMQILTLGRAVL 376
Acyl-CoA_dh_N pfam02771
Acyl-CoA dehydrogenase, N-terminal domain; The N-terminal domain of Acyl-CoA dehydrogenase is ...
 5-118 3.69e-42

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: 143.37  E-value: 3.69e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1253006504   5 DADLELFRDNFRRFMQEHIAPHYAAWEREGIMPRSVWNLLGENGFLCIDVPEEYGGYGVPTHYSLMLVEESARAGySALS 84
Cdd:pfam02771   1 TEEQEALRDTVREFAEEEIAPHAAEWDEEGEFPRELWKKLGELGLLGITIPEEYGGAGLDYLAYALVAEELARAD-ASVA 79

                          90       100       110
                  ....*....|....*....|....*....|....
gi 1253006504  85 TGISCHSEIAAPYILHIGTEEQKQYWLPKMVSGE 118
Cdd:pfam02771  80 LALSVHSSLGAPPILRFGTEEQKERYLPKLASGE 113
Acyl-CoA_dh_1 pfam00441
Acyl-CoA dehydrogenase, C-terminal domain; C-terminal domain of Acyl-CoA dehydrogenase is an ...
 229-377 1.59e-40

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: 140.47  E-value: 1.59e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1253006504 229 GHGFAYLMQELPRERTAIAATALGAIRGSIDVTTQYVQERQAFGQAIGQFQNTRFVLAQAKIDELATAAFYNQNVELYMQ 308
Cdd:pfam00441   1 GRGFRVAMETLNHERLAIAAMALGLARRALDEALAYARRRKAFGRPLIDFQLVRHKLAEMAAEIEAARLLVYRAAEALDA 80

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1253006504 309 GKLDVETAAALKSFATDMQMKIADQLLQLFGGYGYMTEYPISRFFVDARIQRIYGGTNEIMKEIVARGL 377
Cdd:pfam00441  81 GGPDGAEASMAKLYASEAAVEVADLAMQLHGGYGYLREYPVERLYRDARVLRIGEGTSEIQRNIIARRL 149
ACAD_FadE2 cd01155
Acyl-CoA dehydrogenases similar to fadE2; FadE2-like Acyl-CoA dehydrogenase (ACAD). Acyl-CoA ...
 12-375 7.69e-37

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: 137.52  E-value: 7.69e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1253006504  12 RDNFRRFMQEHIAP-------HYA-----AWEREGIMP--------RSVWNLlgengFLcidvPEEYGGYGVPTHYSLML 71
Cdd:cd01155     7 RARVKAFMEEHVYPaeqefleYYAeggdrWWTPPPIIEklkakakaEGLWNL-----FL----PEVSGLSGLTNLEYAYL 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1253006504  72 VEESARAGYSalSTGISChseiAAP-----YILHI-GTEEQKQYWLPKMVSGEVVGAIGMTEPG-AGSDLQAMRTNAILQ 144
Cdd:cd01155    78 AEETGRSFFA--PEVFNC----QAPdtgnmEVLHRyGSEEQKKQWLEPLLDGKIRSAFAMTEPDvASSDATNIECSIERD 151

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1253006504 145 DDHYVLNGSKTFISNGQHADLVVLAV--KTDP--QARAKGVSLMLVDTHLEGFKKGTNLEKIGlhSQDT----SELFFDN 216
Cdd:cd01155   152 GDDYVINGRKWWSSGAGDPRCKIAIVmgRTDPdgAPRHRQQSMILVPMDTPGVTIIRPLSVFG--YDDAphghAEITFDN 229

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1253006504 217 VKVPKNQLLGQAGHGFAYLMQELPRERTAIAATALGAIRGSIDVTTQYVQERQAFGQAIGQFQNTRFVLAQAKID-ELA- 294
Cdd:cd01155   230 VRVPASNLILGEGRGFEIAQGRLGPGRIHHCMRLIGAAERALELMCQRAVSREAFGKKLAQHGVVAHWIAKSRIEiEQAr 309

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1253006504 295 ----TAAfynqnvelYMQGKLDVETA----AALKSFATDMQMKIADQLLQLFGGYGYMTEYPISRFFVDARIQRIYGGTN 366
Cdd:cd01155   310 llvlKAA--------HMIDTVGNKAArkeiAMIKVAAPRMALKIIDRAIQVHGAAGVSQDTPLANMYAWARTLRIADGPD 381


                  ....*....
gi 1253006504 367 EIMKEIVAR 375
Cdd:cd01155   382 EVHLRSIAR 390
PTZ00456 PTZ00456
acyl-CoA dehydrogenase; Provisional
 44-380 5.60e-33

acyl-CoA dehydrogenase; Provisional


Pssm-ID: 185635 [Multi-domain]  Cd Length: 622  Bit Score: 129.99  E-value: 5.60e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1253006504  44 LGENGFLCIDVPEEYGGYGVPTHYSLMLVEESARAG-----YSALSTGischseiAAPYILHIGTEEQKQYWLPKMVSGE 118
Cdd:PTZ00456  108 LKAGGWTGISEPEEYGGQALPLSVGFITRELMATANwgfsmYPGLSIG-------AANTLMAWGSEEQKEQYLTKLVSGE 180

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1253006504 119 VVGAIGMTEPGAGSDLQAMRTNAI-LQDDHYVLNGSKTFISNGQHaDL------VVLAVKTDPQARAKGVSLMLVDTH-- 189
Cdd:PTZ00456  181 WSGTMCLTEPQCGTDLGQVKTKAEpSADGSYKITGTKIFISAGDH-DLtenivhIVLARLPNSLPTTKGLSLFLVPRHvv 259

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1253006504 190 -----LEGFK--KGTNLE-KIGLHSQDTSELFFDNvkvPKNQLLGQAGHGFAYLMQELPRERTAIAATALGAIRGSIDVT 261
Cdd:PTZ00456  260 kpdgsLETAKnvKCIGLEkKMGIKGSSTCQLSFEN---SVGYLIGEPNAGMKQMFTFMNTARVGTALEGVCHAELAFQNA 336

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1253006504 262 TQYVQERQAF------------GQAIGQFQNTRFVLAQAK-IDELATAAFYNQNVEL-YMQGKLDVETAAAL-------- 319
Cdd:PTZ00456  337 LRYARERRSMralsgtkepekpADRIICHANVRQNILFAKaVAEGGRALLLDVGRLLdIHAAAKDAATREALdheigfyt 416

                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1253006504 320 ---KSFATDMQMKIADQLLQLFGGYGYMTEYPISRFFVDARIQRIYGGTNEIMkeivARGLLGR 380
Cdd:PTZ00456  417 piaKGCLTEWGVEAASRCLQVWGGHGYIKGNGMEQILRDARIGTLYEGTTGIQ----ALDFIGR 476
PLN02526 PLN02526
acyl-coenzyme A oxidase
 12-379 1.91e-29

acyl-coenzyme A oxidase


Pssm-ID: 178141 [Multi-domain]  Cd Length: 412  Bit Score: 117.65  E-value: 1.91e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1253006504  12 RDNFRRFMQEHIAPHYAAWEREGIMPRSVWNLLGENGFLCIDVpEEYGGYGVPTHYSLMLVEESARAGYSAlSTGISCHS 91
Cdd:PLN02526   37 RKRVRECMEKEVAPIMTEYWEKAEFPFHIIPKLGSLGIAGGTI-KGYGCPGLSITASAIATAEVARVDASC-STFILVHS 114

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1253006504  92 EIAAPYILHIGTEEQKQYWLPKMVSGEVVGAIGMTEPGAGSDLQAMRTNAILQDDHYVLNGSKTFISNGQHAD-LVVLAV 170
Cdd:PLN02526  115 SLAMLTIALCGSEAQKQKYLPSLAQLDTVACWALTEPDYGSDASSLNTTATKVEGGWILNGQKRWIGNSTFADvLVIFAR 194

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1253006504 171 KTDpqarAKGVSLMLVDTHLEGFkKGTNLE-KIGLHSQDTSELFFDNVKVPKNQLLGQAgHGFAYLMQELPRERTAIAAT 249
Cdd:PLN02526  195 NTT----TNQINGFIVKKGAPGL-KATKIEnKIGLRMVQNGDIVLKDVFVPDEDRLPGV-NSFQDTNKVLAVSRVMVAWQ 268

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1253006504 250 ALGAIRGSIDVTTQYVQERQAFGQAIGQFQNTRFVLAQAKIDELATAAFYNQNVELYMQGKLDVETAAALKSFATDMQMK 329
Cdd:PLN02526  269 PIGISMGVYDMCHRYLKERKQFGAPLAAFQINQEKLVRMLGNIQAMFLVGWRLCKLYESGKMTPGHASLGKAWITKKARE 348

                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|
gi 1253006504 330 IADQLLQLFGGYGYMTEYPISRFFVDARIQRIYGGTNEIMKEIVARGLLG 379
Cdd:PLN02526  349 TVALGRELLGGNGILADFLVAKAFCDLEPIYTYEGTYDINALVTGREITG 398
Acyl-CoA_dh_M pfam02770
Acyl-CoA dehydrogenase, middle domain; Central domain of Acyl-CoA dehydrogenase has a ...
 122-215 7.45e-29

Acyl-CoA dehydrogenase, middle domain; Central domain of Acyl-CoA dehydrogenase has a beta-barrel fold.


Pssm-ID: 460685 [Multi-domain]  Cd Length: 95  Bit Score: 107.75  E-value: 7.45e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1253006504 122 AIGMTEPGAGSDLQAMRTNAILQDD-HYVLNGSKTFISNGQHADLVVLAVKTDPQARAKGVSLMLVDTHLEGFKKGTNLE 200
Cdd:pfam02770   1 AFALTEPGAGSDVASLKTTAADGDGgGWVLNGTKWWITNAGIADLFLVLARTGGDDRHGGISLFLVPKDAPGVSVRRIET 80

                          90
                  ....*....|....*
gi 1253006504 201 KIGLHSQDTSELFFD 215
Cdd:pfam02770  81 KLGVRGLPTGELVFD 95
AidB cd01154
Proteins involved in DNA damage response, similar to the AidB gene product; AidB is one of ...
 78-377 1.34e-27

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: 112.46  E-value: 1.34e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1253006504  78 AGY--SALSTGISCHSEI---AAPYILHIGTEEQKQYWLPKMVSGE---VVGAIGMTEPGAGSDLQAMRTNAILQ-DDHY 148
Cdd:cd01154    98 AGYllSDAAAGLLCPLTMtdaAVYALRKYGPEELKQYLPGLLSDRYktgLLGGTWMTEKQGGSDLGANETTAERSgGGVY 177

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1253006504 149 VLNGSKTFISNGQhADL-VVLAVKTDPQARAKGVSLMLVDTHLE-GFKKGTNLE----KIGLHSQDTSELFFDNVKVpkn 222
Cdd:cd01154   178 RLNGHKWFASAPL-ADAaLVLARPEGAPAGARGLSLFLVPRLLEdGTRNGYRIRrlkdKLGTRSVATGEVEFDDAEA--- 253

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1253006504 223 QLLGQAGHGFAYLMQELPRERTAIAATALGAIRGSIDVTTQYVQERQAFGQAIGQFQNTRFVLAQAKID-ELATAAFYNQ 301
Cdd:cd01154   254 YLIGDEGKGIYYILEMLNISRLDNAVAALGIMRRALSEAYHYARHRRAFGKPLIDHPLMRRDLAEMEVDvEAATALTFRA 333

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1253006504 302 NVELYMQGKLDVETA-------AALKSFATDMQMKIADQLLQLFGGYGYMTEYPISRFFVDARIQRIYGGTNEIMKEIVA 374
Cdd:cd01154   334 ARAFDRAAADKPVEAhmarlatPVAKLIACKRAAPVTSEAMEVFGGNGYLEEWPVARLHREAQVTPIWEGTGNIQALDVL 413


                  ...
gi 1253006504 375 RGL 377
Cdd:cd01154   414 RVL 416
DszC cd01163
Dibenzothiophene (DBT) desulfurization enzyme C; DszC is a flavin reductase dependent enzyme, ...
 11-357 5.55e-22

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: 96.24  E-value: 5.55e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1253006504  11 FRDNFRRfmqehIAPHYAAWEREGIMPRSVWNLLGENGFLCIDVPEEYGGYGVPTHYSLMLVEESARAGySALSTGISCH 90
Cdd:cd01163     3 ARPLAAR-----IAEGAAERDRQRGLPYEEVALLRQSGLGTLRVPKEYGGLGASLPDLYEVVRELAAAD-SNIAQALRAH 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1253006504  91 SEIAAPyILHIGTEEQKQYWLPKMVSGEVVGaigmtepGAGSDLQAMRTNAIL-----QDDHYVLNGSKTFISNGQHADL 165
Cdd:cd01163    77 FGFVEA-LLLAGPEQFRKRWFGRVLNGWIFG-------NAVSERGSVRPGTFLtatvrDGGGYVLNGKKFYSTGALFSDW 148

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1253006504 166 VVLAVkTDPQARAKGVslmLVDTHLEGFKKGTNLEKIGLHSQDTSELFFDNVKVPKNQLLGQAGHGFAylmqelPRERTA 245
Cdd:cd01163   149 VTVSA-LDEEGKLVFA---AVPTDRPGITVVDDWDGFGQRLTASGTVTFDNVRVEPDEVLPRPNAPDR------GTLLTA 218

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1253006504 246 I-----AATALGAIRGSIDVTTQYVQER-------------------QAFGQAIGQFQNTRFVLAQA--KIDELATAAFY 299
Cdd:cd01163   219 IyqlvlAAVLAGIARAALDDAVAYVRSRtrpwihsgaesarddpyvqQVVGDLAARLHAAEALVLQAarALDAAAAAGTA 298

                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1253006504 300 NQNVELymqGKLDVETAAAlKSFATDMQMKIADQLLQLFGGYGYMTEYPISRFFVDAR 357
Cdd:cd01163   299 LTAEAR---GEAALAVAAA-KVVVTRLALDATSRLFEVGGASATAREHNLDRHWRNAR 352
PLN02876 PLN02876
acyl-CoA dehydrogenase
 98-368 8.40e-21

acyl-CoA dehydrogenase


Pssm-ID: 215473 [Multi-domain]  Cd Length: 822  Bit Score: 94.48  E-value: 8.40e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1253006504  98 ILHIGTEEQKQYWLPKMVSGEVVGAIGMTEPG-AGSDLQAMRTNAILQDDHYVLNGSKTFISNGQHADLVVLAV--KTDP 174
Cdd:PLN02876  529 LLRYGNKEQQLEWLIPLLEGKIRSGFAMTEPQvASSDATNIECSIRRQGDSYVINGTKWWTSGAMDPRCRVLIVmgKTDF 608

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1253006504 175 QA-RAKGVSLMLVDTHLEGFKKGTNLEKIGL----HSQdtSELFFDNVKVP-KNQLLGQaGHGFAYLMQELPRERTAIAA 248
Cdd:PLN02876  609 NApKHKQQSMILVDIQTPGVQIKRPLLVFGFddapHGH--AEISFENVRVPaKNILLGE-GRGFEIAQGRLGPGRLHHCM 685

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1253006504 249 TALGAIRGSIDVTTQYVQERQAFGQAIGQFQNTRFVLAQAKID-ELATAAFYNQNVELYMQG-KLDVETAAALKSFATDM 326
Cdd:PLN02876  686 RLIGAAERGMQLMVQRALSRKAFGKLIAQHGSFLSDLAKCRVElEQTRLLVLEAADQLDRLGnKKARGIIAMAKVAAPNM 765

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|..
gi 1253006504 327 QMKIADQLLQLFGGYGYMTEYPISRFFVDARIQRIYGGTNEI 368
Cdd:PLN02876  766 ALKVLDMAMQVHGAAGVSSDTVLAHLWATARTLRIADGPDEV 807
AXO cd01150
Peroxisomal acyl-CoA oxidase; Peroxisomal acyl-CoA oxidases (AXO) catalyze the first set in ...
 48-380 4.00e-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: 88.93  E-value: 4.00e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1253006504  48 GFLCIDVPEEYggygvpthYSLMlveESARAGYSALSTGISCHSEIAAPYILHIGTEEQKQYWLPKMVSGEVVGAIGMTE 127
Cdd:cd01150    74 GELMADDPEKM--------LALT---NSLGGYDLSLGAKLGLHLGLFGNAIKNLGTDEHQDYWLQGANNLEIIGCFAQTE 142

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1253006504 128 PGAGSDLQAMRTNAIL--QDDHYVLN-----GSKTFISN-GQHADLVVLAVKTDPQARAKGVSLMLV-----DTH--LEG 192
Cdd:cd01150   143 LGHGSNLQGLETTATYdpLTQEFVINtpdftATKWWPGNlGKTATHAVVFAQLITPGKNHGLHAFIVpirdpKTHqpLPG 222

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1253006504 193 FKKGTNLEKIGLHSQDTSELFFDNVKVPKNQLLGQAGH----------------GFAYLMQELPRERTAIAATALGAIRG 256
Cdd:cd01150   223 VTVGDIGPKMGLNGVDNGFLQFRNVRIPRENLLNRFGDvspdgtyvspfkdpnkRYGAMLGTRSGGRVGLIYDAAMSLKK 302

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1253006504 257 SIDVTTQYVQERQAFGQAIG---------QFQNTRFV--LAQAKIDELATAAFYNQNVELYMQGKLDVET--------AA 317
Cdd:cd01150   303 AATIAIRYSAVRRQFGPKPSdpevqildyQLQQYRLFpqLAAAYAFHFAAKSLVEMYHEIIKELLQGNSEllaelhalSA 382

                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1253006504 318 ALKSFATDMQMKIADQLLQLFGGYGYMTEYPISRFFVDARIQRIYGGTNEIMKEIVARGLLGR 380
Cdd:cd01150   383 GLKAVATWTAAQGIQECREACGGHGYLAMNRLPTLRDDNDPFCTYEGDNTVLLQQTANYLLKK 445
PRK13026 PRK13026
acyl-CoA dehydrogenase; Reviewed
 36-279 7.43e-19

acyl-CoA dehydrogenase; Reviewed


Pssm-ID: 237277 [Multi-domain]  Cd Length: 774  Bit Score: 88.48  E-value: 7.43e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1253006504  36 MPRSVWNLLGENGFLCIDVPEEYGGYGVpthyslmlveeSARAgYSALSTGISCHSEIAA----------P--YILHIGT 103
Cdd:PRK13026  109 LPPEVWDYLKKEGFFALIIPKEYGGKGF-----------SAYA-NSTIVSKIATRSVSAAvtvmvpnslgPgeLLTHYGT 176

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1253006504 104 EEQKQYWLPKMVSGEVVGAIGMTEPGAGSDLQAMRTNAIL-QDDH-------YVLNGSKTFISNGQHADLVVLAVKT-DP 174
Cdd:PRK13026  177 QEQKDYWLPRLADGTEIPCFALTGPEAGSDAGAIPDTGIVcRGEFegeevlgLRLTWDKRYITLAPVATVLGLAFKLrDP 256

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1253006504 175 QA-----RAKGVSLMLVDTHLEG-------------FKKGTNLEKiglhsqdtselffdNVKVPKNQLLG---QAGHGFA 233
Cdd:PRK13026  257 DGllgdkKELGITCALIPTDHPGveigrrhnplgmaFMNGTTRGK--------------DVFIPLDWIIGgpdYAGRGWR 322

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*...
gi 1253006504 234 YLMQELPRERtAIAATALGAIRGSIDV--TTQYVQERQAFGQAIGQFQ 279
Cdd:PRK13026  323 MLVECLSAGR-GISLPALGTASGHMATrtTGAYAYVRRQFGMPIGQFE 369
fadE PRK09463
acyl-CoA dehydrogenase; Reviewed
 36-287 2.30e-18

acyl-CoA dehydrogenase; Reviewed


Pssm-ID: 236528 [Multi-domain]  Cd Length: 777  Bit Score: 86.79  E-value: 2.30e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1253006504  36 MPRSVWNLLGENGFLCIDVPEEYGGYGVpthyslmlveeSARAgYSALSTGISCHSEIAA----------P--YILHIGT 103
Cdd:PRK09463  110 LPPEVWQFIKEHGFFGMIIPKEYGGLEF-----------SAYA-HSRVLQKLASRSGTLAvtvmvpnslgPgeLLLHYGT 177

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1253006504 104 EEQKQYWLPKMVSGEVVGAIGMTEPGAGSDLQAMRTNAILQDDHYV--------LNGSKTFISNGQHADLVVLAVKT-DP 174
Cdd:PRK09463  178 DEQKDHYLPRLARGEEIPCFALTSPEAGSDAGSIPDTGVVCKGEWQgeevlgmrLTWNKRYITLAPIATVLGLAFKLyDP 257

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1253006504 175 Q-----ARAKGVSLMLVDTHLEGFKKGTNLEKIGLHsqdtselfFDN-------VKVPKNQLLG---QAGHGFAYLMQEL 239
Cdd:PRK09463  258 DgllgdKEDLGITCALIPTDTPGVEIGRRHFPLNVP--------FQNgptrgkdVFIPLDYIIGgpkMAGQGWRMLMECL 329

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|
gi 1253006504 240 PRERtAIA--ATALGAIRGSIDVTTQYVQERQAFGQAIGQFQNTRFVLAQ 287
Cdd:PRK09463  330 SVGR-GISlpSNSTGGAKLAALATGAYARIRRQFKLPIGKFEGIEEPLAR 378
NcnH cd01159
Naphthocyclinone hydroxylase; Naphthocyclinone is an aromatic polyketide and an antibiotic, ...
 23-379 1.34e-13

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


Pssm-ID: 173848 [Multi-domain]  Cd Length: 370  Bit Score: 71.23  E-value: 1.34e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1253006504  23 IAPHYAAWEREGIMPRSVWNLLGENGFLCIDVPEEYGGYGVPTHYSLMLVEESARA-GYSALSTGISC-HSEIAApyilH 100
Cdd:cd01159    10 IRERAPEAERARRLPDEVVRALREIGFFRMFVPKRYGGLEGDFAEFAEAIATLAEAcGSAAWVASIVAtHSRMLA----A 85

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1253006504 101 IGTEEQKQYWL--PKMVSGEVVGAIGMTEPGAGSdlqamrtnailqddhYVLNGSKTFISNGQHADLVVLAVKTDPQARA 178
Cdd:cd01159    86 FPPEAQEEVWGdgPDTLLAGSYAPGGRAERVDGG---------------YRVSGTWPFASGCDHADWILVGAIVEDDDGG 150

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1253006504 179 KGVSLMLVDTHleGFKKGTNLEKIGLHSQDTSELFFDNVKVPKNQLL----GQAGHG-----FAYLMQELPRERTAIAAT 249
Cdd:cd01159   151 PLPRAFVVPRA--EYEIVDTWHVVGLRGTGSNTVVVDDVFVPEHRTLtagdMMAGDGpggstPVYRMPLRQVFPLSFAAV 228

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1253006504 250 ALGAIRGSIDVTTQYVQER-QAFGQAIGQFQN--TRFVLAQAKIDELATAAFYNQNVELYMQGKL-----DVETAAALK- 320
Cdd:cd01159   229 SLGAAEGALAEFLELAGKRvRQYGAAVKMAEApiTQLRLAEAAAELDAARAFLERATRDLWAHALaggpiDVEERARIRr 308

                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1253006504 321 --SFATDMQMKIADQLLQLFGGYGYMTEYPISRFFVDARIQRIYGGTN-EIMKEIVARGLLG 379
Cdd:cd01159   309 daAYAAKLSAEAVDRLFHAAGGSALYTASPLQRIWRDIHAAAQHAALNpETAAEAYGRALLG 370
Acyl-CoA_dh_2 pfam08028
Acyl-CoA dehydrogenase, C-terminal domain;
246-367 2.20e-13

Acyl-CoA dehydrogenase, C-terminal domain;


Pssm-ID: 429790 [Multi-domain]  Cd Length: 133  Bit Score: 66.60  E-value: 2.20e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1253006504 246 IAATALGAIRGSIDVTTQYVQERQ--AFGQAIGQFQNTRFVLAQAKIDELATAAFYNQNVELYM----QGK----LDVET 315
Cdd:pfam08028   2 IAAAALGAARAALAEFTERARGRVraYFGVPLAEDPATQLALAEAAARIDAARLLLERAAARIEaaaaAGKpvtpALRAE 81

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1253006504 316 AAALKSFATDMQMKIADQLLQLFGGYGYMTEYPISRFFVDARIQRIYGGTNE 367
Cdd:pfam08028  82 ARRAAAFATELAVAAVDALFRAAGGSALFQDSPLQRIWRDIHAAAQHAAVNP 133
PLN02636 PLN02636
acyl-coenzyme A oxidase
 98-380 6.35e-11

acyl-coenzyme A oxidase


Pssm-ID: 215342 [Multi-domain]  Cd Length: 686  Bit Score: 63.72  E-value: 6.35e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1253006504  98 ILHIGTEEQKQYWLPKMVSGEVVGAIGMTEPGAGSDLQAMRTNAILQ--DDHYVLN-----GSKTFISNGQ-HADLV-VL 168
Cdd:PLN02636  152 VINLGTKKHRDKYFDGIDNLDYPGCFAMTELHHGSNVQGLQTTATFDplTDEFVINtpndgAIKWWIGNAAvHGKFAtVF 231

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1253006504 169 AVKTDPQARAKGVSLMLV----------DTH--LEGFKKGTNLEKIGLHSQDTSELFFDNVKVPKNQLLGQAG------- 229
Cdd:PLN02636  232 ARLKLPTHDSKGVSDMGVhafivpirdmKTHqvLPGVEIRDCGHKVGLNGVDNGALRFRSVRIPRDNLLNRFGdvsrdgk 311

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1253006504 230 ---------HGFAYLMQELPRERTAIAATALGAIRGSIDVTTQYVQERQAFGQ------AIGQFQNTRF----VLAQAKI 290
Cdd:PLN02636  312 ytsslptinKRFAATLGELVGGRVGLAYGSVGVLKASNTIAIRYSLLRQQFGPpkqpeiSILDYQSQQHklmpMLASTYA 391

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1253006504 291 DELATAAFynqnVELYMQGKL--------DVET-AAALKSFATDMQMKIADQLLQLFGGYGYMTeypISRFFV---DARI 358
Cdd:PLN02636  392 FHFATEYL----VERYSEMKKthddqlvaDVHAlSAGLKAYITSYTAKALSTCREACGGHGYAA---VNRFGSlrnDHDI 464

                         330       340
                  ....*....|....*....|..
gi 1253006504 359 QRIYGGTNEIMKEIVARGLLGR 380
Cdd:PLN02636  465 FQTFEGDNTVLLQQVAADLLKQ 486
PLN02443 PLN02443
acyl-coenzyme A oxidase
 96-378 7.38e-11

acyl-coenzyme A oxidase


Pssm-ID: 178062 [Multi-domain]  Cd Length: 664  Bit Score: 63.70  E-value: 7.38e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1253006504  96 PYILHIGTEEQKQYWLPKMVSGEVVGAIGMTEPGAGSDLQAMRTNAIL--QDDHYVLNgSKTFISN-------GQHADLV 166
Cdd:PLN02443  108 PAIKGQGTEEQQKKWLPLAYKMQIIGCYAQTELGHGSNVQGLETTATFdpKTDEFVIH-SPTLTSSkwwpgglGKVSTHA 186

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1253006504 167 VLAVKTDPQARAKGVSLMLV-----DTH--LEGFKKGTNLEKIG---LHSQDTSELFFDNVKVPKNQLL---GQAGHGFA 233
Cdd:PLN02443  187 VVYARLITNGKDHGIHGFIVqlrslDDHspLPGVTVGDIGMKFGngaYNTMDNGFLRFDHVRIPRDQMLmrlSKVTREGK 266

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1253006504 234 YLMQELPRE---------RTAIAATALGAIRGSIDVTTQYVQERQAFGQAIG--QFQNTRFVLAQAKIDELATAAFYNQN 302
Cdd:PLN02443  267 YVQSDVPRQlvygtmvyvRQTIVADASTALSRAVCIATRYSAVRRQFGSQDGgpETQVIDYKTQQSRLFPLLASAYAFRF 346

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1253006504 303 VELYMQ-------GKL---DVET-------AAALKSFATDMQMKIADQLLQLFGGYGYMTEYPISRFFVDARIQRIYGGT 365
Cdd:PLN02443  347 VGEWLKwlytdvtQRLeanDFSTlpeahacTAGLKSLTTSATADGIEECRKLCGGHGYLCSSGLPELFAVYVPACTYEGD 426

                         330
                  ....*....|...
gi 1253006504 366 NEIMKEIVARGLL 378
Cdd:PLN02443  427 NVVLLLQVARFLM 439
PTZ00460 PTZ00460
acyl-CoA dehydrogenase; Provisional
 64-378 9.48e-10

acyl-CoA dehydrogenase; Provisional


Pssm-ID: 185639 [Multi-domain]  Cd Length: 646  Bit Score: 60.24  E-value: 9.48e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1253006504  64 PTHYSLMLVeesaragYSALSTGISCHSEIAAPYILHIGTEEQKQYWLPKMVSGEVVGAIGMTEPGAGSDLQAMRTNAIL 143
Cdd:PTZ00460   79 PNYYTPNLL-------CPQGTFISTVHFAMVIPAFQVLGTDEQINLWMPSLLNFEIVGCYAQTELGHGSDVQNLETTATY 151

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1253006504 144 --QDDHYVLN-----------GSKTFISNGQ--HADLVVlavktdpQARAKGVSLMLV-----DTH--LEGFKKGTNLEK 201
Cdd:PTZ00460  152 dkQTNEFVIHtpsveavkfwpGELGFLCNFAlvYAKLIV-------NGKNKGVHPFMVrirdkETHkpLQGVEVGDIGPK 224

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1253006504 202 IGLHSQDTSELFFDNVKVPKNQLL---------------GQAGHGFAYLM---QELPRERTAIAATALG-AIRGSIdvtt 262
Cdd:PTZ00460  225 MGYAVKDNGFLSFDHYRIPLDSLLaryikvsedgqverqGNPKVSYASMMymrNLIIDQYPRFAAQALTvAIRYSI---- 300

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1253006504 263 qyvqERQAF----GQAIG----QFQNTRF----------VLAQAKIDELATAAFYNQNVELYMQGKLDVETAAALKSFAT 324
Cdd:PTZ00460  301 ----YRQQFtndnKQENSvleyQTQQQKLlpllaefyacIFGGLKIKELVDDNFNRVQKNDFSLLQLTHAILSAAKANYT 376

                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1253006504 325 DMQMKIADQLLQLFGGYGYMTEYPISRFFVDARIQRIYGGTNEIMKEIVARGLL 378
Cdd:PTZ00460  377 YFVSNCAEWCRLSCGGHGYAHYSGLPAIYFDMSPNITLEGENQIMYLQLARYLL 430
PRK11561 PRK11561
isovaleryl CoA dehydrogenase; Provisional
 123-369 4.83e-07

isovaleryl CoA dehydrogenase; Provisional


Pssm-ID: 183199 [Multi-domain]  Cd Length: 538  Bit Score: 51.68  E-value: 4.83e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1253006504 123 IGMTEPGAGSDLQAMRTNA-ILQDDHYVLNGSKTFISNGQHADLVVLAvktdpQARAkGVSLMLVDTHL-EGFKKGTNLE 200
Cdd:PRK11561  182 MGMTEKQGGSDVLSNTTRAeRLADGSYRLVGHKWFFSVPQSDAHLVLA-----QAKG-GLSCFFVPRFLpDGQRNAIRLE 255

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1253006504 201 ----KIGLHSQDTSELFFDNVkvpKNQLLGQAGHGFAYLMQELPRERTAIAATALGAIRGSIDVTTQYVQERQAFGQAIG 276
Cdd:PRK11561  256 rlkdKLGNRSNASSEVEFQDA---IGWLLGEEGEGIRLILKMGGMTRFDCALGSHGLMRRAFSVAIYHAHQRQVFGKPLI 332

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1253006504 277 QFQNTRFVLAQ---------AKIDELATAafYNQNVELYMQGKLDVETAAAlKSFATDMQMKIADQLLQLFGGYGYMTEY 347
Cdd:PRK11561  333 EQPLMRQVLSRmalqlegqtALLFRLARA--WDRRADAKEALWARLFTPAA-KFVICKRGIPFVAEAMEVLGGIGYCEES 409

                         250       260
                  ....*....|....*....|..
gi 1253006504 348 PISRFFVDARIQRIYGGTNEIM 369
Cdd:PRK11561  410 ELPRLYREMPVNSIWEGSGNIM 431
PLN02312 PLN02312
acyl-CoA oxidase
 98-379 1.73e-05

acyl-CoA oxidase


Pssm-ID: 215178 [Multi-domain]  Cd Length: 680  Bit Score: 46.69  E-value: 1.73e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1253006504  98 ILHIGTEEQKQYWLPKMVSGEVVGAIGMTEPGAGSDLQAMRTNAI--LQDDHYVLN-----GSKTFISNG-QHADLVVLA 169
Cdd:PLN02312  164 IKFLGTKRHHDKWLKDTEDYVVKGCFAMTELGHGSNVRGIETVTTydPKTEEFVINtpcesAQKYWIGGAaNHATHTIVF 243

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1253006504 170 VKTDPQARAKGVSLMLV---DTH---LEGFKKGTNLEKIGLHSQDTSELFFDNVKVPKNQLL---------GQ------- 227
Cdd:PLN02312  244 SQLHINGKNEGVHAFIAqirDQDgniCPNIRIADCGHKIGLNGVDNGRIWFDNLRIPRENLLnsvadvspdGKyvsaikd 323

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1253006504 228 AGHGFAYLMQELPRERTAIAATALGAIRGSIDVTTQYVQERQAFGQAIGQFQ---------NTRFVLAQAKIDELATAAF 298
Cdd:PLN02312  324 PDQRFGAFLAPLTSGRVTIAVSAIYSSKVGLAIAIRYSLSRRAFSVTPNGPEvllldypshQRRLLPLLAKTYAMSFAAN 403

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1253006504 299 YNQNveLYMQGKLDVETA-----AALKSFATDMQMKIADQLLQLFGGYGYMTEYPISRFFVDARIQRIYGGTNEIMKEIV 373
Cdd:PLN02312  404 DLKM--IYVKRTPESNKAihvvsSGFKAVLTWHNMRTLQECREACGGQGLKTENRVGQLKAEYDVQSTFEGDNNVLMQQV 481


                  ....*.
gi 1253006504 374 ARGLLG 379
Cdd:PLN02312  482 SKALLA 487
PTZ00457 PTZ00457
acyl-CoA dehydrogenase; Provisional
 57-255 3.55e-05

acyl-CoA dehydrogenase; Provisional


Pssm-ID: 185636 [Multi-domain]  Cd Length: 520  Bit Score: 45.64  E-value: 3.55e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1253006504  57 EYGGYGVPTHYSLMLVEESARAGYSALSTGIScHSEIAAPYILHIGTEEQKQYWLPKMVSGEVVGAIGmTEPGAGSDLQA 136
Cdd:PTZ00457   73 EYGGLGLGHTAHALIYEEVGTNCDSKLLSTIQ-HSGFCTYLLSTVGSKELKGKYLTAMSDGTIMMGWA-TEEGCGSDISM 150

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1253006504 137 MRTNAILQDD-HYVLNGSKTFISNGQHADLVVLAvKTDPQaRAKGVSLMLVDTH----LEGFKKGTNLEKIGLHSQDTse 211
Cdd:PTZ00457  151 NTTKASLTDDgSYVLTGQKRCEFAASATHFLVLA-KTLTQ-TAAEEGATEVSRNsffiCAKDAKGVSVNGDSVVFENT-- 226

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....
gi 1253006504 212 lffdnvkvPKNQLLGQAGHGFAYLMQELPRERTAIAATALGAIR 255
Cdd:PTZ00457  227 --------PAADVVGVVGEGFKDAMITLFTEQYLYAASLLGIMK 262
 
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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