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Conserved domains on  [gi|700674279|ref|NP_001289483|]
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short-chain specific acyl-CoA dehydrogenase, mitochondrial isoform 2 precursor [Homo sapiens]

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 ...
 36-404 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: 574.99  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 700674279  36 ETHQMLLQTCRDFAEKELFPIAAQVDKEHLFPAAQVKKMGGLGLLAMDVPEELGGAGLDYLAYAIAMEEISRGCASTGVI 115
Cdd:cd01158    1 EEHQMIRKTVRDFAEKEIAPLAAEMDEKGEFPREVIKEMAELGLMGIPIPEEYGGAGLDFLAYAIAIEELAKVDASVAVI 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 700674279 116 MSVNNSLYLGPILKFGSKEQKQAWVTPFTSGDKIGCFALSEPG-----PSL---LGPTGPIFALGqvGCPCPSSAATEAC 187
Cdd:cd01158   81 VSVHNSLGANPIIKFGTEEQKKKYLPPLATGEKIGAFALSEPGagsdaAALkttAKKDGDDYVLN--GSKMWITNGGEAD 158

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 700674279 188 TFprSRQRVSRPELLREGISAFLVPMPTPGLTLGKKEDKLGIRGSSTANLIFEDCRIPKDSILGEPGMGFKIAMQTLDMG 267
Cdd:cd01158  159 FY--IVFAVTDPSKGYRGITAFIVERDTPGLSVGKKEDKLGIRGSSTTELIFEDVRVPKENILGEEGEGFKIAMQTLDGG 236

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 700674279 268 RIGIASQALGIAQTALDCAVNYAENRMAFGAPLTKLQVIQFKLADMALALESARLLTWRAAMLKDNKKPFIKEAAMAKLA 347
Cdd:cd01158  237 RIGIAAQALGIAQAALDAAVDYAKERKQFGKPIADFQGIQFKLADMATEIEAARLLTYKAARLKDNGEPFIKEAAMAKLF 316

                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 700674279 348 ASEAATAISHQAIQILGGMGYVTEMPAERHYRDARITEIYEGTSEIQRLVIAGHLLR 404
Cdd:cd01158  317 ASEVAMRVTTDAVQIFGGYGYTKDYPVERYYRDAKITEIYEGTSEIQRLVIAKHLLK 373
 
Name Accession Description Interval E-value
SCAD_SBCAD cd01158
Short chain acyl-CoA dehydrogenases and eukaryotic short/branched chain acyl-CoA ...
 36-404 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: 574.99  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 700674279  36 ETHQMLLQTCRDFAEKELFPIAAQVDKEHLFPAAQVKKMGGLGLLAMDVPEELGGAGLDYLAYAIAMEEISRGCASTGVI 115
Cdd:cd01158    1 EEHQMIRKTVRDFAEKEIAPLAAEMDEKGEFPREVIKEMAELGLMGIPIPEEYGGAGLDFLAYAIAIEELAKVDASVAVI 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 700674279 116 MSVNNSLYLGPILKFGSKEQKQAWVTPFTSGDKIGCFALSEPG-----PSL---LGPTGPIFALGqvGCPCPSSAATEAC 187
Cdd:cd01158   81 VSVHNSLGANPIIKFGTEEQKKKYLPPLATGEKIGAFALSEPGagsdaAALkttAKKDGDDYVLN--GSKMWITNGGEAD 158

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 700674279 188 TFprSRQRVSRPELLREGISAFLVPMPTPGLTLGKKEDKLGIRGSSTANLIFEDCRIPKDSILGEPGMGFKIAMQTLDMG 267
Cdd:cd01158  159 FY--IVFAVTDPSKGYRGITAFIVERDTPGLSVGKKEDKLGIRGSSTTELIFEDVRVPKENILGEEGEGFKIAMQTLDGG 236

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 700674279 268 RIGIASQALGIAQTALDCAVNYAENRMAFGAPLTKLQVIQFKLADMALALESARLLTWRAAMLKDNKKPFIKEAAMAKLA 347
Cdd:cd01158  237 RIGIAAQALGIAQAALDAAVDYAKERKQFGKPIADFQGIQFKLADMATEIEAARLLTYKAARLKDNGEPFIKEAAMAKLF 316

                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 700674279 348 ASEAATAISHQAIQILGGMGYVTEMPAERHYRDARITEIYEGTSEIQRLVIAGHLLR 404
Cdd:cd01158  317 ASEVAMRVTTDAVQIFGGYGYTKDYPVERYYRDAKITEIYEGTSEIQRLVIAKHLLK 373
CaiA COG1960
Acyl-CoA dehydrogenase related to the alkylation response protein AidB [Lipid transport and ...
 33-407 2.33e-142

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: 410.39  E-value: 2.33e-142
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 700674279  33 ELPETHQMLLQTCRDFAEKELFPIAAQVDKEHLFPAAQVKKMGGLGLLAMDVPEELGGAGLDYLAYAIAMEEISRGCAST 112
Cdd:COG1960    4 ELTEEQRALRDEVREFAEEEIAPEAREWDREGEFPRELWRKLAELGLLGLTIPEEYGGLGLSLVELALVLEELARADASL 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 700674279 113 GVIMSVNNSLyLGPILKFGSKEQKQAWVTPFTSGDKIGCFALSEPG----PSLLG----PTGPIFAL-GQVgcpCPSSAA 183
Cdd:COG1960   84 ALPVGVHNGA-AEALLRFGTEEQKERYLPRLASGEWIGAFALTEPGagsdAAALRttavRDGDGYVLnGQK---TFITNA 159

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 700674279 184 TEA---CTFPRSRqrvsrPELLREGISAFLVPMPTPGLTLGKKEDKLGIRGSSTANLIFEDCRIPKDSILGEPGMGFKIA 260
Cdd:COG1960  160 PVAdviLVLARTD-----PAAGHRGISLFLVPKDTPGVTVGRIEDKMGLRGSDTGELFFDDVRVPAENLLGEEGKGFKIA 234

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 700674279 261 MQTLDMGRIGIASQALGIAQTALDCAVNYAENRMAFGAPLTKLQVIQFKLADMALALESARLLTWRAAMLKDNKKPFIKE 340
Cdd:COG1960  235 MSTLNAGRLGLAAQALGIAEAALELAVAYAREREQFGRPIADFQAVQHRLADMAAELEAARALVYRAAWLLDAGEDAALE 314

                        330       340       350       360       370       380
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 700674279 341 AAMAKLAASEAATAISHQAIQILGGMGYVTEMPAERHYRDARITEIYEGTSEIQRLVIAGHLLRSYR 407
Cdd:COG1960  315 AAMAKLFATEAALEVADEALQIHGGYGYTREYPLERLYRDARILTIYEGTNEIQRLIIARRLLGRPG 381
PLN02519 PLN02519
isovaleryl-CoA dehydrogenase
 6-404 1.34e-77

isovaleryl-CoA dehydrogenase


Pssm-ID: 215284 [Multi-domain]  Cd Length: 404  Bit Score: 245.56  E-value: 1.34e-77
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 700674279   6 LARASGPARRAlcpRAWRQLHTIYQSVELPETHQMLLQTCRDFAEKELFPIAAQVDKEHLFPAAQ--VKKMGGLGLLAMD 83
Cdd:PLN02519   1 MLLSAAKARRR---GLARRFSSSSSSLLFDDTQLQFKESVQQFAQENIAPHAAAIDATNSFPKDVnlWKLMGDFNLHGIT 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 700674279  84 VPEELGGAGLDYLAYAIAMEEISRGCASTGVIMSVNNSLYLGPILKFGSKEQKQAWVTPFTSGDKIGCFALSEP--GPSL 161
Cdd:PLN02519  78 APEEYGGLGLGYLYHCIAMEEISRASGSVGLSYGAHSNLCINQLVRNGTPAQKEKYLPKLISGEHVGALAMSEPnsGSDV 157

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 700674279 162 LG--------PTGPIFALGQVGCPCPSSAAT---EACTFPRSRQRvsrpellreGISAFLVPMPTPGLTLGKKEDKLGIR 230
Cdd:PLN02519 158 VSmkckaervDGGYVLNGNKMWCTNGPVAQTlvvYAKTDVAAGSK---------GITAFIIEKGMPGFSTAQKLDKLGMR 228

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 700674279 231 GSSTANLIFEDCRIPKDSILGEPGMGFKIAMQTLDMGRIGIASQALGIAQTALDCAVNYAENRMAFGAPLTKLQVIQFKL 310
Cdd:PLN02519 229 GSDTCELVFENCFVPEENVLGQEGKGVYVMMSGLDLERLVLAAGPLGLMQACLDVVLPYVRQREQFGRPIGEFQFIQGKL 308

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 700674279 311 ADMALALESARLLTWRAAMLKDNKKPFIKEAAMAKLAASEAATAISHQAIQILGGMGYVTEMPAERHYRDARITEIYEGT 390
Cdd:PLN02519 309 ADMYTSLQSSRSYVYSVARDCDNGKVDRKDCAGVILCAAERATQVALQAIQCLGGNGYINEYPTGRLLRDAKLYEIGAGT 388

                        410
                 ....*....|....
gi 700674279 391 SEIQRLVIAGHLLR 404
Cdd:PLN02519 389 SEIRRMLIGRELFK 402
Acyl-CoA_dh_1 pfam00441
Acyl-CoA dehydrogenase, C-terminal domain; C-terminal domain of Acyl-CoA dehydrogenase is an ...
 254-399 2.72e-54

Acyl-CoA dehydrogenase, C-terminal domain; C-terminal domain of Acyl-CoA dehydrogenase is an all-alpha, four helical up-and-down bundle.


Pssm-ID: 395354 [Multi-domain]  Cd Length: 149  Bit Score: 176.68  E-value: 2.72e-54
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 700674279  254 GMGFKIAMQTLDMGRIGIASQALGIAQTALDCAVNYAENRMAFGAPLTKLQVIQFKLADMALALESARLLTWRAAMLKDN 333
Cdd:pfam00441   1 GRGFRVAMETLNHERLAIAAMALGLARRALDEALAYARRRKAFGRPLIDFQLVRHKLAEMAAEIEAARLLVYRAAEALDA 80

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 700674279  334 KKPFIKEAAMAKLAASEAATAISHQAIQILGGMGYVTEMPAERHYRDARITEIYEGTSEIQRLVIA 399
Cdd:pfam00441  81 GGPDGAEASMAKLYASEAAVEVADLAMQLHGGYGYLREYPVERLYRDARVLRIGEGTSEIQRNIIA 146
 
Name Accession Description Interval E-value
SCAD_SBCAD cd01158
Short chain acyl-CoA dehydrogenases and eukaryotic short/branched chain acyl-CoA ...
 36-404 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: 574.99  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 700674279  36 ETHQMLLQTCRDFAEKELFPIAAQVDKEHLFPAAQVKKMGGLGLLAMDVPEELGGAGLDYLAYAIAMEEISRGCASTGVI 115
Cdd:cd01158    1 EEHQMIRKTVRDFAEKEIAPLAAEMDEKGEFPREVIKEMAELGLMGIPIPEEYGGAGLDFLAYAIAIEELAKVDASVAVI 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 700674279 116 MSVNNSLYLGPILKFGSKEQKQAWVTPFTSGDKIGCFALSEPG-----PSL---LGPTGPIFALGqvGCPCPSSAATEAC 187
Cdd:cd01158   81 VSVHNSLGANPIIKFGTEEQKKKYLPPLATGEKIGAFALSEPGagsdaAALkttAKKDGDDYVLN--GSKMWITNGGEAD 158

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 700674279 188 TFprSRQRVSRPELLREGISAFLVPMPTPGLTLGKKEDKLGIRGSSTANLIFEDCRIPKDSILGEPGMGFKIAMQTLDMG 267
Cdd:cd01158  159 FY--IVFAVTDPSKGYRGITAFIVERDTPGLSVGKKEDKLGIRGSSTTELIFEDVRVPKENILGEEGEGFKIAMQTLDGG 236

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 700674279 268 RIGIASQALGIAQTALDCAVNYAENRMAFGAPLTKLQVIQFKLADMALALESARLLTWRAAMLKDNKKPFIKEAAMAKLA 347
Cdd:cd01158  237 RIGIAAQALGIAQAALDAAVDYAKERKQFGKPIADFQGIQFKLADMATEIEAARLLTYKAARLKDNGEPFIKEAAMAKLF 316

                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 700674279 348 ASEAATAISHQAIQILGGMGYVTEMPAERHYRDARITEIYEGTSEIQRLVIAGHLLR 404
Cdd:cd01158  317 ASEVAMRVTTDAVQIFGGYGYTKDYPVERYYRDAKITEIYEGTSEIQRLVIAKHLLK 373
CaiA COG1960
Acyl-CoA dehydrogenase related to the alkylation response protein AidB [Lipid transport and ...
 33-407 2.33e-142

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: 410.39  E-value: 2.33e-142
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 700674279  33 ELPETHQMLLQTCRDFAEKELFPIAAQVDKEHLFPAAQVKKMGGLGLLAMDVPEELGGAGLDYLAYAIAMEEISRGCAST 112
Cdd:COG1960    4 ELTEEQRALRDEVREFAEEEIAPEAREWDREGEFPRELWRKLAELGLLGLTIPEEYGGLGLSLVELALVLEELARADASL 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 700674279 113 GVIMSVNNSLyLGPILKFGSKEQKQAWVTPFTSGDKIGCFALSEPG----PSLLG----PTGPIFAL-GQVgcpCPSSAA 183
Cdd:COG1960   84 ALPVGVHNGA-AEALLRFGTEEQKERYLPRLASGEWIGAFALTEPGagsdAAALRttavRDGDGYVLnGQK---TFITNA 159

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 700674279 184 TEA---CTFPRSRqrvsrPELLREGISAFLVPMPTPGLTLGKKEDKLGIRGSSTANLIFEDCRIPKDSILGEPGMGFKIA 260
Cdd:COG1960  160 PVAdviLVLARTD-----PAAGHRGISLFLVPKDTPGVTVGRIEDKMGLRGSDTGELFFDDVRVPAENLLGEEGKGFKIA 234

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 700674279 261 MQTLDMGRIGIASQALGIAQTALDCAVNYAENRMAFGAPLTKLQVIQFKLADMALALESARLLTWRAAMLKDNKKPFIKE 340
Cdd:COG1960  235 MSTLNAGRLGLAAQALGIAEAALELAVAYAREREQFGRPIADFQAVQHRLADMAAELEAARALVYRAAWLLDAGEDAALE 314

                        330       340       350       360       370       380
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 700674279 341 AAMAKLAASEAATAISHQAIQILGGMGYVTEMPAERHYRDARITEIYEGTSEIQRLVIAGHLLRSYR 407
Cdd:COG1960  315 AAMAKLFATEAALEVADEALQIHGGYGYTREYPLERLYRDARILTIYEGTNEIQRLIIARRLLGRPG 381
IVD cd01156
Isovaleryl-CoA dehydrogenase; Isovaleryl-CoA dehydrogenase (IVD) is an is an acyl-CoA ...
 34-399 1.29e-100

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: 303.95  E-value: 1.29e-100
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 700674279  34 LPETHQMLLQTCRDFAEKELFPIAAQVDKEHLFPAAQVKKMGGLGLLAMDVPEELGGAGLDYLAYAIAMEEISRGCASTG 113
Cdd:cd01156    2 LDDEIEMLRQSVREFAQKEIAPLAAKIDRDNEFPRDLWRKMGKLGLLGITAPEEYGGSGMGYLAHVIIMEEISRASGSVA 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 700674279 114 VIMSVNNSLYLGPILKFGSKEQKQAWVTPFTSGDKIGCFALSEP--GPSLLG------PTGPIFALGqvGCPCPSSAATE 185
Cdd:cd01156   82 LSYGAHSNLCINQIYRNGSAAQKEKYLPKLISGEHIGALAMSEPnaGSDVVSmklraeKKGDRYVLN--GSKMWITNGPD 159

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 700674279 186 ACTFPRSRQrvSRPELLREGISAFLVPMPTPGLTLGKKEDKLGIRGSSTANLIFEDCRIPKDSILGEPGMGFKIAMQTLD 265
Cdd:cd01156  160 ADTLVVYAK--TDPSAGAHGITAFIVEKGMPGFSRAQKLDKLGMRGSNTCELVFEDCEVPEENILGGENKGVYVLMSGLD 237

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 700674279 266 MGRIGIASQALGIAQTALDCAVNYAENRMAFGAPLTKLQVIQFKLADMALALESARLLTWRAAMLKDNKKPFIKEAAMAK 345
Cdd:cd01156  238 YERLVLAGGPIGIMQAALDVAIPYAHQRKQFGQPIGEFQLVQGKLADMYTRLNASRSYLYTVAKACDRGNMDPKDAAGVI 317

                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|....
gi 700674279 346 LAASEAATAISHQAIQILGGMGYVTEMPAERHYRDARITEIYEGTSEIQRLVIA 399
Cdd:cd01156  318 LYAAEKATQVALDAIQILGGNGYINDYPTGRLLRDAKLYEIGAGTSEIRRMVIG 371
ACAD cd00567
Acyl-CoA dehydrogenase; Both mitochondrial acyl-CoA dehydrogenases (ACAD) and peroxisomal ...
 36-399 7.21e-96

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: 289.95  E-value: 7.21e-96
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 700674279  36 ETHQMLLQTCRDFAEKELFPIAAQVDKEHLFPAAQVKKMGglgllamdvpeELGGAGldylayaiameeisrgcastgvi 115
Cdd:cd00567    1 EEQRELRDSAREFAAEELEPYARERRETPEEPWELLAELG-----------LLLGAA----------------------- 46

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 700674279 116 msvnnslylgPILKFGSKEQKQAWVTPFTSGDKIGCFALSEPGpsllgpTGPIFALGQV------------GCPCPSSAA 183
Cdd:cd00567   47 ----------LLLAYGTEEQKERYLPPLASGEAIAAFALTEPG------AGSDLAGIRTtarkdgdgyvlnGRKIFISNG 110

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 700674279 184 TEA---CTFprsrQRVSRPELLREGISAFLVPMPTPGLTLGKKEDKLGIRGSSTANLIFEDCRIPKDSILGEPGMGFKIA 260
Cdd:cd00567  111 GDAdlfIVL----ARTDEEGPGHRGISAFLVPADTPGVTVGRIWDKMGMRGSGTGELVFDDVRVPEDNLLGEEGGGFELA 186

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 700674279 261 MQTLDMGRIGIASQALGIAQTALDCAVNYAENRMAFGAPLTKLQVIQFKLADMALALESARLLTWRAAMLKDNKKPFI-K 339
Cdd:cd00567  187 MKGLNVGRLLLAAVALGAARAALDEAVEYAKQRKQFGKPLAEFQAVQFKLADMAAELEAARLLLYRAAWLLDQGPDEArL 266

                        330       340       350       360       370       380
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 700674279 340 EAAMAKLAASEAATAISHQAIQILGGMGYVTEMPAERHYRDARITEIYEGTSEIQRLVIA 399
Cdd:cd00567  267 EAAMAKLFATEAAREVADLAMQIHGGRGYSREYPVERYLRDARAARIAEGTAEIQRLIIA 326
IBD cd01162
Isobutyryl-CoA dehydrogenase; Isobutyryl-CoA dehydrogenase (IBD) catalyzes the alpha, beta- ...
 34-404 3.34e-91

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: 279.71  E-value: 3.34e-91
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 700674279  34 LPETHQMLLQTCRDFAEKELFPIAAQVDKEHLFPAAQVKKMGGLGLLAMDVPEELGGAGLDYLAYAIAMEEISRGCASTG 113
Cdd:cd01162    1 LNEEQRAIQEVARAFAAKEMAPHAADWDQKKHFPVDVLRKAAELGFGGIYIRDDVGGSGLSRLDASIIFEALSTGCVSTA 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 700674279 114 VIMSVNNsLYLGPILKFGSKEQKQAWVTPFTSGDKIGCFALSEPGP-----SLLGPT---GPIFALGQVGCPCpSSAATE 185
Cdd:cd01162   81 AYISIHN-MCAWMIDSFGNDEQRERFLPDLCTMEKLASYCLTEPGSgsdaaALRTRAvreGDHYVLNGSKAFI-SGAGDS 158

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 700674279 186 ACTFPRSRQRVSRPEllreGISAFLVPMPTPGLTLGKKEDKLGIRGSSTANLIFEDCRIPKDSILGEPGMGFKIAMQTLD 265
Cdd:cd01162  159 DVYVVMARTGGEGPK----GISCFVVEKGTPGLSFGANEKKMGWNAQPTRAVIFEDCRVPVENRLGGEGQGFGIAMAGLN 234

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 700674279 266 MGRIGIASQALGIAQTALDCAVNYAENRMAFGAPLTKLQVIQFKLADMALALESARLLTWRAAMLKDNKKP-FIKEAAMA 344
Cdd:cd01162  235 GGRLNIASCSLGAAQAALDLARAYLEERKQFGKPLADFQALQFKLADMATELVASRLMVRRAASALDRGDPdAVKLCAMA 314

                        330       340       350       360       370       380
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 700674279 345 KLAASEAATAISHQAIQILGGMGYVTEMPAERHYRDARITEIYEGTSEIQRLVIAGHLLR 404
Cdd:cd01162  315 KRFATDECFDVANQALQLHGGYGYLKDYPVEQYVRDLRVHQILEGTNEIMRLIIARALLT 374
VLCAD cd01161
Very long chain acyl-CoA dehydrogenase; VLCAD is an acyl-CoA dehydrogenase (ACAD), which is ...
 33-406 9.41e-86

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: 267.03  E-value: 9.41e-86
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 700674279  33 ELPETHQMLLQTCRDFAEKELFPiaAQVDKEHLFPAAQVKKMGGLGLLAMDVPEELGGAGLDYLAYAIAMEEISRGcAST 112
Cdd:cd01161   26 EQTEELNMLVGPVEKFFEEVNDP--AKNDQLEKIPRKTLTQLKELGLFGLQVPEEYGGLGLNNTQYARLAEIVGMD-LGF 102

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 700674279 113 GVIMSVNNSLYLGPILKFGSKEQKQAWVTPFTSGDKIGCFALSEPGP----------SLLGPTGPIFALGQVGCPCPSSA 182
Cdd:cd01161  103 SVTLGAHQSIGFKGILLFGTEAQKEKYLPKLASGEWIAAFALTEPSSgsdaasirttAVLSEDGKHYVLNGSKIWITNGG 182

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 700674279 183 ATEACT-FPRSRQRVSRPELlREGISAFLVPMPTPGLTLGKKEDKLGIRGSSTANLIFEDCRIPKDSILGEPGMGFKIAM 261
Cdd:cd01161  183 IADIFTvFAKTEVKDATGSV-KDKITAFIVERSFGGVTNGPPEKKMGIKGSNTAEVYFEDVKIPVENVLGEVGDGFKVAM 261

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 700674279 262 QTLDMGRIGIASQALGIAQTALDCAVNYAENRMAFGAPLTKLQVIQFKLADMALALESARLLTWRAAMLKDN--KKPFIK 339
Cdd:cd01161  262 NILNNGRFGMGAALIGTMKRCIEKAVDYANNRKQFGKKIHEFGLIQEKLANMAILQYATESMAYMTSGNMDRglKAEYQI 341

                        330       340       350       360       370       380
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 700674279 340 EAAMAKLAASEAATAISHQAIQILGGMGYVTEMPAERHYRDARITEIYEGTSEIQRLVIAGHLLRSY 406
Cdd:cd01161  342 EAAISKVFASEAAWLVVDEAIQIHGGMGFMREYGVERVLRDLRIFRIFEGTNEILRLFIALTGLQHA 408
MCAD cd01157
Medium chain acyl-CoA dehydrogenase; MCADs are mitochondrial beta-oxidation enzymes, which ...
 34-403 3.23e-78

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: 246.34  E-value: 3.23e-78
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 700674279  34 LPETHQMLLQTCRDFAEKELFPIAAQVDKEHLFPAAQVKKMGGLGLLAMDVPEELGGAGLDYLAYAIAMEEISRGCasTG 113
Cdd:cd01157    1 LTEQQKEFQETARKFAREEIIPVAAEYDKSGEYPWPLIKRAWELGLMNTHIPEDCGGLGLGTFDTCLITEELAYGC--TG 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 700674279 114 VIMSVN-NSLYLGPILKFGSKEQKQAWVTPFTSGDKIGCFALSEPGP--------SLLGPTGPIFAL-GQVGCPCPSSAA 183
Cdd:cd01157   79 VQTAIEaNSLGQMPVIISGNDEQKKKYLGRMTEEPLMCAYCVTEPGAgsdvagikTKAEKKGDEYIInGQKMWITNGGKA 158

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 700674279 184 TEACTFPRSRQRVSRPEllREGISAFLVPMPTPGLTLGKKEDKLGIRGSSTANLIFEDCRIPKDSILGEPGMGFKIAMQT 263
Cdd:cd01157  159 NWYFLLARSDPDPKCPA--SKAFTGFIVEADTPGIQPGRKELNMGQRCSDTRGITFEDVRVPKENVLIGEGAGFKIAMGA 236

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 700674279 264 LDMGRIGIASQALGIAQTALDCAVNYAENRMAFGAPLTKLQVIQFKLADMALALESARLLTWRAAMLKDNKKPFIKEAAM 343
Cdd:cd01157  237 FDKTRPPVAAGAVGLAQRALDEATKYALERKTFGKLIAEHQAVSFMLADMAMKVELARLAYQRAAWEVDSGRRNTYYASI 316

                        330       340       350       360       370       380
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 700674279 344 AKLAASEAATAISHQAIQILGGMGYVTEMPAERHYRDARITEIYEGTSEIQRLVIAGHLL 403
Cdd:cd01157  317 AKAFAADIANQLATDAVQIFGGNGFNSEYPVEKLMRDAKIYQIYEGTSQIQRLIISREHL 376
LCAD cd01160
Long chain acyl-CoA dehydrogenase; LCAD is an acyl-CoA dehydrogenases (ACAD), which is found ...
 36-403 3.97e-78

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: 245.87  E-value: 3.97e-78
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 700674279  36 ETHQMLLQTCRDFAEKELFPIAAQVDKEHLFPAAQVKKMGGLGLLAMDVPEELGGAGLDYLAYAIAMEEISR-GCASTGV 114
Cdd:cd01160    1 EEHDAFRDVVRRFFAKEVAPFHHEWEKAGEVPREVWRKAGEQGLLGVGFPEEYGGIGGDLLSAAVLWEELARaGGSGPGL 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 700674279 115 imSVNNSLYLGPILKFGSKEQKQAWVTPFTSGDKIGCFALSEPGPSllgptgpifalgqvgcpcpsSAATEACTFPRSR- 193
Cdd:cd01160   81 --SLHTDIVSPYITRAGSPEQKERVLPQMVAGKKIGAIAMTEPGAG--------------------SDLQGIRTTARKDg 138

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 700674279 194 ------------------------QRVSRPELLREGISAFLVPMPTPGLTLGKKEDKLGIRGSSTANLIFEDCRIPKDSI 249
Cdd:cd01160  139 dhyvlngsktfitngmladvvivvARTGGEARGAGGISLFLVERGTPGFSRGRKLKKMGWKAQDTAELFFDDCRVPAENL 218

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 700674279 250 LGEPGMGFKIAMQTLDMGRIGIASQALGIAQTALDCAVNYAENRMAFGAPLTKLQVIQFKLADMALALESARLLTWRAAM 329
Cdd:cd01160  219 LGEENKGFYYLMQNLPQERLLIAAGALAAAEFMLEETRNYVKQRKAFGKTLAQLQVVRHKIAELATKVAVTRAFLDNCAW 298

                        330       340       350       360       370       380       390
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 700674279 330 LKDNKKPFIKEAAMAKLAASEAATAISHQAIQILGGMGYVTEMPAERHYRDARITEIYEGTSEIQRLVIAGHLL 403
Cdd:cd01160  299 RHEQGRLDVAEASMAKYWATELQNRVAYECVQLHGGWGYMREYPIARAYRDARVQPIYGGTTEIMKELISRQMV 372
PLN02519 PLN02519
isovaleryl-CoA dehydrogenase
 6-404 1.34e-77

isovaleryl-CoA dehydrogenase


Pssm-ID: 215284 [Multi-domain]  Cd Length: 404  Bit Score: 245.56  E-value: 1.34e-77
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 700674279   6 LARASGPARRAlcpRAWRQLHTIYQSVELPETHQMLLQTCRDFAEKELFPIAAQVDKEHLFPAAQ--VKKMGGLGLLAMD 83
Cdd:PLN02519   1 MLLSAAKARRR---GLARRFSSSSSSLLFDDTQLQFKESVQQFAQENIAPHAAAIDATNSFPKDVnlWKLMGDFNLHGIT 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 700674279  84 VPEELGGAGLDYLAYAIAMEEISRGCASTGVIMSVNNSLYLGPILKFGSKEQKQAWVTPFTSGDKIGCFALSEP--GPSL 161
Cdd:PLN02519  78 APEEYGGLGLGYLYHCIAMEEISRASGSVGLSYGAHSNLCINQLVRNGTPAQKEKYLPKLISGEHVGALAMSEPnsGSDV 157

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 700674279 162 LG--------PTGPIFALGQVGCPCPSSAAT---EACTFPRSRQRvsrpellreGISAFLVPMPTPGLTLGKKEDKLGIR 230
Cdd:PLN02519 158 VSmkckaervDGGYVLNGNKMWCTNGPVAQTlvvYAKTDVAAGSK---------GITAFIIEKGMPGFSTAQKLDKLGMR 228

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 700674279 231 GSSTANLIFEDCRIPKDSILGEPGMGFKIAMQTLDMGRIGIASQALGIAQTALDCAVNYAENRMAFGAPLTKLQVIQFKL 310
Cdd:PLN02519 229 GSDTCELVFENCFVPEENVLGQEGKGVYVMMSGLDLERLVLAAGPLGLMQACLDVVLPYVRQREQFGRPIGEFQFIQGKL 308

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 700674279 311 ADMALALESARLLTWRAAMLKDNKKPFIKEAAMAKLAASEAATAISHQAIQILGGMGYVTEMPAERHYRDARITEIYEGT 390
Cdd:PLN02519 309 ADMYTSLQSSRSYVYSVARDCDNGKVDRKDCAGVILCAAERATQVALQAIQCLGGNGYINEYPTGRLLRDAKLYEIGAGT 388

                        410
                 ....*....|....
gi 700674279 391 SEIQRLVIAGHLLR 404
Cdd:PLN02519 389 SEIRRMLIGRELFK 402
GCD cd01151
Glutaryl-CoA dehydrogenase; Glutaryl-CoA dehydrogenase (GCD). GCD is an acyl-CoA dehydrogenase, ...
 34-399 5.14e-69

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: 223.00  E-value: 5.14e-69
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 700674279  34 LPETHQMLLQTCRDFAEKELFPIAAQVDKEHLFPAAQVKKMGGLGLLAMdVPEELGGAGLDYLAYAIAMEEISR---GCA 110
Cdd:cd01151   13 LTEEERAIRDTAREFCQEELAPRVLEAYREEKFDRKIIEEMGELGLLGA-TIKGYGCAGLSSVAYGLIAREVERvdsGYR 91

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 700674279 111 STgviMSVNNSLYLGPILKFGSKEQKQAWVTPFTSGDKIGCFALSEPG----PSLLG----PTGPIFAL-GQVGCPCPSS 181
Cdd:cd01151   92 SF---MSVQSSLVMLPIYDFGSEEQKQKYLPKLASGELIGCFGLTEPNhgsdPGGMEtrarKDGGGYKLnGSKTWITNSP 168

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 700674279 182 AATEACTFPRSRQRvsrpellrEGISAFLVPMPTPGLTLGKKEDKLGIRGSSTANLIFEDCRIPKDSILgePGM-GFKIA 260
Cdd:cd01151  169 IADVFVVWARNDET--------GKIRGFILERGMKGLSAPKIQGKFSLRASITGEIVMDNVFVPEENLL--PGAeGLRGP 238

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 700674279 261 MQTLDMGRIGIASQALGIAQTALDCAVNYAENRMAFGAPLTKLQVIQFKLADMALALESARLLTWRAAMLKDNKKPFIKE 340
Cdd:cd01151  239 FKCLNNARYGIAWGALGAAEDCYHTARQYVLDRKQFGRPLAAFQLVQKKLADMLTEIALGLLACLRVGRLKDQGKATPEQ 318

                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 700674279 341 AAMAKLAASEAATAISHQAIQILGGMGYVTEMPAERHYRDARITEIYEGTSEIQRLVIA 399
Cdd:cd01151  319 ISLLKRNNCGKALEIARTAREMLGGNGISDEYHIIRHMVNLESVNTYEGTHDIHALILG 377
PRK12341 PRK12341
acyl-CoA dehydrogenase;
34-407 5.21e-59

acyl-CoA dehydrogenase;


Pssm-ID: 183454 [Multi-domain]  Cd Length: 381  Bit Score: 196.87  E-value: 5.21e-59
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 700674279  34 LPETHQMLLQTCRDFAEKElFPIA--AQVDKEHLFPAAQVKKM--GGLGLLAmdVPEELGGAGLDYLAYAIAMEEISRGC 109
Cdd:PRK12341   5 LTEEQELLLASIRELITRN-FPEEyfRTCDENGTYPREFMRALadNGISMLG--VPEEFGGTPADYVTQMLVLEEVSKCG 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 700674279 110 ASTGVImsvNNSLYLGPILKFGSKEQ-KQAWVTPFTSGDKIGCFALSEPGP----SLLGPT-----GPIFALGQvgcpcp 179
Cdd:PRK12341  82 APAFLI---TNGQCIHSMRRFGSAEQlRKTAESTLETGDPAYALALTEPGAgsdnNSATTTytrknGKVYLNGQ------ 152

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 700674279 180 SSAATEACTFPRS--RQRVSRPELLREGISAFLVPMPTPGLTLGKKEdKLGIRGSSTANLIFEDCRIPKDSILGEPGMGF 257
Cdd:PRK12341 153 KTFITGAKEYPYMlvLARDPQPKDPKKAFTLWWVDSSKPGIKINPLH-KIGWHMLSTCEVYLDNVEVEESDLVGEEGMGF 231

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 700674279 258 KIAMQTLDMGRIGIASQALGIAQTALDCAVNYAENRMAFGAPLTKLQVIQFKLADMALALESARLLTWRAAMLKDNKKPF 337
Cdd:PRK12341 232 LNVMYNFEMERLINAARSLGFAECAFEDAARYANQRIQFGKPIGHNQLIQEKLTLMAIKIENMRNMVYKVAWQADNGQSL 311

                        330       340       350       360       370       380       390
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 700674279 338 IKEAAMAKLAASEAATAISHQAIQILGGMGYVTEMPAERHYRDARITEIYEGTSEIQrLVIAGH-LLRSYR 407
Cdd:PRK12341 312 RTSAALAKLYCARTAMEVIDDAIQIMGGLGYTDEARVSRFWRDVRCERIGGGTDEIM-IYIAGRqILKDYQ 381
Acyl-CoA_dh_1 pfam00441
Acyl-CoA dehydrogenase, C-terminal domain; C-terminal domain of Acyl-CoA dehydrogenase is an ...
 254-399 2.72e-54

Acyl-CoA dehydrogenase, C-terminal domain; C-terminal domain of Acyl-CoA dehydrogenase is an all-alpha, four helical up-and-down bundle.


Pssm-ID: 395354 [Multi-domain]  Cd Length: 149  Bit Score: 176.68  E-value: 2.72e-54
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 700674279  254 GMGFKIAMQTLDMGRIGIASQALGIAQTALDCAVNYAENRMAFGAPLTKLQVIQFKLADMALALESARLLTWRAAMLKDN 333
Cdd:pfam00441   1 GRGFRVAMETLNHERLAIAAMALGLARRALDEALAYARRRKAFGRPLIDFQLVRHKLAEMAAEIEAARLLVYRAAEALDA 80

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 700674279  334 KKPFIKEAAMAKLAASEAATAISHQAIQILGGMGYVTEMPAERHYRDARITEIYEGTSEIQRLVIA 399
Cdd:pfam00441  81 GGPDGAEASMAKLYASEAAVEVADLAMQLHGGYGYLREYPVERLYRDARVLRIGEGTSEIQRNIIA 146
PTZ00461 PTZ00461
isovaleryl-CoA dehydrogenase; Provisional
 35-407 9.61e-52

isovaleryl-CoA dehydrogenase; Provisional


Pssm-ID: 185640 [Multi-domain]  Cd Length: 410  Bit Score: 178.59  E-value: 9.61e-52
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 700674279  35 PEtHQMLLQTCRDFAEKELFPIAAQVDKEHLFPAAQVKKMGGLGLLAMDVPEELGGAGLDYLAYAIAMEEISRGCASTGV 114
Cdd:PTZ00461  39 PE-HAALRETVAKFSREVVDKHAREDDINMHFNRDLFKQLGDLGVMGVTVPEADGGAGMDAVAAVIIHHELSKYDPGFCL 117

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 700674279 115 IMSVNNSLYLGPILKFGSKEQKQAWVTPFTSGDKIGCFALSEP--GPSLLG--PTGPIFALGQV---GCPCPSSAATEAC 187
Cdd:PTZ00461 118 AYLAHSMLFVNNFYYSASPAQRARWLPKVLTGEHVGAMGMSEPgaGTDVLGmrTTAKKDSNGNYvlnGSKIWITNGTVAD 197

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 700674279 188 TFPRSRQRVSRpellregISAFLVPMPTPGLTLGKKEDKLGIRGSSTANLIFEDCRIPKDSILGEPGMGFKIAMQTLDMG 267
Cdd:PTZ00461 198 VFLIYAKVDGK-------ITAFVVERGTKGFTQGPKIDKCGMRASHMCQLFFEDVVVPAENLLGEEGKGMVGMMRNLELE 270

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 700674279 268 RIGIASQALGIAQTALDCAVNYAENRMAFGAPLTKLQVIQFKLADMALALESARLLTWRAA--MLKDNKKPFIKEAamAK 345
Cdd:PTZ00461 271 RVTLAAMAVGIAERSVELMTSYASERKAFGKPISNFGQIQRYIAEGYADTEAAKALVYSVShnVHPGNKNRLGSDA--AK 348

                        330       340       350       360       370       380
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 700674279 346 LAASEAATAISHQAIQILGGMGYVTEMPAERHYRDARITEIYEGTSEIQRLVIAGHLLRSYR 407
Cdd:PTZ00461 349 LFATPIAKKVADSAIQVMGGMGYSRDMPVERLWRDAKLLEIGGGTIEAHHKNITKDLLKGLK 410
Acyl-CoA_dh_N pfam02771
Acyl-CoA dehydrogenase, N-terminal domain; The N-terminal domain of Acyl-CoA dehydrogenase is ...
 35-147 2.06e-48

Acyl-CoA dehydrogenase, N-terminal domain; The N-terminal domain of Acyl-CoA dehydrogenase is an all-alpha domain.


Pssm-ID: 460686 [Multi-domain]  Cd Length: 113  Bit Score: 160.32  E-value: 2.06e-48
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 700674279   35 PETHQMLLQTCRDFAEKELFPIAAQVDKEHLFPAAQVKKMGGLGLLAMDVPEELGGAGLDYLAYAIAMEEISRGCASTGV 114
Cdd:pfam02771   1 TEEQEALRDTVREFAEEEIAPHAAEWDEEGEFPRELWKKLGELGLLGITIPEEYGGAGLDYLAYALVAEELARADASVAL 80

                          90       100       110
                  ....*....|....*....|....*....|...
gi 700674279  115 IMSVNNSLYLGPILKFGSKEQKQAWVTPFTSGD 147
Cdd:pfam02771  81 ALSVHSSLGAPPILRFGTEEQKERYLPKLASGE 113
ACAD_fadE5 cd01153
Putative acyl-CoA dehydrogenases similar to fadE5; Putative acyl-CoA dehydrogenase (ACAD). ...
 42-404 2.15e-47

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: 166.80  E-value: 2.15e-47
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 700674279  42 LQTCRDFAEKELFPIAAQVDKE--------HLFPAA---QVKKMGGLGLLAMDVPEELGGAGLDYLAYAIAMEEISRGCA 110
Cdd:cd01153    2 LEEVARLAENVLAPLNADGDREgpvfddgrVVVPPPfkeALDAFAEAGWMALGVPEEYGGQGLPITVYSALAEIFSRGDA 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 700674279 111 STGVIMSVNNSLYLgpILKFGSKEQKQAWVTPFTSGDKIGCFALSEP--GPSL-LGPT--------------GPIFALGq 173
Cdd:cd01153   82 PLMYASGTQGAAAT--LLAHGTEAQREKWIPRLAEGEWTGTMCLTEPdaGSDLgALRTkavyqadgswringVKRFISA- 158

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 700674279 174 vGCPCPSSAATEaCTFPRSRQrvsrPELLREGISAFLVP-----MPTPGLTLGKKEDKLGIRGSSTANLIFEDCRIPkds 248
Cdd:cd01153  159 -GEHDMSENIVH-LVLARSEG----APPGVKGLSLFLVPkflddGERNGVTVARIEEKMGLHGSPTCELVFDNAKGE--- 229

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 700674279 249 ILGEPGMGFKIAMQTLDMGRIGIASQALGIAQTALDCAVNYAENRMAFGAPL-TKLQV-------IQFKLADMALALESA 320
Cdd:cd01153  230 LIGEEGMGLAQMFAMMNGARLGVGTQGTGLAEAAYLNALAYAKERKQGGDLIkAAPAVtiihhpdVRRSLMTQKAYAEGS 309

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 700674279 321 RLLTWRAAMLKD--NKKPFIKEAA------------MAKLAASEAATAISHQAIQILGGMGYVTEMPAERHYRDARITEI 386
Cdd:cd01153  310 RALDLYTATVQDlaERKATEGEDRkalsaladlltpVVKGFGSEAALEAVSDAIQVHGGSGYTREYPIEQYYRDARITTI 389

                        410
                 ....*....|....*...
gi 700674279 387 YEGTSEIQRLVIAGHLLR 404
Cdd:cd01153  390 YEGTTGIQALDLIGRKIV 407
PRK03354 PRK03354
crotonobetainyl-CoA dehydrogenase; Validated
 34-407 2.41e-44

crotonobetainyl-CoA dehydrogenase; Validated


Pssm-ID: 179566 [Multi-domain]  Cd Length: 380  Bit Score: 158.07  E-value: 2.41e-44
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 700674279  34 LPETHQMLLQTCRDFAEKELF-PIAAQVDKEHLFPAAQVKKMGGLGLLAMDVPEELGGAGLDYLAYAIAMEEISRGCAST 112
Cdd:PRK03354   5 LNDEQELFVAGIRELMASENWeAYFAECDRDSVYPERFVKALADMGIDSLLIPEEHGGLDAGFVTLAAVWMELGRLGAPT 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 700674279 113 GVIMSVNNSLylGPILKFGSKEQKQAWVTPFTSGDKIGCFALSEPGP-----SLLGP----TGPIFALGQvGCPCPSSAA 183
Cdd:PRK03354  85 YVLYQLPGGF--NTFLREGTQEQIDKIMAFRGTGKQMWNSAITEPGAgsdvgSLKTTytrrNGKVYLNGS-KCFITSSAY 161

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 700674279 184 TEACTFPRSRQRVSRPELLREgisaFLVPMPTPGLTLGKKEdKLGIRGSSTANLIFEDCRIPKDSILGEPGMGFKIAMQT 263
Cdd:PRK03354 162 TPYIVVMARDGASPDKPVYTE----WFVDMSKPGIKVTKLE-KLGLRMDSCCEITFDDVELDEKDMFGREGNGFNRVKEE 236

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 700674279 264 LDMGRIGIASQALGIAQTALDCAVNYAENRMAFGAPLTKLQVIQFKLADMALALESARLLTWRAAMLKDNKKPFIKEAAM 343
Cdd:PRK03354 237 FDHERFLVALTNYGTAMCAFEDAARYANQRVQFGEAIGRFQLIQEKFAHMAIKLNSMKNMLYEAAWKADNGTITSGDAAM 316

                        330       340       350       360       370       380
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 700674279 344 AKLAASEAATAISHQAIQILGGMGYVTEMPAERHYRDARITEIYEGTSEIQRLVIAGHLLRSYR 407
Cdd:PRK03354 317 CKYFCANAAFEVVDSAMQVLGGVGIAGNHRISRFWRDLRVDRVSGGSDEMQILTLGRAVLKQYR 380
PLN02526 PLN02526
acyl-coenzyme A oxidase
 29-399 2.84e-39

acyl-coenzyme A oxidase


Pssm-ID: 178141 [Multi-domain]  Cd Length: 412  Bit Score: 145.38  E-value: 2.84e-39
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 700674279  29 YQSVEL--PEtHQMLLQTCRDFAEKELFPIAAQVDKEHLFPAAQVKKMGGLGLLAMDVpEELGGAGLDYLAYAIAMEEIS 106
Cdd:PLN02526  23 YQFDDLltPE-EQALRKRVRECMEKEVAPIMTEYWEKAEFPFHIIPKLGSLGIAGGTI-KGYGCPGLSITASAIATAEVA 100

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 700674279 107 RGCASTGVIMSVNNSLYLGPILKFGSKEQKQAWVTPFTSGDKIGCFALSEPG----PSLLGPT-----GPIFALGQVGCP 177
Cdd:PLN02526 101 RVDASCSTFILVHSSLAMLTIALCGSEAQKQKYLPSLAQLDTVACWALTEPDygsdASSLNTTatkveGGWILNGQKRWI 180

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 700674279 178 CPSSAATEACTFPRSRQRvsrpellrEGISAFLVPMPTPGLTLGKKEDKLGIRGSSTANLIFEDCRIPKDSILgePGM-G 256
Cdd:PLN02526 181 GNSTFADVLVIFARNTTT--------NQINGFIVKKGAPGLKATKIENKIGLRMVQNGDIVLKDVFVPDEDRL--PGVnS 250

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 700674279 257 FKIAMQTLDMGRIGIASQALGIAQTALDCAVNYAENRMAFGAPLTKLQVIQFKLADMALALESARLLTWRAAMLKDNKKP 336
Cdd:PLN02526 251 FQDTNKVLAVSRVMVAWQPIGISMGVYDMCHRYLKERKQFGAPLAAFQINQEKLVRMLGNIQAMFLVGWRLCKLYESGKM 330

                        330       340       350       360       370       380
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 700674279 337 FIKEAAMAKLAASEAATAISHQAIQILGGMGYVTEMPAERHYRDARITEIYEGTSEIQRLVIA 399
Cdd:PLN02526 331 TPGHASLGKAWITKKARETVALGRELLGGNGILADFLVAKAFCDLEPIYTYEGTYDINALVTG 393
ACAD_FadE2 cd01155
Acyl-CoA dehydrogenases similar to fadE2; FadE2-like Acyl-CoA dehydrogenase (ACAD). Acyl-CoA ...
 39-399 3.19e-36

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: 136.37  E-value: 3.19e-36
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 700674279  39 QMLLQTCRDFAEKELFPIAAQVDKE-----HLFPAA-----QVKKMG-GLGLLAMDVPEELGGAGLDYLAYAIAMEEISR 107
Cdd:cd01155    4 QELRARVKAFMEEHVYPAEQEFLEYyaeggDRWWTPppiieKLKAKAkAEGLWNLFLPEVSGLSGLTNLEYAYLAEETGR 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 700674279 108 --------GCAS--TGViMSVnnslylgpILKFGSKEQKQAWVTPFTSGDKIGCFALSEPGPSLLGPTgpifalgQVGCP 177
Cdd:cd01155   84 sffapevfNCQApdTGN-MEV--------LHRYGSEEQKKQWLEPLLDGKIRSAFAMTEPDVASSDAT-------NIECS 147

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 700674279 178 CP--------------SSAA-------------TEACTFPRSRQRvsrpellregiSAFLVPMPTPGLTlgkKEDKLGIR 230
Cdd:cd01155  148 IErdgddyvingrkwwSSGAgdprckiaivmgrTDPDGAPRHRQQ-----------SMILVPMDTPGVT---IIRPLSVF 213

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 700674279 231 GSSTA-----NLIFEDCRIPKDSILGEPGMGFKIAMQTLDMGRIGIASQALGIAQTALDCAVNYAENRMAFGAPLTKLQV 305
Cdd:cd01155  214 GYDDAphghaEITFDNVRVPASNLILGEGRGFEIAQGRLGPGRIHHCMRLIGAAERALELMCQRAVSREAFGKKLAQHGV 293

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 700674279 306 IQFKLADMALALESARLLTWRAAMLKDNKKPFI--KEAAMAKLAASEAATAISHQAIQILGGMGYVTEMPAERHYRDARI 383
Cdd:cd01155  294 VAHWIAKSRIEIEQARLLVLKAAHMIDTVGNKAarKEIAMIKVAAPRMALKIIDRAIQVHGAAGVSQDTPLANMYAWART 373

                        410
                 ....*....|....*.
gi 700674279 384 TEIYEGTSEIQRLVIA 399
Cdd:cd01155  374 LRIADGPDEVHLRSIA 389
ACAD_fadE6_17_26 cd01152
Putative acyl-CoA dehydrogenases similar to fadE6, fadE17, and fadE26; Putative acyl-CoA ...
 71-403 5.70e-36

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: 135.55  E-value: 5.70e-36
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 700674279  71 VKKMGGLGLLAMDVPEELGGAGLDYLAYAIAMEEISRGCASTGVIMSVNNSLylGP-ILKFGSKEQKQAWVTPFTSGDKI 149
Cdd:cd01152   41 QRALAAAGWAAPGWPKEYGGRGASLMEQLIFREEMAAAGAPVPFNQIGIDLA--GPtILAYGTDEQKRRFLPPILSGEEI 118

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 700674279 150 GCFALSEP--GPSL--LGPTG------------PIFalgqvgcpcpSSAATEAC-------TFPRS-RQRvsrpellreG 205
Cdd:cd01152  119 WCQGFSEPgaGSDLagLRTRAvrdgddwvvngqKIW----------TSGAHYADwawllvrTDPEApKHR---------G 179

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 700674279 206 ISAFLVPMPTPGLTLGKKEDKLGirGSSTANLIFEDCRIPKDSILGEPGMGFKIAMQTLDMGRIGIAsqalGIAQTALDC 285
Cdd:cd01152  180 ISILLVDMDSPGVTVRPIRSING--GEFFNEVFLDDVRVPDANRVGEVNDGWKVAMTTLNFERVSIG----GSAATFFEL 253

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 700674279 286 AVNYAENRMAFGAPLTKLQVIQFKLADMALALESARLLTWRAAMLKDNKKPFIKEAAMAKLAASEAATAISHQAIQILGG 365
Cdd:cd01152  254 LLARLLLLTRDGRPLIDDPLVRQRLARLEAEAEALRLLVFRLASALAAGKPPGAEASIAKLFGSELAQELAELALELLGT 333

                        330       340       350       360
                 ....*....|....*....|....*....|....*....|....*.
gi 700674279 366 ---MGYVTEMPA-----ERHYRDARITEIYEGTSEIQRLVIAGHLL 403
Cdd:cd01152  334 aalLRDPAPGAElagrwEADYLRSRATTIYGGTSEIQRNIIAERLL 379
AidB cd01154
Proteins involved in DNA damage response, similar to the AidB gene product; AidB is one of ...
 198-396 9.27e-34

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: 130.18  E-value: 9.27e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 700674279 198 RPELLRE---GISAFLVPMPTPGLTLGKKE-----DKLGIRGSSTANLIFedcripKDSI---LGEPGMGFKIAMQTLDM 266
Cdd:cd01154  199 RPEGAPAgarGLSLFLVPRLLEDGTRNGYRirrlkDKLGTRSVATGEVEF------DDAEaylIGDEGKGIYYILEMLNI 272

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 700674279 267 GRIGIASQALGIAQTALDCAVNYAENRMAFGAPLTKLQVIQFKLADMALALESARLLTWRAAMLKDNK---KPfiKEAAM 343
Cdd:cd01154  273 SRLDNAVAALGIMRRALSEAYHYARHRRAFGKPLIDHPLMRRDLAEMEVDVEAATALTFRAARAFDRAaadKP--VEAHM 350

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 700674279 344 AKLA-------ASEAATAISHQAIQILGGMGYVTEMPAERHYRDARITEIYEGTSEIQRL 396
Cdd:cd01154  351 ARLAtpvakliACKRAAPVTSEAMEVFGGNGYLEEWPVARLHREAQVTPIWEGTGNIQAL 410
PTZ00456 PTZ00456
acyl-CoA dehydrogenase; Provisional
 41-396 1.35e-21

acyl-CoA dehydrogenase; Provisional


Pssm-ID: 185635 [Multi-domain]  Cd Length: 622  Bit Score: 96.86  E-value: 1.35e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 700674279  41 LLQTCRDFAEKELFPIAAQVDKE--HLFPAAQVKKMGGL----------GLLAMDVPEELGGAGLDYLAYAIAMEEISrg 108
Cdd:PTZ00456  63 LLEEASKLATQTLLPLYESSDSEgcVLLKDGNVTTPKGFkeayqalkagGWTGISEPEEYGGQALPLSVGFITRELMA-- 140

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 700674279 109 CASTGVIMSVNNSL-YLGPILKFGSKEQKQAWVTPFTSGDKIGCFALSEPGPSLlgptgpifALGQVGCPC-PSSAATEA 186
Cdd:PTZ00456 141 TANWGFSMYPGLSIgAANTLMAWGSEEQKEQYLTKLVSGEWSGTMCLTEPQCGT--------DLGQVKTKAePSADGSYK 212

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 700674279 187 CTFPR-------------------SRQRVSRPEllREGISAFLVP--MPTPGLTLGKK--------EDKLGIRGSSTANL 237
Cdd:PTZ00456 213 ITGTKifisagdhdltenivhivlARLPNSLPT--TKGLSLFLVPrhVVKPDGSLETAknvkciglEKKMGIKGSSTCQL 290

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 700674279 238 IFEDcriPKDSILGEPGMGFKIAMQTLDMGRIGIASQALGIAQTALDCAVNYAENRMAFGA---------PLTKL----Q 304
Cdd:PTZ00456 291 SFEN---SVGYLIGEPNAGMKQMFTFMNTARVGTALEGVCHAELAFQNALRYARERRSMRAlsgtkepekPADRIichaN 367

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 700674279 305 VIQFKLADMALAlESARLLTWRAAMLKD---NKKPFIKEAAM----------AKLAASEAATAISHQAIQILGGMGYVTE 371
Cdd:PTZ00456 368 VRQNILFAKAVA-EGGRALLLDVGRLLDihaAAKDAATREALdheigfytpiAKGCLTEWGVEAASRCLQVWGGHGYIKG 446

                        410       420
                 ....*....|....*....|....*
gi 700674279 372 MPAERHYRDARITEIYEGTSEIQRL 396
Cdd:PTZ00456 447 NGMEQILRDARIGTLYEGTTGIQAL 471
Acyl-CoA_dh_2 pfam08028
Acyl-CoA dehydrogenase, C-terminal domain;
270-392 7.95e-20

Acyl-CoA dehydrogenase, C-terminal domain;


Pssm-ID: 429790 [Multi-domain]  Cd Length: 133  Bit Score: 84.70  E-value: 7.95e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 700674279  270 GIASQALGIAQTALDCAVNYAENR--MAFGAPLTKLQVIQFKLADMALALESARLLTWRAA----MLKDNKKPF----IK 339
Cdd:pfam08028   1 GIAAAALGAARAALAEFTERARGRvrAYFGVPLAEDPATQLALAEAAARIDAARLLLERAAarieAAAAAGKPVtpalRA 80

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|...
gi 700674279  340 EAAMAKLAASEAATAISHQAIQILGGMGYVTEMPAERHYRDARITEIYEGTSE 392
Cdd:pfam08028  81 EARRAAAFATELAVAAVDALFRAAGGSALFQDSPLQRIWRDIHAAAQHAAVNP 133
PRK13026 PRK13026
acyl-CoA dehydrogenase; Reviewed
 78-367 7.96e-20

acyl-CoA dehydrogenase; Reviewed


Pssm-ID: 237277 [Multi-domain]  Cd Length: 774  Bit Score: 91.94  E-value: 7.96e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 700674279  78 GLLAMDVPEELGGAGLDYLAYAIAMEEISRGCASTGVIMSVNNSLylGP---ILKFGSKEQKQAWVTPFTSGDKIGCFAL 154
Cdd:PRK13026 121 GFFALIIPKEYGGKGFSAYANSTIVSKIATRSVSAAVTVMVPNSL--GPgelLTHYGTQEQKDYWLPRLADGTEIPCFAL 198

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 700674279 155 SEP---------------------GPSLLG----------PTGPIfalgqvgcpcpssAATEACTFprsrqRVSRPELL- 202
Cdd:PRK13026 199 TGPeagsdagaipdtgivcrgefeGEEVLGlrltwdkryiTLAPV-------------ATVLGLAF-----KLRDPDGLl 260

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 700674279 203 ----REGISAFLVPMPTPGLTLGKKEDKLGIR---GSSTANLIFedcrIPKDSILGEP---GMGFKIAMQTLDMGRiGIA 272
Cdd:PRK13026 261 gdkkELGITCALIPTDHPGVEIGRRHNPLGMAfmnGTTRGKDVF----IPLDWIIGGPdyaGRGWRMLVECLSAGR-GIS 335

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 700674279 273 SQALGIA--QTALDCAVNYAENRMAFGAPLTKLQVIQFKLADMA---LALESARLLTwrAAMLKDNKKPFIKeAAMAKLA 347
Cdd:PRK13026 336 LPALGTAsgHMATRTTGAYAYVRRQFGMPIGQFEGVQEALARIAgntYLLEAARRLT--TTGLDLGVKPSVV-TAIAKYH 412

                        330       340
                 ....*....|....*....|
gi 700674279 348 ASEAATAISHQAIQILGGMG 367
Cdd:PRK13026 413 MTELARDVVNDAMDIHAGKG 432
PLN02876 PLN02876
acyl-CoA dehydrogenase
 86-399 8.60e-16

acyl-CoA dehydrogenase


Pssm-ID: 215473 [Multi-domain]  Cd Length: 822  Bit Score: 79.45  E-value: 8.60e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 700674279  86 EELGGAGLDYLAYAIAMEEISR----------GCASTGViMSVnnslylgpILKFGSKEQKQAWVTPFTSGDKIGCFALS 155
Cdd:PLN02876 487 DQLLGAGLSNLEYGYLCEIMGRsvwapqvfncGAPDTGN-MEV--------LLRYGNKEQQLEWLIPLLEGKIRSGFAMT 557

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 700674279 156 EPgpsllgptgpifalgQVGcpcpSSAATE-ACTFPR--------------SRQRVSRPELL------------REGISA 208
Cdd:PLN02876 558 EP---------------QVA----SSDATNiECSIRRqgdsyvingtkwwtSGAMDPRCRVLivmgktdfnapkHKQQSM 618

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 700674279 209 FLVPMPTPGLTLGKKEDKLGIRGS--STANLIFEDCRIPKDSILGEPGMGFKIAMQTLDMGRIGIASQALGIAQTALDCA 286
Cdd:PLN02876 619 ILVDIQTPGVQIKRPLLVFGFDDAphGHAEISFENVRVPAKNILLGEGRGFEIAQGRLGPGRLHHCMRLIGAAERGMQLM 698

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 700674279 287 VNYAENRMAFGAPLTKLQVIQFKLADMALALESARLLTWRAAMLKD---NKKPFiKEAAMAKLAASEAATAISHQAIQIL 363
Cdd:PLN02876 699 VQRALSRKAFGKLIAQHGSFLSDLAKCRVELEQTRLLVLEAADQLDrlgNKKAR-GIIAMAKVAAPNMALKVLDMAMQVH 777

                        330       340       350
                 ....*....|....*....|....*....|....*.
gi 700674279 364 GGMGYVTEMPAERHYRDARITEIYEGTSEIQRLVIA 399
Cdd:PLN02876 778 GAAGVSSDTVLAHLWATARTLRIADGPDEVHLGTIA 813
fadE PRK09463
acyl-CoA dehydrogenase; Reviewed
 78-367 6.45e-15

acyl-CoA dehydrogenase; Reviewed


Pssm-ID: 236528 [Multi-domain]  Cd Length: 777  Bit Score: 76.78  E-value: 6.45e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 700674279  78 GLLAMDVPEELGGAGLDYLAYAIAMEEISRGCASTGVIMSVNNSLylGP---ILKFGSKEQKQAWVTPFTSGDKIGCFAL 154
Cdd:PRK09463 122 GFFGMIIPKEYGGLEFSAYAHSRVLQKLASRSGTLAVTVMVPNSL--GPgelLLHYGTDEQKDHYLPRLARGEEIPCFAL 199

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 700674279 155 SEP--------------------------GPSL--------LGPTGPIFALGqvgcpcpssaateactFprsrqRVSRPE 200
Cdd:PRK09463 200 TSPeagsdagsipdtgvvckgewqgeevlGMRLtwnkryitLAPIATVLGLA----------------F-----KLYDPD 258

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 700674279 201 -LLRE----GISAFLVPMPTPGLTLGKKEDKLG-------IRGsstanlifEDCRIPKDSILGEP---GMGFKIAMQTLD 265
Cdd:PRK09463 259 gLLGDkedlGITCALIPTDTPGVEIGRRHFPLNvpfqngpTRG--------KDVFIPLDYIIGGPkmaGQGWRMLMECLS 330

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 700674279 266 MGR-IGIASQALGIAQTALDCAVNYAENRMAFGAPLTKLQVIQFKLADM---ALALESARLLTWRAAMLKDnkKPFIKeA 341
Cdd:PRK09463 331 VGRgISLPSNSTGGAKLAALATGAYARIRRQFKLPIGKFEGIEEPLARIagnAYLMDAARTLTTAAVDLGE--KPSVL-S 407

                        330       340
                 ....*....|....*....|....*..
gi 700674279 342 AMAKLAASEAA-TAISHqAIQILGGMG 367
Cdd:PRK09463 408 AIAKYHLTERGrQVIND-AMDIHGGKG 433
DszC cd01163
Dibenzothiophene (DBT) desulfurization enzyme C; DszC is a flavin reductase dependent enzyme, ...
 57-382 1.04e-13

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: 71.97  E-value: 1.04e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 700674279  57 AAQVDKEHLFPAAQVKKMGGLGLLAMDVPEELGGAGLDYLAYAIAMEEISRGCASTGVIMSvNNSLYLGPILKFGSKEQK 136
Cdd:cd01163   14 AAERDRQRGLPYEEVALLRQSGLGTLRVPKEYGGLGASLPDLYEVVRELAAADSNIAQALR-AHFGFVEALLLAGPEQFR 92

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 700674279 137 QAWVTPFTSGDKIGCfALSEPGPSLLGP-------TGPIFAL-GQVGcpcpssaateACTFPRSRQRVSRPELLREG-IS 207
Cdd:cd01163   93 KRWFGRVLNGWIFGN-AVSERGSVRPGTfltatvrDGGGYVLnGKKF----------YSTGALFSDWVTVSALDEEGkLV 161

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 700674279 208 AFLVPMPTPGLTLGKKEDKLGIR--GSSTAnlIFEDCRIPKDSILGEPGMGFKIAMQTLdMGRIGIASQALGIAQTALDC 285
Cdd:cd01163  162 FAAVPTDRPGITVVDDWDGFGQRltASGTV--TFDNVRVEPDEVLPRPNAPDRGTLLTA-IYQLVLAAVLAGIARAALDD 238

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 700674279 286 AVNYAEN--RMAFGAPLTK-------LQVIqfklADMALALESARLLTWRAAMLKDN--KKPFIKEA----------AMA 344
Cdd:cd01163  239 AVAYVRSrtRPWIHSGAESarddpyvQQVV----GDLAARLHAAEALVLQAARALDAaaAAGTALTAeargeaalavAAA 314

                        330       340       350
                 ....*....|....*....|....*....|....*...
gi 700674279 345 KLAASEAATAISHQAIQILGGMGYVTEMPAERHYRDAR 382
Cdd:cd01163  315 KVVVTRLALDATSRLFEVGGASATAREHNLDRHWRNAR 352
PRK11561 PRK11561
isovaleryl CoA dehydrogenase; Provisional
 205-393 1.84e-13

isovaleryl CoA dehydrogenase; Provisional


Pssm-ID: 183199 [Multi-domain]  Cd Length: 538  Bit Score: 71.71  E-value: 1.84e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 700674279 205 GISAFLVPMPTP-----GLTLGKKEDKLGIRGSSTANLIFEDCripKDSILGEPGMGFKIAMQTLDMGRIGIASQALGIA 279
Cdd:PRK11561 234 GLSCFFVPRFLPdgqrnAIRLERLKDKLGNRSNASSEVEFQDA---IGWLLGEEGEGIRLILKMGGMTRFDCALGSHGLM 310

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 700674279 280 QTALDCAVNYAENRMAFGAPLTKLQVIQFKLADMALALESARLLTWRAAMLKDnKKPFIKEAAMAKLAASEAATAISHQ- 358
Cdd:PRK11561 311 RRAFSVAIYHAHQRQVFGKPLIEQPLMRQVLSRMALQLEGQTALLFRLARAWD-RRADAKEALWARLFTPAAKFVICKRg 389

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|.
gi 700674279 359 ------AIQILGGMGYVTEMPAERHYRDARITEIYEGTSEI 393
Cdd:PRK11561 390 ipfvaeAMEVLGGIGYCEESELPRLYREMPVNSIWEGSGNI 430
AXO cd01150
Peroxisomal acyl-CoA oxidase; Peroxisomal acyl-CoA oxidases (AXO) catalyze the first set in ...
 111-408 2.06e-10

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: 62.35  E-value: 2.06e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 700674279 111 STGVIMSVNNSLYLGPILKFGSKEQKQAWVTPFTSGDKIGCFALSEPG-------------------------PSLlgpT 165
Cdd:cd01150   97 SLGAKLGLHLGLFGNAIKNLGTDEHQDYWLQGANNLEIIGCFAQTELGhgsnlqglettatydpltqefvintPDF---T 173

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 700674279 166 GPIFALGQVGcpcpsSAATEACTFPRSRQRVSRpellrEGISAFLVPM-------PTPGLTLGKKEDKLGIRGSSTANLI 238
Cdd:cd01150  174 ATKWWPGNLG-----KTATHAVVFAQLITPGKN-----HGLHAFIVPIrdpkthqPLPGVTVGDIGPKMGLNGVDNGFLQ 243

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 700674279 239 FEDCRIPKDSILG----------------EPGMGFKIAMQTLDMGRIGIASQALGIAQTALDCAVNYAENRMAFG----- 297
Cdd:cd01150  244 FRNVRIPRENLLNrfgdvspdgtyvspfkDPNKRYGAMLGTRSGGRVGLIYDAAMSLKKAATIAIRYSAVRRQFGpkpsd 323

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 700674279 298 --APLTKLQVIQFKLADMalaLESARLLTWRAAMLKDNKKPFIKEAAMAK---------LAASEAATAISH--QAIQIL- 363
Cdd:cd01150  324 peVQILDYQLQQYRLFPQ---LAAAYAFHFAAKSLVEMYHEIIKELLQGNsellaelhaLSAGLKAVATWTaaQGIQECr 400

                        330       340       350       360
                 ....*....|....*....|....*....|....*....|....*...
gi 700674279 364 ---GGMGYVTEMPAERHYRDARITEIYEGTSEIQRLVIAGHLLRSYRS 408
Cdd:cd01150  401 eacGGHGYLAMNRLPTLRDDNDPFCTYEGDNTVLLQQTANYLLKKYAQ 448
NcnH cd01159
Naphthocyclinone hydroxylase; Naphthocyclinone is an aromatic polyketide and an antibiotic, ...
 57-382 7.21e-10

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: 60.06  E-value: 7.21e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 700674279  57 AAQVDKEHLFPAAQVKKMGGLGLLAMDVPEELGGAGLDYLAYAIAMEEISRGCASTGVIMSVNN--SLYLGpilKFGSKE 134
Cdd:cd01159   14 APEAERARRLPDEVVRALREIGFFRMFVPKRYGGLEGDFAEFAEAIATLAEACGSAAWVASIVAthSRMLA---AFPPEA 90

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 700674279 135 QKQAWvtpftsgdkigcfalSEPGPSLLG----PTGPI--------------FALGQ-------VGCPCPSSAateactf 189
Cdd:cd01159   91 QEEVW---------------GDGPDTLLAgsyaPGGRAervdggyrvsgtwpFASGCdhadwilVGAIVEDDD------- 148

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 700674279 190 prsrqrvsRPELLRegisAFLVPMPtpGLTLGKKEDKLGIRGSSTANLIFEDCRIPKDSILGEPGM------GFKIA--- 260
Cdd:cd01159  149 --------GGPLPR----AFVVPRA--EYEIVDTWHVVGLRGTGSNTVVVDDVFVPEHRTLTAGDMmagdgpGGSTPvyr 214

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 700674279 261 MQTLDMGRIGIASQALGIAQTALDCAVNYAENRM---AFGAPLTKLQVIQFKLADMALALESARLL---TWRAAM--LKD 332
Cdd:cd01159  215 MPLRQVFPLSFAAVSLGAAEGALAEFLELAGKRVrqyGAAVKMAEAPITQLRLAEAAAELDAARAFlerATRDLWahALA 294

                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|....
gi 700674279 333 NKKPFIKEAAMAKLAASEAATaISHQAIQIL----GGMGYVTEMPAERHYRDAR 382
Cdd:cd01159  295 GGPIDVEERARIRRDAAYAAK-LSAEAVDRLfhaaGGSALYTASPLQRIWRDIH 347
PLN02636 PLN02636
acyl-coenzyme A oxidase
 98-407 1.97e-08

acyl-coenzyme A oxidase


Pssm-ID: 215342 [Multi-domain]  Cd Length: 686  Bit Score: 56.40  E-value: 1.97e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 700674279  98 YAIAMEEISRGCASTGVIMSVNNSLYLGPILKFGSKEQKQAWVTPFTSGDKIGCFALSE--PGPSLLG--------PTGP 167
Cdd:PLN02636 123 YFAITEAVGSVDMSLGIKLGVQYSLWGGSVINLGTKKHRDKYFDGIDNLDYPGCFAMTElhHGSNVQGlqttatfdPLTD 202

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 700674279 168 IFALGQvgcpcPSSAATE------------ACTFPRSRQRVSRPELLRE-GISAFLVPMPT-------PGLTLGKKEDKL 227
Cdd:PLN02636 203 EFVINT-----PNDGAIKwwignaavhgkfATVFARLKLPTHDSKGVSDmGVHAFIVPIRDmkthqvlPGVEIRDCGHKV 277

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 700674279 228 GIRGSSTANLIFEDCRIPKDSILGEPG----------------MGFKIAMQTLDMGRIGIASQALGIAQTALDCAVNYAE 291
Cdd:PLN02636 278 GLNGVDNGALRFRSVRIPRDNLLNRFGdvsrdgkytsslptinKRFAATLGELVGGRVGLAYGSVGVLKASNTIAIRYSL 357

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 700674279 292 NRMAFGAP------LTKLQVIQFKLADM-----ALALESARLLTWRAAMLKDNKKPFIkeAAMAKLAASEAATAISHQAI 360
Cdd:PLN02636 358 LRQQFGPPkqpeisILDYQSQQHKLMPMlastyAFHFATEYLVERYSEMKKTHDDQLV--ADVHALSAGLKAYITSYTAK 435

                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 700674279 361 QI------LGGMGY--VTEMPAERHyrDARITEIYEGTSEIQRLVIAGHLLRSYR 407
Cdd:PLN02636 436 ALstcreaCGGHGYaaVNRFGSLRN--DHDIFQTFEGDNTVLLQQVAADLLKQYK 488
Acyl-CoA_dh_M pfam02770
Acyl-CoA dehydrogenase, middle domain; Central domain of Acyl-CoA dehydrogenase has a ...
 203-240 3.98e-08

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: 50.74  E-value: 3.98e-08
                          10        20        30
                  ....*....|....*....|....*....|....*...
gi 700674279  203 REGISAFLVPMPTPGLTLGKKEDKLGIRGSSTANLIFE 240
Cdd:pfam02770  58 HGGISLFLVPKDAPGVSVRRIETKLGVRGLPTGELVFD 95
PLN02312 PLN02312
acyl-CoA oxidase
 111-296 9.12e-05

acyl-CoA oxidase


Pssm-ID: 215178 [Multi-domain]  Cd Length: 680  Bit Score: 44.76  E-value: 9.12e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 700674279 111 STGVIMSVNNSLYLGPILKFGSKEQKQAWVTPFTSGDKIGCFALSEPGP----------SLLGPTGPIFAlgqVGCPCPS 180
Cdd:PLN02312 148 SLAIKLGVHFFLWGGAIKFLGTKRHHDKWLKDTEDYVVKGCFAMTELGHgsnvrgietvTTYDPKTEEFV---INTPCES 224

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 700674279 181 SA----------ATEACTFPrsrqrvsrpELL----REGISAFLVPMPT------PGLTLGKKEDKLGIRGSSTANLIFE 240
Cdd:PLN02312 225 AQkywiggaanhATHTIVFS---------QLHingkNEGVHAFIAQIRDqdgnicPNIRIADCGHKIGLNGVDNGRIWFD 295

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 700674279 241 DCRIPKDSILG----------------EPGMGFKIAMQTLDMGRIGIASQALGIAQTALDCAVNYAENRMAF 296
Cdd:PLN02312 296 NLRIPRENLLNsvadvspdgkyvsaikDPDQRFGAFLAPLTSGRVTIAVSAIYSSKVGLAIAIRYSLSRRAF 367
 
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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