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Conserved domains on  [gi|4501859|ref|NP_001600|]
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short/branched chain specific acyl-CoA dehydrogenase, mitochondrial isoform 1 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 ...
 59-430 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: 640.86  E-value: 0e+00
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4501859   59 DEEMMIKSSVKKFAQEQIAPLVSTMDENSKMEKSVIQGLFQQGLMGIEVDPEYGGTGASFLSTVLVIEELAKVDASVAVF 138
Cdd:cd01158   1 EEHQMIRKTVRDFAEKEIAPLAAEMDEKGEFPREVIKEMAELGLMGIPIPEEYGGAGLDFLAYAIAIEELAKVDASVAVI 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4501859  139 CEIQNTLINTLIRKHGTEEQKATYLPQLTT-EKVGSFCLSEAGAGSDSFALKTRADKEGDYYVLNGSKMWISSAEHAGLF 217
Cdd:cd01158  81 VSVHNSLGANPIIKFGTEEQKKKYLPPLATgEKIGAFALSEPGAGSDAAALKTTAKKDGDDYVLNGSKMWITNGGEADFY 160

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4501859  218 LVMANVDPTIGYKGITSFLVDRDTPGLHIGKPENKLGLRASSTCPLTFENVKVPEANILGQIGHGYKYAIGSLNEGRIGI 297
Cdd:cd01158 161 IVFAVTDPSKGYRGITAFIVERDTPGLSVGKKEDKLGIRGSSTTELIFEDVRVPKENILGEEGEGFKIAMQTLDGGRIGI 240

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4501859  298 AAQMLGLAQGCFDYTIPYIKERIQFGKRLFDFQGLQHQVAHVATQLEAARLLTYNAARLLEAGKPFIKEASMAKYYASEI 377
Cdd:cd01158 241 AAQALGIAQAALDAAVDYAKERKQFGKPIADFQGIQFKLADMATEIEAARLLTYKAARLKDNGEPFIKEAAMAKLFASEV 320

                       330       340       350       360       370
                ....*....|....*....|....*....|....*....|....*....|...
gi 4501859  378 AGQTTSKCIEWMGGVGYTKDYPVEKYFRDAKIGTIYEGASNIQLNTIAKHIDA 430
Cdd:cd01158 321 AMRVTTDAVQIFGGYGYTKDYPVERYYRDAKITEIYEGTSEIQRLVIAKHLLK 373
 
Name Accession Description Interval E-value
SCAD_SBCAD cd01158
Short chain acyl-CoA dehydrogenases and eukaryotic short/branched chain acyl-CoA ...
 59-430 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: 640.86  E-value: 0e+00
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4501859   59 DEEMMIKSSVKKFAQEQIAPLVSTMDENSKMEKSVIQGLFQQGLMGIEVDPEYGGTGASFLSTVLVIEELAKVDASVAVF 138
Cdd:cd01158   1 EEHQMIRKTVRDFAEKEIAPLAAEMDEKGEFPREVIKEMAELGLMGIPIPEEYGGAGLDFLAYAIAIEELAKVDASVAVI 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4501859  139 CEIQNTLINTLIRKHGTEEQKATYLPQLTT-EKVGSFCLSEAGAGSDSFALKTRADKEGDYYVLNGSKMWISSAEHAGLF 217
Cdd:cd01158  81 VSVHNSLGANPIIKFGTEEQKKKYLPPLATgEKIGAFALSEPGAGSDAAALKTTAKKDGDDYVLNGSKMWITNGGEADFY 160

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4501859  218 LVMANVDPTIGYKGITSFLVDRDTPGLHIGKPENKLGLRASSTCPLTFENVKVPEANILGQIGHGYKYAIGSLNEGRIGI 297
Cdd:cd01158 161 IVFAVTDPSKGYRGITAFIVERDTPGLSVGKKEDKLGIRGSSTTELIFEDVRVPKENILGEEGEGFKIAMQTLDGGRIGI 240

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4501859  298 AAQMLGLAQGCFDYTIPYIKERIQFGKRLFDFQGLQHQVAHVATQLEAARLLTYNAARLLEAGKPFIKEASMAKYYASEI 377
Cdd:cd01158 241 AAQALGIAQAALDAAVDYAKERKQFGKPIADFQGIQFKLADMATEIEAARLLTYKAARLKDNGEPFIKEAAMAKLFASEV 320

                       330       340       350       360       370
                ....*....|....*....|....*....|....*....|....*....|...
gi 4501859  378 AGQTTSKCIEWMGGVGYTKDYPVEKYFRDAKIGTIYEGASNIQLNTIAKHIDA 430
Cdd:cd01158 321 AMRVTTDAVQIFGGYGYTKDYPVERYYRDAKITEIYEGTSEIQRLVIAKHLLK 373
CaiA COG1960
Acyl-CoA dehydrogenase related to the alkylation response protein AidB [Lipid transport and ...
 56-428 5.75e-170

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: 481.26  E-value: 5.75e-170
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4501859   56 TFTDEEMMIKSSVKKFAQEQIAPLVSTMDENSKMEKSVIQGLFQQGLMGIEVDPEYGGTGASFLSTVLVIEELAKVDASV 135
Cdd:COG1960   4 ELTEEQRALRDEVREFAEEEIAPEAREWDREGEFPRELWRKLAELGLLGLTIPEEYGGLGLSLVELALVLEELARADASL 83

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4501859  136 AVFCEIQNTLINTLIRkHGTEEQKATYLPQLTT-EKVGSFCLSEAGAGSDSFALKTRADKEGDYYVLNGSKMWISSAEHA 214
Cdd:COG1960  84 ALPVGVHNGAAEALLR-FGTEEQKERYLPRLASgEWIGAFALTEPGAGSDAAALRTTAVRDGDGYVLNGQKTFITNAPVA 162

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4501859  215 GLFLVMANVDPTIGYKGITSFLVDRDTPGLHIGKPENKLGLRASSTCPLTFENVKVPEANILGQIGHGYKYAIGSLNEGR 294
Cdd:COG1960 163 DVILVLARTDPAAGHRGISLFLVPKDTPGVTVGRIEDKMGLRGSDTGELFFDDVRVPAENLLGEEGKGFKIAMSTLNAGR 242

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4501859  295 IGIAAQMLGLAQGCFDYTIPYIKERIQFGKRLFDFQGLQHQVAHVATQLEAARLLTYNAARLLEAGKPFIKEASMAKYYA 374
Cdd:COG1960 243 LGLAAQALGIAEAALELAVAYAREREQFGRPIADFQAVQHRLADMAAELEAARALVYRAAWLLDAGEDAALEAAMAKLFA 322

                       330       340       350       360       370
                ....*....|....*....|....*....|....*....|....*....|....
gi 4501859  375 SEIAGQTTSKCIEWMGGVGYTKDYPVEKYFRDAKIGTIYEGASNIQLNTIAKHI 428
Cdd:COG1960 323 TEAALEVADEALQIHGGYGYTREYPLERLYRDARILTIYEGTNEIQRLIIARRL 376
PLN02519 PLN02519
isovaleryl-CoA dehydrogenase
 51-428 8.21e-89

isovaleryl-CoA dehydrogenase


Pssm-ID: 215284 [Multi-domain]  Cd Length: 404  Bit Score: 275.60  E-value: 8.21e-89
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4501859    51 FAPLQTFTDEEMMIKSSVKKFAQEQIAPLVSTMDENSKMEKSV----IQGLFqqGLMGIEVDPEYGGTGASFLSTVLVIE 126
Cdd:PLN02519  20 SSSSLLFDDTQLQFKESVQQFAQENIAPHAAAIDATNSFPKDVnlwkLMGDF--NLHGITAPEEYGGLGLGYLYHCIAME 97

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4501859   127 ELAKVDASVAV-FCEIQNTLINTLIRkHGTEEQKATYLPQLTT-EKVGSFCLSEAGAGSDSFALKTRADKEGDYYVLNGS 204
Cdd:PLN02519  98 EISRASGSVGLsYGAHSNLCINQLVR-NGTPAQKEKYLPKLISgEHVGALAMSEPNSGSDVVSMKCKAERVDGGYVLNGN 176

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4501859   205 KMWISSAEHAGLFLVMANVDPTIGYKGITSFLVDRDTPGLHIGKPENKLGLRASSTCPLTFENVKVPEANILGQIGHGYK 284
Cdd:PLN02519 177 KMWCTNGPVAQTLVVYAKTDVAAGSKGITAFIIEKGMPGFSTAQKLDKLGMRGSDTCELVFENCFVPEENVLGQEGKGVY 256

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4501859   285 YAIGSLNEGRIGIAAQMLGLAQGCFDYTIPYIKERIQFGKRLFDFQGLQHQVAHVATQLEAARLLTYNAARLLEAGKPFI 364
Cdd:PLN02519 257 VMMSGLDLERLVLAAGPLGLMQACLDVVLPYVRQREQFGRPIGEFQFIQGKLADMYTSLQSSRSYVYSVARDCDNGKVDR 336

                        330       340       350       360       370       380
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 4501859   365 KEASMAKYYASEIAGQTTSKCIEWMGGVGYTKDYPVEKYFRDAKIGTIYEGASNIQLNTIAKHI 428
Cdd:PLN02519 337 KDCAGVILCAAERATQVALQAIQCLGGNGYINEYPTGRLLRDAKLYEIGAGTSEIRRMLIGREL 400
Acyl-CoA_dh_1 pfam00441
Acyl-CoA dehydrogenase, C-terminal domain; C-terminal domain of Acyl-CoA dehydrogenase is an ...
 280-428 2.78e-60

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: 192.85  E-value: 2.78e-60
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4501859    280 GHGYKYAIGSLNEGRIGIAAQMLGLAQGCFDYTIPYIKERIQFGKRLFDFQGLQHQVAHVATQLEAARLLTYNAARLLEA 359
Cdd:pfam00441   1 GRGFRVAMETLNHERLAIAAMALGLARRALDEALAYARRRKAFGRPLIDFQLVRHKLAEMAAEIEAARLLVYRAAEALDA 80

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 4501859    360 GKPFIKEASMAKYYASEIAGQTTSKCIEWMGGVGYTKDYPVEKYFRDAKIGTIYEGASNIQLNTIAKHI 428
Cdd:pfam00441  81 GGPDGAEASMAKLYASEAAVEVADLAMQLHGGYGYLREYPVERLYRDARVLRIGEGTSEIQRNIIARRL 149
 
Name Accession Description Interval E-value
SCAD_SBCAD cd01158
Short chain acyl-CoA dehydrogenases and eukaryotic short/branched chain acyl-CoA ...
 59-430 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: 640.86  E-value: 0e+00
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4501859   59 DEEMMIKSSVKKFAQEQIAPLVSTMDENSKMEKSVIQGLFQQGLMGIEVDPEYGGTGASFLSTVLVIEELAKVDASVAVF 138
Cdd:cd01158   1 EEHQMIRKTVRDFAEKEIAPLAAEMDEKGEFPREVIKEMAELGLMGIPIPEEYGGAGLDFLAYAIAIEELAKVDASVAVI 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4501859  139 CEIQNTLINTLIRKHGTEEQKATYLPQLTT-EKVGSFCLSEAGAGSDSFALKTRADKEGDYYVLNGSKMWISSAEHAGLF 217
Cdd:cd01158  81 VSVHNSLGANPIIKFGTEEQKKKYLPPLATgEKIGAFALSEPGAGSDAAALKTTAKKDGDDYVLNGSKMWITNGGEADFY 160

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4501859  218 LVMANVDPTIGYKGITSFLVDRDTPGLHIGKPENKLGLRASSTCPLTFENVKVPEANILGQIGHGYKYAIGSLNEGRIGI 297
Cdd:cd01158 161 IVFAVTDPSKGYRGITAFIVERDTPGLSVGKKEDKLGIRGSSTTELIFEDVRVPKENILGEEGEGFKIAMQTLDGGRIGI 240

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4501859  298 AAQMLGLAQGCFDYTIPYIKERIQFGKRLFDFQGLQHQVAHVATQLEAARLLTYNAARLLEAGKPFIKEASMAKYYASEI 377
Cdd:cd01158 241 AAQALGIAQAALDAAVDYAKERKQFGKPIADFQGIQFKLADMATEIEAARLLTYKAARLKDNGEPFIKEAAMAKLFASEV 320

                       330       340       350       360       370
                ....*....|....*....|....*....|....*....|....*....|...
gi 4501859  378 AGQTTSKCIEWMGGVGYTKDYPVEKYFRDAKIGTIYEGASNIQLNTIAKHIDA 430
Cdd:cd01158 321 AMRVTTDAVQIFGGYGYTKDYPVERYYRDAKITEIYEGTSEIQRLVIAKHLLK 373
CaiA COG1960
Acyl-CoA dehydrogenase related to the alkylation response protein AidB [Lipid transport and ...
 56-428 5.75e-170

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: 481.26  E-value: 5.75e-170
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4501859   56 TFTDEEMMIKSSVKKFAQEQIAPLVSTMDENSKMEKSVIQGLFQQGLMGIEVDPEYGGTGASFLSTVLVIEELAKVDASV 135
Cdd:COG1960   4 ELTEEQRALRDEVREFAEEEIAPEAREWDREGEFPRELWRKLAELGLLGLTIPEEYGGLGLSLVELALVLEELARADASL 83

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4501859  136 AVFCEIQNTLINTLIRkHGTEEQKATYLPQLTT-EKVGSFCLSEAGAGSDSFALKTRADKEGDYYVLNGSKMWISSAEHA 214
Cdd:COG1960  84 ALPVGVHNGAAEALLR-FGTEEQKERYLPRLASgEWIGAFALTEPGAGSDAAALRTTAVRDGDGYVLNGQKTFITNAPVA 162

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4501859  215 GLFLVMANVDPTIGYKGITSFLVDRDTPGLHIGKPENKLGLRASSTCPLTFENVKVPEANILGQIGHGYKYAIGSLNEGR 294
Cdd:COG1960 163 DVILVLARTDPAAGHRGISLFLVPKDTPGVTVGRIEDKMGLRGSDTGELFFDDVRVPAENLLGEEGKGFKIAMSTLNAGR 242

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4501859  295 IGIAAQMLGLAQGCFDYTIPYIKERIQFGKRLFDFQGLQHQVAHVATQLEAARLLTYNAARLLEAGKPFIKEASMAKYYA 374
Cdd:COG1960 243 LGLAAQALGIAEAALELAVAYAREREQFGRPIADFQAVQHRLADMAAELEAARALVYRAAWLLDAGEDAALEAAMAKLFA 322

                       330       340       350       360       370
                ....*....|....*....|....*....|....*....|....*....|....
gi 4501859  375 SEIAGQTTSKCIEWMGGVGYTKDYPVEKYFRDAKIGTIYEGASNIQLNTIAKHI 428
Cdd:COG1960 323 TEAALEVADEALQIHGGYGYTREYPLERLYRDARILTIYEGTNEIQRLIIARRL 376
IVD cd01156
Isovaleryl-CoA dehydrogenase; Isovaleryl-CoA dehydrogenase (IVD) is an is an acyl-CoA ...
 57-430 1.64e-120

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: 355.57  E-value: 1.64e-120
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4501859   57 FTDEEMMIKSSVKKFAQEQIAPLVSTMDENSKMEKSVIQGLFQQGLMGIEVDPEYGGTGASFLSTVLVIEELAKVDASVA 136
Cdd:cd01156   2 LDDEIEMLRQSVREFAQKEIAPLAAKIDRDNEFPRDLWRKMGKLGLLGITAPEEYGGSGMGYLAHVIIMEEISRASGSVA 81

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4501859  137 V-FCEIQNTLINTLIRkHGTEEQKATYLPQLTT-EKVGSFCLSEAGAGSDSFALKTRADKEGDYYVLNGSKMWISSAEHA 214
Cdd:cd01156  82 LsYGAHSNLCINQIYR-NGSAAQKEKYLPKLISgEHIGALAMSEPNAGSDVVSMKLRAEKKGDRYVLNGSKMWITNGPDA 160

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4501859  215 GLFLVMANVDPTIGYKGITSFLVDRDTPGLHIGKPENKLGLRASSTCPLTFENVKVPEANILGQIGHGYKYAIGSLNEGR 294
Cdd:cd01156 161 DTLVVYAKTDPSAGAHGITAFIVEKGMPGFSRAQKLDKLGMRGSNTCELVFEDCEVPEENILGGENKGVYVLMSGLDYER 240

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4501859  295 IGIAAQMLGLAQGCFDYTIPYIKERIQFGKRLFDFQGLQHQVAHVATQLEAARLLTYNAARLLEAGKPFIKEASMAKYYA 374
Cdd:cd01156 241 LVLAGGPIGIMQAALDVAIPYAHQRKQFGQPIGEFQLVQGKLADMYTRLNASRSYLYTVAKACDRGNMDPKDAAGVILYA 320

                       330       340       350       360       370
                ....*....|....*....|....*....|....*....|....*....|....*.
gi 4501859  375 SEIAGQTTSKCIEWMGGVGYTKDYPVEKYFRDAKIGTIYEGASNIQLNTIAKHIDA 430
Cdd:cd01156 321 AEKATQVALDAIQILGGNGYINDYPTGRLLRDAKLYEIGAGTSEIRRMVIGRELFK 376
ACAD cd00567
Acyl-CoA dehydrogenase; Both mitochondrial acyl-CoA dehydrogenases (ACAD) and peroxisomal ...
 148-426 2.25e-117

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: 345.81  E-value: 2.25e-117
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4501859  148 TLIRKHGTEEQKATYLPQLTT-EKVGSFCLSEAGAGSDSFALKTRADKEGDYYVLNGSKMWISSAEHAGLFLVMANVDP- 225
Cdd:cd00567  46 ALLLAYGTEEQKERYLPPLASgEAIAAFALTEPGAGSDLAGIRTTARKDGDGYVLNGRKIFISNGGDADLFIVLARTDEe 125

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4501859  226 TIGYKGITSFLVDRDTPGLHIGKPENKLGLRASSTCPLTFENVKVPEANILGQIGHGYKYAIGSLNEGRIGIAAQMLGLA 305
Cdd:cd00567 126 GPGHRGISAFLVPADTPGVTVGRIWDKMGMRGSGTGELVFDDVRVPEDNLLGEEGGGFELAMKGLNVGRLLLAAVALGAA 205

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4501859  306 QGCFDYTIPYIKERIQFGKRLFDFQGLQHQVAHVATQLEAARLLTYNAARLLEAGKPFI-KEASMAKYYASEIAGQTTSK 384
Cdd:cd00567 206 RAALDEAVEYAKQRKQFGKPLAEFQAVQFKLADMAAELEAARLLLYRAAWLLDQGPDEArLEAAMAKLFATEAAREVADL 285

                       250       260       270       280
                ....*....|....*....|....*....|....*....|..
gi 4501859  385 CIEWMGGVGYTKDYPVEKYFRDAKIGTIYEGASNIQLNTIAK 426
Cdd:cd00567 286 AMQIHGGRGYSREYPVERYLRDARAARIAEGTAEIQRLIIAR 327
LCAD cd01160
Long chain acyl-CoA dehydrogenase; LCAD is an acyl-CoA dehydrogenases (ACAD), which is found ...
 60-428 4.46e-106

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: 318.68  E-value: 4.46e-106
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4501859   60 EEMMIKSSVKKFAQEQIAPLVSTMDENSKMEKSVIQGLFQQGLMGIEVDPEYGGTGASFLSTVLVIEELAKVDASVAVFc 139
Cdd:cd01160   2 EHDAFRDVVRRFFAKEVAPFHHEWEKAGEVPREVWRKAGEQGLLGVGFPEEYGGIGGDLLSAAVLWEELARAGGSGPGL- 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4501859  140 EIQNTLINTLIRKHGTEEQKATYLPQLTT-EKVGSFCLSEAGAGSDSFALKTRADKEGDYYVLNGSKMWISSAEHAGLFL 218
Cdd:cd01160  81 SLHTDIVSPYITRAGSPEQKERVLPQMVAgKKIGAIAMTEPGAGSDLQGIRTTARKDGDHYVLNGSKTFITNGMLADVVI 160

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4501859  219 VMANVD-PTIGYKGITSFLVDRDTPGLHIGKPENKLGLRASSTCPLTFENVKVPEANILGQIGHGYKYAIGSLNEGRIGI 297
Cdd:cd01160 161 VVARTGgEARGAGGISLFLVERGTPGFSRGRKLKKMGWKAQDTAELFFDDCRVPAENLLGEENKGFYYLMQNLPQERLLI 240

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4501859  298 AAQMLGLAQGCFDYTIPYIKERIQFGKRLFDFQGLQHQVAHVATQLEAARLLTYNAARLLEAGKPFIKEASMAKYYASEI 377
Cdd:cd01160 241 AAGALAAAEFMLEETRNYVKQRKAFGKTLAQLQVVRHKIAELATKVAVTRAFLDNCAWRHEQGRLDVAEASMAKYWATEL 320

                       330       340       350       360       370
                ....*....|....*....|....*....|....*....|....*....|.
gi 4501859  378 AGQTTSKCIEWMGGVGYTKDYPVEKYFRDAKIGTIYEGASNIQLNTIAKHI 428
Cdd:cd01160 321 QNRVAYECVQLHGGWGYMREYPIARAYRDARVQPIYGGTTEIMKELISRQM 371
IBD cd01162
Isobutyryl-CoA dehydrogenase; Isobutyryl-CoA dehydrogenase (IBD) catalyzes the alpha, beta- ...
 58-428 3.84e-105

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: 316.31  E-value: 3.84e-105
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4501859   58 TDEEMMIKSSVKKFAQEQIAPLVSTMDENSKMEKSVIQGLFQQGLMGIEVDPEYGGTGASFLSTVLVIEELAKVDASVAV 137
Cdd:cd01162   2 NEEQRAIQEVARAFAAKEMAPHAADWDQKKHFPVDVLRKAAELGFGGIYIRDDVGGSGLSRLDASIIFEALSTGCVSTAA 81

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4501859  138 FCEIQNtLINTLIRKHGTEEQKATYLPQLTT-EKVGSFCLSEAGAGSDSFALKTRADKEGDYYVLNGSKMWISSAEHAGL 216
Cdd:cd01162  82 YISIHN-MCAWMIDSFGNDEQRERFLPDLCTmEKLASYCLTEPGSGSDAAALRTRAVREGDHYVLNGSKAFISGAGDSDV 160

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4501859  217 FLVMANVDPTiGYKGITSFLVDRDTPGLHIGKPENKLGLRASSTCPLTFENVKVPEANILGQIGHGYKYAIGSLNEGRIG 296
Cdd:cd01162 161 YVVMARTGGE-GPKGISCFVVEKGTPGLSFGANEKKMGWNAQPTRAVIFEDCRVPVENRLGGEGQGFGIAMAGLNGGRLN 239

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4501859  297 IAAQMLGLAQGCFDYTIPYIKERIQFGKRLFDFQGLQHQVAHVATQLEAARLLTYNAARLLEAGKP-FIKEASMAKYYAS 375
Cdd:cd01162 240 IASCSLGAAQAALDLARAYLEERKQFGKPLADFQALQFKLADMATELVASRLMVRRAASALDRGDPdAVKLCAMAKRFAT 319

                       330       340       350       360       370
                ....*....|....*....|....*....|....*....|....*....|...
gi 4501859  376 EIAGQTTSKCIEWMGGVGYTKDYPVEKYFRDAKIGTIYEGASNIQLNTIAKHI 428
Cdd:cd01162 320 DECFDVANQALQLHGGYGYLKDYPVEQYVRDLRVHQILEGTNEIMRLIIARAL 372
VLCAD cd01161
Very long chain acyl-CoA dehydrogenase; VLCAD is an acyl-CoA dehydrogenase (ACAD), which is ...
 58-426 6.22e-99

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: 301.69  E-value: 6.22e-99
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4501859   58 TDEEMMIKSSVKKFAQEQIAPLVstMDENSKMEKSVIQGLFQQGLMGIEVDPEYGGTGASFLSTVLVIEELAkVDASVAV 137
Cdd:cd01161  28 TEELNMLVGPVEKFFEEVNDPAK--NDQLEKIPRKTLTQLKELGLFGLQVPEEYGGLGLNNTQYARLAEIVG-MDLGFSV 104

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4501859  138 FCEIQNTLINTLIRKHGTEEQKATYLPQLTT-EKVGSFCLSEAGAGSDSFALKTRADK--EGDYYVLNGSKMWISSAEHA 214
Cdd:cd01161 105 TLGAHQSIGFKGILLFGTEAQKEKYLPKLASgEWIAAFALTEPSSGSDAASIRTTAVLseDGKHYVLNGSKIWITNGGIA 184

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4501859  215 GLFLVMAN---VDPTIGYK-GITSFLVDRDTPGLHIGKPENKLGLRASSTCPLTFENVKVPEANILGQIGHGYKYAIGSL 290
Cdd:cd01161 185 DIFTVFAKtevKDATGSVKdKITAFIVERSFGGVTNGPPEKKMGIKGSNTAEVYFEDVKIPVENVLGEVGDGFKVAMNIL 264

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4501859  291 NEGRIGIAAQMLGLAQGCFDYTIPYIKERIQFGKRLFDFQGLQHQVAHVATQLEAARLLTYNAARLLEAG--KPFIKEAS 368
Cdd:cd01161 265 NNGRFGMGAALIGTMKRCIEKAVDYANNRKQFGKKIHEFGLIQEKLANMAILQYATESMAYMTSGNMDRGlkAEYQIEAA 344

                       330       340       350       360       370
                ....*....|....*....|....*....|....*....|....*....|....*...
gi 4501859  369 MAKYYASEIAGQTTSKCIEWMGGVGYTKDYPVEKYFRDAKIGTIYEGASNIQLNTIAK 426
Cdd:cd01161 345 ISKVFASEAAWLVVDEAIQIHGGMGFMREYGVERVLRDLRIFRIFEGTNEILRLFIAL 402
MCAD cd01157
Medium chain acyl-CoA dehydrogenase; MCADs are mitochondrial beta-oxidation enzymes, which ...
 57-430 5.90e-92

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: 282.55  E-value: 5.90e-92
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4501859   57 FTDEEMMIKSSVKKFAQEQIAPLVSTMDENSKMEKSVIQGLFQQGLMGIEVDPEYGGTGASFLSTVLVIEELAKVDASVA 136
Cdd:cd01157   1 LTEQQKEFQETARKFAREEIIPVAAEYDKSGEYPWPLIKRAWELGLMNTHIPEDCGGLGLGTFDTCLITEELAYGCTGVQ 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4501859  137 VFCEiQNTLINTLIRKHGTEEQKATYLPQLTTEK-VGSFCLSEAGAGSDSFALKTRADKEGDYYVLNGSKMWISSAEHAG 215
Cdd:cd01157  81 TAIE-ANSLGQMPVIISGNDEQKKKYLGRMTEEPlMCAYCVTEPGAGSDVAGIKTKAEKKGDEYIINGQKMWITNGGKAN 159

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4501859  216 LFLVMANVDP---TIGYKGITSFLVDRDTPGLHIGKPENKLGLRASSTCPLTFENVKVPEANILGQIGHGYKYAIGSLNE 292
Cdd:cd01157 160 WYFLLARSDPdpkCPASKAFTGFIVEADTPGIQPGRKELNMGQRCSDTRGITFEDVRVPKENVLIGEGAGFKIAMGAFDK 239

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4501859  293 GRIGIAAQMLGLAQGCFDYTIPYIKERIQFGKRLFDFQGLQHQVAHVATQLEAARLLTYNAARLLEAGKPFIKEASMAKY 372
Cdd:cd01157 240 TRPPVAAGAVGLAQRALDEATKYALERKTFGKLIAEHQAVSFMLADMAMKVELARLAYQRAAWEVDSGRRNTYYASIAKA 319

                       330       340       350       360       370
                ....*....|....*....|....*....|....*....|....*....|....*....
gi 4501859  373 YASEIAGQTTSKCIEWMGGVGYTKDYPVEKYFRDAKIGTIYEGASNIQLNTIAK-HIDA 430
Cdd:cd01157 320 FAADIANQLATDAVQIFGGNGFNSEYPVEKLMRDAKIYQIYEGTSQIQRLIISReHLGK 378
PLN02519 PLN02519
isovaleryl-CoA dehydrogenase
 51-428 8.21e-89

isovaleryl-CoA dehydrogenase


Pssm-ID: 215284 [Multi-domain]  Cd Length: 404  Bit Score: 275.60  E-value: 8.21e-89
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4501859    51 FAPLQTFTDEEMMIKSSVKKFAQEQIAPLVSTMDENSKMEKSV----IQGLFqqGLMGIEVDPEYGGTGASFLSTVLVIE 126
Cdd:PLN02519  20 SSSSLLFDDTQLQFKESVQQFAQENIAPHAAAIDATNSFPKDVnlwkLMGDF--NLHGITAPEEYGGLGLGYLYHCIAME 97

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4501859   127 ELAKVDASVAV-FCEIQNTLINTLIRkHGTEEQKATYLPQLTT-EKVGSFCLSEAGAGSDSFALKTRADKEGDYYVLNGS 204
Cdd:PLN02519  98 EISRASGSVGLsYGAHSNLCINQLVR-NGTPAQKEKYLPKLISgEHVGALAMSEPNSGSDVVSMKCKAERVDGGYVLNGN 176

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4501859   205 KMWISSAEHAGLFLVMANVDPTIGYKGITSFLVDRDTPGLHIGKPENKLGLRASSTCPLTFENVKVPEANILGQIGHGYK 284
Cdd:PLN02519 177 KMWCTNGPVAQTLVVYAKTDVAAGSKGITAFIIEKGMPGFSTAQKLDKLGMRGSDTCELVFENCFVPEENVLGQEGKGVY 256

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4501859   285 YAIGSLNEGRIGIAAQMLGLAQGCFDYTIPYIKERIQFGKRLFDFQGLQHQVAHVATQLEAARLLTYNAARLLEAGKPFI 364
Cdd:PLN02519 257 VMMSGLDLERLVLAAGPLGLMQACLDVVLPYVRQREQFGRPIGEFQFIQGKLADMYTSLQSSRSYVYSVARDCDNGKVDR 336

                        330       340       350       360       370       380
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 4501859   365 KEASMAKYYASEIAGQTTSKCIEWMGGVGYTKDYPVEKYFRDAKIGTIYEGASNIQLNTIAKHI 428
Cdd:PLN02519 337 KDCAGVILCAAERATQVALQAIQCLGGNGYINEYPTGRLLRDAKLYEIGAGTSEIRRMLIGREL 400
GCD cd01151
Glutaryl-CoA dehydrogenase; Glutaryl-CoA dehydrogenase (GCD). GCD is an acyl-CoA dehydrogenase, ...
 58-419 3.09e-80

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: 252.66  E-value: 3.09e-80
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4501859   58 TDEEMMIKSSVKKFAQEQIAPLVSTMDENSKMEKSVIQGLFQQGLMGIEVDpEYGGTGASFLSTVLVIEELAKVDASVAV 137
Cdd:cd01151  14 TEEERAIRDTAREFCQEELAPRVLEAYREEKFDRKIIEEMGELGLLGATIK-GYGCAGLSSVAYGLIAREVERVDSGYRS 92

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4501859  138 FCEIQNTLINTLIRKHGTEEQKATYLPQLTT-EKVGSFCLSEAGAGSDSFALKTRADKEGDYYVLNGSKMWISSAEHAGL 216
Cdd:cd01151  93 FMSVQSSLVMLPIYDFGSEEQKQKYLPKLASgELIGCFGLTEPNHGSDPGGMETRARKDGGGYKLNGSKTWITNSPIADV 172

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4501859  217 FLVMANVDPTIGYKGitsFLVDRDTPGLHIGKPENKLGLRASSTCPLTFENVKVPEANILGQIgHGYKYAIGSLNEGRIG 296
Cdd:cd01151 173 FVVWARNDETGKIRG---FILERGMKGLSAPKIQGKFSLRASITGEIVMDNVFVPEENLLPGA-EGLRGPFKCLNNARYG 248

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4501859  297 IAAQMLGLAQGCFDYTIPYIKERIQFGKRLFDFQGLQHQVAHVATQLEAARLLTYNAARLLEAGKPFIKEASMAKYYASE 376
Cdd:cd01151 249 IAWGALGAAEDCYHTARQYVLDRKQFGRPLAAFQLVQKKLADMLTEIALGLLACLRVGRLKDQGKATPEQISLLKRNNCG 328

                       330       340       350       360
                ....*....|....*....|....*....|....*....|...
gi 4501859  377 IAGQTTSKCIEWMGGVGYTKDYPVEKYFRDAKIGTIYEGASNI 419
Cdd:cd01151 329 KALEIARTAREMLGGNGISDEYHIIRHMVNLESVNTYEGTHDI 371
PTZ00461 PTZ00461
isovaleryl-CoA dehydrogenase; Provisional
 45-419 6.15e-71

isovaleryl-CoA dehydrogenase; Provisional


Pssm-ID: 185640 [Multi-domain]  Cd Length: 410  Bit Score: 229.44  E-value: 6.15e-71
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4501859    45 TNNGIHFAPLQTFTDEEMMIKSSVKKFAQEQIAPLVSTMDENSKMEKSVIQGLFQQGLMGIEVDPEYGGTGASFLSTVLV 124
Cdd:PTZ00461  25 TSASRAFMDLYNPTPEHAALRETVAKFSREVVDKHAREDDINMHFNRDLFKQLGDLGVMGVTVPEADGGAGMDAVAAVII 104

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4501859   125 IEELAKVDASVAVFCEIQNTLINTLIRKHGTEEQKATYLPQ-LTTEKVGSFCLSEAGAGSDSFALKTRADKEGD-YYVLN 202
Cdd:PTZ00461 105 HHELSKYDPGFCLAYLAHSMLFVNNFYYSASPAQRARWLPKvLTGEHVGAMGMSEPGAGTDVLGMRTTAKKDSNgNYVLN 184

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4501859   203 GSKMWISSAEHAGLFLVMANVDPTIgykgiTSFLVDRDTPGLHIGKPENKLGLRASSTCPLTFENVKVPEANILGQIGHG 282
Cdd:PTZ00461 185 GSKIWITNGTVADVFLIYAKVDGKI-----TAFVVERGTKGFTQGPKIDKCGMRASHMCQLFFEDVVVPAENLLGEEGKG 259

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4501859   283 YKYAIGSLNEGRIGIAAQMLGLAQGCFDYTIPYIKERIQFGKRLFDFQGLQHQVAHVATQLEAARLLTYNAARLLEAGKP 362
Cdd:PTZ00461 260 MVGMMRNLELERVTLAAMAVGIAERSVELMTSYASERKAFGKPISNFGQIQRYIAEGYADTEAAKALVYSVSHNVHPGNK 339

                        330       340       350       360       370       380
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 4501859   363 FIKEASMAKYYASEIAGQTTSKCIEWMGGVGYTKDYPVEKYFRDAKI-----GTIYEGASNI 419
Cdd:PTZ00461 340 NRLGSDAAKLFATPIAKKVADSAIQVMGGMGYSRDMPVERLWRDAKLleiggGTIEAHHKNI 401
ACAD_fadE5 cd01153
Putative acyl-CoA dehydrogenases similar to fadE5; Putative acyl-CoA dehydrogenase (ACAD). ...
 68-428 5.45e-65

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: 213.79  E-value: 5.45e-65
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4501859   68 VKKFAQEQIAPLVSTMDEN------------SKMEKSViQGLFQQGLMGIEVDPEYGGTGasfLSTVLVI---EELAKVD 132
Cdd:cd01153   5 VARLAENVLAPLNADGDREgpvfddgrvvvpPPFKEAL-DAFAEAGWMALGVPEEYGGQG---LPITVYSalaEIFSRGD 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4501859  133 ASVAVFCEIQNtLINTLIRkHGTEEQKATYLPQLTT-EKVGSFCLSEAGAGSDSFALKTRADKEGD-YYVLNGSKMWISS 210
Cdd:cd01153  81 APLMYASGTQG-AAATLLA-HGTEAQREKWIPRLAEgEWTGTMCLTEPDAGSDLGALRTKAVYQADgSWRINGVKRFISA 158

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4501859  211 AEHAG----LFLVMANV-DPTIGYKGITSFLV-----DRDTPGLHIGKPENKLGLRASSTCPLTFENVKVPeanILGQIG 280
Cdd:cd01153 159 GEHDMseniVHLVLARSeGAPPGVKGLSLFLVpkfldDGERNGVTVARIEEKMGLHGSPTCELVFDNAKGE---LIGEEG 235

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4501859  281 HGYKYAIGSLNEGRIGIAAQMLGLAQGCFDYTIPYIKERIQFGKRLFDFQglQHQVAH-------VATQ---LEAARLLT 350
Cdd:cd01153 236 MGLAQMFAMMNGARLGVGTQGTGLAEAAYLNALAYAKERKQGGDLIKAAP--AVTIIHhpdvrrsLMTQkayAEGSRALD 313

                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4501859  351 YNAARL--LEAGKPFIKEAS------------MAKYYASEIAGQTTSKCIEWMGGVGYTKDYPVEKYFRDAKIGTIYEGA 416
Cdd:cd01153 314 LYTATVqdLAERKATEGEDRkalsaladlltpVVKGFGSEAALEAVSDAIQVHGGSGYTREYPIEQYYRDARITTIYEGT 393

                       410
                ....*....|..
gi 4501859  417 SNIQLNTIAKHI 428
Cdd:cd01153 394 TGIQALDLIGRK 405
PRK12341 PRK12341
acyl-CoA dehydrogenase;
58-432 2.13e-60

acyl-CoA dehydrogenase;


Pssm-ID: 183454 [Multi-domain]  Cd Length: 381  Bit Score: 201.11  E-value: 2.13e-60
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4501859    58 TDE-EMMIKSSVKKFAQEQIAPLVSTMDENSKMEKSVIQGLFQQGLMGIEVDPEYGGTGASFLSTVLVIEELAKVDASVA 136
Cdd:PRK12341   6 TEEqELLLASIRELITRNFPEEYFRTCDENGTYPREFMRALADNGISMLGVPEEFGGTPADYVTQMLVLEEVSKCGAPAF 85

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4501859   137 VFCEIQNtlINTlIRKHGTEEQKA-TYLPQLTTEKVGsFCL--SEAGAGSDSFALKTRAD-KEGDYYvLNGSKMWISSAE 212
Cdd:PRK12341  86 LITNGQC--IHS-MRRFGSAEQLRkTAESTLETGDPA-YALalTEPGAGSDNNSATTTYTrKNGKVY-LNGQKTFITGAK 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4501859   213 HAGLFLVMA-NVDPTIGYKGITSFLVDRDTPGLHIgKPENKLGLRASSTCPLTFENVKVPEANILGQIGHGYKYAIGSLN 291
Cdd:PRK12341 161 EYPYMLVLArDPQPKDPKKAFTLWWVDSSKPGIKI-NPLHKIGWHMLSTCEVYLDNVEVEESDLVGEEGMGFLNVMYNFE 239

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4501859   292 EGRIGIAAQMLGLAQGCFDYTIPYIKERIQFGKRLFDFQGLQHQVAHVATQLEAARLLTYNAARLLEAGKPFIKEASMAK 371
Cdd:PRK12341 240 MERLINAARSLGFAECAFEDAARYANQRIQFGKPIGHNQLIQEKLTLMAIKIENMRNMVYKVAWQADNGQSLRTSAALAK 319

                        330       340       350       360       370       380
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 4501859   372 YYASEIAGQTTSKCIEWMGGVGYTKDYPVEKYFRDAKIGTIYEGASNIQLNTIAKHIDAEY 432
Cdd:PRK12341 320 LYCARTAMEVIDDAIQIMGGLGYTDEARVSRFWRDVRCERIGGGTDEIMIYIAGRQILKDY 380
Acyl-CoA_dh_1 pfam00441
Acyl-CoA dehydrogenase, C-terminal domain; C-terminal domain of Acyl-CoA dehydrogenase is an ...
 280-428 2.78e-60

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: 192.85  E-value: 2.78e-60
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4501859    280 GHGYKYAIGSLNEGRIGIAAQMLGLAQGCFDYTIPYIKERIQFGKRLFDFQGLQHQVAHVATQLEAARLLTYNAARLLEA 359
Cdd:pfam00441   1 GRGFRVAMETLNHERLAIAAMALGLARRALDEALAYARRRKAFGRPLIDFQLVRHKLAEMAAEIEAARLLVYRAAEALDA 80

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 4501859    360 GKPFIKEASMAKYYASEIAGQTTSKCIEWMGGVGYTKDYPVEKYFRDAKIGTIYEGASNIQLNTIAKHI 428
Cdd:pfam00441  81 GGPDGAEASMAKLYASEAAVEVADLAMQLHGGYGYLREYPVERLYRDARVLRIGEGTSEIQRNIIARRL 149
PLN02526 PLN02526
acyl-coenzyme A oxidase
 29-419 1.20e-57

acyl-coenzyme A oxidase


Pssm-ID: 178141 [Multi-domain]  Cd Length: 412  Bit Score: 194.69  E-value: 1.20e-57
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4501859    29 PPHVSKSSQSEALLnitnngihfaplqtfTDEEMMIKSSVKKFAQEQIAPLVSTMDENSKMEKSVIQGLFQQGLMGIEVD 108
Cdd:PLN02526  16 PPSVSDYYQFDDLL---------------TPEEQALRKRVRECMEKEVAPIMTEYWEKAEFPFHIIPKLGSLGIAGGTIK 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4501859   109 PeYGGTGASFLSTVLVIEELAKVDASVAVFCEIQNTLINTLIRKHGTEEQKATYLPQLTT-EKVGSFCLSEAGAGSDSFA 187
Cdd:PLN02526  81 G-YGCPGLSITASAIATAEVARVDASCSTFILVHSSLAMLTIALCGSEAQKQKYLPSLAQlDTVACWALTEPDYGSDASS 159

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4501859   188 LKTRADKEGDYYVLNGSKMWISSAEHAGLFLVMANVDPTigyKGITSFLVDRDTPGLHIGKPENKLGLRASSTCPLTFEN 267
Cdd:PLN02526 160 LNTTATKVEGGWILNGQKRWIGNSTFADVLVIFARNTTT---NQINGFIVKKGAPGLKATKIENKIGLRMVQNGDIVLKD 236

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4501859   268 VKVPEANILGQIgHGYKYAIGSLNEGRIGIAAQMLGLAQGCFDYTIPYIKERIQFGKRLFDFQGLQHQVAHVATQLEAAR 347
Cdd:PLN02526 237 VFVPDEDRLPGV-NSFQDTNKVLAVSRVMVAWQPIGISMGVYDMCHRYLKERKQFGAPLAAFQINQEKLVRMLGNIQAMF 315

                        330       340       350       360       370       380       390
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 4501859   348 LLTYNAARLLEAGKPFIKEASMAKYYASEIAGQTTSKCIEWMGGVGYTKDYPVEKYFRDAKIGTIYEGASNI 419
Cdd:PLN02526 316 LVGWRLCKLYESGKMTPGHASLGKAWITKKARETVALGRELLGGNGILADFLVAKAFCDLEPIYTYEGTYDI 387
ACAD_fadE6_17_26 cd01152
Putative acyl-CoA dehydrogenases similar to fadE6, fadE17, and fadE26; Putative acyl-CoA ...
 97-428 1.15e-55

Putative acyl-CoA dehydrogenases similar to fadE6, fadE17, and fadE26; Putative acyl-CoA dehydrogenases (ACAD). Mitochondrial acyl-CoA dehydrogenases (ACAD) catalyze the alpha, beta dehydrogenation of the corresponding trans-enoyl-CoA by FAD, which becomes reduced. The reduced form of ACAD is reoxidized in the oxidative half-reaction by electron-transferring flavoprotein (ETF), from which the electrons are transferred to the mitochondrial respiratory chain coupled with ATP synthesis. The ACD family includes the eukaryotic beta-oxidation, as well as amino acid catabolism enzymes. These enzymes share high sequence similarity, but differ in their substrate specificities. The mitochondrial ACD's are generally homotetramers and have an active site glutamate at a conserved position.


Pssm-ID: 173841 [Multi-domain]  Cd Length: 380  Bit Score: 188.71  E-value: 1.15e-55
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4501859   97 LFQQGLMGIEVDPEYGGTGASFLSTVLVIEELAKVDASVAVFCEIQNTLINTLIRkHGTEEQKATYLPQ-LTTEKVgsFC 175
Cdd:cd01152  44 LAAAGWAAPGWPKEYGGRGASLMEQLIFREEMAAAGAPVPFNQIGIDLAGPTILA-YGTDEQKRRFLPPiLSGEEI--WC 120

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4501859  176 L--SEAGAGSDSFALKTRADKEGDYYVLNGSKMWISSAEHAGLFLVMANVDPTI-GYKGITSFLVDRDTPGLHIgKPENK 252
Cdd:cd01152 121 QgfSEPGAGSDLAGLRTRAVRDGDDWVVNGQKIWTSGAHYADWAWLLVRTDPEApKHRGISILLVDMDSPGVTV-RPIRS 199

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4501859  253 LgLRASSTCPLTFENVKVPEANILGQIGHGYKYAIGSLNEGR---IGIAAQMLGLAQGCFDYTIPYikeriqfGKRLFDF 329
Cdd:cd01152 200 I-NGGEFFNEVFLDDVRVPDANRVGEVNDGWKVAMTTLNFERvsiGGSAATFFELLLARLLLLTRD-------GRPLIDD 271

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4501859  330 QGLQHQVAHVATQLEAARLLTYNAARLLEAGKPFIKEASMAKYYASEIAGQTTSKCIEWMG--------GVGYTKDYPVE 401
Cdd:cd01152 272 PLVRQRLARLEAEAEALRLLVFRLASALAAGKPPGAEASIAKLFGSELAQELAELALELLGtaallrdpAPGAELAGRWE 351

                       330       340
                ....*....|....*....|....*..
gi 4501859  402 KYFRDAKIGTIYEGASNIQLNTIAKHI 428
Cdd:cd01152 352 ADYLRSRATTIYGGTSEIQRNIIAERL 378
PRK03354 PRK03354
crotonobetainyl-CoA dehydrogenase; Validated
 56-432 9.52e-51

crotonobetainyl-CoA dehydrogenase; Validated


Pssm-ID: 179566 [Multi-domain]  Cd Length: 380  Bit Score: 175.79  E-value: 9.52e-51
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4501859    56 TFTDEEMMIKSSVKKF-AQEQIAPLVSTMDENSKMEKSVIQGLFQQGLMGIEVDPEYGGTGASFLSTVLVIEELAKVDAS 134
Cdd:PRK03354   4 NLNDEQELFVAGIRELmASENWEAYFAECDRDSVYPERFVKALADMGIDSLLIPEEHGGLDAGFVTLAAVWMELGRLGAP 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4501859   135 VAVFCEIQNTlINTLIRkHGTEEQKATYLPQLTT-EKVGSFCLSEAGAGSDSFALKTRADKEGDYYVLNGSKMWISSAEH 213
Cdd:PRK03354  84 TYVLYQLPGG-FNTFLR-EGTQEQIDKIMAFRGTgKQMWNSAITEPGAGSDVGSLKTTYTRRNGKVYLNGSKCFITSSAY 161

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4501859   214 AGLFLVMANVDPTIGYKGITSFLVDRDTPGLHIGKPEnKLGLRASSTCPLTFENVKVPEANILGQIGHGYKYAIGSLNEG 293
Cdd:PRK03354 162 TPYIVVMARDGASPDKPVYTEWFVDMSKPGIKVTKLE-KLGLRMDSCCEITFDDVELDEKDMFGREGNGFNRVKEEFDHE 240

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4501859   294 RIGIAAQMLGLAQGCFDYTIPYIKERIQFGKRLFDFQGLQHQVAHVATQLEAARLLTYNAARLLEAGKPFIKEASMAKYY 373
Cdd:PRK03354 241 RFLVALTNYGTAMCAFEDAARYANQRVQFGEAIGRFQLIQEKFAHMAIKLNSMKNMLYEAAWKADNGTITSGDAAMCKYF 320

                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 4501859   374 ASEIAGQTTSKCIEWMGGVGYTKDYPVEKYFRDAKIGTIYEGASNIQLNTIAKHIDAEY 432
Cdd:PRK03354 321 CANAAFEVVDSAMQVLGGVGIAGNHRISRFWRDLRVDRVSGGSDEMQILTLGRAVLKQY 379
AidB cd01154
Proteins involved in DNA damage response, similar to the AidB gene product; AidB is one of ...
 94-420 2.21e-42

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: 154.45  E-value: 2.21e-42
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4501859   94 IQGLFQQGLMGIEV-DPEYGGTGASFLSTVLVieelakVDASVAVFCEIQNTLINT-LIRKHGTEEQKaTYLPQLTTEKV 171
Cdd:cd01154  71 MRRLIEEGVINIEDgPAGEGRRHVHFAAGYLL------SDAAAGLLCPLTMTDAAVyALRKYGPEELK-QYLPGLLSDRY 143

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4501859  172 -----GSFCLSEAGAGSDSFALKTRADK-EGDYYVLNGSKmWISSAEHAGLFLVMAN-VDPTIGYKGITSFLVDRDTP-- 242
Cdd:cd01154 144 ktgllGGTWMTEKQGGSDLGANETTAERsGGGVYRLNGHK-WFASAPLADAALVLARpEGAPAGARGLSLFLVPRLLEdg 222

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4501859  243 ---GLHIGKPENKLGLRASSTCPLTFENVkvpEANILGQIGHGYKYAIGSLNEGRIGIAAQMLGLAQGCFDYTIPYIKER 319
Cdd:cd01154 223 trnGYRIRRLKDKLGTRSVATGEVEFDDA---EAYLIGDEGKGIYYILEMLNISRLDNAVAALGIMRRALSEAYHYARHR 299

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4501859  320 IQFGKRLFDFQGLQHQVAHVATQLEAARLLTYNAARLL---EAGKPfiKEASMA-------KYYASEIAGQTTSKCIEWM 389
Cdd:cd01154 300 RAFGKPLIDHPLMRRDLAEMEVDVEAATALTFRAARAFdraAADKP--VEAHMArlatpvaKLIACKRAAPVTSEAMEVF 377

                       330       340       350
                ....*....|....*....|....*....|.
gi 4501859  390 GGVGYTKDYPVEKYFRDAKIGTIYEGASNIQ 420
Cdd:cd01154 378 GGNGYLEEWPVARLHREAQVTPIWEGTGNIQ 408
ACAD_FadE2 cd01155
Acyl-CoA dehydrogenases similar to fadE2; FadE2-like Acyl-CoA dehydrogenase (ACAD). Acyl-CoA ...
 68-426 2.15e-40

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: 148.31  E-value: 2.15e-40
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4501859   68 VKKFAQEQIAPLVSTMDE------NSKMEKS-VIQGLFQ----QGLMGIEVDPEYGGTGASFLSTVLVIEELAK-VDASV 135
Cdd:cd01155  10 VKAFMEEHVYPAEQEFLEyyaeggDRWWTPPpIIEKLKAkakaEGLWNLFLPEVSGLSGLTNLEYAYLAEETGRsFFAPE 89

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4501859  136 AVFCEIQNTLINTLIRKHGTEEQKATYLPQLTTEKVGS-FCLSEAG-AGSDSFALKTRADKEGDYYVLNGSKMWISSAEH 213
Cdd:cd01155  90 VFNCQAPDTGNMEVLHRYGSEEQKKQWLEPLLDGKIRSaFAMTEPDvASSDATNIECSIERDGDDYVINGRKWWSSGAGD 169

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4501859  214 --AGLFLVMANVDPTIG--YKGITSFLVDRDTPGLHIGKPENKLGLRAS--STCPLTFENVKVPEANILGQIGHGYKYAI 287
Cdd:cd01155 170 prCKIAIVMGRTDPDGAprHRQQSMILVPMDTPGVTIIRPLSVFGYDDAphGHAEITFDNVRVPASNLILGEGRGFEIAQ 249

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4501859  288 GSLNEGRIGIAAQMLGLAQGCFDYTIPYIKERIQFGKRLFDFQGLQHQVAHVATQLEAARLLTYNAARLLEAGKPFI--K 365
Cdd:cd01155 250 GRLGPGRIHHCMRLIGAAERALELMCQRAVSREAFGKKLAQHGVVAHWIAKSRIEIEQARLLVLKAAHMIDTVGNKAarK 329

                       330       340       350       360       370       380
                ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 4501859  366 EASMAKYYASEIAGQTTSKCIEWMGGVGYTKDYPVEKYFRDAKIGTIYEGASNIQLNTIAK 426
Cdd:cd01155 330 EIAMIKVAAPRMALKIIDRAIQVHGAAGVSQDTPLANMYAWARTLRIADGPDEVHLRSIAR 390
Acyl-CoA_dh_N pfam02771
Acyl-CoA dehydrogenase, N-terminal domain; The N-terminal domain of Acyl-CoA dehydrogenase is ...
 58-168 7.29e-38

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: 133.36  E-value: 7.29e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4501859     58 TDEEMMIKSSVKKFAQEQIAPLVSTMDENSKMEKSVIQGLFQQGLMGIEVDPEYGGTGASFLSTVLVIEELAKVDASVAV 137
Cdd:pfam02771   1 TEEQEALRDTVREFAEEEIAPHAAEWDEEGEFPRELWKKLGELGLLGITIPEEYGGAGLDYLAYALVAEELARADASVAL 80

                          90       100       110
                  ....*....|....*....|....*....|.
gi 4501859    138 FCEIQNTLINTLIRKHGTEEQKATYLPQLTT 168
Cdd:pfam02771  81 ALSVHSSLGAPPILRFGTEEQKERYLPKLAS 111
PTZ00456 PTZ00456
acyl-CoA dehydrogenase; Provisional
 70-428 6.82e-37

acyl-CoA dehydrogenase; Provisional


Pssm-ID: 185635 [Multi-domain]  Cd Length: 622  Bit Score: 142.31  E-value: 6.82e-37
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4501859    70 KFAQEQIAPLVSTMDENS------------KMEKSVIQGLFQQGLMGIEVDPEYGGTGASFLSTVLVIEELAKVDASVAV 137
Cdd:PTZ00456  69 KLATQTLLPLYESSDSEGcvllkdgnvttpKGFKEAYQALKAGGWTGISEPEEYGGQALPLSVGFITRELMATANWGFSM 148

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4501859   138 FCEIQNTLINTLIrKHGTEEQKATYLPQLTT-EKVGSFCLSEAGAGSDSFALKTRADKEGD-YYVLNGSKMWISSAEHAG 215
Cdd:PTZ00456 149 YPGLSIGAANTLM-AWGSEEQKEQYLTKLVSgEWSGTMCLTEPQCGTDLGQVKTKAEPSADgSYKITGTKIFISAGDHDL 227

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4501859   216 ----LFLVMANVDPTI-GYKGITSFLVDRdtpglHIGKP---------------ENKLGLRASSTCPLTFENVKvpeANI 275
Cdd:PTZ00456 228 teniVHIVLARLPNSLpTTKGLSLFLVPR-----HVVKPdgsletaknvkciglEKKMGIKGSSTCQLSFENSV---GYL 299

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4501859   276 LGQIGHGYKYAIGSLNEGRIGIAAQMLGLAQGCFDYTIPYIKERIQF------------GKRLFDFQGLQHQVAHVATQL 343
Cdd:PTZ00456 300 IGEPNAGMKQMFTFMNTARVGTALEGVCHAELAFQNALRYARERRSMralsgtkepekpADRIICHANVRQNILFAKAVA 379

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4501859   344 EAARLLTYNAARLL----EAGKPFIKEA---------SMAKYYASEIAGQTTSKCIEWMGGVGYTKDYPVEKYFRDAKIG 410
Cdd:PTZ00456 380 EGGRALLLDVGRLLdihaAAKDAATREAldheigfytPIAKGCLTEWGVEAASRCLQVWGGHGYIKGNGMEQILRDARIG 459

                        410
                 ....*....|....*....
gi 4501859   411 TIYEGASNIQ-LNTIAKHI 428
Cdd:PTZ00456 460 TLYEGTTGIQaLDFIGRKV 478
Acyl-CoA_dh_M pfam02770
Acyl-CoA dehydrogenase, middle domain; Central domain of Acyl-CoA dehydrogenase has a ...
 173-266 4.36e-30

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


Pssm-ID: 460685 [Multi-domain]  Cd Length: 95  Bit Score: 111.99  E-value: 4.36e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4501859    173 SFCLSEAGAGSDSFALKTRA-DKEGDYYVLNGSKMWISSAEHAGLFLVMANVDPTIGYKGITSFLVDRDTPGLHIGKPEN 251
Cdd:pfam02770   1 AFALTEPGAGSDVASLKTTAaDGDGGGWVLNGTKWWITNAGIADLFLVLARTGGDDRHGGISLFLVPKDAPGVSVRRIET 80

                          90
                  ....*....|....*
gi 4501859    252 KLGLRASSTCPLTFE 266
Cdd:pfam02770  81 KLGVRGLPTGELVFD 95
Acyl-CoA_dh_2 pfam08028
Acyl-CoA dehydrogenase, C-terminal domain;
296-417 4.80e-28

Acyl-CoA dehydrogenase, C-terminal domain;


Pssm-ID: 429790 [Multi-domain]  Cd Length: 133  Bit Score: 107.82  E-value: 4.80e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4501859    296 GIAAQMLGLAQGCFDYTIPYIKERIQ--FGKRLFDFQGLQHQVAHVATQLEAARLLTYNAA----RLLEAGKPF----IK 365
Cdd:pfam08028   1 GIAAAALGAARAALAEFTERARGRVRayFGVPLAEDPATQLALAEAAARIDAARLLLERAAarieAAAAAGKPVtpalRA 80

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|..
gi 4501859    366 EASMAKYYASEIAGQTTSKCIEWMGGVGYTKDYPVEKYFRDAKIGTIYEGAS 417
Cdd:pfam08028  81 EARRAAAFATELAVAAVDALFRAAGGSALFQDSPLQRIWRDIHAAAQHAAVN 132
PLN02876 PLN02876
acyl-CoA dehydrogenase
 152-426 2.42e-27

acyl-CoA dehydrogenase


Pssm-ID: 215473 [Multi-domain]  Cd Length: 822  Bit Score: 114.89  E-value: 2.42e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4501859   152 KHGTEEQKATYLPQLTTEKVGS-FCLSEAG-AGSDSFALKTRADKEGDYYVLNGSKMWISSA--EHAGLFLVMANVDPTI 227
Cdd:PLN02876 531 RYGNKEQQLEWLIPLLEGKIRSgFAMTEPQvASSDATNIECSIRRQGDSYVINGTKWWTSGAmdPRCRVLIVMGKTDFNA 610

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4501859   228 G-YKGITSFLVDRDTPGLHIGKPENKLGLRAS--STCPLTFENVKVPEANILGQIGHGYKYAIGSLNEGRIGIAAQMLGL 304
Cdd:PLN02876 611 PkHKQQSMILVDIQTPGVQIKRPLLVFGFDDAphGHAEISFENVRVPAKNILLGEGRGFEIAQGRLGPGRLHHCMRLIGA 690

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4501859   305 AQGCFDYTIPYIKERIQFGKRLFDFQGLQHQVAHVATQLEAARLLTYNAARLLE--AGKPFIKEASMAKYYASEIAGQTT 382
Cdd:PLN02876 691 AERGMQLMVQRALSRKAFGKLIAQHGSFLSDLAKCRVELEQTRLLVLEAADQLDrlGNKKARGIIAMAKVAAPNMALKVL 770

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....
gi 4501859   383 SKCIEWMGGVGYTKDYPVEKYFRDAKIGTIYEGASNIQLNTIAK 426
Cdd:PLN02876 771 DMAMQVHGAAGVSSDTVLAHLWATARTLRIADGPDEVHLGTIAK 814
PRK13026 PRK13026
acyl-CoA dehydrogenase; Reviewed
 50-378 3.10e-23

acyl-CoA dehydrogenase; Reviewed


Pssm-ID: 237277 [Multi-domain]  Cd Length: 774  Bit Score: 102.73  E-value: 3.10e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4501859    50 HFAPLQTFTDEEmmikssvKKFAQEQIAPLVSTMDE-----NSK-MEKSVIQGLFQQGLMGIEVDPEYGGTGASFLSTVL 123
Cdd:PRK13026  71 HSYPKPTLTAEE-------QAFIDNEVETLLTMLDDwdivqNRKdLPPEVWDYLKKEGFFALIIPKEYGGKGFSAYANST 143

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4501859   124 VIEELAKVDASVAVFCEIQNTL-INTLIRKHGTEEQKATYLPQLTT-EKVGSFCLSEAGAGSDSFALK-----TRADKEG 196
Cdd:PRK13026 144 IVSKIATRSVSAAVTVMVPNSLgPGELLTHYGTQEQKDYWLPRLADgTEIPCFALTGPEAGSDAGAIPdtgivCRGEFEG 223

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4501859   197 DYYV---LNGSKMWISSAEHA---GLFLVMANVDPTIGYK---GITSFLVDRDTPGLHIGKPENKLGLrASSTCPLTFEN 267
Cdd:PRK13026 224 EEVLglrLTWDKRYITLAPVAtvlGLAFKLRDPDGLLGDKkelGITCALIPTDHPGVEIGRRHNPLGM-AFMNGTTRGKD 302

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4501859   268 VKVPEANILG---QIGHGYKYAIGSLNEGRiGIAAQMLGLAQG--CFDYTIPYIKERIQFGKRLFDFQGLQHQVAHVAT- 341
Cdd:PRK13026 303 VFIPLDWIIGgpdYAGRGWRMLVECLSAGR-GISLPALGTASGhmATRTTGAYAYVRRQFGMPIGQFEGVQEALARIAGn 381

                        330       340       350       360
                 ....*....|....*....|....*....|....*....|
gi 4501859   342 --QLEAARLLTYNAarlLEAG-KPFIKEAsMAKYYASEIA 378
Cdd:PRK13026 382 tyLLEAARRLTTTG---LDLGvKPSVVTA-IAKYHMTELA 417
fadE PRK09463
acyl-CoA dehydrogenase; Reviewed
 110-381 2.42e-17

acyl-CoA dehydrogenase; Reviewed


Pssm-ID: 236528 [Multi-domain]  Cd Length: 777  Bit Score: 84.48  E-value: 2.42e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4501859   110 EYGGTGASFLSTVLVIEELAKVDASVAVFCEIQNTL-INTLIRKHGTEEQKATYLPQLTT-EKVGSFCLSEAGAGSDSFA 187
Cdd:PRK09463 131 EYGGLEFSAYAHSRVLQKLASRSGTLAVTVMVPNSLgPGELLLHYGTDEQKDHYLPRLARgEEIPCFALTSPEAGSDAGS 210

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4501859   188 LK-----TRADKEGD---YYVLNGSKMWISSAEHAGLF-LVMANVDPT--IGYK---GITSFLVDRDTPGLHIGKPENKL 253
Cdd:PRK09463 211 IPdtgvvCKGEWQGEevlGMRLTWNKRYITLAPIATVLgLAFKLYDPDglLGDKedlGITCALIPTDTPGVEIGRRHFPL 290

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4501859   254 GLrASSTCPLTFENVKVPEANILG---QIGHGYKYAIGSLNEGR-IGIAAQMLGLAQGCFDYTIPYIKERIQFGKRLFDF 329
Cdd:PRK09463 291 NV-PFQNGPTRGKDVFIPLDYIIGgpkMAGQGWRMLMECLSVGRgISLPSNSTGGAKLAALATGAYARIRRQFKLPIGKF 369

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 4501859   330 QGLQHQVAHVAT---QLEAARLLTYNAARLLEagKPFIKEAsMAKYYASEIAGQT 381
Cdd:PRK09463 370 EGIEEPLARIAGnayLMDAARTLTTAAVDLGE--KPSVLSA-IAKYHLTERGRQV 421
NcnH cd01159
Naphthocyclinone hydroxylase; Naphthocyclinone is an aromatic polyketide and an antibiotic, ...
 74-407 3.87e-17

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: 82.40  E-value: 3.87e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4501859   74 EQIAPLVST----MDENSKMEKSVIQGLFQQGLMGIEVDPEYGGTGASFLSTVLVIEELAKVDASVAVFCEIQntlintl 149
Cdd:cd01159   4 EDLAPLIRErapeAERARRLPDEVVRALREIGFFRMFVPKRYGGLEGDFAEFAEAIATLAEACGSAAWVASIV------- 76

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4501859  150 irkhGTEEQKATYLPQLTTEKVgsfcLSEAGAG--SDSFALKTRADKEGDYYVLNGSKMWISSAEHAGLFLVMANVDPTI 227
Cdd:cd01159  77 ----ATHSRMLAAFPPEAQEEV----WGDGPDTllAGSYAPGGRAERVDGGYRVSGTWPFASGCDHADWILVGAIVEDDD 148

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4501859  228 GYKGITSFLVDRDtpGLHIGKPENKLGLRASSTCPLTFENVKVPEANIL-----------GQIGHGYKYAIGSLNEgrIG 296
Cdd:cd01159 149 GGPLPRAFVVPRA--EYEIVDTWHVVGLRGTGSNTVVVDDVFVPEHRTLtagdmmagdgpGGSTPVYRMPLRQVFP--LS 224

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4501859  297 IAAQMLGLAQGCFDYTIPYIKERIQ---FGKRLFDFQGLQHQVAHVATQLEAARLLTYNAARLLEA----GKPFIKEASM 369
Cdd:cd01159 225 FAAVSLGAAEGALAEFLELAGKRVRqygAAVKMAEAPITQLRLAEAAAELDAARAFLERATRDLWAhalaGGPIDVEERA 304

                       330       340       350       360
                ....*....|....*....|....*....|....*....|..
gi 4501859  370 ----AKYYASEIAGQTTSKCIEWMGGVGYTKDYPVEKYFRDA 407
Cdd:cd01159 305 rirrDAAYAAKLSAEAVDRLFHAAGGSALYTASPLQRIWRDI 346
DszC cd01163
Dibenzothiophene (DBT) desulfurization enzyme C; DszC is a flavin reductase dependent enzyme, ...
 94-408 1.01e-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: 72.36  E-value: 1.01e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4501859   94 IQGLFQQGLMGIEVDPEYGGTGASFLSTVLVIEELAKVDASVAVFCEIQNTLINTLiRKHGTEEQKATYLPQLTTEKVGS 173
Cdd:cd01163  28 VALLRQSGLGTLRVPKEYGGLGASLPDLYEVVRELAAADSNIAQALRAHFGFVEAL-LLAGPEQFRKRWFGRVLNGWIFG 106

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4501859  174 FCLSEAGAGSDSFALkTRADKEGDYYVLNGSKMWISSAEHAGLFLVMAnVDPTigyKGITSFLVDRDTPGLHIGKPENKL 253
Cdd:cd01163 107 NAVSERGSVRPGTFL-TATVRDGGGYVLNGKKFYSTGALFSDWVTVSA-LDEE---GKLVFAAVPTDRPGITVVDDWDGF 181

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4501859  254 GLR--ASSTcpLTFENVKVPEANILGQighGYKYAIGSLNEGRIGI--AAQMLGLAQGCFDYTIPYIKERiqfgKRLF-- 327
Cdd:cd01163 182 GQRltASGT--VTFDNVRVEPDEVLPR---PNAPDRGTLLTAIYQLvlAAVLAGIARAALDDAVAYVRSR----TRPWih 252

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4501859  328 --------DFQGLQHqVAHVATQLEAARLLTYNAARLLE----AGKPFIKEA--------SMAKYYASEIAGQTTSKCIE 387
Cdd:cd01163 253 sgaesardDPYVQQV-VGDLAARLHAAEALVLQAARALDaaaaAGTALTAEArgeaalavAAAKVVVTRLALDATSRLFE 331

                       330       340
                ....*....|....*....|.
gi 4501859  388 WMGGVGYTKDYPVEKYFRDAK 408
Cdd:cd01163 332 VGGASATAREHNLDRHWRNAR 352
AXO cd01150
Peroxisomal acyl-CoA oxidase; Peroxisomal acyl-CoA oxidases (AXO) catalyze the first set in ...
 141-428 3.00e-13

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: 71.59  E-value: 3.00e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4501859  141 IQNTLINTLIRKHGTEEQKATYLP-QLTTEKVGSFCLSEAGAGSDSFALKTRA--DKEGDYYVLN-----GSKMWIS--- 209
Cdd:cd01150 104 LHLGLFGNAIKNLGTDEHQDYWLQgANNLEIIGCFAQTELGHGSNLQGLETTAtyDPLTQEFVINtpdftATKWWPGnlg 183

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4501859  210 -SAEHAGLF--LVMANVDptigyKGITSFLV---DRDT----PGLHIGKPENKLGLRASSTCPLTFENVKVPEANIL--- 276
Cdd:cd01150 184 kTATHAVVFaqLITPGKN-----HGLHAFIVpirDPKThqplPGVTVGDIGPKMGLNGVDNGFLQFRNVRIPRENLLnrf 258

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4501859  277 GQI-------------GHGYKYAIGSLNEGRIGIAaqMLGLAQGCFDYTIP--YIKERIQFGKR-------LFDFQGLQH 334
Cdd:cd01150 259 GDVspdgtyvspfkdpNKRYGAMLGTRSGGRVGLI--YDAAMSLKKAATIAirYSAVRRQFGPKpsdpevqILDYQLQQY 336

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4501859  335 ----QVAHVATQLEAARLL--TYNA--ARLLEAGKPFIKE----ASMAKYYASEIAGQTTSKCIEWMGGVGYTKDYPVEK 402
Cdd:cd01150 337 rlfpQLAAAYAFHFAAKSLveMYHEiiKELLQGNSELLAElhalSAGLKAVATWTAAQGIQECREACGGHGYLAMNRLPT 416

                       330       340
                ....*....|....*....|....*.
gi 4501859  403 YFRDAKIGTIYEGASNIQLNTIAKHI 428
Cdd:cd01150 417 LRDDNDPFCTYEGDNTVLLQQTANYL 442
PRK11561 PRK11561
isovaleryl CoA dehydrogenase; Provisional
 176-419 1.04e-12

isovaleryl CoA dehydrogenase; Provisional


Pssm-ID: 183199 [Multi-domain]  Cd Length: 538  Bit Score: 69.78  E-value: 1.04e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4501859   176 LSEAGAGSDSFALKTRADK-EGDYYVLNGSKmWISSAEHAGLFLVMANVDptigyKGITSFLVDRDTP-----GLHIGKP 249
Cdd:PRK11561 184 MTEKQGGSDVLSNTTRAERlADGSYRLVGHK-WFFSVPQSDAHLVLAQAK-----GGLSCFFVPRFLPdgqrnAIRLERL 257

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4501859   250 ENKLGLRASSTCPLTFENVKvpeANILGQIGHGYKYAIGSLNEGRIGIAAQMLGLAQGCFDYTIPYIKERIQFGKRLFDf 329
Cdd:PRK11561 258 KDKLGNRSNASSEVEFQDAI---GWLLGEEGEGIRLILKMGGMTRFDCALGSHGLMRRAFSVAIYHAHQRQVFGKPLIE- 333

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4501859   330 QGLQHQV-AHVATQLEA-----------------------ARLLTYNAA-RLLEAGKPFIKEAsmakyyaseiagqttsk 384
Cdd:PRK11561 334 QPLMRQVlSRMALQLEGqtallfrlarawdrradakealwARLFTPAAKfVICKRGIPFVAEA----------------- 396

                        250       260       270
                 ....*....|....*....|....*....|....*
gi 4501859   385 cIEWMGGVGYTKDYPVEKYFRDAKIGTIYEGASNI 419
Cdd:PRK11561 397 -MEVLGGIGYCEESELPRLYREMPVNSIWEGSGNI 430
PLN02636 PLN02636
acyl-coenzyme A oxidase
 124-432 1.37e-10

acyl-coenzyme A oxidase


Pssm-ID: 215342 [Multi-domain]  Cd Length: 686  Bit Score: 63.34  E-value: 1.37e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4501859   124 VIEELAKVDASVAVFCEIQNTLINTLIRKHGTEEQKATYLPQLTT-EKVGSFCLSEAGAGSDSFALKTRA--DKEGDYYV 200
Cdd:PLN02636 126 ITEAVGSVDMSLGIKLGVQYSLWGGSVINLGTKKHRDKYFDGIDNlDYPGCFAMTELHHGSNVQGLQTTAtfDPLTDEFV 205

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4501859   201 LN-----GSKMWISSAEHAGLFL-VMANVD-PTIGYKGIT-----SFLVD-RDT------PGLHIGKPENKLGLRASSTC 261
Cdd:PLN02636 206 INtpndgAIKWWIGNAAVHGKFAtVFARLKlPTHDSKGVSdmgvhAFIVPiRDMkthqvlPGVEIRDCGHKVGLNGVDNG 285

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4501859   262 PLTFENVKVPEANILGQIGH-----GYKYAIGSLNE-----------GRIGIAAQMLGLAQGCFDYTIPYIKERIQFGK- 324
Cdd:PLN02636 286 ALRFRSVRIPRDNLLNRFGDvsrdgKYTSSLPTINKrfaatlgelvgGRVGLAYGSVGVLKASNTIAIRYSLLRQQFGPp 365

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4501859   325 -----RLFDFQGLQHQVAHVATQLEAARLLT-YNAARLLEAGKPFIKE--------ASMAKYYASEIAGQTTSKCIEWMG 390
Cdd:PLN02636 366 kqpeiSILDYQSQQHKLMPMLASTYAFHFATeYLVERYSEMKKTHDDQlvadvhalSAGLKAYITSYTAKALSTCREACG 445

                        330       340       350       360
                 ....*....|....*....|....*....|....*....|..
gi 4501859   391 GVGYTKDYPVEKYFRDAKIGTIYEGASNIQLNTIAKHIDAEY 432
Cdd:PLN02636 446 GHGYAAVNRFGSLRNDHDIFQTFEGDNTVLLQQVAADLLKQY 487
PTZ00457 PTZ00457
acyl-CoA dehydrogenase; Provisional
 102-304 1.69e-06

acyl-CoA dehydrogenase; Provisional


Pssm-ID: 185636 [Multi-domain]  Cd Length: 520  Bit Score: 50.26  E-value: 1.69e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4501859   102 LMGIEVDPEYGGTGASFLSTVLVIEEL-AKVDASvaVFCEIQNTLINT-LIRKHGTEEQKATYLPQLTTEKVGSFCLSEA 179
Cdd:PTZ00457  65 LYGARIATEYGGLGLGHTAHALIYEEVgTNCDSK--LLSTIQHSGFCTyLLSTVGSKELKGKYLTAMSDGTIMMGWATEE 142

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4501859   180 GAGSDSFALKTRADKEGD-YYVLNGSKMWIsSAEHAGLFLVMAN-VDPTIGYKGITS------FLVDRDTPGLHIGKPEn 251
Cdd:PTZ00457 143 GCGSDISMNTTKASLTDDgSYVLTGQKRCE-FAASATHFLVLAKtLTQTAAEEGATEvsrnsfFICAKDAKGVSVNGDS- 220

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|...
gi 4501859   252 klglrasstcpLTFENvkVPEANILGQIGHGYKYAIGSLNEGRIGIAAQMLGL 304
Cdd:PTZ00457 221 -----------VVFEN--TPAADVVGVVGEGFKDAMITLFTEQYLYAASLLGI 260
PTZ00460 PTZ00460
acyl-CoA dehydrogenase; Provisional
 150-336 3.73e-04

acyl-CoA dehydrogenase; Provisional


Pssm-ID: 185639 [Multi-domain]  Cd Length: 646  Bit Score: 42.91  E-value: 3.73e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4501859   150 IRKHGTEEQKATYLPQ-LTTEKVGSFCLSEAGAGSDSFALKTRA--DKEGDYYVLN-----GSKMWISS----AEHAglf 217
Cdd:PTZ00460 106 FQVLGTDEQINLWMPSlLNFEIVGCYAQTELGHGSDVQNLETTAtyDKQTNEFVIHtpsveAVKFWPGElgflCNFA--- 182

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4501859   218 LVMANVDPTIGYKGITSFLV---DRDT----PGLHIGKPENKLGLRASSTCPLTFENVKVPEANIL---------GQIG- 280
Cdd:PTZ00460 183 LVYAKLIVNGKNKGVHPFMVrirDKEThkplQGVEVGDIGPKMGYAVKDNGFLSFDHYRIPLDSLLaryikvsedGQVEr 262

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 4501859   281 HGykyaigslNEgRIGIAAQMLGLAQGCFDYT----------IPYIKERIQFGK------RLFDFQGLQHQV 336
Cdd:PTZ00460 263 QG--------NP-KVSYASMMYMRNLIIDQYPrfaaqaltvaIRYSIYRQQFTNdnkqenSVLEYQTQQQKL 325
PLN02312 PLN02312
acyl-CoA oxidase
 82-276 2.10e-03

acyl-CoA oxidase


Pssm-ID: 215178 [Multi-domain]  Cd Length: 680  Bit Score: 40.53  E-value: 2.10e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4501859    82 TMDENSKMEKSVIQ-----GLFQQGLMGIEVDPEyggtgasfLSTVLVIEELAKVDASVAVFCEIQNTLINTLIRKHGTE 156
Cdd:PLN02312  99 TMEQQREITMKRILyllerGVFRGWLTETGPEAE--------LRKLALLEVIGIYDHSLAIKLGVHFFLWGGAIKFLGTK 170

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4501859   157 EQKATYLPQLTTEKV-GSFCLSEAGAGSDSFALKTRA--DKEGDYYVLN-----GSKMWIS-SAEHAGLFLVMANVDPTI 227
Cdd:PLN02312 171 RHHDKWLKDTEDYVVkGCFAMTELGHGSNVRGIETVTtyDPKTEEFVINtpcesAQKYWIGgAANHATHTIVFSQLHING 250

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 4501859   228 GYKGITSFLVD-RDT-----PGLHIGKPENKLGLRASSTCPLTFENVKVPEANIL 276
Cdd:PLN02312 251 KNEGVHAFIAQiRDQdgnicPNIRIADCGHKIGLNGVDNGRIWFDNLRIPRENLL 305
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
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