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Conserved domains on  [gi|187960098|ref|NP_001120800|]
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medium-chain specific acyl-CoA dehydrogenase, mitochondrial isoform b precursor [Homo sapiens]

Protein Classification

medium-chain specific acyl-CoA dehydrogenase( domain architecture ID 10100180)

mitochondrial medium-chain specific acyl-CoA dehydrogenase (MCAD) is one of the acyl-CoA dehydrogenases that catalyze the first step of mitochondrial fatty acid beta-oxidation, an aerobic process breaking down fatty acids into acetyl-CoA and allowing the production of energy from fats

EC:  1.3.8.7
Gene Ontology:  GO:0050660|GO:0016627
PubMed:  12504675

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
MCAD cd01157
Medium chain acyl-CoA dehydrogenase; MCADs are mitochondrial beta-oxidation enzymes, which ...
 45-422 0e+00

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: 797.95  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187960098  45 FTEQQKEFQATARKFAREEIIPVAAEYDKTGEYPVPLIRRAWELGLMNTHIPENCGGLGLGTFDACLISEELAYGCTGVQ 124
Cdd:cd01157    1 LTEQQKEFQETARKFAREEIIPVAAEYDKSGEYPWPLIKRAWELGLMNTHIPEDCGGLGLGTFDTCLITEELAYGCTGVQ 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187960098 125 TAIEGNSLGQMPIIIAGNDQQKKKYLGRMTEEPLMCAYCVTEPGAGSDVAGIKTKAEKKGDEYIINGQKMWITNGGKANW 204
Cdd:cd01157   81 TAIEANSLGQMPVIISGNDEQKKKYLGRMTEEPLMCAYCVTEPGAGSDVAGIKTKAEKKGDEYIINGQKMWITNGGKANW 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187960098 205 YFLLARSDPDPKAPANKAFTGFIVEADTPGIQIGRKELNMGQRCSDTRGIVFEDVKVPKENVLIGDGAGFKVAMGAFDKT 284
Cdd:cd01157  161 YFLLARSDPDPKCPASKAFTGFIVEADTPGIQPGRKELNMGQRCSDTRGITFEDVRVPKENVLIGEGAGFKIAMGAFDKT 240

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187960098 285 RPVVAAGAVGLAQRALDEATKYALERKTFGKLLVEHQAISFMLAEMAMKVELARMSYQRAAWEVDSGRRNTYYASIAKAF 364
Cdd:cd01157  241 RPPVAAGAVGLAQRALDEATKYALERKTFGKLIAEHQAVSFMLADMAMKVELARLAYQRAAWEVDSGRRNTYYASIAKAF 320

                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 187960098 365 AGDIANQLATDAVQILGGNGFNTEYPVEKLMRDAKIYQIYEGTSQIQRLIVAREHIDK 422
Cdd:cd01157  321 AADIANQLATDAVQIFGGNGFNSEYPVEKLMRDAKIYQIYEGTSQIQRLIISREHLGK 378
 
Name Accession Description Interval E-value
MCAD cd01157
Medium chain acyl-CoA dehydrogenase; MCADs are mitochondrial beta-oxidation enzymes, which ...
 45-422 0e+00

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: 797.95  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187960098  45 FTEQQKEFQATARKFAREEIIPVAAEYDKTGEYPVPLIRRAWELGLMNTHIPENCGGLGLGTFDACLISEELAYGCTGVQ 124
Cdd:cd01157    1 LTEQQKEFQETARKFAREEIIPVAAEYDKSGEYPWPLIKRAWELGLMNTHIPEDCGGLGLGTFDTCLITEELAYGCTGVQ 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187960098 125 TAIEGNSLGQMPIIIAGNDQQKKKYLGRMTEEPLMCAYCVTEPGAGSDVAGIKTKAEKKGDEYIINGQKMWITNGGKANW 204
Cdd:cd01157   81 TAIEANSLGQMPVIISGNDEQKKKYLGRMTEEPLMCAYCVTEPGAGSDVAGIKTKAEKKGDEYIINGQKMWITNGGKANW 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187960098 205 YFLLARSDPDPKAPANKAFTGFIVEADTPGIQIGRKELNMGQRCSDTRGIVFEDVKVPKENVLIGDGAGFKVAMGAFDKT 284
Cdd:cd01157  161 YFLLARSDPDPKCPASKAFTGFIVEADTPGIQPGRKELNMGQRCSDTRGITFEDVRVPKENVLIGEGAGFKIAMGAFDKT 240

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187960098 285 RPVVAAGAVGLAQRALDEATKYALERKTFGKLLVEHQAISFMLAEMAMKVELARMSYQRAAWEVDSGRRNTYYASIAKAF 364
Cdd:cd01157  241 RPPVAAGAVGLAQRALDEATKYALERKTFGKLIAEHQAVSFMLADMAMKVELARLAYQRAAWEVDSGRRNTYYASIAKAF 320

                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 187960098 365 AGDIANQLATDAVQILGGNGFNTEYPVEKLMRDAKIYQIYEGTSQIQRLIVAREHIDK 422
Cdd:cd01157  321 AADIANQLATDAVQIFGGNGFNSEYPVEKLMRDAKIYQIYEGTSQIQRLIISREHLGK 378
CaiA COG1960
Acyl-CoA dehydrogenase related to the alkylation response protein AidB [Lipid transport and ...
 43-418 6.35e-161

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: 458.15  E-value: 6.35e-161
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187960098  43 FEFTEQQKEFQATARKFAREEIIPVAAEYDKTGEYPVPLIRRAWELGLMNTHIPENCGGLGLGTFDACLISEELAYGCTG 122
Cdd:COG1960    3 FELTEEQRALRDEVREFAEEEIAPEAREWDREGEFPRELWRKLAELGLLGLTIPEEYGGLGLSLVELALVLEELARADAS 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187960098 123 VQTAIEGNSLGQMPIIIAGNDQQKKKYLGRMTEEPLMCAYCVTEPGAGSDVAGIKTKAEKKGDEYIINGQKMWITNGGKA 202
Cdd:COG1960   83 LALPVGVHNGAAEALLRFGTEEQKERYLPRLASGEWIGAFALTEPGAGSDAAALRTTAVRDGDGYVLNGQKTFITNAPVA 162

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187960098 203 NWYFLLARSDPDPKApanKAFTGFIVEADTPGIQIGRKELNMGQRCSDTRGIVFEDVKVPKENVLIGDGAGFKVAMGAFD 282
Cdd:COG1960  163 DVILVLARTDPAAGH---RGISLFLVPKDTPGVTVGRIEDKMGLRGSDTGELFFDDVRVPAENLLGEEGKGFKIAMSTLN 239

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187960098 283 KTRPVVAAGAVGLAQRALDEATKYALERKTFGKLLVEHQAISFMLAEMAMKVELARMSYQRAAWEVDSGRRNTYYASIAK 362
Cdd:COG1960  240 AGRLGLAAQALGIAEAALELAVAYAREREQFGRPIADFQAVQHRLADMAAELEAARALVYRAAWLLDAGEDAALEAAMAK 319

                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 187960098 363 AFAGDIANQLATDAVQILGGNGFNTEYPVEKLMRDAKIYQIYEGTSQIQRLIVARE 418
Cdd:COG1960  320 LFATEAALEVADEALQIHGGYGYTREYPLERLYRDARILTIYEGTNEIQRLIIARR 375
PLN02519 PLN02519
isovaleryl-CoA dehydrogenase
 27-418 9.78e-85

isovaleryl-CoA dehydrogenase


Pssm-ID: 215284 [Multi-domain]  Cd Length: 404  Bit Score: 264.82  E-value: 9.78e-85
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187960098  27 QHTKANRQREPGLGFSFEFTEQQKEFQATARKFAREEIIPVAAEYDKTGEYP--VPLIRRAWELGLMNTHIPENCGGLGL 104
Cdd:PLN02519   8 ARRRGLARRFSSSSSSLLFDDTQLQFKESVQQFAQENIAPHAAAIDATNSFPkdVNLWKLMGDFNLHGITAPEEYGGLGL 87

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187960098 105 GTFDACLISEEL--AYGCTGVQTAIEGNsLGQMPIIIAGNDQQKKKYLGRMTEEPLMCAYCVTEPGAGSDVAGIKTKAEK 182
Cdd:PLN02519  88 GYLYHCIAMEEIsrASGSVGLSYGAHSN-LCINQLVRNGTPAQKEKYLPKLISGEHVGALAMSEPNSGSDVVSMKCKAER 166

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187960098 183 KGDEYIINGQKMWITNGGKANWYFLLARSDPdpkAPANKAFTGFIVEADTPGIQIGRKELNMGQRCSDTRGIVFEDVKVP 262
Cdd:PLN02519 167 VDGGYVLNGNKMWCTNGPVAQTLVVYAKTDV---AAGSKGITAFIIEKGMPGFSTAQKLDKLGMRGSDTCELVFENCFVP 243

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187960098 263 KENVLIGDGAGFKVAMGAFDKTRPVVAAGAVGLAQRALDEATKYALERKTFGKLLVEHQAISFMLAEMAMKVELARMSYQ 342
Cdd:PLN02519 244 EENVLGQEGKGVYVMMSGLDLERLVLAAGPLGLMQACLDVVLPYVRQREQFGRPIGEFQFIQGKLADMYTSLQSSRSYVY 323

                        330       340       350       360       370       380       390
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 187960098 343 RAAWEVDSGRRNTYYASIAKAFAGDIANQLATDAVQILGGNGFNTEYPVEKLMRDAKIYQIYEGTSQIQRLIVARE 418
Cdd:PLN02519 324 SVARDCDNGKVDRKDCAGVILCAAERATQVALQAIQCLGGNGYINEYPTGRLLRDAKLYEIGAGTSEIRRMLIGRE 399
Acyl-CoA_dh_1 pfam00441
Acyl-CoA dehydrogenase, C-terminal domain; C-terminal domain of Acyl-CoA dehydrogenase is an ...
 271-417 2.62e-53

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: 174.75  E-value: 2.62e-53
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187960098  271 GAGFKVAMGAFDKTRPVVAAGAVGLAQRALDEATKYALERKTFGKLLVEHQAISFMLAEMAMKVELARMSYQRAAWEVDS 350
Cdd:pfam00441   1 GRGFRVAMETLNHERLAIAAMALGLARRALDEALAYARRRKAFGRPLIDFQLVRHKLAEMAAEIEAARLLVYRAAEALDA 80

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 187960098  351 GRRNTYYASIAKAFAGDIANQLATDAVQILGGNGFNTEYPVEKLMRDAKIYQIYEGTSQIQRLIVAR 417
Cdd:pfam00441  81 GGPDGAEASMAKLYASEAAVEVADLAMQLHGGYGYLREYPVERLYRDARVLRIGEGTSEIQRNIIAR 147
 
Name Accession Description Interval E-value
MCAD cd01157
Medium chain acyl-CoA dehydrogenase; MCADs are mitochondrial beta-oxidation enzymes, which ...
 45-422 0e+00

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: 797.95  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187960098  45 FTEQQKEFQATARKFAREEIIPVAAEYDKTGEYPVPLIRRAWELGLMNTHIPENCGGLGLGTFDACLISEELAYGCTGVQ 124
Cdd:cd01157    1 LTEQQKEFQETARKFAREEIIPVAAEYDKSGEYPWPLIKRAWELGLMNTHIPEDCGGLGLGTFDTCLITEELAYGCTGVQ 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187960098 125 TAIEGNSLGQMPIIIAGNDQQKKKYLGRMTEEPLMCAYCVTEPGAGSDVAGIKTKAEKKGDEYIINGQKMWITNGGKANW 204
Cdd:cd01157   81 TAIEANSLGQMPVIISGNDEQKKKYLGRMTEEPLMCAYCVTEPGAGSDVAGIKTKAEKKGDEYIINGQKMWITNGGKANW 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187960098 205 YFLLARSDPDPKAPANKAFTGFIVEADTPGIQIGRKELNMGQRCSDTRGIVFEDVKVPKENVLIGDGAGFKVAMGAFDKT 284
Cdd:cd01157  161 YFLLARSDPDPKCPASKAFTGFIVEADTPGIQPGRKELNMGQRCSDTRGITFEDVRVPKENVLIGEGAGFKIAMGAFDKT 240

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187960098 285 RPVVAAGAVGLAQRALDEATKYALERKTFGKLLVEHQAISFMLAEMAMKVELARMSYQRAAWEVDSGRRNTYYASIAKAF 364
Cdd:cd01157  241 RPPVAAGAVGLAQRALDEATKYALERKTFGKLIAEHQAVSFMLADMAMKVELARLAYQRAAWEVDSGRRNTYYASIAKAF 320

                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 187960098 365 AGDIANQLATDAVQILGGNGFNTEYPVEKLMRDAKIYQIYEGTSQIQRLIVAREHIDK 422
Cdd:cd01157  321 AADIANQLATDAVQIFGGNGFNSEYPVEKLMRDAKIYQIYEGTSQIQRLIISREHLGK 378
CaiA COG1960
Acyl-CoA dehydrogenase related to the alkylation response protein AidB [Lipid transport and ...
 43-418 6.35e-161

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: 458.15  E-value: 6.35e-161
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187960098  43 FEFTEQQKEFQATARKFAREEIIPVAAEYDKTGEYPVPLIRRAWELGLMNTHIPENCGGLGLGTFDACLISEELAYGCTG 122
Cdd:COG1960    3 FELTEEQRALRDEVREFAEEEIAPEAREWDREGEFPRELWRKLAELGLLGLTIPEEYGGLGLSLVELALVLEELARADAS 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187960098 123 VQTAIEGNSLGQMPIIIAGNDQQKKKYLGRMTEEPLMCAYCVTEPGAGSDVAGIKTKAEKKGDEYIINGQKMWITNGGKA 202
Cdd:COG1960   83 LALPVGVHNGAAEALLRFGTEEQKERYLPRLASGEWIGAFALTEPGAGSDAAALRTTAVRDGDGYVLNGQKTFITNAPVA 162

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187960098 203 NWYFLLARSDPDPKApanKAFTGFIVEADTPGIQIGRKELNMGQRCSDTRGIVFEDVKVPKENVLIGDGAGFKVAMGAFD 282
Cdd:COG1960  163 DVILVLARTDPAAGH---RGISLFLVPKDTPGVTVGRIEDKMGLRGSDTGELFFDDVRVPAENLLGEEGKGFKIAMSTLN 239

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187960098 283 KTRPVVAAGAVGLAQRALDEATKYALERKTFGKLLVEHQAISFMLAEMAMKVELARMSYQRAAWEVDSGRRNTYYASIAK 362
Cdd:COG1960  240 AGRLGLAAQALGIAEAALELAVAYAREREQFGRPIADFQAVQHRLADMAAELEAARALVYRAAWLLDAGEDAALEAAMAK 319

                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 187960098 363 AFAGDIANQLATDAVQILGGNGFNTEYPVEKLMRDAKIYQIYEGTSQIQRLIVARE 418
Cdd:COG1960  320 LFATEAALEVADEALQIHGGYGYTREYPLERLYRDARILTIYEGTNEIQRLIIARR 375
SCAD_SBCAD cd01158
Short chain acyl-CoA dehydrogenases and eukaryotic short/branched chain acyl-CoA ...
 47-422 6.11e-152

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: 435.16  E-value: 6.11e-152
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187960098  47 EQQKEFQATARKFAREEIIPVAAEYDKTGEYPVPLIRRAWELGLMNTHIPENCGGLGLGTFDACLISEELAYGCTGVQTA 126
Cdd:cd01158    1 EEHQMIRKTVRDFAEKEIAPLAAEMDEKGEFPREVIKEMAELGLMGIPIPEEYGGAGLDFLAYAIAIEELAKVDASVAVI 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187960098 127 IEG-NSLGQMPIIIAGNDQQKKKYLGRMTEEPLMCAYCVTEPGAGSDVAGIKTKAEKKGDEYIINGQKMWITNGGKANWY 205
Cdd:cd01158   81 VSVhNSLGANPIIKFGTEEQKKKYLPPLATGEKIGAFALSEPGAGSDAAALKTTAKKDGDDYVLNGSKMWITNGGEADFY 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187960098 206 FLLARSDPDPKapaNKAFTGFIVEADTPGIQIGRKELNMGQRCSDTRGIVFEDVKVPKENVLIGDGAGFKVAMGAFDKTR 285
Cdd:cd01158  161 IVFAVTDPSKG---YRGITAFIVERDTPGLSVGKKEDKLGIRGSSTTELIFEDVRVPKENILGEEGEGFKIAMQTLDGGR 237

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187960098 286 PVVAAGAVGLAQRALDEATKYALERKTFGKLLVEHQAISFMLAEMAMKVELARMSYQRAAWEVDSGRRNTYYASIAKAFA 365
Cdd:cd01158  238 IGIAAQALGIAQAALDAAVDYAKERKQFGKPIADFQGIQFKLADMATEIEAARLLTYKAARLKDNGEPFIKEAAMAKLFA 317

                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 187960098 366 GDIANQLATDAVQILGGNGFNTEYPVEKLMRDAKIYQIYEGTSQIQRLIVAReHIDK 422
Cdd:cd01158  318 SEVAMRVTTDAVQIFGGYGYTKDYPVERYYRDAKITEIYEGTSEIQRLVIAK-HLLK 373
ACAD cd00567
Acyl-CoA dehydrogenase; Both mitochondrial acyl-CoA dehydrogenases (ACAD) and peroxisomal ...
 47-417 9.99e-134

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: 387.02  E-value: 9.99e-134
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187960098  47 EQQKEFQATARKFAREEIIPVAAEYDKTGEYPVPLIRRAWELGlmnthipencgglglgtfdacliseelaygctgvqta 126
Cdd:cd00567    1 EEQRELRDSAREFAAEELEPYARERRETPEEPWELLAELGLLL------------------------------------- 43

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187960098 127 iegnslGQMPIIIAGNDQQKKKYLGRMTEEPLMCAYCVTEPGAGSDVAGIKTKAEKKGDEYIINGQKMWITNGGKANWYF 206
Cdd:cd00567   44 ------GAALLLAYGTEEQKERYLPPLASGEAIAAFALTEPGAGSDLAGIRTTARKDGDGYVLNGRKIFISNGGDADLFI 117

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187960098 207 LLARSDPDPkaPANKAFTGFIVEADTPGIQIGRKELNMGQRCSDTRGIVFEDVKVPKENVLIGDGAGFKVAMGAFDKTRP 286
Cdd:cd00567  118 VLARTDEEG--PGHRGISAFLVPADTPGVTVGRIWDKMGMRGSGTGELVFDDVRVPEDNLLGEEGGGFELAMKGLNVGRL 195

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187960098 287 VVAAGAVGLAQRALDEATKYALERKTFGKLLVEHQAISFMLAEMAMKVELARMSYQRAAWEVDSGRRN-TYYASIAKAFA 365
Cdd:cd00567  196 LLAAVALGAARAALDEAVEYAKQRKQFGKPLAEFQAVQFKLADMAAELEAARLLLYRAAWLLDQGPDEaRLEAAMAKLFA 275

                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|..
gi 187960098 366 GDIANQLATDAVQILGGNGFNTEYPVEKLMRDAKIYQIYEGTSQIQRLIVAR 417
Cdd:cd00567  276 TEAAREVADLAMQIHGGRGYSREYPVERYLRDARAARIAEGTAEIQRLIIAR 327
IBD cd01162
Isobutyryl-CoA dehydrogenase; Isobutyryl-CoA dehydrogenase (IBD) catalyzes the alpha, beta- ...
 46-418 5.88e-112

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: 333.64  E-value: 5.88e-112
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187960098  46 TEQQKEFQATARKFAREEIIPVAAEYDKTGEYPVPLIRRAWELGLMNTHIPENCGGLGLGTFDACLISEELAYGCTGVQT 125
Cdd:cd01162    2 NEEQRAIQEVARAFAAKEMAPHAADWDQKKHFPVDVLRKAAELGFGGIYIRDDVGGSGLSRLDASIIFEALSTGCVSTAA 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187960098 126 AIEGNSLGQMPIIIAGNDQQKKKYLGRMTEEPLMCAYCVTEPGAGSDVAGIKTKAEKKGDEYIINGQKMWITNGGKANWY 205
Cdd:cd01162   82 YISIHNMCAWMIDSFGNDEQRERFLPDLCTMEKLASYCLTEPGSGSDAAALRTRAVREGDHYVLNGSKAFISGAGDSDVY 161

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187960098 206 FLLARSDpdpkAPANKAFTGFIVEADTPGIQIGRKELNMGQRCSDTRGIVFEDVKVPKENVLIGDGAGFKVAMGAFDKTR 285
Cdd:cd01162  162 VVMARTG----GEGPKGISCFVVEKGTPGLSFGANEKKMGWNAQPTRAVIFEDCRVPVENRLGGEGQGFGIAMAGLNGGR 237

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187960098 286 PVVAAGAVGLAQRALDEATKYALERKTFGKLLVEHQAISFMLAEMAMKVELARMSYQRAAWEVDSGRRN-TYYASIAKAF 364
Cdd:cd01162  238 LNIASCSLGAAQAALDLARAYLEERKQFGKPLADFQALQFKLADMATELVASRLMVRRAASALDRGDPDaVKLCAMAKRF 317

                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|....
gi 187960098 365 AGDIANQLATDAVQILGGNGFNTEYPVEKLMRDAKIYQIYEGTSQIQRLIVARE 418
Cdd:cd01162  318 ATDECFDVANQALQLHGGYGYLKDYPVEQYVRDLRVHQILEGTNEIMRLIIARA 371
IVD cd01156
Isovaleryl-CoA dehydrogenase; Isovaleryl-CoA dehydrogenase (IVD) is an is an acyl-CoA ...
 45-418 4.68e-111

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: 331.30  E-value: 4.68e-111
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187960098  45 FTEQQKEFQATARKFAREEIIPVAAEYDKTGEYPVPLIRRAWELGLMNTHIPENCGGLGLGTFDACLISEELAYGCTGVQ 124
Cdd:cd01156    2 LDDEIEMLRQSVREFAQKEIAPLAAKIDRDNEFPRDLWRKMGKLGLLGITAPEEYGGSGMGYLAHVIIMEEISRASGSVA 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187960098 125 TAIEGNS---LGQmpIIIAGNDQQKKKYLGRMTEEPLMCAYCVTEPGAGSDVAGIKTKAEKKGDEYIINGQKMWITNGGK 201
Cdd:cd01156   82 LSYGAHSnlcINQ--IYRNGSAAQKEKYLPKLISGEHIGALAMSEPNAGSDVVSMKLRAEKKGDRYVLNGSKMWITNGPD 159

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187960098 202 ANWYFLLARSDPDPKApanKAFTGFIVEADTPGIQIGRKELNMGQRCSDTRGIVFEDVKVPKENVLIGDGAGFKVAMGAF 281
Cdd:cd01156  160 ADTLVVYAKTDPSAGA---HGITAFIVEKGMPGFSRAQKLDKLGMRGSNTCELVFEDCEVPEENILGGENKGVYVLMSGL 236

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187960098 282 DKTRPVVAAGAVGLAQRALDEATKYALERKTFGKLLVEHQAISFMLAEMAMKVELARMSYQRAAWEVDSGRRNTYYASIA 361
Cdd:cd01156  237 DYERLVLAGGPIGIMQAALDVAIPYAHQRKQFGQPIGEFQLVQGKLADMYTRLNASRSYLYTVAKACDRGNMDPKDAAGV 316

                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 187960098 362 KAFAGDIANQLATDAVQILGGNGFNTEYPVEKLMRDAKIYQIYEGTSQIQRLIVARE 418
Cdd:cd01156  317 ILYAAEKATQVALDAIQILGGNGYINDYPTGRLLRDAKLYEIGAGTSEIRRMVIGRE 373
LCAD cd01160
Long chain acyl-CoA dehydrogenase; LCAD is an acyl-CoA dehydrogenases (ACAD), which is found ...
 47-418 2.25e-102

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: 309.05  E-value: 2.25e-102
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187960098  47 EQQKEFQATARKFAREEIIPVAAEYDKTGEYPVPLIRRAWELGLMNTHIPENCGGLGLGTFDACLISEELAY-GCTGVQT 125
Cdd:cd01160    1 EEHDAFRDVVRRFFAKEVAPFHHEWEKAGEVPREVWRKAGEQGLLGVGFPEEYGGIGGDLLSAAVLWEELARaGGSGPGL 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187960098 126 AIEgNSLGQMPIIIAGNDQQKKKYLGRMTEEPLMCAYCVTEPGAGSDVAGIKTKAEKKGDEYIINGQKMWITNGGKANWY 205
Cdd:cd01160   81 SLH-TDIVSPYITRAGSPEQKERVLPQMVAGKKIGAIAMTEPGAGSDLQGIRTTARKDGDHYVLNGSKTFITNGMLADVV 159

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187960098 206 FLLARSDPDPKAPANKAFtgFIVEADTPGIQIGRKELNMGQRCSDTRGIVFEDVKVPKENVLIGDGAGFKVAMGAFDKTR 285
Cdd:cd01160  160 IVVARTGGEARGAGGISL--FLVERGTPGFSRGRKLKKMGWKAQDTAELFFDDCRVPAENLLGEENKGFYYLMQNLPQER 237

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187960098 286 PVVAAGAVGLAQRALDEATKYALERKTFGKLLVEHQAISFMLAEMAMKVELARMSYQRAAWEVDSGRRNTYYASIAKAFA 365
Cdd:cd01160  238 LLIAAGALAAAEFMLEETRNYVKQRKAFGKTLAQLQVVRHKIAELATKVAVTRAFLDNCAWRHEQGRLDVAEASMAKYWA 317

                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|...
gi 187960098 366 GDIANQLATDAVQILGGNGFNTEYPVEKLMRDAKIYQIYEGTSQIQRLIVARE 418
Cdd:cd01160  318 TELQNRVAYECVQLHGGWGYMREYPIARAYRDARVQPIYGGTTEIMKELISRQ 370
VLCAD cd01161
Very long chain acyl-CoA dehydrogenase; VLCAD is an acyl-CoA dehydrogenase (ACAD), which is ...
 44-416 3.38e-92

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: 283.98  E-value: 3.38e-92
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187960098  44 EFTEQQKEFQATARKFAREEIIPvaAEYDKTGEYPVPLIRRAWELGLMNTHIPENCGGLGLGTFDACLISEELAY-GCTG 122
Cdd:cd01161   26 EQTEELNMLVGPVEKFFEEVNDP--AKNDQLEKIPRKTLTQLKELGLFGLQVPEEYGGLGLNNTQYARLAEIVGMdLGFS 103

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187960098 123 VQTAIEgNSLGQMPIIIAGNDQQKKKYLGRMTEEPLMCAYCVTEPGAGSDVAGIKTKAEKK--GDEYIINGQKMWITNGG 200
Cdd:cd01161  104 VTLGAH-QSIGFKGILLFGTEAQKEKYLPKLASGEWIAAFALTEPSSGSDAASIRTTAVLSedGKHYVLNGSKIWITNGG 182

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187960098 201 KANWYFLLARSD-PDPKAPANKAFTGFIVEADTPGIQIGRKELNMGQRCSDTRGIVFEDVKVPKENVLIGDGAGFKVAMG 279
Cdd:cd01161  183 IADIFTVFAKTEvKDATGSVKDKITAFIVERSFGGVTNGPPEKKMGIKGSNTAEVYFEDVKIPVENVLGEVGDGFKVAMN 262

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187960098 280 AFDKTRPVVAAGAVGLAQRALDEATKYALERKTFGKLLVEHQAISFMLAEMAMKVELARMSYQRAAWEVDSGRRNTYY-- 357
Cdd:cd01161  263 ILNNGRFGMGAALIGTMKRCIEKAVDYANNRKQFGKKIHEFGLIQEKLANMAILQYATESMAYMTSGNMDRGLKAEYQie 342

                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 187960098 358 ASIAKAFAGDIANQLATDAVQILGGNGFNTEYPVEKLMRDAKIYQIYEGTSQIQRLIVA 416
Cdd:cd01161  343 AAISKVFASEAAWLVVDEAIQIHGGMGFMREYGVERVLRDLRIFRIFEGTNEILRLFIA 401
PLN02519 PLN02519
isovaleryl-CoA dehydrogenase
 27-418 9.78e-85

isovaleryl-CoA dehydrogenase


Pssm-ID: 215284 [Multi-domain]  Cd Length: 404  Bit Score: 264.82  E-value: 9.78e-85
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187960098  27 QHTKANRQREPGLGFSFEFTEQQKEFQATARKFAREEIIPVAAEYDKTGEYP--VPLIRRAWELGLMNTHIPENCGGLGL 104
Cdd:PLN02519   8 ARRRGLARRFSSSSSSLLFDDTQLQFKESVQQFAQENIAPHAAAIDATNSFPkdVNLWKLMGDFNLHGITAPEEYGGLGL 87

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187960098 105 GTFDACLISEEL--AYGCTGVQTAIEGNsLGQMPIIIAGNDQQKKKYLGRMTEEPLMCAYCVTEPGAGSDVAGIKTKAEK 182
Cdd:PLN02519  88 GYLYHCIAMEEIsrASGSVGLSYGAHSN-LCINQLVRNGTPAQKEKYLPKLISGEHVGALAMSEPNSGSDVVSMKCKAER 166

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187960098 183 KGDEYIINGQKMWITNGGKANWYFLLARSDPdpkAPANKAFTGFIVEADTPGIQIGRKELNMGQRCSDTRGIVFEDVKVP 262
Cdd:PLN02519 167 VDGGYVLNGNKMWCTNGPVAQTLVVYAKTDV---AAGSKGITAFIIEKGMPGFSTAQKLDKLGMRGSDTCELVFENCFVP 243

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187960098 263 KENVLIGDGAGFKVAMGAFDKTRPVVAAGAVGLAQRALDEATKYALERKTFGKLLVEHQAISFMLAEMAMKVELARMSYQ 342
Cdd:PLN02519 244 EENVLGQEGKGVYVMMSGLDLERLVLAAGPLGLMQACLDVVLPYVRQREQFGRPIGEFQFIQGKLADMYTSLQSSRSYVY 323

                        330       340       350       360       370       380       390
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 187960098 343 RAAWEVDSGRRNTYYASIAKAFAGDIANQLATDAVQILGGNGFNTEYPVEKLMRDAKIYQIYEGTSQIQRLIVARE 418
Cdd:PLN02519 324 SVARDCDNGKVDRKDCAGVILCAAERATQVALQAIQCLGGNGYINEYPTGRLLRDAKLYEIGAGTSEIRRMLIGRE 399
GCD cd01151
Glutaryl-CoA dehydrogenase; Glutaryl-CoA dehydrogenase (GCD). GCD is an acyl-CoA dehydrogenase, ...
 39-418 1.94e-72

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: 232.25  E-value: 1.94e-72
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187960098  39 LGFSFEFTEQQKEFQATARKFAREEIIPVAAEYDKTGEYPVPLIRRAWELGLMNThIPENCGGLGLGTFDACLISEELAY 118
Cdd:cd01151    7 LNLDDLLTEEERAIRDTAREFCQEELAPRVLEAYREEKFDRKIIEEMGELGLLGA-TIKGYGCAGLSSVAYGLIAREVER 85

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187960098 119 GCTGVQTAIE-GNSLGQMPIIIAGNDQQKKKYLGRMTEEPLMCAYCVTEPGAGSDVAGIKTKAEKKGDEYIINGQKMWIT 197
Cdd:cd01151   86 VDSGYRSFMSvQSSLVMLPIYDFGSEEQKQKYLPKLASGELIGCFGLTEPNHGSDPGGMETRARKDGGGYKLNGSKTWIT 165

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187960098 198 NGGKANWYFLLARSDPDPKapankaFTGFIVEADTPGIQIGRKELNMGQRCSDTRGIVFEDVKVPKENVLIGdGAGFKVA 277
Cdd:cd01151  166 NSPIADVFVVWARNDETGK------IRGFILERGMKGLSAPKIQGKFSLRASITGEIVMDNVFVPEENLLPG-AEGLRGP 238

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187960098 278 MGAFDKTRPVVAAGAVGLAQRALDEATKYALERKTFGKLLVEHQAISFMLAEMAMKVELArmsyQRAAWEV----DSGRR 353
Cdd:cd01151  239 FKCLNNARYGIAWGALGAAEDCYHTARQYVLDRKQFGRPLAAFQLVQKKLADMLTEIALG----LLACLRVgrlkDQGKA 314

                        330       340       350       360       370       380
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 187960098 354 NTYYASIAKAFAGDIANQLATDAVQILGGNGFNTEYPVEKLMRDAKIYQIYEGTSQIQRLIVARE 418
Cdd:cd01151  315 TPEQISLLKRNNCGKALEIARTAREMLGGNGISDEYHIIRHMVNLESVNTYEGTHDIHALILGRA 379
ACAD_fadE5 cd01153
Putative acyl-CoA dehydrogenases similar to fadE5; Putative acyl-CoA dehydrogenase (ACAD). ...
 54-411 2.10e-61

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: 204.16  E-value: 2.10e-61
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187960098  54 ATARKFAREEIIPVAAEYDKTG--------EYPVP---LIRRAWELGLMNTHIPENCGGLGLGTFDACLISEELAYGCTG 122
Cdd:cd01153    3 EEVARLAENVLAPLNADGDREGpvfddgrvVVPPPfkeALDAFAEAGWMALGVPEEYGGQGLPITVYSALAEIFSRGDAP 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187960098 123 VqtAIEGNSLGQMPIIIA-GNDQQKKKYLGRMTEEPLMCAYCVTEPGAGSDVAGIKTKAEKKGD-EYIINGQKMWITNGG 200
Cdd:cd01153   83 L--MYASGTQGAAATLLAhGTEAQREKWIPRLAEGEWTGTMCLTEPDAGSDLGALRTKAVYQADgSWRINGVKRFISAGE 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187960098 201 KANW----YFLLARSDPDPkaPANKAFTGFIV-----EADTPGIQIGRKELNMGQRCSDTRGIVFEDVKVPkenvLIGD- 270
Cdd:cd01153  161 HDMSenivHLVLARSEGAP--PGVKGLSLFLVpkfldDGERNGVTVARIEEKMGLHGSPTCELVFDNAKGE----LIGEe 234

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187960098 271 GAGFKVAMGAFDKTRPVVAAGAVGLAQRALDEATKYALERKTFGKLLVE--------HQAISFMLAEMAMKVELARMSYQ 342
Cdd:cd01153  235 GMGLAQMFAMMNGARLGVGTQGTGLAEAAYLNALAYAKERKQGGDLIKAapavtiihHPDVRRSLMTQKAYAEGSRALDL 314

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187960098 343 RAAWEVDSGRR--------------NTYYASIAKAFAGDIANQLATDAVQILGGNGFNTEYPVEKLMRDAKIYQIYEGTS 408
Cdd:cd01153  315 YTATVQDLAERkategedrkalsalADLLTPVVKGFGSEAALEAVSDAIQVHGGSGYTREYPIEQYYRDARITTIYEGTT 394


                 ...
gi 187960098 409 QIQ 411
Cdd:cd01153  395 GIQ 397
ACAD_fadE6_17_26 cd01152
Putative acyl-CoA dehydrogenases similar to fadE6, fadE17, and fadE26; Putative acyl-CoA ...
 47-417 2.10e-61

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: 203.35  E-value: 2.10e-61
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187960098  47 EQQKEFQATARKFAREEIIP-----VAAEYDKTGEYPVPLIRRAWELGLMNTHIPENCGGLGLGTFDACLISEELAYGCT 121
Cdd:cd01152    1 PSEEAFRAEVRAWLAAHLPPelreeSALGYREGREDRRRWQRALAAAGWAAPGWPKEYGGRGASLMEQLIFREEMAAAGA 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187960098 122 GVQtaieGNSLGQM---PIIIA-GNDQQKKKYLGRMTEEPLMCAYCVTEPGAGSDVAGIKTKAEKKGDEYIINGQKMWIT 197
Cdd:cd01152   81 PVP----FNQIGIDlagPTILAyGTDEQKRRFLPPILSGEEIWCQGFSEPGAGSDLAGLRTRAVRDGDDWVVNGQKIWTS 156

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187960098 198 NGGKANWYFLLARSDPDpkAPANKAFTGFIVEADTPGIQIgR--KELNMGqrcSDTRGIVFEDVKVPKENVLIGDGAGFK 275
Cdd:cd01152  157 GAHYADWAWLLVRTDPE--APKHRGISILLVDMDSPGVTV-RpiRSINGG---EFFNEVFLDDVRVPDANRVGEVNDGWK 230

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187960098 276 VAMGAFDKTRPVVAAGAVGLAQRALDeatkYALERKTFGKLLVEHQAISFMLAEMAMKVELARMSYQRAAWEVDSGRRNT 355
Cdd:cd01152  231 VAMTTLNFERVSIGGSAATFFELLLA----RLLLLTRDGRPLIDDPLVRQRLARLEAEAEALRLLVFRLASALAAGKPPG 306

                        330       340       350       360       370       380       390
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187960098 356 YYASIAKAFAGDIANQLATDAVQILG--------GNGFNTEYPVEKLMRDAKIYQIYEGTSQIQRLIVAR 417
Cdd:cd01152  307 AEASIAKLFGSELAQELAELALELLGtaallrdpAPGAELAGRWEADYLRSRATTIYGGTSEIQRNIIAE 376
PTZ00461 PTZ00461
isovaleryl-CoA dehydrogenase; Provisional
 46-407 4.29e-61

isovaleryl-CoA dehydrogenase; Provisional


Pssm-ID: 185640 [Multi-domain]  Cd Length: 410  Bit Score: 203.63  E-value: 4.29e-61
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187960098  46 TEQQKEFQATARKFAREEIIPVAAEYDKTGEYPVPLIRRAWELGLMNTHIPENCGGLGLGTFDACLISEELAYGCTGVQT 125
Cdd:PTZ00461  38 TPEHAALRETVAKFSREVVDKHAREDDINMHFNRDLFKQLGDLGVMGVTVPEADGGAGMDAVAAVIIHHELSKYDPGFCL 117

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187960098 126 AIEGNS-LGQMPIIIAGNDQQKKKYLGRMTEEPLMCAYCVTEPGAGSDVAGIKTKAEKKGDE-YIINGQKMWITNGGKAN 203
Cdd:PTZ00461 118 AYLAHSmLFVNNFYYSASPAQRARWLPKVLTGEHVGAMGMSEPGAGTDVLGMRTTAKKDSNGnYVLNGSKIWITNGTVAD 197

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187960098 204 WYFLLARSDpdpkapanKAFTGFIVEADTPGIQIGRKELNMGQRCSDTRGIVFEDVKVPKENVLIGDGAGFKVAMGAFDK 283
Cdd:PTZ00461 198 VFLIYAKVD--------GKITAFVVERGTKGFTQGPKIDKCGMRASHMCQLFFEDVVVPAENLLGEEGKGMVGMMRNLEL 269

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187960098 284 TRPVVAAGAVGLAQRALDEATKYALERKTFGKLLVEHQAISFMLAEMAMKVELARMSYQRAAWEVDSGRRNTYYASIAKA 363
Cdd:PTZ00461 270 ERVTLAAMAVGIAERSVELMTSYASERKAFGKPISNFGQIQRYIAEGYADTEAAKALVYSVSHNVHPGNKNRLGSDAAKL 349

                        330       340       350       360
                 ....*....|....*....|....*....|....*....|....
gi 187960098 364 FAGDIANQLATDAVQILGGNGFNTEYPVEKLMRDAKIYQIYEGT 407
Cdd:PTZ00461 350 FATPIAKKVADSAIQVMGGMGYSRDMPVERLWRDAKLLEIGGGT 393
PRK12341 PRK12341
acyl-CoA dehydrogenase;
43-424 3.72e-60

acyl-CoA dehydrogenase;


Pssm-ID: 183454 [Multi-domain]  Cd Length: 381  Bit Score: 200.34  E-value: 3.72e-60
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187960098  43 FEFTEQQKEFQATARKF-AREEIIPVAAEYDKTGEYPVPLIRRAWELGLMNTHIPENCGGLGLGTFDACLISEELAYgcT 121
Cdd:PRK12341   3 FSLTEEQELLLASIRELiTRNFPEEYFRTCDENGTYPREFMRALADNGISMLGVPEEFGGTPADYVTQMLVLEEVSK--C 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187960098 122 GVQTAIEGNSLGQMPIIIAGNDQQKKKYLgRMTEEPLMCAYC--VTEPGAGSDVAGIKTKAEKKGDEYIINGQKMWITNG 199
Cdd:PRK12341  81 GAPAFLITNGQCIHSMRRFGSAEQLRKTA-ESTLETGDPAYAlaLTEPGAGSDNNSATTTYTRKNGKVYLNGQKTFITGA 159

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187960098 200 GKANWYFLLARsDPDPKAPaNKAFTGFIVEADTPGIQIGRKElNMGQRCSDTRGIVFEDVKVPKENVLIGDGAGFKVAMG 279
Cdd:PRK12341 160 KEYPYMLVLAR-DPQPKDP-KKAFTLWWVDSSKPGIKINPLH-KIGWHMLSTCEVYLDNVEVEESDLVGEEGMGFLNVMY 236

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187960098 280 AFDKTRPVVAAGAVGLAQRALDEATKYALERKTFGKLLVEHQAISFMLAEMAMKVELARMSYQRAAWEVDSGRRNTYYAS 359
Cdd:PRK12341 237 NFEMERLINAARSLGFAECAFEDAARYANQRIQFGKPIGHNQLIQEKLTLMAIKIENMRNMVYKVAWQADNGQSLRTSAA 316

                        330       340       350       360       370       380
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 187960098 360 IAKAFAGDIANQLATDAVQILGGNGFNTEYPVEKLMRDAKIYQIYEGTSQIQRLIVAREHIDKYK 424
Cdd:PRK12341 317 LAKLYCARTAMEVIDDAIQIMGGLGYTDEARVSRFWRDVRCERIGGGTDEIMIYIAGRQILKDYQ 381
Acyl-CoA_dh_1 pfam00441
Acyl-CoA dehydrogenase, C-terminal domain; C-terminal domain of Acyl-CoA dehydrogenase is an ...
 271-417 2.62e-53

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: 174.75  E-value: 2.62e-53
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187960098  271 GAGFKVAMGAFDKTRPVVAAGAVGLAQRALDEATKYALERKTFGKLLVEHQAISFMLAEMAMKVELARMSYQRAAWEVDS 350
Cdd:pfam00441   1 GRGFRVAMETLNHERLAIAAMALGLARRALDEALAYARRRKAFGRPLIDFQLVRHKLAEMAAEIEAARLLVYRAAEALDA 80

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 187960098  351 GRRNTYYASIAKAFAGDIANQLATDAVQILGGNGFNTEYPVEKLMRDAKIYQIYEGTSQIQRLIVAR 417
Cdd:pfam00441  81 GGPDGAEASMAKLYASEAAVEVADLAMQLHGGYGYLREYPVERLYRDARVLRIGEGTSEIQRNIIAR 147
ACAD_FadE2 cd01155
Acyl-CoA dehydrogenases similar to fadE2; FadE2-like Acyl-CoA dehydrogenase (ACAD). Acyl-CoA ...
 47-417 7.18e-53

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: 181.43  E-value: 7.18e-53
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187960098  47 EQQKEFQATARKFAREEIIPVAAEYDktgEYPVPLIRRAW--------------ELGLMNTHIPENCGGLGLGTFDACLI 112
Cdd:cd01155    1 RKAQELRARVKAFMEEHVYPAEQEFL---EYYAEGGDRWWtpppiieklkakakAEGLWNLFLPEVSGLSGLTNLEYAYL 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187960098 113 SEEL--------AYGCTGVQTaiegnslGQMPIIIA-GNDQQKKKYLgrmteEPLM-----CAYCVTEPG-AGSDVAGIK 177
Cdd:cd01155   78 AEETgrsffapeVFNCQAPDT-------GNMEVLHRyGSEEQKKQWL-----EPLLdgkirSAFAMTEPDvASSDATNIE 145

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187960098 178 TKAEKKGDEYIINGQKMWITNGG--KANWYFLLARSDPDpKAPANKAFTGFIVEADTPGIQIGRKELNMGQrcSDTRG-- 253
Cdd:cd01155  146 CSIERDGDDYVINGRKWWSSGAGdpRCKIAIVMGRTDPD-GAPRHRQQSMILVPMDTPGVTIIRPLSVFGY--DDAPHgh 222

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187960098 254 --IVFEDVKVPKENVLIGDGAGFKVAMGAFDKTRPVVAAGAVGLAQRALDEATKYALERKTFGKLLVEHQAISFMLAEMA 331
Cdd:cd01155  223 aeITFDNVRVPASNLILGEGRGFEIAQGRLGPGRIHHCMRLIGAAERALELMCQRAVSREAFGKKLAQHGVVAHWIAKSR 302

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187960098 332 MKVELARMSYQRAAWEVDSGRRNTYYASIA--KAFAGDIANQLATDAVQILGGNGFNTEYPVEKLMRDAKIYQIYEGTSQ 409
Cdd:cd01155  303 IEIEQARLLVLKAAHMIDTVGNKAARKEIAmiKVAAPRMALKIIDRAIQVHGAAGVSQDTPLANMYAWARTLRIADGPDE 382


                 ....*...
gi 187960098 410 IQRLIVAR 417
Cdd:cd01155  383 VHLRSIAR 390
PRK03354 PRK03354
crotonobetainyl-CoA dehydrogenase; Validated
 43-424 6.03e-49

crotonobetainyl-CoA dehydrogenase; Validated


Pssm-ID: 179566 [Multi-domain]  Cd Length: 380  Bit Score: 170.78  E-value: 6.03e-49
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187960098  43 FEFTEQQKEFQATARKF-AREEIIPVAAEYDKTGEYPVPLIRRAWELGLMNTHIPENCGGLGLGTFDACLISEELayGCT 121
Cdd:PRK03354   3 FNLNDEQELFVAGIRELmASENWEAYFAECDRDSVYPERFVKALADMGIDSLLIPEEHGGLDAGFVTLAAVWMEL--GRL 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187960098 122 GVQTAIegnsLGQMP-----IIIAGNDQQKKKYLGRMTEEPLMCAYCVTEPGAGSDVAGIKTKAEKKGDEYIINGQKMWI 196
Cdd:PRK03354  81 GAPTYV----LYQLPggfntFLREGTQEQIDKIMAFRGTGKQMWNSAITEPGAGSDVGSLKTTYTRRNGKVYLNGSKCFI 156

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187960098 197 TNGGKANWYFLLARSDPDPKAPAnkaFTGFIVEADTPGIQIGRKElNMGQRCSDTRGIVFEDVKVPKENVLIGDGAGFKV 276
Cdd:PRK03354 157 TSSAYTPYIVVMARDGASPDKPV---YTEWFVDMSKPGIKVTKLE-KLGLRMDSCCEITFDDVELDEKDMFGREGNGFNR 232

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187960098 277 AMGAFDKTRPVVAAGAVGLAQRALDEATKYALERKTFGKLLVEHQAISFMLAEMAMKVELARMSYQRAAWEVDSGRRNTY 356
Cdd:PRK03354 233 VKEEFDHERFLVALTNYGTAMCAFEDAARYANQRVQFGEAIGRFQLIQEKFAHMAIKLNSMKNMLYEAAWKADNGTITSG 312

                        330       340       350       360       370       380
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 187960098 357 YASIAKAFAGDIANQLATDAVQILGGNGFNTEYPVEKLMRDAKIYQIYEGTSQIQRLIVAREHIDKYK 424
Cdd:PRK03354 313 DAAMCKYFCANAAFEVVDSAMQVLGGVGIAGNHRISRFWRDLRVDRVSGGSDEMQILTLGRAVLKQYR 380
PLN02526 PLN02526
acyl-coenzyme A oxidase
 46-418 4.53e-45

acyl-coenzyme A oxidase


Pssm-ID: 178141 [Multi-domain]  Cd Length: 412  Bit Score: 161.17  E-value: 4.53e-45
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187960098  46 TEQQKEFQATARKFAREEIIPVAAEYDKTGEYPVPLIRRAWELGLMNTHIP-ENCGGLGLgTFDACLISEELAYGCTGVQ 124
Cdd:PLN02526  30 TPEEQALRKRVRECMEKEVAPIMTEYWEKAEFPFHIIPKLGSLGIAGGTIKgYGCPGLSI-TASAIATAEVARVDASCST 108

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187960098 125 TAIEGNSLGQMPIIIAGNDQQKKKYLGRMTEEPLMCAYCVTEPGAGSDVAGIKTKAEKKGDEYIINGQKMWITNGGKANW 204
Cdd:PLN02526 109 FILVHSSLAMLTIALCGSEAQKQKYLPSLAQLDTVACWALTEPDYGSDASSLNTTATKVEGGWILNGQKRWIGNSTFADV 188

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187960098 205 YFLLARSdpdpkaPANKAFTGFIVEADTPGIQIGRKELNMGQRCSDTRGIVFEDVKVPKENVLIGDGAgFKVAMGAFDKT 284
Cdd:PLN02526 189 LVIFARN------TTTNQINGFIVKKGAPGLKATKIENKIGLRMVQNGDIVLKDVFVPDEDRLPGVNS-FQDTNKVLAVS 261

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187960098 285 RPVVAAGAVGLAQRALDEATKYALERKTFGKLLVEHQAISFMLAEMAMKVELARMSYQRAAWEVDSGRRNTYYASIAKAF 364
Cdd:PLN02526 262 RVMVAWQPIGISMGVYDMCHRYLKERKQFGAPLAAFQINQEKLVRMLGNIQAMFLVGWRLCKLYESGKMTPGHASLGKAW 341

                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|....
gi 187960098 365 AGDIANQLATDAVQILGGNGFNTEYPVEKLMRDAKIYQIYEGTSQIQRLIVARE 418
Cdd:PLN02526 342 ITKKARETVALGRELLGGNGILADFLVAKAFCDLEPIYTYEGTYDINALVTGRE 395
Acyl-CoA_dh_N pfam02771
Acyl-CoA dehydrogenase, N-terminal domain; The N-terminal domain of Acyl-CoA dehydrogenase is ...
 46-153 5.69e-39

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: 136.05  E-value: 5.69e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187960098   46 TEQQKEFQATARKFAREEIIPVAAEYDKTGEYPVPLIRRAWELGLMNTHIPENCGGLGLGTFDACLISEELAYGCTGVQT 125
Cdd:pfam02771   1 TEEQEALRDTVREFAEEEIAPHAAEWDEEGEFPRELWKKLGELGLLGITIPEEYGGAGLDYLAYALVAEELARADASVAL 80

                          90       100
                  ....*....|....*....|....*....
gi 187960098  126 AIE-GNSLGQMPIIIAGNDQQKKKYLGRM 153
Cdd:pfam02771  81 ALSvHSSLGAPPILRFGTEEQKERYLPKL 109
AidB cd01154
Proteins involved in DNA damage response, similar to the AidB gene product; AidB is one of ...
 149-417 6.76e-35

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: 133.65  E-value: 6.76e-35
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187960098 149 YLGRMTEEPLMCAYCVTEPGAGSDVAGIKTKAEK-KGDEYIINGQKmWITNGGKANWYFLLARsdPDPKAPANKAFTGFI 227
Cdd:cd01154  138 LLSDRYKTGLLGGTWMTEKQGGSDLGANETTAERsGGGVYRLNGHK-WFASAPLADAALVLAR--PEGAPAGARGLSLFL 214

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187960098 228 VEADTP-----GIQIGRKELNMGQRCSDTRGIVFEDVkvpkENVLIGD-GAGFKVAMGAFDKTRPVVAAGAVGLAQRALD 301
Cdd:cd01154  215 VPRLLEdgtrnGYRIRRLKDKLGTRSVATGEVEFDDA----EAYLIGDeGKGIYYILEMLNISRLDNAVAALGIMRRALS 290

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187960098 302 EATKYALERKTFGKLLVEHQAISFMLAEMAMKVELARMSYQRAA--WEVDSGRRNTYYA------SIAKAFAGDIANQLA 373
Cdd:cd01154  291 EAYHYARHRRAFGKPLIDHPLMRRDLAEMEVDVEAATALTFRAAraFDRAAADKPVEAHmarlatPVAKLIACKRAAPVT 370

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....
gi 187960098 374 TDAVQILGGNGFNTEYPVEKLMRDAKIYQIYEGTSQIQRLIVAR 417
Cdd:cd01154  371 SEAMEVFGGNGYLEEWPVARLHREAQVTPIWEGTGNIQALDVLR 414
PLN02876 PLN02876
acyl-CoA dehydrogenase
 133-410 3.42e-32

acyl-CoA dehydrogenase


Pssm-ID: 215473 [Multi-domain]  Cd Length: 822  Bit Score: 129.53  E-value: 3.42e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187960098 133 GQMPIIIA-GNDQQKKKYLGRMTEEPLMCAYCVTEPG-AGSDVAGIKTKAEKKGDEYIINGQKMWITNGGKANWYFLLAR 210
Cdd:PLN02876 524 GNMEVLLRyGNKEQQLEWLIPLLEGKIRSGFAMTEPQvASSDATNIECSIRRQGDSYVINGTKWWTSGAMDPRCRVLIVM 603

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187960098 211 SDPDPKAPANKAFTGFIVEADTPGIQIGRKELNMGqrCSDT----RGIVFEDVKVPKENVLIGDGAGFKVAMGAFDKTRP 286
Cdd:PLN02876 604 GKTDFNAPKHKQQSMILVDIQTPGVQIKRPLLVFG--FDDAphghAEISFENVRVPAKNILLGEGRGFEIAQGRLGPGRL 681

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187960098 287 VVAAGAVGLAQRALDEATKYALERKTFGKLLVEHQAISFMLAEMAMKVELARMSYQRAAWEVD--SGRRNTYYASIAKAF 364
Cdd:PLN02876 682 HHCMRLIGAAERGMQLMVQRALSRKAFGKLIAQHGSFLSDLAKCRVELEQTRLLVLEAADQLDrlGNKKARGIIAMAKVA 761

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*.
gi 187960098 365 AGDIANQLATDAVQILGGNGFNTEYPVEKLMRDAKIYQIYEGTSQI 410
Cdd:PLN02876 762 APNMALKVLDMAMQVHGAAGVSSDTVLAHLWATARTLRIADGPDEV 807
Acyl-CoA_dh_M pfam02770
Acyl-CoA dehydrogenase, middle domain; Central domain of Acyl-CoA dehydrogenase has a ...
 161-257 7.71e-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: 111.22  E-value: 7.71e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187960098  161 AYCVTEPGAGSDVAGIKTKA-EKKGDEYIINGQKMWITNGGKANWYFLLARSDPDPKApanKAFTGFIVEADTPGIQIGR 239
Cdd:pfam02770   1 AFALTEPGAGSDVASLKTTAaDGDGGGWVLNGTKWWITNAGIADLFLVLARTGGDDRH---GGISLFLVPKDAPGVSVRR 77

                          90
                  ....*....|....*...
gi 187960098  240 KELNMGQRCSDTRGIVFE 257
Cdd:pfam02770  78 IETKLGVRGLPTGELVFD 95
PTZ00456 PTZ00456
acyl-CoA dehydrogenase; Provisional
 45-413 6.03e-22

acyl-CoA dehydrogenase; Provisional


Pssm-ID: 185635 [Multi-domain]  Cd Length: 622  Bit Score: 98.40  E-value: 6.03e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187960098  45 FTEQQKEFQ----ATARKFAREEIIPVAAEYD-------KTGEYPVPL-IRRAWEL----GLMNTHIPENCGGLGLgTFD 108
Cdd:PTZ00456  52 KTDVTKELMdsllEEASKLATQTLLPLYESSDsegcvllKDGNVTTPKgFKEAYQAlkagGWTGISEPEEYGGQAL-PLS 130

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187960098 109 ACLISEELAYGCTGVQTAIEGNSLGQMPIIIA-GNDQQKKKYLGRMTEEPLMCAYCVTEPGAGSDVAGIKTKAEKKGD-E 186
Cdd:PTZ00456 131 VGFITRELMATANWGFSMYPGLSIGAANTLMAwGSEEQKEQYLTKLVSGEWSGTMCLTEPQCGTDLGQVKTKAEPSADgS 210

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187960098 187 YIINGQKMWITNGG---KAN-WYFLLARSDPDPkaPANKAFTGFIVEADTP----------GIQIGRKELNMGQRCSDTR 252
Cdd:PTZ00456 211 YKITGTKIFISAGDhdlTENiVHIVLARLPNSL--PTTKGLSLFLVPRHVVkpdgsletakNVKCIGLEKKMGIKGSSTC 288

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187960098 253 GIVFEDVKvpkeNVLIGD-GAGFKVAMGAFDKTRPVVAAGAVGLAQRALDEATKYALERKTF------------GKLLVE 319
Cdd:PTZ00456 289 QLSFENSV----GYLIGEpNAGMKQMFTFMNTARVGTALEGVCHAELAFQNALRYARERRSMralsgtkepekpADRIIC 364

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187960098 320 HQAISFML------AE--MAMKVELAR-MSYQRAAWEVDS----GRRNTYYASIAKAFAGDIANQLATDAVQILGGNGFN 386
Cdd:PTZ00456 365 HANVRQNIlfakavAEggRALLLDVGRlLDIHAAAKDAATrealDHEIGFYTPIAKGCLTEWGVEAASRCLQVWGGHGYI 444

                        410       420
                 ....*....|....*....|....*..
gi 187960098 387 TEYPVEKLMRDAKIYQIYEGTSQIQRL 413
Cdd:PTZ00456 445 KGNGMEQILRDARIGTLYEGTTGIQAL 471
Acyl-CoA_dh_2 pfam08028
Acyl-CoA dehydrogenase, C-terminal domain;
287-409 5.96e-19

Acyl-CoA dehydrogenase, C-terminal domain;


Pssm-ID: 429790 [Multi-domain]  Cd Length: 133  Bit Score: 82.39  E-value: 5.96e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187960098  287 VVAAGAVGLAQRALDEATKYALERKT--FGKLLVEHQAISFMLAEMAMKVELARMSYQRAAWE----VDSGRRNTYY--- 357
Cdd:pfam08028   1 GIAAAALGAARAALAEFTERARGRVRayFGVPLAEDPATQLALAEAAARIDAARLLLERAAARieaaAAAGKPVTPAlra 80

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|...
gi 187960098  358 -ASIAKAFAGDIANQLATDAVQILGGNGFNTEYPVEKLMRDAKIYQIYEGTSQ 409
Cdd:pfam08028  81 eARRAAAFATELAVAAVDALFRAAGGSALFQDSPLQRIWRDIHAAAQHAAVNP 133
AXO cd01150
Peroxisomal acyl-CoA oxidase; Peroxisomal acyl-CoA oxidases (AXO) catalyze the first set in ...
 135-424 3.41e-14

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: 74.29  E-value: 3.41e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187960098 135 MPIIIA-GNDQQKKKYL-GRMTEEPLMCaYCVTEPGAGSDVAGIKTKA--EKKGDEYIIN-----GQKMWITNGGK-ANW 204
Cdd:cd01150  110 GNAIKNlGTDEHQDYWLqGANNLEIIGC-FAQTELGHGSNLQGLETTAtyDPLTQEFVINtpdftATKWWPGNLGKtATH 188

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187960098 205 YFLLARSDPDPKapaNKAFTGFIV---EADT----PGIQIGRKELNMGQRCSDTRGIVFEDVKVPKENVL------IGDG 271
Cdd:cd01150  189 AVVFAQLITPGK---NHGLHAFIVpirDPKThqplPGVTVGDIGPKMGLNGVDNGFLQFRNVRIPRENLLnrfgdvSPDG 265

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187960098 272 A----------GFKVAMGAFDKTRPVVAAGAVGLAQRALDEATKYALERKTFG--------KLLvEHQ------------ 321
Cdd:cd01150  266 TyvspfkdpnkRYGAMLGTRSGGRVGLIYDAAMSLKKAATIAIRYSAVRRQFGpkpsdpevQIL-DYQlqqyrlfpqlaa 344

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187960098 322 --AISFMLAEMAMK-VELARMSYQRAAwevDSGRRNTYYASIAKAFAGDIANQLATDAVQILGGNGFNTEYPVEKLMRDA 398
Cdd:cd01150  345 ayAFHFAAKSLVEMyHEIIKELLQGNS---ELLAELHALSAGLKAVATWTAAQGIQECREACGGHGYLAMNRLPTLRDDN 421

                        330       340
                 ....*....|....*....|....*.
gi 187960098 399 KIYQIYEGTSQIQRLIVAREHIDKYK 424
Cdd:cd01150  422 DPFCTYEGDNTVLLQQTANYLLKKYA 447
DszC cd01163
Dibenzothiophene (DBT) desulfurization enzyme C; DszC is a flavin reductase dependent enzyme, ...
 52-399 1.48e-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: 71.59  E-value: 1.48e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187960098  52 FQATARKFAREeiipvAAEYDKTGEYPVPLIRRAWELGLMNTHIPENCGGLGLGTFDACLISEELAygctgvqtAIEGNs 131
Cdd:cd01163    3 ARPLAARIAEG-----AAERDRQRGLPYEEVALLRQSGLGTLRVPKEYGGLGASLPDLYEVVRELA--------AADSN- 68

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187960098 132 LGQMP---------IIIAGNDQQKKKYLGRMTEEPLM-CAycVTEPGaGSDVAGIKTKAEKKGDEYIINGQKmWITNGGK 201
Cdd:cd01163   69 IAQALrahfgfveaLLLAGPEQFRKRWFGRVLNGWIFgNA--VSERG-SVRPGTFLTATVRDGGGYVLNGKK-FYSTGAL 144

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187960098 202 ANWYFLLARSDPDPKApankafTGFIVEADTPGIQIGRKELNMGQRCSDTRGIVFEDVKVPKENVLIGDGAGFKVAM-GA 280
Cdd:cd01163  145 FSDWVTVSALDEEGKL------VFAAVPTDRPGITVVDDWDGFGQRLTASGTVTFDNVRVEPDEVLPRPNAPDRGTLlTA 218

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187960098 281 FDKTrpVVAAGAVGLAQRALDEATKYALER-KTFGKLLVEH--------QAIsfmlAEMAMKVELARMSYQRAAWEVD-- 349
Cdd:cd01163  219 IYQL--VLAAVLAGIARAALDDAVAYVRSRtRPWIHSGAESarddpyvqQVV----GDLAARLHAAEALVLQAARALDaa 292

                        330       340       350       360       370       380
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 187960098 350 --SGRRNTYYASI--------AKAFAGDIANQLATDAVQILGGNGFNTEYPVEKLMRDAK 399
Cdd:cd01163  293 aaAGTALTAEARGeaalavaaAKVVVTRLALDATSRLFEVGGASATAREHNLDRHWRNAR 352
PRK11561 PRK11561
isovaleryl CoA dehydrogenase; Provisional
 165-417 4.49e-13

isovaleryl CoA dehydrogenase; Provisional


Pssm-ID: 183199 [Multi-domain]  Cd Length: 538  Bit Score: 70.94  E-value: 4.49e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187960098 165 TEPGAGSDVAGIKTKAEKKGDE-YIINGQKmwitnggkanWYFLLARSDPD-PKAPANKAFTGFIVEADTP-----GIQI 237
Cdd:PRK11561 185 TEKQGGSDVLSNTTRAERLADGsYRLVGHK----------WFFSVPQSDAHlVLAQAKGGLSCFFVPRFLPdgqrnAIRL 254

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187960098 238 GRKELNMGQRCSDTRGIVFEDVK---VPKEnvliGDGAGFKVAMGAFdkTRPVVAAGAVGLAQRALDEATKYALERKTFG 314
Cdd:PRK11561 255 ERLKDKLGNRSNASSEVEFQDAIgwlLGEE----GEGIRLILKMGGM--TRFDCALGSHGLMRRAFSVAIYHAHQRQVFG 328

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187960098 315 KLLVEHQAISFMLAEMAMKVE--------LARMSYQRA-AWEVDSGRRNTYYA--SIAKAFAGDIAnqlatDAVQILGGN 383
Cdd:PRK11561 329 KPLIEQPLMRQVLSRMALQLEgqtallfrLARAWDRRAdAKEALWARLFTPAAkfVICKRGIPFVA-----EAMEVLGGI 403

                        250       260       270
                 ....*....|....*....|....*....|....
gi 187960098 384 GFNTEYPVEKLMRDAKIYQIYEGTSQIQRLIVAR 417
Cdd:PRK11561 404 GYCEESELPRLYREMPVNSIWEGSGNIMCLDVLR 437
NcnH cd01159
Naphthocyclinone hydroxylase; Naphthocyclinone is an aromatic polyketide and an antibiotic, ...
 179-398 3.85e-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: 61.21  E-value: 3.85e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187960098 179 KAEKKGDEYIINGQKMWITNGGKANWYFLLARSDPDPKAPANKAFtgFIVEADtpgIQIGRKELNMGQRCSDTRGIVFED 258
Cdd:cd01159  112 RAERVDGGYRVSGTWPFASGCDHADWILVGAIVEDDDGGPLPRAF--VVPRAE---YEIVDTWHVVGLRGTGSNTVVVDD 186

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187960098 259 VKVPKENVLIGDGA-----------GFKVAMGAFDKtrPVVAAGAVGLAQRALDEATKYALER---KTFGKLLVEHQAIS 324
Cdd:cd01159  187 VFVPEHRTLTAGDMmagdgpggstpVYRMPLRQVFP--LSFAAVSLGAAEGALAEFLELAGKRvrqYGAAVKMAEAPITQ 264

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187960098 325 FMLAEMAMKVELARMSYQRAAWEVDS---------------GRRNTYYASIAKAFAGDIANQLAtdavqilGGNGFNTEY 389
Cdd:cd01159  265 LRLAEAAAELDAARAFLERATRDLWAhalaggpidveerarIRRDAAYAAKLSAEAVDRLFHAA-------GGSALYTAS 337


                 ....*....
gi 187960098 390 PVEKLMRDA 398
Cdd:cd01159  338 PLQRIWRDI 346
PTZ00457 PTZ00457
acyl-CoA dehydrogenase; Provisional
 90-302 7.56e-09

acyl-CoA dehydrogenase; Provisional


Pssm-ID: 185636 [Multi-domain]  Cd Length: 520  Bit Score: 57.58  E-value: 7.56e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187960098  90 LMNTHIPENCGGLGLGTFDACLISEELAYGCTGVQTAIEGNSlGQMPIIIA--GNDQQKKKYLGRMTEEPLMCAYCVTEp 167
Cdd:PTZ00457  65 LYGARIATEYGGLGLGHTAHALIYEEVGTNCDSKLLSTIQHS-GFCTYLLStvGSKELKGKYLTAMSDGTIMMGWATEE- 142

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187960098 168 GAGSDVAGIKTKAEKKGD-EYIINGQKMWItNGGKANWYFLLAR------SDPDPKAPANKAFtgFIVEADTPGIQIgrk 240
Cdd:PTZ00457 143 GCGSDISMNTTKASLTDDgSYVLTGQKRCE-FAASATHFLVLAKtltqtaAEEGATEVSRNSF--FICAKDAKGVSV--- 216

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 187960098 241 elnmgqrcsDTRGIVFEDvkVPKENVLIGDGAGFKVAMGAFDKTRPVVAAGAVGLAQRALDE 302
Cdd:PTZ00457 217 ---------NGDSVVFEN--TPAADVVGVVGEGFKDAMITLFTEQYLYAASLLGIMKRVVQE 267
PLN02636 PLN02636
acyl-coenzyme A oxidase
 122-314 7.84e-09

acyl-coenzyme A oxidase


Pssm-ID: 215342 [Multi-domain]  Cd Length: 686  Bit Score: 57.56  E-value: 7.84e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187960098 122 GVQTAIEGNSlgqmpIIIAGNDQQKKKYLGRMTEEPLMCAYCVTEPGAGSDVAGIKTKA--EKKGDEYIIN-----GQKM 194
Cdd:PLN02636 142 GVQYSLWGGS-----VINLGTKKHRDKYFDGIDNLDYPGCFAMTELHHGSNVQGLQTTAtfDPLTDEFVINtpndgAIKW 216

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187960098 195 WITNG---GK-ANWYFLLARSDPDPKAPANKAFTGFIV-------EADTPGIQIGRKELNMGQRCSDTRGIVFEDVKVPK 263
Cdd:PLN02636 217 WIGNAavhGKfATVFARLKLPTHDSKGVSDMGVHAFIVpirdmktHQVLPGVEIRDCGHKVGLNGVDNGALRFRSVRIPR 296

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 187960098 264 ENVL--IGD--------------GAGFKVAMGAFDKTRPVVAAGAVGLAQRALDEATKYALERKTFG 314
Cdd:PLN02636 297 DNLLnrFGDvsrdgkytsslptiNKRFAATLGELVGGRVGLAYGSVGVLKASNTIAIRYSLLRQQFG 363
PLN02443 PLN02443
acyl-coenzyme A oxidase
 141-314 2.81e-08

acyl-coenzyme A oxidase


Pssm-ID: 178062 [Multi-domain]  Cd Length: 664  Bit Score: 56.00  E-value: 2.81e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187960098 141 GNDQQKKKYLGRMTEEPLMCAYCVTEPGAGSDVAGIKTKA--EKKGDEYIIN-----GQKMWITNGGKANWYFLL-ARSD 212
Cdd:PLN02443 114 GTEEQQKKWLPLAYKMQIIGCYAQTELGHGSNVQGLETTAtfDPKTDEFVIHsptltSSKWWPGGLGKVSTHAVVyARLI 193

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187960098 213 PDPKapaNKAFTGFIVEADT-------PGI---QIGRKELNMGQRCSDTRGIVFEDVKVPKENVL------------IGD 270
Cdd:PLN02443 194 TNGK---DHGIHGFIVQLRSlddhsplPGVtvgDIGMKFGNGAYNTMDNGFLRFDHVRIPRDQMLmrlskvtregkyVQS 270

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....
gi 187960098 271 GAGFKVAMGAFDKTRPVVAAGAVGLAQRALDEATKYALERKTFG 314
Cdd:PLN02443 271 DVPRQLVYGTMVYVRQTIVADASTALSRAVCIATRYSAVRRQFG 314
PRK13026 PRK13026
acyl-CoA dehydrogenase; Reviewed
 95-384 3.72e-08

acyl-CoA dehydrogenase; Reviewed


Pssm-ID: 237277 [Multi-domain]  Cd Length: 774  Bit Score: 55.73  E-value: 3.72e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187960098  95 IPENCGGLGlgtFDA----CLISEELAYGCTGVQTAIEGNSLGQMPIIIA-GNDQQKKKYLGRM---TEEPlmCaYCVTE 166
Cdd:PRK13026 127 IPKEYGGKG---FSAyansTIVSKIATRSVSAAVTVMVPNSLGPGELLTHyGTQEQKDYWLPRLadgTEIP--C-FALTG 200

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187960098 167 PGAGSDVA-----GIKTKAEKKGDEYI---INGQKMWITNGGKANWYFLLAR-SDPDP--KAPANKAFTGFIVEADTPGI 235
Cdd:PRK13026 201 PEAGSDAGaipdtGIVCRGEFEGEEVLglrLTWDKRYITLAPVATVLGLAFKlRDPDGllGDKKELGITCALIPTDHPGV 280

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187960098 236 QIGRKELNMGQRCSD--TRGivfEDVKVPKEnVLIGD----GAGFKVAMGAFDKTRPV-VAAGAVGLAQRALDEATKYAL 308
Cdd:PRK13026 281 EIGRRHNPLGMAFMNgtTRG---KDVFIPLD-WIIGGpdyaGRGWRMLVECLSAGRGIsLPALGTASGHMATRTTGAYAY 356

                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 187960098 309 ERKTFGKLLVEHQAISFMLAEMAMK---VELARMSYQRAaweVDSGRRNTYYASIAKAFAGDIANQLATDAVQILGGNG 384
Cdd:PRK13026 357 VRRQFGMPIGQFEGVQEALARIAGNtylLEAARRLTTTG---LDLGVKPSVVTAIAKYHMTELARDVVNDAMDIHAGKG 432
fadE PRK09463
acyl-CoA dehydrogenase; Reviewed
 141-384 1.13e-07

acyl-CoA dehydrogenase; Reviewed


Pssm-ID: 236528 [Multi-domain]  Cd Length: 777  Bit Score: 54.05  E-value: 1.13e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187960098 141 GNDQQKKKYLGRM---TEEPlmCaYCVTEPGAGSDVA-----GIKTKAEKKGDEYI---INGQKMWITNG------GKAn 203
Cdd:PRK09463 176 GTDEQKDHYLPRLargEEIP--C-FALTSPEAGSDAGsipdtGVVCKGEWQGEEVLgmrLTWNKRYITLApiatvlGLA- 251

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187960098 204 wyFLLarSDPDpkapankaftGFI------------VEADTPGIQIGRKELNMGQRCSD--TRGivfEDVKVPKENVlIG 269
Cdd:PRK09463 252 --FKL--YDPD----------GLLgdkedlgitcalIPTDTPGVEIGRRHFPLNVPFQNgpTRG---KDVFIPLDYI-IG 313

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187960098 270 D----GAGFKVAMGAFDKTR----PVVAAGAVGLAQRAldeATKYALERKTFGKLLVEHQAISFMLAEMAMKvelarmsy 341
Cdd:PRK09463 314 GpkmaGQGWRMLMECLSVGRgislPSNSTGGAKLAALA---TGAYARIRRQFKLPIGKFEGIEEPLARIAGN-------- 382

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....
gi 187960098 342 qraAWEVDSGRRNTYYA-----------SIAKAFAGDIANQLATDAVQILGGNG 384
Cdd:PRK09463 383 ---AYLMDAARTLTTAAvdlgekpsvlsAIAKYHLTERGRQVINDAMDIHGGKG 433
PLN02312 PLN02312
acyl-CoA oxidase
 141-313 1.16e-07

acyl-CoA oxidase


Pssm-ID: 215178 [Multi-domain]  Cd Length: 680  Bit Score: 54.01  E-value: 1.16e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187960098 141 GNDQQKKKYLGRMTEEPLMCAYCVTEPGAGSDVAGIKTKA--EKKGDEYIIN-----GQKMWItnGGKAN---WYFLLAR 210
Cdd:PLN02312 168 GTKRHHDKWLKDTEDYVVKGCFAMTELGHGSNVRGIETVTtyDPKTEEFVINtpcesAQKYWI--GGAANhatHTIVFSQ 245

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187960098 211 SDPDPKAPANKAFTGFIVEAD---TPGIQIGRKELNMGQRCSDTRGIVFEDVKVPKENVL------IGDG---------- 271
Cdd:PLN02312 246 LHINGKNEGVHAFIAQIRDQDgniCPNIRIADCGHKIGLNGVDNGRIWFDNLRIPRENLLnsvadvSPDGkyvsaikdpd 325

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|..
gi 187960098 272 AGFKVAMGAFDKTRPVVAAGAVGLAQRALDEATKYALERKTF 313
Cdd:PLN02312 326 QRFGAFLAPLTSGRVTIAVSAIYSSKVGLAIAIRYSLSRRAF 367
PTZ00460 PTZ00460
acyl-CoA dehydrogenase; Provisional
 141-313 1.01e-05

acyl-CoA dehydrogenase; Provisional


Pssm-ID: 185639 [Multi-domain]  Cd Length: 646  Bit Score: 47.92  E-value: 1.01e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187960098 141 GNDQQKKKYLGRMTEEPLMCAYCVTEPGAGSDVAGIKTKA--EKKGDEYIIN-----GQKMWITN-GGKANWYFLLARSD 212
Cdd:PTZ00460 110 GTDEQINLWMPSLLNFEIVGCYAQTELGHGSDVQNLETTAtyDKQTNEFVIHtpsveAVKFWPGElGFLCNFALVYAKLI 189

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187960098 213 PDPKAPANKAFTGFIVEADT----PGIQIGRKELNMGQRCSDTRGIVFEDVKVPKENVL-----IGDGAGF------KVA 277
Cdd:PTZ00460 190 VNGKNKGVHPFMVRIRDKEThkplQGVEVGDIGPKMGYAVKDNGFLSFDHYRIPLDSLLaryikVSEDGQVerqgnpKVS 269

                        170       180       190
                 ....*....|....*....|....*....|....*.
gi 187960098 278 MGAFDKTRPVVAAGAVGLAQRALDEATKYALERKTF 313
Cdd:PTZ00460 270 YASMMYMRNLIIDQYPRFAAQALTVAIRYSIYRQQF 305
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
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