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Conserved domains on  [gi|4557231|ref|NP_000007|]
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medium-chain specific acyl-CoA dehydrogenase, mitochondrial isoform a 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 ...
41-418 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: 797.18  E-value: 0e+00
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557231   41 FTEQQKEFQATARKFAREEIIPVAAEYDKTGEYPVPLIRRAWELGLMNTHIPENCGGLGLGTFDACLISEELAYGCTGVQ 120
Cdd:cd01157   1 LTEQQKEFQETARKFAREEIIPVAAEYDKSGEYPWPLIKRAWELGLMNTHIPEDCGGLGLGTFDTCLITEELAYGCTGVQ 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557231  121 TAIEGNSLGQMPIIIAGNDQQKKKYLGRMTEEPLMCAYCVTEPGAGSDVAGIKTKAEKKGDEYIINGQKMWITNGGKANW 200
Cdd:cd01157  81 TAIEANSLGQMPVIISGNDEQKKKYLGRMTEEPLMCAYCVTEPGAGSDVAGIKTKAEKKGDEYIINGQKMWITNGGKANW 160
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557231  201 YFLLARSDPDPKAPANKAFTGFIVEADTPGIQIGRKELNMGQRCSDTRGIVFEDVKVPKENVLIGDGAGFKVAMGAFDKT 280
Cdd:cd01157 161 YFLLARSDPDPKCPASKAFTGFIVEADTPGIQPGRKELNMGQRCSDTRGITFEDVRVPKENVLIGEGAGFKIAMGAFDKT 240
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557231  281 RPVVAAGAVGLAQRALDEATKYALERKTFGKLLVEHQAISFMLAEMAMKVELARMSYQRAAWEVDSGRRNTYYASIAKAF 360
Cdd:cd01157 241 RPPVAAGAVGLAQRALDEATKYALERKTFGKLIAEHQAVSFMLADMAMKVELARLAYQRAAWEVDSGRRNTYYASIAKAF 320
                       330       340       350       360       370
                ....*....|....*....|....*....|....*....|....*....|....*...
gi 4557231  361 AGDIANQLATDAVQILGGNGFNTEYPVEKLMRDAKIYQIYEGTSQIQRLIVAREHIDK 418
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 ...
41-418 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: 797.18  E-value: 0e+00
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557231   41 FTEQQKEFQATARKFAREEIIPVAAEYDKTGEYPVPLIRRAWELGLMNTHIPENCGGLGLGTFDACLISEELAYGCTGVQ 120
Cdd:cd01157   1 LTEQQKEFQETARKFAREEIIPVAAEYDKSGEYPWPLIKRAWELGLMNTHIPEDCGGLGLGTFDTCLITEELAYGCTGVQ 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557231  121 TAIEGNSLGQMPIIIAGNDQQKKKYLGRMTEEPLMCAYCVTEPGAGSDVAGIKTKAEKKGDEYIINGQKMWITNGGKANW 200
Cdd:cd01157  81 TAIEANSLGQMPVIISGNDEQKKKYLGRMTEEPLMCAYCVTEPGAGSDVAGIKTKAEKKGDEYIINGQKMWITNGGKANW 160
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557231  201 YFLLARSDPDPKAPANKAFTGFIVEADTPGIQIGRKELNMGQRCSDTRGIVFEDVKVPKENVLIGDGAGFKVAMGAFDKT 280
Cdd:cd01157 161 YFLLARSDPDPKCPASKAFTGFIVEADTPGIQPGRKELNMGQRCSDTRGITFEDVRVPKENVLIGEGAGFKIAMGAFDKT 240
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557231  281 RPVVAAGAVGLAQRALDEATKYALERKTFGKLLVEHQAISFMLAEMAMKVELARMSYQRAAWEVDSGRRNTYYASIAKAF 360
Cdd:cd01157 241 RPPVAAGAVGLAQRALDEATKYALERKTFGKLIAEHQAVSFMLADMAMKVELARLAYQRAAWEVDSGRRNTYYASIAKAF 320
                       330       340       350       360       370
                ....*....|....*....|....*....|....*....|....*....|....*...
gi 4557231  361 AGDIANQLATDAVQILGGNGFNTEYPVEKLMRDAKIYQIYEGTSQIQRLIVAREHIDK 418
Cdd:cd01157 321 AADIANQLATDAVQIFGGNGFNSEYPVEKLMRDAKIYQIYEGTSQIQRLIISREHLGK 378
CaiA COG1960
Acyl-CoA dehydrogenase related to the alkylation response protein AidB [Lipid transport and ...
39-414 1.92e-160

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: 456.99  E-value: 1.92e-160
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557231   39 FEFTEQQKEFQATARKFAREEIIPVAAEYDKTGEYPVPLIRRAWELGLMNTHIPENCGGLGLGTFDACLISEELAYGCTG 118
Cdd:COG1960   3 FELTEEQRALRDEVREFAEEEIAPEAREWDREGEFPRELWRKLAELGLLGLTIPEEYGGLGLSLVELALVLEELARADAS 82
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557231  119 VQTAIEGNSLGQMPIIIAGNDQQKKKYLGRMTEEPLMCAYCVTEPGAGSDVAGIKTKAEKKGDEYIINGQKMWITNGGKA 198
Cdd:COG1960  83 LALPVGVHNGAAEALLRFGTEEQKERYLPRLASGEWIGAFALTEPGAGSDAAALRTTAVRDGDGYVLNGQKTFITNAPVA 162
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557231  199 NWYFLLARSDPDPKApanKAFTGFIVEADTPGIQIGRKELNMGQRCSDTRGIVFEDVKVPKENVLIGDGAGFKVAMGAFD 278
Cdd:COG1960 163 DVILVLARTDPAAGH---RGISLFLVPKDTPGVTVGRIEDKMGLRGSDTGELFFDDVRVPAENLLGEEGKGFKIAMSTLN 239
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557231  279 KTRPVVAAGAVGLAQRALDEATKYALERKTFGKLLVEHQAISFMLAEMAMKVELARMSYQRAAWEVDSGRRNTYYASIAK 358
Cdd:COG1960 240 AGRLGLAAQALGIAEAALELAVAYAREREQFGRPIADFQAVQHRLADMAAELEAARALVYRAAWLLDAGEDAALEAAMAK 319
                       330       340       350       360       370
                ....*....|....*....|....*....|....*....|....*....|....*.
gi 4557231  359 AFAGDIANQLATDAVQILGGNGFNTEYPVEKLMRDAKIYQIYEGTSQIQRLIVARE 414
Cdd:COG1960 320 LFATEAALEVADEALQIHGGYGYTREYPLERLYRDARILTIYEGTNEIQRLIIARR 375
PLN02519 PLN02519
isovaleryl-CoA dehydrogenase
23-414 9.01e-85

isovaleryl-CoA dehydrogenase


Pssm-ID: 215284 [Multi-domain]  Cd Length: 404  Bit Score: 264.82  E-value: 9.01e-85
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557231    23 QHTKANRQREPGLGFSFEFTEQQKEFQATARKFAREEIIPVAAEYDKTGEYP--VPLIRRAWELGLMNTHIPENCGGLGL 100
Cdd:PLN02519   8 ARRRGLARRFSSSSSSLLFDDTQLQFKESVQQFAQENIAPHAAAIDATNSFPkdVNLWKLMGDFNLHGITAPEEYGGLGL 87
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557231   101 GTFDACLISEEL--AYGCTGVQTAIEGNsLGQMPIIIAGNDQQKKKYLGRMTEEPLMCAYCVTEPGAGSDVAGIKTKAEK 178
Cdd:PLN02519  88 GYLYHCIAMEEIsrASGSVGLSYGAHSN-LCINQLVRNGTPAQKEKYLPKLISGEHVGALAMSEPNSGSDVVSMKCKAER 166
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557231   179 KGDEYIINGQKMWITNGGKANWYFLLARSDPdpkAPANKAFTGFIVEADTPGIQIGRKELNMGQRCSDTRGIVFEDVKVP 258
Cdd:PLN02519 167 VDGGYVLNGNKMWCTNGPVAQTLVVYAKTDV---AAGSKGITAFIIEKGMPGFSTAQKLDKLGMRGSDTCELVFENCFVP 243
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557231   259 KENVLIGDGAGFKVAMGAFDKTRPVVAAGAVGLAQRALDEATKYALERKTFGKLLVEHQAISFMLAEMAMKVELARMSYQ 338
Cdd:PLN02519 244 EENVLGQEGKGVYVMMSGLDLERLVLAAGPLGLMQACLDVVLPYVRQREQFGRPIGEFQFIQGKLADMYTSLQSSRSYVY 323
                        330       340       350       360       370       380       390
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 4557231   339 RAAWEVDSGRRNTYYASIAKAFAGDIANQLATDAVQILGGNGFNTEYPVEKLMRDAKIYQIYEGTSQIQRLIVARE 414
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 ...
267-413 3.25e-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: 174.36  E-value: 3.25e-53
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557231    267 GAGFKVAMGAFDKTRPVVAAGAVGLAQRALDEATKYALERKTFGKLLVEHQAISFMLAEMAMKVELARMSYQRAAWEVDS 346
Cdd:pfam00441   1 GRGFRVAMETLNHERLAIAAMALGLARRALDEALAYARRRKAFGRPLIDFQLVRHKLAEMAAEIEAARLLVYRAAEALDA 80
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 4557231    347 GRRNTYYASIAKAFAGDIANQLATDAVQILGGNGFNTEYPVEKLMRDAKIYQIYEGTSQIQRLIVAR 413
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 ...
41-418 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: 797.18  E-value: 0e+00
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557231   41 FTEQQKEFQATARKFAREEIIPVAAEYDKTGEYPVPLIRRAWELGLMNTHIPENCGGLGLGTFDACLISEELAYGCTGVQ 120
Cdd:cd01157   1 LTEQQKEFQETARKFAREEIIPVAAEYDKSGEYPWPLIKRAWELGLMNTHIPEDCGGLGLGTFDTCLITEELAYGCTGVQ 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557231  121 TAIEGNSLGQMPIIIAGNDQQKKKYLGRMTEEPLMCAYCVTEPGAGSDVAGIKTKAEKKGDEYIINGQKMWITNGGKANW 200
Cdd:cd01157  81 TAIEANSLGQMPVIISGNDEQKKKYLGRMTEEPLMCAYCVTEPGAGSDVAGIKTKAEKKGDEYIINGQKMWITNGGKANW 160
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557231  201 YFLLARSDPDPKAPANKAFTGFIVEADTPGIQIGRKELNMGQRCSDTRGIVFEDVKVPKENVLIGDGAGFKVAMGAFDKT 280
Cdd:cd01157 161 YFLLARSDPDPKCPASKAFTGFIVEADTPGIQPGRKELNMGQRCSDTRGITFEDVRVPKENVLIGEGAGFKIAMGAFDKT 240
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557231  281 RPVVAAGAVGLAQRALDEATKYALERKTFGKLLVEHQAISFMLAEMAMKVELARMSYQRAAWEVDSGRRNTYYASIAKAF 360
Cdd:cd01157 241 RPPVAAGAVGLAQRALDEATKYALERKTFGKLIAEHQAVSFMLADMAMKVELARLAYQRAAWEVDSGRRNTYYASIAKAF 320
                       330       340       350       360       370
                ....*....|....*....|....*....|....*....|....*....|....*...
gi 4557231  361 AGDIANQLATDAVQILGGNGFNTEYPVEKLMRDAKIYQIYEGTSQIQRLIVAREHIDK 418
Cdd:cd01157 321 AADIANQLATDAVQIFGGNGFNSEYPVEKLMRDAKIYQIYEGTSQIQRLIISREHLGK 378
CaiA COG1960
Acyl-CoA dehydrogenase related to the alkylation response protein AidB [Lipid transport and ...
39-414 1.92e-160

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: 456.99  E-value: 1.92e-160
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557231   39 FEFTEQQKEFQATARKFAREEIIPVAAEYDKTGEYPVPLIRRAWELGLMNTHIPENCGGLGLGTFDACLISEELAYGCTG 118
Cdd:COG1960   3 FELTEEQRALRDEVREFAEEEIAPEAREWDREGEFPRELWRKLAELGLLGLTIPEEYGGLGLSLVELALVLEELARADAS 82
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557231  119 VQTAIEGNSLGQMPIIIAGNDQQKKKYLGRMTEEPLMCAYCVTEPGAGSDVAGIKTKAEKKGDEYIINGQKMWITNGGKA 198
Cdd:COG1960  83 LALPVGVHNGAAEALLRFGTEEQKERYLPRLASGEWIGAFALTEPGAGSDAAALRTTAVRDGDGYVLNGQKTFITNAPVA 162
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557231  199 NWYFLLARSDPDPKApanKAFTGFIVEADTPGIQIGRKELNMGQRCSDTRGIVFEDVKVPKENVLIGDGAGFKVAMGAFD 278
Cdd:COG1960 163 DVILVLARTDPAAGH---RGISLFLVPKDTPGVTVGRIEDKMGLRGSDTGELFFDDVRVPAENLLGEEGKGFKIAMSTLN 239
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557231  279 KTRPVVAAGAVGLAQRALDEATKYALERKTFGKLLVEHQAISFMLAEMAMKVELARMSYQRAAWEVDSGRRNTYYASIAK 358
Cdd:COG1960 240 AGRLGLAAQALGIAEAALELAVAYAREREQFGRPIADFQAVQHRLADMAAELEAARALVYRAAWLLDAGEDAALEAAMAK 319
                       330       340       350       360       370
                ....*....|....*....|....*....|....*....|....*....|....*.
gi 4557231  359 AFAGDIANQLATDAVQILGGNGFNTEYPVEKLMRDAKIYQIYEGTSQIQRLIVARE 414
Cdd:COG1960 320 LFATEAALEVADEALQIHGGYGYTREYPLERLYRDARILTIYEGTNEIQRLIIARR 375
SCAD_SBCAD cd01158
Short chain acyl-CoA dehydrogenases and eukaryotic short/branched chain acyl-CoA ...
43-418 1.38e-151

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: 434.00  E-value: 1.38e-151
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557231   43 EQQKEFQATARKFAREEIIPVAAEYDKTGEYPVPLIRRAWELGLMNTHIPENCGGLGLGTFDACLISEELAYGCTGVQTA 122
Cdd:cd01158   1 EEHQMIRKTVRDFAEKEIAPLAAEMDEKGEFPREVIKEMAELGLMGIPIPEEYGGAGLDFLAYAIAIEELAKVDASVAVI 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557231  123 IEG-NSLGQMPIIIAGNDQQKKKYLGRMTEEPLMCAYCVTEPGAGSDVAGIKTKAEKKGDEYIINGQKMWITNGGKANWY 201
Cdd:cd01158  81 VSVhNSLGANPIIKFGTEEQKKKYLPPLATGEKIGAFALSEPGAGSDAAALKTTAKKDGDDYVLNGSKMWITNGGEADFY 160
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557231  202 FLLARSDPDPKapaNKAFTGFIVEADTPGIQIGRKELNMGQRCSDTRGIVFEDVKVPKENVLIGDGAGFKVAMGAFDKTR 281
Cdd:cd01158 161 IVFAVTDPSKG---YRGITAFIVERDTPGLSVGKKEDKLGIRGSSTTELIFEDVRVPKENILGEEGEGFKIAMQTLDGGR 237
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557231  282 PVVAAGAVGLAQRALDEATKYALERKTFGKLLVEHQAISFMLAEMAMKVELARMSYQRAAWEVDSGRRNTYYASIAKAFA 361
Cdd:cd01158 238 IGIAAQALGIAQAALDAAVDYAKERKQFGKPIADFQGIQFKLADMATEIEAARLLTYKAARLKDNGEPFIKEAAMAKLFA 317
                       330       340       350       360       370
                ....*....|....*....|....*....|....*....|....*....|....*..
gi 4557231  362 GDIANQLATDAVQILGGNGFNTEYPVEKLMRDAKIYQIYEGTSQIQRLIVAReHIDK 418
Cdd:cd01158 318 SEVAMRVTTDAVQIFGGYGYTKDYPVERYYRDAKITEIYEGTSEIQRLVIAK-HLLK 373
ACAD cd00567
Acyl-CoA dehydrogenase; Both mitochondrial acyl-CoA dehydrogenases (ACAD) and peroxisomal ...
43-413 2.47e-133

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: 385.87  E-value: 2.47e-133
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557231   43 EQQKEFQATARKFAREEIIPVAAEYDKTGEYPVPLIRRAWELGlmnthipencgglglgtfdacliseelaygctgvqta 122
Cdd:cd00567   1 EEQRELRDSAREFAAEELEPYARERRETPEEPWELLAELGLLL------------------------------------- 43
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557231  123 iegnslGQMPIIIAGNDQQKKKYLGRMTEEPLMCAYCVTEPGAGSDVAGIKTKAEKKGDEYIINGQKMWITNGGKANWYF 202
Cdd:cd00567  44 ------GAALLLAYGTEEQKERYLPPLASGEAIAAFALTEPGAGSDLAGIRTTARKDGDGYVLNGRKIFISNGGDADLFI 117
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557231  203 LLARSDPDPkaPANKAFTGFIVEADTPGIQIGRKELNMGQRCSDTRGIVFEDVKVPKENVLIGDGAGFKVAMGAFDKTRP 282
Cdd:cd00567 118 VLARTDEEG--PGHRGISAFLVPADTPGVTVGRIWDKMGMRGSGTGELVFDDVRVPEDNLLGEEGGGFELAMKGLNVGRL 195
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557231  283 VVAAGAVGLAQRALDEATKYALERKTFGKLLVEHQAISFMLAEMAMKVELARMSYQRAAWEVDSGRRN-TYYASIAKAFA 361
Cdd:cd00567 196 LLAAVALGAARAALDEAVEYAKQRKQFGKPLAEFQAVQFKLADMAAELEAARLLLYRAAWLLDQGPDEaRLEAAMAKLFA 275
                       330       340       350       360       370
                ....*....|....*....|....*....|....*....|....*....|..
gi 4557231  362 GDIANQLATDAVQILGGNGFNTEYPVEKLMRDAKIYQIYEGTSQIQRLIVAR 413
Cdd:cd00567 276 TEAAREVADLAMQIHGGRGYSREYPVERYLRDARAARIAEGTAEIQRLIIAR 327
IBD cd01162
Isobutyryl-CoA dehydrogenase; Isobutyryl-CoA dehydrogenase (IBD) catalyzes the alpha, beta- ...
42-414 5.85e-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: 333.26  E-value: 5.85e-112
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557231   42 TEQQKEFQATARKFAREEIIPVAAEYDKTGEYPVPLIRRAWELGLMNTHIPENCGGLGLGTFDACLISEELAYGCTGVQT 121
Cdd:cd01162   2 NEEQRAIQEVARAFAAKEMAPHAADWDQKKHFPVDVLRKAAELGFGGIYIRDDVGGSGLSRLDASIIFEALSTGCVSTAA 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557231  122 AIEGNSLGQMPIIIAGNDQQKKKYLGRMTEEPLMCAYCVTEPGAGSDVAGIKTKAEKKGDEYIINGQKMWITNGGKANWY 201
Cdd:cd01162  82 YISIHNMCAWMIDSFGNDEQRERFLPDLCTMEKLASYCLTEPGSGSDAAALRTRAVREGDHYVLNGSKAFISGAGDSDVY 161
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557231  202 FLLARSDpdpkAPANKAFTGFIVEADTPGIQIGRKELNMGQRCSDTRGIVFEDVKVPKENVLIGDGAGFKVAMGAFDKTR 281
Cdd:cd01162 162 VVMARTG----GEGPKGISCFVVEKGTPGLSFGANEKKMGWNAQPTRAVIFEDCRVPVENRLGGEGQGFGIAMAGLNGGR 237
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557231  282 PVVAAGAVGLAQRALDEATKYALERKTFGKLLVEHQAISFMLAEMAMKVELARMSYQRAAWEVDSGRRN-TYYASIAKAF 360
Cdd:cd01162 238 LNIASCSLGAAQAALDLARAYLEERKQFGKPLADFQALQFKLADMATELVASRLMVRRAASALDRGDPDaVKLCAMAKRF 317
                       330       340       350       360       370
                ....*....|....*....|....*....|....*....|....*....|....
gi 4557231  361 AGDIANQLATDAVQILGGNGFNTEYPVEKLMRDAKIYQIYEGTSQIQRLIVARE 414
Cdd:cd01162 318 ATDECFDVANQALQLHGGYGYLKDYPVEQYVRDLRVHQILEGTNEIMRLIIARA 371
IVD cd01156
Isovaleryl-CoA dehydrogenase; Isovaleryl-CoA dehydrogenase (IVD) is an is an acyl-CoA ...
41-414 7.66e-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: 330.53  E-value: 7.66e-111
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557231   41 FTEQQKEFQATARKFAREEIIPVAAEYDKTGEYPVPLIRRAWELGLMNTHIPENCGGLGLGTFDACLISEELAYGCTGVQ 120
Cdd:cd01156   2 LDDEIEMLRQSVREFAQKEIAPLAAKIDRDNEFPRDLWRKMGKLGLLGITAPEEYGGSGMGYLAHVIIMEEISRASGSVA 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557231  121 TAIEGNS---LGQmpIIIAGNDQQKKKYLGRMTEEPLMCAYCVTEPGAGSDVAGIKTKAEKKGDEYIINGQKMWITNGGK 197
Cdd:cd01156  82 LSYGAHSnlcINQ--IYRNGSAAQKEKYLPKLISGEHIGALAMSEPNAGSDVVSMKLRAEKKGDRYVLNGSKMWITNGPD 159
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557231  198 ANWYFLLARSDPDPKApanKAFTGFIVEADTPGIQIGRKELNMGQRCSDTRGIVFEDVKVPKENVLIGDGAGFKVAMGAF 277
Cdd:cd01156 160 ADTLVVYAKTDPSAGA---HGITAFIVEKGMPGFSRAQKLDKLGMRGSNTCELVFEDCEVPEENILGGENKGVYVLMSGL 236
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557231  278 DKTRPVVAAGAVGLAQRALDEATKYALERKTFGKLLVEHQAISFMLAEMAMKVELARMSYQRAAWEVDSGRRNTYYASIA 357
Cdd:cd01156 237 DYERLVLAGGPIGIMQAALDVAIPYAHQRKQFGQPIGEFQLVQGKLADMYTRLNASRSYLYTVAKACDRGNMDPKDAAGV 316
                       330       340       350       360       370
                ....*....|....*....|....*....|....*....|....*....|....*..
gi 4557231  358 KAFAGDIANQLATDAVQILGGNGFNTEYPVEKLMRDAKIYQIYEGTSQIQRLIVARE 414
Cdd:cd01156 317 ILYAAEKATQVALDAIQILGGNGYINDYPTGRLLRDAKLYEIGAGTSEIRRMVIGRE 373
LCAD cd01160
Long chain acyl-CoA dehydrogenase; LCAD is an acyl-CoA dehydrogenases (ACAD), which is found ...
43-414 3.74e-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: 308.27  E-value: 3.74e-102
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557231   43 EQQKEFQATARKFAREEIIPVAAEYDKTGEYPVPLIRRAWELGLMNTHIPENCGGLGLGTFDACLISEELAY-GCTGVQT 121
Cdd:cd01160   1 EEHDAFRDVVRRFFAKEVAPFHHEWEKAGEVPREVWRKAGEQGLLGVGFPEEYGGIGGDLLSAAVLWEELARaGGSGPGL 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557231  122 AIEgNSLGQMPIIIAGNDQQKKKYLGRMTEEPLMCAYCVTEPGAGSDVAGIKTKAEKKGDEYIINGQKMWITNGGKANWY 201
Cdd:cd01160  81 SLH-TDIVSPYITRAGSPEQKERVLPQMVAGKKIGAIAMTEPGAGSDLQGIRTTARKDGDHYVLNGSKTFITNGMLADVV 159
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557231  202 FLLARSDPDPKAPANKAFtgFIVEADTPGIQIGRKELNMGQRCSDTRGIVFEDVKVPKENVLIGDGAGFKVAMGAFDKTR 281
Cdd:cd01160 160 IVVARTGGEARGAGGISL--FLVERGTPGFSRGRKLKKMGWKAQDTAELFFDDCRVPAENLLGEENKGFYYLMQNLPQER 237
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557231  282 PVVAAGAVGLAQRALDEATKYALERKTFGKLLVEHQAISFMLAEMAMKVELARMSYQRAAWEVDSGRRNTYYASIAKAFA 361
Cdd:cd01160 238 LLIAAGALAAAEFMLEETRNYVKQRKAFGKTLAQLQVVRHKIAELATKVAVTRAFLDNCAWRHEQGRLDVAEASMAKYWA 317
                       330       340       350       360       370
                ....*....|....*....|....*....|....*....|....*....|...
gi 4557231  362 GDIANQLATDAVQILGGNGFNTEYPVEKLMRDAKIYQIYEGTSQIQRLIVARE 414
Cdd:cd01160 318 TELQNRVAYECVQLHGGWGYMREYPIARAYRDARVQPIYGGTTEIMKELISRQ 370
VLCAD cd01161
Very long chain acyl-CoA dehydrogenase; VLCAD is an acyl-CoA dehydrogenase (ACAD), which is ...
40-412 4.38e-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: 283.59  E-value: 4.38e-92
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557231   40 EFTEQQKEFQATARKFAREEIIPvaAEYDKTGEYPVPLIRRAWELGLMNTHIPENCGGLGLGTFDACLISEELAY-GCTG 118
Cdd:cd01161  26 EQTEELNMLVGPVEKFFEEVNDP--AKNDQLEKIPRKTLTQLKELGLFGLQVPEEYGGLGLNNTQYARLAEIVGMdLGFS 103
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557231  119 VQTAIEgNSLGQMPIIIAGNDQQKKKYLGRMTEEPLMCAYCVTEPGAGSDVAGIKTKAEKK--GDEYIINGQKMWITNGG 196
Cdd:cd01161 104 VTLGAH-QSIGFKGILLFGTEAQKEKYLPKLASGEWIAAFALTEPSSGSDAASIRTTAVLSedGKHYVLNGSKIWITNGG 182
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557231  197 KANWYFLLARSD-PDPKAPANKAFTGFIVEADTPGIQIGRKELNMGQRCSDTRGIVFEDVKVPKENVLIGDGAGFKVAMG 275
Cdd:cd01161 183 IADIFTVFAKTEvKDATGSVKDKITAFIVERSFGGVTNGPPEKKMGIKGSNTAEVYFEDVKIPVENVLGEVGDGFKVAMN 262
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557231  276 AFDKTRPVVAAGAVGLAQRALDEATKYALERKTFGKLLVEHQAISFMLAEMAMKVELARMSYQRAAWEVDSGRRNTYY-- 353
Cdd:cd01161 263 ILNNGRFGMGAALIGTMKRCIEKAVDYANNRKQFGKKIHEFGLIQEKLANMAILQYATESMAYMTSGNMDRGLKAEYQie 342
                       330       340       350       360       370
                ....*....|....*....|....*....|....*....|....*....|....*....
gi 4557231  354 ASIAKAFAGDIANQLATDAVQILGGNGFNTEYPVEKLMRDAKIYQIYEGTSQIQRLIVA 412
Cdd:cd01161 343 AAISKVFASEAAWLVVDEAIQIHGGMGFMREYGVERVLRDLRIFRIFEGTNEILRLFIA 401
PLN02519 PLN02519
isovaleryl-CoA dehydrogenase
23-414 9.01e-85

isovaleryl-CoA dehydrogenase


Pssm-ID: 215284 [Multi-domain]  Cd Length: 404  Bit Score: 264.82  E-value: 9.01e-85
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557231    23 QHTKANRQREPGLGFSFEFTEQQKEFQATARKFAREEIIPVAAEYDKTGEYP--VPLIRRAWELGLMNTHIPENCGGLGL 100
Cdd:PLN02519   8 ARRRGLARRFSSSSSSLLFDDTQLQFKESVQQFAQENIAPHAAAIDATNSFPkdVNLWKLMGDFNLHGITAPEEYGGLGL 87
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557231   101 GTFDACLISEEL--AYGCTGVQTAIEGNsLGQMPIIIAGNDQQKKKYLGRMTEEPLMCAYCVTEPGAGSDVAGIKTKAEK 178
Cdd:PLN02519  88 GYLYHCIAMEEIsrASGSVGLSYGAHSN-LCINQLVRNGTPAQKEKYLPKLISGEHVGALAMSEPNSGSDVVSMKCKAER 166
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557231   179 KGDEYIINGQKMWITNGGKANWYFLLARSDPdpkAPANKAFTGFIVEADTPGIQIGRKELNMGQRCSDTRGIVFEDVKVP 258
Cdd:PLN02519 167 VDGGYVLNGNKMWCTNGPVAQTLVVYAKTDV---AAGSKGITAFIIEKGMPGFSTAQKLDKLGMRGSDTCELVFENCFVP 243
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557231   259 KENVLIGDGAGFKVAMGAFDKTRPVVAAGAVGLAQRALDEATKYALERKTFGKLLVEHQAISFMLAEMAMKVELARMSYQ 338
Cdd:PLN02519 244 EENVLGQEGKGVYVMMSGLDLERLVLAAGPLGLMQACLDVVLPYVRQREQFGRPIGEFQFIQGKLADMYTSLQSSRSYVY 323
                        330       340       350       360       370       380       390
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 4557231   339 RAAWEVDSGRRNTYYASIAKAFAGDIANQLATDAVQILGGNGFNTEYPVEKLMRDAKIYQIYEGTSQIQRLIVARE 414
Cdd:PLN02519 324 SVARDCDNGKVDRKDCAGVILCAAERATQVALQAIQCLGGNGYINEYPTGRLLRDAKLYEIGAGTSEIRRMLIGRE 399
GCD cd01151
Glutaryl-CoA dehydrogenase; Glutaryl-CoA dehydrogenase (GCD). GCD is an acyl-CoA dehydrogenase, ...
35-414 2.28e-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: 231.86  E-value: 2.28e-72
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557231   35 LGFSFEFTEQQKEFQATARKFAREEIIPVAAEYDKTGEYPVPLIRRAWELGLMNThIPENCGGLGLGTFDACLISEELAY 114
Cdd:cd01151   7 LNLDDLLTEEERAIRDTAREFCQEELAPRVLEAYREEKFDRKIIEEMGELGLLGA-TIKGYGCAGLSSVAYGLIAREVER 85
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557231  115 GCTGVQTAIE-GNSLGQMPIIIAGNDQQKKKYLGRMTEEPLMCAYCVTEPGAGSDVAGIKTKAEKKGDEYIINGQKMWIT 193
Cdd:cd01151  86 VDSGYRSFMSvQSSLVMLPIYDFGSEEQKQKYLPKLASGELIGCFGLTEPNHGSDPGGMETRARKDGGGYKLNGSKTWIT 165
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557231  194 NGGKANWYFLLARSDPDPKapankaFTGFIVEADTPGIQIGRKELNMGQRCSDTRGIVFEDVKVPKENVLIGdGAGFKVA 273
Cdd:cd01151 166 NSPIADVFVVWARNDETGK------IRGFILERGMKGLSAPKIQGKFSLRASITGEIVMDNVFVPEENLLPG-AEGLRGP 238
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557231  274 MGAFDKTRPVVAAGAVGLAQRALDEATKYALERKTFGKLLVEHQAISFMLAEMAMKVELArmsyQRAAWEV----DSGRR 349
Cdd:cd01151 239 FKCLNNARYGIAWGALGAAEDCYHTARQYVLDRKQFGRPLAAFQLVQKKLADMLTEIALG----LLACLRVgrlkDQGKA 314
                       330       340       350       360       370       380
                ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 4557231  350 NTYYASIAKAFAGDIANQLATDAVQILGGNGFNTEYPVEKLMRDAKIYQIYEGTSQIQRLIVARE 414
Cdd:cd01151 315 TPEQISLLKRNNCGKALEIARTAREMLGGNGISDEYHIIRHMVNLESVNTYEGTHDIHALILGRA 379
ACAD_fadE5 cd01153
Putative acyl-CoA dehydrogenases similar to fadE5; Putative acyl-CoA dehydrogenase (ACAD). ...
50-407 2.94e-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: 203.78  E-value: 2.94e-61
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557231   50 ATARKFAREEIIPVAAEYDKTG--------EYPVP---LIRRAWELGLMNTHIPENCGGLGLGTFDACLISEELAYGCTG 118
Cdd:cd01153   3 EEVARLAENVLAPLNADGDREGpvfddgrvVVPPPfkeALDAFAEAGWMALGVPEEYGGQGLPITVYSALAEIFSRGDAP 82
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557231  119 VqtAIEGNSLGQMPIIIA-GNDQQKKKYLGRMTEEPLMCAYCVTEPGAGSDVAGIKTKAEKKGD-EYIINGQKMWITNGG 196
Cdd:cd01153  83 L--MYASGTQGAAATLLAhGTEAQREKWIPRLAEGEWTGTMCLTEPDAGSDLGALRTKAVYQADgSWRINGVKRFISAGE 160
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557231  197 KANW----YFLLARSDPDPkaPANKAFTGFIV-----EADTPGIQIGRKELNMGQRCSDTRGIVFEDVKVPkenvLIGD- 266
Cdd:cd01153 161 HDMSenivHLVLARSEGAP--PGVKGLSLFLVpkfldDGERNGVTVARIEEKMGLHGSPTCELVFDNAKGE----LIGEe 234
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557231  267 GAGFKVAMGAFDKTRPVVAAGAVGLAQRALDEATKYALERKTFGKLLVE--------HQAISFMLAEMAMKVELARMSYQ 338
Cdd:cd01153 235 GMGLAQMFAMMNGARLGVGTQGTGLAEAAYLNALAYAKERKQGGDLIKAapavtiihHPDVRRSLMTQKAYAEGSRALDL 314
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557231  339 RAAWEVDSGRR--------------NTYYASIAKAFAGDIANQLATDAVQILGGNGFNTEYPVEKLMRDAKIYQIYEGTS 404
Cdd:cd01153 315 YTATVQDLAERkategedrkalsalADLLTPVVKGFGSEAALEAVSDAIQVHGGSGYTREYPIEQYYRDARITTIYEGTT 394

                ...
gi 4557231  405 QIQ 407
Cdd:cd01153 395 GIQ 397
ACAD_fadE6_17_26 cd01152
Putative acyl-CoA dehydrogenases similar to fadE6, fadE17, and fadE26; Putative acyl-CoA ...
43-413 3.72e-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: 202.58  E-value: 3.72e-61
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557231   43 EQQKEFQATARKFAREEIIP-----VAAEYDKTGEYPVPLIRRAWELGLMNTHIPENCGGLGLGTFDACLISEELAYGCT 117
Cdd:cd01152   1 PSEEAFRAEVRAWLAAHLPPelreeSALGYREGREDRRRWQRALAAAGWAAPGWPKEYGGRGASLMEQLIFREEMAAAGA 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557231  118 GVQtaieGNSLGQM---PIIIA-GNDQQKKKYLGRMTEEPLMCAYCVTEPGAGSDVAGIKTKAEKKGDEYIINGQKMWIT 193
Cdd:cd01152  81 PVP----FNQIGIDlagPTILAyGTDEQKRRFLPPILSGEEIWCQGFSEPGAGSDLAGLRTRAVRDGDDWVVNGQKIWTS 156
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557231  194 NGGKANWYFLLARSDPDpkAPANKAFTGFIVEADTPGIQIgR--KELNMGqrcSDTRGIVFEDVKVPKENVLIGDGAGFK 271
Cdd:cd01152 157 GAHYADWAWLLVRTDPE--APKHRGISILLVDMDSPGVTV-RpiRSINGG---EFFNEVFLDDVRVPDANRVGEVNDGWK 230
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557231  272 VAMGAFDKTRPVVAAGAVGLAQRALDeatkYALERKTFGKLLVEHQAISFMLAEMAMKVELARMSYQRAAWEVDSGRRNT 351
Cdd:cd01152 231 VAMTTLNFERVSIGGSAATFFELLLA----RLLLLTRDGRPLIDDPLVRQRLARLEAEAEALRLLVFRLASALAAGKPPG 306
                       330       340       350       360       370       380       390
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557231  352 YYASIAKAFAGDIANQLATDAVQILG--------GNGFNTEYPVEKLMRDAKIYQIYEGTSQIQRLIVAR 413
Cdd:cd01152 307 AEASIAKLFGSELAQELAELALELLGtaallrdpAPGAELAGRWEADYLRSRATTIYGGTSEIQRNIIAE 376
PTZ00461 PTZ00461
isovaleryl-CoA dehydrogenase; Provisional
42-403 4.66e-61

isovaleryl-CoA dehydrogenase; Provisional


Pssm-ID: 185640 [Multi-domain]  Cd Length: 410  Bit Score: 203.25  E-value: 4.66e-61
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557231    42 TEQQKEFQATARKFAREEIIPVAAEYDKTGEYPVPLIRRAWELGLMNTHIPENCGGLGLGTFDACLISEELAYGCTGVQT 121
Cdd:PTZ00461  38 TPEHAALRETVAKFSREVVDKHAREDDINMHFNRDLFKQLGDLGVMGVTVPEADGGAGMDAVAAVIIHHELSKYDPGFCL 117
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557231   122 AIEGNS-LGQMPIIIAGNDQQKKKYLGRMTEEPLMCAYCVTEPGAGSDVAGIKTKAEKKGDE-YIINGQKMWITNGGKAN 199
Cdd:PTZ00461 118 AYLAHSmLFVNNFYYSASPAQRARWLPKVLTGEHVGAMGMSEPGAGTDVLGMRTTAKKDSNGnYVLNGSKIWITNGTVAD 197
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557231   200 WYFLLARSDpdpkapanKAFTGFIVEADTPGIQIGRKELNMGQRCSDTRGIVFEDVKVPKENVLIGDGAGFKVAMGAFDK 279
Cdd:PTZ00461 198 VFLIYAKVD--------GKITAFVVERGTKGFTQGPKIDKCGMRASHMCQLFFEDVVVPAENLLGEEGKGMVGMMRNLEL 269
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557231   280 TRPVVAAGAVGLAQRALDEATKYALERKTFGKLLVEHQAISFMLAEMAMKVELARMSYQRAAWEVDSGRRNTYYASIAKA 359
Cdd:PTZ00461 270 ERVTLAAMAVGIAERSVELMTSYASERKAFGKPISNFGQIQRYIAEGYADTEAAKALVYSVSHNVHPGNKNRLGSDAAKL 349
                        330       340       350       360
                 ....*....|....*....|....*....|....*....|....
gi 4557231   360 FAGDIANQLATDAVQILGGNGFNTEYPVEKLMRDAKIYQIYEGT 403
Cdd:PTZ00461 350 FATPIAKKVADSAIQVMGGMGYSRDMPVERLWRDAKLLEIGGGT 393
PRK12341 PRK12341
acyl-CoA dehydrogenase;
39-420 4.35e-60

acyl-CoA dehydrogenase;


Pssm-ID: 183454 [Multi-domain]  Cd Length: 381  Bit Score: 199.95  E-value: 4.35e-60
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557231    39 FEFTEQQKEFQATARKF-AREEIIPVAAEYDKTGEYPVPLIRRAWELGLMNTHIPENCGGLGLGTFDACLISEELAYgcT 117
Cdd:PRK12341   3 FSLTEEQELLLASIRELiTRNFPEEYFRTCDENGTYPREFMRALADNGISMLGVPEEFGGTPADYVTQMLVLEEVSK--C 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557231   118 GVQTAIEGNSLGQMPIIIAGNDQQKKKYLgRMTEEPLMCAYC--VTEPGAGSDVAGIKTKAEKKGDEYIINGQKMWITNG 195
Cdd:PRK12341  81 GAPAFLITNGQCIHSMRRFGSAEQLRKTA-ESTLETGDPAYAlaLTEPGAGSDNNSATTTYTRKNGKVYLNGQKTFITGA 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557231   196 GKANWYFLLARsDPDPKAPaNKAFTGFIVEADTPGIQIGRKElNMGQRCSDTRGIVFEDVKVPKENVLIGDGAGFKVAMG 275
Cdd:PRK12341 160 KEYPYMLVLAR-DPQPKDP-KKAFTLWWVDSSKPGIKINPLH-KIGWHMLSTCEVYLDNVEVEESDLVGEEGMGFLNVMY 236
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557231   276 AFDKTRPVVAAGAVGLAQRALDEATKYALERKTFGKLLVEHQAISFMLAEMAMKVELARMSYQRAAWEVDSGRRNTYYAS 355
Cdd:PRK12341 237 NFEMERLINAARSLGFAECAFEDAARYANQRIQFGKPIGHNQLIQEKLTLMAIKIENMRNMVYKVAWQADNGQSLRTSAA 316
                        330       340       350       360       370       380
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 4557231   356 IAKAFAGDIANQLATDAVQILGGNGFNTEYPVEKLMRDAKIYQIYEGTSQIQRLIVAREHIDKYK 420
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 ...
267-413 3.25e-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: 174.36  E-value: 3.25e-53
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557231    267 GAGFKVAMGAFDKTRPVVAAGAVGLAQRALDEATKYALERKTFGKLLVEHQAISFMLAEMAMKVELARMSYQRAAWEVDS 346
Cdd:pfam00441   1 GRGFRVAMETLNHERLAIAAMALGLARRALDEALAYARRRKAFGRPLIDFQLVRHKLAEMAAEIEAARLLVYRAAEALDA 80
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 4557231    347 GRRNTYYASIAKAFAGDIANQLATDAVQILGGNGFNTEYPVEKLMRDAKIYQIYEGTSQIQRLIVAR 413
Cdd:pfam00441  81 GGPDGAEASMAKLYASEAAVEVADLAMQLHGGYGYLREYPVERLYRDARVLRIGEGTSEIQRNIIAR 147
ACAD_FadE2 cd01155
Acyl-CoA dehydrogenases similar to fadE2; FadE2-like Acyl-CoA dehydrogenase (ACAD). Acyl-CoA ...
43-413 7.77e-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: 7.77e-53
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557231   43 EQQKEFQATARKFAREEIIPVAAEYDktgEYPVPLIRRAW--------------ELGLMNTHIPENCGGLGLGTFDACLI 108
Cdd:cd01155   1 RKAQELRARVKAFMEEHVYPAEQEFL---EYYAEGGDRWWtpppiieklkakakAEGLWNLFLPEVSGLSGLTNLEYAYL 77
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557231  109 SEEL--------AYGCTGVQTaiegnslGQMPIIIA-GNDQQKKKYLgrmteEPLM-----CAYCVTEPG-AGSDVAGIK 173
Cdd:cd01155  78 AEETgrsffapeVFNCQAPDT-------GNMEVLHRyGSEEQKKQWL-----EPLLdgkirSAFAMTEPDvASSDATNIE 145
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557231  174 TKAEKKGDEYIINGQKMWITNGG--KANWYFLLARSDPDpKAPANKAFTGFIVEADTPGIQIGRKELNMGQrcSDTRG-- 249
Cdd:cd01155 146 CSIERDGDDYVINGRKWWSSGAGdpRCKIAIVMGRTDPD-GAPRHRQQSMILVPMDTPGVTIIRPLSVFGY--DDAPHgh 222
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557231  250 --IVFEDVKVPKENVLIGDGAGFKVAMGAFDKTRPVVAAGAVGLAQRALDEATKYALERKTFGKLLVEHQAISFMLAEMA 327
Cdd:cd01155 223 aeITFDNVRVPASNLILGEGRGFEIAQGRLGPGRIHHCMRLIGAAERALELMCQRAVSREAFGKKLAQHGVVAHWIAKSR 302
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557231  328 MKVELARMSYQRAAWEVDSGRRNTYYASIA--KAFAGDIANQLATDAVQILGGNGFNTEYPVEKLMRDAKIYQIYEGTSQ 405
Cdd:cd01155 303 IEIEQARLLVLKAAHMIDTVGNKAARKEIAmiKVAAPRMALKIIDRAIQVHGAAGVSQDTPLANMYAWARTLRIADGPDE 382

                ....*...
gi 4557231  406 IQRLIVAR 413
Cdd:cd01155 383 VHLRSIAR 390
PRK03354 PRK03354
crotonobetainyl-CoA dehydrogenase; Validated
39-420 5.97e-49

crotonobetainyl-CoA dehydrogenase; Validated


Pssm-ID: 179566 [Multi-domain]  Cd Length: 380  Bit Score: 170.78  E-value: 5.97e-49
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557231    39 FEFTEQQKEFQATARKF-AREEIIPVAAEYDKTGEYPVPLIRRAWELGLMNTHIPENCGGLGLGTFDACLISEELayGCT 117
Cdd:PRK03354   3 FNLNDEQELFVAGIRELmASENWEAYFAECDRDSVYPERFVKALADMGIDSLLIPEEHGGLDAGFVTLAAVWMEL--GRL 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557231   118 GVQTAIegnsLGQMP-----IIIAGNDQQKKKYLGRMTEEPLMCAYCVTEPGAGSDVAGIKTKAEKKGDEYIINGQKMWI 192
Cdd:PRK03354  81 GAPTYV----LYQLPggfntFLREGTQEQIDKIMAFRGTGKQMWNSAITEPGAGSDVGSLKTTYTRRNGKVYLNGSKCFI 156
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557231   193 TNGGKANWYFLLARSDPDPKAPAnkaFTGFIVEADTPGIQIGRKElNMGQRCSDTRGIVFEDVKVPKENVLIGDGAGFKV 272
Cdd:PRK03354 157 TSSAYTPYIVVMARDGASPDKPV---YTEWFVDMSKPGIKVTKLE-KLGLRMDSCCEITFDDVELDEKDMFGREGNGFNR 232
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557231   273 AMGAFDKTRPVVAAGAVGLAQRALDEATKYALERKTFGKLLVEHQAISFMLAEMAMKVELARMSYQRAAWEVDSGRRNTY 352
Cdd:PRK03354 233 VKEEFDHERFLVALTNYGTAMCAFEDAARYANQRVQFGEAIGRFQLIQEKFAHMAIKLNSMKNMLYEAAWKADNGTITSG 312
                        330       340       350       360       370       380
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 4557231   353 YASIAKAFAGDIANQLATDAVQILGGNGFNTEYPVEKLMRDAKIYQIYEGTSQIQRLIVAREHIDKYK 420
Cdd:PRK03354 313 DAAMCKYFCANAAFEVVDSAMQVLGGVGIAGNHRISRFWRDLRVDRVSGGSDEMQILTLGRAVLKQYR 380
PLN02526 PLN02526
acyl-coenzyme A oxidase
42-414 4.27e-45

acyl-coenzyme A oxidase


Pssm-ID: 178141 [Multi-domain]  Cd Length: 412  Bit Score: 161.17  E-value: 4.27e-45
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557231    42 TEQQKEFQATARKFAREEIIPVAAEYDKTGEYPVPLIRRAWELGLMNTHIP-ENCGGLGLgTFDACLISEELAYGCTGVQ 120
Cdd:PLN02526  30 TPEEQALRKRVRECMEKEVAPIMTEYWEKAEFPFHIIPKLGSLGIAGGTIKgYGCPGLSI-TASAIATAEVARVDASCST 108
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557231   121 TAIEGNSLGQMPIIIAGNDQQKKKYLGRMTEEPLMCAYCVTEPGAGSDVAGIKTKAEKKGDEYIINGQKMWITNGGKANW 200
Cdd:PLN02526 109 FILVHSSLAMLTIALCGSEAQKQKYLPSLAQLDTVACWALTEPDYGSDASSLNTTATKVEGGWILNGQKRWIGNSTFADV 188
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557231   201 YFLLARSdpdpkaPANKAFTGFIVEADTPGIQIGRKELNMGQRCSDTRGIVFEDVKVPKENVLIGDGAgFKVAMGAFDKT 280
Cdd:PLN02526 189 LVIFARN------TTTNQINGFIVKKGAPGLKATKIENKIGLRMVQNGDIVLKDVFVPDEDRLPGVNS-FQDTNKVLAVS 261
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557231   281 RPVVAAGAVGLAQRALDEATKYALERKTFGKLLVEHQAISFMLAEMAMKVELARMSYQRAAWEVDSGRRNTYYASIAKAF 360
Cdd:PLN02526 262 RVMVAWQPIGISMGVYDMCHRYLKERKQFGAPLAAFQINQEKLVRMLGNIQAMFLVGWRLCKLYESGKMTPGHASLGKAW 341
                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|....
gi 4557231   361 AGDIANQLATDAVQILGGNGFNTEYPVEKLMRDAKIYQIYEGTSQIQRLIVARE 414
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 ...
42-149 7.64e-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: 135.67  E-value: 7.64e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557231     42 TEQQKEFQATARKFAREEIIPVAAEYDKTGEYPVPLIRRAWELGLMNTHIPENCGGLGLGTFDACLISEELAYGCTGVQT 121
Cdd:pfam02771   1 TEEQEALRDTVREFAEEEIAPHAAEWDEEGEFPRELWKKLGELGLLGITIPEEYGGAGLDYLAYALVAEELARADASVAL 80
                          90       100
                  ....*....|....*....|....*....
gi 4557231    122 AIE-GNSLGQMPIIIAGNDQQKKKYLGRM 149
Cdd:pfam02771  81 ALSvHSSLGAPPILRFGTEEQKERYLPKL 109
AidB cd01154
Proteins involved in DNA damage response, similar to the AidB gene product; AidB is one of ...
145-413 8.94e-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: 133.27  E-value: 8.94e-35
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557231  145 YLGRMTEEPLMCAYCVTEPGAGSDVAGIKTKAEK-KGDEYIINGQKmWITNGGKANWYFLLARsdPDPKAPANKAFTGFI 223
Cdd:cd01154 138 LLSDRYKTGLLGGTWMTEKQGGSDLGANETTAERsGGGVYRLNGHK-WFASAPLADAALVLAR--PEGAPAGARGLSLFL 214
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557231  224 VEADTP-----GIQIGRKELNMGQRCSDTRGIVFEDVkvpkENVLIGD-GAGFKVAMGAFDKTRPVVAAGAVGLAQRALD 297
Cdd:cd01154 215 VPRLLEdgtrnGYRIRRLKDKLGTRSVATGEVEFDDA----EAYLIGDeGKGIYYILEMLNISRLDNAVAALGIMRRALS 290
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557231  298 EATKYALERKTFGKLLVEHQAISFMLAEMAMKVELARMSYQRAA--WEVDSGRRNTYYA------SIAKAFAGDIANQLA 369
Cdd:cd01154 291 EAYHYARHRRAFGKPLIDHPLMRRDLAEMEVDVEAATALTFRAAraFDRAAADKPVEAHmarlatPVAKLIACKRAAPVT 370
                       250       260       270       280
                ....*....|....*....|....*....|....*....|....
gi 4557231  370 TDAVQILGGNGFNTEYPVEKLMRDAKIYQIYEGTSQIQRLIVAR 413
Cdd:cd01154 371 SEAMEVFGGNGYLEEWPVARLHREAQVTPIWEGTGNIQALDVLR 414
PLN02876 PLN02876
acyl-CoA dehydrogenase
129-406 4.01e-32

acyl-CoA dehydrogenase


Pssm-ID: 215473 [Multi-domain]  Cd Length: 822  Bit Score: 129.14  E-value: 4.01e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557231   129 GQMPIIIA-GNDQQKKKYLGRMTEEPLMCAYCVTEPG-AGSDVAGIKTKAEKKGDEYIINGQKMWITNGGKANWYFLLAR 206
Cdd:PLN02876 524 GNMEVLLRyGNKEQQLEWLIPLLEGKIRSGFAMTEPQvASSDATNIECSIRRQGDSYVINGTKWWTSGAMDPRCRVLIVM 603
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557231   207 SDPDPKAPANKAFTGFIVEADTPGIQIGRKELNMGqrCSDT----RGIVFEDVKVPKENVLIGDGAGFKVAMGAFDKTRP 282
Cdd:PLN02876 604 GKTDFNAPKHKQQSMILVDIQTPGVQIKRPLLVFG--FDDAphghAEISFENVRVPAKNILLGEGRGFEIAQGRLGPGRL 681
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557231   283 VVAAGAVGLAQRALDEATKYALERKTFGKLLVEHQAISFMLAEMAMKVELARMSYQRAAWEVD--SGRRNTYYASIAKAF 360
Cdd:PLN02876 682 HHCMRLIGAAERGMQLMVQRALSRKAFGKLIAQHGSFLSDLAKCRVELEQTRLLVLEAADQLDrlGNKKARGIIAMAKVA 761
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*.
gi 4557231   361 AGDIANQLATDAVQILGGNGFNTEYPVEKLMRDAKIYQIYEGTSQI 406
Cdd:PLN02876 762 APNMALKVLDMAMQVHGAAGVSSDTVLAHLWATARTLRIADGPDEV 807
Acyl-CoA_dh_M pfam02770
Acyl-CoA dehydrogenase, middle domain; Central domain of Acyl-CoA dehydrogenase has a ...
157-253 1.02e-29

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


Pssm-ID: 460685 [Multi-domain]  Cd Length: 95  Bit Score: 110.83  E-value: 1.02e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557231    157 AYCVTEPGAGSDVAGIKTKA-EKKGDEYIINGQKMWITNGGKANWYFLLARSDPDPKApanKAFTGFIVEADTPGIQIGR 235
Cdd:pfam02770   1 AFALTEPGAGSDVASLKTTAaDGDGGGWVLNGTKWWITNAGIADLFLVLARTGGDDRH---GGISLFLVPKDAPGVSVRR 77
                          90
                  ....*....|....*...
gi 4557231    236 KELNMGQRCSDTRGIVFE 253
Cdd:pfam02770  78 IETKLGVRGLPTGELVFD 95
PTZ00456 PTZ00456
acyl-CoA dehydrogenase; Provisional
41-409 5.75e-22

acyl-CoA dehydrogenase; Provisional


Pssm-ID: 185635 [Multi-domain]  Cd Length: 622  Bit Score: 98.40  E-value: 5.75e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557231    41 FTEQQKEFQ----ATARKFAREEIIPVAAEYD-------KTGEYPVPL-IRRAWEL----GLMNTHIPENCGGLGLgTFD 104
Cdd:PTZ00456  52 KTDVTKELMdsllEEASKLATQTLLPLYESSDsegcvllKDGNVTTPKgFKEAYQAlkagGWTGISEPEEYGGQAL-PLS 130
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557231   105 ACLISEELAYGCTGVQTAIEGNSLGQMPIIIA-GNDQQKKKYLGRMTEEPLMCAYCVTEPGAGSDVAGIKTKAEKKGD-E 182
Cdd:PTZ00456 131 VGFITRELMATANWGFSMYPGLSIGAANTLMAwGSEEQKEQYLTKLVSGEWSGTMCLTEPQCGTDLGQVKTKAEPSADgS 210
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557231   183 YIINGQKMWITNGG---KAN-WYFLLARSDPDPkaPANKAFTGFIVEADTP----------GIQIGRKELNMGQRCSDTR 248
Cdd:PTZ00456 211 YKITGTKIFISAGDhdlTENiVHIVLARLPNSL--PTTKGLSLFLVPRHVVkpdgsletakNVKCIGLEKKMGIKGSSTC 288
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557231   249 GIVFEDVKvpkeNVLIGD-GAGFKVAMGAFDKTRPVVAAGAVGLAQRALDEATKYALERKTF------------GKLLVE 315
Cdd:PTZ00456 289 QLSFENSV----GYLIGEpNAGMKQMFTFMNTARVGTALEGVCHAELAFQNALRYARERRSMralsgtkepekpADRIIC 364
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557231   316 HQAISFML------AE--MAMKVELAR-MSYQRAAWEVDS----GRRNTYYASIAKAFAGDIANQLATDAVQILGGNGFN 382
Cdd:PTZ00456 365 HANVRQNIlfakavAEggRALLLDVGRlLDIHAAAKDAATrealDHEIGFYTPIAKGCLTEWGVEAASRCLQVWGGHGYI 444
                        410       420
                 ....*....|....*....|....*..
gi 4557231   383 TEYPVEKLMRDAKIYQIYEGTSQIQRL 409
Cdd:PTZ00456 445 KGNGMEQILRDARIGTLYEGTTGIQAL 471
Acyl-CoA_dh_2 pfam08028
Acyl-CoA dehydrogenase, C-terminal domain;
283-405 6.95e-19

Acyl-CoA dehydrogenase, C-terminal domain;


Pssm-ID: 429790 [Multi-domain]  Cd Length: 133  Bit Score: 82.39  E-value: 6.95e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557231    283 VVAAGAVGLAQRALDEATKYALERKT--FGKLLVEHQAISFMLAEMAMKVELARMSYQRAAWE----VDSGRRNTYY--- 353
Cdd:pfam08028   1 GIAAAALGAARAALAEFTERARGRVRayFGVPLAEDPATQLALAEAAARIDAARLLLERAAARieaaAAAGKPVTPAlra 80
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|...
gi 4557231    354 -ASIAKAFAGDIANQLATDAVQILGGNGFNTEYPVEKLMRDAKIYQIYEGTSQ 405
Cdd:pfam08028  81 eARRAAAFATELAVAAVDALFRAAGGSALFQDSPLQRIWRDIHAAAQHAAVNP 133
AXO cd01150
Peroxisomal acyl-CoA oxidase; Peroxisomal acyl-CoA oxidases (AXO) catalyze the first set in ...
131-420 3.40e-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: 3.40e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557231  131 MPIIIA-GNDQQKKKYL-GRMTEEPLMCaYCVTEPGAGSDVAGIKTKA--EKKGDEYIIN-----GQKMWITNGGK-ANW 200
Cdd:cd01150 110 GNAIKNlGTDEHQDYWLqGANNLEIIGC-FAQTELGHGSNLQGLETTAtyDPLTQEFVINtpdftATKWWPGNLGKtATH 188
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557231  201 YFLLARSDPDPKapaNKAFTGFIV---EADT----PGIQIGRKELNMGQRCSDTRGIVFEDVKVPKENVL------IGDG 267
Cdd:cd01150 189 AVVFAQLITPGK---NHGLHAFIVpirDPKThqplPGVTVGDIGPKMGLNGVDNGFLQFRNVRIPRENLLnrfgdvSPDG 265
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557231  268 A----------GFKVAMGAFDKTRPVVAAGAVGLAQRALDEATKYALERKTFG--------KLLvEHQ------------ 317
Cdd:cd01150 266 TyvspfkdpnkRYGAMLGTRSGGRVGLIYDAAMSLKKAATIAIRYSAVRRQFGpkpsdpevQIL-DYQlqqyrlfpqlaa 344
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557231  318 --AISFMLAEMAMK-VELARMSYQRAAwevDSGRRNTYYASIAKAFAGDIANQLATDAVQILGGNGFNTEYPVEKLMRDA 394
Cdd:cd01150 345 ayAFHFAAKSLVEMyHEIIKELLQGNS---ELLAELHALSAGLKAVATWTAAQGIQECREACGGHGYLAMNRLPTLRDDN 421
                       330       340
                ....*....|....*....|....*.
gi 4557231  395 KIYQIYEGTSQIQRLIVAREHIDKYK 420
Cdd:cd01150 422 DPFCTYEGDNTVLLQQTANYLLKKYA 447
DszC cd01163
Dibenzothiophene (DBT) desulfurization enzyme C; DszC is a flavin reductase dependent enzyme, ...
48-395 2.19e-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: 71.20  E-value: 2.19e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557231   48 FQATARKFAREeiipvAAEYDKTGEYPVPLIRRAWELGLMNTHIPENCGGLGLGTFDACLISEELAygctgvqtAIEGNs 127
Cdd:cd01163   3 ARPLAARIAEG-----AAERDRQRGLPYEEVALLRQSGLGTLRVPKEYGGLGASLPDLYEVVRELA--------AADSN- 68
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557231  128 LGQMP---------IIIAGNDQQKKKYLGRMTEEPLM-CAycVTEPGaGSDVAGIKTKAEKKGDEYIINGQKmWITNGGK 197
Cdd:cd01163  69 IAQALrahfgfveaLLLAGPEQFRKRWFGRVLNGWIFgNA--VSERG-SVRPGTFLTATVRDGGGYVLNGKK-FYSTGAL 144
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557231  198 ANWYFLLARSDPDPKApankafTGFIVEADTPGIQIGRKELNMGQRCSDTRGIVFEDVKVPKENVLIGDGAGFKVAM-GA 276
Cdd:cd01163 145 FSDWVTVSALDEEGKL------VFAAVPTDRPGITVVDDWDGFGQRLTASGTVTFDNVRVEPDEVLPRPNAPDRGTLlTA 218
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557231  277 FDKTrpVVAAGAVGLAQRALDEATKYALER-KTFGKLLVEH--------QAIsfmlAEMAMKVELARMSYQRAAWEVD-- 345
Cdd:cd01163 219 IYQL--VLAAVLAGIARAALDDAVAYVRSRtRPWIHSGAESarddpyvqQVV----GDLAARLHAAEALVLQAARALDaa 292
                       330       340       350       360       370       380
                ....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557231  346 --SGRRNTYYASI--------AKAFAGDIANQLATDAVQILGGNGFNTEYPVEKLMRDAK 395
Cdd:cd01163 293 aaAGTALTAEARGeaalavaaAKVVVTRLALDATSRLFEVGGASATAREHNLDRHWRNAR 352
PRK11561 PRK11561
isovaleryl CoA dehydrogenase; Provisional
161-413 4.26e-13

isovaleryl CoA dehydrogenase; Provisional


Pssm-ID: 183199 [Multi-domain]  Cd Length: 538  Bit Score: 70.94  E-value: 4.26e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557231   161 TEPGAGSDVAGIKTKAEKKGDE-YIINGQKmwitnggkanWYFLLARSDPD-PKAPANKAFTGFIVEADTP-----GIQI 233
Cdd:PRK11561 185 TEKQGGSDVLSNTTRAERLADGsYRLVGHK----------WFFSVPQSDAHlVLAQAKGGLSCFFVPRFLPdgqrnAIRL 254
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557231   234 GRKELNMGQRCSDTRGIVFEDVK---VPKEnvliGDGAGFKVAMGAFdkTRPVVAAGAVGLAQRALDEATKYALERKTFG 310
Cdd:PRK11561 255 ERLKDKLGNRSNASSEVEFQDAIgwlLGEE----GEGIRLILKMGGM--TRFDCALGSHGLMRRAFSVAIYHAHQRQVFG 328
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557231   311 KLLVEHQAISFMLAEMAMKVE--------LARMSYQRA-AWEVDSGRRNTYYA--SIAKAFAGDIAnqlatDAVQILGGN 379
Cdd:PRK11561 329 KPLIEQPLMRQVLSRMALQLEgqtallfrLARAWDRRAdAKEALWARLFTPAAkfVICKRGIPFVA-----EAMEVLGGI 403
                        250       260       270
                 ....*....|....*....|....*....|....
gi 4557231   380 GFNTEYPVEKLMRDAKIYQIYEGTSQIQRLIVAR 413
Cdd:PRK11561 404 GYCEESELPRLYREMPVNSIWEGSGNIMCLDVLR 437
NcnH cd01159
Naphthocyclinone hydroxylase; Naphthocyclinone is an aromatic polyketide and an antibiotic, ...
175-394 5.36e-10

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


Pssm-ID: 173848 [Multi-domain]  Cd Length: 370  Bit Score: 60.44  E-value: 5.36e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557231  175 KAEKKGDEYIINGQKMWITNGGKANWYFLLARSDPDPKAPANKAFtgFIVEADtpgIQIGRKELNMGQRCSDTRGIVFED 254
Cdd:cd01159 112 RAERVDGGYRVSGTWPFASGCDHADWILVGAIVEDDDGGPLPRAF--VVPRAE---YEIVDTWHVVGLRGTGSNTVVVDD 186
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557231  255 VKVPKENVLIGDGA-----------GFKVAMGAFDKtrPVVAAGAVGLAQRALDEATKYALER---KTFGKLLVEHQAIS 320
Cdd:cd01159 187 VFVPEHRTLTAGDMmagdgpggstpVYRMPLRQVFP--LSFAAVSLGAAEGALAEFLELAGKRvrqYGAAVKMAEAPITQ 264
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557231  321 FMLAEMAMKVELARMSYQRAAWEVDS---------------GRRNTYYASIAKAFAGDIANQLAtdavqilGGNGFNTEY 385
Cdd:cd01159 265 LRLAEAAAELDAARAFLERATRDLWAhalaggpidveerarIRRDAAYAAKLSAEAVDRLFHAA-------GGSALYTAS 337

                ....*....
gi 4557231  386 PVEKLMRDA 394
Cdd:cd01159 338 PLQRIWRDI 346
PTZ00457 PTZ00457
acyl-CoA dehydrogenase; Provisional
86-298 6.97e-09

acyl-CoA dehydrogenase; Provisional


Pssm-ID: 185636 [Multi-domain]  Cd Length: 520  Bit Score: 57.58  E-value: 6.97e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557231    86 LMNTHIPENCGGLGLGTFDACLISEELAYGCTGVQTAIEGNSlGQMPIIIA--GNDQQKKKYLGRMTEEPLMCAYCVTEp 163
Cdd:PTZ00457  65 LYGARIATEYGGLGLGHTAHALIYEEVGTNCDSKLLSTIQHS-GFCTYLLStvGSKELKGKYLTAMSDGTIMMGWATEE- 142
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557231   164 GAGSDVAGIKTKAEKKGD-EYIINGQKMWItNGGKANWYFLLAR------SDPDPKAPANKAFtgFIVEADTPGIQIgrk 236
Cdd:PTZ00457 143 GCGSDISMNTTKASLTDDgSYVLTGQKRCE-FAASATHFLVLAKtltqtaAEEGATEVSRNSF--FICAKDAKGVSV--- 216
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 4557231   237 elnmgqrcsDTRGIVFEDvkVPKENVLIGDGAGFKVAMGAFDKTRPVVAAGAVGLAQRALDE 298
Cdd:PTZ00457 217 ---------NGDSVVFEN--TPAADVVGVVGEGFKDAMITLFTEQYLYAASLLGIMKRVVQE 267
PLN02636 PLN02636
acyl-coenzyme A oxidase
118-310 7.75e-09

acyl-coenzyme A oxidase


Pssm-ID: 215342 [Multi-domain]  Cd Length: 686  Bit Score: 57.56  E-value: 7.75e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557231   118 GVQTAIEGNSlgqmpIIIAGNDQQKKKYLGRMTEEPLMCAYCVTEPGAGSDVAGIKTKA--EKKGDEYIIN-----GQKM 190
Cdd:PLN02636 142 GVQYSLWGGS-----VINLGTKKHRDKYFDGIDNLDYPGCFAMTELHHGSNVQGLQTTAtfDPLTDEFVINtpndgAIKW 216
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557231   191 WITNG---GK-ANWYFLLARSDPDPKAPANKAFTGFIV-------EADTPGIQIGRKELNMGQRCSDTRGIVFEDVKVPK 259
Cdd:PLN02636 217 WIGNAavhGKfATVFARLKLPTHDSKGVSDMGVHAFIVpirdmktHQVLPGVEIRDCGHKVGLNGVDNGALRFRSVRIPR 296
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 4557231   260 ENVL--IGD--------------GAGFKVAMGAFDKTRPVVAAGAVGLAQRALDEATKYALERKTFG 310
Cdd:PLN02636 297 DNLLnrFGDvsrdgkytsslptiNKRFAATLGELVGGRVGLAYGSVGVLKASNTIAIRYSLLRQQFG 363
PLN02443 PLN02443
acyl-coenzyme A oxidase
137-310 2.76e-08

acyl-coenzyme A oxidase


Pssm-ID: 178062 [Multi-domain]  Cd Length: 664  Bit Score: 56.00  E-value: 2.76e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557231   137 GNDQQKKKYLGRMTEEPLMCAYCVTEPGAGSDVAGIKTKA--EKKGDEYIIN-----GQKMWITNGGKANWYFLL-ARSD 208
Cdd:PLN02443 114 GTEEQQKKWLPLAYKMQIIGCYAQTELGHGSNVQGLETTAtfDPKTDEFVIHsptltSSKWWPGGLGKVSTHAVVyARLI 193
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557231   209 PDPKapaNKAFTGFIVEADT-------PGI---QIGRKELNMGQRCSDTRGIVFEDVKVPKENVL------------IGD 266
Cdd:PLN02443 194 TNGK---DHGIHGFIVQLRSlddhsplPGVtvgDIGMKFGNGAYNTMDNGFLRFDHVRIPRDQMLmrlskvtregkyVQS 270
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....
gi 4557231   267 GAGFKVAMGAFDKTRPVVAAGAVGLAQRALDEATKYALERKTFG 310
Cdd:PLN02443 271 DVPRQLVYGTMVYVRQTIVADASTALSRAVCIATRYSAVRRQFG 314
PRK13026 PRK13026
acyl-CoA dehydrogenase; Reviewed
91-380 3.58e-08

acyl-CoA dehydrogenase; Reviewed


Pssm-ID: 237277 [Multi-domain]  Cd Length: 774  Bit Score: 55.73  E-value: 3.58e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557231    91 IPENCGGLGlgtFDA----CLISEELAYGCTGVQTAIEGNSLGQMPIIIA-GNDQQKKKYLGRM---TEEPlmCaYCVTE 162
Cdd:PRK13026 127 IPKEYGGKG---FSAyansTIVSKIATRSVSAAVTVMVPNSLGPGELLTHyGTQEQKDYWLPRLadgTEIP--C-FALTG 200
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557231   163 PGAGSDVA-----GIKTKAEKKGDEYI---INGQKMWITNGGKANWYFLLAR-SDPDP--KAPANKAFTGFIVEADTPGI 231
Cdd:PRK13026 201 PEAGSDAGaipdtGIVCRGEFEGEEVLglrLTWDKRYITLAPVATVLGLAFKlRDPDGllGDKKELGITCALIPTDHPGV 280
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557231   232 QIGRKELNMGQRCSD--TRGivfEDVKVPKEnVLIGD----GAGFKVAMGAFDKTRPV-VAAGAVGLAQRALDEATKYAL 304
Cdd:PRK13026 281 EIGRRHNPLGMAFMNgtTRG---KDVFIPLD-WIIGGpdyaGRGWRMLVECLSAGRGIsLPALGTASGHMATRTTGAYAY 356
                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 4557231   305 ERKTFGKLLVEHQAISFMLAEMAMK---VELARMSYQRAaweVDSGRRNTYYASIAKAFAGDIANQLATDAVQILGGNG 380
Cdd:PRK13026 357 VRRQFGMPIGQFEGVQEALARIAGNtylLEAARRLTTTG---LDLGVKPSVVTAIAKYHMTELARDVVNDAMDIHAGKG 432
PLN02312 PLN02312
acyl-CoA oxidase
137-309 1.14e-07

acyl-CoA oxidase


Pssm-ID: 215178 [Multi-domain]  Cd Length: 680  Bit Score: 54.01  E-value: 1.14e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557231   137 GNDQQKKKYLGRMTEEPLMCAYCVTEPGAGSDVAGIKTKA--EKKGDEYIIN-----GQKMWItnGGKAN---WYFLLAR 206
Cdd:PLN02312 168 GTKRHHDKWLKDTEDYVVKGCFAMTELGHGSNVRGIETVTtyDPKTEEFVINtpcesAQKYWI--GGAANhatHTIVFSQ 245
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557231   207 SDPDPKAPANKAFTGFIVEAD---TPGIQIGRKELNMGQRCSDTRGIVFEDVKVPKENVL------IGDG---------- 267
Cdd:PLN02312 246 LHINGKNEGVHAFIAQIRDQDgniCPNIRIADCGHKIGLNGVDNGRIWFDNLRIPRENLLnsvadvSPDGkyvsaikdpd 325
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|..
gi 4557231   268 AGFKVAMGAFDKTRPVVAAGAVGLAQRALDEATKYALERKTF 309
Cdd:PLN02312 326 QRFGAFLAPLTSGRVTIAVSAIYSSKVGLAIAIRYSLSRRAF 367
fadE PRK09463
acyl-CoA dehydrogenase; Reviewed
137-380 1.33e-07

acyl-CoA dehydrogenase; Reviewed


Pssm-ID: 236528 [Multi-domain]  Cd Length: 777  Bit Score: 53.67  E-value: 1.33e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557231   137 GNDQQKKKYLGRM---TEEPlmCaYCVTEPGAGSDVA-----GIKTKAEKKGDEYI---INGQKMWITNG------GKAn 199
Cdd:PRK09463 176 GTDEQKDHYLPRLargEEIP--C-FALTSPEAGSDAGsipdtGVVCKGEWQGEEVLgmrLTWNKRYITLApiatvlGLA- 251
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557231   200 wyFLLarSDPDpkapankaftGFI------------VEADTPGIQIGRKELNMGQRCSD--TRGivfEDVKVPKENVlIG 265
Cdd:PRK09463 252 --FKL--YDPD----------GLLgdkedlgitcalIPTDTPGVEIGRRHFPLNVPFQNgpTRG---KDVFIPLDYI-IG 313
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557231   266 D----GAGFKVAMGAFDKTR----PVVAAGAVGLAQRAldeATKYALERKTFGKLLVEHQAISFMLAEMAMKvelarmsy 337
Cdd:PRK09463 314 GpkmaGQGWRMLMECLSVGRgislPSNSTGGAKLAALA---TGAYARIRRQFKLPIGKFEGIEEPLARIAGN-------- 382
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....
gi 4557231   338 qraAWEVDSGRRNTYYA-----------SIAKAFAGDIANQLATDAVQILGGNG 380
Cdd:PRK09463 383 ---AYLMDAARTLTTAAvdlgekpsvlsAIAKYHLTERGRQVINDAMDIHGGKG 433
PTZ00460 PTZ00460
acyl-CoA dehydrogenase; Provisional
137-309 9.97e-06

acyl-CoA dehydrogenase; Provisional


Pssm-ID: 185639 [Multi-domain]  Cd Length: 646  Bit Score: 47.92  E-value: 9.97e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557231   137 GNDQQKKKYLGRMTEEPLMCAYCVTEPGAGSDVAGIKTKA--EKKGDEYIIN-----GQKMWITN-GGKANWYFLLARSD 208
Cdd:PTZ00460 110 GTDEQINLWMPSLLNFEIVGCYAQTELGHGSDVQNLETTAtyDKQTNEFVIHtpsveAVKFWPGElGFLCNFALVYAKLI 189
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557231   209 PDPKAPANKAFTGFIVEADT----PGIQIGRKELNMGQRCSDTRGIVFEDVKVPKENVL-----IGDGAGF------KVA 273
Cdd:PTZ00460 190 VNGKNKGVHPFMVRIRDKEThkplQGVEVGDIGPKMGYAVKDNGFLSFDHYRIPLDSLLaryikVSEDGQVerqgnpKVS 269
                        170       180       190
                 ....*....|....*....|....*....|....*.
gi 4557231   274 MGAFDKTRPVVAAGAVGLAQRALDEATKYALERKTF 309
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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