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Conserved domains on  [gi|557006922|ref|XP_006004877|]
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medium-chain specific acyl-CoA dehydrogenase, mitochondrial isoform X1 [Latimeria chalumnae]

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 ...
 42-418 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: 758.27  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557006922  42 LTDQQKEFQATARKFAREEIIPVAAHYDRTGEYPVPIIRRVWELGLMNGHIPESCGGLGLGIFDTCLTSEELAYGCTGIQ 121
Cdd:cd01157    1 LTEQQKEFQETARKFAREEIIPVAAEYDKSGEYPWPLIKRAWELGLMNTHIPEDCGGLGLGTFDTCLITEELAYGCTGVQ 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557006922 122 TAIEANSLGQMPVIIAGNEQQKKKYLGRLMEEPLMCAYCVTEPGAGSDVAGIKTRAEKKGDEYIINGQKMWITNGGKANW 201
Cdd:cd01157   81 TAIEANSLGQMPVIISGNDEQKKKYLGRMTEEPLMCAYCVTEPGAGSDVAGIKTKAEKKGDEYIINGQKMWITNGGKANW 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557006922 202 YFVLTRTNPDPKAPPSGAFTGFIVDGDTPGIQIGRKELNMGQRCSDTRGIVFEDVRVPKENVLIAEGAGFKVAMGAFDKT 281
Cdd:cd01157  161 YFLLARSDPDPKCPASKAFTGFIVEADTPGIQPGRKELNMGQRCSDTRGITFEDVRVPKENVLIGEGAGFKIAMGAFDKT 240

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557006922 282 RPPVAAAATGLAQRALDEAVKYAMERKTFGRLIVEHQAVSFMLAEMAMKTVLARMAYQRSAWEVDEGRKNTFFASVAKAF 361
Cdd:cd01157  241 RPPVAAGAVGLAQRALDEATKYALERKTFGKLIAEHQAVSFMLADMAMKVELARLAYQRAAWEVDSGRRNTYYASIAKAF 320

                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 557006922 362 AGDIANQVASDAVQIFGGNGYNSEYPVEKLMRDAKIYQIYEGTAQIQRMIIVRELLG 418
Cdd:cd01157  321 AADIANQLATDAVQIFGGNGFNSEYPVEKLMRDAKIYQIYEGTSQIQRLIISREHLG 377
 
Name Accession Description Interval E-value
MCAD cd01157
Medium chain acyl-CoA dehydrogenase; MCADs are mitochondrial beta-oxidation enzymes, which ...
 42-418 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: 758.27  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557006922  42 LTDQQKEFQATARKFAREEIIPVAAHYDRTGEYPVPIIRRVWELGLMNGHIPESCGGLGLGIFDTCLTSEELAYGCTGIQ 121
Cdd:cd01157    1 LTEQQKEFQETARKFAREEIIPVAAEYDKSGEYPWPLIKRAWELGLMNTHIPEDCGGLGLGTFDTCLITEELAYGCTGVQ 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557006922 122 TAIEANSLGQMPVIIAGNEQQKKKYLGRLMEEPLMCAYCVTEPGAGSDVAGIKTRAEKKGDEYIINGQKMWITNGGKANW 201
Cdd:cd01157   81 TAIEANSLGQMPVIISGNDEQKKKYLGRMTEEPLMCAYCVTEPGAGSDVAGIKTKAEKKGDEYIINGQKMWITNGGKANW 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557006922 202 YFVLTRTNPDPKAPPSGAFTGFIVDGDTPGIQIGRKELNMGQRCSDTRGIVFEDVRVPKENVLIAEGAGFKVAMGAFDKT 281
Cdd:cd01157  161 YFLLARSDPDPKCPASKAFTGFIVEADTPGIQPGRKELNMGQRCSDTRGITFEDVRVPKENVLIGEGAGFKIAMGAFDKT 240

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557006922 282 RPPVAAAATGLAQRALDEAVKYAMERKTFGRLIVEHQAVSFMLAEMAMKTVLARMAYQRSAWEVDEGRKNTFFASVAKAF 361
Cdd:cd01157  241 RPPVAAGAVGLAQRALDEATKYALERKTFGKLIAEHQAVSFMLADMAMKVELARLAYQRAAWEVDSGRRNTYYASIAKAF 320

                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 557006922 362 AGDIANQVASDAVQIFGGNGYNSEYPVEKLMRDAKIYQIYEGTAQIQRMIIVRELLG 418
Cdd:cd01157  321 AADIANQLATDAVQIFGGNGFNSEYPVEKLMRDAKIYQIYEGTSQIQRLIISREHLG 377
CaiA COG1960
Acyl-CoA dehydrogenase related to the alkylation response protein AidB [Lipid transport and ...
 40-421 2.93e-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: 456.22  E-value: 2.93e-160
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557006922  40 FNLTDQQKEFQATARKFAREEIIPVAAHYDRTGEYPVPIIRRVWELGLMNGHIPESCGGLGLGIFDTCLTSEELAYGCTG 119
Cdd:COG1960    3 FELTEEQRALRDEVREFAEEEIAPEAREWDREGEFPRELWRKLAELGLLGLTIPEEYGGLGLSLVELALVLEELARADAS 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557006922 120 IQTAIEANSLGQMPVIIAGNEQQKKKYLGRLMEEPLMCAYCVTEPGAGSDVAGIKTRAEKKGDEYIINGQKMWITNGGKA 199
Cdd:COG1960   83 LALPVGVHNGAAEALLRFGTEEQKERYLPRLASGEWIGAFALTEPGAGSDAAALRTTAVRDGDGYVLNGQKTFITNAPVA 162

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557006922 200 NWYFVLTRTNPDPKAppsGAFTGFIVDGDTPGIQIGRKELNMGQRCSDTRGIVFEDVRVPKENVLIAEGAGFKVAMGAFD 279
Cdd:COG1960  163 DVILVLARTDPAAGH---RGISLFLVPKDTPGVTVGRIEDKMGLRGSDTGELFFDDVRVPAENLLGEEGKGFKIAMSTLN 239

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557006922 280 KTRPPVAAAATGLAQRALDEAVKYAMERKTFGRLIVEHQAVSFMLAEMAMKTVLARMAYQRSAWEVDEGRKNTFFASVAK 359
Cdd:COG1960  240 AGRLGLAAQALGIAEAALELAVAYAREREQFGRPIADFQAVQHRLADMAAELEAARALVYRAAWLLDAGEDAALEAAMAK 319

                        330       340       350       360       370       380
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 557006922 360 AFAGDIANQVASDAVQIFGGNGYNSEYPVEKLMRDAKIYQIYEGTAQIQRMIIVRELLGTYK 421
Cdd:COG1960  320 LFATEAALEVADEALQIHGGYGYTREYPLERLYRDARILTIYEGTNEIQRLIIARRLLGRPG 381
PLN02519 PLN02519
isovaleryl-CoA dehydrogenase
 35-416 1.09e-82

isovaleryl-CoA dehydrogenase


Pssm-ID: 215284 [Multi-domain]  Cd Length: 404  Bit Score: 259.42  E-value: 1.09e-82
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557006922  35 GYGFSFNLTDQQKEFQATARKFAREEIIPVAAHYDRTGEYP--VPIIRRVWELGLMNGHIPESCGGLGLGIFDTCLTSEE 112
Cdd:PLN02519  19 SSSSSLLFDDTQLQFKESVQQFAQENIAPHAAAIDATNSFPkdVNLWKLMGDFNLHGITAPEEYGGLGLGYLYHCIAMEE 98

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557006922 113 L--AYGCTGIQTAIEANsLGQMPVIIAGNEQQKKKYLGRLMEEPLMCAYCVTEPGAGSDVAGIKTRAEKKGDEYIINGQK 190
Cdd:PLN02519  99 IsrASGSVGLSYGAHSN-LCINQLVRNGTPAQKEKYLPKLISGEHVGALAMSEPNSGSDVVSMKCKAERVDGGYVLNGNK 177

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557006922 191 MWITNGGKANWYFVLTRTnpDPKAPPSGaFTGFIVDGDTPGIQIGRKELNMGQRCSDTRGIVFEDVRVPKENVLIAEGAG 270
Cdd:PLN02519 178 MWCTNGPVAQTLVVYAKT--DVAAGSKG-ITAFIIEKGMPGFSTAQKLDKLGMRGSDTCELVFENCFVPEENVLGQEGKG 254

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557006922 271 FKVAMGAFDKTRPPVAAAATGLAQRALDEAVKYAMERKTFGRLIVEHQAVSFMLAEMAMKTVLARMAYQRSAWEVDEGRK 350
Cdd:PLN02519 255 VYVMMSGLDLERLVLAAGPLGLMQACLDVVLPYVRQREQFGRPIGEFQFIQGKLADMYTSLQSSRSYVYSVARDCDNGKV 334

                        330       340       350       360       370       380
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 557006922 351 NTFFASVAKAFAGDIANQVASDAVQIFGGNGYNSEYPVEKLMRDAKIYQIYEGTAQIQRMIIVREL 416
Cdd:PLN02519 335 DRKDCAGVILCAAERATQVALQAIQCLGGNGYINEYPTGRLLRDAKLYEIGAGTSEIRRMLIGREL 400
Acyl-CoA_dh_1 pfam00441
Acyl-CoA dehydrogenase, C-terminal domain; C-terminal domain of Acyl-CoA dehydrogenase is an ...
 268-416 3.73e-51

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: 168.97  E-value: 3.73e-51
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557006922  268 GAGFKVAMGAFDKTRPPVAAAATGLAQRALDEAVKYAMERKTFGRLIVEHQAVSFMLAEMAMKTVLARMAYQRSAWEVDE 347
Cdd:pfam00441   1 GRGFRVAMETLNHERLAIAAMALGLARRALDEALAYARRRKAFGRPLIDFQLVRHKLAEMAAEIEAARLLVYRAAEALDA 80

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 557006922  348 GRKNTFFASVAKAFAGDIANQVASDAVQIFGGNGYNSEYPVEKLMRDAKIYQIYEGTAQIQRMIIVREL 416
Cdd:pfam00441  81 GGPDGAEASMAKLYASEAAVEVADLAMQLHGGYGYLREYPVERLYRDARVLRIGEGTSEIQRNIIARRL 149
 
Name Accession Description Interval E-value
MCAD cd01157
Medium chain acyl-CoA dehydrogenase; MCADs are mitochondrial beta-oxidation enzymes, which ...
 42-418 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: 758.27  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557006922  42 LTDQQKEFQATARKFAREEIIPVAAHYDRTGEYPVPIIRRVWELGLMNGHIPESCGGLGLGIFDTCLTSEELAYGCTGIQ 121
Cdd:cd01157    1 LTEQQKEFQETARKFAREEIIPVAAEYDKSGEYPWPLIKRAWELGLMNTHIPEDCGGLGLGTFDTCLITEELAYGCTGVQ 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557006922 122 TAIEANSLGQMPVIIAGNEQQKKKYLGRLMEEPLMCAYCVTEPGAGSDVAGIKTRAEKKGDEYIINGQKMWITNGGKANW 201
Cdd:cd01157   81 TAIEANSLGQMPVIISGNDEQKKKYLGRMTEEPLMCAYCVTEPGAGSDVAGIKTKAEKKGDEYIINGQKMWITNGGKANW 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557006922 202 YFVLTRTNPDPKAPPSGAFTGFIVDGDTPGIQIGRKELNMGQRCSDTRGIVFEDVRVPKENVLIAEGAGFKVAMGAFDKT 281
Cdd:cd01157  161 YFLLARSDPDPKCPASKAFTGFIVEADTPGIQPGRKELNMGQRCSDTRGITFEDVRVPKENVLIGEGAGFKIAMGAFDKT 240

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557006922 282 RPPVAAAATGLAQRALDEAVKYAMERKTFGRLIVEHQAVSFMLAEMAMKTVLARMAYQRSAWEVDEGRKNTFFASVAKAF 361
Cdd:cd01157  241 RPPVAAGAVGLAQRALDEATKYALERKTFGKLIAEHQAVSFMLADMAMKVELARLAYQRAAWEVDSGRRNTYYASIAKAF 320

                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 557006922 362 AGDIANQVASDAVQIFGGNGYNSEYPVEKLMRDAKIYQIYEGTAQIQRMIIVRELLG 418
Cdd:cd01157  321 AADIANQLATDAVQIFGGNGFNSEYPVEKLMRDAKIYQIYEGTSQIQRLIISREHLG 377
CaiA COG1960
Acyl-CoA dehydrogenase related to the alkylation response protein AidB [Lipid transport and ...
 40-421 2.93e-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: 456.22  E-value: 2.93e-160
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557006922  40 FNLTDQQKEFQATARKFAREEIIPVAAHYDRTGEYPVPIIRRVWELGLMNGHIPESCGGLGLGIFDTCLTSEELAYGCTG 119
Cdd:COG1960    3 FELTEEQRALRDEVREFAEEEIAPEAREWDREGEFPRELWRKLAELGLLGLTIPEEYGGLGLSLVELALVLEELARADAS 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557006922 120 IQTAIEANSLGQMPVIIAGNEQQKKKYLGRLMEEPLMCAYCVTEPGAGSDVAGIKTRAEKKGDEYIINGQKMWITNGGKA 199
Cdd:COG1960   83 LALPVGVHNGAAEALLRFGTEEQKERYLPRLASGEWIGAFALTEPGAGSDAAALRTTAVRDGDGYVLNGQKTFITNAPVA 162

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557006922 200 NWYFVLTRTNPDPKAppsGAFTGFIVDGDTPGIQIGRKELNMGQRCSDTRGIVFEDVRVPKENVLIAEGAGFKVAMGAFD 279
Cdd:COG1960  163 DVILVLARTDPAAGH---RGISLFLVPKDTPGVTVGRIEDKMGLRGSDTGELFFDDVRVPAENLLGEEGKGFKIAMSTLN 239

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557006922 280 KTRPPVAAAATGLAQRALDEAVKYAMERKTFGRLIVEHQAVSFMLAEMAMKTVLARMAYQRSAWEVDEGRKNTFFASVAK 359
Cdd:COG1960  240 AGRLGLAAQALGIAEAALELAVAYAREREQFGRPIADFQAVQHRLADMAAELEAARALVYRAAWLLDAGEDAALEAAMAK 319

                        330       340       350       360       370       380
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 557006922 360 AFAGDIANQVASDAVQIFGGNGYNSEYPVEKLMRDAKIYQIYEGTAQIQRMIIVRELLGTYK 421
Cdd:COG1960  320 LFATEAALEVADEALQIHGGYGYTREYPLERLYRDARILTIYEGTNEIQRLIIARRLLGRPG 381
SCAD_SBCAD cd01158
Short chain acyl-CoA dehydrogenases and eukaryotic short/branched chain acyl-CoA ...
 44-418 1.70e-147

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: 423.60  E-value: 1.70e-147
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557006922  44 DQQKEFQATARKFAREEIIPVAAHYDRTGEYPVPIIRRVWELGLMNGHIPESCGGLGLGIFDTCLTSEELAYGCTGIQTA 123
Cdd:cd01158    1 EEHQMIRKTVRDFAEKEIAPLAAEMDEKGEFPREVIKEMAELGLMGIPIPEEYGGAGLDFLAYAIAIEELAKVDASVAVI 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557006922 124 IEA-NSLGQMPVIIAGNEQQKKKYLGRLMEEPLMCAYCVTEPGAGSDVAGIKTRAEKKGDEYIINGQKMWITNGGKANWY 202
Cdd:cd01158   81 VSVhNSLGANPIIKFGTEEQKKKYLPPLATGEKIGAFALSEPGAGSDAAALKTTAKKDGDDYVLNGSKMWITNGGEADFY 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557006922 203 FVLTRTNPDPKAPpsgAFTGFIVDGDTPGIQIGRKELNMGQRCSDTRGIVFEDVRVPKENVLIAEGAGFKVAMGAFDKTR 282
Cdd:cd01158  161 IVFAVTDPSKGYR---GITAFIVERDTPGLSVGKKEDKLGIRGSSTTELIFEDVRVPKENILGEEGEGFKIAMQTLDGGR 237

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557006922 283 PPVAAAATGLAQRALDEAVKYAMERKTFGRLIVEHQAVSFMLAEMAMKTVLARMAYQRSAWEVDEGRKNTFFASVAKAFA 362
Cdd:cd01158  238 IGIAAQALGIAQAALDAAVDYAKERKQFGKPIADFQGIQFKLADMATEIEAARLLTYKAARLKDNGEPFIKEAAMAKLFA 317

                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 557006922 363 GDIANQVASDAVQIFGGNGYNSEYPVEKLMRDAKIYQIYEGTAQIQRMIIVRELLG 418
Cdd:cd01158  318 SEVAMRVTTDAVQIFGGYGYTKDYPVERYYRDAKITEIYEGTSEIQRLVIAKHLLK 373
ACAD cd00567
Acyl-CoA dehydrogenase; Both mitochondrial acyl-CoA dehydrogenases (ACAD) and peroxisomal ...
 44-414 1.34e-130

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: 378.94  E-value: 1.34e-130
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557006922  44 DQQKEFQATARKFAREEIIPVAAHYDRTGEYPVPIIRRVWELGlmnghipescgglglgifdtcltseelaygctgiqta 123
Cdd:cd00567    1 EEQRELRDSAREFAAEELEPYARERRETPEEPWELLAELGLLL------------------------------------- 43

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557006922 124 ieanslGQMPVIIAGNEQQKKKYLGRLMEEPLMCAYCVTEPGAGSDVAGIKTRAEKKGDEYIINGQKMWITNGGKANWYF 203
Cdd:cd00567   44 ------GAALLLAYGTEEQKERYLPPLASGEAIAAFALTEPGAGSDLAGIRTTARKDGDGYVLNGRKIFISNGGDADLFI 117

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557006922 204 VLTRTnpDPKAPPSGAFTGFIVDGDTPGIQIGRKELNMGQRCSDTRGIVFEDVRVPKENVLIAEGAGFKVAMGAFDKTRP 283
Cdd:cd00567  118 VLART--DEEGPGHRGISAFLVPADTPGVTVGRIWDKMGMRGSGTGELVFDDVRVPEDNLLGEEGGGFELAMKGLNVGRL 195

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557006922 284 PVAAAATGLAQRALDEAVKYAMERKTFGRLIVEHQAVSFMLAEMAMKTVLARMAYQRSAWEVDEGRKN-TFFASVAKAFA 362
Cdd:cd00567  196 LLAAVALGAARAALDEAVEYAKQRKQFGKPLAEFQAVQFKLADMAAELEAARLLLYRAAWLLDQGPDEaRLEAAMAKLFA 275

                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|..
gi 557006922 363 GDIANQVASDAVQIFGGNGYNSEYPVEKLMRDAKIYQIYEGTAQIQRMIIVR 414
Cdd:cd00567  276 TEAAREVADLAMQIHGGRGYSREYPVERYLRDARAARIAEGTAEIQRLIIAR 327
IBD cd01162
Isobutyryl-CoA dehydrogenase; Isobutyryl-CoA dehydrogenase (IBD) catalyzes the alpha, beta- ...
 42-418 1.99e-110

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: 329.40  E-value: 1.99e-110
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557006922  42 LTDQQKEFQATARKFAREEIIPVAAHYDRTGEYPVPIIRRVWELGLMNGHIPESCGGLGLGIFDTCLTSEELAYGCTGIQ 121
Cdd:cd01162    1 LNEEQRAIQEVARAFAAKEMAPHAADWDQKKHFPVDVLRKAAELGFGGIYIRDDVGGSGLSRLDASIIFEALSTGCVSTA 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557006922 122 TAIEANSLGQMPVIIAGNEQQKKKYLGRLMEEPLMCAYCVTEPGAGSDVAGIKTRAEKKGDEYIINGQKMWITNGGKANW 201
Cdd:cd01162   81 AYISIHNMCAWMIDSFGNDEQRERFLPDLCTMEKLASYCLTEPGSGSDAAALRTRAVREGDHYVLNGSKAFISGAGDSDV 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557006922 202 YFVLTRTNPDPkapPSGAFTgFIVDGDTPGIQIGRKELNMGQRCSDTRGIVFEDVRVPKENVLIAEGAGFKVAMGAFDKT 281
Cdd:cd01162  161 YVVMARTGGEG---PKGISC-FVVEKGTPGLSFGANEKKMGWNAQPTRAVIFEDCRVPVENRLGGEGQGFGIAMAGLNGG 236

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557006922 282 RPPVAAAATGLAQRALDEAVKYAMERKTFGRLIVEHQAVSFMLAEMAMKTVLARMAYQRSAWEVDEGRKN-TFFASVAKA 360
Cdd:cd01162  237 RLNIASCSLGAAQAALDLARAYLEERKQFGKPLADFQALQFKLADMATELVASRLMVRRAASALDRGDPDaVKLCAMAKR 316

                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 557006922 361 FAGDIANQVASDAVQIFGGNGYNSEYPVEKLMRDAKIYQIYEGTAQIQRMIIVRELLG 418
Cdd:cd01162  317 FATDECFDVANQALQLHGGYGYLKDYPVEQYVRDLRVHQILEGTNEIMRLIIARALLT 374
IVD cd01156
Isovaleryl-CoA dehydrogenase; Isovaleryl-CoA dehydrogenase (IVD) is an is an acyl-CoA ...
 42-416 6.94e-109

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: 325.52  E-value: 6.94e-109
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557006922  42 LTDQQKEFQATARKFAREEIIPVAAHYDRTGEYPVPIIRRVWELGLMNGHIPESCGGLGLGIFDTCLTSEELAYGCTGIQ 121
Cdd:cd01156    2 LDDEIEMLRQSVREFAQKEIAPLAAKIDRDNEFPRDLWRKMGKLGLLGITAPEEYGGSGMGYLAHVIIMEEISRASGSVA 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557006922 122 TAIEANS---LGQMpvIIAGNEQQKKKYLGRLMEEPLMCAYCVTEPGAGSDVAGIKTRAEKKGDEYIINGQKMWITNGGK 198
Cdd:cd01156   82 LSYGAHSnlcINQI--YRNGSAAQKEKYLPKLISGEHIGALAMSEPNAGSDVVSMKLRAEKKGDRYVLNGSKMWITNGPD 159

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557006922 199 ANWYFVLTRTNPDPKAPpsgAFTGFIVDGDTPGIQIGRKELNMGQRCSDTRGIVFEDVRVPKENVLIAEGAGFKVAMGAF 278
Cdd:cd01156  160 ADTLVVYAKTDPSAGAH---GITAFIVEKGMPGFSRAQKLDKLGMRGSNTCELVFEDCEVPEENILGGENKGVYVLMSGL 236

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557006922 279 DKTRPPVAAAATGLAQRALDEAVKYAMERKTFGRLIVEHQAVSFMLAEMAMKTVLARMAYQRSAWEVDEGRKNTFFASVA 358
Cdd:cd01156  237 DYERLVLAGGPIGIMQAALDVAIPYAHQRKQFGQPIGEFQLVQGKLADMYTRLNASRSYLYTVAKACDRGNMDPKDAAGV 316

                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 557006922 359 KAFAGDIANQVASDAVQIFGGNGYNSEYPVEKLMRDAKIYQIYEGTAQIQRMIIVREL 416
Cdd:cd01156  317 ILYAAEKATQVALDAIQILGGNGYINDYPTGRLLRDAKLYEIGAGTSEIRRMVIGREL 374
LCAD cd01160
Long chain acyl-CoA dehydrogenase; LCAD is an acyl-CoA dehydrogenases (ACAD), which is found ...
 49-417 3.19e-105

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: 315.98  E-value: 3.19e-105
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557006922  49 FQATARKFAREEIIPVAAHYDRTGEYPVPIIRRVWELGLMNGHIPESCGGLGLGIFDTCLTSEELAY-GCTGIQTAIEaN 127
Cdd:cd01160    6 FRDVVRRFFAKEVAPFHHEWEKAGEVPREVWRKAGEQGLLGVGFPEEYGGIGGDLLSAAVLWEELARaGGSGPGLSLH-T 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557006922 128 SLGQMPVIIAGNEQQKKKYLGRLMEEPLMCAYCVTEPGAGSDVAGIKTRAEKKGDEYIINGQKMWITNGGKANWYFVLTR 207
Cdd:cd01160   85 DIVSPYITRAGSPEQKERVLPQMVAGKKIGAIAMTEPGAGSDLQGIRTTARKDGDHYVLNGSKTFITNGMLADVVIVVAR 164

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557006922 208 TNPDpkAPPSGAFTGFIVDGDTPGIQIGRKELNMGQRCSDTRGIVFEDVRVPKENVLIAEGAGFKVAMGAFDKTRPPVAA 287
Cdd:cd01160  165 TGGE--ARGAGGISLFLVERGTPGFSRGRKLKKMGWKAQDTAELFFDDCRVPAENLLGEENKGFYYLMQNLPQERLLIAA 242

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557006922 288 AATGLAQRALDEAVKYAMERKTFGRLIVEHQAVSFMLAEMAMKTVLARMAYQRSAWEVDEGRKNTFFASVAKAFAGDIAN 367
Cdd:cd01160  243 GALAAAEFMLEETRNYVKQRKAFGKTLAQLQVVRHKIAELATKVAVTRAFLDNCAWRHEQGRLDVAEASMAKYWATELQN 322

                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|
gi 557006922 368 QVASDAVQIFGGNGYNSEYPVEKLMRDAKIYQIYEGTAQIQRMIIVRELL 417
Cdd:cd01160  323 RVAYECVQLHGGWGYMREYPIARAYRDARVQPIYGGTTEIMKELISRQMV 372
VLCAD cd01161
Very long chain acyl-CoA dehydrogenase; VLCAD is an acyl-CoA dehydrogenase (ACAD), which is ...
 38-412 3.22e-91

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: 281.28  E-value: 3.22e-91
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557006922  38 FSFNLTDQQKEFQ----ATARKFAREEIIPvaAHYDRTGEYPVPIIRRVWELGLMNGHIPESCGGLGLGIFDTCLTSEEL 113
Cdd:cd01161   19 YPSVLTEEQTEELnmlvGPVEKFFEEVNDP--AKNDQLEKIPRKTLTQLKELGLFGLQVPEEYGGLGLNNTQYARLAEIV 96

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557006922 114 AYGcTGIQTAIEAN-SLGQMPVIIAGNEQQKKKYLGRLMEEPLMCAYCVTEPGAGSDVAGIKTRAEKK--GDEYIINGQK 190
Cdd:cd01161   97 GMD-LGFSVTLGAHqSIGFKGILLFGTEAQKEKYLPKLASGEWIAAFALTEPSSGSDAASIRTTAVLSedGKHYVLNGSK 175

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557006922 191 MWITNGGKANWYFVLTRTN-PDPKAPPSGAFTGFIVDGDTPGIQIGRKELNMGQRCSDTRGIVFEDVRVPKENVLIAEGA 269
Cdd:cd01161  176 IWITNGGIADIFTVFAKTEvKDATGSVKDKITAFIVERSFGGVTNGPPEKKMGIKGSNTAEVYFEDVKIPVENVLGEVGD 255

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557006922 270 GFKVAMGAFDKTRPPVAAAATGLAQRALDEAVKYAMERKTFGRLIVEHQAVSFMLAEMAMKT-VLARMAYQRSAwEVDEG 348
Cdd:cd01161  256 GFKVAMNILNNGRFGMGAALIGTMKRCIEKAVDYANNRKQFGKKIHEFGLIQEKLANMAILQyATESMAYMTSG-NMDRG 334

                        330       340       350       360       370       380
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 557006922 349 RKNTFF--ASVAKAFAGDIANQVASDAVQIFGGNGYNSEYPVEKLMRDAKIYQIYEGTAQIQRMII 412
Cdd:cd01161  335 LKAEYQieAAISKVFASEAAWLVVDEAIQIHGGMGFMREYGVERVLRDLRIFRIFEGTNEILRLFI 400
PLN02519 PLN02519
isovaleryl-CoA dehydrogenase
 35-416 1.09e-82

isovaleryl-CoA dehydrogenase


Pssm-ID: 215284 [Multi-domain]  Cd Length: 404  Bit Score: 259.42  E-value: 1.09e-82
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557006922  35 GYGFSFNLTDQQKEFQATARKFAREEIIPVAAHYDRTGEYP--VPIIRRVWELGLMNGHIPESCGGLGLGIFDTCLTSEE 112
Cdd:PLN02519  19 SSSSSLLFDDTQLQFKESVQQFAQENIAPHAAAIDATNSFPkdVNLWKLMGDFNLHGITAPEEYGGLGLGYLYHCIAMEE 98

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557006922 113 L--AYGCTGIQTAIEANsLGQMPVIIAGNEQQKKKYLGRLMEEPLMCAYCVTEPGAGSDVAGIKTRAEKKGDEYIINGQK 190
Cdd:PLN02519  99 IsrASGSVGLSYGAHSN-LCINQLVRNGTPAQKEKYLPKLISGEHVGALAMSEPNSGSDVVSMKCKAERVDGGYVLNGNK 177

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557006922 191 MWITNGGKANWYFVLTRTnpDPKAPPSGaFTGFIVDGDTPGIQIGRKELNMGQRCSDTRGIVFEDVRVPKENVLIAEGAG 270
Cdd:PLN02519 178 MWCTNGPVAQTLVVYAKT--DVAAGSKG-ITAFIIEKGMPGFSTAQKLDKLGMRGSDTCELVFENCFVPEENVLGQEGKG 254

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557006922 271 FKVAMGAFDKTRPPVAAAATGLAQRALDEAVKYAMERKTFGRLIVEHQAVSFMLAEMAMKTVLARMAYQRSAWEVDEGRK 350
Cdd:PLN02519 255 VYVMMSGLDLERLVLAAGPLGLMQACLDVVLPYVRQREQFGRPIGEFQFIQGKLADMYTSLQSSRSYVYSVARDCDNGKV 334

                        330       340       350       360       370       380
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 557006922 351 NTFFASVAKAFAGDIANQVASDAVQIFGGNGYNSEYPVEKLMRDAKIYQIYEGTAQIQRMIIVREL 416
Cdd:PLN02519 335 DRKDCAGVILCAAERATQVALQAIQCLGGNGYINEYPTGRLLRDAKLYEIGAGTSEIRRMLIGREL 400
GCD cd01151
Glutaryl-CoA dehydrogenase; Glutaryl-CoA dehydrogenase (GCD). GCD is an acyl-CoA dehydrogenase, ...
 33-418 3.49e-71

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: 229.17  E-value: 3.49e-71
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557006922  33 QDGYGFSFNLTDQQKEFQATARKFAREEIIPVAAHYDRTGEYPVPIIRRVWELGLMnGHIPESCGGLGLGIFDTCLTSEE 112
Cdd:cd01151    4 EDPLNLDDLLTEEERAIRDTAREFCQEELAPRVLEAYREEKFDRKIIEEMGELGLL-GATIKGYGCAGLSSVAYGLIARE 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557006922 113 LAYGCTGIQTAIEA-NSLGQMPVIIAGNEQQKKKYLGRLMEEPLMCAYCVTEPGAGSDVAGIKTRAEKKGDEYIINGQKM 191
Cdd:cd01151   83 VERVDSGYRSFMSVqSSLVMLPIYDFGSEEQKQKYLPKLASGELIGCFGLTEPNHGSDPGGMETRARKDGGGYKLNGSKT 162

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557006922 192 WITNGGKANWYFVLTRTNPDpkappsGAFTGFIVDGDTPGIQIGRKELNMGQRCSDTRGIVFEDVRVPKENVLiAEGAGF 271
Cdd:cd01151  163 WITNSPIADVFVVWARNDET------GKIRGFILERGMKGLSAPKIQGKFSLRASITGEIVMDNVFVPEENLL-PGAEGL 235

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557006922 272 KVAMGAFDKTRPPVAAAATGLAQRALDEAVKYAMERKTFGRLIVEHQAVSFMLAEMAMKTVLARMAYQRSAWEVDEGRKN 351
Cdd:cd01151  236 RGPFKCLNNARYGIAWGALGAAEDCYHTARQYVLDRKQFGRPLAAFQLVQKKLADMLTEIALGLLACLRVGRLKDQGKAT 315

                        330       340       350       360       370       380
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 557006922 352 TFFASVAKAFAGDIANQVASDAVQIFGGNGYNSEYPVEKLMRDAKIYQIYEGTAQIQRMIIVRELLG 418
Cdd:cd01151  316 PEQISLLKRNNCGKALEIARTAREMLGGNGISDEYHIIRHMVNLESVNTYEGTHDIHALILGRAITG 382
PTZ00461 PTZ00461
isovaleryl-CoA dehydrogenase; Provisional
 24-421 4.51e-62

isovaleryl-CoA dehydrogenase; Provisional


Pssm-ID: 185640 [Multi-domain]  Cd Length: 410  Bit Score: 205.94  E-value: 4.51e-62
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557006922  24 TPAAKAKLKQDGYGFSFNLTDQQKEFQATARKFAREEIIPVAAHYDRTGEYPVPIIRRVWELGLMNGHIPESCGGLGLGI 103
Cdd:PTZ00461  19 TAAATMTSASRAFMDLYNPTPEHAALRETVAKFSREVVDKHAREDDINMHFNRDLFKQLGDLGVMGVTVPEADGGAGMDA 98

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557006922 104 FDTCLTSEELAYGCTGIQTAIEANS-LGQMPVIIAGNEQQKKKYLGRLMEEPLMCAYCVTEPGAGSDVAGIKTRAEKKGD 182
Cdd:PTZ00461  99 VAAVIIHHELSKYDPGFCLAYLAHSmLFVNNFYYSASPAQRARWLPKVLTGEHVGAMGMSEPGAGTDVLGMRTTAKKDSN 178

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557006922 183 E-YIINGQKMWITNGGKANWYFVLTRTNpdpkappsGAFTGFIVDGDTPGIQIGRKELNMGQRCSDTRGIVFEDVRVPKE 261
Cdd:PTZ00461 179 GnYVLNGSKIWITNGTVADVFLIYAKVD--------GKITAFVVERGTKGFTQGPKIDKCGMRASHMCQLFFEDVVVPAE 250

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557006922 262 NVLIAEGAGFKVAMGAFDKTRPPVAAAATGLAQRALDEAVKYAMERKTFGRLIVEHQAVSFMLAEMAMKTVLARMAYQRS 341
Cdd:PTZ00461 251 NLLGEEGKGMVGMMRNLELERVTLAAMAVGIAERSVELMTSYASERKAFGKPISNFGQIQRYIAEGYADTEAAKALVYSV 330

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557006922 342 AWEVDEGRKNTFFASVAKAFAGDIANQVASDAVQIFGGNGYNSEYPVEKLMRDAKIYQIYEGTAQIQRMIIVRELLGTYK 421
Cdd:PTZ00461 331 SHNVHPGNKNRLGSDAAKLFATPIAKKVADSAIQVMGGMGYSRDMPVERLWRDAKLLEIGGGTIEAHHKNITKDLLKGLK 410
ACAD_fadE5 cd01153
Putative acyl-CoA dehydrogenases similar to fadE5; Putative acyl-CoA dehydrogenase (ACAD). ...
 51-408 1.23e-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: 204.93  E-value: 1.23e-61
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557006922  51 ATARKFAREEIIPVAAHYDRTG--------EYPVPI---IRRVWELGLMNGHIPESCGGLGL---------GIFDTCLTS 110
Cdd:cd01153    3 EEVARLAENVLAPLNADGDREGpvfddgrvVVPPPFkeaLDAFAEAGWMALGVPEEYGGQGLpitvysalaEIFSRGDAP 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557006922 111 EELAYGCTGIQTAIEANslgqmpviiaGNEQQKKKYLGRLMEEPLMCAYCVTEPGAGSDVAGIKTRAEKKGD-EYIINGQ 189
Cdd:cd01153   83 LMYASGTQGAAATLLAH----------GTEAQREKWIPRLAEGEWTGTMCLTEPDAGSDLGALRTKAVYQADgSWRINGV 152

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557006922 190 KMWITNGGKANW----YFVLTRtnpdPKAPPSGA-------FTGFIVDGDTPGIQIGRKELNMGQRCSDTRGIVFEDVRV 258
Cdd:cd01153  153 KRFISAGEHDMSenivHLVLAR----SEGAPPGVkglslflVPKFLDDGERNGVTVARIEEKMGLHGSPTCELVFDNAKG 228

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557006922 259 PkenVLIAEGAGFKVAMGAFDKTRPPVAAAATGLAQRALDEAVKYAMERKTFGRL--------IVEHQAVSFMLAEMAMK 330
Cdd:cd01153  229 E---LIGEEGMGLAQMFAMMNGARLGVGTQGTGLAEAAYLNALAYAKERKQGGDLikaapavtIIHHPDVRRSLMTQKAY 305

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557006922 331 TVLARMAYQRSAWEVDEGRK--------------NTFFASVAKAFAGDIANQVASDAVQIFGGNGYNSEYPVEKLMRDAK 396
Cdd:cd01153  306 AEGSRALDLYTATVQDLAERkategedrkalsalADLLTPVVKGFGSEAALEAVSDAIQVHGGSGYTREYPIEQYYRDAR 385

                        410
                 ....*....|..
gi 557006922 397 IYQIYEGTAQIQ 408
Cdd:cd01153  386 ITTIYEGTTGIQ 397
ACAD_fadE6_17_26 cd01152
Putative acyl-CoA dehydrogenases similar to fadE6, fadE17, and fadE26; Putative acyl-CoA ...
 44-418 1.88e-60

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: 201.04  E-value: 1.88e-60
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557006922  44 DQQKEFQATARKFAREEIIP-----VAAHYDRTGEYPVPIIRRVWELGLMNGHIPESCGGLGLGIFDTCLTSEELAYGCT 118
Cdd:cd01152    1 PSEEAFRAEVRAWLAAHLPPelreeSALGYREGREDRRRWQRALAAAGWAAPGWPKEYGGRGASLMEQLIFREEMAAAGA 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557006922 119 GIQtaieANSLGQM---PVIIA-GNEQQKKKYLGRLMEEPLMCAYCVTEPGAGSDVAGIKTRAEKKGDEYIINGQKMWIT 194
Cdd:cd01152   81 PVP----FNQIGIDlagPTILAyGTDEQKRRFLPPILSGEEIWCQGFSEPGAGSDLAGLRTRAVRDGDDWVVNGQKIWTS 156

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557006922 195 NGGKANWYFVLTRTNPDpkAPPSGAFTGFIVDGDTPGIQIgR--KELNMGqrcSDTRGIVFEDVRVPKENVLIAEGAGFK 272
Cdd:cd01152  157 GAHYADWAWLLVRTDPE--APKHRGISILLVDMDSPGVTV-RpiRSINGG---EFFNEVFLDDVRVPDANRVGEVNDGWK 230

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557006922 273 VAMGAFDKTRppvaAAATGLAQRALDEAVKYAMERKTFGRLIVEHQAVSFMLAEMAMKTVLARMAYQRSAWEVDEGRKNT 352
Cdd:cd01152  231 VAMTTLNFER----VSIGGSAATFFELLLARLLLLTRDGRPLIDDPLVRQRLARLEAEAEALRLLVFRLASALAAGKPPG 306

                        330       340       350       360       370       380       390
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 557006922 353 FFASVAKAFAGDIANQVASDAVQIFG--------GNGYNSEYPVEKLMRDAKIYQIYEGTAQIQRMIIVRELLG 418
Cdd:cd01152  307 AEASIAKLFGSELAQELAELALELLGtaallrdpAPGAELAGRWEADYLRSRATTIYGGTSEIQRNIIAERLLG 380
PRK12341 PRK12341
acyl-CoA dehydrogenase;
40-421 1.08e-58

acyl-CoA dehydrogenase;


Pssm-ID: 183454 [Multi-domain]  Cd Length: 381  Bit Score: 196.49  E-value: 1.08e-58
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557006922  40 FNLTDQQKEFQATARKF-AREEIIPVAAHYDRTGEYPVPIIRRVWELGLMNGHIPESCGGLGLGIFDTCLTSEELAYGCT 118
Cdd:PRK12341   3 FSLTEEQELLLASIRELiTRNFPEEYFRTCDENGTYPREFMRALADNGISMLGVPEEFGGTPADYVTQMLVLEEVSKCGA 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557006922 119 GIQTAIEANSLGQMpvIIAGNEQQKKKylgrLMEEPLM---CAYC--VTEPGAGSDVAGIKTRAEKKGDEYIINGQKMWI 193
Cdd:PRK12341  83 PAFLITNGQCIHSM--RRFGSAEQLRK----TAESTLEtgdPAYAlaLTEPGAGSDNNSATTTYTRKNGKVYLNGQKTFI 156

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557006922 194 TNGGKANWYFVLTRtNPDPKAPPSgAFTGFIVDGDTPGIQIGRKElNMGQRCSDTRGIVFEDVRVPKENVLIAEGAGFKV 273
Cdd:PRK12341 157 TGAKEYPYMLVLAR-DPQPKDPKK-AFTLWWVDSSKPGIKINPLH-KIGWHMLSTCEVYLDNVEVEESDLVGEEGMGFLN 233

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557006922 274 AMGAFDKTRPPVAAAATGLAQRALDEAVKYAMERKTFGRLIVEHQAVSFMLAEMAMKTVLAR-MAYqRSAWEVDEGRKNT 352
Cdd:PRK12341 234 VMYNFEMERLINAARSLGFAECAFEDAARYANQRIQFGKPIGHNQLIQEKLTLMAIKIENMRnMVY-KVAWQADNGQSLR 312

                        330       340       350       360       370       380
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 557006922 353 FFASVAKAFAGDIANQVASDAVQIFGGNGYNSEYPVEKLMRDAKIYQIYEGTAQIQRMIIVRELLGTYK 421
Cdd:PRK12341 313 TSAALAKLYCARTAMEVIDDAIQIMGGLGYTDEARVSRFWRDVRCERIGGGTDEIMIYIAGRQILKDYQ 381
ACAD_FadE2 cd01155
Acyl-CoA dehydrogenases similar to fadE2; FadE2-like Acyl-CoA dehydrogenase (ACAD). Acyl-CoA ...
 47-414 2.55e-51

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: 177.20  E-value: 2.55e-51
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557006922  47 KEFQATARKFAREEIIPVAAHY-------DRTGEYPVPIIRRVWE----LGLMNGHIPESCGGLGLGIFDTCLTSEEL-- 113
Cdd:cd01155    4 QELRARVKAFMEEHVYPAEQEFleyyaegGDRWWTPPPIIEKLKAkakaEGLWNLFLPEVSGLSGLTNLEYAYLAEETgr 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557006922 114 ------AYGCTGIQTaieanslGQMPVIIA-GNEQQKKKYLGRLMEEPLMCAYCVTEPG-AGSDVAGIKTRAEKKGDEYI 185
Cdd:cd01155   84 sffapeVFNCQAPDT-------GNMEVLHRyGSEEQKKQWLEPLLDGKIRSAFAMTEPDvASSDATNIECSIERDGDDYV 156

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557006922 186 INGQKMWITNGG--KANWYFVLTRTNPDpKAPPSGAFTGFIVDGDTPGIQIGRKELNMGQrcSDTRG----IVFEDVRVP 259
Cdd:cd01155  157 INGRKWWSSGAGdpRCKIAIVMGRTDPD-GAPRHRQQSMILVPMDTPGVTIIRPLSVFGY--DDAPHghaeITFDNVRVP 233

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557006922 260 KENVLIAEGAGFKVAMGAFDKTRPPVAAAATGLAQRALDEAVKYAMERKTFGRLIVEHQAVSFMLAEMAMKTVLARMAYQ 339
Cdd:cd01155  234 ASNLILGEGRGFEIAQGRLGPGRIHHCMRLIGAAERALELMCQRAVSREAFGKKLAQHGVVAHWIAKSRIEIEQARLLVL 313

                        330       340       350       360       370       380       390
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 557006922 340 RSAWEVDEG--RKNTFFASVAKAFAGDIANQVASDAVQIFGGNGYNSEYPVEKLMRDAKIYQIYEGTAQIQRMIIVR 414
Cdd:cd01155  314 KAAHMIDTVgnKAARKEIAMIKVAAPRMALKIIDRAIQVHGAAGVSQDTPLANMYAWARTLRIADGPDEVHLRSIAR 390
Acyl-CoA_dh_1 pfam00441
Acyl-CoA dehydrogenase, C-terminal domain; C-terminal domain of Acyl-CoA dehydrogenase is an ...
 268-416 3.73e-51

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: 168.97  E-value: 3.73e-51
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557006922  268 GAGFKVAMGAFDKTRPPVAAAATGLAQRALDEAVKYAMERKTFGRLIVEHQAVSFMLAEMAMKTVLARMAYQRSAWEVDE 347
Cdd:pfam00441   1 GRGFRVAMETLNHERLAIAAMALGLARRALDEALAYARRRKAFGRPLIDFQLVRHKLAEMAAEIEAARLLVYRAAEALDA 80

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 557006922  348 GRKNTFFASVAKAFAGDIANQVASDAVQIFGGNGYNSEYPVEKLMRDAKIYQIYEGTAQIQRMIIVREL 416
Cdd:pfam00441  81 GGPDGAEASMAKLYASEAAVEVADLAMQLHGGYGYLREYPVERLYRDARVLRIGEGTSEIQRNIIARRL 149
PRK03354 PRK03354
crotonobetainyl-CoA dehydrogenase; Validated
 40-421 1.09e-49

crotonobetainyl-CoA dehydrogenase; Validated


Pssm-ID: 179566 [Multi-domain]  Cd Length: 380  Bit Score: 172.71  E-value: 1.09e-49
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557006922  40 FNLTDQQKEFQATARKF-AREEIIPVAAHYDRTGEYPVPIIRRVWELGLMNGHIPESCGGLGLGIFDTCLTSEELayGCT 118
Cdd:PRK03354   3 FNLNDEQELFVAGIRELmASENWEAYFAECDRDSVYPERFVKALADMGIDSLLIPEEHGGLDAGFVTLAAVWMEL--GRL 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557006922 119 GIQTAIeansLGQMP-----VIIAGNEQQKKKYLGRLMEEPLMCAYCVTEPGAGSDVAGIKTRAEKKGDEYIINGQKMWI 193
Cdd:PRK03354  81 GAPTYV----LYQLPggfntFLREGTQEQIDKIMAFRGTGKQMWNSAITEPGAGSDVGSLKTTYTRRNGKVYLNGSKCFI 156

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557006922 194 TNGGKANWYFVLTRtnpDPKAPPSGAFTGFIVDGDTPGIQIGRKElNMGQRCSDTRGIVFEDVRVPKENVLIAEGAGFKV 273
Cdd:PRK03354 157 TSSAYTPYIVVMAR---DGASPDKPVYTEWFVDMSKPGIKVTKLE-KLGLRMDSCCEITFDDVELDEKDMFGREGNGFNR 232

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557006922 274 AMGAFDKTRPPVAAAATGLAQRALDEAVKYAMERKTFGRLIVEHQAVSFMLAEMAMK-TVLARMAYQrSAWEVDEGRKNT 352
Cdd:PRK03354 233 VKEEFDHERFLVALTNYGTAMCAFEDAARYANQRVQFGEAIGRFQLIQEKFAHMAIKlNSMKNMLYE-AAWKADNGTITS 311

                        330       340       350       360       370       380
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 557006922 353 FFASVAKAFAGDIANQVASDAVQIFGGNGYNSEYPVEKLMRDAKIYQIYEGTAQIQRMIIVRELLGTYK 421
Cdd:PRK03354 312 GDAAMCKYFCANAAFEVVDSAMQVLGGVGIAGNHRISRFWRDLRVDRVSGGSDEMQILTLGRAVLKQYR 380
PLN02526 PLN02526
acyl-coenzyme A oxidase
 23-418 3.12e-43

acyl-coenzyme A oxidase


Pssm-ID: 178141 [Multi-domain]  Cd Length: 412  Bit Score: 156.17  E-value: 3.12e-43
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557006922  23 STPAAK-AKLKQDGYGFSFNLTDQQKEFQATARKFAREEIIPVAAHYDRTGEYPVPIIRRVWELGLMNGHIpESCGGLGL 101
Cdd:PLN02526   9 ATPASIfPPSVSDYYQFDDLLTPEEQALRKRVRECMEKEVAPIMTEYWEKAEFPFHIIPKLGSLGIAGGTI-KGYGCPGL 87

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557006922 102 GIFDTCLTSEELAYGCTGIQTAIEANS-LGQMPVIIAGNEQQKKKYLGRLMEEPLMCAYCVTEPGAGSDVAGIKTRAEKK 180
Cdd:PLN02526  88 SITASAIATAEVARVDASCSTFILVHSsLAMLTIALCGSEAQKQKYLPSLAQLDTVACWALTEPDYGSDASSLNTTATKV 167

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557006922 181 GDEYIINGQKMWITNGGKANWYFVLTRTNpdpkapPSGAFTGFIVDGDTPGIQIGRKELNMGQRCSDTRGIVFEDVRVPK 260
Cdd:PLN02526 168 EGGWILNGQKRWIGNSTFADVLVIFARNT------TTNQINGFIVKKGAPGLKATKIENKIGLRMVQNGDIVLKDVFVPD 241

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557006922 261 ENVLIAEGAgFKVAMGAFDKTRPPVAAAATGLAQRALDEAVKYAMERKTFGRLIVEHQAVSFMLAEM-----AMKTVLAR 335
Cdd:PLN02526 242 EDRLPGVNS-FQDTNKVLAVSRVMVAWQPIGISMGVYDMCHRYLKERKQFGAPLAAFQINQEKLVRMlgniqAMFLVGWR 320

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557006922 336 MA--YqrsawevDEGRKNTFFASVAKAFAGDIANQVASDAVQIFGGNGYNSEYPVEKLMRDAKIYQIYEGTAQIQRMIIV 413
Cdd:PLN02526 321 LCklY-------ESGKMTPGHASLGKAWITKKARETVALGRELLGGNGILADFLVAKAFCDLEPIYTYEGTYDINALVTG 393


                 ....*
gi 557006922 414 RELLG 418
Cdd:PLN02526 394 REITG 398
AidB cd01154
Proteins involved in DNA damage response, similar to the AidB gene product; AidB is one of ...
 63-414 3.50e-37

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: 139.81  E-value: 3.50e-37
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557006922  63 PVAAHYDRTGE------YP---VPIIRRVWELGLMNG--HIPESCGGLGLGIFDTCLTSEELAYGCTGIQTAIEANSLGQ 131
Cdd:cd01154   46 PVLEMWDRWGRrvdrvwVHpawHALMRRLIEEGVINIedGPAGEGRRHVHFAAGYLLSDAAAGLLCPLTMTDAAVYALRK 125

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557006922 132 MpviiaGNEQQKKK---YLGRLMEEPLMCAYCVTEPGAGSDVAGIKTRAEK-KGDEYIINGQKmWITNGGKANWYFVLTR 207
Cdd:cd01154  126 Y-----GPEELKQYlpgLLSDRYKTGLLGGTWMTEKQGGSDLGANETTAERsGGGVYRLNGHK-WFASAPLADAALVLAR 199

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557006922 208 TNPDPkaPPSGAFTGFIV-----DGDTPGIQIGRKELNMGQRCSDTRGIVFEDVrvpkENVLIA-EGAGFKVAMGAFDKT 281
Cdd:cd01154  200 PEGAP--AGARGLSLFLVprlleDGTRNGYRIRRLKDKLGTRSVATGEVEFDDA----EAYLIGdEGKGIYYILEMLNIS 273

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557006922 282 RPPVAAAATGLAQRALDEAVKYAMERKTFGRLIVEHQAVSFMLAEMAMKT--------VLARMAYQRSAWEVDEGRKNTF 353
Cdd:cd01154  274 RLDNAVAALGIMRRALSEAYHYARHRRAFGKPLIDHPLMRRDLAEMEVDVeaataltfRAARAFDRAAADKPVEAHMARL 353

                        330       340       350       360       370       380
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 557006922 354 FASVAKAFAGDIANQVASDAVQIFGGNGYNSEYPVEKLMRDAKIYQIYEGTAQIQRMIIVR 414
Cdd:cd01154  354 ATPVAKLIACKRAAPVTSEAMEVFGGNGYLEEWPVARLHREAQVTPIWEGTGNIQALDVLR 414
Acyl-CoA_dh_N pfam02771
Acyl-CoA dehydrogenase, N-terminal domain; The N-terminal domain of Acyl-CoA dehydrogenase is ...
 43-150 4.35e-36

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: 128.35  E-value: 4.35e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557006922   43 TDQQKEFQATARKFAREEIIPVAAHYDRTGEYPVPIIRRVWELGLMNGHIPESCGGLGLGIFDTCLTSEELAYGCTGIQT 122
Cdd:pfam02771   1 TEEQEALRDTVREFAEEEIAPHAAEWDEEGEFPRELWKKLGELGLLGITIPEEYGGAGLDYLAYALVAEELARADASVAL 80

                          90       100
                  ....*....|....*....|....*....
gi 557006922  123 AIEA-NSLGQMPVIIAGNEQQKKKYLGRL 150
Cdd:pfam02771  81 ALSVhSSLGAPPILRFGTEEQKERYLPKL 109
PLN02876 PLN02876
acyl-CoA dehydrogenase
 130-403 5.25e-32

acyl-CoA dehydrogenase


Pssm-ID: 215473 [Multi-domain]  Cd Length: 822  Bit Score: 128.76  E-value: 5.25e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557006922 130 GQMPVIIA-GNEQQKKKYLGRLMEEPLMCAYCVTEPG-AGSDVAGIKTRAEKKGDEYIINGQKMWiTNGG---KANWYFV 204
Cdd:PLN02876 524 GNMEVLLRyGNKEQQLEWLIPLLEGKIRSGFAMTEPQvASSDATNIECSIRRQGDSYVINGTKWW-TSGAmdpRCRVLIV 602

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557006922 205 LTRTnpDPKAPPSGAFTGFIVDGDTPGIQIGRKELNMGqrCSDT----RGIVFEDVRVPKENVLIAEGAGFKVAMGAFDK 280
Cdd:PLN02876 603 MGKT--DFNAPKHKQQSMILVDIQTPGVQIKRPLLVFG--FDDAphghAEISFENVRVPAKNILLGEGRGFEIAQGRLGP 678

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557006922 281 TRPPVAAAATGLAQRALDEAVKYAMERKTFGRLIVEHQAVSFMLAEMAMKTVLARMAYQRSAWEVDE--GRKNTFFASVA 358
Cdd:PLN02876 679 GRLHHCMRLIGAAERGMQLMVQRALSRKAFGKLIAQHGSFLSDLAKCRVELEQTRLLVLEAADQLDRlgNKKARGIIAMA 758

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*
gi 557006922 359 KAFAGDIANQVASDAVQIFGGNGYNSEYPVEKLMRDAKIYQIYEG 403
Cdd:PLN02876 759 KVAAPNMALKVLDMAMQVHGAAGVSSDTVLAHLWATARTLRIADG 803
Acyl-CoA_dh_M pfam02770
Acyl-CoA dehydrogenase, middle domain; Central domain of Acyl-CoA dehydrogenase has a ...
 158-254 1.32e-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: 110.45  E-value: 1.32e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557006922  158 AYCVTEPGAGSDVAGIKTRA-EKKGDEYIINGQKMWITNGGKANWYFVLTRTNPDPKAppsGAFTGFIVDGDTPGIQIGR 236
Cdd:pfam02770   1 AFALTEPGAGSDVASLKTTAaDGDGGGWVLNGTKWWITNAGIADLFLVLARTGGDDRH---GGISLFLVPKDAPGVSVRR 77

                          90
                  ....*....|....*...
gi 557006922  237 KELNMGQRCSDTRGIVFE 254
Cdd:pfam02770  78 IETKLGVRGLPTGELVFD 95
PTZ00456 PTZ00456
acyl-CoA dehydrogenase; Provisional
 93-419 4.43e-23

acyl-CoA dehydrogenase; Provisional


Pssm-ID: 185635 [Multi-domain]  Cd Length: 622  Bit Score: 101.48  E-value: 4.43e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557006922  93 PESCGGLGLGIFDTCLTSEELAYGCTGIQTaIEANSLGQMPVIIA-GNEQQKKKYLGRLMEEPLMCAYCVTEPGAGSDVA 171
Cdd:PTZ00456 119 PEEYGGQALPLSVGFITRELMATANWGFSM-YPGLSIGAANTLMAwGSEEQKEQYLTKLVSGEWSGTMCLTEPQCGTDLG 197

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557006922 172 GIKTRAEKKGD-EYIINGQKMWITNGG---KAN-WYFVLTRTnpdPKAPPSG-AFTGFIV-------DGD---TPGIQIG 235
Cdd:PTZ00456 198 QVKTKAEPSADgSYKITGTKIFISAGDhdlTENiVHIVLARL---PNSLPTTkGLSLFLVprhvvkpDGSletAKNVKCI 274

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557006922 236 RKELNMGQRCSDTRGIVFEDvrvpKENVLIAE-GAGFKVAMGAFDKTRppVAAAATGL--AQRALDEAVKYAMERKTFGR 312
Cdd:PTZ00456 275 GLEKKMGIKGSSTCQLSFEN----SVGYLIGEpNAGMKQMFTFMNTAR--VGTALEGVchAELAFQNALRYARERRSMRA 348

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557006922 313 L------------IVEHQAVSFML------AE--MAMKTVLARMA-YQRSAWEVDE----GRKNTFFASVAKAFAGDIAN 367
Cdd:PTZ00456 349 LsgtkepekpadrIICHANVRQNIlfakavAEggRALLLDVGRLLdIHAAAKDAATrealDHEIGFYTPIAKGCLTEWGV 428

                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|...
gi 557006922 368 QVASDAVQIFGGNGYNSEYPVEKLMRDAKIYQIYEGTAQIQRM-IIVRELLGT 419
Cdd:PTZ00456 429 EAASRCLQVWGGHGYIKGNGMEQILRDARIGTLYEGTTGIQALdFIGRKVLSL 481
Acyl-CoA_dh_2 pfam08028
Acyl-CoA dehydrogenase, C-terminal domain;
285-404 1.58e-18

Acyl-CoA dehydrogenase, C-terminal domain;


Pssm-ID: 429790 [Multi-domain]  Cd Length: 133  Bit Score: 81.24  E-value: 1.58e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557006922  285 VAAAATGLAQRALDEAVKYAMERKT--FGRLIVEHQAVSFMLAEMAMKTVLARMAYQRSAWE----VDEGRKNTFF---- 354
Cdd:pfam08028   2 IAAAALGAARAALAEFTERARGRVRayFGVPLAEDPATQLALAEAAARIDAARLLLERAAARieaaAAAGKPVTPAlrae 81

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|
gi 557006922  355 ASVAKAFAGDIANQVASDAVQIFGGNGYNSEYPVEKLMRDAKIYQIYEGT 404
Cdd:pfam08028  82 ARRAAAFATELAVAAVDALFRAAGGSALFQDSPLQRIWRDIHAAAQHAAV 131
AXO cd01150
Peroxisomal acyl-CoA oxidase; Peroxisomal acyl-CoA oxidases (AXO) catalyze the first set in ...
 132-422 1.24e-16

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: 81.99  E-value: 1.24e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557006922 132 MPVIIA-GNEQQKKKYL-GRLMEEPLMCaYCVTEPGAGSDVAGIKTRA--EKKGDEYIIN-----GQKMWITNGGK-ANW 201
Cdd:cd01150  110 GNAIKNlGTDEHQDYWLqGANNLEIIGC-FAQTELGHGSNLQGLETTAtyDPLTQEFVINtpdftATKWWPGNLGKtATH 188

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557006922 202 YFVLTRTNPDPKappSGAFTGFIV---DGDT----PGIQIGRKELNMGQRCSDTRGIVFEDVRVPKENVL------IAEG 268
Cdd:cd01150  189 AVVFAQLITPGK---NHGLHAFIVpirDPKThqplPGVTVGDIGPKMGLNGVDNGFLQFRNVRIPRENLLnrfgdvSPDG 265

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557006922 269 A----------GFKVAMGAFDKTRPPVAAAATGLAQRALDEAVKYAMERKTFGRL-------IVEHQ------------- 318
Cdd:cd01150  266 TyvspfkdpnkRYGAMLGTRSGGRVGLIYDAAMSLKKAATIAIRYSAVRRQFGPKpsdpevqILDYQlqqyrlfpqlaaa 345

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557006922 319 -AVSFMLAEMAMKTVLARMA-YQRSAwevDEGRKNTFFASVAKAFAGDIANQVASDAVQIFGGNGYNSEYPVEKLMRDAK 396
Cdd:cd01150  346 yAFHFAAKSLVEMYHEIIKElLQGNS---ELLAELHALSAGLKAVATWTAAQGIQECREACGGHGYLAMNRLPTLRDDND 422

                        330       340
                 ....*....|....*....|....*.
gi 557006922 397 IYQIYEGTAQIQRMIIVRELLGTYKQ 422
Cdd:cd01150  423 PFCTYEGDNTVLLQQTANYLLKKYAQ 448
DszC cd01163
Dibenzothiophene (DBT) desulfurization enzyme C; DszC is a flavin reductase dependent enzyme, ...
 49-396 1.86e-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: 1.86e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557006922  49 FQATARKFAREeiipvAAHYDRTGEYPVPIIRRVWELGLMNGHIPESCGGLGLGIFDTCLTSEELAygctgiqtaiEANS 128
Cdd:cd01163    3 ARPLAARIAEG-----AAERDRQRGLPYEEVALLRQSGLGTLRVPKEYGGLGASLPDLYEVVRELA----------AADS 67

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557006922 129 -LGQMP---------VIIAGNEQQKKKYLGRLMEEPLM-CAycVTEPGaGSDVAGIKTRAEKKGDEYIINGQKmWITNGG 197
Cdd:cd01163   68 nIAQALrahfgfveaLLLAGPEQFRKRWFGRVLNGWIFgNA--VSERG-SVRPGTFLTATVRDGGGYVLNGKK-FYSTGA 143

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557006922 198 KANWYFVLTRTNPDpkappsGAFTGFIVDGDTPGIQIGRKELNMGQRCSDTRGIVFEDVRVPKENVLIAEGAGFKVAMga 277
Cdd:cd01163  144 LFSDWVTVSALDEE------GKLVFAAVPTDRPGITVVDDWDGFGQRLTASGTVTFDNVRVEPDEVLPRPNAPDRGTL-- 215

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557006922 278 fdktRPPV-----AAAATGLAQRALDEAVKYAMER-KTFGRLIVEH--------QAVsfmlAEMAMKTVLARMAYQRSAW 343
Cdd:cd01163  216 ----LTAIyqlvlAAVLAGIARAALDDAVAYVRSRtRPWIHSGAESarddpyvqQVV----GDLAARLHAAEALVLQAAR 287

                        330       340       350       360       370       380
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 557006922 344 EVDE----GRKNTFFASV--------AKAFAGDIANQVASDAVQIFGGNGYNSEYPVEKLMRDAK 396
Cdd:cd01163  288 ALDAaaaaGTALTAEARGeaalavaaAKVVVTRLALDATSRLFEVGGASATAREHNLDRHWRNAR 352
PRK11561 PRK11561
isovaleryl CoA dehydrogenase; Provisional
 162-416 1.36e-12

isovaleryl CoA dehydrogenase; Provisional


Pssm-ID: 183199 [Multi-domain]  Cd Length: 538  Bit Score: 69.40  E-value: 1.36e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557006922 162 TEPGAGSDVAGIKTRAEKKGDE-YIINGQKmWITNGGKANWYFVLTRTNpdpkappsGAFTGFIV-----DGDTPGIQIG 235
Cdd:PRK11561 185 TEKQGGSDVLSNTTRAERLADGsYRLVGHK-WFFSVPQSDAHLVLAQAK--------GGLSCFFVprflpDGQRNAIRLE 255

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557006922 236 RKELNMGQRCSDTRGIVFEDVrvpKENVLIAEGAGFK--VAMGAFdkTRPPVAAAATGLAQRALDEAVKYAMERKTFGRL 313
Cdd:PRK11561 256 RLKDKLGNRSNASSEVEFQDA---IGWLLGEEGEGIRliLKMGGM--TRFDCALGSHGLMRRAFSVAIYHAHQRQVFGKP 330

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557006922 314 IVEHQAVSFMLAEMAMK-----TVLARMAyqrSAWEVDEGRKNTFFA---------SVAKAFAGDIAnqvasDAVQIFGG 379
Cdd:PRK11561 331 LIEQPLMRQVLSRMALQlegqtALLFRLA---RAWDRRADAKEALWArlftpaakfVICKRGIPFVA-----EAMEVLGG 402

                        250       260       270
                 ....*....|....*....|....*....|....*..
gi 557006922 380 NGYNSEYPVEKLMRDAKIYQIYEGTAQIQRMIIVREL 416
Cdd:PRK11561 403 IGYCEESELPRLYREMPVNSIWEGSGNIMCLDVLRVL 439
PLN02312 PLN02312
acyl-CoA oxidase
 138-310 5.41e-09

acyl-CoA oxidase


Pssm-ID: 215178 [Multi-domain]  Cd Length: 680  Bit Score: 58.25  E-value: 5.41e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557006922 138 GNEQQKKKYLGRLMEEPLMCAYCVTEPGAGSDVAGIKTRA--EKKGDEYIIN-----GQKMWItnGGKANW---YFVLTR 207
Cdd:PLN02312 168 GTKRHHDKWLKDTEDYVVKGCFAMTELGHGSNVRGIETVTtyDPKTEEFVINtpcesAQKYWI--GGAANHathTIVFSQ 245

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557006922 208 TNPDPKAPPSGAFTGFIVDGD---TPGIQIGRKELNMGQRCSDTRGIVFEDVRVPKENVL-----IAEGAGFKVAM---- 275
Cdd:PLN02312 246 LHINGKNEGVHAFIAQIRDQDgniCPNIRIADCGHKIGLNGVDNGRIWFDNLRIPRENLLnsvadVSPDGKYVSAIkdpd 325

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|..
gi 557006922 276 ---GAF----DKTRPPVAAAATGLAQRALDEAVKYAMERKTF 310
Cdd:PLN02312 326 qrfGAFlaplTSGRVTIAVSAIYSSKVGLAIAIRYSLSRRAF 367
PRK13026 PRK13026
acyl-CoA dehydrogenase; Reviewed
 127-381 8.60e-09

acyl-CoA dehydrogenase; Reviewed


Pssm-ID: 237277 [Multi-domain]  Cd Length: 774  Bit Score: 57.66  E-value: 8.60e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557006922 127 NSLGQMPVIIA-GNEQQKKKYLGRLME-EPLMCaYCVTEPGAGSDVA-----GIKTRAEKKGDEYI---INGQKMWITNG 196
Cdd:PRK13026 163 NSLGPGELLTHyGTQEQKDYWLPRLADgTEIPC-FALTGPEAGSDAGaipdtGIVCRGEFEGEEVLglrLTWDKRYITLA 241

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557006922 197 gkanwyfvltrtnpdPKAPPSG-AFTGFIVDG-----------------DTPGIQIGRKELNMGQRCSD--TRGivfEDV 256
Cdd:PRK13026 242 ---------------PVATVLGlAFKLRDPDGllgdkkelgitcaliptDHPGVEIGRRHNPLGMAFMNgtTRG---KDV 303

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557006922 257 RVPKENVLIAE---GAGFKVAMGAFDKTR----PPVAAAATGLAQRALDEavkYAMERKTFGRLIVEHQAVSFMLAEMAM 329
Cdd:PRK13026 304 FIPLDWIIGGPdyaGRGWRMLVECLSAGRgislPALGTASGHMATRTTGA---YAYVRRQFGMPIGQFEGVQEALARIAG 380

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|..
gi 557006922 330 KTVLARMAYQRSAWEVDEGRKNTFFASVAKAFAGDIANQVASDAVQIFGGNG 381
Cdd:PRK13026 381 NTYLLEAARRLTTTGLDLGVKPSVVTAIAKYHMTELARDVVNDAMDIHAGKG 432
NcnH cd01159
Naphthocyclinone hydroxylase; Naphthocyclinone is an aromatic polyketide and an antibiotic, ...
 59-407 3.94e-08

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: 54.66  E-value: 3.94e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557006922  59 EEIIPV----AAHYDRTGEYPVPIIRRVWELGLMNGHIPESCGGLGLGIFDTCLTSEELAYGCTGiqTAIEANSLGQMPV 134
Cdd:cd01159    4 EDLAPLirerAPEAERARRLPDEVVRALREIGFFRMFVPKRYGGLEGDFAEFAEAIATLAEACGS--AAWVASIVATHSR 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557006922 135 IIA--GNEQQKKKYlgrlMEEPLMCAYCVTEPGAgsdvagiktRAEKKGDEYIINGQKMWITNGGKANWYFVLTRTNPDP 212
Cdd:cd01159   82 MLAafPPEAQEEVW----GDGPDTLLAGSYAPGG---------RAERVDGGYRVSGTWPFASGCDHADWILVGAIVEDDD 148

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557006922 213 KAPPSGAFTgfivdgdtpgiqIGRKEL-------NMGQRCSDTRGIVFEDVRVPKENVLIaegagFKVAM------GAFD 279
Cdd:cd01159  149 GGPLPRAFV------------VPRAEYeivdtwhVVGLRGTGSNTVVVDDVFVPEHRTLT-----AGDMMagdgpgGSTP 211

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557006922 280 KTRPPV--------AAAATGLAQRALDEAVKYAMER---KTFGRLIVEHQAVSFMLAEMAMKTVLARM---AYQRSAWEV 345
Cdd:cd01159  212 VYRMPLrqvfplsfAAVSLGAAEGALAEFLELAGKRvrqYGAAVKMAEAPITQLRLAEAAAELDAARAfleRATRDLWAH 291

                        330       340       350       360       370       380       390
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 557006922 346 DEGRKNTFFASVAKAF--AGDIANQVASDAVQIF---GGNGYNSEYPVEKLMRDAK-----IYQIYEGTAQI 407
Cdd:cd01159  292 ALAGGPIDVEERARIRrdAAYAAKLSAEAVDRLFhaaGGSALYTASPLQRIWRDIHaaaqhAALNPETAAEA 363
PLN02636 PLN02636
acyl-coenzyme A oxidase
 119-422 4.03e-08

acyl-coenzyme A oxidase


Pssm-ID: 215342 [Multi-domain]  Cd Length: 686  Bit Score: 55.25  E-value: 4.03e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557006922 119 GIQTAIEANSlgqmpVIIAGNEQQKKKYLGRLMEEPLMCAYCVTEPGAGSDVAGIKTRA--EKKGDEYIIN-----GQKM 191
Cdd:PLN02636 142 GVQYSLWGGS-----VINLGTKKHRDKYFDGIDNLDYPGCFAMTELHHGSNVQGLQTTAtfDPLTDEFVINtpndgAIKW 216

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557006922 192 WITNG---GK-ANWYFVLTRTNPDPKAPPSGAFTGFIV---DGDT----PGIQIGRKELNMGQRCSDTRGIVFEDVRVPK 260
Cdd:PLN02636 217 WIGNAavhGKfATVFARLKLPTHDSKGVSDMGVHAFIVpirDMKThqvlPGVEIRDCGHKVGLNGVDNGALRFRSVRIPR 296

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557006922 261 ENVLIAEG----------------AGFKVAMGAFDKTRPPVAAAATGLAQRALDEAVKYAMERKTFGR------LIVEHQ 318
Cdd:PLN02636 297 DNLLNRFGdvsrdgkytsslptinKRFAATLGELVGGRVGLAYGSVGVLKASNTIAIRYSLLRQQFGPpkqpeiSILDYQ 376

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557006922 319 AVSFMLAEMAMKTVLARMAYQRSAWEVDEGRKNTFFASVA---------KAFAGDIANQVASDAVQIFGGNGYNSEYPVE 389
Cdd:PLN02636 377 SQQHKLMPMLASTYAFHFATEYLVERYSEMKKTHDDQLVAdvhalsaglKAYITSYTAKALSTCREACGGHGYAAVNRFG 456

                        330       340       350
                 ....*....|....*....|....*....|...
gi 557006922 390 KLMRDAKIYQIYEGTAQIQRMIIVRELLGTYKQ 422
Cdd:PLN02636 457 SLRNDHDIFQTFEGDNTVLLQQVAADLLKQYKE 489
PLN02443 PLN02443
acyl-coenzyme A oxidase
 138-311 4.07e-08

acyl-coenzyme A oxidase


Pssm-ID: 178062 [Multi-domain]  Cd Length: 664  Bit Score: 55.23  E-value: 4.07e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557006922 138 GNEQQKKKYLGRLMEEPLMCAYCVTEPGAGSDVAGIKTRA--EKKGDEYIIN-----GQKMWITNGGKANWY-FVLTRTN 209
Cdd:PLN02443 114 GTEEQQKKWLPLAYKMQIIGCYAQTELGHGSNVQGLETTAtfDPKTDEFVIHsptltSSKWWPGGLGKVSTHaVVYARLI 193

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557006922 210 PDPKappSGAFTGFIVDGDT-------PGI---QIGRKELNMGQRCSDTRGIVFEDVRVPKENVLIA------EGAGF-- 271
Cdd:PLN02443 194 TNGK---DHGIHGFIVQLRSlddhsplPGVtvgDIGMKFGNGAYNTMDNGFLRFDHVRIPRDQMLMRlskvtrEGKYVqs 270

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....
gi 557006922 272 ----KVAMGAFDKTRPPVAAAATGLAQRALDEAVKYAMERKTFG 311
Cdd:PLN02443 271 dvprQLVYGTMVYVRQTIVADASTALSRAVCIATRYSAVRRQFG 314
PTZ00460 PTZ00460
acyl-CoA dehydrogenase; Provisional
 138-310 6.09e-08

acyl-CoA dehydrogenase; Provisional


Pssm-ID: 185639 [Multi-domain]  Cd Length: 646  Bit Score: 54.85  E-value: 6.09e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557006922 138 GNEQQKKKYLGRLMEEPLMCAYCVTEPGAGSDVAGIKTRA--EKKGDEYIIN-----GQKMWITN-GGKANWYFVLTRTN 209
Cdd:PTZ00460 110 GTDEQINLWMPSLLNFEIVGCYAQTELGHGSDVQNLETTAtyDKQTNEFVIHtpsveAVKFWPGElGFLCNFALVYAKLI 189

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557006922 210 PDPKAPPSGAFTGFIVDGDT----PGIQIGRKELNMGQRCSDTRGIVFEDVRVPKENVL-----IAEGAGF------KVA 274
Cdd:PTZ00460 190 VNGKNKGVHPFMVRIRDKEThkplQGVEVGDIGPKMGYAVKDNGFLSFDHYRIPLDSLLaryikVSEDGQVerqgnpKVS 269

                        170       180       190
                 ....*....|....*....|....*....|....*.
gi 557006922 275 MGAFDKTRPPVAAAATGLAQRALDEAVKYAMERKTF 310
Cdd:PTZ00460 270 YASMMYMRNLIIDQYPRFAAQALTVAIRYSIYRQQF 305
fadE PRK09463
acyl-CoA dehydrogenase; Reviewed
 138-381 1.65e-07

acyl-CoA dehydrogenase; Reviewed


Pssm-ID: 236528 [Multi-domain]  Cd Length: 777  Bit Score: 53.67  E-value: 1.65e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557006922 138 GNEQQKKKYLGRLME-EPLMCaYCVTEPGAGSDVA-----GIKTRAEKKGDEYI---INGQKMWITNG------GKAnwy 202
Cdd:PRK09463 176 GTDEQKDHYLPRLARgEEIPC-FALTSPEAGSDAGsipdtGVVCKGEWQGEEVLgmrLTWNKRYITLApiatvlGLA--- 251

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557006922 203 FVLTrtnpDPKappsgaftGFIVDG------------DTPGIQIGRKELNMGQRCSD--TRGivfEDVRVPKENVLIAE- 267
Cdd:PRK09463 252 FKLY----DPD--------GLLGDKedlgitcaliptDTPGVEIGRRHFPLNVPFQNgpTRG---KDVFIPLDYIIGGPk 316

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557006922 268 --GAGFKVAMGAFDKTR----PPVAAAATGLAQRAldeAVKYAMERKTFGRLIVEHQAVSFMLAEMAMKTVLARMAYQRS 341
Cdd:PRK09463 317 maGQGWRMLMECLSVGRgislPSNSTGGAKLAALA---TGAYARIRRQFKLPIGKFEGIEEPLARIAGNAYLMDAARTLT 393

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|
gi 557006922 342 AWEVDEGRKNTFFASVAKAFAGDIANQVASDAVQIFGGNG 381
Cdd:PRK09463 394 TAAVDLGEKPSVLSAIAKYHLTERGRQVINDAMDIHGGKG 433
PTZ00457 PTZ00457
acyl-CoA dehydrogenase; Provisional
 87-299 2.96e-07

acyl-CoA dehydrogenase; Provisional


Pssm-ID: 185636 [Multi-domain]  Cd Length: 520  Bit Score: 52.58  E-value: 2.96e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557006922  87 LMNGHIPESCGGLGLGIFDTCLTSEELAYGCTG--IQTaIEANSLGQMPVIIAGNEQQKKKYLGRLMEEPLMCAYCVTEp 164
Cdd:PTZ00457  65 LYGARIATEYGGLGLGHTAHALIYEEVGTNCDSklLST-IQHSGFCTYLLSTVGSKELKGKYLTAMSDGTIMMGWATEE- 142

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557006922 165 GAGSDVAGIKTRAEKKGD-EYIINGQKMWItNGGKANWYFVL----TRTNPDPKAPPSGAFTGFIVDGDTPGIQIgrkel 239
Cdd:PTZ00457 143 GCGSDISMNTTKASLTDDgSYVLTGQKRCE-FAASATHFLVLaktlTQTAAEEGATEVSRNSFFICAKDAKGVSV----- 216

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 557006922 240 nmgqrcsDTRGIVFEDvrVPKENVLIAEGAGFKVAMGAFDKTRPPVAAAATGLAQRALDE 299
Cdd:PTZ00457 217 -------NGDSVVFEN--TPAADVVGVVGEGFKDAMITLFTEQYLYAASLLGIMKRVVQE 267
 
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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