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Conserved domains on  [gi|554506558|ref|NP_001272973|]
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medium-chain specific acyl-CoA dehydrogenase, mitochondrial isoform e [Homo sapiens]

Protein Classification

acyl-CoA dehydrogenase family protein( domain architecture ID 550)

acyl-CoA dehydrogenase (ACAD) family protein similar to acyl-CoA dehydrogenase that catalyzes the alpha,beta dehydrogenation of an acyl-CoA to form 2,3-dehydroacyl-CoA; requires an acceptor such as FAD, which becomes reduced

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
ACAD super family cl09933
Acyl-CoA dehydrogenase; Both mitochondrial acyl-CoA dehydrogenases (ACAD) and peroxisomal ...
 1-229 2.85e-174

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)


The actual alignment was detected with superfamily member cd01157:

Pssm-ID: 447864 [Multi-domain]  Cd Length: 378  Bit Score: 483.63  E-value: 2.85e-174
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 554506558   1 MWITNGGKANWYFLLARSDPDPKAPANKAFTGFIVEADTPGIQIGRKELNMGQRCSDTRGIVFEDVKVPKENVLIGDGAG 80
Cdd:cd01157  150 MWITNGGKANWYFLLARSDPDPKCPASKAFTGFIVEADTPGIQPGRKELNMGQRCSDTRGITFEDVRVPKENVLIGEGAG 229

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 554506558  81 FKVAMGAFDKTRPVVAAGAVGLAQRALDEATKYALERKTFGKLLVEHQAISFMLAEMAMKVELARMSYQRAAWEVDSGRR 160
Cdd:cd01157  230 FKIAMGAFDKTRPPVAAGAVGLAQRALDEATKYALERKTFGKLIAEHQAVSFMLADMAMKVELARLAYQRAAWEVDSGRR 309

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 554506558 161 NTYYASIAKAFAGDIANQLATDAVQILGGNGFNTEYPVEKLMRDAKIYQIYEGTSQIQRLIVAREHIDK 229
Cdd:cd01157  310 NTYYASIAKAFAADIANQLATDAVQIFGGNGFNSEYPVEKLMRDAKIYQIYEGTSQIQRLIISREHLGK 378
 
Name Accession Description Interval E-value
MCAD cd01157
Medium chain acyl-CoA dehydrogenase; MCADs are mitochondrial beta-oxidation enzymes, which ...
 1-229 2.85e-174

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: 483.63  E-value: 2.85e-174
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 554506558   1 MWITNGGKANWYFLLARSDPDPKAPANKAFTGFIVEADTPGIQIGRKELNMGQRCSDTRGIVFEDVKVPKENVLIGDGAG 80
Cdd:cd01157  150 MWITNGGKANWYFLLARSDPDPKCPASKAFTGFIVEADTPGIQPGRKELNMGQRCSDTRGITFEDVRVPKENVLIGEGAG 229

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 554506558  81 FKVAMGAFDKTRPVVAAGAVGLAQRALDEATKYALERKTFGKLLVEHQAISFMLAEMAMKVELARMSYQRAAWEVDSGRR 160
Cdd:cd01157  230 FKIAMGAFDKTRPPVAAGAVGLAQRALDEATKYALERKTFGKLIAEHQAVSFMLADMAMKVELARLAYQRAAWEVDSGRR 309

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 554506558 161 NTYYASIAKAFAGDIANQLATDAVQILGGNGFNTEYPVEKLMRDAKIYQIYEGTSQIQRLIVAREHIDK 229
Cdd:cd01157  310 NTYYASIAKAFAADIANQLATDAVQIFGGNGFNSEYPVEKLMRDAKIYQIYEGTSQIQRLIISREHLGK 378
CaiA COG1960
Acyl-CoA dehydrogenase related to the alkylation response protein AidB [Lipid transport and ...
 1-225 1.63e-94

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: 281.34  E-value: 1.63e-94
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 554506558   1 MWITNGGKANWYFLLARSDPDPKApanKAFTGFIVEADTPGIQIGRKELNMGQRCSDTRGIVFEDVKVPKENVLIGDGAG 80
Cdd:COG1960  154 TFITNAPVADVILVLARTDPAAGH---RGISLFLVPKDTPGVTVGRIEDKMGLRGSDTGELFFDDVRVPAENLLGEEGKG 230

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 554506558  81 FKVAMGAFDKTRPVVAAGAVGLAQRALDEATKYALERKTFGKLLVEHQAISFMLAEMAMKVELARMSYQRAAWEVDSGRR 160
Cdd:COG1960  231 FKIAMSTLNAGRLGLAAQALGIAEAALELAVAYAREREQFGRPIADFQAVQHRLADMAAELEAARALVYRAAWLLDAGED 310

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 554506558 161 NTYYASIAKAFAGDIANQLATDAVQILGGNGFNTEYPVEKLMRDAKIYQIYEGTSQIQRLIVARE 225
Cdd:COG1960  311 AALEAAMAKLFATEAALEVADEALQIHGGYGYTREYPLERLYRDARILTIYEGTNEIQRLIIARR 375
Acyl-CoA_dh_1 pfam00441
Acyl-CoA dehydrogenase, C-terminal domain; C-terminal domain of Acyl-CoA dehydrogenase is an ...
 78-224 4.53e-54

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


Pssm-ID: 395354 [Multi-domain]  Cd Length: 149  Bit Score: 170.51  E-value: 4.53e-54
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 554506558   78 GAGFKVAMGAFDKTRPVVAAGAVGLAQRALDEATKYALERKTFGKLLVEHQAISFMLAEMAMKVELARMSYQRAAWEVDS 157
Cdd:pfam00441   1 GRGFRVAMETLNHERLAIAAMALGLARRALDEALAYARRRKAFGRPLIDFQLVRHKLAEMAAEIEAARLLVYRAAEALDA 80

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 554506558  158 GRRNTYYASIAKAFAGDIANQLATDAVQILGGNGFNTEYPVEKLMRDAKIYQIYEGTSQIQRLIVAR 224
Cdd:pfam00441  81 GGPDGAEASMAKLYASEAAVEVADLAMQLHGGYGYLREYPVERLYRDARVLRIGEGTSEIQRNIIAR 147
PLN02519 PLN02519
isovaleryl-CoA dehydrogenase
 1-225 3.30e-52

isovaleryl-CoA dehydrogenase


Pssm-ID: 215284 [Multi-domain]  Cd Length: 404  Bit Score: 173.52  E-value: 3.30e-52
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 554506558   1 MWITNGGKANWYFLLARSDPdpkAPANKAFTGFIVEADTPGIQIGRKELNMGQRCSDTRGIVFEDVKVPKENVLIGDGAG 80
Cdd:PLN02519 178 MWCTNGPVAQTLVVYAKTDV---AAGSKGITAFIIEKGMPGFSTAQKLDKLGMRGSDTCELVFENCFVPEENVLGQEGKG 254

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 554506558  81 FKVAMGAFDKTRPVVAAGAVGLAQRALDEATKYALERKTFGKLLVEHQAISFMLAEMAMKVELARMSYQRAAWEVDSGRR 160
Cdd:PLN02519 255 VYVMMSGLDLERLVLAAGPLGLMQACLDVVLPYVRQREQFGRPIGEFQFIQGKLADMYTSLQSSRSYVYSVARDCDNGKV 334

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 554506558 161 NTYYASIAKAFAGDIANQLATDAVQILGGNGFNTEYPVEKLMRDAKIYQIYEGTSQIQRLIVARE 225
Cdd:PLN02519 335 DRKDCAGVILCAAERATQVALQAIQCLGGNGYINEYPTGRLLRDAKLYEIGAGTSEIRRMLIGRE 399
 
Name Accession Description Interval E-value
MCAD cd01157
Medium chain acyl-CoA dehydrogenase; MCADs are mitochondrial beta-oxidation enzymes, which ...
 1-229 2.85e-174

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: 483.63  E-value: 2.85e-174
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 554506558   1 MWITNGGKANWYFLLARSDPDPKAPANKAFTGFIVEADTPGIQIGRKELNMGQRCSDTRGIVFEDVKVPKENVLIGDGAG 80
Cdd:cd01157  150 MWITNGGKANWYFLLARSDPDPKCPASKAFTGFIVEADTPGIQPGRKELNMGQRCSDTRGITFEDVRVPKENVLIGEGAG 229

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 554506558  81 FKVAMGAFDKTRPVVAAGAVGLAQRALDEATKYALERKTFGKLLVEHQAISFMLAEMAMKVELARMSYQRAAWEVDSGRR 160
Cdd:cd01157  230 FKIAMGAFDKTRPPVAAGAVGLAQRALDEATKYALERKTFGKLIAEHQAVSFMLADMAMKVELARLAYQRAAWEVDSGRR 309

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 554506558 161 NTYYASIAKAFAGDIANQLATDAVQILGGNGFNTEYPVEKLMRDAKIYQIYEGTSQIQRLIVAREHIDK 229
Cdd:cd01157  310 NTYYASIAKAFAADIANQLATDAVQIFGGNGFNSEYPVEKLMRDAKIYQIYEGTSQIQRLIISREHLGK 378
CaiA COG1960
Acyl-CoA dehydrogenase related to the alkylation response protein AidB [Lipid transport and ...
 1-225 1.63e-94

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: 281.34  E-value: 1.63e-94
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 554506558   1 MWITNGGKANWYFLLARSDPDPKApanKAFTGFIVEADTPGIQIGRKELNMGQRCSDTRGIVFEDVKVPKENVLIGDGAG 80
Cdd:COG1960  154 TFITNAPVADVILVLARTDPAAGH---RGISLFLVPKDTPGVTVGRIEDKMGLRGSDTGELFFDDVRVPAENLLGEEGKG 230

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 554506558  81 FKVAMGAFDKTRPVVAAGAVGLAQRALDEATKYALERKTFGKLLVEHQAISFMLAEMAMKVELARMSYQRAAWEVDSGRR 160
Cdd:COG1960  231 FKIAMSTLNAGRLGLAAQALGIAEAALELAVAYAREREQFGRPIADFQAVQHRLADMAAELEAARALVYRAAWLLDAGED 310

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 554506558 161 NTYYASIAKAFAGDIANQLATDAVQILGGNGFNTEYPVEKLMRDAKIYQIYEGTSQIQRLIVARE 225
Cdd:COG1960  311 AALEAAMAKLFATEAALEVADEALQIHGGYGYTREYPLERLYRDARILTIYEGTNEIQRLIIARR 375
SCAD_SBCAD cd01158
Short chain acyl-CoA dehydrogenases and eukaryotic short/branched chain acyl-CoA ...
 1-229 7.25e-93

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: 276.84  E-value: 7.25e-93
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 554506558   1 MWITNGGKANWYFLLARSDPDPKapaNKAFTGFIVEADTPGIQIGRKELNMGQRCSDTRGIVFEDVKVPKENVLIGDGAG 80
Cdd:cd01158  149 MWITNGGEADFYIVFAVTDPSKG---YRGITAFIVERDTPGLSVGKKEDKLGIRGSSTTELIFEDVRVPKENILGEEGEG 225

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 554506558  81 FKVAMGAFDKTRPVVAAGAVGLAQRALDEATKYALERKTFGKLLVEHQAISFMLAEMAMKVELARMSYQRAAWEVDSGRR 160
Cdd:cd01158  226 FKIAMQTLDGGRIGIAAQALGIAQAALDAAVDYAKERKQFGKPIADFQGIQFKLADMATEIEAARLLTYKAARLKDNGEP 305

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 554506558 161 NTYYASIAKAFAGDIANQLATDAVQILGGNGFNTEYPVEKLMRDAKIYQIYEGTSQIQRLIVAReHIDK 229
Cdd:cd01158  306 FIKEAAMAKLFASEVAMRVTTDAVQIFGGYGYTKDYPVERYYRDAKITEIYEGTSEIQRLVIAK-HLLK 373
ACAD cd00567
Acyl-CoA dehydrogenase; Both mitochondrial acyl-CoA dehydrogenases (ACAD) and peroxisomal ...
 1-224 8.36e-93

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: 275.32  E-value: 8.36e-93
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 554506558   1 MWITNGGKANWYFLLARSDPDPkaPANKAFTGFIVEADTPGIQIGRKELNMGQRCSDTRGIVFEDVKVPKENVLIGDGAG 80
Cdd:cd00567  105 IFISNGGDADLFIVLARTDEEG--PGHRGISAFLVPADTPGVTVGRIWDKMGMRGSGTGELVFDDVRVPEDNLLGEEGGG 182

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 554506558  81 FKVAMGAFDKTRPVVAAGAVGLAQRALDEATKYALERKTFGKLLVEHQAISFMLAEMAMKVELARMSYQRAAWEVDSGRR 160
Cdd:cd00567  183 FELAMKGLNVGRLLLAAVALGAARAALDEAVEYAKQRKQFGKPLAEFQAVQFKLADMAAELEAARLLLYRAAWLLDQGPD 262

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 554506558 161 N-TYYASIAKAFAGDIANQLATDAVQILGGNGFNTEYPVEKLMRDAKIYQIYEGTSQIQRLIVAR 224
Cdd:cd00567  263 EaRLEAAMAKLFATEAAREVADLAMQIHGGRGYSREYPVERYLRDARAARIAEGTAEIQRLIIAR 327
IVD cd01156
Isovaleryl-CoA dehydrogenase; Isovaleryl-CoA dehydrogenase (IVD) is an is an acyl-CoA ...
 1-225 2.81e-65

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: 206.49  E-value: 2.81e-65
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 554506558   1 MWITNGGKANWYFLLARSDPDPKApanKAFTGFIVEADTPGIQIGRKELNMGQRCSDTRGIVFEDVKVPKENVLIGDGAG 80
Cdd:cd01156  152 MWITNGPDADTLVVYAKTDPSAGA---HGITAFIVEKGMPGFSRAQKLDKLGMRGSNTCELVFEDCEVPEENILGGENKG 228

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 554506558  81 FKVAMGAFDKTRPVVAAGAVGLAQRALDEATKYALERKTFGKLLVEHQAISFMLAEMAMKVELARMSYQRAAWEVDSGRR 160
Cdd:cd01156  229 VYVLMSGLDYERLVLAGGPIGIMQAALDVAIPYAHQRKQFGQPIGEFQLVQGKLADMYTRLNASRSYLYTVAKACDRGNM 308

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 554506558 161 NTYYASIAKAFAGDIANQLATDAVQILGGNGFNTEYPVEKLMRDAKIYQIYEGTSQIQRLIVARE 225
Cdd:cd01156  309 DPKDAAGVILYAAEKATQVALDAIQILGGNGYINDYPTGRLLRDAKLYEIGAGTSEIRRMVIGRE 373
IBD cd01162
Isobutyryl-CoA dehydrogenase; Isobutyryl-CoA dehydrogenase (IBD) catalyzes the alpha, beta- ...
 2-225 1.67e-60

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: 194.20  E-value: 1.67e-60
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 554506558   2 WITNGGKANWYFLLARSDpdpkAPANKAFTGFIVEADTPGIQIGRKELNMGQRCSDTRGIVFEDVKVPKENVLIGDGAGF 81
Cdd:cd01162  151 FISGAGDSDVYVVMARTG----GEGPKGISCFVVEKGTPGLSFGANEKKMGWNAQPTRAVIFEDCRVPVENRLGGEGQGF 226

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 554506558  82 KVAMGAFDKTRPVVAAGAVGLAQRALDEATKYALERKTFGKLLVEHQAISFMLAEMAMKVELARMSYQRAAWEVDSGRRN 161
Cdd:cd01162  227 GIAMAGLNGGRLNIASCSLGAAQAALDLARAYLEERKQFGKPLADFQALQFKLADMATELVASRLMVRRAASALDRGDPD 306

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 554506558 162 -TYYASIAKAFAGDIANQLATDAVQILGGNGFNTEYPVEKLMRDAKIYQIYEGTSQIQRLIVARE 225
Cdd:cd01162  307 aVKLCAMAKRFATDECFDVANQALQLHGGYGYLKDYPVEQYVRDLRVHQILEGTNEIMRLIIARA 371
LCAD cd01160
Long chain acyl-CoA dehydrogenase; LCAD is an acyl-CoA dehydrogenases (ACAD), which is found ...
 1-225 1.92e-60

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: 193.87  E-value: 1.92e-60
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 554506558   1 MWITNGGKANWYFLLARSDPDPKAPANKAFtgFIVEADTPGIQIGRKELNMGQRCSDTRGIVFEDVKVPKENVLIGDGAG 80
Cdd:cd01160  148 TFITNGMLADVVIVVARTGGEARGAGGISL--FLVERGTPGFSRGRKLKKMGWKAQDTAELFFDDCRVPAENLLGEENKG 225

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 554506558  81 FKVAMGAFDKTRPVVAAGAVGLAQRALDEATKYALERKTFGKLLVEHQAISFMLAEMAMKVELARMSYQRAAWEVDSGRR 160
Cdd:cd01160  226 FYYLMQNLPQERLLIAAGALAAAEFMLEETRNYVKQRKAFGKTLAQLQVVRHKIAELATKVAVTRAFLDNCAWRHEQGRL 305

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 554506558 161 NTYYASIAKAFAGDIANQLATDAVQILGGNGFNTEYPVEKLMRDAKIYQIYEGTSQIQRLIVARE 225
Cdd:cd01160  306 DVAEASMAKYWATELQNRVAYECVQLHGGWGYMREYPIARAYRDARVQPIYGGTTEIMKELISRQ 370
VLCAD cd01161
Very long chain acyl-CoA dehydrogenase; VLCAD is an acyl-CoA dehydrogenase (ACAD), which is ...
 2-223 2.98e-55

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: 181.51  E-value: 2.98e-55
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 554506558   2 WITNGGKANWYFLLARSD-PDPKAPANKAFTGFIVEADTPGIQIGRKELNMGQRCSDTRGIVFEDVKVPKENVLIGDGAG 80
Cdd:cd01161  177 WITNGGIADIFTVFAKTEvKDATGSVKDKITAFIVERSFGGVTNGPPEKKMGIKGSNTAEVYFEDVKIPVENVLGEVGDG 256

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 554506558  81 FKVAMGAFDKTRPVVAAGAVGLAQRALDEATKYALERKTFGKLLVEHQAISFMLAEMAMKVELARMSYQRAAWEVDSGRR 160
Cdd:cd01161  257 FKVAMNILNNGRFGMGAALIGTMKRCIEKAVDYANNRKQFGKKIHEFGLIQEKLANMAILQYATESMAYMTSGNMDRGLK 336

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 554506558 161 NTYY--ASIAKAFAGDIANQLATDAVQILGGNGFNTEYPVEKLMRDAKIYQIYEGTSQIQRLIVA 223
Cdd:cd01161  337 AEYQieAAISKVFASEAAWLVVDEAIQIHGGMGFMREYGVERVLRDLRIFRIFEGTNEILRLFIA 401
Acyl-CoA_dh_1 pfam00441
Acyl-CoA dehydrogenase, C-terminal domain; C-terminal domain of Acyl-CoA dehydrogenase is an ...
 78-224 4.53e-54

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


Pssm-ID: 395354 [Multi-domain]  Cd Length: 149  Bit Score: 170.51  E-value: 4.53e-54
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 554506558   78 GAGFKVAMGAFDKTRPVVAAGAVGLAQRALDEATKYALERKTFGKLLVEHQAISFMLAEMAMKVELARMSYQRAAWEVDS 157
Cdd:pfam00441   1 GRGFRVAMETLNHERLAIAAMALGLARRALDEALAYARRRKAFGRPLIDFQLVRHKLAEMAAEIEAARLLVYRAAEALDA 80

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 554506558  158 GRRNTYYASIAKAFAGDIANQLATDAVQILGGNGFNTEYPVEKLMRDAKIYQIYEGTSQIQRLIVAR 224
Cdd:pfam00441  81 GGPDGAEASMAKLYASEAAVEVADLAMQLHGGYGYLREYPVERLYRDARVLRIGEGTSEIQRNIIAR 147
PLN02519 PLN02519
isovaleryl-CoA dehydrogenase
 1-225 3.30e-52

isovaleryl-CoA dehydrogenase


Pssm-ID: 215284 [Multi-domain]  Cd Length: 404  Bit Score: 173.52  E-value: 3.30e-52
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 554506558   1 MWITNGGKANWYFLLARSDPdpkAPANKAFTGFIVEADTPGIQIGRKELNMGQRCSDTRGIVFEDVKVPKENVLIGDGAG 80
Cdd:PLN02519 178 MWCTNGPVAQTLVVYAKTDV---AAGSKGITAFIIEKGMPGFSTAQKLDKLGMRGSDTCELVFENCFVPEENVLGQEGKG 254

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 554506558  81 FKVAMGAFDKTRPVVAAGAVGLAQRALDEATKYALERKTFGKLLVEHQAISFMLAEMAMKVELARMSYQRAAWEVDSGRR 160
Cdd:PLN02519 255 VYVMMSGLDLERLVLAAGPLGLMQACLDVVLPYVRQREQFGRPIGEFQFIQGKLADMYTSLQSSRSYVYSVARDCDNGKV 334

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 554506558 161 NTYYASIAKAFAGDIANQLATDAVQILGGNGFNTEYPVEKLMRDAKIYQIYEGTSQIQRLIVARE 225
Cdd:PLN02519 335 DRKDCAGVILCAAERATQVALQAIQCLGGNGYINEYPTGRLLRDAKLYEIGAGTSEIRRMLIGRE 399
PRK12341 PRK12341
acyl-CoA dehydrogenase;
2-231 3.05e-43

acyl-CoA dehydrogenase;


Pssm-ID: 183454 [Multi-domain]  Cd Length: 381  Bit Score: 149.49  E-value: 3.05e-43
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 554506558   2 WITNGGKANWYFLLARsDPDPKAPaNKAFTGFIVEADTPGIQIGRKElNMGQRCSDTRGIVFEDVKVPKENVLIGDGAGF 81
Cdd:PRK12341 155 FITGAKEYPYMLVLAR-DPQPKDP-KKAFTLWWVDSSKPGIKINPLH-KIGWHMLSTCEVYLDNVEVEESDLVGEEGMGF 231

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 554506558  82 KVAMGAFDKTRPVVAAGAVGLAQRALDEATKYALERKTFGKLLVEHQAISFMLAEMAMKVELARMSYQRAAWEVDSGRRN 161
Cdd:PRK12341 232 LNVMYNFEMERLINAARSLGFAECAFEDAARYANQRIQFGKPIGHNQLIQEKLTLMAIKIENMRNMVYKVAWQADNGQSL 311

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 554506558 162 TYYASIAKAFAGDIANQLATDAVQILGGNGFNTEYPVEKLMRDAKIYQIYEGTSQIQRLIVAREHIDKYK 231
Cdd:PRK12341 312 RTSAALAKLYCARTAMEVIDDAIQIMGGLGYTDEARVSRFWRDVRCERIGGGTDEIMIYIAGRQILKDYQ 381
ACAD_fadE5 cd01153
Putative acyl-CoA dehydrogenases similar to fadE5; Putative acyl-CoA dehydrogenase (ACAD). ...
 1-218 1.39e-37

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: 135.21  E-value: 1.39e-37
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 554506558   1 MWITNGGKANW----YFLLARSDPDPkaPANKAFTGFIV-----EADTPGIQIGRKELNMGQRCSDTRGIVFEDVKVPke 71
Cdd:cd01153  154 RFISAGEHDMSenivHLVLARSEGAP--PGVKGLSLFLVpkfldDGERNGVTVARIEEKMGLHGSPTCELVFDNAKGE-- 229

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 554506558  72 nvLIGD-GAGFKVAMGAFDKTRPVVAAGAVGLAQRALDEATKYALERKTFGKLLVE--------HQAISFMLAEMAMKVE 142
Cdd:cd01153  230 --LIGEeGMGLAQMFAMMNGARLGVGTQGTGLAEAAYLNALAYAKERKQGGDLIKAapavtiihHPDVRRSLMTQKAYAE 307

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 554506558 143 LARMSYQRAAWEVDSGRR--------------NTYYASIAKAFAGDIANQLATDAVQILGGNGFNTEYPVEKLMRDAKIY 208
Cdd:cd01153  308 GSRALDLYTATVQDLAERkategedrkalsalADLLTPVVKGFGSEAALEAVSDAIQVHGGSGYTREYPIEQYYRDARIT 387

                        250
                 ....*....|
gi 554506558 209 QIYEGTSQIQ 218
Cdd:cd01153  388 TIYEGTTGIQ 397
PTZ00461 PTZ00461
isovaleryl-CoA dehydrogenase; Provisional
 2-214 1.49e-36

isovaleryl-CoA dehydrogenase; Provisional


Pssm-ID: 185640 [Multi-domain]  Cd Length: 410  Bit Score: 132.75  E-value: 1.49e-36
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 554506558   2 WITNGGKANWYFLLARSDpdpkapanKAFTGFIVEADTPGIQIGRKELNMGQRCSDTRGIVFEDVKVPKENVLIGDGAGF 81
Cdd:PTZ00461 189 WITNGTVADVFLIYAKVD--------GKITAFVVERGTKGFTQGPKIDKCGMRASHMCQLFFEDVVVPAENLLGEEGKGM 260

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 554506558  82 KVAMGAFDKTRPVVAAGAVGLAQRALDEATKYALERKTFGKLLVEHQAISFMLAEMAMKVELARMSYQRAAWEVDSGRRN 161
Cdd:PTZ00461 261 VGMMRNLELERVTLAAMAVGIAERSVELMTSYASERKAFGKPISNFGQIQRYIAEGYADTEAAKALVYSVSHNVHPGNKN 340

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|...
gi 554506558 162 TYYASIAKAFAGDIANQLATDAVQILGGNGFNTEYPVEKLMRDAKIYQIYEGT 214
Cdd:PTZ00461 341 RLGSDAAKLFATPIAKKVADSAIQVMGGMGYSRDMPVERLWRDAKLLEIGGGT 393
GCD cd01151
Glutaryl-CoA dehydrogenase; Glutaryl-CoA dehydrogenase (GCD). GCD is an acyl-CoA dehydrogenase, ...
 1-225 6.40e-36

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: 130.56  E-value: 6.40e-36
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 554506558   1 MWITNGGKANWYFLLARSDPDPKapankaFTGFIVEADTPGIQIGRKELNMGQRCSDTRGIVFEDVKVPKENVLIGdGAG 80
Cdd:cd01151  162 TWITNSPIADVFVVWARNDETGK------IRGFILERGMKGLSAPKIQGKFSLRASITGEIVMDNVFVPEENLLPG-AEG 234

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 554506558  81 FKVAMGAFDKTRPVVAAGAVGLAQRALDEATKYALERKTFGKLLVEHQAISFMLAEMAMKVELArmsyQRAAWEV----D 156
Cdd:cd01151  235 LRGPFKCLNNARYGIAWGALGAAEDCYHTARQYVLDRKQFGRPLAAFQLVQKKLADMLTEIALG----LLACLRVgrlkD 310

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 554506558 157 SGRRNTYYASIAKAFAGDIANQLATDAVQILGGNGFNTEYPVEKLMRDAKIYQIYEGTSQIQRLIVARE 225
Cdd:cd01151  311 QGKATPEQISLLKRNNCGKALEIARTAREMLGGNGISDEYHIIRHMVNLESVNTYEGTHDIHALILGRA 379
ACAD_fadE6_17_26 cd01152
Putative acyl-CoA dehydrogenases similar to fadE6, fadE17, and fadE26; Putative acyl-CoA ...
 2-224 6.64e-29

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: 111.67  E-value: 6.64e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 554506558   2 WITNGGK--------ANWYFLLARSDPDpkAPANKAFTGFIVEADTPGIQIgR--KELNMGqrcSDTRGIVFEDVKVPKE 71
Cdd:cd01152  146 WVVNGQKiwtsgahyADWAWLLVRTDPE--APKHRGISILLVDMDSPGVTV-RpiRSINGG---EFFNEVFLDDVRVPDA 219

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 554506558  72 NVLIGDGAGFKVAMGAFDKTRPVVAAGAVGLAQRALDeatkYALERKTFGKLLVEHQAISFMLAEMAMKVELARMSYQRA 151
Cdd:cd01152  220 NRVGEVNDGWKVAMTTLNFERVSIGGSAATFFELLLA----RLLLLTRDGRPLIDDPLVRQRLARLEAEAEALRLLVFRL 295

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 554506558 152 AWEVDSGRRNTYYASIAKAFAGDIANQLATDAVQILG--------GNGFNTEYPVEKLMRDAKIYQIYEGTSQIQRLIVA 223
Cdd:cd01152  296 ASALAAGKPPGAEASIAKLFGSELAQELAELALELLGtaallrdpAPGAELAGRWEADYLRSRATTIYGGTSEIQRNIIA 375


                 .
gi 554506558 224 R 224
Cdd:cd01152  376 E 376
PRK03354 PRK03354
crotonobetainyl-CoA dehydrogenase; Validated
 2-231 3.44e-27

crotonobetainyl-CoA dehydrogenase; Validated


Pssm-ID: 179566 [Multi-domain]  Cd Length: 380  Bit Score: 106.84  E-value: 3.44e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 554506558   2 WITNGGKANWYFLLARSDPDPKAPAnkaFTGFIVEADTPGIQIGRKElNMGQRCSDTRGIVFEDVKVPKENVLIGDGAGF 81
Cdd:PRK03354 155 FITSSAYTPYIVVMARDGASPDKPV---YTEWFVDMSKPGIKVTKLE-KLGLRMDSCCEITFDDVELDEKDMFGREGNGF 230

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 554506558  82 KVAMGAFDKTRPVVAAGAVGLAQRALDEATKYALERKTFGKLLVEHQAISFMLAEMAMKVELARMSYQRAAWEVDSGRRN 161
Cdd:PRK03354 231 NRVKEEFDHERFLVALTNYGTAMCAFEDAARYANQRVQFGEAIGRFQLIQEKFAHMAIKLNSMKNMLYEAAWKADNGTIT 310

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 554506558 162 TYYASIAKAFAGDIANQLATDAVQILGGNGFNTEYPVEKLMRDAKIYQIYEGTSQIQRLIVAREHIDKYK 231
Cdd:PRK03354 311 SGDAAMCKYFCANAAFEVVDSAMQVLGGVGIAGNHRISRFWRDLRVDRVSGGSDEMQILTLGRAVLKQYR 380
ACAD_FadE2 cd01155
Acyl-CoA dehydrogenases similar to fadE2; FadE2-like Acyl-CoA dehydrogenase (ACAD). Acyl-CoA ...
 2-224 4.97e-27

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: 106.71  E-value: 4.97e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 554506558   2 WITNGG--KANWYFLLARSDPDpKAPANKAFTGFIVEADTPGIQIGRKELNMGQrcSDTRG----IVFEDVKVPKENVLI 75
Cdd:cd01155  163 WSSGAGdpRCKIAIVMGRTDPD-GAPRHRQQSMILVPMDTPGVTIIRPLSVFGY--DDAPHghaeITFDNVRVPASNLIL 239

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 554506558  76 GDGAGFKVAMGAFDKTRPVVAAGAVGLAQRALDEATKYALERKTFGKLLVEHQAISFMLAEMAMKVELARMSYQRAAWEV 155
Cdd:cd01155  240 GEGRGFEIAQGRLGPGRIHHCMRLIGAAERALELMCQRAVSREAFGKKLAQHGVVAHWIAKSRIEIEQARLLVLKAAHMI 319

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 554506558 156 DSGRRNTYYASIA--KAFAGDIANQLATDAVQILGGNGFNTEYPVEKLMRDAKIYQIYEGTSQIQRLIVAR 224
Cdd:cd01155  320 DTVGNKAARKEIAmiKVAAPRMALKIIDRAIQVHGAAGVSQDTPLANMYAWARTLRIADGPDEVHLRSIAR 390
AidB cd01154
Proteins involved in DNA damage response, similar to the AidB gene product; AidB is one of ...
 41-224 3.07e-26

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: 104.76  E-value: 3.07e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 554506558  41 GIQIGRKELNMGQRCSDTRGIVFEDVkvpkENVLIGD-GAGFKVAMGAFDKTRPVVAAGAVGLAQRALDEATKYALERKT 119
Cdd:cd01154  226 GYRIRRLKDKLGTRSVATGEVEFDDA----EAYLIGDeGKGIYYILEMLNISRLDNAVAALGIMRRALSEAYHYARHRRA 301

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 554506558 120 FGKLLVEHQAISFMLAEMAMKVELARMSYQRAA--WEVDSGRRNTYYA------SIAKAFAGDIANQLATDAVQILGGNG 191
Cdd:cd01154  302 FGKPLIDHPLMRRDLAEMEVDVEAATALTFRAAraFDRAAADKPVEAHmarlatPVAKLIACKRAAPVTSEAMEVFGGNG 381

                        170       180       190
                 ....*....|....*....|....*....|...
gi 554506558 192 FNTEYPVEKLMRDAKIYQIYEGTSQIQRLIVAR 224
Cdd:cd01154  382 YLEEWPVARLHREAQVTPIWEGTGNIQALDVLR 414
PLN02526 PLN02526
acyl-coenzyme A oxidase
 2-225 1.85e-21

acyl-coenzyme A oxidase


Pssm-ID: 178141 [Multi-domain]  Cd Length: 412  Bit Score: 91.45  E-value: 1.85e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 554506558   2 WITNGGKANWYFLLARSDpdpkapANKAFTGFIVEADTPGIQIGRKELNMGQRCSDTRGIVFEDVKVPKENVLIGDGAgF 81
Cdd:PLN02526 179 WIGNSTFADVLVIFARNT------TTNQINGFIVKKGAPGLKATKIENKIGLRMVQNGDIVLKDVFVPDEDRLPGVNS-F 251

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 554506558  82 KVAMGAFDKTRPVVAAGAVGLAQRALDEATKYALERKTFGKLLVEHQAISFMLAEMAMKVELARMSYQRAAWEVDSGRRN 161
Cdd:PLN02526 252 QDTNKVLAVSRVMVAWQPIGISMGVYDMCHRYLKERKQFGAPLAAFQINQEKLVRMLGNIQAMFLVGWRLCKLYESGKMT 331

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 554506558 162 TYYASIAKAFAGDIANQLATDAVQILGGNGFNTEYPVEKLMRDAKIYQIYEGTSQIQRLIVARE 225
Cdd:PLN02526 332 PGHASLGKAWITKKARETVALGRELLGGNGILADFLVAKAFCDLEPIYTYEGTYDINALVTGRE 395
PLN02876 PLN02876
acyl-CoA dehydrogenase
 21-217 2.40e-21

acyl-CoA dehydrogenase


Pssm-ID: 215473 [Multi-domain]  Cd Length: 822  Bit Score: 92.17  E-value: 2.40e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 554506558  21 DPKAPANKAFTGFIVEADTPGIQIGRKELNMGqrCSDT----RGIVFEDVKVPKENVLIGDGAGFKVAMGAFDKTRPVVA 96
Cdd:PLN02876 607 DFNAPKHKQQSMILVDIQTPGVQIKRPLLVFG--FDDAphghAEISFENVRVPAKNILLGEGRGFEIAQGRLGPGRLHHC 684

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 554506558  97 AGAVGLAQRALDEATKYALERKTFGKLLVEHQAISFMLAEMAMKVELARMSYQRAAWEVD--SGRRNTYYASIAKAFAGD 174
Cdd:PLN02876 685 MRLIGAAERGMQLMVQRALSRKAFGKLIAQHGSFLSDLAKCRVELEQTRLLVLEAADQLDrlGNKKARGIIAMAKVAAPN 764

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|...
gi 554506558 175 IANQLATDAVQILGGNGFNTEYPVEKLMRDAKIYQIYEGTSQI 217
Cdd:PLN02876 765 MALKVLDMAMQVHGAAGVSSDTVLAHLWATARTLRIADGPDEV 807
Acyl-CoA_dh_2 pfam08028
Acyl-CoA dehydrogenase, C-terminal domain;
94-216 2.02e-18

Acyl-CoA dehydrogenase, C-terminal domain;


Pssm-ID: 429790 [Multi-domain]  Cd Length: 133  Bit Score: 78.16  E-value: 2.02e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 554506558   94 VVAAGAVGLAQRALDEATKYALERKT--FGKLLVEHQAISFMLAEMAMKVELARMSYQRAAWE----VDSGRRNTYY--- 164
Cdd:pfam08028   1 GIAAAALGAARAALAEFTERARGRVRayFGVPLAEDPATQLALAEAAARIDAARLLLERAAARieaaAAAGKPVTPAlra 80

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|...
gi 554506558  165 -ASIAKAFAGDIANQLATDAVQILGGNGFNTEYPVEKLMRDAKIYQIYEGTSQ 216
Cdd:pfam08028  81 eARRAAAFATELAVAAVDALFRAAGGSALFQDSPLQRIWRDIHAAAQHAAVNP 133
Acyl-CoA_dh_M pfam02770
Acyl-CoA dehydrogenase, middle domain; Central domain of Acyl-CoA dehydrogenase has a ...
 1-64 8.94e-12

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: 59.60  E-value: 8.94e-12
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 554506558    1 MWITNGGKANWYFLLARSDPDPKApanKAFTGFIVEADTPGIQIGRKELNMGQRCSDTRGIVFE 64
Cdd:pfam02770  35 WWITNAGIADLFLVLARTGGDDRH---GGISLFLVPKDAPGVSVRRIETKLGVRGLPTGELVFD 95
PRK11561 PRK11561
isovaleryl CoA dehydrogenase; Provisional
 76-224 1.21e-10

isovaleryl CoA dehydrogenase; Provisional


Pssm-ID: 183199 [Multi-domain]  Cd Length: 538  Bit Score: 60.54  E-value: 1.21e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 554506558  76 GDGAGFKVAMGAFdkTRPVVAAGAVGLAQRALDEATKYALERKTFGKLLVEHQAISFMLAEMAMKVE--------LARMS 147
Cdd:PRK11561 285 GEGIRLILKMGGM--TRFDCALGSHGLMRRAFSVAIYHAHQRQVFGKPLIEQPLMRQVLSRMALQLEgqtallfrLARAW 362

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 554506558 148 YQRA-AWEVDSGRRNTYYA--SIAKAFAGDIAnqlatDAVQILGGNGFNTEYPVEKLMRDAKIYQIYEGTSQIQRLIVAR 224
Cdd:PRK11561 363 DRRAdAKEALWARLFTPAAkfVICKRGIPFVA-----EAMEVLGGIGYCEESELPRLYREMPVNSIWEGSGNIMCLDVLR 437
PTZ00456 PTZ00456
acyl-CoA dehydrogenase; Provisional
 12-220 2.81e-08

acyl-CoA dehydrogenase; Provisional


Pssm-ID: 185635 [Multi-domain]  Cd Length: 622  Bit Score: 53.72  E-value: 2.81e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 554506558  12 YFLLARSDPDPkaPANKAFTGFIVEADTP----------GIQIGRKELNMGQRCSDTRGIVFEDVKvpkeNVLIGD-GAG 80
Cdd:PTZ00456 233 HIVLARLPNSL--PTTKGLSLFLVPRHVVkpdgsletakNVKCIGLEKKMGIKGSSTCQLSFENSV----GYLIGEpNAG 306

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 554506558  81 FKVAMGAFDKTRPVVAAGAVGLAQRALDEATKYALERKTF------------GKLLVEHQAISFML------AE--MAMK 140
Cdd:PTZ00456 307 MKQMFTFMNTARVGTALEGVCHAELAFQNALRYARERRSMralsgtkepekpADRIICHANVRQNIlfakavAEggRALL 386

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 554506558 141 VELAR-MSYQRAAWEVDS----GRRNTYYASIAKAFAGDIANQLATDAVQILGGNGFNTEYPVEKLMRDAKIYQIYEGTS 215
Cdd:PTZ00456 387 LDVGRlLDIHAAAKDAATrealDHEIGFYTPIAKGCLTEWGVEAASRCLQVWGGHGYIKGNGMEQILRDARIGTLYEGTT 466


                 ....*
gi 554506558 216 QIQRL 220
Cdd:PTZ00456 467 GIQAL 471
NcnH cd01159
Naphthocyclinone hydroxylase; Naphthocyclinone is an aromatic polyketide and an antibiotic, ...
 9-205 4.50e-07

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: 49.65  E-value: 4.50e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 554506558   9 ANWYFLLARSDPDPKAPANKAFTgfIVEADtpgIQIGRKELNMGQRCSDTRGIVFEDVKVPKENVLIGDGA--------- 79
Cdd:cd01159  135 ADWILVGAIVEDDDGGPLPRAFV--VPRAE---YEIVDTWHVVGLRGTGSNTVVVDDVFVPEHRTLTAGDMmagdgpggs 209

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 554506558  80 --GFKVAMGAFDKtrPVVAAGAVGLAQRALDEATKYALER---KTFGKLLVEHQAISFMLAEMAMKVELARMSYQRAAWE 154
Cdd:cd01159  210 tpVYRMPLRQVFP--LSFAAVSLGAAEGALAEFLELAGKRvrqYGAAVKMAEAPITQLRLAEAAAELDAARAFLERATRD 287

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 554506558 155 VDS---------------GRRNTYYASIAKAFAGDIANQLAtdavqilGGNGFNTEYPVEKLMRDA 205
Cdd:cd01159  288 LWAhalaggpidveerarIRRDAAYAAKLSAEAVDRLFHAA-------GGSALYTASPLQRIWRDI 346
DszC cd01163
Dibenzothiophene (DBT) desulfurization enzyme C; DszC is a flavin reductase dependent enzyme, ...
 31-206 2.84e-05

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: 44.24  E-value: 2.84e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 554506558  31 TGFIVEADTPGIQIGRKELNMGQRCSDTRGIVFEDVKVPKENVLIGDGAGFKVAM-GAFDKTrpVVAAGAVGLAQRALDE 109
Cdd:cd01163  161 VFAAVPTDRPGITVVDDWDGFGQRLTASGTVTFDNVRVEPDEVLPRPNAPDRGTLlTAIYQL--VLAAVLAGIARAALDD 238

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 554506558 110 ATKYALER-KTFGKLLVEH--------QAIsfmlAEMAMKVELARMSYQRAAWEVD----SGRRNTYYASI--------A 168
Cdd:cd01163  239 AVAYVRSRtRPWIHSGAESarddpyvqQVV----GDLAARLHAAEALVLQAARALDaaaaAGTALTAEARGeaalavaaA 314

                        170       180       190
                 ....*....|....*....|....*....|....*...
gi 554506558 169 KAFAGDIANQLATDAVQILGGNGFNTEYPVEKLMRDAK 206
Cdd:cd01163  315 KVVVTRLALDATSRLFEVGGASATAREHNLDRHWRNAR 352
AXO cd01150
Peroxisomal acyl-CoA oxidase; Peroxisomal acyl-CoA oxidases (AXO) catalyze the first set in ...
 32-231 1.57e-04

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: 42.32  E-value: 1.57e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 554506558  32 GFIV---EADT----PGIQIGRKELNMGQRCSDTRGIVFEDVKVPKENVL------IGDGA----------GFKVAMGAF 88
Cdd:cd01150  206 AFIVpirDPKThqplPGVTVGDIGPKMGLNGVDNGFLQFRNVRIPRENLLnrfgdvSPDGTyvspfkdpnkRYGAMLGTR 285

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 554506558  89 DKTRPVVAAGAVGLAQRALDEATKYALERKTFG--------KLLvEHQ--------------AISFMLAEMAMK-VELAR 145
Cdd:cd01150  286 SGGRVGLIYDAAMSLKKAATIAIRYSAVRRQFGpkpsdpevQIL-DYQlqqyrlfpqlaaayAFHFAAKSLVEMyHEIIK 364

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 554506558 146 MSYQRAAwevDSGRRNTYYASIAKAFAGDIANQLATDAVQILGGNGFNTEYPVEKLMRDAKIYQIYEGTSQIQRLIVARE 225
Cdd:cd01150  365 ELLQGNS---ELLAELHALSAGLKAVATWTAAQGIQECREACGGHGYLAMNRLPTLRDDNDPFCTYEGDNTVLLQQTANY 441


                 ....*.
gi 554506558 226 HIDKYK 231
Cdd:cd01150  442 LLKKYA 447
fadE PRK09463
acyl-CoA dehydrogenase; Reviewed
 35-191 1.78e-03

acyl-CoA dehydrogenase; Reviewed


Pssm-ID: 236528 [Multi-domain]  Cd Length: 777  Bit Score: 39.03  E-value: 1.78e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 554506558  35 VEADTPGIQIGRKELNMGQRCSD--TRGivfEDVKVPKENVlIGD----GAGFKVAMGAFDKTR----PVVAAGAVGLAQ 104
Cdd:PRK09463 274 IPTDTPGVEIGRRHFPLNVPFQNgpTRG---KDVFIPLDYI-IGGpkmaGQGWRMLMECLSVGRgislPSNSTGGAKLAA 349

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 554506558 105 RAldeATKYALERKTFGKLLVEHQAISFMLAEMAMKvelarmsyqraAWEVDSGRRNTYYA-----------SIAKAFAG 173
Cdd:PRK09463 350 LA---TGAYARIRRQFKLPIGKFEGIEEPLARIAGN-----------AYLMDAARTLTTAAvdlgekpsvlsAIAKYHLT 415

                        170
                 ....*....|....*...
gi 554506558 174 DIANQLATDAVQILGGNG 191
Cdd:PRK09463 416 ERGRQVINDAMDIHGGKG 433
 
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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