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Conserved domains on  [gi|1734321320|ref|NP_001360428|]
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Acyl-CoA_dh_N domain-containing protein [Caenorhabditis elegans]

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 ...
 38-261 4.26e-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)


The actual alignment was detected with superfamily member cd01158:

Pssm-ID: 447864 [Multi-domain]  Cd Length: 373  Bit Score: 279.15  E-value: 4.26e-93
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1734321320  38 ENEKKLVEKVKNFAQSSVKPLVREMDRDARINKQLLKKAFDLKLMGLKIDPKYGGSGVSFFELVLAVEELSKIDPAIALI 117
Cdd:cd01158     1 EEHQMIRKTVRDFAEKEIAPLAAEMDEKGEFPREVIKEMAELGLMGIPIPEEYGGAGLDFLAYAIAIEELAKVDASVAVI 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1734321320 118 MHLQNALVAPLIEEFGNEELKEKYLKKLCK-DSVGAFALSEVVSGSDAFAMQTVAKKDGDHFILNGSKWGISNAPIADFF 196
Cdd:cd01158    81 VSVHNSLGANPIIKFGTEEQKKKYLPPLATgEKIGAFALSEPGAGSDAAALKTTAKKDGDDYVLNGSKMWITNGGEADFY 160

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1734321320 197 LVLANADPEKGYRGVTCFIVDRDHEGVVLGEQDDNLGMRAGTIAQVHLNSVRVPKTSIVGEYGKG 261
Cdd:cd01158   161 IVFAVTDPSKGYRGITAFIVERDTPGLSVGKKEDKLGIRGSSTTELIFEDVRVPKENILGEEGEG 225
 
Name Accession Description Interval E-value
SCAD_SBCAD cd01158
Short chain acyl-CoA dehydrogenases and eukaryotic short/branched chain acyl-CoA ...
 38-261 4.26e-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: 279.15  E-value: 4.26e-93
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1734321320  38 ENEKKLVEKVKNFAQSSVKPLVREMDRDARINKQLLKKAFDLKLMGLKIDPKYGGSGVSFFELVLAVEELSKIDPAIALI 117
Cdd:cd01158     1 EEHQMIRKTVRDFAEKEIAPLAAEMDEKGEFPREVIKEMAELGLMGIPIPEEYGGAGLDFLAYAIAIEELAKVDASVAVI 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1734321320 118 MHLQNALVAPLIEEFGNEELKEKYLKKLCK-DSVGAFALSEVVSGSDAFAMQTVAKKDGDHFILNGSKWGISNAPIADFF 196
Cdd:cd01158    81 VSVHNSLGANPIIKFGTEEQKKKYLPPLATgEKIGAFALSEPGAGSDAAALKTTAKKDGDDYVLNGSKMWITNGGEADFY 160

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1734321320 197 LVLANADPEKGYRGVTCFIVDRDHEGVVLGEQDDNLGMRAGTIAQVHLNSVRVPKTSIVGEYGKG 261
Cdd:cd01158   161 IVFAVTDPSKGYRGITAFIVERDTPGLSVGKKEDKLGIRGSSTTELIFEDVRVPKENILGEEGEG 225
CaiA COG1960
Acyl-CoA dehydrogenase related to the alkylation response protein AidB [Lipid transport and ...
 35-261 3.77e-84

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: 256.69  E-value: 3.77e-84
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1734321320  35 HLNENEKKLVEKVKNFAQSSVKPLVREMDRDARINKQLLKKAFDLKLMGLKIDPKYGGSGVSFFELVLAVEELSKIDPAI 114
Cdd:COG1960     4 ELTEEQRALRDEVREFAEEEIAPEAREWDREGEFPRELWRKLAELGLLGLTIPEEYGGLGLSLVELALVLEELARADASL 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1734321320 115 ALIMHLQNAlVAPLIEEFGNEELKEKYLKKLCK-DSVGAFALSEVVSGSDAFAMQTVAKKDGDHFILNGSKWGISNAPIA 193
Cdd:COG1960    84 ALPVGVHNG-AAEALLRFGTEEQKERYLPRLASgEWIGAFALTEPGAGSDAAALRTTAVRDGDGYVLNGQKTFITNAPVA 162

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1734321320 194 DFFLVLANADPEKGYRGVTCFIVDRDHEGVVLGEQDDNLGMRAGTIAQVHLNSVRVPKTSIVGEYGKG 261
Cdd:COG1960   163 DVILVLARTDPAAGHRGISLFLVPKDTPGVTVGRIEDKMGLRGSDTGELFFDDVRVPAENLLGEEGKG 230
PTZ00461 PTZ00461
isovaleryl-CoA dehydrogenase; Provisional
 41-261 1.16e-37

isovaleryl-CoA dehydrogenase; Provisional


Pssm-ID: 185640 [Multi-domain]  Cd Length: 410  Bit Score: 136.99  E-value: 1.16e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1734321320  41 KKLVEKVKNFAQSSVKPLVREMDRDARINKQLLKKAFDLKLMGLKIDPKYGGSGVSFFELVLAVEELSKIDPAIALIMHL 120
Cdd:PTZ00461   42 AALRETVAKFSREVVDKHAREDDINMHFNRDLFKQLGDLGVMGVTVPEADGGAGMDAVAAVIIHHELSKYDPGFCLAYLA 121

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1734321320 121 QNALVAPLIEEFGNEELKEKYLKK-LCKDSVGAFALSEVVSGSDAFAMQTVAKKDGD-HFILNGSKWGISNAPIADFFLV 198
Cdd:PTZ00461  122 HSMLFVNNFYYSASPAQRARWLPKvLTGEHVGAMGMSEPGAGTDVLGMRTTAKKDSNgNYVLNGSKIWITNGTVADVFLI 201

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1734321320 199 LANADPEkgyrgVTCFIVDRDHEGVVLGEQDDNLGMRAGTIAQVHLNSVRVPKTSIVGEYGKG 261
Cdd:PTZ00461  202 YAKVDGK-----ITAFVVERGTKGFTQGPKIDKCGMRASHMCQLFFEDVVVPAENLLGEEGKG 259
Acyl-CoA_dh_N pfam02771
Acyl-CoA dehydrogenase, N-terminal domain; The N-terminal domain of Acyl-CoA dehydrogenase is ...
 37-147 2.85e-34

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: 119.88  E-value: 2.85e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1734321320  37 NENEKKLVEKVKNFAQSSVKPLVREMDRDARINKQLLKKAFDLKLMGLKIDPKYGGSGVSFFELVLAVEELSKIDPAIAL 116
Cdd:pfam02771   1 TEEQEALRDTVREFAEEEIAPHAAEWDEEGEFPRELWKKLGELGLLGITIPEEYGGAGLDYLAYALVAEELARADASVAL 80

                          90       100       110
                  ....*....|....*....|....*....|.
gi 1734321320 117 IMHLQNALVAPLIEEFGNEELKEKYLKKLCK 147
Cdd:pfam02771  81 ALSVHSSLGAPPILRFGTEEQKERYLPKLAS 111
 
Name Accession Description Interval E-value
SCAD_SBCAD cd01158
Short chain acyl-CoA dehydrogenases and eukaryotic short/branched chain acyl-CoA ...
 38-261 4.26e-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: 279.15  E-value: 4.26e-93
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1734321320  38 ENEKKLVEKVKNFAQSSVKPLVREMDRDARINKQLLKKAFDLKLMGLKIDPKYGGSGVSFFELVLAVEELSKIDPAIALI 117
Cdd:cd01158     1 EEHQMIRKTVRDFAEKEIAPLAAEMDEKGEFPREVIKEMAELGLMGIPIPEEYGGAGLDFLAYAIAIEELAKVDASVAVI 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1734321320 118 MHLQNALVAPLIEEFGNEELKEKYLKKLCK-DSVGAFALSEVVSGSDAFAMQTVAKKDGDHFILNGSKWGISNAPIADFF 196
Cdd:cd01158    81 VSVHNSLGANPIIKFGTEEQKKKYLPPLATgEKIGAFALSEPGAGSDAAALKTTAKKDGDDYVLNGSKMWITNGGEADFY 160

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1734321320 197 LVLANADPEKGYRGVTCFIVDRDHEGVVLGEQDDNLGMRAGTIAQVHLNSVRVPKTSIVGEYGKG 261
Cdd:cd01158   161 IVFAVTDPSKGYRGITAFIVERDTPGLSVGKKEDKLGIRGSSTTELIFEDVRVPKENILGEEGEG 225
CaiA COG1960
Acyl-CoA dehydrogenase related to the alkylation response protein AidB [Lipid transport and ...
 35-261 3.77e-84

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: 256.69  E-value: 3.77e-84
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1734321320  35 HLNENEKKLVEKVKNFAQSSVKPLVREMDRDARINKQLLKKAFDLKLMGLKIDPKYGGSGVSFFELVLAVEELSKIDPAI 114
Cdd:COG1960     4 ELTEEQRALRDEVREFAEEEIAPEAREWDREGEFPRELWRKLAELGLLGLTIPEEYGGLGLSLVELALVLEELARADASL 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1734321320 115 ALIMHLQNAlVAPLIEEFGNEELKEKYLKKLCK-DSVGAFALSEVVSGSDAFAMQTVAKKDGDHFILNGSKWGISNAPIA 193
Cdd:COG1960    84 ALPVGVHNG-AAEALLRFGTEEQKERYLPRLASgEWIGAFALTEPGAGSDAAALRTTAVRDGDGYVLNGQKTFITNAPVA 162

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1734321320 194 DFFLVLANADPEKGYRGVTCFIVDRDHEGVVLGEQDDNLGMRAGTIAQVHLNSVRVPKTSIVGEYGKG 261
Cdd:COG1960   163 DVILVLARTDPAAGHRGISLFLVPKDTPGVTVGRIEDKMGLRGSDTGELFFDDVRVPAENLLGEEGKG 230
IVD cd01156
Isovaleryl-CoA dehydrogenase; Isovaleryl-CoA dehydrogenase (IVD) is an is an acyl-CoA ...
 35-261 2.07e-63

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: 203.41  E-value: 2.07e-63
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1734321320  35 HLNENEKKLVEKVKNFAQSSVKPLVREMDRDARINKQLLKKAFDLKLMGLKIDPKYGGSGVSFFELVLAVEELSKIDPAI 114
Cdd:cd01156     1 GLDDEIEMLRQSVREFAQKEIAPLAAKIDRDNEFPRDLWRKMGKLGLLGITAPEEYGGSGMGYLAHVIIMEEISRASGSV 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1734321320 115 ALIMHLQNALVAPLIEEFGNEELKEKYLKKLCK-DSVGAFALSEVVSGSDAFAMQTVAKKDGDHFILNGSKWGISNAPIA 193
Cdd:cd01156    81 ALSYGAHSNLCINQIYRNGSAAQKEKYLPKLISgEHIGALAMSEPNAGSDVVSMKLRAEKKGDRYVLNGSKMWITNGPDA 160

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1734321320 194 DFFLVLANADPEKGYRGVTCFIVDRDHEGVVLGEQDDNLGMRAGTIAQVHLNSVRVPKTSIVGEYGKG 261
Cdd:cd01156   161 DTLVVYAKTDPSAGAHGITAFIVEKGMPGFSRAQKLDKLGMRGSNTCELVFEDCEVPEENILGGENKG 228
ACAD cd00567
Acyl-CoA dehydrogenase; Both mitochondrial acyl-CoA dehydrogenases (ACAD) and peroxisomal ...
 38-261 1.52e-47

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: 160.91  E-value: 1.52e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1734321320  38 ENEKKLVEKVKNFAQSSVKPLVREMDRDARINKQLLKKafdlklMGLkidpkyggsgvsffelvlaveelskidpaiali 117
Cdd:cd00567     1 EEQRELRDSAREFAAEELEPYARERRETPEEPWELLAE------LGL--------------------------------- 41

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1734321320 118 mhlqnALVAPLIEEFGNEELKEKYLKKLCKDS-VGAFALSEVVSGSDAFAMQTVAKKDGDHFILNGSKWGISNAPIADFF 196
Cdd:cd00567    42 -----LLGAALLLAYGTEEQKERYLPPLASGEaIAAFALTEPGAGSDLAGIRTTARKDGDGYVLNGRKIFISNGGDADLF 116

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1734321320 197 LVLANADPE-KGYRGVTCFIVDRDHEGVVLGEQDDNLGMRAGTIAQVHLNSVRVPKTSIVGEYGKG 261
Cdd:cd00567   117 IVLARTDEEgPGHRGISAFLVPADTPGVTVGRIWDKMGMRGSGTGELVFDDVRVPEDNLLGEEGGG 182
IBD cd01162
Isobutyryl-CoA dehydrogenase; Isobutyryl-CoA dehydrogenase (IBD) catalyzes the alpha, beta- ...
 36-261 1.91e-45

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: 156.83  E-value: 1.91e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1734321320  36 LNENEKKLVEKVKNFAQSSVKPLVREMDRDARINKQLLKKAFDLKLMGLKIDPKYGGSGVSFFELVLAVEELSKIDPAIA 115
Cdd:cd01162     1 LNEEQRAIQEVARAFAAKEMAPHAADWDQKKHFPVDVLRKAAELGFGGIYIRDDVGGSGLSRLDASIIFEALSTGCVSTA 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1734321320 116 LIMHLQNaLVAPLIEEFGNEELKEKYLKKLCK-DSVGAFALSEVVSGSDAFAMQTVAKKDGDHFILNGSKWGISNAPIAD 194
Cdd:cd01162    81 AYISIHN-MCAWMIDSFGNDEQRERFLPDLCTmEKLASYCLTEPGSGSDAAALRTRAVREGDHYVLNGSKAFISGAGDSD 159

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1734321320 195 FFLVLANADpEKGYRGVTCFIVDRDHEGVVLGEQDDNLGMRAGTIAQVHLNSVRVPKTSIVGEYGKG 261
Cdd:cd01162   160 VYVVMARTG-GEGPKGISCFVVEKGTPGLSFGANEKKMGWNAQPTRAVIFEDCRVPVENRLGGEGQG 225
GCD cd01151
Glutaryl-CoA dehydrogenase; Glutaryl-CoA dehydrogenase (GCD). GCD is an acyl-CoA dehydrogenase, ...
 32-251 1.35e-44

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: 154.82  E-value: 1.35e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1734321320  32 PLQH---LNENEKKLVEKVKNFAQSSVKPLVREMDRDARINKQLLKKAFDLKLMGLKIDpKYGGSGVSFFELVLAVEELS 108
Cdd:cd01151     6 PLNLddlLTEEERAIRDTAREFCQEELAPRVLEAYREEKFDRKIIEEMGELGLLGATIK-GYGCAGLSSVAYGLIAREVE 84

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1734321320 109 KIDPAIALIMHLQNALVAPLIEEFGNEELKEKYLKKLCK-DSVGAFALSEVVSGSDAFAMQTVAKKDGDHFILNGSKWGI 187
Cdd:cd01151    85 RVDSGYRSFMSVQSSLVMLPIYDFGSEEQKQKYLPKLASgELIGCFGLTEPNHGSDPGGMETRARKDGGGYKLNGSKTWI 164

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1734321320 188 SNAPIADFFLVLANADPEKGYRGvtcFIVDRDHEGVVLGEQDDNLGMRAGTIAQVHLNSVRVPK 251
Cdd:cd01151   165 TNSPIADVFVVWARNDETGKIRG---FILERGMKGLSAPKIQGKFSLRASITGEIVMDNVFVPE 225
VLCAD cd01161
Very long chain acyl-CoA dehydrogenase; VLCAD is an acyl-CoA dehydrogenase (ACAD), which is ...
 20-261 7.50e-42

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: 148.00  E-value: 7.50e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1734321320  20 GSISAQQqprVFPL-----QHLNENEKKLVEKVKNFAQSSVKPlvREMDRDARINKQLLKKAFDLKLMGLKIDPKYGGSG 94
Cdd:cd01161     9 GDIVTKQ---VFPYpsvltEEQTEELNMLVGPVEKFFEEVNDP--AKNDQLEKIPRKTLTQLKELGLFGLQVPEEYGGLG 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1734321320  95 VSFFELVLAVEELSkIDPAIALIMHLQNALVAPLIEEFGNEELKEKYLKKLCK-DSVGAFALSEVVSGSDAFAMQTVAKK 173
Cdd:cd01161    84 LNNTQYARLAEIVG-MDLGFSVTLGAHQSIGFKGILLFGTEAQKEKYLPKLASgEWIAAFALTEPSSGSDAASIRTTAVL 162

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1734321320 174 --DGDHFILNGSKWGISNAPIADFFLVLAN-----ADPEKGyRGVTCFIVDRDHEGVVLGEQDDNLGMRAGTIAQVHLNS 246
Cdd:cd01161   163 seDGKHYVLNGSKIWITNGGIADIFTVFAKtevkdATGSVK-DKITAFIVERSFGGVTNGPPEKKMGIKGSNTAEVYFED 241

                         250
                  ....*....|....*
gi 1734321320 247 VRVPKTSIVGEYGKG 261
Cdd:cd01161   242 VKIPVENVLGEVGDG 256
LCAD cd01160
Long chain acyl-CoA dehydrogenase; LCAD is an acyl-CoA dehydrogenases (ACAD), which is found ...
 47-261 1.90e-40

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: 143.41  E-value: 1.90e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1734321320  47 VKNFAQSSVKPLVREMDRDARINKQLLKKAFDLKLMGLKIDPKYGGSGVSFFELVLAVEELSKID-PAIALIMHlqNALV 125
Cdd:cd01160    10 VRRFFAKEVAPFHHEWEKAGEVPREVWRKAGEQGLLGVGFPEEYGGIGGDLLSAAVLWEELARAGgSGPGLSLH--TDIV 87

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1734321320 126 APLIEEFGNEELKEKYLKKLCK-DSVGAFALSEVVSGSDAFAMQTVAKKDGDHFILNGSKWGISNAPIADFFLVLANADP 204
Cdd:cd01160    88 SPYITRAGSPEQKERVLPQMVAgKKIGAIAMTEPGAGSDLQGIRTTARKDGDHYVLNGSKTFITNGMLADVVIVVARTGG 167

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1734321320 205 E-KGYRGVTCFIVDRDHEGVVLGEQDDNLGMRAGTIAQVHLNSVRVPKTSIVGEYGKG 261
Cdd:cd01160   168 EaRGAGGISLFLVERGTPGFSRGRKLKKMGWKAQDTAELFFDDCRVPAENLLGEENKG 225
PTZ00461 PTZ00461
isovaleryl-CoA dehydrogenase; Provisional
 41-261 1.16e-37

isovaleryl-CoA dehydrogenase; Provisional


Pssm-ID: 185640 [Multi-domain]  Cd Length: 410  Bit Score: 136.99  E-value: 1.16e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1734321320  41 KKLVEKVKNFAQSSVKPLVREMDRDARINKQLLKKAFDLKLMGLKIDPKYGGSGVSFFELVLAVEELSKIDPAIALIMHL 120
Cdd:PTZ00461   42 AALRETVAKFSREVVDKHAREDDINMHFNRDLFKQLGDLGVMGVTVPEADGGAGMDAVAAVIIHHELSKYDPGFCLAYLA 121

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1734321320 121 QNALVAPLIEEFGNEELKEKYLKK-LCKDSVGAFALSEVVSGSDAFAMQTVAKKDGD-HFILNGSKWGISNAPIADFFLV 198
Cdd:PTZ00461  122 HSMLFVNNFYYSASPAQRARWLPKvLTGEHVGAMGMSEPGAGTDVLGMRTTAKKDSNgNYVLNGSKIWITNGTVADVFLI 201

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1734321320 199 LANADPEkgyrgVTCFIVDRDHEGVVLGEQDDNLGMRAGTIAQVHLNSVRVPKTSIVGEYGKG 261
Cdd:PTZ00461  202 YAKVDGK-----ITAFVVERGTKGFTQGPKIDKCGMRASHMCQLFFEDVVVPAENLLGEEGKG 259
MCAD cd01157
Medium chain acyl-CoA dehydrogenase; MCADs are mitochondrial beta-oxidation enzymes, which ...
 36-261 4.87e-36

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: 131.94  E-value: 4.87e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1734321320  36 LNENEKKLVEKVKNFAQSSVKPLVREMDRDARINKQLLKKAFDLKLMGLKIDPKYGGSGVSFFELVLAVEELSKIDPAIA 115
Cdd:cd01157     1 LTEQQKEFQETARKFAREEIIPVAAEYDKSGEYPWPLIKRAWELGLMNTHIPEDCGGLGLGTFDTCLITEELAYGCTGVQ 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1734321320 116 LIMHLQNALVAPLIEEfGNEELKEKYLKKLCKDS-VGAFALSEVVSGSDAFAMQTVAKKDGDHFILNGSKWGISNAPIAD 194
Cdd:cd01157    81 TAIEANSLGQMPVIIS-GNDEQKKKYLGRMTEEPlMCAYCVTEPGAGSDVAGIKTKAEKKGDEYIINGQKMWITNGGKAN 159

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1734321320 195 FFLVLANADPE---KGYRGVTCFIVDRDHEGVVLGEQDDNLGMRAGTIAQVHLNSVRVPKTSIVGEYGKG 261
Cdd:cd01157   160 WYFLLARSDPDpkcPASKAFTGFIVEADTPGIQPGRKELNMGQRCSDTRGITFEDVRVPKENVLIGEGAG 229
PLN02519 PLN02519
isovaleryl-CoA dehydrogenase
 36-261 8.64e-36

isovaleryl-CoA dehydrogenase


Pssm-ID: 215284 [Multi-domain]  Cd Length: 404  Bit Score: 131.92  E-value: 8.64e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1734321320  36 LNENEKKLVEKVKNFAQSSVKPLVREMDRDARINKQ--LLKKAFDLKLMGLKIDPKYGGSGVSFFELVLAVEELSKIDPA 113
Cdd:PLN02519   26 FDDTQLQFKESVQQFAQENIAPHAAAIDATNSFPKDvnLWKLMGDFNLHGITAPEEYGGLGLGYLYHCIAMEEISRASGS 105

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1734321320 114 IALIMHLQNALVAPLIEEFGNEELKEKYLKKLCK-DSVGAFALSEVVSGSDAFAMQTVAKKDGDHFILNGSKWGISNAPI 192
Cdd:PLN02519  106 VGLSYGAHSNLCINQLVRNGTPAQKEKYLPKLISgEHVGALAMSEPNSGSDVVSMKCKAERVDGGYVLNGNKMWCTNGPV 185

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1734321320 193 ADFFLVLANADPEKGYRGVTCFIVDRDHEGVVLGEQDDNLGMRAGTIAQVHLNSVRVPKTSIVGEYGKG 261
Cdd:PLN02519  186 AQTLVVYAKTDVAAGSKGITAFIIEKGMPGFSTAQKLDKLGMRGSDTCELVFENCFVPEENVLGQEGKG 254
Acyl-CoA_dh_N pfam02771
Acyl-CoA dehydrogenase, N-terminal domain; The N-terminal domain of Acyl-CoA dehydrogenase is ...
 37-147 2.85e-34

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: 119.88  E-value: 2.85e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1734321320  37 NENEKKLVEKVKNFAQSSVKPLVREMDRDARINKQLLKKAFDLKLMGLKIDPKYGGSGVSFFELVLAVEELSKIDPAIAL 116
Cdd:pfam02771   1 TEEQEALRDTVREFAEEEIAPHAAEWDEEGEFPRELWKKLGELGLLGITIPEEYGGAGLDYLAYALVAEELARADASVAL 80

                          90       100       110
                  ....*....|....*....|....*....|.
gi 1734321320 117 IMHLQNALVAPLIEEFGNEELKEKYLKKLCK 147
Cdd:pfam02771  81 ALSVHSSLGAPPILRFGTEEQKERYLPKLAS 111
Acyl-CoA_dh_M pfam02770
Acyl-CoA dehydrogenase, middle domain; Central domain of Acyl-CoA dehydrogenase has a ...
 152-236 4.46e-28

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: 103.51  E-value: 4.46e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1734321320 152 AFALSEVVSGSDAFAMQTVA-KKDGDHFILNGSKWGISNAPIADFFLVLANADPEKGYRGVTCFIVDRDHEGVVLGEQDD 230
Cdd:pfam02770   1 AFALTEPGAGSDVASLKTTAaDGDGGGWVLNGTKWWITNAGIADLFLVLARTGGDDRHGGISLFLVPKDAPGVSVRRIET 80


                  ....*.
gi 1734321320 231 NLGMRA 236
Cdd:pfam02770  81 KLGVRG 86
PLN02526 PLN02526
acyl-coenzyme A oxidase
 36-250 2.09e-21

acyl-coenzyme A oxidase


Pssm-ID: 178141 [Multi-domain]  Cd Length: 412  Bit Score: 92.61  E-value: 2.09e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1734321320  36 LNENEKKLVEKVKNFAQSSVKPLVREMDRDARINKQLLKKAFDLKLMGLKIDpKYGGSGVSFFELVLAVEELSKIDPAIA 115
Cdd:PLN02526   29 LTPEEQALRKRVRECMEKEVAPIMTEYWEKAEFPFHIIPKLGSLGIAGGTIK-GYGCPGLSITASAIATAEVARVDASCS 107

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1734321320 116 LIMHLQNALVAPLIEEFGNEELKEKYLKKLCK-DSVGAFALSEVVSGSDAFAMQTVAKKDGDHFILNGSKWGISNAPIAD 194
Cdd:PLN02526  108 TFILVHSSLAMLTIALCGSEAQKQKYLPSLAQlDTVACWALTEPDYGSDASSLNTTATKVEGGWILNGQKRWIGNSTFAD 187

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1734321320 195 FFLVLA-NADPEKgyrgVTCFIVDRDHEGVVLGEQDDNLGMRAGTIAQVHLNSVRVP 250
Cdd:PLN02526  188 VLVIFArNTTTNQ----INGFIVKKGAPGLKATKIENKIGLRMVQNGDIVLKDVFVP 240
ACAD_fadE6_17_26 cd01152
Putative acyl-CoA dehydrogenases similar to fadE6, fadE17, and fadE26; Putative acyl-CoA ...
 88-261 1.31e-20

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: 90.10  E-value: 1.31e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1734321320  88 PK-YGGSGVSFFELVLAVEELSKIDPAIALIMHLQNaLVAPLIEEFGNEELKEKYLKKLCK-DSVGAFALSEVVSGSDAF 165
Cdd:cd01152    55 PKeYGGRGASLMEQLIFREEMAAAGAPVPFNQIGID-LAGPTILAYGTDEQKRRFLPPILSgEEIWCQGFSEPGAGSDLA 133

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1734321320 166 AMQTVAKKDGDHFILNGSKWGISNAPIADFFLVLANADPE-KGYRGVTCFIVDRDHEGVV-------LGEQDDNlgmrag 237
Cdd:cd01152   134 GLRTRAVRDGDDWVVNGQKIWTSGAHYADWAWLLVRTDPEaPKHRGISILLVDMDSPGVTvrpirsiNGGEFFN------ 207

                         170       180
                  ....*....|....*....|....
gi 1734321320 238 tiaQVHLNSVRVPKTSIVGEYGKG 261
Cdd:cd01152   208 ---EVFLDDVRVPDANRVGEVNDG 228
ACAD_FadE2 cd01155
Acyl-CoA dehydrogenases similar to fadE2; FadE2-like Acyl-CoA dehydrogenase (ACAD). Acyl-CoA ...
 41-261 5.02e-20

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: 88.60  E-value: 5.02e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1734321320  41 KKLVEKVKNFAQSSVKPLVREMDRDARINK-----------QLLKKAFDLKLMGLKIDPKYGGSGVSFFELVLAVEELSK 109
Cdd:cd01155     4 QELRARVKAFMEEHVYPAEQEFLEYYAEGGdrwwtpppiieKLKAKAKAEGLWNLFLPEVSGLSGLTNLEYAYLAEETGR 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1734321320 110 idpaialimhlqnALVAP--------------LIEEFGNEELKEKYLKKLCKDSV-GAFALSEV-VSGSDAFAMQTVAKK 173
Cdd:cd01155    84 -------------SFFAPevfncqapdtgnmeVLHRYGSEEQKKQWLEPLLDGKIrSAFAMTEPdVASSDATNIECSIER 150

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1734321320 174 DGDHFILNGSKWGISNA--PIADFFLVLANADP--EKGYRGVTCFIVDRDHEGV-------VLGEQDDNLGMragtiAQV 242
Cdd:cd01155   151 DGDDYVINGRKWWSSGAgdPRCKIAIVMGRTDPdgAPRHRQQSMILVPMDTPGVtiirplsVFGYDDAPHGH-----AEI 225

                         250
                  ....*....|....*....
gi 1734321320 243 HLNSVRVPKTSIVGEYGKG 261
Cdd:cd01155   226 TFDNVRVPASNLILGEGRG 244
PRK12341 PRK12341
acyl-CoA dehydrogenase;
59-261 7.46e-18

acyl-CoA dehydrogenase;


Pssm-ID: 183454 [Multi-domain]  Cd Length: 381  Bit Score: 82.08  E-value: 7.46e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1734321320  59 VREMDRDARINKQLLKKAFDLKLMGLKIDPKYGGSGVSFFELVLAVEELSKIDPAIALImhlQNALVAPLIEEFGNEELK 138
Cdd:PRK12341   29 FRTCDENGTYPREFMRALADNGISMLGVPEEFGGTPADYVTQMLVLEEVSKCGAPAFLI---TNGQCIHSMRRFGSAEQL 105

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1734321320 139 EKYLKKLCKDSVGAFAL--SEVVSGSDAFAMQTVA-KKDGDhFILNGSKWGISNAPIADFFLVLA-NADPEKGYRGVTCF 214
Cdd:PRK12341  106 RKTAESTLETGDPAYALalTEPGAGSDNNSATTTYtRKNGK-VYLNGQKTFITGAKEYPYMLVLArDPQPKDPKKAFTLW 184

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*..
gi 1734321320 215 IVDRDHEGVVLgEQDDNLGMRAGTIAQVHLNSVRVPKTSIVGEYGKG 261
Cdd:PRK12341  185 WVDSSKPGIKI-NPLHKIGWHMLSTCEVYLDNVEVEESDLVGEEGMG 230
DszC cd01163
Dibenzothiophene (DBT) desulfurization enzyme C; DszC is a flavin reductase dependent enzyme, ...
 50-259 8.38e-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: 67.35  E-value: 8.38e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1734321320  50 FAQSSVKplvREMDRD-ARINKQLLKkafDLKLMGLKIDPKYGGSGVSFFELVLAVEELSKIDPAIALIMHLQNALVAPL 128
Cdd:cd01163    10 IAEGAAE---RDRQRGlPYEEVALLR---QSGLGTLRVPKEYGGLGASLPDLYEVVRELAAADSNIAQALRAHFGFVEAL 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1734321320 129 IeEFGNEELKEKYLKKLCK-DSVGAfALSEvVSGSDAFAMQTVAKKDGDHFILNGSKWGISNAPIADFFLVLANADPEKg 207
Cdd:cd01163    84 L-LAGPEQFRKRWFGRVLNgWIFGN-AVSE-RGSVRPGTFLTATVRDGGGYVLNGKKFYSTGALFSDWVTVSALDEEGK- 159

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1734321320 208 yrgVTCFIVDRDHEGVVLGEQDDNLGMR---AGTiaqVHLNSVRVPKTSIVGEYG 259
Cdd:cd01163   160 ---LVFAAVPTDRPGITVVDDWDGFGQRltaSGT---VTFDNVRVEPDEVLPRPN 208
ACAD_fadE5 cd01153
Putative acyl-CoA dehydrogenases similar to fadE5; Putative acyl-CoA dehydrogenase (ACAD). ...
 45-261 2.56e-12

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: 66.26  E-value: 2.56e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1734321320  45 EKVKNFAQSSVKPLVREMDR------DARIN-----KQLLKKAFDLKLMGLKIDPKYGGSGVSFFELVLAVEELSKIDPA 113
Cdd:cd01153     3 EEVARLAENVLAPLNADGDRegpvfdDGRVVvpppfKEALDAFAEAGWMALGVPEEYGGQGLPITVYSALAEIFSRGDAP 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1734321320 114 IALIMHLQNAlvAPLIEEFGNEELKEKYLKKLC-KDSVGAFALSEVVSGSDAFAMQTVAKKDGD-HFILNGSKWGISNA- 190
Cdd:cd01153    83 LMYASGTQGA--AATLLAHGTEAQREKWIPRLAeGEWTGTMCLTEPDAGSDLGALRTKAVYQADgSWRINGVKRFISAGe 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1734321320 191 -----PIadFFLVLANA-DPEKGYRGVTCFIV-----DRDHEGVVLGEQDDNLGMRAGTIAQVHLNSVRVPktsIVGEYG 259
Cdd:cd01153   161 hdmseNI--VHLVLARSeGAPPGVKGLSLFLVpkfldDGERNGVTVARIEEKMGLHGSPTCELVFDNAKGE---LIGEEG 235


                  ..
gi 1734321320 260 KG 261
Cdd:cd01153   236 MG 237
PRK13026 PRK13026
acyl-CoA dehydrogenase; Reviewed
 71-235 2.81e-11

acyl-CoA dehydrogenase; Reviewed


Pssm-ID: 237277 [Multi-domain]  Cd Length: 774  Bit Score: 63.44  E-value: 2.81e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1734321320  71 QLLKKAfdlKLMGLKIDPKYGGSGVSFFELVLAVEELSKIDPAIALIMHLQNALvAP--LIEEFGNEELKEKYLKKLCK- 147
Cdd:PRK13026  115 DYLKKE---GFFALIIPKEYGGKGFSAYANSTIVSKIATRSVSAAVTVMVPNSL-GPgeLLTHYGTQEQKDYWLPRLADg 190

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1734321320 148 DSVGAFALSEVVSGSDAFAMQTVA-----KKDGDHFI---LNGSKWGISNAPIADfflVLANA----DPE-----KGYRG 210
Cdd:PRK13026  191 TEIPCFALTGPEAGSDAGAIPDTGivcrgEFEGEEVLglrLTWDKRYITLAPVAT---VLGLAfklrDPDgllgdKKELG 267

                         170       180
                  ....*....|....*....|....*
gi 1734321320 211 VTCFIVDRDHEGVVLGEQDDNLGMR 235
Cdd:PRK13026  268 ITCALIPTDHPGVEIGRRHNPLGMA 292
AidB cd01154
Proteins involved in DNA damage response, similar to the AidB gene product; AidB is one of ...
 126-218 5.36e-11

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: 62.39  E-value: 5.36e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1734321320 126 APLIEEFGNEELKEKYLKKLCKDS----VGAFALSEVVSGSDAFAMQTVAKKD-GDHFILNGSKWgISNAPIADFFLVLA 200
Cdd:cd01154   120 VYALRKYGPEELKQYLPGLLSDRYktglLGGTWMTEKQGGSDLGANETTAERSgGGVYRLNGHKW-FASAPLADAALVLA 198

                          90
                  ....*....|....*....
gi 1734321320 201 N-ADPEKGYRGVTCFIVDR 218
Cdd:cd01154   199 RpEGAPAGARGLSLFLVPR 217
PRK03354 PRK03354
crotonobetainyl-CoA dehydrogenase; Validated
 36-261 2.01e-10

crotonobetainyl-CoA dehydrogenase; Validated


Pssm-ID: 179566 [Multi-domain]  Cd Length: 380  Bit Score: 60.62  E-value: 2.01e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1734321320  36 LNENEKKLVEKVKNF-AQSSVKPLVREMDRDARINKQLLKKAFDLKLMGLKIDPKYGGSGVSFFELVLAVEELSKIDPAI 114
Cdd:PRK03354    5 LNDEQELFVAGIRELmASENWEAYFAECDRDSVYPERFVKALADMGIDSLLIPEEHGGLDAGFVTLAAVWMELGRLGAPT 84

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1734321320 115 ALIMHLQNALVAPLIEefGNEELKEKYLKKL-CKDSVGAFALSEVVSGSDAFAMQTVAKKDGDHFILNGSKWGISNAPIA 193
Cdd:PRK03354   85 YVLYQLPGGFNTFLRE--GTQEQIDKIMAFRgTGKQMWNSAITEPGAGSDVGSLKTTYTRRNGKVYLNGSKCFITSSAYT 162

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1734321320 194 DFFLVLA--NADPEKGYrgVTCFIVDRDHEGVVLgEQDDNLGMRAGTIAQVHLNSVRVPKTSIVGEYGKG 261
Cdd:PRK03354  163 PYIVVMArdGASPDKPV--YTEWFVDMSKPGIKV-TKLEKLGLRMDSCCEITFDDVELDEKDMFGREGNG 229
PLN02636 PLN02636
acyl-coenzyme A oxidase
 104-262 1.10e-06

acyl-coenzyme A oxidase


Pssm-ID: 215342 [Multi-domain]  Cd Length: 686  Bit Score: 49.47  E-value: 1.10e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1734321320 104 VEELSKIDPAIALIMHLQNALVAPLIEEFGNEELKEKYLKKLCK-DSVGAFALSEVVSGSDAFAMQTVAKKD--GDHFIL 180
Cdd:PLN02636  127 TEAVGSVDMSLGIKLGVQYSLWGGSVINLGTKKHRDKYFDGIDNlDYPGCFAMTELHHGSNVQGLQTTATFDplTDEFVI 206

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1734321320 181 N-----GSKWGISNAPI----ADFF--LVLANADpEKGYR--GVTCFIVD----RDHE---GVVLGEQDDNLGMRAGTIA 240
Cdd:PLN02636  207 NtpndgAIKWWIGNAAVhgkfATVFarLKLPTHD-SKGVSdmGVHAFIVPirdmKTHQvlpGVEIRDCGHKVGLNGVDNG 285

                         170       180
                  ....*....|....*....|..
gi 1734321320 241 QVHLNSVRVPKTSIVGEYGKGS 262
Cdd:PLN02636  286 ALRFRSVRIPRDNLLNRFGDVS 307
PLN02876 PLN02876
acyl-CoA dehydrogenase
 132-261 7.58e-06

acyl-CoA dehydrogenase


Pssm-ID: 215473 [Multi-domain]  Cd Length: 822  Bit Score: 47.10  E-value: 7.58e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1734321320 132 FGNEELKEKYLKKLCKDSV-GAFALSEV-VSGSDAFAMQTVAKKDGDHFILNGSKWGISNA--PIADFFLVLANADPEKG 207
Cdd:PLN02876  532 YGNKEQQLEWLIPLLEGKIrSGFAMTEPqVASSDATNIECSIRRQGDSYVINGTKWWTSGAmdPRCRVLIVMGKTDFNAP 611

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1734321320 208 -YRGVTCFIVDRDHEGV-------VLGEQDDNLGMragtiAQVHLNSVRVPKTSIVGEYGKG 261
Cdd:PLN02876  612 kHKQQSMILVDIQTPGVqikrpllVFGFDDAPHGH-----AEISFENVRVPAKNILLGEGRG 668
fadE PRK09463
acyl-CoA dehydrogenase; Reviewed
 80-233 1.52e-05

acyl-CoA dehydrogenase; Reviewed


Pssm-ID: 236528 [Multi-domain]  Cd Length: 777  Bit Score: 45.96  E-value: 1.52e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1734321320  80 KLMGLKIDPKYGGSGVSFFELVLAVEELSKIDPAIALIMHLQNAL-VAPLIEEFGNEELKEKYLKKLCK-DSVGAFALSE 157
Cdd:PRK09463  122 GFFGMIIPKEYGGLEFSAYAHSRVLQKLASRSGTLAVTVMVPNSLgPGELLLHYGTDEQKDHYLPRLARgEEIPCFALTS 201

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1734321320 158 VVSGSDAFAMQ---TVAKkdGDH-------FILNGSKWGISNAPIADfflVLANA----DPE-----KGYRGVTCFIVDR 218
Cdd:PRK09463  202 PEAGSDAGSIPdtgVVCK--GEWqgeevlgMRLTWNKRYITLAPIAT---VLGLAfklyDPDgllgdKEDLGITCALIPT 276

                         170
                  ....*....|....*
gi 1734321320 219 DHEGVVLGEQDDNLG 233
Cdd:PRK09463  277 DTPGVEIGRRHFPLN 291
PTZ00457 PTZ00457
acyl-CoA dehydrogenase; Provisional
 60-223 3.13e-05

acyl-CoA dehydrogenase; Provisional


Pssm-ID: 185636 [Multi-domain]  Cd Length: 520  Bit Score: 44.87  E-value: 3.13e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1734321320  60 REMDRDARINKQLL-----KKAFDL-KLMGLKIDPKYGGSGVSFFELVLAVEEL--SKIDPAIALIMHlqNALVAPLIEE 131
Cdd:PTZ00457   38 RKLDGDEAENLQSLleqirSNDKILgNLYGARIATEYGGLGLGHTAHALIYEEVgtNCDSKLLSTIQH--SGFCTYLLST 115

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1734321320 132 FGNEELKEKYLKKLCKDSVGAFALSEVVSGSDaFAMQTV--AKKDGDHFILNGSKwGISNAPIADFFLVLANA----DPE 205
Cdd:PTZ00457  116 VGSKELKGKYLTAMSDGTIMMGWATEEGCGSD-ISMNTTkaSLTDDGSYVLTGQK-RCEFAASATHFLVLAKTltqtAAE 193

                         170       180
                  ....*....|....*....|.
gi 1734321320 206 KGYRGV---TCFIVDRDHEGV 223
Cdd:PTZ00457  194 EGATEVsrnSFFICAKDAKGV 214
PTZ00456 PTZ00456
acyl-CoA dehydrogenase; Provisional
 1-261 5.84e-05

acyl-CoA dehydrogenase; Provisional


Pssm-ID: 185635 [Multi-domain]  Cd Length: 622  Bit Score: 44.09  E-value: 5.84e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1734321320   1 MFKVPRKLPISAISTFSTTGSISAQQQPRVFPLQHLNEN--------EK------------KLVEKVKNFAQSSVKPLVR 60
Cdd:PTZ00456    1 MFRRVCSSAAASHAAAVSASARSLQYQPRIRDVQFLVEEvfnmydhyEKlgktdvtkelmdSLLEEASKLATQTLLPLYE 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1734321320  61 EMDRDARI---NKQL-----LKKAFD-LK---LMGLKIDPKYGGSGVSFFELVLAVEELSKIDPAIA----LIMHLQNAL 124
Cdd:PTZ00456   81 SSDSEGCVllkDGNVttpkgFKEAYQaLKaggWTGISEPEEYGGQALPLSVGFITRELMATANWGFSmypgLSIGAANTL 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1734321320 125 VAplieeFGNEELKEKYLKKLCKDS-VGAFALSEVVSGSDAFAMQTVAKKDGD-HFILNGSKWGISnAPIADF-----FL 197
Cdd:PTZ00456  161 MA-----WGSEEQKEQYLTKLVSGEwSGTMCLTEPQCGTDLGQVKTKAEPSADgSYKITGTKIFIS-AGDHDLtenivHI 234

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1734321320 198 VLA---NADPekGYRGVTCFIVDR----------DHEGVVLGEQDDNLGMRAGTIAQVHL-NSVrvpkTSIVGEYGKG 261
Cdd:PTZ00456  235 VLArlpNSLP--TTKGLSLFLVPRhvvkpdgsleTAKNVKCIGLEKKMGIKGSSTCQLSFeNSV----GYLIGEPNAG 306
AXO cd01150
Peroxisomal acyl-CoA oxidase; Peroxisomal acyl-CoA oxidases (AXO) catalyze the first set in ...
 97-260 1.09e-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: 43.47  E-value: 1.09e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1734321320  97 FFELVLAVEELSKIDP--AIALI-------------MHLQNALVAPLIEEFGNEELKEKYLKK-LCKDSVGAFALSEVVS 160
Cdd:cd01150    66 AKTDVERMGELMADDPekMLALTnslggydlslgakLGLHLGLFGNAIKNLGTDEHQDYWLQGaNNLEIIGCFAQTELGH 145

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1734321320 161 GSDAFAMQTVAKKD--GDHFILN-----GSKWGISN-APIADFFLVLANADPEKGYRGVTCFIVD-RDHE------GVVL 225
Cdd:cd01150   146 GSNLQGLETTATYDplTQEFVINtpdftATKWWPGNlGKTATHAVVFAQLITPGKNHGLHAFIVPiRDPKthqplpGVTV 225

                         170       180       190
                  ....*....|....*....|....*....|....*
gi 1734321320 226 GEQDDNLGMRAGTIAQVHLNSVRVPKTSIVGEYGK 260
Cdd:cd01150   226 GDIGPKMGLNGVDNGFLQFRNVRIPRENLLNRFGD 260
PTZ00460 PTZ00460
acyl-CoA dehydrogenase; Provisional
 123-263 5.34e-03

acyl-CoA dehydrogenase; Provisional


Pssm-ID: 185639 [Multi-domain]  Cd Length: 646  Bit Score: 37.90  E-value: 5.34e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1734321320 123 ALVAPLIEEFGNEELKEKYLKKLCK-DSVGAFALSEVVSGSDAFAMQTVAKKD--GDHFILNGSK------WGISNAPIA 193
Cdd:PTZ00460  100 AMVIPAFQVLGTDEQINLWMPSLLNfEIVGCYAQTELGHGSDVQNLETTATYDkqTNEFVIHTPSveavkfWPGELGFLC 179

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1734321320 194 DFFLVLANADPEKGYRGVTCFIVD-RDHE------GVVLGEQDDNLGMRAGTIAQVHLNSVRVPKTSIVGEYGKGSS 263
Cdd:PTZ00460  180 NFALVYAKLIVNGKNKGVHPFMVRiRDKEthkplqGVEVGDIGPKMGYAVKDNGFLSFDHYRIPLDSLLARYIKVSE 256
 
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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