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0GCDH_HUMAN*   SwissProt (?) | Description Local Annotation Link Reference
General Information
NameGCDH
DescriptionGlutaryl-coa dehydrogenase, mitochondrial precursor (ec 1.3.99.7) (gcd).
SpeciesHomo sapiens (NCBI taxonomy ID: 9606)
GO0005739 mitochondrion (TAS)
0004361 glutaryl-CoA dehydrogenase activity (TAS)

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schematic display of those terms with internal associations, click the node and browse the corresponding GO term
Domain Architecture (Details)
InterPro domains unassigned to SynO:
Mammalian Co-A dehydrogenases () are enzymes that catalyse the first step in each cycle of beta-oxidation in mitochondion. Acyl-CoA dehydrogenases catalyze the alpha.eta-dehydrogenation of acyl-CoA thioesters to the corresponding trans 2.-enoyl CoA-products with concommitant reduction of enzyme-bound FAD. Reoxidation of the flavin involves transfer of electrons to ETF (electron transfering flavoprotein). These enzymes are homodimers containing one molecule of FAD. The monomeric enzyme is folded into three domains of approximately equal size. The N-terminal and the C-terminal are mainly alpha-helices packed together.nd the middle domain consists of two orthogonal beta-sheets. The flavin ring is buried in the crevise between two alpha-helical domains and the beta-sheet of one subunit.nd the adenosine pyrophosphate moiety is stretched into the subunit junction with one formed by two C-terminal domains . The C-terminal domain of Acyl-CoA dehydrogenase is an all-alpha.our helical up-and-down bundle.
  IPR006090:Acyl-CoA dehydrogenase, type 1
Mammalian Co-A dehydrogenases () are enzymes that catalyse the first step in each cycle of beta-oxidation in mitochondion. Acyl-CoA dehydrogenases catalyze the alpha.eta-dehydrogenation of acyl-CoA thioesters to the corresponding trans 2.-enoyl CoA-products with concommitant reduction of enzyme-bound FAD. Reoxidation of the flavin involves transfer of electrons to ETF (electron transfering flavoprotein). These enzymes are homodimers containing one molecule of FAD. The monomeric enzyme is folded into three domains of approximately equal size. The N-terminal and the C-terminal are mainly alpha-helices packed together.nd the middle domain consists of two orthogonal beta-sheets. The flavin ring is buried in the crevise between two alpha-helical domains and the beta-sheet of one subunit.nd the adenosine pyrophosphate moiety is stretched into the subunit junction with one formed by two C-terminal domains . The N-terminal domain of Acyl-CoA dehydrogenase is an all-alpha domain.n dimerisation.he N-terminal of one molecule extends into the other dimer and lies on the surface of the molecule.
  IPR006092:Acyl-CoA dehydrogenase, N-terminal
Acyl-CoA dehydrogenases () are a family of flavoproteins that catalyse the alpha.eta-dehydrogenation of acyl-CoA thioesters to the corresponding trans 2.-enoyl CoA-products with the concomitant reduction of enzyme-bound FAD. Different family members share a high sequence identity.atalytic mechanisms.nd structural properties.ut differ in the position of their catalytic bases and in their substrate binding specificity. Butyryl-CoA dehydrogenase prefers short chain substrates.edium chain- and long-chain acyl-CoA dehydrogenases prefer medium and long chain substrates.espectively.nd Isovaleryl-CoA dehydrogenase prefers branched-chain substrates. The monomeric enzyme is folded into three domains of approximately equal size.here the N-terminal domain is all-alpha.he middle domain is an open (5.) barrel.nd the C-terminal domain is a four-helical bundle. The constituent families differ in the numbers of C-terminal domains. This entry represents the middle beta-barrel domain found in medium chain acyl-CoA dehydrogenases.s well as in the related peroxisomal acyl-CoA oxidase-II enzymes. Acyl-CoA oxidase (ACO; ) catalyzes the first and rate-determining step of the peroxisomal beta-oxidation of fatty acids .
  IPR006091:Acyl-CoA dehydrogenase/oxidase, central region
Acyl-CoA dehydrogenases () are a family of flavoproteins that catalyse the alpha.eta-dehydrogenation of acyl-CoA thioesters to the corresponding trans 2.-enoyl CoA-products with the concomitant reduction of enzyme-bound FAD. Different family members share a high sequence identity.atalytic mechanisms.nd structural properties.ut differ in the position of their catalytic bases and in their substrate binding specificity. Butyryl-CoA dehydrogenase prefers short chain substrates.edium chain- and long-chain acyl-CoA dehydrogenases prefer medium and long chain substrates.espectively.nd Isovaleryl-CoA dehydrogenase prefers branched-chain substrates.The monomeric enzyme is folded into three domains of approximately equal size.here the N-terminal domain is all-alpha.he middle domain is an open .arrel.nd the C-terminal domain is a four-helical bundle. This entry represents the C-terminal domain found in medium chain acyl-CoA dehydrogenases.s well as in the related peroxisomal acyl-CoA oxidase-II enzymes.here this domain occurs as a tandem duplication. Acyl-CoA oxidase (ACO; ) catalyzes the first and rate-determining step of the peroxisomal beta-oxidation of fatty acids .The SSF signature in this entry is currently under review. Please be aware that some of the protein hits may be false positives.
  IPR009075:Acyl-CoA dehydrogenase/oxidase C-terminal
Acyl-CoA dehydrogenases () are a family of flavoproteins that catalyse the alpha.eta-dehydrogenation of acyl-CoA thioesters to the corresponding trans 2.-enoyl CoA-products with the concomitant reduction of enzyme-bound FAD. Different family members share a high sequence identity.atalytic mechanisms.nd structural properties.ut differ in the position of their catalytic bases and in their substrate binding specificity. Butyryl-CoA dehydrogenase prefers short chain substrates.edium chain- and long-chain acyl-CoA dehydrogenases prefer medium and long chain substrates.espectively.nd Isovaleryl-CoA dehydrogenase prefers branched-chain substrates.The monomeric enzyme is folded into three domains of approximately equal size.here the N-terminal domain is all-alpha.he middle domain is an open (5.) barrel.nd the C-terminal domain is a four-helical bundle. The constituent families differ in the numbers of C-terminal domains. This entry represents both the N-terminal and middle domains found in medium chain acyl-CoA dehydrogenases.s well as in the related peroxisomal acyl-CoA oxidase-II enzymes. Acyl-CoA oxidase (ACO; ) catalyzes the first and rate-determining step of the peroxisomal beta-oxidation of fatty acids .The SSF signature in this entry is currently under review. Please be aware that some of the protein hits may be false positives.
  IPR009100:Acyl-CoA dehydrogenase/oxidase, middle and N-terminal
Acyl-CoA dehydrogenases are a family of flavoproteins that catalyse the alpha.eta-dehydrogenation of acyl-CoA thioesters to the corresponding trans 2.-enoyl CoA-products with the concomitant reduction of enzyme-bound FAD. Different family members share a high sequence identity.atalytic mechanisms.nd structural properties.ut differ in the position of their catalytic bases and in their substrate binding specificity. Butyryl-CoA dehydrogenase prefers short chain substrates.edium chain- and long-chain acyl-CoA dehydrogenases prefer medium and long chain substrates.espectively.nd Isovaleryl-CoA dehydrogenase prefers branched-chain substrates. The monomeric enzyme is folded into three domains of approximately equal size.here the N-terminal domain is all-alpha.he middle domain is an open (5.) barrel.nd the C-terminal domain is a four-helical bundle. The constituent families differ in the number of C-terminal domains. This entry represents the C-terminal domain found in both type 1 and type 2 enzymes.
  IPR013764:Acyl-CoA dehydrogenase, type1/2, C-terminal
Acyl-CoA dehydrogenases () are a family of flavoproteins that catalyse the alpha.eta-dehydrogenation of acyl-CoA thioesters to the corresponding trans 2.-enoyl CoA-products with the concomitant reduction of enzyme-bound FAD. Different family members share a high sequence identity.atalytic mechanisms.nd structural properties.ut differ in the position of their catalytic bases and in their substrate binding specificity. Butyryl-CoA dehydrogenase prefers short chain substrates.edium chain- and long-chain acyl-CoA dehydrogenases prefer medium and long chain substrates.espectively.nd Isovaleryl-CoA dehydrogenase prefers branched-chain substrates. The monomeric enzyme is folded into three domains of approximately equal size.here the N-terminal domain is all-alpha.he middle domain is an open (5.) barrel.nd the C-terminal domain is a four-helical bundle. The constituent families differ in the numbers of C-terminal domains. This entry represents the N-terminal alpha-helical domain found in medium chain acyl-CoA dehydrogenases.s well as in the related peroxisomal acyl-CoA oxidase-II enzymes. Acyl-CoA oxidase (ACO; ) catalyzes the first and rate-determining step of the peroxisomal beta-oxidation of fatty acids .
  IPR013786:Acyl-CoA dehydrogenase/oxidase, N-terminal
IPR006090:Acyl-CoA_dh_1 
Evalue:-28.9586067199707 
Location:283-429IPR006091:Acyl-CoA_dh_M 
Evalue:-24.3665313720703 
Location:176-230IPR006092:Acyl-CoA_dh_N 
Evalue:-12.7212467193604 
Location:61-172
SequencesProtein: GCDH_HUMAN (438 aa)
mRNA: NM_000159
Local Annotation
Synapse Ontology
mitochondria are frequently observed in the vicinity of the synaptic vesicle clusters, in agreement with the ATP requirement of several steps of the vesicle cycle.
sdb:0118 mitochondria  (Evidence:keywords)
KO assignmentK00252
  Level 3 annotation:
    glutaryl-CoA dehydrogenase
  Level 2 annotation:
    Fatty acid metabolism
    Lysine degradation
    Tryptophan metabolism
    Benzoate degradation via CoA ligation
Loci Structure (Details)Loci index, Chromosomal location, Length, Possible relational loci clusterExon1: 15 residues, 12862973-12863016Exon2: 43 residues, 12863084-12863209Exon3: 14 residues, 12863300-12863336Exon4: 50 residues, 12863644-12863788Exon5: 23 residues, 12863929-12863992Exon6: 59 residues, 12865296-12865467Exon7: 45 residues, 12867805-12867935Exon8: 74 residues, 12868018-12868235Exon9: 36 residues, 12868723-12868827Exon10: 44 residues, 12869116-12869242Exon11: 55 residues, 12869516-12869677Exon12: 169 residues, 12871281-12871782Exon13: 2 residues, -Jump to GCDH_HUMAN  
Tune and view alternative isoforms
Loci Cluster (Details)Loci: 4368 12768634-12773694 ~-5K 18105(PRDX2)(-)Loci: 3091 12810347-12846765 ~-36K 18111(MAST1)(+)Loci: 3092 12862973-12871782 ~-9K 18114(GCDH)(+)Loci: 4369 13115902-13122052 ~-6K 18133(STX10)(-)Loci: 4370 13179114-13478317 ~-299K 18136(CACNA1A)(-)Loci: 4367 12734816-12747337 ~-13K 18101(HOOK2)(-)Link out to UCSC