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0IVD_HUMAN*   SwissProt (?) | Description Local Annotation Link Reference
General Information
NameIVD
DescriptionIsovaleryl-coa dehydrogenase, mitochondrial precursor (ec 1.3.99.10) (ivd).
SpeciesHomo sapiens (NCBI taxonomy ID: 9606)
GO0005759 mitochondrial matrix (NAS)
0008470 isovaleryl-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 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
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
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
IPR006092:Acyl-CoA_dh_N 
Evalue:-60.9208183288574 
Location:43-157IPR006090:Acyl-CoA_dh_1 
Evalue:-52.0915145874023 
Location:270-419IPR006091:Acyl-CoA_dh_M 
Evalue:-26.9208183288574 
Location:161-212
SequencesProtein: IVD_HUMAN (423 aa)
mRNA: NM_002225
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)
Microglias, one kind of glias in CNS, are responsible for removing most of the waste and cellular debris from the CNS
sdb:0267 removing metabolic mass  (Evidence:keywords)
KO assignmentK00253
  Level 3 annotation:
    isovaleryl-CoA dehydrogenase
  Level 2 annotation:
    Valine
     leucine and isoleucine degradation
Loci Structure (Details)Loci index, Chromosomal location, Length, Possible relational loci clusterExon1: 163 residues, 38484977-38485464Exon2: 32 residues, 38487128-38487218Exon3: 19 residues, 38487429-38487481Exon4: 58 residues, 38490118-38490288Exon5: 33 residues, 38490750-38490844Exon6: 47 residues, 38491045-38491182Exon7: 34 residues, 38492481-38492578Exon8: 33 residues, 38494379-38494473Exon9: 29 residues, 38494891-38494973Exon10: 37 residues, 38495568-38495673Exon11: 26 residues, 38495780-38495853Exon12: 247 residues, 38497620-38498355Exon13: 2 residues, -Jump to IVD_HUMAN  
Tune and view alternative isoforms
Loci Cluster (Details)Loci: 2873 38484977-38498355 ~-13K 12090(IVD)(+)Loci: 2874 38550504-38552645 ~-2K 12093(D4ST1)(+)Loci: 2875 38673738-38743829 ~-70K 12099(CASC5)(+)Loci: 2876 38843576-38847203 ~-4K 12107(GCHFR)(+)Loci: 2877 38973919-38983464 ~-10K 12116(VPS18)(+)Loci: 4163 38367401-38387330 ~-20K 12082(PLCB2)(-)Link out to UCSC