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0ECHA_HUMAN*   SwissProt (?) | Description Local Annotation Link Reference
General Information
NameHADHA
DescriptionTrifunctional enzyme alpha subunit, mitochondrial precursor (tp-alpha) (78 kda gastrin-binding protein) .
SpeciesHomo sapiens (NCBI taxonomy ID: 9606)
GO0003857 3-hydroxyacyl-CoA dehydrogenase activity (TAS)
0003985 acetyl-CoA C-acetyltransferase activity (TAS)
0004300 enoyl-CoA hydratase 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:
Enoyl-CoA hydratase () (ECH) and 3-2trans-enoyl-CoA isomerase () (ECI) are two enzymes involved in fatty acid metabolism. ECH catalyzes the hydratation of 2-trans-enoyl-CoA into 3-hydroxyacyl-CoA and ECI shifts the 3- double bond of the intermediates of unsaturated fatty acid oxidation to the 2-trans position.Most eukaryotic cells have two fatty-acid beta-oxidation systems.ne located in mitochondria and the other in peroxisomes. In mitochondria.CH and ECI are separate yet structurally related monofunctional enzymes. Peroxisomes contain a trifunctional enzyme consisting of an N-terminal domain that bears both ECH and ECI activity.nd a C-terminal domain responsible for 3-hydroxyacyl-CoA dehydrogenase (HCDH) activity.In Escherichia coli (gene fadB) and Pseudomonas fragi (gene faoA).CH and ECI are also part of a multifunctional enzyme which contains both a HCDH and a 3-hydroxybutyryl-CoA epimerase domain .A number of other proteins have been found to be evolutionary related to the ECH/ECI enzymes or domains:3-hydroxbutyryl-coa dehydratase () (crotonase). bacterial enzyme involved in the butyrate/butanol-producing pathway.Naphthoate synthase () (DHNA synthetase) (gene menB) . bacterial enzyme involved in the biosynthesis of menaquinone (vitamin K2). DHNA synthetase converts O-succinyl-benzoyl-CoA (OSB-CoA) to 1.-dihydroxy-2- naphthoic acid (DHNA).4-chlorobenzoate dehalogenase () . Pseudomonas enzyme which catalyzes the conversion of 4-chlorobenzoate-CoA to 4-hydroxybenzoate-CoA.A Rhodobacter capsulatus protein of unknown function (ORF257) .Bacillus subtilis putative polyketide biosynthesis proteins pksH and pksI.E. coli carnitine racemase (gene caiD) . E. coli hypothetical protein ygfG. Yeast hypothetical protein YDR036c.
  IPR001753:Enoyl-CoA hydratase/isomerase
3-hydroxyacyl-CoA dehydrogenase () (HCDH) is an enzyme involved in fatty acid metabolism.t catalyzes the reduction of 3-hydroxyacyl-CoA to 3-oxoacyl-CoA. Most eukaryotic cells have 2 fatty-acid beta-oxidation systems.ne located in mitochondria and the other in peroxisomes. In peroxisomes 3-hydroxyacyl-CoA dehydrogenase forms.ith enoyl-CoA hydratase (ECH) and 3.-trans-enoyl-CoA isomerase (ECI) a multifunctional enzyme where the N-terminal domain bears the hydratase/isomerase activities and the C-terminal domain the dehydrogenase activity. There are two mitochondrial enzymes: one which is monofunctional and the other which is.ike its peroxisomal counterpart.ultifunctional.In Escherichia coli (gene fadB) and Pseudomonas fragi (gene faoA) HCDH is part of a multifunctional enzyme which also contains an ECH/ECI domain as well as a 3-hydroxybutyryl-CoA epimerase domain .There are two major regions of similarity in the sequences of proteins of the HCDH family.he first one located in the N-terminal.orresponds to the NAD-binding site.he second one is located in the center of the sequence. This represents the C-terminal domain which is also found in lambda crystallin. Some proteins include two copies of this domain.
  IPR006176:3-hydroxyacyl-CoA dehydrogenase, NAD-binding
3-hydroxyacyl-CoA dehydrogenase () (HCDH) is an enzyme involved in fatty acid metabolism.t catalyzes the reduction of 3-hydroxyacyl-CoA to 3-oxoacyl-CoA. Most eukaryotic cells have 2 fatty-acid beta-oxidation systems.ne located in mitochondria and the other in peroxisomes. In peroxisomes 3-hydroxyacyl-CoA dehydrogenase forms.ith enoyl-CoA hydratase (ECH) and 3.-trans-enoyl-CoA isomerase (ECI) a multifunctional enzyme where the N-terminal domain bears the hydratase/isomerase activities and the C-terminal domain the dehydrogenase activity. There are two mitochondrial enzymes: one which is monofunctional and the other which is.ike its peroxisomal counterpart.ultifunctional.In Escherichia coli (gene fadB) and Pseudomonas fragi (gene faoA) HCDH is part of a multifunctional enzyme which also contains an ECH/ECI domain as well as a 3-hydroxybutyryl-CoA epimerase domain .There are two major region of similarities in the sequences of proteins of the HCDH family.he first one located in the N-terminal.orresponds to the NAD-binding site.he second one is located in the center of the sequence. This represents the C-terminal domain which is also found in lambda crystallin. Some proteins include two copies of this domain.
  IPR006108:3-hydroxyacyl-CoA dehydrogenase, C-terminal
6-phosphogluconate dehydrogenase () catalyses the oxidative decarboxylation of 6-phosphogluconate to ribulose 5-phosphate with the concomitant reduction of NADP to NADPH. The metazoan 6PGDHs have a well-conserved glycine-serine rich sequence at the C-terminus.hich is lacking from bacterial enzymes and from those of the parasitic protozoan Trypanosoma brucei. The active dimer of the mammalian enzyme assembles with the C-terminal tail of one subunit threaded through the other.orming part of the substrate-binding site. The tail of T. brucei 6PGDH is shorter than that of the mammalian enzyme and its terminal residues associate tightly with the second monomer. The three-dimensional structure shows this generates additional interactions between the subunits close to the active site; the coenzyme-binding domain is thereby associated more tightly with the helical domain. Three residues.onserved in all other known sequences.re important in creating a salt bridge between monomers close to the substrate-binding site .This domain is structurally similar to domains found in several different families.ncluding those represented by mannitol 2-dehydrogenase.cetohydroxy acid isomeroreductase.hort chain L-3-hydroxyacyl CoA dehydrogenase.DP-glucose/GDP-mannose dehydrogenase (dimerisation domain).-(1-D-carboxylethyl)-L-norvaline dehydrogenase.lycerol-3-phosphate dehydrogenase.nd ketopantoate reductase (PanE).
  IPR008927:6-phosphogluconate dehydrogenase, C-terminal-like
Members of this family represent the alpha subunit of the mitochondrial multifunctional fatty acid degradation enzyme complex. Subunit activities include: enoyl-CoA hydratase () and 3-hydroxyacyl-CoA dehydrogenase (). Some characterization of these proteins has been done in human ().ig () and rat (). The beta subunit has acetyl-CoA C-acyltransferase () activity.
  IPR012803:Fatty acid oxidation complex, alpha subunit, mitochondrial
IPR001753:ECH 
Evalue:-92.5228805541992 
Location:50-223IPR006176:3HCDH_N 
Evalue:-72.8860549926758 
Location:361-542IPR006108:3HCDH 
Evalue:-40.4559326171875 
Location:544-639IPR008927:6DGDH_C_like 
Evalue:0 
Location:671-763IPR001128:CYTOCHROME_P450 
Evalue:0 
Location:0-0
SequencesProtein: ECHA_HUMAN (763 aa)
mRNA: NM_000182
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 assignmentK07510
  Level 3 annotation:
    long-chain 3-hydroxyacyl-CoA dehydrogenase
  Level 2 annotation:
    Fatty acid elongation in mitochondria
    Fatty acid metabolism
K07515
  Level 3 annotation:
    enoyl-CoA hydratase
  Level 2 annotation:
    Propanoate metabolism
    Butanoate metabolism
    Fatty acid elongation in mitochondria
    Fatty acid metabolism
    Valine
     leucine and isoleucine degradation
    Lysine degradation
    Tryptophan metabolism
    beta-Alanine metabolism
    Limonene and pinene degradation
    Caprolactam degradation
    Benzoate degradation via CoA ligation
Loci Structure (Details)Loci index, Chromosomal location, Length, Possible relational loci clusterExon1: 253 residues, 26267012-26267768Exon2: 50 residues, 26267855-26268001Exon3: 40 residues, 26268682-26268797Exon4: 67 residues, 26269949-26270145Exon5: 25 residues, 26270942-26271011Exon6: 49 residues, 26271464-26271605Exon7: 31 residues, 26274063-26274150Exon8: 59 residues, 26277521-26277693Exon9: 47 residues, 26280434-26280569Exon10: 38 residues, 26286152-26286262Exon11: 21 residues, 26288942-26288999Exon12: 41 residues, 26290815-26290934Exon13: 43 residues, 26291425-26291548Exon14: 36 residues, 26306563-26306666Exon15: 42 residues, 26308531-26308651Exon16: 48 residues, 26310588-26310727Exon17: 46 residues, 26313226-26313360Exon18: 25 residues, 26315305-26315376Exon19: 16 residues, 26315473-26315515Exon20: 32 residues, 26320901-26320993Exon21: 2 residues, -Jump to ECHA_HUMAN  
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Loci Cluster (Details)Loci: 4427 26267012-26320993 ~-54K 20116(HADHA)(-)Loci: 3150 26321324-26366836 ~-46K 20117(HADHB)(+)Loci: 3149 26110477-26213782 ~-103K 20115(RAB10)(+)Link out to UCSC