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0ECHP_HUMAN*   SwissProt (?) | Description Local Annotation Link Reference
General Information
NameEHHADH
DescriptionPeroxisomal bifunctional enzyme (pbe) (pbfe) .
SpeciesHomo sapiens (NCBI taxonomy ID: 9606)
GO0005777 peroxisome (TAS)
0003857 3-hydroxyacyl-CoA dehydrogenase 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
IPR001753:ECH 
Evalue:-84.5686340332031 
Location:11-173IPR006176:3HCDH_N 
Evalue:-70.0409622192383 
Location:296-475IPR006108:3HCDH 
Evalue:-43.2291488647461 
Location:477-581IPR008927:6DGDH_C_like 
Evalue:0 
Location:616-709
SequencesProtein: ECHP_HUMAN (722 aa)
mRNA: NM_001966
Local Annotation
Synapse Ontology
Calcium release from RyR (Ryanodine Receptor) in the SR (Sarcoplasmic Reticulum) is activated by the calcium induced-calcium-release
sdb:0325 RyR-CICR  (Evidence:keywords)
KO assignmentK07514
  Level 3 annotation:
    enoyl-CoA hydratase
  Level 2 annotation:
    Propanoate metabolism
    Butanoate metabolism
    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
K07516
  Level 3 annotation:
    3-hydroxyacyl-CoA dehydrogenase
  Level 2 annotation:
    Butanoate metabolism
    Fatty acid metabolism
    Valine
     leucine and isoleucine degradation
    Lysine degradation
    Tryptophan metabolism
    Caprolactam degradation
K07517
  Level 3 annotation:
    3,2-trans-enoyl-CoA isomerase
  Level 2 annotation:
    Fatty acid metabolism
Loci Structure (Details)Loci index, Chromosomal location, Length, Possible relational loci clusterExon1: 955 residues, 186391107-186393969Exon2: 116 residues, 186404897-186405239Exon3: 37 residues, 186418617-186418722Exon4: 39 residues, 186429913-186430025Exon5: 59 residues, 186435771-186435944Exon6: 36 residues, 186448895-186448999Exon7: 35 residues, 186454430-186454531Exon8: 2 residues, -Jump to ECHP_HUMAN  
Tune and view alternative isoforms
Loci Cluster (Details)Loci: 3392 186563663-186683318 ~-120K 26969(MAP3K13)(+)Loci: 4651 186391107-186454531 ~-63K 26968(EHHADH)(-)Link out to UCSC