Ehhadh enoyl-CoA hydratase and 3-hydroxyacyl CoA dehydrogenase [Rattus norvegicus (Norway rat)] - Gene

Summary

Official Symbol: Ehhadhprovided by RGD
Official Full Name: enoyl-CoA hydratase and 3-hydroxyacyl CoA dehydrogenaseprovided by RGD
Primary source: RGD:621441
See related: EnsemblRapid:ENSRNOG00000001770 AllianceGenome:RGD:621441
Gene type: protein coding
RefSeq status: PROVISIONAL
Organism: Rattus norvegicus
Lineage: Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae; Murinae; Rattus
Also known as: Lbp; MEF; Mfe; Pbe; MFP1; Mfe1; Pbfe; pe-CoA; perMFE-1
Summary: Enables several functions, including 3-hydroxyacyl-CoA dehydrogenase activity; delta(3)-delta(2)-enoyl-CoA isomerase activity; and enoyl-CoA hydratase activity. Involved in fatty acid beta-oxidation. Located in cytosol and peroxisome. Human ortholog(s) of this gene implicated in Fanconi renotubular syndrome 3. Orthologous to human EHHADH (enoyl-CoA hydratase and 3-hydroxyacyl CoA dehydrogenase). [provided by Alliance of Genome Resources, Dec 2024]
Expression: Biased expression in Liver (RPKM 1089.6), Kidney (RPKM 920.8) and 2 other tissues See more
Orthologs: human mouse all
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Genomic context

Location:: 11q23

Exon count:: 7

Annotation release	Status	Assembly	Chr	Location
RS_2024_02	current	GRCr8 (GCF_036323735.1)	11	NC_086029.1 (92746409..92779647)
RS_2023_06	previous assembly	mRatBN7.2 (GCF_015227675.2)	11	NC_051346.1 (79241927..79275173)
106	previous assembly	Rnor_6.0 (GCF_000001895.5)	11	NC_005110.4 (82945104..82978364)

Chromosome 11 - NC_086029.1 Genomic Context describing neighboring genes

Genomic regions, transcripts, and products

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Genomic Sequence:

Go to nucleotide: Graphics FASTA GenBank

Bibliography

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GeneRIFs: Gene References Into Functions

What's a GeneRIF?

Structural enzymology studies with the substrate 3S-hydroxybutanoyl-CoA: bifunctional MFE1 is a less efficient dehydrogenase than monofunctional HAD.
Title: Structural enzymology studies with the substrate 3S-hydroxybutanoyl-CoA: bifunctional MFE1 is a less efficient dehydrogenase than monofunctional HAD.
Data from crystallographic binding studies suggest that a catalytic water molecule, bound between two catalytic glutamates (Glu103/Glu123), plays important role in enoyl-CoA isomerase and enoyl-CoA hydratase reaction mechanisms of MFE1.
Title: The isomerase and hydratase reaction mechanism of the crotonase active site of the multifunctional enzyme (type-1), as deduced from structures of complexes with 3S-hydroxy-acyl-CoA.
liganded rat peroxisomal multifunctional enzyme type 1 is a flexible molecule with two interconnected active sites [rpMFE1]
Title: Crystal structure of liganded rat peroxisomal multifunctional enzyme type 1: a flexible molecule with two interconnected active sites.
N-terminal helix of multifunctional enzyme type 1-DH (residues 260-722 and referred to as MFE1-DH) corresponds to the alphaFOM linker helix, located between its hydratase and dehydrogenase part [multifunctional enzyme type 1 ]
Title: Structural studies of MFE-1: the 1.9 A crystal structure of the dehydrogenase part of rat peroxisomal MFE-1.
C-terminal domain E in perMFE-1 serves three functions: participation in folding of N-terminus into a functionally competent H1/I fold, stabilization of the dehydrogenation domains, targeting of the perMFE-1 to peroxisomes
Title: Organization of the multifunctional enzyme type 1: interaction between N- and C-terminal domains is required for the hydratase-1/isomerase activity.

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General gene information

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Gene Ontology Provided by RGD

Function	Evidence Code	Pubs
enables 3-hydroxyacyl-CoA dehydrogenase activity	IBA Inferred from Biological aspect of Ancestor more info
enables 3-hydroxyacyl-CoA dehydrogenase activity	IDA Inferred from Direct Assay more info	PubMed
enables 3-hydroxyacyl-CoA dehydrogenase activity	ISO Inferred from Sequence Orthology more info
enables NAD+ binding	IEA Inferred from Electronic Annotation more info
enables delta(3)-delta(2)-enoyl-CoA isomerase activity	IDA Inferred from Direct Assay more info	PubMed
enables enoyl-CoA hydratase activity	IDA Inferred from Direct Assay more info	PubMed
enables enoyl-CoA hydratase activity	ISO Inferred from Sequence Orthology more info
enables enzyme binding	IPI Inferred from Physical Interaction more info	PubMed
enables enzyme binding	ISO Inferred from Sequence Orthology more info
enables intramolecular oxidoreductase activity, transposing C=C bonds	IDA Inferred from Direct Assay more info	PubMed
enables isomerase activity	IEA Inferred from Electronic Annotation more info
enables long-chain-3-hydroxyacyl-CoA dehydrogenase activity	ISO Inferred from Sequence Orthology more info
enables long-chain-3-hydroxyacyl-CoA dehydrogenase activity	ISS Inferred from Sequence or Structural Similarity more info
enables lyase activity	IEA Inferred from Electronic Annotation more info
enables oxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor	IEA Inferred from Electronic Annotation more info

Process	Evidence Code	Pubs
involved_in fatty acid beta-oxidation	IBA Inferred from Biological aspect of Ancestor more info
involved_in fatty acid beta-oxidation	IDA Inferred from Direct Assay more info	PubMed
involved_in fatty acid beta-oxidation	IEA Inferred from Electronic Annotation more info
acts_upstream_of_or_within fatty acid beta-oxidation	ISO Inferred from Sequence Orthology more info
involved_in fatty acid beta-oxidation	ISO Inferred from Sequence Orthology more info

Component	Evidence Code	Pubs
located_in cytosol	IDA Inferred from Direct Assay more info	PubMed
is_active_in peroxisome	IBA Inferred from Biological aspect of Ancestor more info
located_in peroxisome	IDA Inferred from Direct Assay more info	PubMed
located_in peroxisome	IEA Inferred from Electronic Annotation more info
located_in peroxisome	ISO Inferred from Sequence Orthology more info

General protein information

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Preferred Names: peroxisomal bifunctional enzyme

Names: L-specific bifunctional protein; enoyl-CoA, hydratase/3-hydroxyacyl CoA dehydrogenase; enoyl-Coenzyme A, hydratase/3-hydroxyacyl Coenzyme A dehydrogenase; multifunctional enzyme 1; multifunctional enzyme type 1; multifunctional protein 1; peroxisomal bifunctional enzyme type 1; peroxisomal enoyl-CoA/hydrotase-3-hydroxyacyl-CoA

NP_598290.1

EC 1.1.1.35

EC 4.2.1.17

EC 5.3.3.8

NCBI Reference Sequences (RefSeq)

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RefSeqs maintained independently of Annotated Genomes

These reference sequences exist independently of genome builds. Explain

These reference sequences are curated independently of the genome annotation cycle, so their versions may not match the RefSeq versions in the current genome build. Identify version mismatches by comparing the version of the RefSeq in this section to the one reported in Genomic regions, transcripts, and products above.

mRNA and Protein(s)

NM_133606.3 → NP_598290.1 peroxisomal bifunctional enzyme

See identical proteins and their annotated locations for NP_598290.1

Status: PROVISIONAL

Source sequence(s)

JAXUCZ010000011

UniProtKB/Swiss-Prot

P07896, Q5EBD2

UniProtKB/TrEMBL

A0A8I5ZNC3, A6JS69

Related

ENSRNOP00000002410.2, ENSRNOT00000002410.6

Conserved Domains (4) summary

cd06558
Location:12 → 187

crotonase-like; Crotonase/Enoyl-Coenzyme A (CoA) hydratase superfamily. This superfamily contains a diverse set of enzymes including enoyl-CoA hydratase, napthoate synthase, methylmalonyl-CoA decarboxylase, 3-hydoxybutyryl-CoA dehydratase, and dienoyl-CoA isomerase. ...

PRK11154
Location:20 → 706

fadJ; multifunctional fatty acid oxidation complex subunit alpha; Reviewed

pfam00725
Location:477 → 581

3HCDH; 3-hydroxyacyl-CoA dehydrogenase, C-terminal domain

pfam02737
Location:298 → 475

3HCDH_N; 3-hydroxyacyl-CoA dehydrogenase, NAD binding domain