Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Entry version 185 (25 May 2022)
Sequence version 2 (23 Jan 2007)
Previous versions | rss
Add a publicationFeedback
Protein

Peroxisomal bifunctional enzyme

Gene

Ehhadh

Organism
Rattus norvegicus (Rat)
Status
Reviewed-Annotation score:

Annotation score:5 out of 5

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the 'correct annotation' for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>
-Experimental evidence at protein leveli <p>This indicates the type of evidence that supports the existence of the protein. Note that the 'protein existence' evidence does not give information on the accuracy or correctness of the sequence(s) displayed.<p><a href='/help/protein_existence' target='_top'>More...</a></p>

<p>This section provides any useful information about the protein, mostly biological knowledge.<p><a href='/help/function_section' target='_top'>More...</a></p>Functioni

Peroxisomal trifunctional enzyme possessing 2-enoyl-CoA hydratase, 3-hydroxyacyl-CoA dehydrogenase, and delta 3, delta 2-enoyl-CoA isomerase activities (PubMed:2303409, PubMed:12106015, PubMed:23351063).

Catalyzes two of the four reactions of the long chain fatty acids peroxisomal beta-oxidation pathway (PubMed:2303409, PubMed:12106015).

Can also use branched-chain fatty acids such as 2-methyl-2E-butenoyl-CoA as a substrate, which is hydrated into (2S,3S)-3-hydroxy-2-methylbutanoyl-CoA (Probable). Optimal isomerase for 2,5 double bonds into 3,5 form isomerization in a range of enoyl-CoA species. Also able to isomerize both 3-cis and 3-trans double bonds into the 2-trans form in a range of enoyl-CoA species (PubMed:11781327).

Regulates the amount of medium-chain dicarboxylic fatty acids which are essential regulators of all fatty acid oxidation pathways (By similarity).

Also involved in the degradation of long-chain dicarboxylic acids through peroxisomal beta-oxidation (By similarity).

By similarity1 Publication3 Publications

<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">Function</a> section describes the catalytic activity of an enzyme, i.e. a chemical reaction that the enzyme catalyzes.<p><a href='/help/catalytic_activity' target='_top'>More...</a></p>Catalytic activityi

<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">Function</a> section describes regulatory mechanisms for enzymes, transporters or microbial transcription factors, and reports the components which regulate (by activation or inhibition) the reaction.<p><a href='/help/activity_regulation' target='_top'>More...</a></p>Activity regulationi

Enzyme activity enhanced by acetylation.By similarity

<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">'Function'</a> section describes the metabolic pathway(s) associated with a protein.<p><a href='/help/pathway' target='_top'>More...</a></p>Pathwayi: fatty acid beta-oxidation

This protein is involved in the pathway fatty acid beta-oxidation, which is part of Lipid metabolism.3 Publications
View all proteins of this organism that are known to be involved in the pathway fatty acid beta-oxidation and in Lipid metabolism.

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">Function</a> section describes the interaction between a single amino acid and another chemical entity. Priority is given to the annotation of physiological ligands.<p><a href='/help/binding' target='_top'>More...</a></p>Binding sitei100Substrate; via amide nitrogenBy similarity1
<p>This subsection describes interesting single amino acid sites on the sequence that are not defined in any other subsection. This subsection can be displayed in different sections ('Function', 'PTM / Processing', 'Pathology and Biotech') according to its content.<p><a href='/help/site' target='_top'>More...</a></p>Sitei103Important for catalytic activityBy similarity1
Sitei123Important for catalytic activityBy similarity1

<p>The <a href="http://www.geneontology.org/">Gene Ontology (GO)</a> project provides a set of hierarchical controlled vocabulary split into 3 categories:<p><a href='/help/gene_ontology' target='_top'>More...</a></p>GO - Molecular functioni

GO - Biological processi

<p>UniProtKB Keywords constitute a <a href="http://www.uniprot.org/keywords">controlled vocabulary</a> with a hierarchical structure. Keywords summarise the content of a UniProtKB entry and facilitate the search for proteins of interest.<p><a href='/help/keywords' target='_top'>More...</a></p>Keywordsi

Molecular functionIsomerase, Lyase, Multifunctional enzyme, Oxidoreductase
Biological processFatty acid metabolism, Lipid metabolism
LigandNAD

Enzyme and pathway databases

BRENDA Comprehensive Enzyme Information System

More...
BRENDAi
4.2.1.17, 5301

Reactome - a knowledgebase of biological pathways and processes

More...
Reactomei
R-RNO-390247, Beta-oxidation of very long chain fatty acids
R-RNO-9033241, Peroxisomal protein import

SABIO-RK: Biochemical Reaction Kinetics Database

More...
SABIO-RKi
P07896

UniPathway: a resource for the exploration and annotation of metabolic pathways

More...
UniPathwayi
UPA00659

Chemistry databases

SwissLipids knowledge resource for lipid biology

More...
SwissLipidsi
SLP:000001144

<p>This section provides information about the protein and gene name(s) and synonym(s) and about the organism that is the source of the protein sequence.<p><a href='/help/names_and_taxonomy_section' target='_top'>More...</a></p>Names & Taxonomyi

<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section provides an exhaustive list of all names of the protein, from commonly used to obsolete, to allow unambiguous identification of a protein.<p><a href='/help/protein_names' target='_top'>More...</a></p>Protein namesi
Recommended name:
Peroxisomal bifunctional enzymeCurated
Short name:
PBE
Short name:
PBFE
Alternative name(s):
Multifunctional enzyme 11 Publication
Short name:
MFE1
Multifunctional protein 1
Short name:
MFP1
Including the following 2 domains:
Enoyl-CoA hydratase/3,2-trans-enoyl-CoA isomerase (EC:4.2.1.172 Publications, EC:5.3.3.83 Publications)
3-hydroxyacyl-CoA dehydrogenase (EC:1.1.1.351 Publication)
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section indicates the name(s) of the gene(s) that code for the protein sequence(s) described in the entry. Four distinct tokens exist: 'Name', 'Synonyms', 'Ordered locus names' and 'ORF names'.<p><a href='/help/gene_name' target='_top'>More...</a></p>Gene namesi
Name:EhhadhImported
Synonyms:Mfe11 Publication
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section provides information on the name(s) of the organism that is the source of the protein sequence.<p><a href='/help/organism-name' target='_top'>More...</a></p>OrganismiRattus norvegicus (Rat)
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section shows the unique identifier assigned by the NCBI to the source organism of the protein. This is known as the 'taxonomic identifier' or 'taxid'.<p><a href='/help/taxonomic_identifier' target='_top'>More...</a></p>Taxonomic identifieri10116 [NCBI]
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section contains the taxonomic hierarchical classification lineage of the source organism. It lists the nodes as they appear top-down in the taxonomic tree, with the more general grouping listed first.<p><a href='/help/taxonomic_lineage' target='_top'>More...</a></p>Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaMyomorphaMuroideaMuridaeMurinaeRattus
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section is present for entries that are part of a <a href="http://www.uniprot.org/proteomes">proteome</a>, i.e. of a set of proteins thought to be expressed by organisms whose genomes have been completely sequenced.<p><a href='/help/proteomes_manual' target='_top'>More...</a></p>Proteomesi
  • UP000002494 <p>A UniProt <a href="http://www.uniprot.org/manual/proteomes%5Fmanual">proteome</a> can consist of several components.<br></br>The component name refers to the genomic component encoding a set of proteins.<p><a href='/help/proteome_component' target='_top'>More...</a></p> Componenti: Chromosome 11

Organism-specific databases

Rat genome database

More...
RGDi
621441, Ehhadh

<p>This section provides information on the location and the topology of the mature protein in the cell.<p><a href='/help/subcellular_location_section' target='_top'>More...</a></p>Subcellular locationi

Keywords - Cellular componenti

Peroxisome

<p>This section provides information on the disease(s) and phenotype(s) associated with a protein.<p><a href='/help/pathology_and_biotech_section' target='_top'>More...</a></p>Pathology & Biotechi

Chemistry databases

ChEMBL database of bioactive drug-like small molecules

More...
ChEMBLi
CHEMBL3232

<p>This section describes post-translational modifications (PTMs) and/or processing events.<p><a href='/help/ptm_processing_section' target='_top'>More...</a></p>PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the 'PTM / Processing' section describes the extent of a polypeptide chain in the mature protein following processing or proteolytic cleavage.<p><a href='/help/chain' target='_top'>More...</a></p>ChainiPRO_00001092491 – 722Peroxisomal bifunctional enzymeAdd BLAST722

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the 'PTM / Processing' section specifies the position and type of each modified residue excluding <a href="http://www.uniprot.org/manual/lipid">lipids</a>, <a href="http://www.uniprot.org/manual/carbohyd">glycans</a> and <a href="http://www.uniprot.org/manual/crosslnk">protein cross-links</a>.<p><a href='/help/mod_res' target='_top'>More...</a></p>Modified residuei2Blocked amino end (Ala)1
Modified residuei38N6-succinyllysineBy similarity1
Modified residuei173N6-acetyllysine; alternateBy similarity1
Modified residuei173N6-succinyllysine; alternateBy similarity1
Modified residuei182N6-succinyllysineBy similarity1
Modified residuei190N6-acetyllysine; alternateBy similarity1
Modified residuei190N6-succinyllysine; alternateBy similarity1
Modified residuei218N6-acetyllysine; alternateBy similarity1
Modified residuei218N6-succinyllysine; alternateBy similarity1
Modified residuei241N6-succinyllysineBy similarity1
Modified residuei249N6-acetyllysineBy similarity1
Modified residuei253N6-succinyllysineBy similarity1
Modified residuei275N6-acetyllysine; alternateBy similarity1
Modified residuei275N6-succinyllysine; alternateBy similarity1
Modified residuei279N6-succinyllysineBy similarity1
Modified residuei289N6-succinyllysineBy similarity1
Modified residuei330N6-succinyllysineBy similarity1
Modified residuei345N6-acetyllysineBy similarity1
Modified residuei359N6-acetyllysineBy similarity1
Modified residuei463N6-acetyllysineBy similarity1
Modified residuei531N6-succinyllysineBy similarity1
Modified residuei547PhosphothreonineBy similarity1
Modified residuei576N6-succinyllysineBy similarity1
Modified residuei583N6-acetyllysine; alternateBy similarity1
Modified residuei583N6-succinyllysine; alternateBy similarity1
Modified residuei590N6-acetyllysine; alternateBy similarity1
Modified residuei590N6-succinyllysine; alternateBy similarity1
Modified residuei709N6-acetyllysine; alternateBy similarity1
Modified residuei709N6-succinyllysine; alternateBy similarity1
Modified residuei721N6-succinyllysineBy similarity1

<p>This subsection of the <a href="http://www.uniprot.org/help/ptm%5Fprocessing%5Fsection">PTM/processing</a> section describes post-translational modifications (PTMs). This subsection <strong>complements</strong> the information provided at the sequence level or describes modifications for which <strong>position-specific data is not yet available</strong>.<p><a href='/help/post-translational_modification' target='_top'>More...</a></p>Post-translational modificationi

Acetylated, leading to enhanced enzyme activity. Acetylation is enhanced by up to 80% after treatment either with trichostin A (TCA) or with nicotinamide (NAM) with highest increase on Lys-345. Acetylation and enzyme activity increased by about 1.5% on addition of fatty acids (By similarity).By similarity

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

PaxDb, a database of protein abundance averages across all three domains of life

More...
PaxDbi
P07896

PRoteomics IDEntifications database

More...
PRIDEi
P07896

PTM databases

iPTMnet integrated resource for PTMs in systems biology context

More...
iPTMneti
P07896

Comprehensive resource for the study of protein post-translational modifications (PTMs) in human, mouse and rat.

More...
PhosphoSitePlusi
P07896

<p>This section provides information on the expression of a gene at the mRNA or protein level in cells or in tissues of multicellular organisms.<p><a href='/help/expression_section' target='_top'>More...</a></p>Expressioni

Gene expression databases

Bgee dataBase for Gene Expression Evolution

More...
Bgeei
ENSRNOG00000001770, Expressed in liver and 19 other tissues

Genevisible search portal to normalized and curated expression data from Genevestigator

More...
Genevisiblei
P07896, RN

<p>This section provides information on the quaternary structure of a protein and on interaction(s) with other proteins or protein complexes.<p><a href='/help/interaction_section' target='_top'>More...</a></p>Interactioni

<p>This subsection of the <a href="http://www.uniprot.org/help/interaction%5Fsection">'Interaction'</a> section provides information about the protein quaternary structure and interaction(s) with other proteins or protein complexes (with the exception of physiological receptor-ligand interactions which are annotated in the <a href="http://www.uniprot.org/help/function%5Fsection">'Function'</a> section).<p><a href='/help/subunit_structure' target='_top'>More...</a></p>Subunit structurei

Monomer.

1 Publication

GO - Molecular functioni

Protein-protein interaction databases

Protein interaction database and analysis system

More...
IntActi
P07896, 7 interactors

Molecular INTeraction database

More...
MINTi
P07896

STRING: functional protein association networks

More...
STRINGi
10116.ENSRNOP00000002410

<p>This section provides information on the tertiary and secondary structure of a protein.<p><a href='/help/structure_section' target='_top'>More...</a></p>Structurei

Secondary structure

1722
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details

3D structure databases

AlphaFold Protein Structure Database

More...
AlphaFoldDBi
P07896

SWISS-MODEL Repository - a database of annotated 3D protein structure models

More...
SMRi
P07896

Database of comparative protein structure models

More...
ModBasei
Search...

Protein Data Bank in Europe - Knowledge Base

More...
PDBe-KBi
Search...

Miscellaneous databases

Relative evolutionary importance of amino acids within a protein sequence

More...
EvolutionaryTracei
P07896

<p>This section provides information on sequence similarities with other proteins and the domain(s) present in a protein.<p><a href='/help/family_and_domains_section' target='_top'>More...</a></p>Family & Domainsi

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the 'Family and Domains' section describes a region of interest that cannot be described in other subsections.<p><a href='/help/region' target='_top'>More...</a></p>Regioni1 – 281Enoyl-CoA hydratase / isomeraseAdd BLAST281
Regioni282 – 5713-hydroxyacyl-CoA dehydrogenaseAdd BLAST290

Motif

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the 'Family and Domains' section describes a short (usually not more than 20 amino acids) conserved sequence motif of biological significance.<p><a href='/help/motif' target='_top'>More...</a></p>Motifi720 – 722Microbody targeting signal3

<p>This subsection of the 'Family and domains' section provides information about the sequence similarity with other proteins.<p><a href='/help/sequence_similarities' target='_top'>More...</a></p>Sequence similaritiesi

In the N-terminal section; belongs to the enoyl-CoA hydratase/isomerase family.1 Publication
In the C-terminal section; belongs to the 3-hydroxyacyl-CoA dehydrogenase family.1 Publication

Phylogenomic databases

evolutionary genealogy of genes: Non-supervised Orthologous Groups

More...
eggNOGi
KOG1683, Eukaryota

Ensembl GeneTree

More...
GeneTreei
ENSGT00940000157516

The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

More...
HOGENOMi
CLU_009834_16_3_1

InParanoid: Eukaryotic Ortholog Groups

More...
InParanoidi
P07896

Identification of Orthologs from Complete Genome Data

More...
OMAi
TGAGWPF

Database of Orthologous Groups

More...
OrthoDBi
219667at2759

Database for complete collections of gene phylogenies

More...
PhylomeDBi
P07896

TreeFam database of animal gene trees

More...
TreeFami
TF316708

Family and domain databases

Integrated resource of protein families, domains and functional sites

More...
InterProi
View protein in InterPro
IPR006180, 3-OHacyl-CoA_DH_CS
IPR006176, 3-OHacyl-CoA_DH_NAD-bd
IPR006108, 3HC_DH_C
IPR008927, 6-PGluconate_DH-like_C_sf
IPR029045, ClpP/crotonase-like_dom_sf
IPR018376, Enoyl-CoA_hyd/isom_CS
IPR001753, Enoyl-CoA_hydra/iso
IPR036291, NAD(P)-bd_dom_sf

Pfam protein domain database

More...
Pfami
View protein in Pfam
PF00725, 3HCDH, 2 hits
PF02737, 3HCDH_N, 1 hit
PF00378, ECH_1, 1 hit

Superfamily database of structural and functional annotation

More...
SUPFAMi
SSF48179, SSF48179, 2 hits
SSF51735, SSF51735, 1 hit
SSF52096, SSF52096, 1 hit

PROSITE; a protein domain and family database

More...
PROSITEi
View protein in PROSITE
PS00067, 3HCDH, 1 hit
PS00166, ENOYL_COA_HYDRATASE, 1 hit

<p>This section displays by default the canonical protein sequence and upon request all isoforms described in the entry. It also includes information pertinent to the sequence(s), including <a href="http://www.uniprot.org/help/sequence%5Flength">length</a> and <a href="http://www.uniprot.org/help/sequences">molecular weight</a>. The information is filed in different subsections. The current subsections and their content are listed below:<p><a href='/help/sequences_section' target='_top'>More...</a></p>Sequence (1+)i

<p>This subsection of the <a href="http://www.uniprot.org/help/sequences%5Fsection">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical%5Fand%5Fisoforms">canonical sequence</a> displayed by default in the entry is complete or not.<p><a href='/help/sequence_status' target='_top'>More...</a></p>Sequence statusi: Complete.

This entry has 1 described isoform and 1 potential isoform that is computationally mapped.Show allAlign All

P07896-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MAEYLRLPHS LAMIRLCNPP VNAVSPTVIR EVRNGLQKAG SDHTVKAIVI
60 70 80 90 100
CGANGNFCAG ADIHGFSAFT PGLALGSLVD EIQRYQKPVL AAIQGVALGG
110 120 130 140 150
GLELALGCHY RIANAKARVG LPEVTLGILP GARGTQLLPR VVGVPVALDL
160 170 180 190 200
ITSGKYLSAD EALRLGILDA VVKSDPVEEA IKFAQKIIDK PIEPRRIFNK
210 220 230 240 250
PVPSLPNMDS VFAEAIAKVR KQYPGVLAPE TCVRSIQASV KHPYEVGIKE
260 270 280 290 300
EEKLFMYLRA SGQAKALQYA FFAEKSANKW STPSGASWKT ASAQPVSSVG
310 320 330 340 350
VLGLGTMGRG IAISFARVGI SVVAVESDPK QLDAAKKIIT FTLEKEASRA
360 370 380 390 400
HQNGQASAKP KLRFSSSTKE LSTVDLVVEA VFEDMNLKKK VFAELSALCK
410 420 430 440 450
PGAFLCTNTS ALNVDDIASS TDRPQLVIGT HFFSPAHVMR LLEVIPSRYS
460 470 480 490 500
SPTTIATVMS LSKKIGKIGV VVGNCYGFVG NRMLAPYYNQ GFFLLEEGSK
510 520 530 540 550
PEDVDGVLEE FGFKMGPFRV SDLAGLDVGW KIRKGQGLTG PSLPPGTPVR
560 570 580 590 600
KRGNSRYSPL GDMLCEAGRF GQKTGKGWYQ YDKPLGRIHK PDPWLSTFLS
610 620 630 640 650
QYREVHHIEQ RTISKEEILE RCLYSLINEA FRILEEGMAA RPEHIDVIYL
660 670 680 690 700
HGYGWPRHKG GPMFYAASVG LPTVLEKLQK YYRQNPDIPQ LEPSDYLRRL
710 720
VAQGSPPLKE WQSLAGPHGS KL
Length:722
Mass (Da):78,658
Last modified:January 23, 2007 - v2
<p>The checksum is a form of redundancy check that is calculated from the sequence. It is useful for tracking sequence updates.</p> <p>It should be noted that while, in theory, two different sequences could have the same checksum value, the likelihood that this would happen is extremely low.</p> <p>However UniProtKB may contain entries with identical sequences in case of multiple genes (paralogs).</p> <p>The checksum is computed as the sequence 64-bit Cyclic Redundancy Check value (CRC64) using the generator polynomial: x<sup>64</sup> + x<sup>4</sup> + x<sup>3</sup> + x + 1. The algorithm is described in the ISO 3309 standard. </p> <p class="publication">Press W.H., Flannery B.P., Teukolsky S.A. and Vetterling W.T.<br /> <strong>Cyclic redundancy and other checksums</strong><br /> <a href="http://www.nrbook.com/b/bookcpdf.php">Numerical recipes in C 2nd ed., pp896-902, Cambridge University Press (1993)</a>)</p> Checksum:i76ACC709C5F23E86
GO

<p>In eukaryotic reference proteomes, unreviewed entries that are likely to belong to the same gene are computationally mapped, based on gene identifiers from Ensembl, EnsemblGenomes and model organism databases.<p><a href='/help/gene_centric_isoform_mapping' target='_top'>More...</a></p>Computationally mapped potential isoform sequencesi

There is 1 potential isoform mapped to this entry.BLASTAlignShow allAdd to basket
EntryEntry nameProtein names
Gene namesLengthAnnotation
A0A8I5ZNC3A0A8I5ZNC3_RAT
Peroxisomal bifunctional enzyme
Ehhadh
673Annotation score:

Annotation score:1 out of 5

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the 'correct annotation' for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>

Sequence databases

Select the link destinations:

EMBL nucleotide sequence database

More...
EMBLi

GenBank nucleotide sequence database

More...
GenBanki

DNA Data Bank of Japan; a nucleotide sequence database

More...
DDBJi
Links Updated
K03249 mRNA Translation: AAA41825.1
BC089777 mRNA Translation: AAH89777.1
J02748 Genomic DNA Translation: AAA41826.1

Protein sequence database of the Protein Information Resource

More...
PIRi
A23575, DWRTEP

NCBI Reference Sequences

More...
RefSeqi
NP_598290.1, NM_133606.1

Genome annotation databases

Ensembl eukaryotic genome annotation project

More...
Ensembli
ENSRNOT00000002410; ENSRNOP00000002410; ENSRNOG00000001770

Database of genes from NCBI RefSeq genomes

More...
GeneIDi
171142

KEGG: Kyoto Encyclopedia of Genes and Genomes

More...
KEGGi
rno:171142

UCSC genome browser

More...
UCSCi
RGD:621441, rat

<p>This section provides links to proteins that are similar to the protein sequence(s) described in this entry at different levels of sequence identity thresholds (100%, 90% and 50%) based on their membership in UniProt Reference Clusters (<a href="http://www.uniprot.org/help/uniref">UniRef</a>).<p><a href='/help/similar_proteins_section' target='_top'>More...</a></p>Similar proteinsi

<p>This section is used to point to information related to entries and found in data collections other than UniProtKB.<p><a href='/help/cross_references_section' target='_top'>More...</a></p>Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
K03249 mRNA Translation: AAA41825.1
BC089777 mRNA Translation: AAH89777.1
J02748 Genomic DNA Translation: AAA41826.1
PIRiA23575, DWRTEP
RefSeqiNP_598290.1, NM_133606.1

3D structure databases

Select the link destinations:

Protein Data Bank Europe

More...
PDBei

Protein Data Bank RCSB

More...
RCSB PDBi

Protein Data Bank Japan

More...
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1ZCJX-ray1.90A260-722[»]
2X58X-ray2.80A/B1-722[»]
3ZW8X-ray2.50A/B1-722[»]
3ZW9X-ray2.90A/B1-722[»]
3ZWAX-ray2.47A/B1-722[»]
3ZWBX-ray3.10A/B1-722[»]
3ZWCX-ray2.30A/B1-722[»]
5MGBX-ray2.80A/B1-722[»]
5OMOX-ray2.49A/B1-722[»]
6Z5FX-ray2.25AAA/BBB1-722[»]
6Z5OX-ray1.70AAA1-722[»]
6Z5VX-ray2.33AAA/BBB1-722[»]
6ZIBX-ray2.70AAA/BBB1-722[»]
6ZICX-ray2.20AAA/BBB1-722[»]
AlphaFoldDBiP07896
SMRiP07896
ModBaseiSearch...
PDBe-KBiSearch...

Protein-protein interaction databases

IntActiP07896, 7 interactors
MINTiP07896
STRINGi10116.ENSRNOP00000002410

Chemistry databases

ChEMBLiCHEMBL3232
SwissLipidsiSLP:000001144

PTM databases

iPTMnetiP07896
PhosphoSitePlusiP07896

Proteomic databases

PaxDbiP07896
PRIDEiP07896

Genome annotation databases

EnsembliENSRNOT00000002410; ENSRNOP00000002410; ENSRNOG00000001770
GeneIDi171142
KEGGirno:171142
UCSCiRGD:621441, rat

Organism-specific databases

Comparative Toxicogenomics Database

More...
CTDi
1962
RGDi621441, Ehhadh

Phylogenomic databases

eggNOGiKOG1683, Eukaryota
GeneTreeiENSGT00940000157516
HOGENOMiCLU_009834_16_3_1
InParanoidiP07896
OMAiTGAGWPF
OrthoDBi219667at2759
PhylomeDBiP07896
TreeFamiTF316708

Enzyme and pathway databases

UniPathwayiUPA00659
BRENDAi4.2.1.17, 5301
ReactomeiR-RNO-390247, Beta-oxidation of very long chain fatty acids
R-RNO-9033241, Peroxisomal protein import
SABIO-RKiP07896

Miscellaneous databases

EvolutionaryTraceiP07896

Protein Ontology

More...
PROi
PR:P07896

Gene expression databases

BgeeiENSRNOG00000001770, Expressed in liver and 19 other tissues
GenevisibleiP07896, RN

Family and domain databases

InterProiView protein in InterPro
IPR006180, 3-OHacyl-CoA_DH_CS
IPR006176, 3-OHacyl-CoA_DH_NAD-bd
IPR006108, 3HC_DH_C
IPR008927, 6-PGluconate_DH-like_C_sf
IPR029045, ClpP/crotonase-like_dom_sf
IPR018376, Enoyl-CoA_hyd/isom_CS
IPR001753, Enoyl-CoA_hydra/iso
IPR036291, NAD(P)-bd_dom_sf
PfamiView protein in Pfam
PF00725, 3HCDH, 2 hits
PF02737, 3HCDH_N, 1 hit
PF00378, ECH_1, 1 hit
SUPFAMiSSF48179, SSF48179, 2 hits
SSF51735, SSF51735, 1 hit
SSF52096, SSF52096, 1 hit
PROSITEiView protein in PROSITE
PS00067, 3HCDH, 1 hit
PS00166, ENOYL_COA_HYDRATASE, 1 hit

MobiDB: a database of protein disorder and mobility annotations

More...
MobiDBi
Search...

<p>This section provides general information on the entry.<p><a href='/help/entry_information_section' target='_top'>More...</a></p>Entry informationi

<p>This subsection of the 'Entry information' section provides a mnemonic identifier for a UniProtKB entry, but it is not a stable identifier. Each reviewed entry is assigned a unique entry name upon integration into UniProtKB/Swiss-Prot.<p><a href='/help/entry_name' target='_top'>More...</a></p>Entry nameiECHP_RAT
<p>This subsection of the 'Entry information' section provides one or more accession number(s). These are stable identifiers and should be used to cite UniProtKB entries. Upon integration into UniProtKB, each entry is assigned a unique accession number, which is called 'Primary (citable) accession number'.<p><a href='/help/accession_numbers' target='_top'>More...</a></p>AccessioniPrimary (citable) accession number: P07896
Secondary accession number(s): Q5EBD2
<p>This subsection of the 'Entry information' section shows the date of integration of the entry into UniProtKB, the date of the last sequence update and the date of the last annotation modification ('Last modified'). The version number for both the entry and the <a href="http://www.uniprot.org/help/canonical%5Fand%5Fisoforms">canonical sequence</a> are also displayed.<p><a href='/help/entry_history' target='_top'>More...</a></p>Entry historyiIntegrated into UniProtKB/Swiss-Prot: August 1, 1988
Last sequence update: January 23, 2007
Last modified: May 25, 2022
This is version 185 of the entry and version 2 of the sequence. See complete history.
<p>This subsection of the 'Entry information' section indicates whether the entry has been manually annotated and reviewed by UniProtKB curators or not, in other words, if the entry belongs to the Swiss-Prot section of UniProtKB (<strong>reviewed</strong>) or to the computer-annotated TrEMBL section (<strong>unreviewed</strong>).<p><a href='/help/entry_status' target='_top'>More...</a></p>Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

<p>This section contains any relevant information that doesn't fit in any other defined sections<p><a href='/help/miscellaneous_section' target='_top'>More...</a></p>Miscellaneousi

Keywords - Technical termi

3D-structure, Direct protein sequencing, Reference proteome

Documents

  1. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. SIMILARITY comments
    Index of protein domains and families
UniProt is an ELIXIR core data resource
Main funding by: National Institutes of Health

We'd like to inform you that we have updated our Privacy Notice to comply with Europe’s new General Data Protection Regulation (GDPR) that applies since 25 May 2018.

Do not show this banner again