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Protein

3-hydroxyisobutyryl-CoA hydrolase, mitochondrial

Gene

HIBCH

Organism
Bos taurus (Bovine)
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Experimental evidence at transcript leveli

Functioni

Hydrolyzes 3-hydroxyisobutyryl-CoA (HIBYL-CoA), a saline catabolite. Has high activity toward isobutyryl-CoA. Could be an isobutyryl-CoA dehydrogenase that functions in valine catabolism. Also hydrolyzes 3-hydroxypropanoyl-CoA (By similarity).By similarity

Catalytic activityi

3-hydroxy-2-methylpropanoyl-CoA + H2O = CoA + 3-hydroxy-2-methylpropanoate.

Pathwayi: L-valine degradation

This protein is involved in the pathway L-valine degradation, which is part of Amino-acid degradation.
View all proteins of this organism that are known to be involved in the pathway L-valine degradation and in Amino-acid degradation.

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Binding sitei121SubstrateBy similarity1
Binding sitei146Substrate; via amide nitrogenBy similarity1
Binding sitei169SubstrateBy similarity1
Binding sitei177SubstrateBy similarity1

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Hydrolase

Keywords - Biological processi

Branched-chain amino acid catabolism

Enzyme and pathway databases

UniPathwayiUPA00362.

Names & Taxonomyi

Protein namesi
Recommended name:
3-hydroxyisobutyryl-CoA hydrolase, mitochondrial (EC:3.1.2.4)
Alternative name(s):
3-hydroxyisobutyryl-coenzyme A hydrolase
Short name:
HIB-CoA hydrolase
Short name:
HIBYL-CoA-H
Gene namesi
Name:HIBCH
OrganismiBos taurus (Bovine)
Taxonomic identifieri9913 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaLaurasiatheriaCetartiodactylaRuminantiaPecoraBovidaeBovinaeBos
Proteomesi
  • UP000009136 Componenti: Unplaced

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Mitochondrion

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Transit peptidei1 – 32MitochondrionBy similarityAdd BLAST32
ChainiPRO_000028492833 – 3863-hydroxyisobutyryl-CoA hydrolase, mitochondrialAdd BLAST354

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei92N6-acetyllysine; alternateBy similarity1
Modified residuei92N6-succinyllysine; alternateBy similarity1
Modified residuei221N6-acetyllysine; alternateBy similarity1
Modified residuei221N6-succinyllysine; alternateBy similarity1
Modified residuei234PhosphoserineBy similarity1
Modified residuei250N6-succinyllysineBy similarity1
Modified residuei257N6-succinyllysineBy similarity1
Modified residuei297N6-acetyllysine; alternateBy similarity1
Modified residuei297N6-succinyllysine; alternateBy similarity1
Modified residuei301N6-succinyllysineBy similarity1
Modified residuei353N6-acetyllysine; alternateBy similarity1
Modified residuei353N6-succinyllysine; alternateBy similarity1
Modified residuei356PhosphoserineBy similarity1
Modified residuei360N6-acetyllysineBy similarity1
Modified residuei365N6-acetyllysineBy similarity1
Modified residuei377N6-succinyllysineBy similarity1

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

PeptideAtlasiQ2HJ73.
PRIDEiQ2HJ73.

Structurei

3D structure databases

ProteinModelPortaliQ2HJ73.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Keywords - Domaini

Transit peptide

Phylogenomic databases

HOGENOMiHOG000217005.
HOVERGENiHBG054809.
InParanoidiQ2HJ73.
KOiK05605.

Family and domain databases

Gene3Di1.10.12.10. 1 hit.
3.90.226.10. 1 hit.
InterProiIPR029045. ClpP/crotonase-like_dom.
IPR014748. Crontonase_C.
IPR032259. HIBYL-CoA-H.
[Graphical view]
PfamiPF16113. ECH_2. 1 hit.
[Graphical view]
SUPFAMiSSF52096. SSF52096. 2 hits.

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

Q2HJ73-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MGLQGLCRLM SRFNSYKRTN IILQHLKMSN HTDAAAEVLL ERKGCAGVIT
60 70 80 90 100
LNRPRFLNTL TLGMIRQIYA QLKKWEQDPK TFLIIIKGAG EKAFCAGGDI
110 120 130 140 150
RALSEARNTN QKMLQDLFRE EYILNNAIDS CQKPYIALIH GITMGGGVGV
160 170 180 190 200
SVHGQFRVAT EKSVFAMPET AIGLFPDVGG GYFLPRLQGK LGYFLALTGF
210 220 230 240 250
RLKGRDVYTA GIATHFVDFE KLGMLEEDLL ALKSPSKENI ADVLETYHAK
260 270 280 290 300
SKTDQDKPFI LEEHMDKINS WFSANTVEQI VDNLQQDGSS FALEQLKVIK
310 320 330 340 350
KMSPTSLKIT LRQLMEGSSK TLPEVLIMEY RLSQACMKGH DFHEGVRAVL
360 370 380
IDKDQSPKWK PADLKEVTDE DLNDYFKSLG SNDLKF
Length:386
Mass (Da):43,349
Last modified:March 21, 2006 - v1
Checksum:i3920F7D82D6CBB09
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
BC113274 mRNA. Translation: AAI13275.1.
RefSeqiXP_010800133.1. XM_010801831.1.
XP_015317723.1. XM_015462237.1.
UniGeneiBt.56752.

Genome annotation databases

GeneIDi535883.
KEGGibta:535883.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
BC113274 mRNA. Translation: AAI13275.1.
RefSeqiXP_010800133.1. XM_010801831.1.
XP_015317723.1. XM_015462237.1.
UniGeneiBt.56752.

3D structure databases

ProteinModelPortaliQ2HJ73.
ModBaseiSearch...
MobiDBiSearch...

Proteomic databases

PeptideAtlasiQ2HJ73.
PRIDEiQ2HJ73.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

GeneIDi535883.
KEGGibta:535883.

Organism-specific databases

CTDi26275.

Phylogenomic databases

HOGENOMiHOG000217005.
HOVERGENiHBG054809.
InParanoidiQ2HJ73.
KOiK05605.

Enzyme and pathway databases

UniPathwayiUPA00362.

Family and domain databases

Gene3Di1.10.12.10. 1 hit.
3.90.226.10. 1 hit.
InterProiIPR029045. ClpP/crotonase-like_dom.
IPR014748. Crontonase_C.
IPR032259. HIBYL-CoA-H.
[Graphical view]
PfamiPF16113. ECH_2. 1 hit.
[Graphical view]
SUPFAMiSSF52096. SSF52096. 2 hits.
ProtoNetiSearch...

Entry informationi

Entry nameiHIBCH_BOVIN
AccessioniPrimary (citable) accession number: Q2HJ73
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 1, 2007
Last sequence update: March 21, 2006
Last modified: October 5, 2016
This is version 80 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  2. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.