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Q5ZJ60 (HIBCH_CHICK) Reviewed, UniProtKB/Swiss-Prot

Last modified April 3, 2013. Version 53. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
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Names and origin

Protein namesRecommended 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 names
Name:HIBCH
ORF Names:RCJMB04_20j11
OrganismGallus gallus (Chicken) [Reference proteome]
Taxonomic identifier9031 [NCBI]
Taxonomic lineageEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Archosauria › Dinosauria › Saurischia › Theropoda › Coelurosauria › Aves › Neognathae › Galliformes › Phasianidae › Phasianinae › Gallus

Protein attributes

Sequence length385 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at transcript level

General annotation (Comments)

Function

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.

Catalytic activity

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

Pathway

Amino-acid degradation; L-valine degradation.

Subcellular location

Mitochondrion By similarity.

Sequence similarities

Belongs to the enoyl-CoA hydratase/isomerase family.

Ontologies

Keywords
   Biological processBranched-chain amino acid catabolism
   Cellular componentMitochondrion
   DomainTransit peptide
   Molecular functionHydrolase
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processvaline catabolic process

Inferred from electronic annotation. Source: UniProtKB-UniPathway

   Cellular_componentmitochondrion

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular_function3-hydroxyisobutyryl-CoA hydrolase activity

Inferred from electronic annotation. Source: EC

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Transit peptide1 – ?Mitochondrion Potential
Chain? – 3853-hydroxyisobutyryl-CoA hydrolase, mitochondrialPRO_0000284932

Sites

Binding site1201Substrate By similarity
Binding site1451Substrate; via amide nitrogen By similarity
Binding site1681Substrate By similarity
Binding site1761Substrate By similarity

Sequences

Sequence LengthMass (Da)Tools
Q5ZJ60 [UniParc].

Last modified November 23, 2004. Version 1.
Checksum: C9737F7C2F3DE7DA

FASTA38542,829
        10         20         30         40         50         60 
MAARVLMAPR RLKPFNRLQV ILQHLKTCKH TDSAADVLLQ KQGGAGIITL NRPKVLNALS 

        70         80         90        100        110        120 
FKMIQQIYPQ IKAWEQDPET FLIIIKGTGE KAFCAGGDVR AIADAGKAGD TMTRDYFREE 

       130        140        150        160        170        180 
YRLDNAIGTC KKPYVALIDG ITMGGGVGLS VHGHFRVATE KTVFAMPETA IGLFPDVGGG 

       190        200        210        220        230        240 
YFLPRLSGKI GHLLALTGFR LKGRDVLKAG IATHFVESGK LPELEKDLIA LKSPSKENIA 

       250        260        270        280        290        300 
DLLNSYHMQT KIDQEKEFVL DEHMERINSI FSANSMEEIV QKLKQDGSPF ATKQLEAINK 

       310        320        330        340        350        360 
MSPTSLKLTL RQLREGATMS LQDVFTMEYR LSQACMRGHD FYEGVRAVLI DKDQSPRWKP 

       370        380 
AALEEVSDEF VDNCFKPLGN NDLKL

« Hide

References

[1]"Full-length cDNAs from chicken bursal lymphocytes to facilitate gene function analysis."
Caldwell R.B., Kierzek A.M., Arakawa H., Bezzubov Y., Zaim J., Fiedler P., Kutter S., Blagodatski A., Kostovska D., Koter M., Plachy J., Carninci P., Hayashizaki Y., Buerstedde J.-M.
Genome Biol. 6:R6.1-R6.9(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Strain: CB.
Tissue: Bursa of Fabricius.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		AJ720574 mRNA. Translation: CAG32233.1.
IPIIPI00594431.
RefSeqNP_001026414.1. NM_001031243.1.
UniGeneGga.9512.

3D structure databases

HSSPHSSP built from PDB template 1MJ3 based on UniProtKB P14604.
ProteinModelPortalQ5ZJ60.
SMRQ5ZJ60. Positions 31-385.
ModBaseSearch...

Protein-protein interaction databases

STRING9031.ENSGALP00000003623.

Proteomic databases

PaxDbQ5ZJ60.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID423979.
KEGGgga:423979.

Organism-specific databases

CTD26275.

Phylogenomic databases

eggNOGCOG1024.
HOGENOMHOG000217005.
HOVERGENHBG054809.
InParanoidQ5ZJ60.
KOK05605.
OrthoDBEOG4G7BZM.

Enzyme and pathway databases

UniPathwayUPA00362.

Family and domain databases

Gene3D1.10.12.10. 1 hit.
InterProIPR014748. Crontonase_C.
[Graphical view]
PROSITEPS00166. ENOYL_COA_HYDRATASE. False negative.
[Graphical view]
ProtoNetSearch...

Other

NextBio20826370.

Entry information

Entry nameHIBCH_CHICK
AccessionPrimary (citable) accession number: Q5ZJ60
Entry history
Integrated into UniProtKB/Swiss-Prot: May 1, 2007
Last sequence update: November 23, 2004
Last modified: April 3, 2013
This is version 53 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

PATHWAY comments

Index of metabolic and biosynthesis pathways

SIMILARITY comments

Index of protein domains and families

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