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Q8QZS1 (HIBCH_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified April 3, 2013. Version 82. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

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
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Mus › Mus

Protein attributes

Sequence length385 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein 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
   PTMAcetylation
   Technical termComplete proteome
Direct protein sequencing
Reference proteome
Gene Ontology (GO)
   Biological_processvaline catabolic process

Inferred from electronic annotation. Source: UniProtKB-UniPathway

   Cellular_componentmitochondrion

Inferred from direct assay PubMed 18614015. Source: MGI

   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 – 3232Mitochondrion By similarity
Chain33 – 3853533-hydroxyisobutyryl-CoA hydrolase, mitochondrial
PRO_0000284930

Sites

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

Amino acid modifications

Modified residue911N6-acetyllysine By similarity

Sequences

Sequence LengthMass (Da)Tools
Q8QZS1 [UniParc].

Last modified June 1, 2002. Version 1.
Checksum: FC2B45BF4DF4BE55

FASTA38543,038
        10         20         30         40         50         60 
MGQPYAWRLL SRVSSFRRAS VILQHLRMSM HTEAAEVLLE RRGCGGVITL NRPKFLNALS 

        70         80         90        100        110        120 
LNMIRQIYPQ LKTWEQDPDT FLIIIKGAGG KAFCAGGDIK ALSEAKKARQ NLTQDLFREE 

       130        140        150        160        170        180 
YILNNAIASC QKPYVALIDG ITMGGGVGLS VHGQFRVATE RSLFAMPETG IGLFPDVGGG 

       190        200        210        220        230        240 
YFLPRLQGKL GYFLALTGYR LKGRDVHRAG IATHFVDSEK LRVLEEELLA LKSPSAEDVA 

       250        260        270        280        290        300 
GVLESYHAKS KMDQDKSIIF EEHMDKINSC FSANTVEQII ENLRQDGSPF AIEQMKVINK 

       310        320        330        340        350        360 
MSPTSLKITL RQLMEGSSKT LQEVLIMEYR ITQACMEGHD FHEGVRAVLI DKDQTPKWKP 

       370        380 
ANLKDVTDED LNSYFKSLGS SDLKF

« Hide

References

« Hide 'large scale' references
[1]"The transcriptional landscape of the mammalian genome."
Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J. expand/collapse author list , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Strain: C57BL/6J.
[2]"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
The MGC Project Team
Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Strain: FVB/N.
Tissue: Kidney.
[3]Lubec G., Sunyer B., Chen W.-Q.
Submitted (JAN-2009) to UniProtKB
Cited for: PROTEIN SEQUENCE OF 223-232, MASS SPECTROMETRY.
Strain: OF1.
Tissue: Hippocampus.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		AK076038 mRNA. Translation: BAC36138.1.
BC026437 mRNA. Translation: AAH26437.1.
IPIIPI00154047.
RefSeqNP_666220.1. NM_146108.1.
UniGeneMm.222063.

3D structure databases

HSSPHSSP built from PDB template 1MJ3 based on UniProtKB P14604.
ProteinModelPortalQ8QZS1.
SMRQ8QZS1. Positions 34-385.
ModBaseSearch...

Protein-protein interaction databases

STRING10090.ENSMUSP00000045606.

PTM databases

PhosphoSiteQ8QZS1.

Proteomic databases

PaxDbQ8QZS1.
PRIDEQ8QZS1.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000044478; ENSMUSP00000045606; ENSMUSG00000041426.
GeneID227095.
KEGGmmu:227095.
UCSCuc007ayp.1. mouse.

Organism-specific databases

CTD26275.
MGIMGI:1923792. Hibch.

Phylogenomic databases

eggNOGCOG1024.
GeneTreeENSGT00570000079226.
HOGENOMHOG000217005.
HOVERGENHBG054809.
InParanoidQ8QZS1.
KOK05605.
OMALMSGASH.
OrthoDBEOG4G7BZM.

Enzyme and pathway databases

UniPathwayUPA00362.

Gene expression databases

ArrayExpressQ8QZS1.
BgeeQ8QZS1.
CleanExMM_HIBCH.
GenevestigatorQ8QZS1.

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

ChiTaRSHIBCH. mouse.
NextBio378470.
SOURCESearch...

Entry information

Entry nameHIBCH_MOUSE
AccessionPrimary (citable) accession number: Q8QZS1
Entry history
Integrated into UniProtKB/Swiss-Prot: May 1, 2007
Last sequence update: June 1, 2002
Last modified: April 3, 2013
This is version 82 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot

PATHWAY comments

Index of metabolic and biosynthesis pathways

SIMILARITY comments

Index of protein domains and families

to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents