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P28817 (HIBCH_YEAST) Reviewed, UniProtKB/Swiss-Prot

Last modified May 1, 2013. Version 100. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (4) | 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:EHD3
Synonyms:MRP5
Ordered Locus Names:YDR036C
ORF Names:YD9673.08C
OrganismSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) [Reference proteome]
Taxonomic identifier559292 [NCBI]
Taxonomic lineageEukaryota › Fungi › Dikarya › Ascomycota › Saccharomycotina › Saccharomycetes › Saccharomycetales › Saccharomycetaceae › Saccharomyces ›

Protein attributes

Sequence length500 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. Has an indirect role in endocytic membrane trafficking. May have a function in protein biosynthesis in mitochondrial small ribosomal subunit. Ref.6 Ref.10

Catalytic activity

3-hydroxy-2-methylpropanoyl-CoA + H2O = CoA + 3-hydroxy-2-methylpropanoate. Ref.7

Pathway

Amino-acid degradation; L-valine degradation.

Subcellular location

Mitochondrion Ref.5 Ref.8 Ref.11 Ref.12.

Miscellaneous

Present with 3950 molecules/cell in log phase SD medium.

Sequence similarities

Belongs to the enoyl-CoA hydratase/isomerase family.

Ontologies

Keywords
   Biological processBranched-chain amino acid catabolism
   Cellular componentMitochondrion
   DomainTransit peptide
   Molecular functionHydrolase
   PTMPhosphoprotein
   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 Ref.8Ref.11Ref.12PubMed 17054397. Source: SGD

   Molecular_function3-hydroxyisobutyryl-CoA hydrolase activity

Inferred from direct assay Ref.7. Source: SGD

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Transit peptide1 – ?Mitochondrion By similarity
Chain? – 5003-hydroxyisobutyryl-CoA hydrolase, mitochondrialPRO_0000109357

Sites

Binding site1241Substrate By similarity
Binding site1491Substrate; via amide nitrogen By similarity
Binding site1721Substrate By similarity
Binding site1801Substrate By similarity

Amino acid modifications

Modified residue3261Phosphothreonine Ref.5
Modified residue3281Phosphoserine Ref.5

Experimental info

Sequence conflict1391V → A in AAU09686. Ref.3

Sequences

Sequence LengthMass (Da)Tools
P28817 [UniParc].

Last modified November 1, 1997. Version 2.
Checksum: 7187506B4F4BCDC6

FASTA50056,288
        10         20         30         40         50         60 
MLRNTLKCAQ LSSKYGFKTT TRTFMTTQPQ LNVTDAPPVL FTVQDTARVI TLNRPKKLNA 

        70         80         90        100        110        120 
LNAEMSESMF KTLNEYAKSD TTNLVILKSS NRPRSFCAGG DVATVAIFNF NKEFAKSIKF 

       130        140        150        160        170        180 
FTDEYSLNFQ IATYLKPIVT FMDGITMGGG VGLSIHTPFR IATENTKWAM PEMDIGFFPD 

       190        200        210        220        230        240 
VGSTFALPRI VTLANSNSQM ALYLCLTGEV VTGADAYMLG LASHYVSSEN LDALQKRLGE 

       250        260        270        280        290        300 
ISPPFNNDPQ SAYFFGMVNE SIDEFVSPLP KDYVFKYSNE KLNVIEACFN LSKNGTIEDI 

       310        320        330        340        350        360 
MNNLRQYEGS AEGKAFAQEI KTKLLTKSPS SLQIALRLVQ ENSRDHIESA IKRDLYTAAN 

       370        380        390        400        410        420 
MCMNQDSLVE FSEATKHKLI DKQRVPYPWT KKEQLFVSQL TSITSPKPSL PMSLLRNTSN 

       430        440        450        460        470        480 
VTWTQYPYHS KYQLPTEQEI AAYIEKRTND DTGAKVTERE VLNHFANVIP SRRGKLGIQS 

       490        500 
LCKIVCERKC EEVNDGLRWK

« Hide

References

« Hide 'large scale' references
[1]"The nucleotide sequence of Saccharomyces cerevisiae chromosome IV."
Jacq C., Alt-Moerbe J., Andre B., Arnold W., Bahr A., Ballesta J.P.G., Bargues M., Baron L., Becker A., Biteau N., Bloecker H., Blugeon C., Boskovic J., Brandt P., Brueckner M., Buitrago M.J., Coster F., Delaveau T. expand/collapse author list , del Rey F., Dujon B., Eide L.G., Garcia-Cantalejo J.M., Goffeau A., Gomez-Peris A., Granotier C., Hanemann V., Hankeln T., Hoheisel J.D., Jaeger W., Jimenez A., Jonniaux J.-L., Kraemer C., Kuester H., Laamanen P., Legros Y., Louis E.J., Moeller-Rieker S., Monnet A., Moro M., Mueller-Auer S., Nussbaumer B., Paricio N., Paulin L., Perea J., Perez-Alonso M., Perez-Ortin J.E., Pohl T.M., Prydz H., Purnelle B., Rasmussen S.W., Remacha M.A., Revuelta J.L., Rieger M., Salom D., Saluz H.P., Saiz J.E., Saren A.-M., Schaefer M., Scharfe M., Schmidt E.R., Schneider C., Scholler P., Schwarz S., Soler-Mira A., Urrestarazu L.A., Verhasselt P., Vissers S., Voet M., Volckaert G., Wagner G., Wambutt R., Wedler E., Wedler H., Woelfl S., Harris D.E., Bowman S., Brown D., Churcher C.M., Connor R., Dedman K., Gentles S., Hamlin N., Hunt S., Jones L., McDonald S., Murphy L.D., Niblett D., Odell C., Oliver K., Rajandream M.A., Richards C., Shore L., Walsh S.V., Barrell B.G., Dietrich F.S., Mulligan J.T., Allen E., Araujo R., Aviles E., Berno A., Carpenter J., Chen E., Cherry J.M., Chung E., Duncan M., Hunicke-Smith S., Hyman R.W., Komp C., Lashkari D., Lew H., Lin D., Mosedale D., Nakahara K., Namath A., Oefner P., Oh C., Petel F.X., Roberts D., Schramm S., Schroeder M., Shogren T., Shroff N., Winant A., Yelton M.A., Botstein D., Davis R.W., Johnston M., Andrews S., Brinkman R., Cooper J., Ding H., Du Z., Favello A., Fulton L., Gattung S., Greco T., Hallsworth K., Hawkins J., Hillier L.W., Jier M., Johnson D., Johnston L., Kirsten J., Kucaba T., Langston Y., Latreille P., Le T., Mardis E., Menezes S., Miller N., Nhan M., Pauley A., Peluso D., Rifkin L., Riles L., Taich A., Trevaskis E., Vignati D., Wilcox L., Wohldman P., Vaudin M., Wilson R., Waterston R., Albermann K., Hani J., Heumann K., Kleine K., Mewes H.-W., Zollner A., Zaccaria P.
Nature 387:75-78(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 204508 / S288c.
[2]Saccharomyces Genome Database
Submitted (DEC-2009) to the EMBL/GenBank/DDBJ databases
Cited for: GENOME REANNOTATION.
Strain: ATCC 204508 / S288c.
[3]"Approaching a complete repository of sequence-verified protein-encoding clones for Saccharomyces cerevisiae."
Hu Y., Rolfs A., Bhullar B., Murthy T.V.S., Zhu C., Berger M.F., Camargo A.A., Kelley F., McCarron S., Jepson D., Richardson A., Raphael J., Moreira D., Taycher E., Zuo D., Mohr S., Kane M.F., Williamson J. expand/collapse author list , Simpson A.J.G., Bulyk M.L., Harlow E., Marsischky G., Kolodner R.D., LaBaer J.
Genome Res. 17:536-543(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: ATCC 204508 / S288c.
[4]"The yeast lysyl-tRNA synthetase gene. Evidence for general amino acid control of its expression and domain structure of the encoded protein."
Mirande M., Waller J.-P.
J. Biol. Chem. 263:18443-18451(1988) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-265.
Strain: ATCC 26109 / X2180.
[5]"Profiling phosphoproteins of yeast mitochondria reveals a role of phosphorylation in assembly of the ATP synthase."
Reinders J., Wagner K., Zahedi R.P., Stojanovski D., Eyrich B., van der Laan M., Rehling P., Sickmann A., Pfanner N., Meisinger C.
Mol. Cell. Proteomics 6:1896-1906(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 324-337, SUBCELLULAR LOCATION, PHOSPHORYLATION AT THR-326 AND SER-328, MASS SPECTROMETRY.
Strain: ATCC 76625 / YPH499.
[6]"Identification and characterization of Saccharomyces cerevisiae mutants defective in fluid-phase endocytosis."
Wiederkehr A., Meier K.D., Riezman H.
Yeast 18:759-773(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION.
[7]"The biochemistry of peroxisomal beta-oxidation in the yeast Saccharomyces cerevisiae."
Hiltunen J.K., Mursula A.M., Rottensteiner H., Wierenga R.K., Kastaniotis A.J., Gurvitz A.
FEMS Microbiol. Rev. 27:35-64(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: ENZYME ACTIVITY.
[8]"Global analysis of protein localization in budding yeast."
Huh W.-K., Falvo J.V., Gerke L.C., Carroll A.S., Howson R.W., Weissman J.S., O'Shea E.K.
Nature 425:686-691(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
[9]"Global analysis of protein expression in yeast."
Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A., Dephoure N., O'Shea E.K., Weissman J.S.
Nature 425:737-741(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
[10]"Predicting protein functions from redundancies in large-scale protein interaction networks."
Samanta M.P., Liang S.
Proc. Natl. Acad. Sci. U.S.A. 100:12579-12583(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION.
[11]"The proteome of Saccharomyces cerevisiae mitochondria."
Sickmann A., Reinders J., Wagner Y., Joppich C., Zahedi R.P., Meyer H.E., Schoenfisch B., Perschil I., Chacinska A., Guiard B., Rehling P., Pfanner N., Meisinger C.
Proc. Natl. Acad. Sci. U.S.A. 100:13207-13212(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS], MASS SPECTROMETRY.
Strain: ATCC 76625 / YPH499.
[12]"Toward the complete yeast mitochondrial proteome: multidimensional separation techniques for mitochondrial proteomics."
Reinders J., Zahedi R.P., Pfanner N., Meisinger C., Sickmann A.
J. Proteome Res. 5:1543-1554(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS], MASS SPECTROMETRY.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		Z68196 Genomic DNA. Translation: CAA92375.1.
Z74332 Genomic DNA. Translation: CAA98862.1.
AY723769 Genomic DNA. Translation: AAU09686.1.
J04186 Genomic DNA. Translation: AAA66915.1.
BK006938 Genomic DNA. Translation: DAA11884.1.
PIRS61591.
RefSeqNP_010321.1. NM_001180344.1.

3D structure databases

ProteinModelPortalP28817.
SMRP28817. Positions 39-370.
ModBaseSearch...

Protein-protein interaction databases

DIPDIP-6509N.
IntActP28817. 23 interactions.
MINTMINT-615925.
STRING4932.YDR036C.

Proteomic databases

PaxDbP28817.
PeptideAtlasP28817.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblFungiYDR036C; YDR036C; YDR036C.
GeneID851606.
KEGGsce:YDR036C.

Organism-specific databases

CYGDYDR036c.
SGDS000002443. EHD3.

Phylogenomic databases

eggNOGCOG1024.
GeneTreeENSGT00570000079226.
HOGENOMHOG000217005.
KOK05605.
OMAKLAMPEM.
OrthoDBEOG4ZW8KR.

Enzyme and pathway databases

UniPathwayUPA00362.

Gene expression databases

GenevestigatorP28817.
GermOnlineYDR036C. Saccharomyces cerevisiae.

Family and domain databases

InterProIPR001753. Crotonase_core_superfam.
IPR018376. Enoyl-CoA_hyd/isom_CS.
[Graphical view]
PfamPF00378. ECH. 1 hit.
[Graphical view]
PROSITEPS00166. ENOYL_COA_HYDRATASE. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

NextBio969112.

Entry information

Entry nameHIBCH_YEAST
AccessionPrimary (citable) accession number: P28817
Secondary accession number(s): D6VS24, Q66RH2
Entry history
Integrated into UniProtKB/Swiss-Prot: December 1, 1992
Last sequence update: November 1, 1997
Last modified: May 1, 2013
This is version 100 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Relevant documents

Yeast

Yeast (Saccharomyces cerevisiae): entries, gene names and cross-references to SGD

Yeast chromosome IV

Yeast (Saccharomyces cerevisiae) chromosome IV: entries and gene names

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