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Protein

3-hydroxyisobutyryl-CoA hydrolase, mitochondrial

Gene

EHD3

Organism
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein 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). Has an indirect role in endocytic membrane trafficking. May have a function in protein biosynthesis in mitochondrial small ribosomal subunit.By similarity2 Publications

Catalytic activityi

3-hydroxy-2-methylpropanoyl-CoA + H2O = CoA + 3-hydroxy-2-methylpropanoate.1 Publication

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)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei124 – 1241SubstrateBy similarity
Binding sitei149 – 1491Substrate; via amide nitrogenBy similarity
Binding sitei172 – 1721SubstrateBy similarity
Binding sitei180 – 1801SubstrateBy similarity

GO - Molecular functioni

  • 3-hydroxyisobutyryl-CoA hydrolase activity Source: SGD
  • hydro-lyase activity Source: InterPro

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Hydrolase

Keywords - Biological processi

Branched-chain amino acid catabolism

Enzyme and pathway databases

BioCyciYEAST:G3O-29650-MONOMER.
ReactomeiR-SCE-70895. Branched-chain amino acid catabolism.
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:EHD3
Synonyms:MRP5
Ordered Locus Names:YDR036C
ORF Names:YD9673.08C
OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Taxonomic identifieri559292 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
Proteomesi
  • UP000002311 Componenti: Chromosome IV

Organism-specific databases

EuPathDBiFungiDB:YDR036C.
SGDiS000002443. EHD3.

Subcellular locationi

GO - Cellular componenti

  • mitochondrion Source: SGD
Complete GO annotation...

Keywords - Cellular componenti

Mitochondrion

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini? – 5003-hydroxyisobutyryl-CoA hydrolase, mitochondrialPRO_0000109357
Transit peptidei1 – ?MitochondrionBy similarity

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei326 – 3261PhosphothreonineCombined sources

Keywords - PTMi

Phosphoprotein

Proteomic databases

MaxQBiP28817.
PeptideAtlasiP28817.

PTM databases

iPTMnetiP28817.

Interactioni

Protein-protein interaction databases

BioGridi32091. 33 interactions.
DIPiDIP-6509N.
IntActiP28817. 23 interactions.
MINTiMINT-615925.

Structurei

3D structure databases

ProteinModelPortaliP28817.
SMRiP28817. Positions 39-370.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Keywords - Domaini

Transit peptide

Phylogenomic databases

GeneTreeiENSGT00570000079226.
HOGENOMiHOG000217005.
InParanoidiP28817.
KOiK05605.
OMAiATENTKW.
OrthoDBiEOG75TMNR.

Family and domain databases

Gene3Di3.90.226.10. 1 hit.
InterProiIPR029045. ClpP/crotonase-like_dom.
IPR018376. Enoyl-CoA_hyd/isom_CS.
IPR032259. HIBYL-CoA-H.
[Graphical view]
PfamiPF16113. ECH_2. 1 hit.
[Graphical view]
SUPFAMiSSF52096. SSF52096. 2 hits.
PROSITEiPS00166. ENOYL_COA_HYDRATASE. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

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

P28817-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MLRNTLKCAQ LSSKYGFKTT TRTFMTTQPQ LNVTDAPPVL FTVQDTARVI
60 70 80 90 100
TLNRPKKLNA LNAEMSESMF KTLNEYAKSD TTNLVILKSS NRPRSFCAGG
110 120 130 140 150
DVATVAIFNF NKEFAKSIKF FTDEYSLNFQ IATYLKPIVT FMDGITMGGG
160 170 180 190 200
VGLSIHTPFR IATENTKWAM PEMDIGFFPD VGSTFALPRI VTLANSNSQM
210 220 230 240 250
ALYLCLTGEV VTGADAYMLG LASHYVSSEN LDALQKRLGE ISPPFNNDPQ
260 270 280 290 300
SAYFFGMVNE SIDEFVSPLP KDYVFKYSNE KLNVIEACFN LSKNGTIEDI
310 320 330 340 350
MNNLRQYEGS AEGKAFAQEI KTKLLTKSPS SLQIALRLVQ ENSRDHIESA
360 370 380 390 400
IKRDLYTAAN MCMNQDSLVE FSEATKHKLI DKQRVPYPWT KKEQLFVSQL
410 420 430 440 450
TSITSPKPSL PMSLLRNTSN VTWTQYPYHS KYQLPTEQEI AAYIEKRTND
460 470 480 490 500
DTGAKVTERE VLNHFANVIP SRRGKLGIQS LCKIVCERKC EEVNDGLRWK
Length:500
Mass (Da):56,288
Last modified:November 1, 1997 - v2
Checksum:i7187506B4F4BCDC6
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti139 – 1391V → A in AAU09686 (PubMed:17322287).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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.
PIRiS61591.
RefSeqiNP_010321.1. NM_001180344.1.

Genome annotation databases

EnsemblFungiiYDR036C; YDR036C; YDR036C.
GeneIDi851606.
KEGGisce:YDR036C.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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.
PIRiS61591.
RefSeqiNP_010321.1. NM_001180344.1.

3D structure databases

ProteinModelPortaliP28817.
SMRiP28817. Positions 39-370.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi32091. 33 interactions.
DIPiDIP-6509N.
IntActiP28817. 23 interactions.
MINTiMINT-615925.

PTM databases

iPTMnetiP28817.

Proteomic databases

MaxQBiP28817.
PeptideAtlasiP28817.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblFungiiYDR036C; YDR036C; YDR036C.
GeneIDi851606.
KEGGisce:YDR036C.

Organism-specific databases

EuPathDBiFungiDB:YDR036C.
SGDiS000002443. EHD3.

Phylogenomic databases

GeneTreeiENSGT00570000079226.
HOGENOMiHOG000217005.
InParanoidiP28817.
KOiK05605.
OMAiATENTKW.
OrthoDBiEOG75TMNR.

Enzyme and pathway databases

UniPathwayiUPA00362.
BioCyciYEAST:G3O-29650-MONOMER.
ReactomeiR-SCE-70895. Branched-chain amino acid catabolism.

Miscellaneous databases

PROiP28817.

Family and domain databases

Gene3Di3.90.226.10. 1 hit.
InterProiIPR029045. ClpP/crotonase-like_dom.
IPR018376. Enoyl-CoA_hyd/isom_CS.
IPR032259. HIBYL-CoA-H.
[Graphical view]
PfamiPF16113. ECH_2. 1 hit.
[Graphical view]
SUPFAMiSSF52096. SSF52096. 2 hits.
PROSITEiPS00166. ENOYL_COA_HYDRATASE. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  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.
    , 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. Cited for: GENOME REANNOTATION.
    Strain: ATCC 204508 / S288c.
  3. 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. "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.
  6. "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.
  7. Cited for: SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
  8. Cited for: LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
  9. "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.
  10. Cited for: SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
    Strain: ATCC 76625 / YPH499.
  11. "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].
  12. "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: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-326, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Strain: ATCC 76625 / YPH499.

Entry informationi

Entry nameiHIBCH_YEAST
AccessioniPrimary (citable) accession number: P28817
Secondary accession number(s): D6VS24, Q66RH2
Entry historyi
Integrated into UniProtKB/Swiss-Prot: December 1, 1992
Last sequence update: November 1, 1997
Last modified: June 8, 2016
This is version 125 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Miscellaneousi

Miscellaneous

Present with 3950 molecules/cell in log phase SD medium.1 Publication

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
  3. Yeast
    Yeast (Saccharomyces cerevisiae): entries, gene names and cross-references to SGD
  4. Yeast chromosome IV
    Yeast (Saccharomyces cerevisiae) chromosome IV: entries and gene names

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.