ID   HIBCH_SCHPO             Reviewed;         429 AA.
AC   O74802;
DT   13-NOV-2007, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1998, sequence version 1.
DT   03-AUG-2022, entry version 125.
DE   RecName: Full=3-hydroxyisobutyryl-CoA hydrolase, mitochondrial;
DE            EC=3.1.2.4;
DE   AltName: Full=3-hydroxyisobutyryl-coenzyme A hydrolase;
DE            Short=HIB-CoA hydrolase;
DE            Short=HIBYL-CoA-H;
DE   Flags: Precursor;
GN   Name=ehd3; ORFNames=SPBC2D10.09;
OS   Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Taphrinomycotina;
OC   Schizosaccharomycetes; Schizosaccharomycetales; Schizosaccharomycetaceae;
OC   Schizosaccharomyces.
OX   NCBI_TaxID=284812;
RN   [1] {ECO:0000312|EMBL:CAA21167.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=972 / ATCC 24843;
RX   PubMed=11859360; DOI=10.1038/nature724;
RA   Wood V., Gwilliam R., Rajandream M.A., Lyne M.H., Lyne R., Stewart A.,
RA   Sgouros J.G., Peat N., Hayles J., Baker S.G., Basham D., Bowman S.,
RA   Brooks K., Brown D., Brown S., Chillingworth T., Churcher C.M., Collins M.,
RA   Connor R., Cronin A., Davis P., Feltwell T., Fraser A., Gentles S.,
RA   Goble A., Hamlin N., Harris D.E., Hidalgo J., Hodgson G., Holroyd S.,
RA   Hornsby T., Howarth S., Huckle E.J., Hunt S., Jagels K., James K.D.,
RA   Jones L., Jones M., Leather S., McDonald S., McLean J., Mooney P.,
RA   Moule S., Mungall K.L., Murphy L.D., Niblett D., Odell C., Oliver K.,
RA   O'Neil S., Pearson D., Quail M.A., Rabbinowitsch E., Rutherford K.M.,
RA   Rutter S., Saunders D., Seeger K., Sharp S., Skelton J., Simmonds M.N.,
RA   Squares R., Squares S., Stevens K., Taylor K., Taylor R.G., Tivey A.,
RA   Walsh S.V., Warren T., Whitehead S., Woodward J.R., Volckaert G., Aert R.,
RA   Robben J., Grymonprez B., Weltjens I., Vanstreels E., Rieger M.,
RA   Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Duesterhoeft A.,
RA   Fritzc C., Holzer E., Moestl D., Hilbert H., Borzym K., Langer I., Beck A.,
RA   Lehrach H., Reinhardt R., Pohl T.M., Eger P., Zimmermann W., Wedler H.,
RA   Wambutt R., Purnelle B., Goffeau A., Cadieu E., Dreano S., Gloux S.,
RA   Lelaure V., Mottier S., Galibert F., Aves S.J., Xiang Z., Hunt C.,
RA   Moore K., Hurst S.M., Lucas M., Rochet M., Gaillardin C., Tallada V.A.,
RA   Garzon A., Thode G., Daga R.R., Cruzado L., Jimenez J., Sanchez M.,
RA   del Rey F., Benito J., Dominguez A., Revuelta J.L., Moreno S.,
RA   Armstrong J., Forsburg S.L., Cerutti L., Lowe T., McCombie W.R.,
RA   Paulsen I., Potashkin J., Shpakovski G.V., Ussery D., Barrell B.G.,
RA   Nurse P.;
RT   "The genome sequence of Schizosaccharomyces pombe.";
RL   Nature 415:871-880(2002).
CC   -!- FUNCTION: Hydrolyzes 3-hydroxyisobutyryl-CoA (HIBYL-CoA), a saline
CC       catabolite. Has an indirect role in endocytic membrane trafficking. May
CC       have a function in protein biosynthesis in mitochondrial small
CC       ribosomal subunit (By similarity). {ECO:0000250|UniProtKB:P28817}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=3-hydroxy-2-methylpropanoyl-CoA + H2O = 3-hydroxy-2-
CC         methylpropanoate + CoA + H(+); Xref=Rhea:RHEA:20888,
CC         ChEBI:CHEBI:11805, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:57287, ChEBI:CHEBI:57340; EC=3.1.2.4;
CC         Evidence={ECO:0000250|UniProtKB:P28817};
CC   -!- PATHWAY: Amino-acid degradation; L-valine degradation.
CC       {ECO:0000250|UniProtKB:P28817}.
CC   -!- INTERACTION:
CC       O74802; Q09892: sty1; NbExp=3; IntAct=EBI-16823313, EBI-3648525;
CC   -!- SUBCELLULAR LOCATION: Mitochondrion {ECO:0000250|UniProtKB:Q5XIE6}.
CC   -!- SIMILARITY: Belongs to the enoyl-CoA hydratase/isomerase family.
CC       Mitochondrion-specific ribosomal protein mS47 subfamily. {ECO:0000255}.
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DR   EMBL; CU329671; CAA21167.1; -; Genomic_DNA.
DR   PIR; T40112; T40112.
DR   RefSeq; NP_596228.1; NM_001022148.2.
DR   AlphaFoldDB; O74802; -.
DR   SMR; O74802; -.
DR   BioGRID; 276922; 42.
DR   IntAct; O74802; 4.
DR   STRING; 4896.SPBC2D10.09.1; -.
DR   MaxQB; O74802; -.
DR   PaxDb; O74802; -.
DR   EnsemblFungi; SPBC2D10.09.1; SPBC2D10.09.1:pep; SPBC2D10.09.
DR   GeneID; 2540394; -.
DR   KEGG; spo:SPBC2D10.09; -.
DR   PomBase; SPBC2D10.09; -.
DR   VEuPathDB; FungiDB:SPBC2D10.09; -.
DR   eggNOG; KOG1684; Eukaryota.
DR   HOGENOM; CLU_009834_22_1_1; -.
DR   InParanoid; O74802; -.
DR   OMA; CNHIHTY; -.
DR   PhylomeDB; O74802; -.
DR   Reactome; R-SPO-70895; Branched-chain amino acid catabolism.
DR   UniPathway; UPA00362; -.
DR   PRO; PR:O74802; -.
DR   Proteomes; UP000002485; Chromosome II.
DR   GO; GO:0005763; C:mitochondrial small ribosomal subunit; ISO:PomBase.
DR   GO; GO:0005739; C:mitochondrion; IBA:GO_Central.
DR   GO; GO:0003860; F:3-hydroxyisobutyryl-CoA hydrolase activity; ISO:PomBase.
DR   GO; GO:0032543; P:mitochondrial translation; ISO:PomBase.
DR   GO; GO:0006574; P:valine catabolic process; IBA:GO_Central.
DR   InterPro; IPR029045; ClpP/crotonase-like_dom_sf.
DR   InterPro; IPR045004; ECH_dom.
DR   InterPro; IPR032259; HIBYL-CoA-H.
DR   PANTHER; PTHR43176; PTHR43176; 1.
DR   Pfam; PF16113; ECH_2; 1.
DR   SUPFAM; SSF52096; SSF52096; 1.
PE   1: Evidence at protein level;
KW   Branched-chain amino acid catabolism; Hydrolase; Mitochondrion;
KW   Reference proteome; Ribonucleoprotein; Ribosomal protein; Transit peptide.
FT   TRANSIT         1..?
FT                   /note="Mitochondrion"
FT                   /evidence="ECO:0000250|UniProtKB:Q5XIE6, ECO:0000305"
FT   CHAIN           ?..429
FT                   /note="3-hydroxyisobutyryl-CoA hydrolase, mitochondrial"
FT                   /id="PRO_0000311721"
FT   BINDING         141
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         166
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         189
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         197
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   429 AA;  47934 MW;  4A3BF890ED14FBF3 CRC64;
     MGLKLNISND LKKSGFMLRQ SLLKTSVSNF LSLNASSTMS RAFIRNPKFY STSSNDTVLY
     ESKNGARIFT LNRPKVLNAI NVDMIDSILP KLVSLEESNL AKVIILKGNG RSFSSGGDIK
     AAALSIQDGK LPEVRHAFAQ EYRLSHTLAT YQKPVVALMN GITMGGGSGL AMHVPFRIAC
     EDTMFAMPET GIGYFTDVAA SFFFSRLPGY FGTYLGLTSQ IVKGYDCLRT GIATHFVPKH
     MFPHLEDRLA ELNTSDISKI NNTILEFAEF ASSSPPTFTP DVMDVINKCF CKNDTVDIIR
     ALKEYASNTS ALAEFAKSTV KTLYSKSPTS IAVTNRLIKS AAKWSISEAF YYDHIVSYYM
     LKQPDFVEGV NAQLITKTKN PKWSKSHEYH FKDLENYFKL PSEYNNGISF AAKGRRKTPL
     WNYKTYPYL