ID   HIBCH_DICDI             Reviewed;         381 AA.
AC   Q55GS6;
DT   08-APR-2008, integrated into UniProtKB/Swiss-Prot.
DT   24-MAY-2005, sequence version 1.
DT   03-AUG-2022, entry version 100.
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=hibch; ORFNames=DDB_G0267536;
OS   Dictyostelium discoideum (Slime mold).
OC   Eukaryota; Amoebozoa; Evosea; Eumycetozoa; Dictyostelia; Dictyosteliales;
OC   Dictyosteliaceae; Dictyostelium.
OX   NCBI_TaxID=44689;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=AX4;
RX   PubMed=15875012; DOI=10.1038/nature03481;
RA   Eichinger L., Pachebat J.A., Gloeckner G., Rajandream M.A., Sucgang R.,
RA   Berriman M., Song J., Olsen R., Szafranski K., Xu Q., Tunggal B.,
RA   Kummerfeld S., Madera M., Konfortov B.A., Rivero F., Bankier A.T.,
RA   Lehmann R., Hamlin N., Davies R., Gaudet P., Fey P., Pilcher K., Chen G.,
RA   Saunders D., Sodergren E.J., Davis P., Kerhornou A., Nie X., Hall N.,
RA   Anjard C., Hemphill L., Bason N., Farbrother P., Desany B., Just E.,
RA   Morio T., Rost R., Churcher C.M., Cooper J., Haydock S., van Driessche N.,
RA   Cronin A., Goodhead I., Muzny D.M., Mourier T., Pain A., Lu M., Harper D.,
RA   Lindsay R., Hauser H., James K.D., Quiles M., Madan Babu M., Saito T.,
RA   Buchrieser C., Wardroper A., Felder M., Thangavelu M., Johnson D.,
RA   Knights A., Loulseged H., Mungall K.L., Oliver K., Price C., Quail M.A.,
RA   Urushihara H., Hernandez J., Rabbinowitsch E., Steffen D., Sanders M.,
RA   Ma J., Kohara Y., Sharp S., Simmonds M.N., Spiegler S., Tivey A.,
RA   Sugano S., White B., Walker D., Woodward J.R., Winckler T., Tanaka Y.,
RA   Shaulsky G., Schleicher M., Weinstock G.M., Rosenthal A., Cox E.C.,
RA   Chisholm R.L., Gibbs R.A., Loomis W.F., Platzer M., Kay R.R.,
RA   Williams J.G., Dear P.H., Noegel A.A., Barrell B.G., Kuspa A.;
RT   "The genome of the social amoeba Dictyostelium discoideum.";
RL   Nature 435:43-57(2005).
CC   -!- FUNCTION: Hydrolyzes 3-hydroxyisobutyryl-CoA (HIBYL-CoA), a saline
CC       catabolite. {ECO:0000250}.
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   -!- PATHWAY: Amino-acid degradation; L-valine degradation.
CC   -!- SUBCELLULAR LOCATION: Mitochondrion {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the enoyl-CoA hydratase/isomerase family.
CC       {ECO:0000305}.
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DR   EMBL; AAFI02000003; EAL73221.1; -; Genomic_DNA.
DR   RefSeq; XP_647108.1; XM_642016.1.
DR   AlphaFoldDB; Q55GS6; -.
DR   SMR; Q55GS6; -.
DR   STRING; 44689.DDB0233831; -.
DR   PaxDb; Q55GS6; -.
DR   EnsemblProtists; EAL73221; EAL73221; DDB_G0267536.
DR   GeneID; 8615912; -.
DR   KEGG; ddi:DDB_G0267536; -.
DR   dictyBase; DDB_G0267536; hibch.
DR   eggNOG; KOG1684; Eukaryota.
DR   HOGENOM; CLU_009834_22_1_1; -.
DR   InParanoid; Q55GS6; -.
DR   OMA; GKPYIAF; -.
DR   PhylomeDB; Q55GS6; -.
DR   Reactome; R-DDI-70895; Branched-chain amino acid catabolism.
DR   UniPathway; UPA00362; -.
DR   PRO; PR:Q55GS6; -.
DR   Proteomes; UP000002195; Chromosome 1.
DR   GO; GO:0005739; C:mitochondrion; IBA:GO_Central.
DR   GO; GO:0003860; F:3-hydroxyisobutyryl-CoA hydrolase activity; ISS:dictyBase.
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   3: Inferred from homology;
KW   Branched-chain amino acid catabolism; Hydrolase; Mitochondrion;
KW   Reference proteome; Transit peptide.
FT   TRANSIT         1..25
FT                   /note="Mitochondrion"
FT                   /evidence="ECO:0000255"
FT   CHAIN           26..381
FT                   /note="3-hydroxyisobutyryl-CoA hydrolase, mitochondrial"
FT                   /id="PRO_0000327927"
FT   BINDING         116
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         141
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         164
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         172
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   381 AA;  42882 MW;  E95B4541434ECD30 CRC64;
     MDRLLTISNH IGKNIRQFST STEEVLFEKK GKCLKVLLNR PKALNALNPN MVKILTPKYL
     EMKTKKDGEG VIVMKGAGEK AFCAGGDIRA IYDYKQLNEE QKSKTNDIGD LFFREEYILN
     NLIGTNPIAQ VSIYNGFAMG GGIGLSVHGK FRVATENTVF AMPETGIGFF CDVGGSYFLP
     RLPNNYGMYL ALTGSKLKGN NVYLAGVATH FVSNEHIQAL EKEIEECENP TSQTINSILT
     KYHDKSKSTS NEYNDNLGDI ERIFGKNSVK EIFEQLELLE NSEWAKQTLK TLKSVSPSSL
     MVVFEQMKQG AKLPSLAKCL EMEFRISQHF LEKPDFFEGV RALLVDKDKN PKWLPPSIDQ
     IDQTLVNSYF KPLSNNKELK F