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Database: UniProt
Entry: A0A2Y9MVB7_DELLE
LinkDB: A0A2Y9MVB7_DELLE
Original site: A0A2Y9MVB7_DELLE 
ID   A0A2Y9MVB7_DELLE        Unreviewed;       338 AA.
AC   A0A2Y9MVB7;
DT   12-SEP-2018, integrated into UniProtKB/TrEMBL.
DT   12-SEP-2018, sequence version 1.
DT   27-MAR-2024, entry version 19.
DE   RecName: Full=3-hydroxyisobutyryl-CoA hydrolase {ECO:0000256|RuleBase:RU369070};
DE            Short=HIB-CoA hydrolase {ECO:0000256|RuleBase:RU369070};
DE            Short=HIBYL-CoA-H {ECO:0000256|RuleBase:RU369070};
DE            EC=3.1.2.4 {ECO:0000256|RuleBase:RU369070};
DE   AltName: Full=3-hydroxyisobutyryl-coenzyme A hydrolase {ECO:0000256|RuleBase:RU369070};
GN   Name=HIBCH {ECO:0000313|RefSeq:XP_022422962.1};
OS   Delphinapterus leucas (Beluga whale).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Artiodactyla; Whippomorpha; Cetacea; Odontoceti;
OC   Monodontidae; Delphinapterus.
OX   NCBI_TaxID=9749 {ECO:0000313|Proteomes:UP000248483, ECO:0000313|RefSeq:XP_022422962.1};
RN   [1] {ECO:0000313|RefSeq:XP_022422962.1}
RP   IDENTIFICATION.
RC   TISSUE=Blood {ECO:0000313|RefSeq:XP_022422962.1};
RG   RefSeq;
RL   Submitted (NOV-2023) to UniProtKB.
CC   -!- FUNCTION: Hydrolyzes 3-hydroxyisobutyryl-CoA (HIBYL-CoA), a saline
CC       catabolite. Has high activity toward isobutyryl-CoA. Could be an
CC       isobutyryl-CoA dehydrogenase that functions in valine catabolism. Also
CC       hydrolyzes 3-hydroxypropanoyl-CoA. {ECO:0000256|ARBA:ARBA00024871}.
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:0000256|ARBA:ARBA00001709,
CC         ECO:0000256|RuleBase:RU369070};
CC   -!- PATHWAY: Amino-acid degradation; L-valine degradation.
CC       {ECO:0000256|ARBA:ARBA00005109, ECO:0000256|RuleBase:RU369070}.
CC   -!- SUBCELLULAR LOCATION: Mitochondrion {ECO:0000256|RuleBase:RU369070}.
CC   -!- SIMILARITY: Belongs to the enoyl-CoA hydratase/isomerase family.
CC       {ECO:0000256|ARBA:ARBA00005254, ECO:0000256|RuleBase:RU369070}.
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DR   RefSeq; XP_022422962.1; XM_022567254.2.
DR   AlphaFoldDB; A0A2Y9MVB7; -.
DR   UniPathway; UPA00362; -.
DR   Proteomes; UP000248483; Unplaced.
DR   GO; GO:0005739; C:mitochondrion; IEA:UniProtKB-SubCell.
DR   GO; GO:0003860; F:3-hydroxyisobutyryl-CoA hydrolase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0006574; P:valine catabolic process; IEA:UniProtKB-UniRule.
DR   CDD; cd06558; crotonase-like; 1.
DR   InterPro; IPR029045; ClpP/crotonase-like_dom_sf.
DR   InterPro; IPR045004; ECH_dom.
DR   InterPro; IPR032259; HIBYL-CoA-H.
DR   PANTHER; PTHR43176:SF3; 3-HYDROXYISOBUTYRYL-COA HYDROLASE, MITOCHONDRIAL; 1.
DR   PANTHER; PTHR43176; 3-HYDROXYISOBUTYRYL-COA HYDROLASE-RELATED; 1.
DR   Pfam; PF16113; ECH_2; 1.
DR   SUPFAM; SSF52096; ClpP/crotonase; 1.
PE   3: Inferred from homology;
KW   Branched-chain amino acid catabolism {ECO:0000256|ARBA:ARBA00022456};
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|RuleBase:RU369070};
KW   Mitochondrion {ECO:0000256|RuleBase:RU369070};
KW   Reference proteome {ECO:0000313|Proteomes:UP000248483}.
FT   DOMAIN          47..337
FT                   /note="Enoyl-CoA hydratase/isomerase"
FT                   /evidence="ECO:0000259|Pfam:PF16113"
SQ   SEQUENCE   338 AA;  37951 MW;  01282C0A5C464A3E CRC64;
     MGLREMWRLM SRFNSSRRTN IILQHLRMSK HTDAAAEVLL ERKGCAGVIT LNRPKFLNAL
     NLSMIRQIYP QLKKWEQDPE TFLIIIKGAG GKAFCAGGDI RVISEARKAN QKIAQDFFRE
     EYMLNNAIDS CQKPYIALIH GITMGGGVGL SVHGQFRVAT EKSLFAMPET AIGLFPDVGG
     GYFLPRLQGK LGCFLALTGF RLKGRDVYAA GIATHFVDSE KLGMLEEDLL ALKSPSKENI
     AEVLETYHAK SKIDQDKSFI LEEHMDKINS WFSANTVEQI IENLQQDGSS FALEQLKVIN
     KMSPTSLKIT LRQLMEGSSK TLQEVLTMEY RMSQACMF
//
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