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Database: UniProt
Entry: A0A1S3VE38_VIGRR
LinkDB: A0A1S3VE38_VIGRR
Original site: A0A1S3VE38_VIGRR 
ID   A0A1S3VE38_VIGRR        Unreviewed;       382 AA.
AC   A0A1S3VE38;
DT   12-APR-2017, integrated into UniProtKB/TrEMBL.
DT   12-APR-2017, sequence version 1.
DT   27-MAR-2024, entry version 24.
DE   RecName: Full=3-hydroxyisobutyryl-CoA hydrolase {ECO:0000256|ARBA:ARBA00011915, 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|ARBA:ARBA00011915, ECO:0000256|RuleBase:RU369070};
DE   AltName: Full=3-hydroxyisobutyryl-coenzyme A hydrolase {ECO:0000256|RuleBase:RU369070};
GN   Name=LOC106774224 {ECO:0000313|RefSeq:XP_014516626.1};
OS   Vigna radiata var. radiata (Mung bean) (Phaseolus aureus).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   rosids; fabids; Fabales; Fabaceae; Papilionoideae; 50 kb inversion clade;
OC   NPAAA clade; indigoferoid/millettioid clade; Phaseoleae; Vigna.
OX   NCBI_TaxID=3916 {ECO:0000313|Proteomes:UP000087766, ECO:0000313|RefSeq:XP_014516626.1};
RN   [1] {ECO:0000313|RefSeq:XP_014516626.1}
RP   IDENTIFICATION.
RC   TISSUE=Leaf {ECO:0000313|RefSeq:XP_014516626.1};
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.
CC       {ECO:0000256|RuleBase:RU369070}.
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|RuleBase:RU369070}.
CC   -!- SIMILARITY: Belongs to the enoyl-CoA hydratase/isomerase family.
CC       {ECO:0000256|RuleBase:RU369070}.
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DR   RefSeq; XP_014516626.1; XM_014661140.2.
DR   AlphaFoldDB; A0A1S3VE38; -.
DR   GeneID; 106774224; -.
DR   OrthoDB; 3639304at2759; -.
DR   Proteomes; UP000087766; Chromosome 9.
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   Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|RuleBase:RU369070};
KW   Plastid {ECO:0000256|ARBA:ARBA00022640};
KW   Reference proteome {ECO:0000313|Proteomes:UP000087766}.
FT   DOMAIN          21..354
FT                   /note="Enoyl-CoA hydratase/isomerase"
FT                   /evidence="ECO:0000259|Pfam:PF16113"
SQ   SEQUENCE   382 AA;  42667 MW;  BBC902547808DA10 CRC64;
     MASFSESDHQ QILVERKSHA RVLTLNRPKQ LNALSFYMVS RLLEVFTEDE ENSDIKLVVV
     KGNGRSFCAG GDVAAVAREG SKGDWKSGAK FFRTEYTMNY VMATYSKPQV SILNGIVMGG
     GAGASVHGRF RVVTENTVFA MPETALGLFP DVGVPYFLSR LPGFFGEYVG LTGARLNGAE
     MLACGLATHF VPSSKLSLLE EALCKVETSD PNAVSAIIDK YSEQPFLKDD SVYHRMDVIN
     KCFSRKSVEG IISSLEIEAT SKADHWISET VQTLKKASPT SLKIFLRLIR EVRLLGIGPS
     LVLEYRIVCH ILKGHYSKDF FEGCRAILLD KDRNPKWEPS KLELLSDSDV DRYFSKLDDE
     EWEELELPKR LKNLPTYAIA KL
//
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