ID A0A498HFA1_MALDO Unreviewed; 254 AA.
AC A0A498HFA1;
DT 05-JUN-2019, integrated into UniProtKB/TrEMBL.
DT 05-JUN-2019, sequence version 1.
DT 27-MAR-2024, entry version 13.
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 ORFNames=DVH24_027880 {ECO:0000313|EMBL:RXH67733.1};
OS Malus domestica (Apple) (Pyrus malus).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; fabids; Rosales; Rosaceae; Amygdaloideae; Maleae; Malus.
OX NCBI_TaxID=3750 {ECO:0000313|EMBL:RXH67733.1, ECO:0000313|Proteomes:UP000290289};
RN [1] {ECO:0000313|EMBL:RXH67733.1, ECO:0000313|Proteomes:UP000290289}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. HFTH1 {ECO:0000313|Proteomes:UP000290289};
RC TISSUE=Young leaf {ECO:0000313|EMBL:RXH67733.1};
RA Hu J.;
RT "A high-quality apple genome assembly.";
RL Submitted (OCT-2018) to the EMBL/GenBank/DDBJ databases.
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|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}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:RXH67733.1}.
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DR EMBL; RDQH01000343; RXH67733.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A498HFA1; -.
DR STRING; 3750.A0A498HFA1; -.
DR Proteomes; UP000290289; Chromosome 17.
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:SF2; 3-HYDROXYISOBUTYRYL-COA HYDROLASE-LIKE PROTEIN 5; 1.
DR PANTHER; PTHR43176; 3-HYDROXYISOBUTYRYL-COA HYDROLASE-RELATED; 1.
DR Pfam; PF16113; ECH_2; 2.
DR SUPFAM; SSF52096; ClpP/crotonase; 1.
PE 3: Inferred from homology;
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|RuleBase:RU369070};
KW Reference proteome {ECO:0000313|Proteomes:UP000290289}.
FT DOMAIN 13..101
FT /note="Enoyl-CoA hydratase/isomerase"
FT /evidence="ECO:0000259|Pfam:PF16113"
FT DOMAIN 141..250
FT /note="Enoyl-CoA hydratase/isomerase"
FT /evidence="ECO:0000259|Pfam:PF16113"
SQ SEQUENCE 254 AA; 28413 MW; 6F4C421AC0A63CC7 CRC64;
MFKIVVGEQI EHVRLITLNR PRQLNVISSK VVSLLAEHLE KWEKDDNAEL VIIKGSGGAF
SAGGDLKMFY DSTKSKDSCL EVVSRMYWLC YHIHTYKKTR VFATPEASIG FHTDCGFSYM
LFHLPGHLGE FLALTGARLN VKAAIEEFSV EVKAPDEESV LNKKSVIGGC FSKDTVAEII
QSFEAEANKE GNGWIGPVLK GLKRSSPTGL RITLRSNREG RKQTLSESLK KEFRLTINIL
RSTISEDVYE VIVV
//
