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Database: UniProt
Entry: A0A445D572_ARAHY
LinkDB: A0A445D572_ARAHY
Original site: A0A445D572_ARAHY 
ID   A0A445D572_ARAHY        Unreviewed;       351 AA.
AC   A0A445D572;
DT   08-MAY-2019, integrated into UniProtKB/TrEMBL.
DT   08-MAY-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=Ahy_A05g023845 {ECO:0000313|EMBL:RYR58170.1};
OS   Arachis hypogaea (Peanut).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   rosids; fabids; Fabales; Fabaceae; Papilionoideae; 50 kb inversion clade;
OC   dalbergioids sensu lato; Dalbergieae; Pterocarpus clade; Arachis.
OX   NCBI_TaxID=3818 {ECO:0000313|EMBL:RYR58170.1, ECO:0000313|Proteomes:UP000289738};
RN   [1] {ECO:0000313|EMBL:RYR58170.1, ECO:0000313|Proteomes:UP000289738}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. Fuhuasheng {ECO:0000313|Proteomes:UP000289738};
RC   TISSUE=Leaves {ECO:0000313|EMBL:RYR58170.1};
RA   Chen X.;
RT   "Sequencing of cultivated peanut Arachis hypogaea provides insights into
RT   genome evolution and oil improvement.";
RL   Submitted (JAN-2019) 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:RYR58170.1}.
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DR   EMBL; SDMP01000005; RYR58170.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A445D572; -.
DR   STRING; 3818.A0A445D572; -.
DR   Proteomes; UP000289738; Chromosome a05.
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:SF6; 3-HYDROXYISOBUTYRYL-COA HYDROLASE; 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:UP000289738}.
FT   DOMAIN          45..324
FT                   /note="Enoyl-CoA hydratase/isomerase"
FT                   /evidence="ECO:0000259|Pfam:PF16113"
SQ   SEQUENCE   351 AA;  39206 MW;  B4B44D36FC5BAE97 CRC64;
     MALLSFKFDT QPINQVLSAG NSAVKLVILN RPHKLNSLNY EMGNGKGFCA GGDVVSVISS
     SLTGHWTYPL KFYGKQLILD HLAATYKKPL VSVINGVVMG GGAGLSMNTT FRIVTEKAVF
     AMPETYIGFF PDVSASYFLS RLPGYFGEYL GLTGARLDGI EMAACGLATH FIHSTKLNAL
     ENALQAITSS NVSTVSALIE TFTEKPTVKK DSPFKRYLRI DTMHENELEN GAEKKWITNA
     LNSMRSSSPM SLKIFLKSIR KGRIQNIEQC LHRDYNIASH LFKRTVSNDF YEGSRAKLFD
     KDNKPKWEPS KLELVSEEMV EQHFTNITDH AWEPLQLPQR FHSPIITASR L
//
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