ID A0A0R0J3C7_SOYBN Unreviewed; 398 AA.
AC A0A0R0J3C7;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 27-MAR-2024, entry version 38.
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=100811550 {ECO:0000313|EnsemblPlants:KRH46020};
GN ORFNames=GLYMA_08G307800 {ECO:0000313|EMBL:KRH46020.1};
OS Glycine max (Soybean) (Glycine hispida).
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; Glycine;
OC Glycine subgen. Soja.
OX NCBI_TaxID=3847 {ECO:0000313|EMBL:KRH46020.1};
RN [1] {ECO:0000313|EMBL:KRH46020.1, ECO:0000313|EnsemblPlants:KRH46020}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Williams 82 {ECO:0000313|EnsemblPlants:KRH46020};
RC TISSUE=Callus {ECO:0000313|EMBL:KRH46020.1};
RX PubMed=20075913; DOI=10.1038/nature08670;
RA Schmutz J., Cannon S.B., Schlueter J., Ma J., Mitros T., Nelson W.,
RA Hyten D.L., Song Q., Thelen J.J., Cheng J., Xu D., Hellsten U., May G.D.,
RA Yu Y., Sakurai T., Umezawa T., Bhattacharyya M.K., Sandhu D.,
RA Valliyodan B., Lindquist E., Peto M., Grant D., Shu S., Goodstein D.,
RA Barry K., Futrell-Griggs M., Abernathy B., Du J., Tian Z., Zhu L., Gill N.,
RA Joshi T., Libault M., Sethuraman A., Zhang X.-C., Shinozaki K.,
RA Nguyen H.T., Wing R.A., Cregan P., Specht J., Grimwood J., Rokhsar D.,
RA Stacey G., Shoemaker R.C., Jackson S.A.;
RT "Genome sequence of the palaeopolyploid soybean.";
RL Nature 463:178-183(2010).
RN [2] {ECO:0000313|EnsemblPlants:KRH46020}
RP IDENTIFICATION.
RC STRAIN=Williams 82 {ECO:0000313|EnsemblPlants:KRH46020};
RG EnsemblPlants;
RL Submitted (FEB-2018) to UniProtKB.
RN [3] {ECO:0000313|EMBL:KRH46020.1}
RP NUCLEOTIDE SEQUENCE.
RC TISSUE=Callus {ECO:0000313|EMBL:KRH46020.1};
RA Schmutz J., Cannon S., Schlueter J., Ma J., Mitros T., Nelson W., Hyten D.,
RA Song Q., Thelen J., Cheng J., Xu D., Hellsten U., May G., Yu Y.,
RA Sakurai T., Umezawa T., Bhattacharyya M., Sandhu D., Valliyodan B.,
RA Lindquist E., Peto M., Grant D., Shu S., Goodstein D., Barry K.,
RA Futrell-Griggs M., Abernathy B., Du J., Tian Z., Zhu L., Gill N., Joshi T.,
RA Libault M., Sethuraman A., Zhang X., Shinozaki K., Nguyen H., Wing R.,
RA Cregan P., Specht J., Grimwood J., Rokhsar D., Stacey G., Shoemaker R.,
RA Jackson S.;
RT "WGS assembly of Glycine max.";
RL Submitted (JUL-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}.
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DR EMBL; CM000841; KRH46020.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0R0J3C7; -.
DR SMR; A0A0R0J3C7; -.
DR STRING; 3847.A0A0R0J3C7; -.
DR EnsemblPlants; KRH46020; KRH46020; GLYMA_08G307800.
DR Gramene; KRH46020; KRH46020; GLYMA_08G307800.
DR InParanoid; A0A0R0J3C7; -.
DR Proteomes; UP000008827; Chromosome 8.
DR ExpressionAtlas; A0A0R0J3C7; baseline and differential.
DR GO; GO:0003860; F:3-hydroxyisobutyryl-CoA hydrolase activity; IBA:GO_Central.
DR GO; GO:0006574; P:valine catabolic process; IBA:GO_Central.
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; 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:UP000008827};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..19
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 20..398
FT /note="3-hydroxyisobutyryl-CoA hydrolase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5014521980"
FT DOMAIN 34..366
FT /note="Enoyl-CoA hydratase/isomerase"
FT /evidence="ECO:0000259|Pfam:PF16113"
SQ SEQUENCE 398 AA; 44674 MW; AAE567B0F154DF90 CRC64;
MPFIVWLCSI LTSMAPSSAV PDEQVVVGEE IEHVRVITLN RPRQLNAISP ELVSLLATYL
EKWEKDEEAE LVIIKGSGRA FCAGGDLRVF YDGRKIKDAC LEVVYRFYWL CYHISTYKKT
QVALVHGISM GGGAALMVPL KFSVVTEKTV FATPEASFGF HIDCGFSYYH SRLPGHLGEY
LALTGGRLSG KEIVAAGLAT HFVPFEKIVE LENRLISLNS GDENAVRSVI EEFSSEVKLD
EESILNKQSI IKECFSKDSV EEIIKSLEAE ANNKGNVWIG AVLKGMKRSS PTALKIALRS
VREGRNQTLS ECLKKEFRLT MNILRTTISE DMYEGIRALT IDKDNAPKWE PSSLDKVEDG
KLDLIFQPFE KNLELQIPES EEYRWDGKYE NSAYALPN
//
