ID R0H246_9BRAS Unreviewed; 418 AA.
AC R0H246;
DT 26-JUN-2013, integrated into UniProtKB/TrEMBL.
DT 26-JUN-2013, sequence version 1.
DT 27-MAR-2024, entry version 33.
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=CARUB_v10007321mg {ECO:0000313|EMBL:EOA18740.1};
OS Capsella rubella.
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; malvids; Brassicales; Brassicaceae; Camelineae; Capsella.
OX NCBI_TaxID=81985 {ECO:0000313|EMBL:EOA18740.1, ECO:0000313|Proteomes:UP000029121};
RN [1] {ECO:0000313|Proteomes:UP000029121}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Monte Gargano {ECO:0000313|Proteomes:UP000029121};
RX PubMed=23749190; DOI=10.1038/ng.2669;
RA Slotte T., Hazzouri K.M., Agren J.A., Koenig D., Maumus F., Guo Y.L.,
RA Steige K., Platts A.E., Escobar J.S., Newman L.K., Wang W., Mandakova T.,
RA Vello E., Smith L.M., Henz S.R., Steffen J., Takuno S., Brandvain Y.,
RA Coop G., Andolfatto P., Hu T.T., Blanchette M., Clark R.M., Quesneville H.,
RA Nordborg M., Gaut B.S., Lysak M.A., Jenkins J., Grimwood J., Chapman J.,
RA Prochnik S., Shu S., Rokhsar D., Schmutz J., Weigel D., Wright S.I.;
RT "The Capsella rubella genome and the genomic consequences of rapid mating
RT system evolution.";
RL Nat. Genet. 45:831-835(2013).
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; KB870811; EOA18740.1; -; Genomic_DNA.
DR RefSeq; XP_006285842.1; XM_006285780.1.
DR AlphaFoldDB; R0H246; -.
DR STRING; 81985.R0H246; -.
DR GeneID; 17877559; -.
DR KEGG; crb:17877559; -.
DR eggNOG; KOG1684; Eukaryota.
DR OrthoDB; 3639304at2759; -.
DR Proteomes; UP000029121; Unassembled WGS sequence.
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:SF16; 3-HYDROXYISOBUTYRYL-COA HYDROLASE-LIKE PROTEIN 3, 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 Reference proteome {ECO:0000313|Proteomes:UP000029121}.
FT DOMAIN 57..406
FT /note="Enoyl-CoA hydratase/isomerase"
FT /evidence="ECO:0000259|Pfam:PF16113"
SQ SEQUENCE 418 AA; 45881 MW; F9384F8E730638AC CRC64;
MIIKTLAHRI FFPKFSSSTF SSHHRLRLSI SDRNRKFSVM AGEDDFVKGN VYPNGVALIT
LDRTKALNAM NLDMDVKYKS FLDECESDPR VKCVIVEGST PRAFCAGMDI KGVAAEIQKD
KNTPLVQKVF TAEYTLICAI AGYKKPYISL MDGITMGFGL GLSGHGRYRV ITERTVLAMP
ENGIGLFPDV GFSYIAAHSP GGGSVGAYLG LTGKRISTPS DALFVGLGTH YVPSEKLTSL
KEAILSANFS EDPDQDIQET LSKYSGNPES EPHLKLLLPQ IESAFSSNKS VKETIEVLKK
YQQSTEPSVV EWANEALKGL EKGAPFSLNL TQKYFANVAC AKGKTANELT TLNGVMKTEY
RIALRSALRC DFAEGVRAVL IDKDQNPKWN PASIEEVDEN EVEALFKPLG PEVEELKV
//
