ID R0FNT9_9BRAS Unreviewed; 401 AA.
AC R0FNT9;
DT 26-JUN-2013, integrated into UniProtKB/TrEMBL.
DT 26-JUN-2013, sequence version 1.
DT 27-MAR-2024, entry version 32.
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_v10017386mg {ECO:0000313|EMBL:EOA24152.1};
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:EOA24152.1, 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; KB870809; EOA24152.1; -; Genomic_DNA.
DR RefSeq; XP_006291254.1; XM_006291192.1.
DR AlphaFoldDB; R0FNT9; -.
DR STRING; 81985.R0FNT9; -.
DR GeneID; 17886660; -.
DR KEGG; crb:17886660; -.
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:SF4; 3-HYDROXYISOBUTYRYL-COA HYDROLASE-LIKE PROTEIN 1, 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 48..381
FT /note="Enoyl-CoA hydratase/isomerase"
FT /evidence="ECO:0000259|Pfam:PF16113"
SQ SEQUENCE 401 AA; 44671 MW; 59E5246B18BE6276 CRC64;
MHNAKGLLGG VVRDKLWRLC HRRSFCSLKL TPEDLDNQVL VEGNGCSRTA ILNRPPQLNA
LTPHMGYRLQ KLYKNWEEDP NIGFVMMKGS GRAFCAGGDV VSLYHLIKRG SPDAIREFFS
SLYSFIYLLG TYLKPHVAIL NGVTMGGGTG VSIPGTFRVA TDRTIFATPE TIIGFHPDAG
ASFNLSHLPG RLGEYLGLTG LKLSGAEMLT CGLATHYIRS EEVLVMEEQL KKLLTDDPSV
VESSLEKYSE VAHPEKTSVL CRIDLLDKCF GHDTVEEIID SLETEAGRRK DTWCTTTLRR
LKANSPLSLK VALRSIREAR FLTLDQCLIR EYRMSLQGTI GPMCGNFCEG VRARLIDKDE
VPKWDPPSLE KVSEDMVDDY FSALTATEPD LDLPIKLRES I
//
