ID   HIBC2_ARATH             Reviewed;         378 AA.
AC   Q1PEY5; O49330;
DT   23-MAR-2010, integrated into UniProtKB/Swiss-Prot.
DT   16-MAY-2006, sequence version 1.
DT   03-AUG-2022, entry version 99.
DE   RecName: Full=Probable 3-hydroxyisobutyryl-CoA hydrolase 2;
DE            EC=3.1.2.4;
GN   OrderedLocusNames=At2g30650; ORFNames=T11J7.4;
OS   Arabidopsis thaliana (Mouse-ear cress).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   rosids; malvids; Brassicales; Brassicaceae; Camelineae; Arabidopsis.
OX   NCBI_TaxID=3702;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. Columbia;
RX   PubMed=10617197; DOI=10.1038/45471;
RA   Lin X., Kaul S., Rounsley S.D., Shea T.P., Benito M.-I., Town C.D.,
RA   Fujii C.Y., Mason T.M., Bowman C.L., Barnstead M.E., Feldblyum T.V.,
RA   Buell C.R., Ketchum K.A., Lee J.J., Ronning C.M., Koo H.L., Moffat K.S.,
RA   Cronin L.A., Shen M., Pai G., Van Aken S., Umayam L., Tallon L.J.,
RA   Gill J.E., Adams M.D., Carrera A.J., Creasy T.H., Goodman H.M.,
RA   Somerville C.R., Copenhaver G.P., Preuss D., Nierman W.C., White O.,
RA   Eisen J.A., Salzberg S.L., Fraser C.M., Venter J.C.;
RT   "Sequence and analysis of chromosome 2 of the plant Arabidopsis thaliana.";
RL   Nature 402:761-768(1999).
RN   [2]
RP   GENOME REANNOTATION.
RC   STRAIN=cv. Columbia;
RX   PubMed=27862469; DOI=10.1111/tpj.13415;
RA   Cheng C.Y., Krishnakumar V., Chan A.P., Thibaud-Nissen F., Schobel S.,
RA   Town C.D.;
RT   "Araport11: a complete reannotation of the Arabidopsis thaliana reference
RT   genome.";
RL   Plant J. 89:789-804(2017).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=cv. Columbia;
RX   PubMed=17147637; DOI=10.1111/j.1467-7652.2006.00183.x;
RA   Underwood B.A., Vanderhaeghen R., Whitford R., Town C.D., Hilson P.;
RT   "Simultaneous high-throughput recombinational cloning of open reading
RT   frames in closed and open configurations.";
RL   Plant Biotechnol. J. 4:317-324(2006).
RN   [4]
RP   GENE FAMILY.
RX   PubMed=11404361; DOI=10.1074/jbc.m104679200;
RA   Zolman B.K., Monroe-Augustus M., Thompson B., Hawes J.W., Krukenberg K.A.,
RA   Matsuda S.P., Bartel B.;
RT   "chy1, an Arabidopsis mutant with impaired beta-oxidation, is defective in
RT   a peroxisomal beta-hydroxyisobutyryl-CoA hydrolase.";
RL   J. Biol. Chem. 276:31037-31046(2001).
CC   -!- FUNCTION: Involved in valine catabolism. {ECO:0000250}.
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   -!- PATHWAY: Amino-acid degradation; L-valine degradation.
CC   -!- SUBCELLULAR LOCATION: Peroxisome {ECO:0000305}.
CC   -!- SIMILARITY: Belongs to the enoyl-CoA hydratase/isomerase family.
CC       {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAC02736.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR   EMBL; AC002340; AAC02736.1; ALT_SEQ; Genomic_DNA.
DR   EMBL; CP002685; AEC08423.1; -; Genomic_DNA.
DR   EMBL; DQ446582; ABE65876.1; -; mRNA.
DR   PIR; A84711; A84711.
DR   RefSeq; NP_180623.3; NM_128617.4.
DR   AlphaFoldDB; Q1PEY5; -.
DR   SMR; Q1PEY5; -.
DR   STRING; 3702.AT2G30650.1; -.
DR   iPTMnet; Q1PEY5; -.
DR   PaxDb; Q1PEY5; -.
DR   PRIDE; Q1PEY5; -.
DR   ProteomicsDB; 230205; -.
DR   EnsemblPlants; AT2G30650.1; AT2G30650.1; AT2G30650.
DR   GeneID; 817615; -.
DR   Gramene; AT2G30650.1; AT2G30650.1; AT2G30650.
DR   KEGG; ath:AT2G30650; -.
DR   Araport; AT2G30650; -.
DR   TAIR; locus:2054517; AT2G30650.
DR   eggNOG; ENOG502RY3N; Eukaryota.
DR   HOGENOM; CLU_009834_22_1_1; -.
DR   InParanoid; Q1PEY5; -.
DR   OrthoDB; 1369862at2759; -.
DR   PhylomeDB; Q1PEY5; -.
DR   BioCyc; ARA:AT2G30650-MON; -.
DR   UniPathway; UPA00362; -.
DR   PRO; PR:Q1PEY5; -.
DR   Proteomes; UP000006548; Chromosome 2.
DR   ExpressionAtlas; Q1PEY5; baseline and differential.
DR   Genevisible; Q1PEY5; AT.
DR   GO; GO:0005777; C:peroxisome; IEA:UniProtKB-SubCell.
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   InterPro; IPR029045; ClpP/crotonase-like_dom_sf.
DR   InterPro; IPR045004; ECH_dom.
DR   InterPro; IPR032259; HIBYL-CoA-H.
DR   PANTHER; PTHR43176; PTHR43176; 1.
DR   Pfam; PF16113; ECH_2; 1.
DR   SUPFAM; SSF52096; SSF52096; 1.
PE   2: Evidence at transcript level;
KW   Branched-chain amino acid catabolism; Hydrolase; Peroxisome;
KW   Reference proteome.
FT   CHAIN           1..378
FT                   /note="Probable 3-hydroxyisobutyryl-CoA hydrolase 2"
FT                   /id="PRO_0000392978"
FT   MOTIF           376..378
FT                   /note="Microbody targeting signal"
FT                   /evidence="ECO:0000305"
FT   BINDING         115
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         138
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         146
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   378 AA;  42256 MW;  28F7BFF9F42AE735 CRC64;
     MASHSQVLVE EKSSVRILTF NRPKQLNALS FHMVSRLLQL FLAYEEDPSV KLVVLKGQGR
     AFSAGGDIPP IVRDILQGKL IRGAHYFKVG YTLNYVLSTY RKPQVSILNG IVMGGGAGLS
     TNGRFRIATE NTVFAMPETA LGLFPDVGAS YFLSRLPGFF GEYVGLTGAR LDGAEMLACG
     LATHFVPSIS LTALEAELYK VGSSNQTFIS TILDAYAEYP HLNQHSSYHR LDVIDRCFSK
     RTVEEIFSAL EREVTQKPND WLLATIQALE KASPSCLKIS LRSIREGRLQ GVGQCLIREY
     RMVCHVMKGD ISKDFVEGCR AVLIDKDRNP KWQPRRLEDV TDSMVDQYFE RVEDEEGWED
     LKFPPRNNLP ALAIAAKL