HIBC1_ARATH
ID HIBC1_ARATH Reviewed; 378 AA.
AC Q9LKJ1; A8MQ94; C0Z2V8; Q2V2U8;
DT 23-MAR-2010, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 03-AUG-2022, entry version 133.
DE RecName: Full=3-hydroxyisobutyryl-CoA hydrolase 1;
DE EC=3.1.2.-;
DE EC=3.1.2.4;
DE AltName: Full=CoA-thioester hydrolase CHY1;
GN Name=CHY1; OrderedLocusNames=At5g65940; ORFNames=K14B20.11;
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 [MRNA], FUNCTION, CATALYTIC ACTIVITY,
RP BIOPHYSICOCHEMICAL PROPERTIES, MUTAGENESIS OF GLY-70; GLU-142 AND ASP-150,
RP AND DISRUPTION PHENOTYPE.
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).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=10718197; DOI=10.1093/dnares/7.1.31;
RA Sato S., Nakamura Y., Kaneko T., Katoh T., Asamizu E., Kotani H.,
RA Tabata S.;
RT "Structural analysis of Arabidopsis thaliana chromosome 5. X. Sequence
RT features of the regions of 3,076,755 bp covered by sixty P1 and TAC
RT clones.";
RL DNA Res. 7:31-63(2000).
RN [3]
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 [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC STRAIN=cv. Columbia;
RX PubMed=14593172; DOI=10.1126/science.1088305;
RA Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J., Southwick A.M.,
RA Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F., Karlin-Newmann G.,
RA Liu S.X., Lam B., Sakano H., Wu T., Yu G., Miranda M., Quach H.L.,
RA Tripp M., Chang C.H., Lee J.M., Toriumi M.J., Chan M.M., Tang C.C.,
RA Onodera C.S., Deng J.M., Akiyama K., Ansari Y., Arakawa T., Banh J.,
RA Banno F., Bowser L., Brooks S.Y., Carninci P., Chao Q., Choy N., Enju A.,
RA Goldsmith A.D., Gurjal M., Hansen N.F., Hayashizaki Y., Johnson-Hopson C.,
RA Hsuan V.W., Iida K., Karnes M., Khan S., Koesema E., Ishida J., Jiang P.X.,
RA Jones T., Kawai J., Kamiya A., Meyers C., Nakajima M., Narusaka M.,
RA Seki M., Sakurai T., Satou M., Tamse R., Vaysberg M., Wallender E.K.,
RA Wong C., Yamamura Y., Yuan S., Shinozaki K., Davis R.W., Theologis A.,
RA Ecker J.R.;
RT "Empirical analysis of transcriptional activity in the Arabidopsis
RT genome.";
RL Science 302:842-846(2003).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 2 AND 4).
RC STRAIN=cv. Columbia;
RX PubMed=19423640; DOI=10.1093/dnares/dsp009;
RA Iida K., Fukami-Kobayashi K., Toyoda A., Sakaki Y., Kobayashi M., Seki M.,
RA Shinozaki K.;
RT "Analysis of multiple occurrences of alternative splicing events in
RT Arabidopsis thaliana using novel sequenced full-length cDNAs.";
RL DNA Res. 16:155-164(2009).
RN [6]
RP FUNCTION, DISRUPTION PHENOTYPE, INDUCTION, DEVELOPMENTAL STAGE, AND TISSUE
RP SPECIFICITY.
RX PubMed=15280033; DOI=10.1016/j.febslet.2004.06.071;
RA Lange P.R., Eastmond P.J., Madagan K., Graham I.A.;
RT "An Arabidopsis mutant disrupted in valine catabolism is also compromised
RT in peroxisomal fatty acid beta-oxidation.";
RL FEBS Lett. 571:147-153(2004).
RN [7]
RP FUNCTION.
RX PubMed=17580301; DOI=10.1074/jbc.m701028200;
RA Lucas K.A., Filley J.R., Erb J.M., Graybill E.R., Hawes J.W.;
RT "Peroxisomal metabolism of propionic acid and isobutyric acid in plants.";
RL J. Biol. Chem. 282:24980-24989(2007).
RN [8]
RP FUNCTION.
RX PubMed=19529827; DOI=10.1093/mp/ssn063;
RA Dong C.H., Zolman B.K., Bartel B., Lee B.H., Stevenson B., Agarwal M.,
RA Zhu J.K.;
RT "Disruption of Arabidopsis CHY1 reveals an important role of metabolic
RT status in plant cold stress signaling.";
RL Mol. Plant 2:59-72(2009).
RN [9]
RP FUNCTION, DISRUPTION PHENOTYPE, AND BIOPHYSICOCHEMICAL PROPERTIES.
RX PubMed=19538395; DOI=10.1111/j.1438-8677.2008.00160.x;
RA Ibdah M., Pichersky E.;
RT "Arabidopsis Chy1 null mutants are deficient in benzoic acid-containing
RT glucosinolates in the seeds.";
RL Plant Biol. 11:574-581(2009).
RN [10]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, CLEAVAGE OF INITIATOR
RP METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY
RP [LARGE SCALE ANALYSIS].
RX PubMed=22223895; DOI=10.1074/mcp.m111.015131;
RA Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C., Meinnel T.,
RA Giglione C.;
RT "Comparative large-scale characterisation of plant vs. mammal proteins
RT reveals similar and idiosyncratic N-alpha acetylation features.";
RL Mol. Cell. Proteomics 11:M111.015131-M111.015131(2012).
CC -!- FUNCTION: Involved in valine catabolism. May be indirectly involved in
CC benzoic acid biosynthesis and in cold signaling and cold tolerance.
CC {ECO:0000269|PubMed:11404361, ECO:0000269|PubMed:15280033,
CC ECO:0000269|PubMed:17580301, ECO:0000269|PubMed:19529827,
CC ECO:0000269|PubMed:19538395}.
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:0000269|PubMed:11404361};
CC -!- ACTIVITY REGULATION: Inhibited by copper.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=3.7 uM for 3-hydroxyisobutyryl-CoA {ECO:0000269|PubMed:11404361,
CC ECO:0000269|PubMed:19538395};
CC KM=2.9 uM for cinnamoyl-CoA {ECO:0000269|PubMed:11404361,
CC ECO:0000269|PubMed:19538395};
CC Vmax=24.2 umol/min/mg enzyme toward 3-hydroxyisobutyryl-CoA
CC {ECO:0000269|PubMed:11404361, ECO:0000269|PubMed:19538395};
CC Vmax=12.6 umol/sec/mg enzyme toward cinnamoyl-CoA
CC {ECO:0000269|PubMed:11404361, ECO:0000269|PubMed:19538395};
CC Note=Can also use 3-hydroxy-3-phenoylpropionoyl-CoA and p-coumaroyl-
CC CoA as substrates, but not benzoyl-CoA.;
CC pH dependence:
CC Optimum pH is 7-9. {ECO:0000269|PubMed:11404361,
CC ECO:0000269|PubMed:19538395};
CC -!- PATHWAY: Amino-acid degradation; L-valine degradation.
CC -!- SUBCELLULAR LOCATION: Peroxisome {ECO:0000305}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=4;
CC Name=1;
CC IsoId=Q9LKJ1-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9LKJ1-2; Sequence=VSP_038863, VSP_038864;
CC Name=3;
CC IsoId=Q9LKJ1-3; Sequence=VSP_038861, VSP_038862;
CC Name=4;
CC IsoId=Q9LKJ1-4; Sequence=VSP_038860, VSP_038861, VSP_038862;
CC -!- TISSUE SPECIFICITY: Expressed in roots, leaves, flowers and siliques.
CC {ECO:0000269|PubMed:15280033}.
CC -!- DEVELOPMENTAL STAGE: Induced during post-germinative growth. Detected
CC in imbibed seeds. {ECO:0000269|PubMed:15280033}.
CC -!- INDUCTION: Down-regulated by sugar. {ECO:0000269|PubMed:15280033}.
CC -!- DISRUPTION PHENOTYPE: Resistant to inhibition of root elongation and
CC promotion of lateral root formation by the auxin precursor indole-3-
CC butyric acid (IBA). Deficiency of benzoic acid-containing
CC glucosinolates in the seeds. Resistance to the pro-herbicide 2,4-
CC dichlorophenoxybutyric acid (2,4-DB). {ECO:0000269|PubMed:11404361,
CC ECO:0000269|PubMed:15280033, ECO:0000269|PubMed:19538395}.
CC -!- MISCELLANEOUS: Loss of function mutants are defective in beta-
CC oxidization of fatty acids and in the conversion of indole-3-butyric
CC acid (IBA) to indole-3-acetic acid (IAA). These inhibitions may be due
CC to the accumulation of a toxic intermediate. The mutants are also less
CC tolerant to freezing stress after cold acclimation.
CC -!- SIMILARITY: Belongs to the enoyl-CoA hydratase/isomerase family.
CC {ECO:0000305}.
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DR EMBL; AF276301; AAF77193.1; -; mRNA.
DR EMBL; AB018108; BAB11141.1; -; Genomic_DNA.
DR EMBL; CP002688; AED98128.1; -; Genomic_DNA.
DR EMBL; CP002688; AED98129.1; -; Genomic_DNA.
DR EMBL; CP002688; AED98130.1; -; Genomic_DNA.
DR EMBL; CP002688; ANM68816.1; -; Genomic_DNA.
DR EMBL; BT000956; AAN41356.1; -; mRNA.
DR EMBL; AK316713; BAH19440.1; -; mRNA.
DR EMBL; AK318922; BAH57037.1; -; mRNA.
DR RefSeq; NP_001032155.1; NM_001037078.2. [Q9LKJ1-3]
DR RefSeq; NP_001078804.1; NM_001085335.1. [Q9LKJ1-2]
DR RefSeq; NP_001330538.1; NM_001345728.1. [Q9LKJ1-1]
DR RefSeq; NP_201395.1; NM_125991.4. [Q9LKJ1-1]
DR AlphaFoldDB; Q9LKJ1; -.
DR SMR; Q9LKJ1; -.
DR BioGRID; 21966; 12.
DR IntAct; Q9LKJ1; 12.
DR STRING; 3702.AT5G65940.1; -.
DR iPTMnet; Q9LKJ1; -.
DR PaxDb; Q9LKJ1; -.
DR PRIDE; Q9LKJ1; -.
DR ProteomicsDB; 230321; -. [Q9LKJ1-1]
DR EnsemblPlants; AT5G65940.1; AT5G65940.1; AT5G65940. [Q9LKJ1-1]
DR EnsemblPlants; AT5G65940.2; AT5G65940.2; AT5G65940. [Q9LKJ1-3]
DR EnsemblPlants; AT5G65940.3; AT5G65940.3; AT5G65940. [Q9LKJ1-2]
DR EnsemblPlants; AT5G65940.4; AT5G65940.4; AT5G65940. [Q9LKJ1-1]
DR GeneID; 836724; -.
DR Gramene; AT5G65940.1; AT5G65940.1; AT5G65940. [Q9LKJ1-1]
DR Gramene; AT5G65940.2; AT5G65940.2; AT5G65940. [Q9LKJ1-3]
DR Gramene; AT5G65940.3; AT5G65940.3; AT5G65940. [Q9LKJ1-2]
DR Gramene; AT5G65940.4; AT5G65940.4; AT5G65940. [Q9LKJ1-1]
DR KEGG; ath:AT5G65940; -.
DR Araport; AT5G65940; -.
DR TAIR; locus:2152069; AT5G65940.
DR eggNOG; ENOG502RY3N; Eukaryota.
DR InParanoid; Q9LKJ1; -.
DR OMA; GKPYIAF; -.
DR OrthoDB; 1369862at2759; -.
DR PhylomeDB; Q9LKJ1; -.
DR BioCyc; ARA:AT5G65940-MON; -.
DR BRENDA; 3.1.2.4; 399.
DR SABIO-RK; Q9LKJ1; -.
DR UniPathway; UPA00362; -.
DR PRO; PR:Q9LKJ1; -.
DR Proteomes; UP000006548; Chromosome 5.
DR ExpressionAtlas; Q9LKJ1; baseline and differential.
DR Genevisible; Q9LKJ1; AT.
DR GO; GO:0005777; C:peroxisome; IEA:UniProtKB-SubCell.
DR GO; GO:0009536; C:plastid; HDA:TAIR.
DR GO; GO:0003860; F:3-hydroxyisobutyryl-CoA hydrolase activity; IDA:UniProtKB.
DR GO; GO:0009409; P:response to cold; IMP:TAIR.
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 1: Evidence at protein level;
KW Acetylation; Alternative splicing; Branched-chain amino acid catabolism;
KW Hydrolase; Peroxisome; Reference proteome.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0007744|PubMed:22223895"
FT CHAIN 2..378
FT /note="3-hydroxyisobutyryl-CoA hydrolase 1"
FT /id="PRO_0000392977"
FT BINDING 94
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 119
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 142
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 150
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT MOD_RES 2
FT /note="N-acetylalanine"
FT /evidence="ECO:0007744|PubMed:22223895"
FT VAR_SEQ 1..116
FT /note="Missing (in isoform 4)"
FT /evidence="ECO:0000303|PubMed:19423640"
FT /id="VSP_038860"
FT VAR_SEQ 322..328
FT /note="GCRAILV -> VLQAFSI (in isoform 3 and isoform 4)"
FT /evidence="ECO:0000303|PubMed:19423640"
FT /id="VSP_038861"
FT VAR_SEQ 329..378
FT /note="Missing (in isoform 3 and isoform 4)"
FT /evidence="ECO:0000303|PubMed:19423640"
FT /id="VSP_038862"
FT VAR_SEQ 336..342
FT /note="WEPRRLE -> ATGGHEG (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:19423640"
FT /id="VSP_038863"
FT VAR_SEQ 343..378
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:19423640"
FT /id="VSP_038864"
FT MUTAGEN 70
FT /note="G->S: Loss of activity."
FT /evidence="ECO:0000269|PubMed:11404361"
FT MUTAGEN 142
FT /note="E->A: Loss of activity."
FT /evidence="ECO:0000269|PubMed:11404361"
FT MUTAGEN 150
FT /note="D->G: Reduced activity."
FT /evidence="ECO:0000269|PubMed:11404361"
SQ SEQUENCE 378 AA; 42073 MW; 25E5D810F7158A75 CRC64;
MAVEMASQSQ VLVEEKSSVR ILTLNRPKQL NALSFHMISR LLQLFLAFEE DPSVKLVILK
GHGRAFCAGG DVAAVVRDIN QGNWRLGANY FSSEYMLNYV MATYSKAQVS ILNGIVMGGG
AGVSVHGRFR IATENTVFAM PETALGLFPD VGASYFLSRL PGFFGEYVGL TGARLDGAEM
LACGLATHFV PSTRLTALEA DLCRINSNDP TFASTILDAY TQHPRLKQQS AYRRLDVIDR
CFSRRTVEEI ISALEREATQ EADGWISATI QALKKGSPAS LKISLRSIRE GRLQGVGQCL
IREYRMVCHV MKGEISKDFV EGCRAILVDK DKNPKWEPRR LEDMKDSMVE QYFERVERED
DLKLPPRNNL PALGIAKL
