HIBC6_ARATH
ID HIBC6_ARATH Reviewed; 421 AA.
AC Q9T0K7;
DT 23-MAR-2010, integrated into UniProtKB/Swiss-Prot.
DT 31-MAY-2011, sequence version 2.
DT 03-AUG-2022, entry version 130.
DE RecName: Full=3-hydroxyisobutyryl-CoA hydrolase-like protein 3, mitochondrial;
DE EC=3.1.2.-;
DE Flags: Precursor;
GN OrderedLocusNames=At4g13360; ORFNames=T9E8.100;
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=10617198; DOI=10.1038/47134;
RA Mayer K.F.X., Schueller C., Wambutt R., Murphy G., Volckaert G., Pohl T.,
RA Duesterhoeft A., Stiekema W., Entian K.-D., Terryn N., Harris B.,
RA Ansorge W., Brandt P., Grivell L.A., Rieger M., Weichselgartner M.,
RA de Simone V., Obermaier B., Mache R., Mueller M., Kreis M., Delseny M.,
RA Puigdomenech P., Watson M., Schmidtheini T., Reichert B., Portetelle D.,
RA Perez-Alonso M., Boutry M., Bancroft I., Vos P., Hoheisel J.,
RA Zimmermann W., Wedler H., Ridley P., Langham S.-A., McCullagh B.,
RA Bilham L., Robben J., van der Schueren J., Grymonprez B., Chuang Y.-J.,
RA Vandenbussche F., Braeken M., Weltjens I., Voet M., Bastiaens I., Aert R.,
RA Defoor E., Weitzenegger T., Bothe G., Ramsperger U., Hilbert H., Braun M.,
RA Holzer E., Brandt A., Peters S., van Staveren M., Dirkse W., Mooijman P.,
RA Klein Lankhorst R., Rose M., Hauf J., Koetter P., Berneiser S., Hempel S.,
RA Feldpausch M., Lamberth S., Van den Daele H., De Keyser A., Buysshaert C.,
RA Gielen J., Villarroel R., De Clercq R., van Montagu M., Rogers J.,
RA Cronin A., Quail M.A., Bray-Allen S., Clark L., Doggett J., Hall S.,
RA Kay M., Lennard N., McLay K., Mayes R., Pettett A., Rajandream M.A.,
RA Lyne M., Benes V., Rechmann S., Borkova D., Bloecker H., Scharfe M.,
RA Grimm M., Loehnert T.-H., Dose S., de Haan M., Maarse A.C., Schaefer M.,
RA Mueller-Auer S., Gabel C., Fuchs M., Fartmann B., Granderath K., Dauner D.,
RA Herzl A., Neumann S., Argiriou A., Vitale D., Liguori R., Piravandi E.,
RA Massenet O., Quigley F., Clabauld G., Muendlein A., Felber R., Schnabl S.,
RA Hiller R., Schmidt W., Lecharny A., Aubourg S., Chefdor F., Cooke R.,
RA Berger C., Monfort A., Casacuberta E., Gibbons T., Weber N., Vandenbol M.,
RA Bargues M., Terol J., Torres A., Perez-Perez A., Purnelle B., Bent E.,
RA Johnson S., Tacon D., Jesse T., Heijnen L., Schwarz S., Scholler P.,
RA Heber S., Francs P., Bielke C., Frishman D., Haase D., Lemcke K.,
RA Mewes H.-W., Stocker S., Zaccaria P., Bevan M., Wilson R.K.,
RA de la Bastide M., Habermann K., Parnell L., Dedhia N., Gnoj L., Schutz K.,
RA Huang E., Spiegel L., Sekhon M., Murray J., Sheet P., Cordes M.,
RA Abu-Threideh J., Stoneking T., Kalicki J., Graves T., Harmon G.,
RA Edwards J., Latreille P., Courtney L., Cloud J., Abbott A., Scott K.,
RA Johnson D., Minx P., Bentley D., Fulton B., Miller N., Greco T., Kemp K.,
RA Kramer J., Fulton L., Mardis E., Dante M., Pepin K., Hillier L.W.,
RA Nelson J., Spieth J., Ryan E., Andrews S., Geisel C., Layman D., Du H.,
RA Ali J., Berghoff A., Jones K., Drone K., Cotton M., Joshu C., Antonoiu B.,
RA Zidanic M., Strong C., Sun H., Lamar B., Yordan C., Ma P., Zhong J.,
RA Preston R., Vil D., Shekher M., Matero A., Shah R., Swaby I.K.,
RA O'Shaughnessy A., Rodriguez M., Hoffman J., Till S., Granat S., Shohdy N.,
RA Hasegawa A., Hameed A., Lodhi M., Johnson A., Chen E., Marra M.A.,
RA Martienssen R., McCombie W.R.;
RT "Sequence and analysis of chromosome 4 of the plant Arabidopsis thaliana.";
RL Nature 402:769-777(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] OF 5-421.
RA Brover V.V., Troukhan M.E., Alexandrov N.A., Lu Y.-P., Flavell R.B.,
RA Feldmann K.A.;
RT "Full-length cDNA from Arabidopsis thaliana.";
RL Submitted (MAR-2002) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 8-421.
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 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).
RN [6]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-42, CLEAVAGE OF TRANSIT PEPTIDE
RP [LARGE SCALE ANALYSIS] AFTER MET-41, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [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 -!- SUBCELLULAR LOCATION: Mitochondrion {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the enoyl-CoA hydratase/isomerase family.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAK55723.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC Sequence=AAM60849.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC Sequence=CAB40771.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC Sequence=CAB78378.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AL049608; CAB40771.1; ALT_INIT; Genomic_DNA.
DR EMBL; AL161536; CAB78378.1; ALT_INIT; Genomic_DNA.
DR EMBL; CP002687; AEE83270.1; -; Genomic_DNA.
DR EMBL; AY084255; AAM60849.1; ALT_INIT; mRNA.
DR EMBL; AF380642; AAK55723.1; ALT_INIT; mRNA.
DR EMBL; AY057737; AAL15367.1; -; mRNA.
DR PIR; T06293; T06293.
DR RefSeq; NP_193072.2; NM_117410.7.
DR AlphaFoldDB; Q9T0K7; -.
DR SMR; Q9T0K7; -.
DR BioGRID; 12264; 1.
DR STRING; 3702.AT4G13360.1; -.
DR iPTMnet; Q9T0K7; -.
DR PaxDb; Q9T0K7; -.
DR PRIDE; Q9T0K7; -.
DR ProteomicsDB; 230325; -.
DR EnsemblPlants; AT4G13360.1; AT4G13360.1; AT4G13360.
DR GeneID; 826967; -.
DR Gramene; AT4G13360.1; AT4G13360.1; AT4G13360.
DR KEGG; ath:AT4G13360; -.
DR Araport; AT4G13360; -.
DR TAIR; locus:2142050; AT4G13360.
DR eggNOG; KOG1684; Eukaryota.
DR HOGENOM; CLU_009834_22_1_1; -.
DR InParanoid; Q9T0K7; -.
DR OMA; AYRNNEH; -.
DR OrthoDB; 1369862at2759; -.
DR BioCyc; ARA:AT4G13360-MON; -.
DR PRO; PR:Q9T0K7; -.
DR Proteomes; UP000006548; Chromosome 4.
DR ExpressionAtlas; Q9T0K7; baseline and differential.
DR Genevisible; Q9T0K7; AT.
DR GO; GO:0005829; C:cytosol; HDA:TAIR.
DR GO; GO:0005739; C:mitochondrion; 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 1: Evidence at protein level;
KW Acetylation; Hydrolase; Mitochondrion; Reference proteome; Transit peptide.
FT TRANSIT 1..41
FT /note="Mitochondrion"
FT /evidence="ECO:0007744|PubMed:22223895"
FT CHAIN 42..421
FT /note="3-hydroxyisobutyryl-CoA hydrolase-like protein 3,
FT mitochondrial"
FT /id="PRO_0000392982"
FT MOD_RES 42
FT /note="N-acetylalanine"
FT /evidence="ECO:0007744|PubMed:22223895"
SQ SEQUENCE 421 AA; 46251 MW; 8ACDB1BE78A9036D CRC64;
MIIIKTLSHR IFFPKFSQTF SSQFHQTLRF SISDRRKFSA MAGAGVDDFV KGNVFPNGVA
LITLDRTKAL NAMNLDMDIK YKSFLDEWES DPRVKCVIVE GSTSRAFCAG MDIKGVAAEI
QKDKNTPLVQ KVFTAEYTLI CAIAAYKKPY ISLMDGITMG FGLGLSGHGR YRVITERTVL
AMPENGIGLF PDVGFSYIAA HSPGGGSVGA YLGLTGKRIS APSDALFVGL GTHYVPSEKL
ASLKEAILSA NLSEDPNQDI QATLSKYSSN PESEAHLKSL LPHIESAFSS NKSIKETIEE
LKKYQQSTES SVVEWANEAL KGLEKGAPFS LYLTQKYFSN VACAKSKPEN ELATLNGVMK
TEYRIALRSA LRGDFAEGVR AVLIDKDQNP KWNPTSIEEV DENEVEALFK PLSPEVEELK
V