ILVH1_ARATH
ID ILVH1_ARATH Reviewed; 477 AA.
AC Q9FFF4; B9DFL8;
DT 09-JAN-2013, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2001, sequence version 1.
DT 03-AUG-2022, entry version 124.
DE RecName: Full=Acetolactate synthase small subunit 1, chloroplastic;
DE AltName: Full=Acetohydroxy-acid synthase small subunit;
DE Short=AHAS;
DE Short=ALS;
DE AltName: Full=Protein valine-tolerant 1;
DE Flags: Precursor;
GN Name=VAT1; OrderedLocusNames=At5g16290; ORFNames=MQK4.1;
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=9330910; DOI=10.1093/dnares/4.3.215;
RA Sato S., Kotani H., Nakamura Y., Kaneko T., Asamizu E., Fukami M.,
RA Miyajima N., Tabata S.;
RT "Structural analysis of Arabidopsis thaliana chromosome 5. I. Sequence
RT features of the 1.6 Mb regions covered by twenty physically assigned P1
RT clones.";
RL DNA Res. 4:215-230(1997).
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].
RA Cheuk R., Chen H., Kim C.J., Shinn P., Ecker J.R.;
RT "Arabidopsis ORF clones.";
RL Submitted (MAY-2005) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=cv. Columbia;
RA Totoki Y., Seki M., Ishida J., Nakajima M., Enju A., Kamiya A.,
RA Narusaka M., Shin-i T., Nakagawa M., Sakamoto N., Oishi K., Kohara Y.,
RA Kobayashi M., Toyoda A., Sakaki Y., Sakurai T., Iida K., Akiyama K.,
RA Satou M., Toyoda T., Konagaya A., Carninci P., Kawai J., Hayashizaki Y.,
RA Shinozaki K.;
RT "Large-scale analysis of RIKEN Arabidopsis full-length (RAFL) cDNAs.";
RL Submitted (JUL-2006) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=cv. Columbia; TISSUE=Rosette leaf;
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, MUTAGENESIS OF GLY-88; THR-119 AND ARG-453, AND TISSUE
RP SPECIFICITY.
RC STRAIN=cv. Columbia;
RX PubMed=20497381; DOI=10.1111/j.1365-313x.2010.04261.x;
RA Chen H., Saksa K., Zhao F., Qiu J., Xiong L.;
RT "Genetic analysis of pathway regulation for enhancing branched-chain amino
RT acid biosynthesis in plants.";
RL Plant J. 63:573-583(2010).
CC -!- FUNCTION: Regulatory subunit of acetohydroxy-acid synthase. Involved in
CC the feed-back inhibition by branched-chain amino acids but not in
CC herbicide tolerance. {ECO:0000269|PubMed:20497381}.
CC -!- PATHWAY: Amino-acid biosynthesis; L-isoleucine biosynthesis; L-
CC isoleucine from 2-oxobutanoate: step 1/4.
CC -!- PATHWAY: Amino-acid biosynthesis; L-valine biosynthesis; L-valine from
CC pyruvate: step 1/4.
CC -!- SUBUNIT: The acetolactate synthase complex contains both large
CC catalytic subunits and small regulatory subunits. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Plastid, chloroplast {ECO:0000305}.
CC -!- TISSUE SPECIFICITY: Expressed in roots in the vascular tissuem in cells
CC around the quiescent center, in floral organs at the tips of young
CC siliques and in the joint region between the silique and the pedicel.
CC Barely detectable in mature leaves or siliques.
CC {ECO:0000269|PubMed:20497381}.
CC -!- SIMILARITY: Belongs to the acetolactate synthase small subunit family.
CC {ECO:0000305}.
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DR EMBL; AB005242; BAB09596.1; -; Genomic_DNA.
DR EMBL; CP002688; AED92272.1; -; Genomic_DNA.
DR EMBL; CP002688; AED92273.1; -; Genomic_DNA.
DR EMBL; BT021989; AAY25401.1; -; mRNA.
DR EMBL; AK226906; BAE98982.1; -; mRNA.
DR EMBL; AK316823; BAH19535.1; -; mRNA.
DR RefSeq; NP_197133.1; NM_121634.4.
DR RefSeq; NP_850829.1; NM_180498.3.
DR AlphaFoldDB; Q9FFF4; -.
DR SMR; Q9FFF4; -.
DR STRING; 3702.AT5G16290.2; -.
DR PaxDb; Q9FFF4; -.
DR PRIDE; Q9FFF4; -.
DR ProMEX; Q9FFF4; -.
DR ProteomicsDB; 247367; -.
DR EnsemblPlants; AT5G16290.1; AT5G16290.1; AT5G16290.
DR EnsemblPlants; AT5G16290.2; AT5G16290.2; AT5G16290.
DR GeneID; 831490; -.
DR Gramene; AT5G16290.1; AT5G16290.1; AT5G16290.
DR Gramene; AT5G16290.2; AT5G16290.2; AT5G16290.
DR KEGG; ath:AT5G16290; -.
DR Araport; AT5G16290; -.
DR TAIR; locus:2171292; AT5G16290.
DR eggNOG; KOG2663; Eukaryota.
DR HOGENOM; CLU_032954_1_0_1; -.
DR InParanoid; Q9FFF4; -.
DR OMA; VSRITHT; -.
DR OrthoDB; 582538at2759; -.
DR PhylomeDB; Q9FFF4; -.
DR BioCyc; ARA:AT5G16290-MON; -.
DR UniPathway; UPA00047; UER00055.
DR UniPathway; UPA00049; UER00059.
DR PRO; PR:Q9FFF4; -.
DR Proteomes; UP000006548; Chromosome 5.
DR ExpressionAtlas; Q9FFF4; baseline and differential.
DR Genevisible; Q9FFF4; AT.
DR GO; GO:0009507; C:chloroplast; IDA:TAIR.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:0005777; C:peroxisome; IDA:TAIR.
DR GO; GO:1990610; F:acetolactate synthase regulator activity; IEA:InterPro.
DR GO; GO:0043621; F:protein self-association; IPI:TAIR.
DR GO; GO:0009097; P:isoleucine biosynthetic process; IBA:GO_Central.
DR GO; GO:0006551; P:leucine metabolic process; IMP:TAIR.
DR GO; GO:0050790; P:regulation of catalytic activity; IDA:TAIR.
DR GO; GO:0009099; P:valine biosynthetic process; IMP:TAIR.
DR GO; GO:0006573; P:valine metabolic process; IMP:TAIR.
DR CDD; cd04878; ACT_AHAS; 2.
DR Gene3D; 3.30.70.1150; -; 2.
DR InterPro; IPR004789; Acetalactate_synth_ssu.
DR InterPro; IPR027271; Acetolactate_synth/TF_NikR_C.
DR InterPro; IPR019455; Acetolactate_synth_ssu_C.
DR InterPro; IPR045865; ACT-like_dom_sf.
DR InterPro; IPR002912; ACT_dom.
DR InterPro; IPR039557; AHAS_ACT.
DR PANTHER; PTHR30239; PTHR30239; 1.
DR Pfam; PF01842; ACT; 2.
DR Pfam; PF10369; ALS_ss_C; 2.
DR SUPFAM; SSF55021; SSF55021; 4.
DR TIGRFAMs; TIGR00119; acolac_sm; 2.
DR PROSITE; PS51671; ACT; 2.
PE 1: Evidence at protein level;
KW Amino-acid biosynthesis; Branched-chain amino acid biosynthesis;
KW Chloroplast; Plastid; Reference proteome; Repeat; Transit peptide.
FT TRANSIT 1..62
FT /note="Chloroplast"
FT /evidence="ECO:0000255"
FT CHAIN 63..477
FT /note="Acetolactate synthase small subunit 1,
FT chloroplastic"
FT /id="PRO_0000420865"
FT DOMAIN 78..150
FT /note="ACT 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01007"
FT DOMAIN 309..383
FT /note="ACT 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01007"
FT MUTAGEN 88
FT /note="G->D: Resistance to valine ihibition."
FT /evidence="ECO:0000269|PubMed:20497381"
FT MUTAGEN 119
FT /note="T->I: In vat1-1; resistance to valine ihibition."
FT /evidence="ECO:0000269|PubMed:20497381"
FT MUTAGEN 453
FT /note="R->Q: In vat1-3; resistance to valine ihibition."
FT /evidence="ECO:0000269|PubMed:20497381"
FT CONFLICT 216
FT /note="K -> Q (in Ref. 5; BAH19535)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 477 AA; 52331 MW; E210A4854A12E46E CRC64;
MAATTTATSL FSSRLHFQNQ NQGYGFPAKT PNSLQVNQII DGRKMRNATV LSAASTDKAI
TTAQSVAPTA CDRVRRHTIS VFVGDESGII NRIAGVFARR GYNIESLAVG LNEDKALFTI
VVLGTDKVLQ QVVEQLNKLV NVIKVEDLSK EPHVERELML IKLNADPSTR SEIMWLVDIF
RAKIVDTSEQ SLTIEVTGDP GKMVALTTNL EKFGIKEIAR TGKIALRREK MGETAPFWRF
SAASYPHLVK ESSHETVAEK TKLALTGNGN ASSGGDVYPV EPYNDFKPVL DAHWGMVYDE
DSSGLRSHTL SLLVANVPGV LNLITGAISR RGYNIQSLAV GPAEKEGLSR ITTVIPGTDE
NIDKLVRQLQ KLIDLQEIQN ITHMPFAERE LMLIKVAADT SARRDVLDIA QVFRAKAIDV
SDHTITLEVT GDLRKMSALQ TQLEAYGICE VARTGRVALV RESGVDSTYL RGYSLPL
