ILVH2_ARATH
ID ILVH2_ARATH Reviewed; 491 AA.
AC Q93YZ7; C0Z282; F4IRS9; Q3E6W5; Q9SKB9;
DT 09-JAN-2013, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-2001, sequence version 1.
DT 03-AUG-2022, entry version 119.
DE RecName: Full=Acetolactate synthase small subunit 2, chloroplastic;
DE AltName: Full=Acetohydroxy-acid synthase small subunit;
DE Short=AHAS;
DE Short=ALS;
DE Flags: Precursor;
GN OrderedLocusNames=At2g31810; ORFNames=F20M17.15;
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] (ISOFORM 1), FUNCTION, AND SUBUNIT.
RX PubMed=11389597; DOI=10.1021/bi002775q;
RA Lee Y.T., Duggleby R.G.;
RT "Identification of the regulatory subunit of Arabidopsis thaliana
RT acetohydroxyacid synthase and reconstitution with its catalytic subunit.";
RL Biochemistry 40:6836-6844(2001).
RN [2]
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 [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].
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 [5]
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 [6]
RP FUNCTION, 3D-STRUCTURE MODELING, AND MUTAGENESIS OF GLY-98; PHE-107;
RP TYR-112; ASN-113; GLY-331; PHE-340; TYR-345 AND ASN-346.
RX PubMed=11852076; DOI=10.1016/s0014-5793(02)02253-6;
RA Lee Y.T., Duggleby R.G.;
RT "Regulatory interactions in Arabidopsis thaliana acetohydroxyacid
RT synthase.";
RL FEBS Lett. 512:180-184(2002).
CC -!- FUNCTION: Regulatory subunit of acetohydroxy-acid synthase. Involved in
CC the feed-back inhibition by branched-chain amino acids. Contains 2
CC repeats, each of them being able to activate partially the catalytic
CC subunit. The enzyme reconstituted with the first repeat is inhibited by
CC leucine, but not by valine or isoleucine and the enzyme reconstituted
CC with the second repeat is not inhibited by any branched-chain amino
CC acid. {ECO:0000269|PubMed:11389597, ECO:0000269|PubMed:11852076}.
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. The active enzyme may
CC have an alpha(4)beta(4) structure (Probable).
CC {ECO:0000305|PubMed:11389597}.
CC -!- SUBCELLULAR LOCATION: Plastid, chloroplast {ECO:0000305}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1;
CC IsoId=Q93YZ7-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q93YZ7-2; Sequence=VSP_044766, VSP_044767;
CC Name=3;
CC IsoId=Q93YZ7-3; Sequence=VSP_044768;
CC -!- SIMILARITY: Belongs to the acetolactate synthase small subunit family.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAD32291.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AC006533; AAD32291.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002685; AEC08586.1; -; Genomic_DNA.
DR EMBL; CP002685; AEC08587.1; -; Genomic_DNA.
DR EMBL; CP002685; AEC08588.1; -; Genomic_DNA.
DR EMBL; AY058881; AAL24267.1; -; mRNA.
DR EMBL; AY103307; AAM65359.1; -; mRNA.
DR EMBL; AK318696; BAH56811.1; -; mRNA.
DR PIR; D84725; D84725.
DR RefSeq; NP_850172.1; NM_179841.3. [Q93YZ7-1]
DR RefSeq; NP_850173.2; NM_179842.2. [Q93YZ7-2]
DR RefSeq; NP_850174.1; NM_179843.1. [Q93YZ7-3]
DR PDB; 6U9H; EM; 3.80 A; F/G/J/K/N/O/R/S=1-491.
DR PDB; 6VZ8; EM; 3.45 A; F/G/J/K/N/O/R/S=1-491.
DR PDBsum; 6U9H; -.
DR PDBsum; 6VZ8; -.
DR AlphaFoldDB; Q93YZ7; -.
DR SMR; Q93YZ7; -.
DR BioGRID; 3085; 1.
DR STRING; 3702.AT2G31810.1; -.
DR PaxDb; Q93YZ7; -.
DR PRIDE; Q93YZ7; -.
DR ProteomicsDB; 247368; -. [Q93YZ7-1]
DR EnsemblPlants; AT2G31810.1; AT2G31810.1; AT2G31810. [Q93YZ7-1]
DR EnsemblPlants; AT2G31810.2; AT2G31810.2; AT2G31810. [Q93YZ7-2]
DR EnsemblPlants; AT2G31810.3; AT2G31810.3; AT2G31810. [Q93YZ7-3]
DR GeneID; 817738; -.
DR Gramene; AT2G31810.1; AT2G31810.1; AT2G31810. [Q93YZ7-1]
DR Gramene; AT2G31810.2; AT2G31810.2; AT2G31810. [Q93YZ7-2]
DR Gramene; AT2G31810.3; AT2G31810.3; AT2G31810. [Q93YZ7-3]
DR KEGG; ath:AT2G31810; -.
DR Araport; AT2G31810; -.
DR TAIR; locus:2045248; AT2G31810.
DR eggNOG; KOG2663; Eukaryota.
DR InParanoid; Q93YZ7; -.
DR OMA; DVYPVEQ; -.
DR PhylomeDB; Q93YZ7; -.
DR BioCyc; ARA:AT2G31810-MON; -.
DR UniPathway; UPA00047; UER00055.
DR UniPathway; UPA00049; UER00059.
DR PRO; PR:Q93YZ7; -.
DR Proteomes; UP000006548; Chromosome 2.
DR ExpressionAtlas; Q93YZ7; baseline and differential.
DR Genevisible; Q93YZ7; 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:0003984; F:acetolactate synthase activity; IBA:GO_Central.
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:0050790; P:regulation of catalytic activity; IDA:TAIR.
DR GO; GO:0001666; P:response to hypoxia; IEP:TAIR.
DR GO; GO:0009099; P:valine biosynthetic 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; 1.
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 3D-structure; Alternative splicing; Amino-acid biosynthesis;
KW Branched-chain amino acid biosynthesis; Chloroplast; Plastid;
KW Reference proteome; Repeat; Transit peptide.
FT TRANSIT 1..27
FT /note="Chloroplast"
FT /evidence="ECO:0000255"
FT CHAIN 28..491
FT /note="Acetolactate synthase small subunit 2,
FT chloroplastic"
FT /id="PRO_0000420866"
FT DOMAIN 88..160
FT /note="ACT 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01007"
FT DOMAIN 321..395
FT /note="ACT 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01007"
FT VAR_SEQ 1..105
FT /note="MAAISVSSSPSIRCLRSACSDSSPALVSSTRVSFPAKISYLSGISSHRGDEM
FT GKRMEGFVRSVDGKISDASFSEASSATPKSKVRKHTISVFVGDESGMINRIAG -> MK
FT WVREWKDSLEASMGRSLMRLSPKLHLRLQNRR (in isoform 2)"
FT /evidence="ECO:0000305"
FT /id="VSP_044766"
FT VAR_SEQ 349
FT /note="S -> AY (in isoform 2)"
FT /evidence="ECO:0000305"
FT /id="VSP_044767"
FT VAR_SEQ 441..464
FT /note="LTGDLDKMVALQRLLEPYGICEVA -> VA (in isoform 3)"
FT /evidence="ECO:0000305"
FT /id="VSP_044768"
FT MUTAGEN 98
FT /note="G->E: Increased feedback inhibition by
FT valine/isoleucine."
FT /evidence="ECO:0000269|PubMed:11852076"
FT MUTAGEN 107
FT /note="F->A: Decreased feedback inhibition by leucine and
FT valine/isoleucine."
FT /evidence="ECO:0000269|PubMed:11852076"
FT MUTAGEN 112
FT /note="Y->A: Increased feedback inhibition by leucine."
FT /evidence="ECO:0000269|PubMed:11852076"
FT MUTAGEN 113
FT /note="N->A: Decreased feedback inhibition by
FT valine/isoleucine."
FT /evidence="ECO:0000269|PubMed:11852076"
FT MUTAGEN 331
FT /note="G->D: Decreased feedback inhibition by leucine and
FT valine/isoleucine."
FT /evidence="ECO:0000269|PubMed:11852076"
FT MUTAGEN 340
FT /note="F->A: Decreased feedback inhibition by
FT valine/isoleucine."
FT /evidence="ECO:0000269|PubMed:11852076"
FT MUTAGEN 345
FT /note="Y->A: No effect."
FT /evidence="ECO:0000269|PubMed:11852076"
FT MUTAGEN 346
FT /note="N->A,H: Decreased feedback inhibition by leucine and
FT increased feedback inhibition by valine/isoleucine."
FT /evidence="ECO:0000269|PubMed:11852076"
FT STRAND 85..94
FT /evidence="ECO:0007829|PDB:6VZ8"
FT HELIX 99..110
FT /evidence="ECO:0007829|PDB:6VZ8"
FT STRAND 114..121
FT /evidence="ECO:0007829|PDB:6VZ8"
FT STRAND 123..134
FT /evidence="ECO:0007829|PDB:6VZ8"
FT HELIX 136..145
FT /evidence="ECO:0007829|PDB:6VZ8"
FT HELIX 146..148
FT /evidence="ECO:0007829|PDB:6VZ8"
FT STRAND 152..157
FT /evidence="ECO:0007829|PDB:6VZ8"
FT STRAND 163..174
FT /evidence="ECO:0007829|PDB:6VZ8"
FT HELIX 177..190
FT /evidence="ECO:0007829|PDB:6VZ8"
FT STRAND 193..197
FT /evidence="ECO:0007829|PDB:6VZ8"
FT STRAND 199..208
FT /evidence="ECO:0007829|PDB:6VZ8"
FT HELIX 210..220
FT /evidence="ECO:0007829|PDB:6VZ8"
FT STRAND 225..230
FT /evidence="ECO:0007829|PDB:6VZ8"
FT STRAND 234..237
FT /evidence="ECO:0007829|PDB:6VZ8"
FT STRAND 318..326
FT /evidence="ECO:0007829|PDB:6VZ8"
FT HELIX 332..342
FT /evidence="ECO:0007829|PDB:6VZ8"
FT STRAND 348..354
FT /evidence="ECO:0007829|PDB:6VZ8"
FT STRAND 361..369
FT /evidence="ECO:0007829|PDB:6VZ8"
FT HELIX 371..381
FT /evidence="ECO:0007829|PDB:6VZ8"
FT STRAND 385..392
FT /evidence="ECO:0007829|PDB:6VZ8"
FT STRAND 398..409
FT /evidence="ECO:0007829|PDB:6VZ8"
FT HELIX 412..425
FT /evidence="ECO:0007829|PDB:6VZ8"
FT STRAND 428..432
FT /evidence="ECO:0007829|PDB:6VZ8"
FT STRAND 434..443
FT /evidence="ECO:0007829|PDB:6VZ8"
FT HELIX 445..454
FT /evidence="ECO:0007829|PDB:6VZ8"
FT TURN 455..457
FT /evidence="ECO:0007829|PDB:6VZ8"
FT STRAND 458..463
FT /evidence="ECO:0007829|PDB:6VZ8"
FT STRAND 469..472
FT /evidence="ECO:0007829|PDB:6VZ8"
SQ SEQUENCE 491 AA; 53873 MW; A6800F3235E74D2E CRC64;
MAAISVSSSP SIRCLRSACS DSSPALVSST RVSFPAKISY LSGISSHRGD EMGKRMEGFV
RSVDGKISDA SFSEASSATP KSKVRKHTIS VFVGDESGMI NRIAGVFARR GYNIESLAVG
LNRDKALFTI VVCGTERVLQ QVIEQLQKLV NVLKVEDISS EPQVERELML VKVNAHPESR
AEIMWLVDTF RARVVDIAEH ALTIEVTGDP GKMIAVERNL KKFQIREIVR TGKIALRREK
MGATAPFWRF SAASYPDLKE QAPVSVLRSS KKGAIVPQKE TSAGGDVYPV EPFFDPKVHR
ILDAHWGLLT DEDTSGLRSH TLSLLVNDIP GVLNIVTGVF ARRGYNIQSL AVGHAETKGI
SRITTVIPAT DESVSKLVQQ LYKLVDVHEV HDLTHLPFSE RELMLIKIAV NAAARRDVLD
IASIFRAKAV DVSDHTITLQ LTGDLDKMVA LQRLLEPYGI CEVARTGRVA LARESGVDSK
YLRGYSFPLT G
