ID   ILVB2_BRANA             Reviewed;         637 AA.
AC   P14874;
DT   01-APR-1990, integrated into UniProtKB/Swiss-Prot.
DT   01-APR-1990, sequence version 1.
DT   27-MAR-2024, entry version 133.
DE   RecName: Full=Acetolactate synthase 2, chloroplastic;
DE            EC=2.2.1.6;
DE   AltName: Full=ALS II;
DE   AltName: Full=Acetohydroxy-acid synthase II;
DE   AltName: Full=Acetolactate synthase II;
DE   Flags: Precursor;
OS   Brassica napus (Rape).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   rosids; malvids; Brassicales; Brassicaceae; Brassiceae; Brassica.
OX   NCBI_TaxID=3708;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=cv. Topas;
RX   PubMed=1896019; DOI=10.1007/bf00264210;
RA   Rutledge R.G., Ouellet T., Hattori J., Miki B.L.A.;
RT   "Molecular characterization and genetic origin of the Brassica napus
RT   acetohydroxyacid synthase multigene family.";
RL   Mol. Gen. Genet. 229:31-40(1991).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=cv. Westar; TISSUE=Leaf;
RX   PubMed=2482934; DOI=10.1007/bf00259614;
RA   Wiersma P.A., Schmiemann M.G., Condie J.A., Crosby W.L., Moloney M.M.;
RT   "Isolation, expression and phylogenetic inheritance of an acetolactate
RT   synthase gene from Brassica napus.";
RL   Mol. Gen. Genet. 219:413-420(1989).
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=H(+) + 2 pyruvate = (2S)-2-acetolactate + CO2;
CC         Xref=Rhea:RHEA:25249, ChEBI:CHEBI:15361, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:16526, ChEBI:CHEBI:58476; EC=2.2.1.6;
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250};
CC       Note=Binds 1 Mg(2+) ion per subunit. {ECO:0000250};
CC   -!- COFACTOR:
CC       Name=thiamine diphosphate; Xref=ChEBI:CHEBI:58937;
CC         Evidence={ECO:0000250};
CC       Note=Binds 1 thiamine pyrophosphate per subunit. {ECO:0000250};
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   -!- SUBCELLULAR LOCATION: Plastid, chloroplast.
CC   -!- MISCELLANEOUS: Acetolactate synthase is the target enzyme for
CC       sulfonylurea and imidazolinone herbicides.
CC   -!- SIMILARITY: Belongs to the TPP enzyme family. {ECO:0000305}.
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DR   EMBL; Z11525; CAA77614.1; -; Genomic_DNA.
DR   EMBL; X16708; CAA34680.1; -; Genomic_DNA.
DR   PIR; JQ0357; YCRP.
DR   AlphaFoldDB; P14874; -.
DR   SMR; P14874; -.
DR   EnsemblPlants; CDX79849; CDX79849; GSBRNA2T00132697001.
DR   Gramene; CDX79849; CDX79849; GSBRNA2T00132697001.
DR   OMA; GQNQLWC; -.
DR   UniPathway; UPA00047; UER00055.
DR   UniPathway; UPA00049; UER00059.
DR   GO; GO:0009507; C:chloroplast; IEA:UniProtKB-SubCell.
DR   GO; GO:0003984; F:acetolactate synthase activity; IEA:UniProtKB-EC.
DR   GO; GO:0050660; F:flavin adenine dinucleotide binding; IEA:InterPro.
DR   GO; GO:0000287; F:magnesium ion binding; IEA:InterPro.
DR   GO; GO:0030976; F:thiamine pyrophosphate binding; IEA:InterPro.
DR   GO; GO:0009097; P:isoleucine biosynthetic process; IEA:UniProtKB-UniPathway.
DR   GO; GO:0009635; P:response to herbicide; IEA:UniProtKB-KW.
DR   GO; GO:0009099; P:valine biosynthetic process; IEA:UniProtKB-UniPathway.
DR   CDD; cd02015; TPP_AHAS; 1.
DR   CDD; cd07035; TPP_PYR_POX_like; 1.
DR   Gene3D; 3.40.50.970; -; 2.
DR   Gene3D; 3.40.50.1220; TPP-binding domain; 1.
DR   InterPro; IPR012846; Acetolactate_synth_lsu.
DR   InterPro; IPR039368; AHAS_TPP.
DR   InterPro; IPR029035; DHS-like_NAD/FAD-binding_dom.
DR   InterPro; IPR029061; THDP-binding.
DR   InterPro; IPR012000; Thiamin_PyroP_enz_cen_dom.
DR   InterPro; IPR012001; Thiamin_PyroP_enz_TPP-bd_dom.
DR   InterPro; IPR000399; TPP-bd_CS.
DR   InterPro; IPR045229; TPP_enz.
DR   InterPro; IPR011766; TPP_enzyme_TPP-bd.
DR   NCBIfam; TIGR00118; acolac_lg; 1.
DR   PANTHER; PTHR18968:SF13; ACETOLACTATE SYNTHASE CATALYTIC SUBUNIT, MITOCHONDRIAL; 1.
DR   PANTHER; PTHR18968; THIAMINE PYROPHOSPHATE ENZYMES; 1.
DR   Pfam; PF02775; TPP_enzyme_C; 1.
DR   Pfam; PF00205; TPP_enzyme_M; 1.
DR   Pfam; PF02776; TPP_enzyme_N; 1.
DR   SUPFAM; SSF52467; DHS-like NAD/FAD-binding domain; 1.
DR   SUPFAM; SSF52518; Thiamin diphosphate-binding fold (THDP-binding); 2.
DR   PROSITE; PS00187; TPP_ENZYMES; 1.
PE   3: Inferred from homology;
KW   Amino-acid biosynthesis; Branched-chain amino acid biosynthesis;
KW   Chloroplast; FAD; Flavoprotein; Herbicide resistance; Magnesium;
KW   Metal-binding; Plastid; Thiamine pyrophosphate; Transferase;
KW   Transit peptide.
FT   TRANSIT         1..73
FT                   /note="Chloroplast"
FT                   /evidence="ECO:0000250"
FT   CHAIN           74..637
FT                   /note="Acetolactate synthase 2, chloroplastic"
FT                   /id="PRO_0000035657"
FT   REGION          35..69
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          462..542
FT                   /note="Thiamine pyrophosphate binding"
FT   BINDING         120
FT                   /ligand="thiamine diphosphate"
FT                   /ligand_id="ChEBI:CHEBI:58937"
FT                   /evidence="ECO:0000250"
FT   BINDING         222
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000250"
FT   BINDING         329..350
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000250"
FT   BINDING         372..391
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000250"
FT   BINDING         513
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000250"
FT   BINDING         540
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   637 AA;  69970 MW;  9FC6A6E8124C2455 CRC64;
     MASFSFFGTI PSSPTKASVF SLPVSVTTLP SFPRRRATRV SVSANSKKDQ DRTASRRENP
     STFSSKYAPN VPRSGADILV EALERQGVDV VFAYPGGASM EIHQALTRSN TIRNVLPRHE
     QGGIFAAEGY ARSSGKPGIC IATSGPGAMN LVSGLADALF DSVPLIAITG QVPRRMIGTM
     AFQETPVVEV TRTITKHNYL VMEVDDIPRI VREAFFLATS VRPGPVLIDV PKDVQQQFAI
     PNWEQPMRLP LYMSTMPKPP KVSHLEQILR LVSESKRPVL YVGGGCLNSS EELRRFVELT
     GIPVASTFMG LGSYPCDDEE FSLQMLGMHG TVYANYAVEY SDLLLAFGVR FDDRVTGKLE
     AFASRAKIVH IDIDSTEIGK NKTPHVSVCC DVQLALQGMN EVLENRRDVL DFGEWRCELN
     EQRLKFPLRY KTFGEEIPPQ YAIQLLDELT DGKAIITTGV GQHQMWAAQF YRFKKPRQWL
     SSGGLGAMGF GLPAAMGAAI ANPGAVVVDI DGDGSFIMNI QELATIRVEN LPVKVLLINN
     QHLGMVLQWE DHFYAANRAD SFLGDPANPE AVFPDMLLFA ASCGIPAARV TRREDLREAI
     QTMLDTPGPF LLDVVCPHQD HVLPLIPSGG TFKDIIV
//