ILVB2_BRANA
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 03-AUG-2022, entry version 126.
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}.
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; 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 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 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-bd_C.
DR PANTHER; PTHR18968; PTHR18968; 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; SSF52467; 1.
DR SUPFAM; SSF52518; SSF52518; 2.
DR TIGRFAMs; TIGR00118; acolac_lg; 1.
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
