ILVB2_MAIZE
ID ILVB2_MAIZE Reviewed; 638 AA.
AC Q41769;
DT 16-MAY-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 105.
DE RecName: Full=Acetolactate synthase 2, chloroplastic;
DE EC=2.2.1.6;
DE AltName: Full=Acetohydroxy-acid synthase 2;
DE Flags: Precursor;
GN Name=ALS2; Synonyms=AHAS109;
OS Zea mays (Maize).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; PACMAD clade;
OC Panicoideae; Andropogonodae; Andropogoneae; Tripsacinae; Zea.
OX NCBI_TaxID=4577;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=1600154; DOI=10.1007/bf00047723;
RA Fang L.Y., Gross P.R., Chen C.-H., Lillis M.;
RT "Sequence of two acetohydroxyacid synthase genes from Zea mays.";
RL Plant Mol. Biol. 18:1185-1187(1992).
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 {ECO:0000250}.
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; X63554; CAA45117.1; -; Genomic_DNA.
DR PIR; S22491; S22491.
DR AlphaFoldDB; Q41769; -.
DR SMR; Q41769; -.
DR STRING; 4577.GRMZM2G143357_P01; -.
DR ChEMBL; CHEMBL2366574; -.
DR PaxDb; Q41769; -.
DR PRIDE; Q41769; -.
DR eggNOG; KOG4166; Eukaryota.
DR UniPathway; UPA00047; UER00055.
DR UniPathway; UPA00049; UER00059.
DR Proteomes; UP000007305; Unplaced.
DR ExpressionAtlas; Q41769; baseline and differential.
DR GO; GO:0005948; C:acetolactate synthase complex; IBA:GO_Central.
DR GO; GO:0009507; C:chloroplast; IEA:UniProtKB-SubCell.
DR GO; GO:0003984; F:acetolactate synthase activity; IBA:GO_Central.
DR GO; GO:0050660; F:flavin adenine dinucleotide binding; IBA:GO_Central.
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; IBA:GO_Central.
DR GO; GO:0009635; P:response to herbicide; IEA:UniProtKB-KW.
DR GO; GO:0009099; P:valine biosynthetic process; IBA:GO_Central.
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; 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.
PE 3: Inferred from homology;
KW Amino-acid biosynthesis; Branched-chain amino acid biosynthesis;
KW Chloroplast; Disulfide bond; FAD; Flavoprotein; Herbicide resistance;
KW Magnesium; Metal-binding; Plastid; Reference proteome;
KW Thiamine pyrophosphate; Transferase; Transit peptide.
FT TRANSIT 1..39
FT /note="Chloroplast"
FT /evidence="ECO:0000255"
FT CHAIN 40..638
FT /note="Acetolactate synthase 2, chloroplastic"
FT /id="PRO_0000235808"
FT REGION 44..67
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 455..535
FT /note="Thiamine pyrophosphate binding"
FT /evidence="ECO:0000250"
FT BINDING 112
FT /ligand="thiamine diphosphate"
FT /ligand_id="ChEBI:CHEBI:58937"
FT /evidence="ECO:0000250"
FT BINDING 214
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250"
FT BINDING 320..341
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250"
FT BINDING 363..382
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250"
FT BINDING 506
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
FT BINDING 533
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
FT DISULFID 132..278
FT /evidence="ECO:0000250"
SQ SEQUENCE 638 AA; 69025 MW; 25A19AC4F3D119F1 CRC64;
MATAATAAAA LTGATTATPK SRRRAHHLAT RRALAAPIRC SALSRATPTA PPATPLRPWG
PNEPRKGSDI LVEALERCGV RDVFAYPGGA SMEIHQALTR SPVIANHLFR HEQGEAFAAS
AYARSSGRVG VCIATSGPGA TNLVSALADA LLDSVPMVAI TGQVPRRMIG TDAFQETPIV
EVTRSITKHN YLVLDVDDIP RVVQEAFFLA SSGRPGPVLV DIPKDIQQQM AVPAWDTPMS
LPGYIARLPK PPATEFLEQV LRLVGESRRP VLYVGGGCAA SGEELCRFVE LTGIPVTTTL
MGLGNFPSDD PLSLRMLGMH GTVYANYAVD KADLLLAFGV RFDDRVTGKI EAFAGRAKIV
HIDIDPAEIG KNKQPHVSIC ADVKLALQGM NTLLEGSTSK KSFDFGSWHD ELDQQKREFP
LGYKIFNEEI QPQYAIQVLD ELTKGEAIIA TGVGQHQMWA AQYYTYKRPR QWLSSAGLGA
MGFGLPAAAG AAVANPGVTV VDIDGDGSFL MNIQELAMIR IENLPVKVFV LNNQHLGMVV
QWEDRFYKAN RAHTFLGNPE NESEIYPDFV AIAKGFNIPA VRVTKKSEVH AAIKKMLEAP
GPYLLDIIVP HQEHVLPMIP SGGAFKDMIL DGDGRTVY
