ILVB2_TOBAC
ID ILVB2_TOBAC Reviewed; 664 AA.
AC P09114;
DT 01-JUL-1989, integrated into UniProtKB/Swiss-Prot.
DT 01-JUL-1989, sequence version 1.
DT 03-AUG-2022, entry version 135.
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;
GN Name=ALS SURB;
OS Nicotiana tabacum (Common tobacco).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC asterids; lamiids; Solanales; Solanaceae; Nicotianoideae; Nicotianeae;
OC Nicotiana.
OX NCBI_TaxID=4097;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND MUTAGENESIS OF PRO-191 AND TRP-568.
RX PubMed=16453837; DOI=10.1002/j.1460-2075.1988.tb02937.x;
RA Lee K.Y., Townsend J., Tepperman J., Black M., Chui C.-F., Mazur B.,
RA Dunsmuir P., Bedbrook J.;
RT "The molecular basis of sulfonylurea herbicide resistance in tobacco.";
RL EMBO J. 7:1241-1248(1988).
RN [2]
RP SEQUENCE REVISION.
RA Lee K.Y.;
RL Submitted (AUG-1988) to the EMBL/GenBank/DDBJ databases.
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: There are two distinct ALS genes in tobacco. The enzyme
CC shown here is derived from the ALS gene on locus SuRB.
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; X07645; CAA30485.1; -; Genomic_DNA.
DR PIR; S00546; YCNT2.
DR AlphaFoldDB; P09114; -.
DR SMR; P09114; -.
DR STRING; 4097.P09114; -.
DR BindingDB; P09114; -.
DR SABIO-RK; P09114; -.
DR UniPathway; UPA00047; UER00055.
DR UniPathway; UPA00049; UER00059.
DR Proteomes; UP000084051; Unplaced.
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 1: Evidence at protein level;
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..91
FT /note="Chloroplast"
FT CHAIN 92..664
FT /note="Acetolactate synthase 2, chloroplastic"
FT /id="PRO_0000035660"
FT REGION 1..51
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 481..561
FT /note="Thiamine pyrophosphate binding"
FT COMPBIAS 10..30
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 138
FT /ligand="thiamine diphosphate"
FT /ligand_id="ChEBI:CHEBI:58937"
FT /evidence="ECO:0000250"
FT BINDING 240
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250"
FT BINDING 346..367
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250"
FT BINDING 389..408
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250"
FT BINDING 532
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
FT BINDING 559
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
FT DISULFID 158..304
FT /evidence="ECO:0000250"
FT MUTAGEN 191
FT /note="P->A: In S4-Hra; highly resistant to sulfonylurea
FT herbicides; when associated with L-568."
FT /evidence="ECO:0000269|PubMed:16453837"
FT MUTAGEN 568
FT /note="W->L: In S4-Hra; highly resistant to sulfonylurea
FT herbicides; when associated with A-191."
FT /evidence="ECO:0000269|PubMed:16453837"
SQ SEQUENCE 664 AA; 72418 MW; 0CDB9EE8E6513460 CRC64;
MAAAAAAPSP SFSKTLSSSS SKSSTLLPRS TFPFPHHPHK TTPPPLHLTP THIHSQRRRF
TISNVISTTQ KVSETQKAET FVSRFAPDEP RKGSDVLVEA LEREGVTDVF AYPGGASMEI
HQALTRSSII RNVLPRHEQG GVFAAEGYAR ATGFPGVCIA TSGPGATNLV SGLADALLDS
VPIVAITGQV PRRMIGTDAF QETPIVEVTR SITKHNYLVM DVEDIPRVVR EAFFLARSGR
PGPVLIDVPK DIQQQLVIPD WDQPMRLPGY MSRLPKLPNE MLLEQIVRLI SESKKPVLYV
GGGCSQSSEE LRRFVELTGI PVASTLMGLG AFPTGDELSL SMLGMHGTVY ANYAVDSSDL
LLAFGVRFDD RVTGKLEAFA SRAKIVHIDI DSAEIGKNKQ PHVSICADIK LALQGLNSIL
ESKEGKLKLD FSAWRQELTV QKVKYPLNFK TFGDAIPPQY AIQVLDELTN GSAIISTGVG
QHQMWAAQYY KYRKPRQWLT SGGLGAMGFG LPAAIGAAVG RPDEVVVDID GDGSFIMNVQ
ELATIKVENL PVKIMLLNNQ HLGMVVQWED RFYKANRAHT YLGNPSNEAE IFPNMLKFAE
ACGVPAARVT HRDDLRAAIQ KMLDTPGPYL LDVIVPHQEH VLPMIPSGGA FKDVITEGDG
RSSY
