ID Q2WFB5_MONVA Unreviewed; 642 AA.
AC Q2WFB5;
DT 10-JAN-2006, integrated into UniProtKB/TrEMBL.
DT 10-JAN-2006, sequence version 1.
DT 27-MAR-2024, entry version 92.
DE RecName: Full=Acetolactate synthase {ECO:0000256|ARBA:ARBA00013145, ECO:0000256|RuleBase:RU003591};
DE EC=2.2.1.6 {ECO:0000256|ARBA:ARBA00013145, ECO:0000256|RuleBase:RU003591};
GN Name=als1 {ECO:0000313|EMBL:BAE53592.1};
OS Monochoria vaginalis (Heartshape false pickerel-weed) (Pontederia
OS vaginalis).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; Liliopsida; Commelinales; Pontederiaceae;
OC Pontederia; Pontederia subgen. Monochoria.
OX NCBI_TaxID=44972 {ECO:0000313|EMBL:BAE53592.1};
RN [1] {ECO:0000313|EMBL:BAE53592.1}
RP NUCLEOTIDE SEQUENCE.
RX PubMed=17660691; DOI=10.1266/ggs.82.207;
RA Ohsako T., Tominaga T.;
RT "Nucleotide substitutions in the acetolactate synthase genes of
RT sulfonylurea-resistant biotypes of Monochoria vaginalis (Pontederiaceae).";
RL Genes Genet. Syst. 82:207-215(2007).
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 Evidence={ECO:0000256|ARBA:ARBA00000673,
CC ECO:0000256|RuleBase:RU003591};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000256|RuleBase:RU003591};
CC Note=Binds 1 Mg(2+) ion per subunit. {ECO:0000256|RuleBase:RU003591};
CC -!- COFACTOR:
CC Name=thiamine diphosphate; Xref=ChEBI:CHEBI:58937;
CC Evidence={ECO:0000256|RuleBase:RU003591};
CC Note=Binds 1 thiamine pyrophosphate per subunit.
CC {ECO:0000256|RuleBase:RU003591};
CC -!- PATHWAY: Amino-acid biosynthesis; L-isoleucine biosynthesis; L-
CC isoleucine from 2-oxobutanoate: step 1/4.
CC {ECO:0000256|ARBA:ARBA00004974, ECO:0000256|RuleBase:RU003591}.
CC -!- PATHWAY: Amino-acid biosynthesis; L-valine biosynthesis; L-valine from
CC pyruvate: step 1/4. {ECO:0000256|ARBA:ARBA00005025,
CC ECO:0000256|RuleBase:RU003591}.
CC -!- SIMILARITY: Belongs to the TPP enzyme family.
CC {ECO:0000256|ARBA:ARBA00007812, ECO:0000256|RuleBase:RU003591}.
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DR EMBL; AB243610; BAE53591.1; -; Genomic_DNA.
DR EMBL; AB243611; BAE53592.1; -; Genomic_DNA.
DR AlphaFoldDB; Q2WFB5; -.
DR UniPathway; UPA00047; UER00055.
DR UniPathway; UPA00049; UER00059.
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:UniProtKB-UniRule.
DR GO; GO:0030976; F:thiamine pyrophosphate binding; IEA:UniProtKB-UniRule.
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 {ECO:0000256|ARBA:ARBA00022605,
KW ECO:0000256|RuleBase:RU003591};
KW Branched-chain amino acid biosynthesis {ECO:0000256|ARBA:ARBA00023304,
KW ECO:0000256|RuleBase:RU003591};
KW Flavoprotein {ECO:0000256|ARBA:ARBA00022630};
KW Herbicide resistance {ECO:0000256|ARBA:ARBA00022646};
KW Magnesium {ECO:0000256|RuleBase:RU003591};
KW Metal-binding {ECO:0000256|RuleBase:RU003591};
KW Thiamine pyrophosphate {ECO:0000256|RuleBase:RU003591};
KW Transferase {ECO:0000256|RuleBase:RU003591}.
FT DOMAIN 70..181
FT /note="Thiamine pyrophosphate enzyme N-terminal TPP-
FT binding"
FT /evidence="ECO:0000259|Pfam:PF02776"
FT DOMAIN 261..393
FT /note="Thiamine pyrophosphate enzyme central"
FT /evidence="ECO:0000259|Pfam:PF00205"
FT DOMAIN 456..611
FT /note="Thiamine pyrophosphate enzyme TPP-binding"
FT /evidence="ECO:0000259|Pfam:PF02775"
SQ SEQUENCE 642 AA; 70206 MW; 7352BF3EE2302DA6 CRC64;
MAASKPSPFP SSASSSRLLL HPFSKPLHPS PKLQRQQRIF VPLVTSSTTV AAPDAVFPPR
RNFAPDEPRK GADILVEALE REGVTDLFAY PGGASMEIHQ ALTRSPSITN HLLRHEQGEA
FAASGYARST GRPGVCIATS GPGATNLVSA LADALLDSIP MVAITGQVPR RMIGTDAFQE
TPIVEVTRSI TKHNYLVLDV DDIPRIIKEA FFIATSGRPG PVLVDIPKDI QQQLAVPVWN
PPVRLPGYVS RLPKPPALHL LQQIVRIVSE SSRPVLYVGG GSLHASEELR RFADLTGIPI
ASTLMGIGVY PLDGPLSLKM LGMHGTVYAN YAIDKADLLL AFGVRFDDRV TGKLEAFASR
AKIVHIDIDP AEIGKNKQPH VSICGDIKLA LQEMNEMIEE SGIHNKLDFS AWREELDQQK
KNYPLEYKTF GDLIPPQHAI ELLEELTNGE AIITTGVGQH QMWAAQYYSY KRPRQWLTSA
GLGAMGFGLP AAVGAAVGNP GVMVVDIDGD GSFQMNAQEL AIIRIENLDV KMLILNNQHL
GMVVQWEDRF YKSNRAHTYL GNPANESKVF PDFVKLAESY DIPAARVSKK SEVRDAIRKM
IQTPGPYLLD VIVPHEEHVL PMIPSGGAFK DMILDGDGRT VH
//
