ILVB_LACLA
ID ILVB_LACLA Reviewed; 575 AA.
AC Q02137; Q9CG84;
DT 01-JUL-1993, integrated into UniProtKB/Swiss-Prot.
DT 26-SEP-2001, sequence version 2.
DT 03-AUG-2022, entry version 144.
DE RecName: Full=Acetolactate synthase large subunit;
DE Short=AHAS;
DE EC=2.2.1.6;
DE AltName: Full=Acetohydroxy-acid synthase large subunit;
DE Short=ALS;
GN Name=ilvB; OrderedLocusNames=LL1224; ORFNames=L0078;
OS Lactococcus lactis subsp. lactis (strain IL1403) (Streptococcus lactis).
OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae;
OC Lactococcus.
OX NCBI_TaxID=272623;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=NCDO 2118;
RX PubMed=1400210; DOI=10.1128/jb.174.20.6580-6589.1992;
RA Godon J.-J., Chopin M.-C., Ehrlich S.D.;
RT "Branched-chain amino acid biosynthesis genes in Lactococcus lactis subsp.
RT lactis.";
RL J. Bacteriol. 174:6580-6589(1992).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=IL1403;
RX PubMed=11337471; DOI=10.1101/gr.gr-1697r;
RA Bolotin A., Wincker P., Mauger S., Jaillon O., Malarme K., Weissenbach J.,
RA Ehrlich S.D., Sorokin A.;
RT "The complete genome sequence of the lactic acid bacterium Lactococcus
RT lactis ssp. lactis IL1403.";
RL Genome Res. 11:731-753(2001).
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 -!- SUBUNIT: Dimer of large and small chains.
CC -!- MISCELLANEOUS: Contains 1 molecule of FAD per monomer. The role of this
CC cofactor is not clear considering that the reaction does not involve
CC redox chemistry (By similarity). {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the TPP enzyme family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAK05322.1; Type=Erroneous termination; Note=Truncated C-terminus.; Evidence={ECO:0000305};
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DR EMBL; U92974; AAB81919.1; -; Genomic_DNA.
DR EMBL; AE005176; AAK05322.1; ALT_SEQ; Genomic_DNA.
DR PIR; H86777; H86777.
DR PIR; S35138; S35138.
DR RefSeq; NP_267380.1; NC_002662.1.
DR AlphaFoldDB; Q02137; -.
DR SMR; Q02137; -.
DR STRING; 272623.L0078; -.
DR PaxDb; Q02137; -.
DR EnsemblBacteria; AAK05322; AAK05322; L0078.
DR KEGG; lla:L0078; -.
DR PATRIC; fig|272623.7.peg.1323; -.
DR eggNOG; COG0028; Bacteria.
DR HOGENOM; CLU_013748_1_2_9; -.
DR UniPathway; UPA00047; UER00055.
DR UniPathway; UPA00049; UER00059.
DR Proteomes; UP000002196; Chromosome.
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: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; FAD;
KW Flavoprotein; Magnesium; Metal-binding; Reference proteome;
KW Thiamine pyrophosphate; Transferase.
FT CHAIN 1..575
FT /note="Acetolactate synthase large subunit"
FT /id="PRO_0000090785"
FT REGION 395..475
FT /note="Thiamine pyrophosphate binding"
FT BINDING 57
FT /ligand="thiamine diphosphate"
FT /ligand_id="ChEBI:CHEBI:58937"
FT /evidence="ECO:0000250"
FT BINDING 159
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250"
FT BINDING 265..286
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250"
FT BINDING 308..327
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250"
FT BINDING 446
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
FT BINDING 473
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
FT CONFLICT 111..112
FT /note="PL -> RQ (in Ref. 1; AAB81919)"
FT /evidence="ECO:0000305"
FT CONFLICT 298
FT /note="V -> F (in Ref. 1; AAB81919)"
FT /evidence="ECO:0000305"
FT CONFLICT 353..354
FT /note="TK -> IE (in Ref. 1; AAB81919)"
FT /evidence="ECO:0000305"
FT CONFLICT 557
FT /note="S -> N (in Ref. 1; AAB81919)"
FT /evidence="ECO:0000305"
FT CONFLICT 568
FT /note="E -> K (in Ref. 1; AAB81919)"
FT /evidence="ECO:0000305"
FT CONFLICT 572
FT /note="V -> I (in Ref. 1; AAB81919)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 575 AA; 62850 MW; 2F7168C50409035F CRC64;
MKKIKLEKPT SGSQLVLQTL KELGVEIIFG YPGGAMLPLY DAIHNFEGIQ HILARHEQGA
THEAEGYAKS SGKVGVVVVT SGPGATNAVT GIADAYLDSV PLLVFTGQVG PLSIGKDAFQ
EADTVGITAP ITKYNYQIRE TADIPRIVTE AYYLARTGRP GPVEIDLPKD VSTLEVTEIN
DPSLNLPHYH ESEKATDEQL QELLTELSVS KKPVIIAGGG INYSGSVDIF RAFVEKYQIP
VVSTLLGLGT LPISHELQLG MAGMHGSYAA NMALVEADYI INLGSRFDDR VVSNPAKVAK
NAVVAHIDID AAELGKIVKT DIPILSDLKA ALSRLLQLNK VRTDFNDWIK TVTKNKEKAP
FTYEPQNHDI RPQETIKLIG EYTQGDAIIV TDVGQHQMWV AQYYPYKNAR QLITSGGMGT
MGFGIPAAIG AKLAQPNKNV IVFVGDGGFQ MTNQELALLN GYGIAIKVVL INNHSLGMVR
QWQESFYEER RSQSVFDVEP NFQLLAEAYG IKHVKLDNPK TLADDLKIIT EDEPMLIEVL
ISKSEHVLPM IPAGLHSDEM IGLHFTDENE EVDNA
