ILVG_MYCBO
ID ILVG_MYCBO Reviewed; 547 AA.
AC P66947; A0A1R3Y084; Q50613; X2BJA5;
DT 11-OCT-2004, integrated into UniProtKB/Swiss-Prot.
DT 11-OCT-2004, sequence version 1.
DT 03-AUG-2022, entry version 95.
DE RecName: Full=Probable acetolactate synthase;
DE EC=2.2.1.6;
DE AltName: Full=ALS;
DE AltName: Full=Acetohydroxy-acid synthase;
GN Name=ilvG; OrderedLocusNames=BQ2027_MB1851;
OS Mycobacterium bovis (strain ATCC BAA-935 / AF2122/97).
OC Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC Mycobacterium; Mycobacterium tuberculosis complex.
OX NCBI_TaxID=233413;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-935 / AF2122/97;
RX PubMed=12788972; DOI=10.1073/pnas.1130426100;
RA Garnier T., Eiglmeier K., Camus J.-C., Medina N., Mansoor H., Pryor M.,
RA Duthoy S., Grondin S., Lacroix C., Monsempe C., Simon S., Harris B.,
RA Atkin R., Doggett J., Mayes R., Keating L., Wheeler P.R., Parkhill J.,
RA Barrell B.G., Cole S.T., Gordon S.V., Hewinson R.G.;
RT "The complete genome sequence of Mycobacterium bovis.";
RL Proc. Natl. Acad. Sci. U.S.A. 100:7877-7882(2003).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND GENOME REANNOTATION.
RC STRAIN=ATCC BAA-935 / AF2122/97;
RX PubMed=28385856; DOI=10.1128/genomea.00157-17;
RA Malone K.M., Farrell D., Stuber T.P., Schubert O.T., Aebersold R.,
RA Robbe-Austerman S., Gordon S.V.;
RT "Updated reference genome sequence and annotation of Mycobacterium bovis
RT AF2122/97.";
RL Genome Announc. 5:E00157-E00157(2017).
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 -!- SIMILARITY: Belongs to the TPP enzyme family. {ECO:0000305}.
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DR EMBL; LT708304; SIU00455.1; -; Genomic_DNA.
DR RefSeq; NP_855503.1; NC_002945.3.
DR RefSeq; WP_003409218.1; NC_002945.4.
DR AlphaFoldDB; P66947; -.
DR SMR; P66947; -.
DR EnsemblBacteria; SIU00455; SIU00455; BQ2027_MB1851.
DR PATRIC; fig|233413.5.peg.2031; -.
DR OMA; PGPYGCL; -.
DR UniPathway; UPA00047; UER00055.
DR UniPathway; UPA00049; UER00059.
DR Proteomes; UP000001419; Chromosome.
DR GO; GO:0003984; F:acetolactate synthase activity; IEA:UniProtKB-EC.
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 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 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; Thiamine pyrophosphate;
KW Transferase.
FT CHAIN 1..547
FT /note="Probable acetolactate synthase"
FT /id="PRO_0000090804"
FT REGION 388..468
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 299..318
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250"
FT BINDING 439
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
FT BINDING 466
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
SQ SEQUENCE 547 AA; 57521 MW; 2D5CC10B21406887 CRC64;
MSTDTAPAQT MHAGRLIARR LKASGIDTVF TLSGGHLFSI YDGCREEGIR LIDTRHEQTA
AFAAEGWSKV TRVPGVAALT AGPGITNGMS AMAAAQQNQS PLVVLGGRAP ALRWGMGSLQ
EIDHVPFVAP VARFAATAQS AENAGLLVDQ ALQAAVSAPS GVAFVDFPMD HAFSMSSDNG
RPGALTELPA GPTPAGDALD RAAGLLSTAQ RPVIMAGTNV WWGHAEAALL RLVEERHIPV
LMNGMARGVV PADHRLAFSR ARSKALGEAD VALIVGVPMD FRLGFGGVFG STTQLIVADR
VEPAREHPRP VAAGLYGDLT ATLSALAGSG GTDHQGWIEE LATAETMARD LEKAELVDDR
IPLHPMRVYA ELAALLERDA LVVIDAGDFG SYAGRMIDSY LPGCWLDSGP FGCLGSGPGY
ALAAKLARPQ RQVVLLQGDG AFGFSGMEWD TLVRHNVAVV SVIGNNGIWG LEKHPMEALY
GYSVVAELRP GTRYDEVVRA LGGHGELVSV PAELRPALER AFASGLPAVV NVLTDPSVAY
PRRSNLA
