ILVI_SALTY
ID ILVI_SALTY Reviewed; 574 AA.
AC P40811;
DT 01-FEB-1995, integrated into UniProtKB/Swiss-Prot.
DT 19-DEC-2001, sequence version 3.
DT 03-AUG-2022, entry version 142.
DE RecName: Full=Acetolactate synthase isozyme 3 large subunit;
DE EC=2.2.1.6;
DE AltName: Full=AHAS-III;
DE AltName: Full=ALS-III;
DE AltName: Full=Acetohydroxy-acid synthase III large subunit;
GN Name=ilvI; OrderedLocusNames=STM0116;
OS Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Salmonella.
OX NCBI_TaxID=99287;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=LT2 / SGSC1412 / ATCC 700720;
RX PubMed=11677609; DOI=10.1038/35101614;
RA McClelland M., Sanderson K.E., Spieth J., Clifton S.W., Latreille P.,
RA Courtney L., Porwollik S., Ali J., Dante M., Du F., Hou S., Layman D.,
RA Leonard S., Nguyen C., Scott K., Holmes A., Grewal N., Mulvaney E.,
RA Ryan E., Sun H., Florea L., Miller W., Stoneking T., Nhan M., Waterston R.,
RA Wilson R.K.;
RT "Complete genome sequence of Salmonella enterica serovar Typhimurium LT2.";
RL Nature 413:852-856(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 516-574.
RC STRAIN=LT2;
RX PubMed=1851954; DOI=10.1007/bf00273623;
RA Jahreis K., Postma P.W., Lengeler J.W.;
RT "Nucleotide sequence of the ilvH-fruR gene region of Escherichia coli K12
RT and Salmonella typhimurium LT2.";
RL Mol. Gen. Genet. 226:332-336(1991).
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 -!- ACTIVITY REGULATION: Sensitive to valine inhibition.
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 chain H and chain I.
CC -!- MISCELLANEOUS: S.typhimurium contains genes for 3 AHAS isozymes: ilvBN,
CC ilvGM and ilvIH.
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=AAL19080.1; Type=Erroneous termination; Note=Truncated C-terminus.; Evidence={ECO:0000305};
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DR EMBL; AE006468; AAL19080.1; ALT_SEQ; Genomic_DNA.
DR EMBL; X55456; CAA39101.1; -; Genomic_DNA.
DR PIR; S15939; S15939.
DR RefSeq; NP_459121.1; NC_003197.2.
DR AlphaFoldDB; P40811; -.
DR SMR; P40811; -.
DR STRING; 99287.STM0116; -.
DR PaxDb; P40811; -.
DR EnsemblBacteria; AAL19080; AAL19080; STM0116.
DR GeneID; 1251634; -.
DR KEGG; stm:STM0116; -.
DR PATRIC; fig|99287.12.peg.121; -.
DR HOGENOM; CLU_013748_1_2_6; -.
DR OMA; CFGTSGP; -.
DR PhylomeDB; P40811; -.
DR UniPathway; UPA00047; UER00055.
DR UniPathway; UPA00049; UER00059.
DR Proteomes; UP000001014; Chromosome.
DR GO; GO:0005948; C:acetolactate synthase complex; IBA:GO_Central.
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: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; 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..574
FT /note="Acetolactate synthase isozyme 3 large subunit"
FT /id="PRO_0000090790"
FT REGION 397..477
FT /note="Thiamine pyrophosphate binding"
FT BINDING 51
FT /ligand="thiamine diphosphate"
FT /ligand_id="ChEBI:CHEBI:58937"
FT /evidence="ECO:0000250"
FT BINDING 153
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250"
FT BINDING 261..282
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250"
FT BINDING 304..323
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250"
FT BINDING 448
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
FT BINDING 475
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
SQ SEQUENCE 574 AA; 62896 MW; 72EB67FA2667B398 CRC64;
MEMLSGAEMV VRSLIDQGVK QVFGYPGGAV LDIYDALHTV GGIDHVLVRH EQAAVHMADG
LARATGDVGV VLVTSGPGAT NAITGIATAY MDSIPLVILS GQVATSLIGY DAFQECDMVG
ISRPVVKHSF LVKQTEDIPL VLKKAFWLAA SGRPGPVVVD LPKDILNPAK KMPYAWPETV
SMRSYNPTTS GHKGQIKRAL QTLASAKKPV VYVGGGAISA ACYAPLRHII ETFNLPVVSS
LMGLGAFPAT HRQSLGMLGM HGTYEANMTM HNADVIFAVG VRFDDRTTNN LAKYCPNATV
LHIDIDPTSI SKTVNADIPV VGDARLVLEQ MLELLAQDAP SQPQDDIRDW WQQIESWRAR
QCLKYDAESE SIKPQAVIET LWRLTKGDAY VTSDVGQHQM FAALYYPFDK PRRWINSGGL
GTMGFGLPAA LGVKMALPKE MVVCVTGDGS IQMNIQELST ALQYELPVLV LNLNNRYLGM
VKQWQDMIYS GRHSQSYMQS LPDFVRLAEA YGHVGLQINR PDELESKLSE ALEHVRNNRL
VFVDVTVDGS EHVYPMQIRG GGMDEMWLSK TERT
