ILVI_ECOLI
ID ILVI_ECOLI Reviewed; 574 AA.
AC P00893; P78045;
DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1997, sequence version 2.
DT 03-AUG-2022, entry version 181.
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=b0077, JW0076;
OS Escherichia coli (strain K12).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=83333;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=6308579; DOI=10.1093/nar/11.15.5299;
RA Squires C.H., Defelice M., Devereux J., Calvo J.M.;
RT "Molecular structure of ilvIH and its evolutionary relationship to ilvG in
RT Escherichia coli K12.";
RL Nucleic Acids Res. 11:5299-5313(1983).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12;
RX PubMed=1630901; DOI=10.1093/nar/20.13.3305;
RA Yura T., Mori H., Nagai H., Nagata T., Ishihama A., Fujita N., Isono K.,
RA Mizobuchi K., Nakata A.;
RT "Systematic sequencing of the Escherichia coli genome: analysis of the 0-
RT 2.4 min region.";
RL Nucleic Acids Res. 20:3305-3308(1992).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=9278503; DOI=10.1126/science.277.5331.1453;
RA Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V.,
RA Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F.,
RA Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B.,
RA Shao Y.;
RT "The complete genome sequence of Escherichia coli K-12.";
RL Science 277:1453-1462(1997).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND SEQUENCE REVISION.
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=16738553; DOI=10.1038/msb4100049;
RA Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S.,
RA Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.;
RT "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655
RT and W3110.";
RL Mol. Syst. Biol. 2:E1-E5(2006).
RN [5]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RA Ayala J.A.;
RT "Regulation of transcription at the 2-minute region of the genetic map of
RT Escherichia coli.";
RL Submitted (JAN-1991) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-8.
RX PubMed=3891724; DOI=10.1128/jb.163.1.186-198.1985;
RA Haughn G.W., Squires C.H., Defelice M., Largo C.T., Calvo J.M.;
RT "Unusual organization of the ilvIH promoter of Escherichia coli.";
RL J. Bacteriol. 163:186-198(1985).
RN [7]
RP PROTEIN SEQUENCE OF 1-12.
RC STRAIN=K12 / EMG2;
RX PubMed=9298646; DOI=10.1002/elps.1150180807;
RA Link A.J., Robison K., Church G.M.;
RT "Comparing the predicted and observed properties of proteins encoded in the
RT genome of Escherichia coli K-12.";
RL Electrophoresis 18:1259-1313(1997).
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 large and small chains.
CC -!- MISCELLANEOUS: E.coli contains genes for 3 AHAS isozymes: ilvBN, ilvGM
CC 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=CAA25755.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; X01609; CAA25755.1; ALT_FRAME; Genomic_DNA.
DR EMBL; U00096; AAC73188.2; -; Genomic_DNA.
DR EMBL; AP009048; BAB96646.2; -; Genomic_DNA.
DR EMBL; X55034; CAA38854.1; -; Genomic_DNA.
DR EMBL; M10738; AAA24026.1; -; Genomic_DNA.
DR PIR; E64729; YCEC3I.
DR RefSeq; WP_001295534.1; NZ_STEB01000010.1.
DR RefSeq; YP_025294.2; NC_000913.3.
DR AlphaFoldDB; P00893; -.
DR SMR; P00893; -.
DR BioGRID; 4259380; 38.
DR BioGRID; 853076; 5.
DR ComplexPortal; CPX-3575; Acetolactate synthase III complex.
DR DIP; DIP-6850N; -.
DR IntAct; P00893; 7.
DR STRING; 511145.b0077; -.
DR jPOST; P00893; -.
DR PaxDb; P00893; -.
DR PRIDE; P00893; -.
DR EnsemblBacteria; AAC73188; AAC73188; b0077.
DR EnsemblBacteria; BAB96646; BAB96646; BAB96646.
DR GeneID; 948793; -.
DR KEGG; ecj:JW0076; -.
DR KEGG; eco:b0077; -.
DR PATRIC; fig|1411691.4.peg.2203; -.
DR EchoBASE; EB0495; -.
DR eggNOG; COG0028; Bacteria.
DR HOGENOM; CLU_013748_1_2_6; -.
DR InParanoid; P00893; -.
DR OMA; CFGTSGP; -.
DR PhylomeDB; P00893; -.
DR BioCyc; EcoCyc:ACETOLACTSYNIII-ICHAIN-MON; -.
DR BioCyc; MetaCyc:ACETOLACTSYNIII-ICHAIN-MON; -.
DR BRENDA; 2.2.1.6; 2026.
DR UniPathway; UPA00047; UER00055.
DR UniPathway; UPA00049; UER00059.
DR PRO; PR:P00893; -.
DR Proteomes; UP000000318; Chromosome.
DR Proteomes; UP000000625; Chromosome.
DR GO; GO:0005948; C:acetolactate synthase complex; IPI:ComplexPortal.
DR GO; GO:0005829; C:cytosol; IDA:EcoCyc.
DR GO; GO:0003984; F:acetolactate synthase activity; IDA:EcoCyc.
DR GO; GO:0050660; F:flavin adenine dinucleotide binding; IBA:GO_Central.
DR GO; GO:0000287; F:magnesium ion binding; IDA:EcoCyc.
DR GO; GO:0030976; F:thiamine pyrophosphate binding; IDA:EcoCyc.
DR GO; GO:0009082; P:branched-chain amino acid biosynthetic process; IDA:ComplexPortal.
DR GO; GO:0009097; P:isoleucine biosynthetic process; IDA:EcoCyc.
DR GO; GO:0009099; P:valine biosynthetic process; IDA:EcoCyc.
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 Direct protein sequencing; FAD; Flavoprotein; Magnesium; Metal-binding;
KW Reference proteome; Thiamine pyrophosphate; Transferase.
FT CHAIN 1..574
FT /note="Acetolactate synthase isozyme 3 large subunit"
FT /id="PRO_0000090789"
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"
FT CONFLICT 202..203
FT /note="TL -> SV (in Ref. 1; CAA25755 and 5; CAA38854)"
FT /evidence="ECO:0000305"
FT CONFLICT 206
FT /note="A -> V (in Ref. 1; CAA25755 and 5; CAA38854)"
FT /evidence="ECO:0000305"
FT CONFLICT 254
FT /note="A -> V (in Ref. 1; CAA25755 and 5; CAA38854)"
FT /evidence="ECO:0000305"
FT CONFLICT 422
FT /note="T -> S (in Ref. 1; CAA25755 and 5; CAA38854)"
FT /evidence="ECO:0000305"
FT CONFLICT 437..438
FT /note="LP -> FA (in Ref. 5; CAA38854)"
FT /evidence="ECO:0000305"
FT CONFLICT 507..509
FT /note="LAE -> RG (in Ref. 1; CAA25755 and 5; CAA38854)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 574 AA; 62984 MW; B62DEF64338CBF8C CRC64;
MEMLSGAEMV VRSLIDQGVK QVFGYPGGAV LDIYDALHTV GGIDHVLVRH EQAAVHMADG
LARATGEVGV VLVTSGPGAT NAITGIATAY MDSIPLVVLS GQVATSLIGY DAFQECDMVG
ISRPVVKHSF LVKQTEDIPQ VLKKAFWLAA SGRPGPVVVD LPKDILNPAN KLPYVWPESV
SMRSYNPTTT GHKGQIKRAL QTLVAAKKPV VYVGGGAITA GCHQQLKETV EALNLPVVCS
LMGLGAFPAT HRQALGMLGM HGTYEANMTM HNADVIFAVG VRFDDRTTNN LAKYCPNATV
LHIDIDPTSI SKTVTADIPI VGDARQVLEQ MLELLSQESA HQPLDEIRDW WQQIEQWRAR
QCLKYDTHSE KIKPQAVIET LWRLTKGDAY VTSDVGQHQM FAALYYPFDK PRRWINSGGL
GTMGFGLPAA LGVKMALPEE TVVCVTGDGS IQMNIQELST ALQYELPVLV VNLNNRYLGM
VKQWQDMIYS GRHSQSYMQS LPDFVRLAEA YGHVGIQISH PHELESKLSE ALEQVRNNRL
VFVDVTVDGS EHVYPMQIRG GGMDEMWLSK TERT
