ILVN_ECOLI
ID ILVN_ECOLI Reviewed; 96 AA.
AC P0ADF8; P08143; Q2M7Y3;
DT 01-AUG-1988, integrated into UniProtKB/Swiss-Prot.
DT 06-DEC-2005, sequence version 1.
DT 03-AUG-2022, entry version 117.
DE RecName: Full=Acetolactate synthase isozyme 1 small subunit;
DE EC=2.2.1.6;
DE AltName: Full=Acetohydroxy-acid synthase I small subunit;
DE Short=AHAS-I;
DE Short=ALS-I;
GN Name=ilvN; OrderedLocusNames=b3670, JW3645;
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=2989782; DOI=10.1093/nar/13.11.3995;
RA Wek R.C., Hausser C.A., Hatfield G.W.;
RT "The nucleotide sequence of the ilvBN operon of Escherichia coli: sequence
RT homologies of the acetohydroxy acid synthase isozymes.";
RL Nucleic Acids Res. 13:3995-4010(1985).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=2989781; DOI=10.1093/nar/13.11.3979;
RA Friden P., Donegan J., Mullen J., Tsui P., Freundlich M.;
RT "The ilvB locus of Escherichia coli K-12 is an operon encoding both
RT subunits of acetohydroxyacid synthase I.";
RL Nucleic Acids Res. 13:3979-3993(1985).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=7686882; DOI=10.1006/geno.1993.1230;
RA Burland V.D., Plunkett G. III, Daniels D.L., Blattner F.R.;
RT "DNA sequence and analysis of 136 kilobases of the Escherichia coli genome:
RT organizational symmetry around the origin of replication.";
RL Genomics 16:551-561(1993).
RN [4]
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 [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
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 [6]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 69-96.
RX PubMed=3301805; DOI=10.1128/jb.169.8.3556-3563.1987;
RA Friedrich M.J., Kadner R.J.;
RT "Nucleotide sequence of the uhp region of Escherichia coli.";
RL J. Bacteriol. 169:3556-3563(1987).
RN [7]
RP IDENTIFICATION BY 2D-GEL.
RX PubMed=9298644; DOI=10.1002/elps.1150180805;
RA VanBogelen R.A., Abshire K.Z., Moldover B., Olson E.R., Neidhardt F.C.;
RT "Escherichia coli proteome analysis using the gene-protein database.";
RL Electrophoresis 18:1243-1251(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 -!- 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 -!- INTERACTION:
CC P0ADF8; P08142: ilvB; NbExp=4; IntAct=EBI-1133508, EBI-552948;
CC -!- MISCELLANEOUS: E.coli contains genes for 3 AHAS isozymes: ilvBN, ilvGM
CC and ilvIH.
CC -!- SIMILARITY: Belongs to the acetolactate synthase small subunit family.
CC {ECO:0000305}.
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DR EMBL; X02541; CAA26388.1; -; Genomic_DNA.
DR EMBL; L10328; AAA62022.1; -; Genomic_DNA.
DR EMBL; U00096; AAC76693.1; -; Genomic_DNA.
DR EMBL; AP009048; BAE77623.1; -; Genomic_DNA.
DR EMBL; M17102; AAA24719.1; -; Genomic_DNA.
DR PIR; G65168; YCEC1S.
DR RefSeq; NP_418126.1; NC_000913.3.
DR RefSeq; WP_001181706.1; NZ_STEB01000015.1.
DR PDB; 2LVW; NMR; -; A/B=1-96.
DR PDB; 5YPP; X-ray; 1.90 A; A/B/C/D/E/F=1-96.
DR PDB; 5YPY; X-ray; 1.97 A; A/B/C/D=1-96.
DR PDB; 5YUM; X-ray; 2.43 A; A=1-96.
DR PDB; 6LPI; X-ray; 2.85 A; E/F/G/H=1-96.
DR PDBsum; 2LVW; -.
DR PDBsum; 5YPP; -.
DR PDBsum; 5YPY; -.
DR PDBsum; 5YUM; -.
DR PDBsum; 6LPI; -.
DR AlphaFoldDB; P0ADF8; -.
DR BMRB; P0ADF8; -.
DR SMR; P0ADF8; -.
DR BioGRID; 4262585; 7.
DR BioGRID; 852489; 3.
DR ComplexPortal; CPX-3573; Acetolactate synthase I complex.
DR IntAct; P0ADF8; 6.
DR STRING; 511145.b3670; -.
DR jPOST; P0ADF8; -.
DR PaxDb; P0ADF8; -.
DR PRIDE; P0ADF8; -.
DR EnsemblBacteria; AAC76693; AAC76693; b3670.
DR EnsemblBacteria; BAE77623; BAE77623; BAE77623.
DR GeneID; 66672433; -.
DR GeneID; 948183; -.
DR KEGG; ecj:JW3645; -.
DR KEGG; eco:b3670; -.
DR PATRIC; fig|1411691.4.peg.3035; -.
DR EchoBASE; EB0497; -.
DR eggNOG; COG0440; Bacteria.
DR HOGENOM; CLU_165363_0_0_6; -.
DR OMA; NEQSRIW; -.
DR PhylomeDB; P0ADF8; -.
DR BioCyc; EcoCyc:SMALLILVN-MON; -.
DR BioCyc; MetaCyc:SMALLILVN-MON; -.
DR BRENDA; 2.2.1.6; 2026.
DR UniPathway; UPA00047; UER00055.
DR UniPathway; UPA00049; UER00059.
DR PRO; PR:P0ADF8; -.
DR Proteomes; UP000000318; Chromosome.
DR Proteomes; UP000000625; Chromosome.
DR GO; GO:0005948; C:acetolactate synthase complex; IDA:EcoCyc.
DR GO; GO:0003984; F:acetolactate synthase activity; IDA:EcoCyc.
DR GO; GO:1990610; F:acetolactate synthase regulator activity; IEA:InterPro.
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; cd04878; ACT_AHAS; 1.
DR InterPro; IPR004789; Acetalactate_synth_ssu.
DR InterPro; IPR045865; ACT-like_dom_sf.
DR InterPro; IPR002912; ACT_dom.
DR InterPro; IPR039557; AHAS_ACT.
DR PANTHER; PTHR30239; PTHR30239; 1.
DR SUPFAM; SSF55021; SSF55021; 1.
DR PROSITE; PS51671; ACT; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Amino-acid biosynthesis;
KW Branched-chain amino acid biosynthesis; Reference proteome; Transferase.
FT CHAIN 1..96
FT /note="Acetolactate synthase isozyme 1 small subunit"
FT /id="PRO_0000151419"
FT DOMAIN 10..83
FT /note="ACT"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01007"
FT CONFLICT 24
FT /note="H -> D (in Ref. 1 and 2)"
FT /evidence="ECO:0000305"
FT STRAND 8..16
FT /evidence="ECO:0007829|PDB:5YPP"
FT HELIX 21..30
FT /evidence="ECO:0007829|PDB:5YPP"
FT TURN 31..33
FT /evidence="ECO:0007829|PDB:5YPP"
FT STRAND 38..43
FT /evidence="ECO:0007829|PDB:5YPP"
FT STRAND 47..57
FT /evidence="ECO:0007829|PDB:5YPP"
FT HELIX 61..71
FT /evidence="ECO:0007829|PDB:5YPP"
FT STRAND 75..81
FT /evidence="ECO:0007829|PDB:5YPP"
FT HELIX 87..95
FT /evidence="ECO:0007829|PDB:5YPP"
SQ SEQUENCE 96 AA; 11106 MW; 7F37DD421EDD3802 CRC64;
MQNTTHDNVI LELTVRNHPG VMTHVCGLFA RRAFNVEGIL CLPIQDSDKS HIWLLVNDDQ
RLEQMISQID KLEDVVKVQR NQSDPTMFNK IAVFFQ
