ID ILVB_ECOLI Reviewed; 562 AA.
AC P08142; Q2M7Y4;
DT 01-AUG-1988, integrated into UniProtKB/Swiss-Prot.
DT 01-AUG-1988, sequence version 1.
DT 27-MAR-2024, entry version 188.
DE RecName: Full=Acetolactate synthase isozyme 1 large subunit;
DE Short=AHAS-I;
DE EC=2.2.1.6;
DE AltName: Full=Acetohydroxy-acid synthase I large subunit;
DE Short=ALS-I;
GN Name=ilvB; OrderedLocusNames=b3671, JW3646;
OS Escherichia coli (strain K12).
OC Bacteria; Pseudomonadota; 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 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 -!- 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 -!- INTERACTION:
CC P08142; P0ADF8: ilvN; NbExp=4; IntAct=EBI-552948, EBI-1133508;
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}.
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DR EMBL; X02541; CAA26387.1; -; Genomic_DNA.
DR EMBL; L10328; AAA62023.1; -; Genomic_DNA.
DR EMBL; U00096; AAC76694.1; -; Genomic_DNA.
DR EMBL; AP009048; BAE77622.1; -; Genomic_DNA.
DR PIR; A93569; YCEC1L.
DR RefSeq; NP_418127.1; NC_000913.3.
DR RefSeq; WP_000168475.1; NZ_SSZK01000043.1.
DR PDB; 6LPI; X-ray; 2.85 A; A/B/C/D=1-562.
DR PDBsum; 6LPI; -.
DR AlphaFoldDB; P08142; -.
DR SMR; P08142; -.
DR BioGRID; 4262586; 11.
DR BioGRID; 852488; 3.
DR ComplexPortal; CPX-3573; Acetolactate synthase I complex.
DR DIP; DIP-10019N; -.
DR IntAct; P08142; 9.
DR STRING; 511145.b3671; -.
DR SWISS-2DPAGE; P08142; -.
DR jPOST; P08142; -.
DR PaxDb; 511145-b3671; -.
DR EnsemblBacteria; AAC76694; AAC76694; b3671.
DR GeneID; 948182; -.
DR KEGG; ecj:JW3646; -.
DR KEGG; eco:b3671; -.
DR PATRIC; fig|511145.12.peg.3793; -.
DR EchoBASE; EB0489; -.
DR eggNOG; COG0028; Bacteria.
DR HOGENOM; CLU_013748_1_2_6; -.
DR InParanoid; P08142; -.
DR OMA; WREPRSF; -.
DR OrthoDB; 9785953at2; -.
DR PhylomeDB; P08142; -.
DR BioCyc; EcoCyc:LARGEILVB-MONOMER; -.
DR BioCyc; MetaCyc:LARGEILVB-MONOMER; -.
DR BRENDA; 2.2.1.6; 2026.
DR UniPathway; UPA00047; UER00055.
DR UniPathway; UPA00049; UER00059.
DR PRO; PR:P08142; -.
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: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: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 CDD; cd07035; TPP_PYR_POX_like; 1.
DR Gene3D; 3.40.50.970; -; 2.
DR Gene3D; 3.40.50.1220; TPP-binding domain; 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_TPP-bd.
DR NCBIfam; TIGR00118; acolac_lg; 1.
DR PANTHER; PTHR18968:SF171; ACETOLACTATE SYNTHASE ISOZYME 1 LARGE SUBUNIT; 1.
DR PANTHER; PTHR18968; THIAMINE PYROPHOSPHATE ENZYMES; 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; DHS-like NAD/FAD-binding domain; 1.
DR SUPFAM; SSF52518; Thiamin diphosphate-binding fold (THDP-binding); 2.
DR PROSITE; PS00187; TPP_ENZYMES; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Amino-acid biosynthesis;
KW Branched-chain amino acid biosynthesis; FAD; Flavoprotein; Magnesium;
KW Metal-binding; Reference proteome; Thiamine pyrophosphate; Transferase.
FT CHAIN 1..562
FT /note="Acetolactate synthase isozyme 1 large subunit"
FT /id="PRO_0000090784"
FT REGION 393..473
FT /note="Thiamine pyrophosphate binding"
FT BINDING 60
FT /ligand="thiamine diphosphate"
FT /ligand_id="ChEBI:CHEBI:58937"
FT /evidence="ECO:0000250"
FT BINDING 162
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250"
FT BINDING 264..285
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250"
FT BINDING 307..326
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250"
FT BINDING 444
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
FT BINDING 471
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
FT STRAND 12..14
FT /evidence="ECO:0007829|PDB:6LPI"
FT HELIX 15..25
FT /evidence="ECO:0007829|PDB:6LPI"
FT STRAND 30..33
FT /evidence="ECO:0007829|PDB:6LPI"
FT HELIX 37..39
FT /evidence="ECO:0007829|PDB:6LPI"
FT HELIX 40..47
FT /evidence="ECO:0007829|PDB:6LPI"
FT STRAND 53..56
FT /evidence="ECO:0007829|PDB:6LPI"
FT HELIX 60..74
FT /evidence="ECO:0007829|PDB:6LPI"
FT STRAND 78..82
FT /evidence="ECO:0007829|PDB:6LPI"
FT HELIX 86..101
FT /evidence="ECO:0007829|PDB:6LPI"
FT STRAND 105..111
FT /evidence="ECO:0007829|PDB:6LPI"
FT TURN 117..120
FT /evidence="ECO:0007829|PDB:6LPI"
FT HELIX 127..131
FT /evidence="ECO:0007829|PDB:6LPI"
FT HELIX 132..134
FT /evidence="ECO:0007829|PDB:6LPI"
FT STRAND 135..140
FT /evidence="ECO:0007829|PDB:6LPI"
FT HELIX 144..146
FT /evidence="ECO:0007829|PDB:6LPI"
FT HELIX 147..159
FT /evidence="ECO:0007829|PDB:6LPI"
FT STRAND 160..162
FT /evidence="ECO:0007829|PDB:6LPI"
FT STRAND 166..171
FT /evidence="ECO:0007829|PDB:6LPI"
FT HELIX 172..175
FT /evidence="ECO:0007829|PDB:6LPI"
FT STRAND 178..180
FT /evidence="ECO:0007829|PDB:6LPI"
FT HELIX 198..210
FT /evidence="ECO:0007829|PDB:6LPI"
FT STRAND 212..218
FT /evidence="ECO:0007829|PDB:6LPI"
FT HELIX 220..222
FT /evidence="ECO:0007829|PDB:6LPI"
FT HELIX 226..235
FT /evidence="ECO:0007829|PDB:6LPI"
FT STRAND 240..242
FT /evidence="ECO:0007829|PDB:6LPI"
FT HELIX 244..246
FT /evidence="ECO:0007829|PDB:6LPI"
FT STRAND 257..260
FT /evidence="ECO:0007829|PDB:6LPI"
FT HELIX 267..273
FT /evidence="ECO:0007829|PDB:6LPI"
FT STRAND 277..283
FT /evidence="ECO:0007829|PDB:6LPI"
FT HELIX 288..291
FT /evidence="ECO:0007829|PDB:6LPI"
FT HELIX 294..296
FT /evidence="ECO:0007829|PDB:6LPI"
FT STRAND 302..308
FT /evidence="ECO:0007829|PDB:6LPI"
FT HELIX 310..312
FT /evidence="ECO:0007829|PDB:6LPI"
FT STRAND 315..317
FT /evidence="ECO:0007829|PDB:6LPI"
FT STRAND 320..325
FT /evidence="ECO:0007829|PDB:6LPI"
FT HELIX 327..334
FT /evidence="ECO:0007829|PDB:6LPI"
FT HELIX 335..337
FT /evidence="ECO:0007829|PDB:6LPI"
FT HELIX 344..354
FT /evidence="ECO:0007829|PDB:6LPI"
FT HELIX 370..378
FT /evidence="ECO:0007829|PDB:6LPI"
FT STRAND 386..389
FT /evidence="ECO:0007829|PDB:6LPI"
FT HELIX 393..401
FT /evidence="ECO:0007829|PDB:6LPI"
FT HELIX 422..432
FT /evidence="ECO:0007829|PDB:6LPI"
FT STRAND 434..436
FT /evidence="ECO:0007829|PDB:6LPI"
FT STRAND 438..443
FT /evidence="ECO:0007829|PDB:6LPI"
FT HELIX 444..447
FT /evidence="ECO:0007829|PDB:6LPI"
FT TURN 448..452
FT /evidence="ECO:0007829|PDB:6LPI"
FT HELIX 453..459
FT /evidence="ECO:0007829|PDB:6LPI"
FT STRAND 464..470
FT /evidence="ECO:0007829|PDB:6LPI"
FT HELIX 476..484
FT /evidence="ECO:0007829|PDB:6LPI"
FT HELIX 500..506
FT /evidence="ECO:0007829|PDB:6LPI"
FT STRAND 510..513
FT /evidence="ECO:0007829|PDB:6LPI"
FT HELIX 521..529
FT /evidence="ECO:0007829|PDB:6LPI"
FT STRAND 530..532
FT /evidence="ECO:0007829|PDB:6LPI"
FT STRAND 534..539
FT /evidence="ECO:0007829|PDB:6LPI"
SQ SEQUENCE 562 AA; 60441 MW; 70F8A3128031353C CRC64;
MASSGTTSTR KRFTGAEFIV HFLEQQGIKI VTGIPGGSIL PVYDALSQST QIRHILARHE
QGAGFIAQGM ARTDGKPAVC MACSGPGATN LVTAIADARL DSIPLICITG QVPASMIGTD
AFQEVDTYGI SIPITKHNYL VRHIEELPQV MSDAFRIAQS GRPGPVWIDI PKDVQTAVFE
IETQPAMAEK AAAPAFSEES IRDAAAMINA AKRPVLYLGG GVINAPARVR ELAEKAQLPT
TMTLMALGML PKAHPLSLGM LGMHGVRSTN YILQEADLLI VLGARFDDRA IGKTEQFCPN
AKIIHVDIDR AELGKIKQPH VAIQADVDDV LAQLIPLVEA QPRAEWHQLV ADLQREFPCP
IPKACDPLSH YGLINAVAAC VDDNAIITTD VGQHQMWTAQ AYPLNRPRQW LTSGGLGTMG
FGLPAAIGAA LANPDRKVLC FSGDGSLMMN IQEMATASEN QLDVKIILMN NEALGLVHQQ
QSLFYEQGVF AATYPGKINF MQIAAGFGLE TCDLNNEADP QASLQEIINR PGPALIHVRI
DAEEKVYPMV PPGAANTEMV GE
//
