ILVH_ECOLI
ID ILVH_ECOLI Reviewed; 163 AA.
AC P00894; P78046; Q47637;
DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT 19-JUL-2003, sequence version 3.
DT 03-AUG-2022, entry version 180.
DE RecName: Full=Acetolactate synthase isozyme 3 small subunit;
DE EC=2.2.1.6;
DE AltName: Full=ALS-III;
DE AltName: Full=Acetohydroxy-acid synthase III small subunit;
DE Short=AHAS-III;
GN Name=ilvH; Synonyms=brnP; OrderedLocusNames=b0078, JW0077;
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 TO
RP 132.
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] OF 130-163.
RC STRAIN=K12;
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).
RN [6]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 130-163.
RX PubMed=2198273; DOI=10.1128/jb.172.8.4696-4700.1990;
RA Leclerc G., Noel G., Drapeau G.R.;
RT "Molecular cloning, nucleotide sequence, and expression of shl, a new gene
RT in the 2-minute region of the genetic map of Escherichia coli.";
RL J. Bacteriol. 172:4696-4700(1990).
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 -!- 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 -!- SIMILARITY: Belongs to the acetolactate synthase small subunit family.
CC {ECO:0000305}.
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DR EMBL; X01609; CAA25756.1; -; Genomic_DNA.
DR EMBL; X55457; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; X55034; CAA38855.1; -; Genomic_DNA.
DR EMBL; U00096; AAC73189.1; -; Genomic_DNA.
DR EMBL; AP009048; BAB96647.2; -; Genomic_DNA.
DR EMBL; M35034; AAA24627.1; -; Genomic_DNA.
DR PIR; F64729; YCEC3H.
DR RefSeq; NP_414620.1; NC_000913.3.
DR RefSeq; WP_001300383.1; NZ_STEB01000010.1.
DR PDB; 2F1F; X-ray; 1.75 A; A/B=1-163.
DR PDBsum; 2F1F; -.
DR AlphaFoldDB; P00894; -.
DR SMR; P00894; -.
DR BioGRID; 4259381; 5.
DR BioGRID; 851597; 2.
DR ComplexPortal; CPX-3575; Acetolactate synthase III complex.
DR DIP; DIP-10024N; -.
DR IntAct; P00894; 2.
DR STRING; 511145.b0078; -.
DR SWISS-2DPAGE; P00894; -.
DR jPOST; P00894; -.
DR PaxDb; P00894; -.
DR PRIDE; P00894; -.
DR EnsemblBacteria; AAC73189; AAC73189; b0078.
DR EnsemblBacteria; BAB96647; BAB96647; BAB96647.
DR GeneID; 947267; -.
DR KEGG; ecj:JW0077; -.
DR KEGG; eco:b0078; -.
DR PATRIC; fig|1411691.4.peg.2202; -.
DR EchoBASE; EB0494; -.
DR eggNOG; COG0440; Bacteria.
DR HOGENOM; CLU_055003_1_3_6; -.
DR InParanoid; P00894; -.
DR OMA; EPYGIKE; -.
DR PhylomeDB; P00894; -.
DR BioCyc; EcoCyc:ACETOLACTSYNIII-HCHAIN-MON; -.
DR BioCyc; MetaCyc:ACETOLACTSYNIII-HCHAIN-MON; -.
DR BRENDA; 2.2.1.6; 2026.
DR UniPathway; UPA00047; UER00055.
DR UniPathway; UPA00049; UER00059.
DR EvolutionaryTrace; P00894; -.
DR PRO; PR:P00894; -.
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: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 Gene3D; 3.30.70.1150; -; 1.
DR InterPro; IPR004789; Acetalactate_synth_ssu.
DR InterPro; IPR027271; Acetolactate_synth/TF_NikR_C.
DR InterPro; IPR019455; Acetolactate_synth_ssu_C.
DR InterPro; IPR045865; ACT-like_dom_sf.
DR InterPro; IPR002912; ACT_dom.
DR InterPro; IPR039557; AHAS_ACT.
DR PANTHER; PTHR30239; PTHR30239; 1.
DR Pfam; PF01842; ACT; 1.
DR Pfam; PF10369; ALS_ss_C; 1.
DR SUPFAM; SSF55021; SSF55021; 2.
DR TIGRFAMs; TIGR00119; acolac_sm; 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..163
FT /note="Acetolactate synthase isozyme 3 small subunit"
FT /id="PRO_0000151410"
FT DOMAIN 4..78
FT /note="ACT"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01007"
FT CONFLICT 132
FT /note="D -> S (in Ref. 1, 2 and 5)"
FT /evidence="ECO:0000305"
FT CONFLICT 159..163
FT /note="DKIMR -> VK (in Ref. 1; CAA25756)"
FT /evidence="ECO:0000305"
FT STRAND 2..10
FT /evidence="ECO:0007829|PDB:2F1F"
FT HELIX 15..24
FT /evidence="ECO:0007829|PDB:2F1F"
FT TURN 25..27
FT /evidence="ECO:0007829|PDB:2F1F"
FT STRAND 31..37
FT /evidence="ECO:0007829|PDB:2F1F"
FT STRAND 41..52
FT /evidence="ECO:0007829|PDB:2F1F"
FT HELIX 54..66
FT /evidence="ECO:0007829|PDB:2F1F"
FT STRAND 70..75
FT /evidence="ECO:0007829|PDB:2F1F"
FT HELIX 76..78
FT /evidence="ECO:0007829|PDB:2F1F"
FT STRAND 81..92
FT /evidence="ECO:0007829|PDB:2F1F"
FT HELIX 96..107
FT /evidence="ECO:0007829|PDB:2F1F"
FT STRAND 111..115
FT /evidence="ECO:0007829|PDB:2F1F"
FT STRAND 117..126
FT /evidence="ECO:0007829|PDB:2F1F"
FT HELIX 128..138
FT /evidence="ECO:0007829|PDB:2F1F"
FT TURN 139..141
FT /evidence="ECO:0007829|PDB:2F1F"
FT STRAND 142..149
FT /evidence="ECO:0007829|PDB:2F1F"
FT STRAND 153..157
FT /evidence="ECO:0007829|PDB:2F1F"
SQ SEQUENCE 163 AA; 17977 MW; D6E28AE94A55606E CRC64;
MRRILSVLLE NESGALSRVI GLFSQRGYNI ESLTVAPTDD PTLSRMTIQT VGDEKVLEQI
EKQLHKLVDV LRVSELGQGA HVEREIMLVK IQASGYGRDE VKRNTEIFRG QIIDVTPSLY
TVQLAGTSGK LDAFLASIRD VAKIVEVARS GVVGLSRGDK IMR
