ILVE_ECOLI
ID ILVE_ECOLI Reviewed; 309 AA.
AC P0AB80; P00510; Q2M879; Q47299;
DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 2.
DT 03-AUG-2022, entry version 132.
DE RecName: Full=Branched-chain-amino-acid aminotransferase;
DE Short=BCAT;
DE EC=2.6.1.42;
DE AltName: Full=Transaminase B;
GN Name=ilvE; OrderedLocusNames=b3770, JW5606;
OS Escherichia coli (strain K12).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=83333;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=K12;
RX PubMed=3897211; DOI=10.1093/oxfordjournals.jbchem.a135176;
RA Kuramitsu S., Ogawa T., Ogawa H., Kagamiyama H.;
RT "Branched-chain amino acid aminotransferase of Escherichia coli: nucleotide
RT sequence of the ilvE gene and the deduced amino acid sequence.";
RL J. Biochem. 97:993-999(1985).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=K12;
RX PubMed=3550695; DOI=10.1093/nar/15.5.2137;
RA Lawther R.P., Wek R.C., Lopes J.M., Pereira R., Taillon B.E.,
RA Hatfield G.W.;
RT "The complete nucleotide sequence of the ilvGMEDA operon of Escherichia
RT coli K-12.";
RL Nucleic Acids Res. 15:2137-2155(1987).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=1379743; DOI=10.1126/science.1379743;
RA Daniels D.L., Plunkett G. III, Burland V.D., Blattner F.R.;
RT "Analysis of the Escherichia coli genome: DNA sequence of the region from
RT 84.5 to 86.5 minutes.";
RL Science 257:771-778(1992).
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 SEQUENCE REVISION TO 151.
RX PubMed=16397293; DOI=10.1093/nar/gkj405;
RA Riley M., Abe T., Arnaud M.B., Berlyn M.K.B., Blattner F.R.,
RA Chaudhuri R.R., Glasner J.D., Horiuchi T., Keseler I.M., Kosuge T.,
RA Mori H., Perna N.T., Plunkett G. III, Rudd K.E., Serres M.H., Thomas G.H.,
RA Thomson N.R., Wishart D., Wanner B.L.;
RT "Escherichia coli K-12: a cooperatively developed annotation snapshot
RT -- 2005.";
RL Nucleic Acids Res. 34:1-9(2006).
RN [6]
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 [7]
RP PRELIMINARY NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-81.
RC STRAIN=K12;
RX PubMed=392469; DOI=10.1093/nar/7.8.2289;
RA Lawther R.P., Nichols B.P., Zurawski G., Hatfield G.W.;
RT "The nucleotide sequence preceding and including the beginning of the ilvE
RT gene of the ilvGEDA operon of Escherichia coli K12.";
RL Nucleic Acids Res. 7:2289-2301(1979).
RN [8]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-34.
RX PubMed=1569580; DOI=10.1016/0022-2836(92)90460-2;
RA Pagel J.M., Winkelman J.W., Adams C.W., Hatfield G.W.;
RT "DNA topology-mediated regulation of transcription initiation from the
RT tandem promoters of the ilvGMEDA operon of Escherichia coli.";
RL J. Mol. Biol. 224:919-935(1992).
RN [9]
RP PYRIDOXAL PHOSPHATE AT LYS-160.
RX PubMed=3069843; DOI=10.1093/oxfordjournals.jbchem.a122549;
RA Inoue K., Kuramitsu S., Aki K., Watanabe Y., Takagi T., Nishigai M.,
RA Ikaiu A., Kagamiyama H.;
RT "Branched-chain amino acid aminotransferase of Escherichia coli:
RT overproduction and properties.";
RL J. Biochem. 104:777-784(1988).
RN [10]
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).
RN [11]
RP X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS).
RX PubMed=9163511; DOI=10.1093/oxfordjournals.jbchem.a021633;
RA Okada K., Hirotsu K., Sato M., Hyashi H., Kagamiyama H.;
RT "Three-dimensional structure of Escherichia coli branched-chain amino acid
RT aminotransferase at 2.5-A resolution.";
RL J. Biochem. 121:637-641(1997).
CC -!- FUNCTION: Acts on leucine, isoleucine and valine.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=2-oxoglutarate + L-leucine = 4-methyl-2-oxopentanoate + L-
CC glutamate; Xref=Rhea:RHEA:18321, ChEBI:CHEBI:16810,
CC ChEBI:CHEBI:17865, ChEBI:CHEBI:29985, ChEBI:CHEBI:57427; EC=2.6.1.42;
CC -!- CATALYTIC ACTIVITY:
CC Reaction=2-oxoglutarate + L-isoleucine = (S)-3-methyl-2-oxopentanoate +
CC L-glutamate; Xref=Rhea:RHEA:24801, ChEBI:CHEBI:16810,
CC ChEBI:CHEBI:29985, ChEBI:CHEBI:35146, ChEBI:CHEBI:58045; EC=2.6.1.42;
CC -!- CATALYTIC ACTIVITY:
CC Reaction=2-oxoglutarate + L-valine = 3-methyl-2-oxobutanoate + L-
CC glutamate; Xref=Rhea:RHEA:24813, ChEBI:CHEBI:11851,
CC ChEBI:CHEBI:16810, ChEBI:CHEBI:29985, ChEBI:CHEBI:57762; EC=2.6.1.42;
CC -!- COFACTOR:
CC Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC -!- PATHWAY: Amino-acid biosynthesis; L-isoleucine biosynthesis; L-
CC isoleucine from 2-oxobutanoate: step 4/4.
CC -!- PATHWAY: Amino-acid biosynthesis; L-leucine biosynthesis; L-leucine
CC from 3-methyl-2-oxobutanoate: step 4/4.
CC -!- PATHWAY: Amino-acid biosynthesis; L-valine biosynthesis; L-valine from
CC pyruvate: step 4/4.
CC -!- SUBUNIT: Homohexamer.
CC -!- SIMILARITY: Belongs to the class-IV pyridoxal-phosphate-dependent
CC aminotransferase family. {ECO:0000305}.
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DR EMBL; X02413; CAA26262.1; -; Genomic_DNA.
DR EMBL; M32253; AAA24022.1; -; Genomic_DNA.
DR EMBL; M10313; AAB59052.1; -; Genomic_DNA.
DR EMBL; X04890; CAA28575.1; -; Genomic_DNA.
DR EMBL; M87049; AAA67573.1; -; Genomic_DNA.
DR EMBL; U00096; AAT48207.1; -; Genomic_DNA.
DR EMBL; AP009048; BAE77527.1; -; Genomic_DNA.
DR EMBL; V00290; CAA23559.1; -; Genomic_DNA.
DR PIR; E65180; XNECV.
DR RefSeq; WP_000208520.1; NZ_STEB01000021.1.
DR RefSeq; YP_026247.1; NC_000913.3.
DR PDB; 1A3G; X-ray; 2.50 A; A/B/C=2-309.
DR PDB; 1I1K; X-ray; 2.10 A; A/B/C=1-309.
DR PDB; 1I1L; X-ray; 2.40 A; A/B/C=1-309.
DR PDB; 1I1M; X-ray; 2.40 A; A/B/C=1-309.
DR PDB; 1IYD; X-ray; 2.15 A; A/B/C=1-309.
DR PDB; 1IYE; X-ray; 1.82 A; A/B/C=1-309.
DR PDBsum; 1A3G; -.
DR PDBsum; 1I1K; -.
DR PDBsum; 1I1L; -.
DR PDBsum; 1I1M; -.
DR PDBsum; 1IYD; -.
DR PDBsum; 1IYE; -.
DR AlphaFoldDB; P0AB80; -.
DR SMR; P0AB80; -.
DR BioGRID; 4261272; 73.
DR DIP; DIP-10022N; -.
DR STRING; 511145.b3770; -.
DR DrugBank; DB04063; alpha-Methylleucine.
DR DrugBank; DB03553; Glutaric Acid.
DR DrugBank; DB03993; Isocaproic acid.
DR DrugBank; DB01813; Pyridoxyl-Glutamic Acid-5'-Monophosphate.
DR SWISS-2DPAGE; P0AB80; -.
DR jPOST; P0AB80; -.
DR PaxDb; P0AB80; -.
DR PRIDE; P0AB80; -.
DR EnsemblBacteria; AAT48207; AAT48207; b3770.
DR EnsemblBacteria; BAE77527; BAE77527; BAE77527.
DR GeneID; 60902519; -.
DR GeneID; 948278; -.
DR KEGG; ecj:JW5606; -.
DR KEGG; eco:b3770; -.
DR PATRIC; fig|511145.12.peg.3887; -.
DR EchoBASE; EB0492; -.
DR eggNOG; COG0115; Bacteria.
DR HOGENOM; CLU_020844_3_1_6; -.
DR InParanoid; P0AB80; -.
DR OMA; LTEVFAC; -.
DR PhylomeDB; P0AB80; -.
DR BioCyc; EcoCyc:BRANCHED-CHAINAMINOTRANSFER-MON; -.
DR BioCyc; MetaCyc:BRANCHED-CHAINAMINOTRANSFER-MON; -.
DR BRENDA; 2.6.1.42; 2026.
DR UniPathway; UPA00047; UER00058.
DR UniPathway; UPA00048; UER00073.
DR UniPathway; UPA00049; UER00062.
DR EvolutionaryTrace; P0AB80; -.
DR PRO; PR:P0AB80; -.
DR Proteomes; UP000000318; Chromosome.
DR Proteomes; UP000000625; Chromosome.
DR GO; GO:0005829; C:cytosol; IDA:EcoCyc.
DR GO; GO:0004084; F:branched-chain-amino-acid transaminase activity; IDA:EcoCyc.
DR GO; GO:0042802; F:identical protein binding; IDA:EcoCyc.
DR GO; GO:0052656; F:L-isoleucine transaminase activity; IEA:UniProtKB-EC.
DR GO; GO:0052654; F:L-leucine transaminase activity; IEA:UniProtKB-EC.
DR GO; GO:0050048; F:L-leucine:2-oxoglutarate aminotransferase activity; IEA:RHEA.
DR GO; GO:0052655; F:L-valine transaminase activity; IEA:UniProtKB-EC.
DR GO; GO:0006532; P:aspartate biosynthetic process; IGI:EcoliWiki.
DR GO; GO:0019752; P:carboxylic acid metabolic process; IBA:GO_Central.
DR GO; GO:0009097; P:isoleucine biosynthetic process; IEA:UniProtKB-UniPathway.
DR GO; GO:0009098; P:leucine biosynthetic process; IDA:EcoCyc.
DR GO; GO:0009099; P:valine biosynthetic process; IDA:EcoCyc.
DR CDD; cd01557; BCAT_beta_family; 1.
DR Gene3D; 3.20.10.10; -; 1.
DR Gene3D; 3.30.470.10; -; 1.
DR InterPro; IPR001544; Aminotrans_IV.
DR InterPro; IPR018300; Aminotrans_IV_CS.
DR InterPro; IPR036038; Aminotransferase-like.
DR InterPro; IPR005785; B_amino_transI.
DR InterPro; IPR043132; BCAT-like_C.
DR InterPro; IPR043131; BCAT-like_N.
DR InterPro; IPR033939; BCAT_family.
DR Pfam; PF01063; Aminotran_4; 1.
DR SUPFAM; SSF56752; SSF56752; 1.
DR TIGRFAMs; TIGR01122; ilvE_I; 1.
DR PROSITE; PS00770; AA_TRANSFER_CLASS_4; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Amino-acid biosynthesis; Aminotransferase;
KW Branched-chain amino acid biosynthesis; Pyridoxal phosphate;
KW Reference proteome; Transferase.
FT INIT_MET 1
FT /note="Removed"
FT CHAIN 2..309
FT /note="Branched-chain-amino-acid aminotransferase"
FT /id="PRO_0000103262"
FT MOD_RES 160
FT /note="N6-(pyridoxal phosphate)lysine"
FT CONFLICT 151
FT /note="A -> R (in Ref. 3; AAA67573)"
FT /evidence="ECO:0000305"
FT STRAND 7..11
FT /evidence="ECO:0007829|PDB:1IYE"
FT STRAND 14..17
FT /evidence="ECO:0007829|PDB:1IYE"
FT HELIX 18..20
FT /evidence="ECO:0007829|PDB:1IYE"
FT HELIX 28..32
FT /evidence="ECO:0007829|PDB:1IYE"
FT STRAND 35..37
FT /evidence="ECO:0007829|PDB:1IYE"
FT STRAND 40..43
FT /evidence="ECO:0007829|PDB:1IYE"
FT STRAND 48..52
FT /evidence="ECO:0007829|PDB:1IYE"
FT HELIX 54..68
FT /evidence="ECO:0007829|PDB:1IYE"
FT HELIX 76..89
FT /evidence="ECO:0007829|PDB:1IYE"
FT STRAND 93..103
FT /evidence="ECO:0007829|PDB:1IYE"
FT STRAND 108..111
FT /evidence="ECO:0007829|PDB:1IYE"
FT STRAND 118..125
FT /evidence="ECO:0007829|PDB:1IYE"
FT HELIX 135..138
FT /evidence="ECO:0007829|PDB:1IYE"
FT STRAND 140..144
FT /evidence="ECO:0007829|PDB:1IYE"
FT TURN 152..154
FT /evidence="ECO:0007829|PDB:1IYE"
FT STRAND 157..159
FT /evidence="ECO:0007829|PDB:1I1L"
FT HELIX 162..164
FT /evidence="ECO:0007829|PDB:1IYE"
FT HELIX 165..177
FT /evidence="ECO:0007829|PDB:1IYE"
FT STRAND 181..186
FT /evidence="ECO:0007829|PDB:1IYE"
FT STRAND 190..195
FT /evidence="ECO:0007829|PDB:1IYE"
FT STRAND 198..204
FT /evidence="ECO:0007829|PDB:1IYE"
FT STRAND 207..210
FT /evidence="ECO:0007829|PDB:1IYE"
FT HELIX 213..215
FT /evidence="ECO:0007829|PDB:1IYE"
FT HELIX 221..232
FT /evidence="ECO:0007829|PDB:1IYE"
FT STRAND 237..239
FT /evidence="ECO:0007829|PDB:1IYE"
FT HELIX 246..249
FT /evidence="ECO:0007829|PDB:1IYE"
FT STRAND 251..257
FT /evidence="ECO:0007829|PDB:1IYE"
FT TURN 258..260
FT /evidence="ECO:0007829|PDB:1IYE"
FT STRAND 261..268
FT /evidence="ECO:0007829|PDB:1IYE"
FT HELIX 274..276
FT /evidence="ECO:0007829|PDB:1I1K"
FT HELIX 280..290
FT /evidence="ECO:0007829|PDB:1IYE"
FT TURN 291..294
FT /evidence="ECO:0007829|PDB:1IYE"
FT STRAND 295..297
FT /evidence="ECO:0007829|PDB:1IYE"
FT STRAND 304..306
FT /evidence="ECO:0007829|PDB:1IYE"
SQ SEQUENCE 309 AA; 34094 MW; E8A2B953168CD09D CRC64;
MTTKKADYIW FNGEMVRWED AKVHVMSHAL HYGTSVFEGI RCYDSHKGPV VFRHREHMQR
LHDSAKIYRF PVSQSIDELM EACRDVIRKN NLTSAYIRPL IFVGDVGMGV NPPAGYSTDV
IIAAFPWGAY LGAEALEQGI DAMVSSWNRA APNTIPTAAK AGGNYLSSLL VGSEARRHGY
QEGIALDVNG YISEGAGENL FEVKDGVLFT PPFTSSALPG ITRDAIIKLA KELGIEVREQ
VLSRESLYLA DEVFMSGTAA EITPVRSVDG IQVGEGRCGP VTKRIQQAFF GLFTGETEDK
WGWLDQVNQ
