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   27-MAR-2024, entry version 139.
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; Pseudomonadota; 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   jPOST; P0AB80; -.
DR   PaxDb; 511145-b3770; -.
DR   EnsemblBacteria; AAT48207; AAT48207; b3770.
DR   GeneID; 75204761; -.
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   OrthoDB; 21319at2; -.
DR   PhylomeDB; P0AB80; -.
DR   BioCyc; EcoCyc:BRANCHED-CHAINAMINOTRANSFER-MONOMER; -.
DR   BioCyc; MetaCyc:BRANCHED-CHAINAMINOTRANSFER-MONOMER; -.
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: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; 3.30.470.10; -; 1.
DR   Gene3D; 3.20.10.10; D-amino Acid Aminotransferase, subunit A, domain 2; 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   NCBIfam; TIGR01122; ilvE_I; 1.
DR   PANTHER; PTHR42743; AMINO-ACID AMINOTRANSFERASE; 1.
DR   PANTHER; PTHR42743:SF20; BRANCHED-CHAIN-AMINO-ACID AMINOTRANSFERASE-LIKE PROTEIN 2; 1.
DR   Pfam; PF01063; Aminotran_4; 1.
DR   SUPFAM; SSF56752; D-aminoacid aminotransferase-like PLP-dependent enzymes; 1.
DR   PROSITE; PS00770; AA_TRANSFER_CLASS_4; 1.
DR   SWISS-2DPAGE; P0AB80; -.
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
//