ID   ILVE_ECOL6              Reviewed;         309 AA.
AC   P0AB81; P00510; Q47299;
DT   21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 2.
DT   03-AUG-2022, entry version 86.
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=c4692;
OS   Escherichia coli O6:H1 (strain CFT073 / ATCC 700928 / UPEC).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=199310;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CFT073 / ATCC 700928 / UPEC;
RX   PubMed=12471157; DOI=10.1073/pnas.252529799;
RA   Welch R.A., Burland V., Plunkett G. III, Redford P., Roesch P., Rasko D.,
RA   Buckles E.L., Liou S.-R., Boutin A., Hackett J., Stroud D., Mayhew G.F.,
RA   Rose D.J., Zhou S., Schwartz D.C., Perna N.T., Mobley H.L.T.,
RA   Donnenberg M.S., Blattner F.R.;
RT   "Extensive mosaic structure revealed by the complete genome sequence of
RT   uropathogenic Escherichia coli.";
RL   Proc. Natl. Acad. Sci. U.S.A. 99:17020-17024(2002).
CC   -!- FUNCTION: Acts on leucine, isoleucine and valine. {ECO:0000250}.
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         Evidence={ECO:0000250};
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. {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the class-IV pyridoxal-phosphate-dependent
CC       aminotransferase family. {ECO:0000305}.
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DR   EMBL; AE014075; AAN83124.1; -; Genomic_DNA.
DR   RefSeq; WP_000208520.1; NC_004431.1.
DR   AlphaFoldDB; P0AB81; -.
DR   SMR; P0AB81; -.
DR   STRING; 199310.c4692; -.
DR   EnsemblBacteria; AAN83124; AAN83124; c4692.
DR   GeneID; 60902519; -.
DR   KEGG; ecc:c4692; -.
DR   eggNOG; COG0115; Bacteria.
DR   HOGENOM; CLU_020844_3_1_6; -.
DR   OMA; LTEVFAC; -.
DR   BioCyc; ECOL199310:C4692-MON; -.
DR   UniPathway; UPA00047; UER00058.
DR   UniPathway; UPA00048; UER00073.
DR   UniPathway; UPA00049; UER00062.
DR   Proteomes; UP000001410; Chromosome.
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:0009097; P:isoleucine biosynthetic process; IEA:UniProtKB-UniPathway.
DR   GO; GO:0009098; P:leucine biosynthetic process; IEA:UniProtKB-UniPathway.
DR   GO; GO:0009099; P:valine biosynthetic process; IEA:UniProtKB-UniPathway.
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   3: Inferred from homology;
KW   Amino-acid biosynthesis; Aminotransferase;
KW   Branched-chain amino acid biosynthesis; Pyridoxal phosphate; Transferase.
FT   INIT_MET        1
FT                   /note="Removed"
FT                   /evidence="ECO:0000250"
FT   CHAIN           2..309
FT                   /note="Branched-chain-amino-acid aminotransferase"
FT                   /id="PRO_0000103264"
FT   MOD_RES         160
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000250"
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