ID   ILVE_MYCLE              Reviewed;         368 AA.
AC   O32954;
DT   15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT   01-JAN-1998, sequence version 1.
DT   25-MAY-2022, entry version 122.
DE   RecName: Full=Probable branched-chain-amino-acid aminotransferase;
DE            Short=BCAT;
DE            EC=2.6.1.42;
GN   Name=ilvE; OrderedLocusNames=ML0866; ORFNames=MLCB22.12c;
OS   Mycobacterium leprae (strain TN).
OC   Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC   Mycobacterium.
OX   NCBI_TaxID=272631;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=TN;
RX   PubMed=11234002; DOI=10.1038/35059006;
RA   Cole S.T., Eiglmeier K., Parkhill J., James K.D., Thomson N.R.,
RA   Wheeler P.R., Honore N., Garnier T., Churcher C.M., Harris D.E.,
RA   Mungall K.L., Basham D., Brown D., Chillingworth T., Connor R.,
RA   Davies R.M., Devlin K., Duthoy S., Feltwell T., Fraser A., Hamlin N.,
RA   Holroyd S., Hornsby T., Jagels K., Lacroix C., Maclean J., Moule S.,
RA   Murphy L.D., Oliver K., Quail M.A., Rajandream M.A., Rutherford K.M.,
RA   Rutter S., Seeger K., Simon S., Simmonds M., Skelton J., Squares R.,
RA   Squares S., Stevens K., Taylor K., Whitehead S., Woodward J.R.,
RA   Barrell B.G.;
RT   "Massive gene decay in the leprosy bacillus.";
RL   Nature 409:1007-1011(2001).
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   -!- 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   -!- SIMILARITY: Belongs to the class-IV pyridoxal-phosphate-dependent
CC       aminotransferase family. {ECO:0000305}.
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DR   EMBL; Z98741; CAB11377.1; -; Genomic_DNA.
DR   EMBL; AL583920; CAC31247.1; -; Genomic_DNA.
DR   PIR; T44887; T44887.
DR   RefSeq; NP_301654.1; NC_002677.1.
DR   RefSeq; WP_010907978.1; NC_002677.1.
DR   AlphaFoldDB; O32954; -.
DR   SMR; O32954; -.
DR   STRING; 272631.ML0866; -.
DR   EnsemblBacteria; CAC31247; CAC31247; CAC31247.
DR   KEGG; mle:ML0866; -.
DR   PATRIC; fig|272631.5.peg.1593; -.
DR   Leproma; ML0866; -.
DR   eggNOG; COG0115; Bacteria.
DR   HOGENOM; CLU_031922_0_2_11; -.
DR   OMA; LTEVFAC; -.
DR   UniPathway; UPA00047; UER00058.
DR   UniPathway; UPA00048; UER00073.
DR   UniPathway; UPA00049; UER00062.
DR   Proteomes; UP000000806; 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; IPR005786; B_amino_transII.
DR   InterPro; IPR043132; BCAT-like_C.
DR   InterPro; IPR043131; BCAT-like_N.
DR   InterPro; IPR033939; BCAT_family.
DR   PANTHER; PTHR11825; PTHR11825; 1.
DR   Pfam; PF01063; Aminotran_4; 1.
DR   PIRSF; PIRSF006468; BCAT1; 1.
DR   SUPFAM; SSF56752; SSF56752; 1.
DR   TIGRFAMs; TIGR01123; ilvE_II; 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;
KW   Reference proteome; Transferase.
FT   CHAIN           1..368
FT                   /note="Probable branched-chain-amino-acid aminotransferase"
FT                   /id="PRO_0000103273"
FT   MOD_RES         204
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   368 AA;  39715 MW;  AD466EE985F5505A CRC64;
     MTSGFLEFTV SLSAHPVTDA ERESILAEPG FGKYHTDHMV SIDYIDGRGW HDARVIPYGP
     IQLDPSAIVL HYAQEVFEGL KAYRWADGSI VSFRPDANAA RLRSSARRIA IPELPDELFI
     DSLCQLIAVD NAWVPRVGGE EALYLRPFIF ATEPGLGVRP AKQYRYLLIA SPVGAYFKGG
     INPVTVWVSM EYVRASPGGT GAAKFGGNYA ASLLAQTEAA ANGCDQVVWL DAVERRFVEE
     MGGMNIFFVL GSGGSARLVT PELSGSLLPG VTRASLLQLA IDAGFSVEER KIDIDEWQKK
     AAAGEITEVF ACGTAAFITP VSRVKYGDTE FTIAGGAPGE VTMALRDTLT GIQRGTFADT
     HGWMARLG