ID   ALAA_ECOL6              Reviewed;         405 AA.
AC   P0A960; P77727;
DT   19-JUL-2005, integrated into UniProtKB/Swiss-Prot.
DT   19-JUL-2005, sequence version 1.
DT   27-MAR-2024, entry version 101.
DE   RecName: Full=Glutamate-pyruvate aminotransferase AlaA;
DE            EC=2.6.1.2 {ECO:0000250|UniProtKB:P0A959};
GN   Name=alaA; Synonyms=yfbQ; OrderedLocusNames=c2831;
OS   Escherichia coli O6:H1 (strain CFT073 / ATCC 700928 / UPEC).
OC   Bacteria; Pseudomonadota; 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: Involved in the biosynthesis of alanine. Catalyzes the
CC       transamination of pyruvate by glutamate, leading to the formation of L-
CC       alanine and 2-oxoglutarate. Is also able to catalyze the reverse
CC       reaction. {ECO:0000250|UniProtKB:P0A959}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=2-oxoglutarate + L-alanine = L-glutamate + pyruvate;
CC         Xref=Rhea:RHEA:19453, ChEBI:CHEBI:15361, ChEBI:CHEBI:16810,
CC         ChEBI:CHEBI:29985, ChEBI:CHEBI:57972; EC=2.6.1.2;
CC         Evidence={ECO:0000250|UniProtKB:P0A959};
CC       PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:19455;
CC         Evidence={ECO:0000250|UniProtKB:P0A959};
CC   -!- COFACTOR:
CC       Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC         Evidence={ECO:0000250|UniProtKB:P0A959};
CC   -!- PATHWAY: Amino-acid biosynthesis; L-alanine biosynthesis.
CC       {ECO:0000250|UniProtKB:P0A959}.
CC   -!- SUBUNIT: Homodimer. {ECO:0000250|UniProtKB:P0A959}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the class-I pyridoxal-phosphate-dependent
CC       aminotransferase family. {ECO:0000305}.
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DR   EMBL; AE014075; AAN81285.1; -; Genomic_DNA.
DR   RefSeq; WP_000074527.1; NZ_CP051263.1.
DR   AlphaFoldDB; P0A960; -.
DR   SMR; P0A960; -.
DR   STRING; 199310.c2831; -.
DR   GeneID; 75205664; -.
DR   KEGG; ecc:c2831; -.
DR   eggNOG; COG0436; Bacteria.
DR   HOGENOM; CLU_017584_4_2_6; -.
DR   BioCyc; ECOL199310:C2831-MONOMER; -.
DR   UniPathway; UPA00133; -.
DR   Proteomes; UP000001410; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0004021; F:L-alanine:2-oxoglutarate aminotransferase activity; IEA:UniProtKB-EC.
DR   GO; GO:0030170; F:pyridoxal phosphate binding; IEA:InterPro.
DR   GO; GO:0030632; P:D-alanine biosynthetic process; ISS:UniProtKB.
DR   CDD; cd00609; AAT_like; 1.
DR   Gene3D; 3.90.1150.10; Aspartate Aminotransferase, domain 1; 1.
DR   Gene3D; 3.40.640.10; Type I PLP-dependent aspartate aminotransferase-like (Major domain); 1.
DR   InterPro; IPR004839; Aminotransferase_I/II.
DR   InterPro; IPR015424; PyrdxlP-dep_Trfase.
DR   InterPro; IPR015421; PyrdxlP-dep_Trfase_major.
DR   InterPro; IPR015422; PyrdxlP-dep_Trfase_small.
DR   PANTHER; PTHR43488; GLUTAMATE-PYRUVATE AMINOTRANSFERASE ALAA; 1.
DR   PANTHER; PTHR43488:SF2; GLUTAMATE-PYRUVATE AMINOTRANSFERASE ALAA; 1.
DR   Pfam; PF00155; Aminotran_1_2; 1.
DR   SUPFAM; SSF53383; PLP-dependent transferases; 1.
PE   3: Inferred from homology;
KW   Amino-acid biosynthesis; Aminotransferase; Cytoplasm; Pyridoxal phosphate;
KW   Reference proteome; Transferase.
FT   CHAIN           1..405
FT                   /note="Glutamate-pyruvate aminotransferase AlaA"
FT                   /id="PRO_0000123867"
FT   BINDING         41
FT                   /ligand="L-alanine"
FT                   /ligand_id="ChEBI:CHEBI:57972"
FT                   /evidence="ECO:0000250|UniProtKB:P0A959"
FT   BINDING         179
FT                   /ligand="L-alanine"
FT                   /ligand_id="ChEBI:CHEBI:57972"
FT                   /evidence="ECO:0000250|UniProtKB:P0A959"
FT   BINDING         378
FT                   /ligand="L-alanine"
FT                   /ligand_id="ChEBI:CHEBI:57972"
FT                   /evidence="ECO:0000250|UniProtKB:P0A959"
FT   MOD_RES         240
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000250|UniProtKB:P0A959"
SQ   SEQUENCE   405 AA;  45517 MW;  6A5E78876CC3C388 CRC64;
     MSPIEKSSKL ENVCYDIRGP VLKEAKRLEE EGNKVLKLNI GNPAPFGFDA PDEILVDVIR
     NLPTAQGYCD SKGLYSARKA IMQHYQARGM RDVTVEDIYI GNGVSELIVQ AMQALLNSGD
     EMLVPAPDYP LWTAAVSLSS GKAVHYLCDE SSDWFPDLDD IRAKITPRTR GIVIINPNNP
     TGAVYSKELL MEIVEIARQH NLIIFADEIY DKILYDDAEH HSIAPLAPDL LTITFNGLSK
     TYRVAGFRQG WMVLNGPKKH AKGYIEGLEM LASMRLCANV PAQHAIQTAL GGYQSISEFI
     TPGGRLYEQR NRAWELINDI PGVSCVKPRG ALYMFPKIDA KRFNIHDDQK MVLDFLLQEK
     VLLVQGTAFN WPWPDHFRIV TLPRVDDIEL SLSKFARFLS GYHQL
//