ALAA_ECOL6
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 03-AUG-2022, entry version 93.
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; 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: 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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AE014075; AAN81285.1; -; Genomic_DNA.
DR RefSeq; WP_000074527.1; NC_004431.1.
DR AlphaFoldDB; P0A960; -.
DR SMR; P0A960; -.
DR STRING; 199310.c2831; -.
DR PRIDE; P0A960; -.
DR EnsemblBacteria; AAN81285; AAN81285; c2831.
DR GeneID; 66673827; -.
DR KEGG; ecc:c2831; -.
DR eggNOG; COG0436; Bacteria.
DR HOGENOM; CLU_017584_4_2_6; -.
DR OMA; WRMGWII; -.
DR BioCyc; ECOL199310:C2831-MON; -.
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 Gene3D; 3.40.640.10; -; 1.
DR Gene3D; 3.90.1150.10; -; 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 Pfam; PF00155; Aminotran_1_2; 1.
DR SUPFAM; SSF53383; SSF53383; 1.
PE 3: Inferred from homology;
KW Amino-acid biosynthesis; Aminotransferase; Cytoplasm; Pyridoxal phosphate;
KW 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