ALAA_SHIFL
ID ALAA_SHIFL Reviewed; 405 AA.
AC P0A961; P77727;
DT 19-JUL-2005, integrated into UniProtKB/Swiss-Prot.
DT 19-JUL-2005, sequence version 1.
DT 03-AUG-2022, entry version 109.
DE RecName: Full=Glutamate-pyruvate aminotransferase AlaA;
DE EC=2.6.1.2 {ECO:0000250|UniProtKB:P0A959};
GN Name=alaA; Synonyms=yfbQ; OrderedLocusNames=SF2366, S2501;
OS Shigella flexneri.
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Shigella.
OX NCBI_TaxID=623;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=301 / Serotype 2a;
RX PubMed=12384590; DOI=10.1093/nar/gkf566;
RA Jin Q., Yuan Z., Xu J., Wang Y., Shen Y., Lu W., Wang J., Liu H., Yang J.,
RA Yang F., Zhang X., Zhang J., Yang G., Wu H., Qu D., Dong J., Sun L.,
RA Xue Y., Zhao A., Gao Y., Zhu J., Kan B., Ding K., Chen S., Cheng H.,
RA Yao Z., He B., Chen R., Ma D., Qiang B., Wen Y., Hou Y., Yu J.;
RT "Genome sequence of Shigella flexneri 2a: insights into pathogenicity
RT through comparison with genomes of Escherichia coli K12 and O157.";
RL Nucleic Acids Res. 30:4432-4441(2002).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700930 / 2457T / Serotype 2a;
RX PubMed=12704152; DOI=10.1128/iai.71.5.2775-2786.2003;
RA Wei J., Goldberg M.B., Burland V., Venkatesan M.M., Deng W., Fournier G.,
RA Mayhew G.F., Plunkett G. III, Rose D.J., Darling A., Mau B., Perna N.T.,
RA Payne S.M., Runyen-Janecky L.J., Zhou S., Schwartz D.C., Blattner F.R.;
RT "Complete genome sequence and comparative genomics of Shigella flexneri
RT serotype 2a strain 2457T.";
RL Infect. Immun. 71:2775-2786(2003).
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; AE005674; AAN43879.1; -; Genomic_DNA.
DR EMBL; AE014073; AAP17697.1; -; Genomic_DNA.
DR RefSeq; NP_708172.1; NC_004337.2.
DR RefSeq; WP_000074527.1; NZ_WPGW01000016.1.
DR AlphaFoldDB; P0A961; -.
DR SMR; P0A961; -.
DR STRING; 198214.SF2366; -.
DR EnsemblBacteria; AAN43879; AAN43879; SF2366.
DR EnsemblBacteria; AAP17697; AAP17697; S2501.
DR GeneID; 1027308; -.
DR GeneID; 66673827; -.
DR KEGG; sfl:SF2366; -.
DR KEGG; sfx:S2501; -.
DR PATRIC; fig|198214.7.peg.2832; -.
DR HOGENOM; CLU_017584_4_2_6; -.
DR OMA; WRMGWII; -.
DR OrthoDB; 554560at2; -.
DR UniPathway; UPA00133; -.
DR Proteomes; UP000001006; Chromosome.
DR Proteomes; UP000002673; 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 Reference proteome; Transferase.
FT CHAIN 1..405
FT /note="Glutamate-pyruvate aminotransferase AlaA"
FT /id="PRO_0000123868"
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
