ID   AAT_SALTI               Reviewed;         396 AA.
AC   Q56114;
DT   01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT   05-DEC-2001, sequence version 2.
DT   03-AUG-2022, entry version 140.
DE   RecName: Full=Aspartate aminotransferase;
DE            Short=AspAT;
DE            EC=2.6.1.1;
DE   AltName: Full=Transaminase A;
GN   Name=aspC; OrderedLocusNames=STY1000, t1936;
OS   Salmonella typhi.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Salmonella.
OX   NCBI_TaxID=90370;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CT18;
RX   PubMed=11677608; DOI=10.1038/35101607;
RA   Parkhill J., Dougan G., James K.D., Thomson N.R., Pickard D., Wain J.,
RA   Churcher C.M., Mungall K.L., Bentley S.D., Holden M.T.G., Sebaihia M.,
RA   Baker S., Basham D., Brooks K., Chillingworth T., Connerton P., Cronin A.,
RA   Davis P., Davies R.M., Dowd L., White N., Farrar J., Feltwell T.,
RA   Hamlin N., Haque A., Hien T.T., Holroyd S., Jagels K., Krogh A.,
RA   Larsen T.S., Leather S., Moule S., O'Gaora P., Parry C., Quail M.A.,
RA   Rutherford K.M., Simmonds M., Skelton J., Stevens K., Whitehead S.,
RA   Barrell B.G.;
RT   "Complete genome sequence of a multiple drug resistant Salmonella enterica
RT   serovar Typhi CT18.";
RL   Nature 413:848-852(2001).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 700931 / Ty2;
RX   PubMed=12644504; DOI=10.1128/jb.185.7.2330-2337.2003;
RA   Deng W., Liou S.-R., Plunkett G. III, Mayhew G.F., Rose D.J., Burland V.,
RA   Kodoyianni V., Schwartz D.C., Blattner F.R.;
RT   "Comparative genomics of Salmonella enterica serovar Typhi strains Ty2 and
RT   CT18.";
RL   J. Bacteriol. 185:2330-2337(2003).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-74.
RC   STRAIN=IMSS-1;
RA   Fernandez-Mora M., Calva E.;
RL   Submitted (JUN-1996) to the EMBL/GenBank/DDBJ databases.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=2-oxoglutarate + L-aspartate = L-glutamate + oxaloacetate;
CC         Xref=Rhea:RHEA:21824, ChEBI:CHEBI:16452, ChEBI:CHEBI:16810,
CC         ChEBI:CHEBI:29985, ChEBI:CHEBI:29991; EC=2.6.1.1;
CC   -!- COFACTOR:
CC       Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC         Evidence={ECO:0000250};
CC   -!- SUBUNIT: Homodimer. {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm.
CC   -!- SIMILARITY: Belongs to the class-I pyridoxal-phosphate-dependent
CC       aminotransferase family. {ECO:0000305}.
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DR   EMBL; AL513382; CAD05398.1; -; Genomic_DNA.
DR   EMBL; AE014613; AAO69551.1; -; Genomic_DNA.
DR   EMBL; X89757; CAA61906.1; -; Genomic_DNA.
DR   RefSeq; NP_455484.1; NC_003198.1.
DR   RefSeq; WP_000462648.1; NZ_WSUR01000013.1.
DR   AlphaFoldDB; Q56114; -.
DR   SMR; Q56114; -.
DR   STRING; 220341.16502160; -.
DR   EnsemblBacteria; AAO69551; AAO69551; t1936.
DR   KEGG; stt:t1936; -.
DR   KEGG; sty:STY1000; -.
DR   PATRIC; fig|220341.7.peg.1008; -.
DR   eggNOG; COG1448; Bacteria.
DR   HOGENOM; CLU_032440_1_2_6; -.
DR   OMA; VGACTIV; -.
DR   Proteomes; UP000000541; Chromosome.
DR   Proteomes; UP000002670; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0004069; F:L-aspartate:2-oxoglutarate aminotransferase activity; IEA:UniProtKB-EC.
DR   GO; GO:0030170; F:pyridoxal phosphate binding; IEA:InterPro.
DR   GO; GO:1901605; P:alpha-amino acid metabolic process; IEA:UniProt.
DR   GO; GO:0009058; P:biosynthetic process; IEA:InterPro.
DR   Gene3D; 3.40.640.10; -; 1.
DR   Gene3D; 3.90.1150.10; -; 1.
DR   InterPro; IPR004839; Aminotransferase_I/II.
DR   InterPro; IPR000796; Asp_trans.
DR   InterPro; IPR004838; NHTrfase_class1_PyrdxlP-BS.
DR   InterPro; IPR015424; PyrdxlP-dep_Trfase.
DR   InterPro; IPR015421; PyrdxlP-dep_Trfase_major.
DR   InterPro; IPR015422; PyrdxlP-dep_Trfase_small.
DR   PANTHER; PTHR11879; PTHR11879; 1.
DR   Pfam; PF00155; Aminotran_1_2; 1.
DR   PRINTS; PR00799; TRANSAMINASE.
DR   SUPFAM; SSF53383; SSF53383; 1.
DR   PROSITE; PS00105; AA_TRANSFER_CLASS_1; 1.
PE   3: Inferred from homology;
KW   Aminotransferase; Cytoplasm; Pyridoxal phosphate; Transferase.
FT   CHAIN           1..396
FT                   /note="Aspartate aminotransferase"
FT                   /id="PRO_0000123839"
FT   BINDING         34
FT                   /ligand="L-aspartate"
FT                   /ligand_id="ChEBI:CHEBI:29991"
FT                   /evidence="ECO:0000250"
FT   BINDING         130
FT                   /ligand="L-aspartate"
FT                   /ligand_id="ChEBI:CHEBI:29991"
FT                   /evidence="ECO:0000250"
FT   BINDING         183
FT                   /ligand="L-aspartate"
FT                   /ligand_id="ChEBI:CHEBI:29991"
FT                   /evidence="ECO:0000250"
FT   BINDING         374
FT                   /ligand="L-aspartate"
FT                   /ligand_id="ChEBI:CHEBI:29991"
FT                   /evidence="ECO:0000250"
FT   MOD_RES         246
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   396 AA;  43507 MW;  974C1585438D02FB CRC64;
     MFENITAAPA DPILGLADLF RADDRPGKIN LGIGVYKDET GKTPVLTSVK KAEQYLLENE
     TTKNYLGIDG IPEFARCTQE LLFGKGSALI NDKRARTAQT PGGTGALRIA ADFLAKNTPV
     KRVWVSNPSW PNHKSVFNAA GLEVREYAYY DAENHSLDFE ALQASLSEAQ AGDVVLFHGC
     CHNPTGIDPT LEQWQVLAEL SVEKGWLPLF DFAYQGFARG LEEDAEGLRA FAALHKELIV
     ASSYSKNFGL YNERVGACTL VAADAETVDR AFSQMKSAIR ANYSNPPAHG ASIVATILSN
     DALRAIWEQE LTDMRQRIQR MRQLFVNTLQ EKGANRDFSF IIKQNGMFSF SGLTKDQVLR
     LREEFGVYAV ASGRVNVAGM TPDNMAPLCE AIVAVL