ID   AAT_SALTY               Reviewed;         396 AA.
AC   P58661;
DT   31-JAN-2002, integrated into UniProtKB/Swiss-Prot.
DT   31-JAN-2002, sequence version 1.
DT   03-AUG-2022, entry version 117.
DE   RecName: Full=Aspartate aminotransferase;
DE            Short=AspAT;
DE            EC=2.6.1.1;
DE   AltName: Full=Transaminase A;
GN   Name=aspC; OrderedLocusNames=STM0998;
OS   Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Salmonella.
OX   NCBI_TaxID=99287;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=LT2 / SGSC1412 / ATCC 700720;
RX   PubMed=11677609; DOI=10.1038/35101614;
RA   McClelland M., Sanderson K.E., Spieth J., Clifton S.W., Latreille P.,
RA   Courtney L., Porwollik S., Ali J., Dante M., Du F., Hou S., Layman D.,
RA   Leonard S., Nguyen C., Scott K., Holmes A., Grewal N., Mulvaney E.,
RA   Ryan E., Sun H., Florea L., Miller W., Stoneking T., Nhan M., Waterston R.,
RA   Wilson R.K.;
RT   "Complete genome sequence of Salmonella enterica serovar Typhimurium LT2.";
RL   Nature 413:852-856(2001).
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; AE006468; AAL19932.1; -; Genomic_DNA.
DR   RefSeq; NP_459973.1; NC_003197.2.
DR   RefSeq; WP_000462653.1; NC_003197.2.
DR   AlphaFoldDB; P58661; -.
DR   SMR; P58661; -.
DR   STRING; 99287.STM0998; -.
DR   PaxDb; P58661; -.
DR   EnsemblBacteria; AAL19932; AAL19932; STM0998.
DR   GeneID; 1252516; -.
DR   KEGG; stm:STM0998; -.
DR   PATRIC; fig|99287.12.peg.1051; -.
DR   HOGENOM; CLU_032440_1_2_6; -.
DR   OMA; VGACTIV; -.
DR   PhylomeDB; P58661; -.
DR   BioCyc; SENT99287:STM0998-MON; -.
DR   Proteomes; UP000001014; Chromosome.
DR   GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR   GO; GO:0042802; F:identical protein binding; IBA:GO_Central.
DR   GO; GO:0004069; F:L-aspartate:2-oxoglutarate aminotransferase activity; IBA:GO_Central.
DR   GO; GO:0004838; F:L-tyrosine:2-oxoglutarate aminotransferase activity; IBA:GO_Central.
DR   GO; GO:0030170; F:pyridoxal phosphate binding; IBA:GO_Central.
DR   GO; GO:0008483; F:transaminase activity; IBA:GO_Central.
DR   GO; GO:0033585; P:L-phenylalanine biosynthetic process from chorismate via phenylpyruvate; IBA:GO_Central.
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; Reference proteome;
KW   Transferase.
FT   CHAIN           1..396
FT                   /note="Aspartate aminotransferase"
FT                   /id="PRO_0000123840"
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;  43521 MW;  960940D0148D02FB CRC64;
     MFENITAAPA DPILGLADLF RADDRPGKIN LGIGVYKDET GKTPVLTSVK KAEQYLLENE
     TTKNYLGIDG IPEFARCTQE LLFGKGSALI NDKRARTAQT PGGTGALRIA ADFLAKNTPV
     KRVWVSNPSW PNHKSVFNAA GLEVREYAYY DAENHTLDFE ALQASLSEAQ AGDVVLFHGC
     CHNPTGIDPT LEQWQVLAEL SVEKGWLPLF DFAYQGFARG LEEDAEGLRA FAALHKELIV
     ASSYSKNFGL YNERVGACTL VAADAETVDR AFSQMKSAIR ANYSNPPAHG ASIVATILSN
     DALRAIWEQE LTDMRQRIQR MRQLFVNTLQ EKGANRDFSF IIKQNGMFSF SGLTKDQVLR
     LREEFGVYAV ASGRVNVAGM TPDNMAPLCE AIVAVL