ID   AAT_STRVG               Reviewed;         397 AA.
AC   Q60013;
DT   30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1996, sequence version 1.
DT   03-AUG-2022, entry version 84.
DE   RecName: Full=Aspartate aminotransferase;
DE            Short=AspAT;
DE            EC=2.6.1.1;
DE   AltName: Full=Transaminase A;
GN   Name=aspC; Synonyms=aat;
OS   Streptomyces virginiae.
OC   Bacteria; Actinobacteria; Streptomycetales; Streptomycetaceae;
OC   Streptomyces; Streptomyces virginiae group.
OX   NCBI_TaxID=1961;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=8675024; DOI=10.1016/0378-1119(96)00067-4;
RA   Katayama M., Sakai Y., Okamoto S., Ihara F., Nihira T., Yamada Y.;
RT   "Gene organization in the ada-rplL region of Streptomyces virginiae.";
RL   Gene 171:135-136(1996).
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 {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the class-I pyridoxal-phosphate-dependent
CC       aminotransferase family. {ECO:0000305}.
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DR   EMBL; D50624; BAA09299.1; -; Genomic_DNA.
DR   PIR; T11786; T11786.
DR   AlphaFoldDB; Q60013; -.
DR   SMR; Q60013; -.
DR   STRING; 1961.JOAK01000021_gene7141; -.
DR   eggNOG; COG0436; Bacteria.
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:0044249; P:cellular biosynthetic process; IEA:UniProt.
DR   Gene3D; 3.40.640.10; -; 1.
DR   Gene3D; 3.90.1150.10; -; 1.
DR   InterPro; IPR004839; Aminotransferase_I/II.
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   Pfam; PF00155; Aminotran_1_2; 1.
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..397
FT                   /note="Aspartate aminotransferase"
FT                   /id="PRO_0000123853"
FT   BINDING         36
FT                   /ligand="L-aspartate"
FT                   /ligand_id="ChEBI:CHEBI:29991"
FT                   /evidence="ECO:0000250"
FT   BINDING         123
FT                   /ligand="L-aspartate"
FT                   /ligand_id="ChEBI:CHEBI:29991"
FT                   /evidence="ECO:0000250"
FT   BINDING         173
FT                   /ligand="L-aspartate"
FT                   /ligand_id="ChEBI:CHEBI:29991"
FT                   /evidence="ECO:0000250"
FT   BINDING         371
FT                   /ligand="L-aspartate"
FT                   /ligand_id="ChEBI:CHEBI:29991"
FT                   /evidence="ECO:0000250"
FT   MOD_RES         236
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   397 AA;  42381 MW;  EEFEDCEB7D923065 CRC64;
     MSARIGAISE SATLAVDAKA KALKAAGRPV IGFGAGEPDF PTPDYIVEAA VEACRNPKYH
     RYTPAGGLPE LKAAIAAKTL RDSGYEVEAS QVLVTNGGKQ AIYEAFAAIL DPGDEVIVPA
     PYWTTYPESI RLAGGVPVDV VADETTGYRV SVEQLEAART ERTKVVLFVS PSNPTGSVYS
     EADAKAIGEW AAEHGLWVLT DEIYEHLVYG EAKFTSLPVL VPALRDKCII VNGVAKTYAM
     TGWRVGWVIA PQDVIKAATN LQSHATSNVS NVAQVAALAA VSGNLDAVAE MRKAFDRRRQ
     TMVKMLNEID GVFCPTPEGA FYAYPSVKEL LGKEIRGKRP QSSVELAALI LDEVEVAVVP
     GEAFGTPGYL RLSYALGDED LVEGVSRIQK LLAEAKA