ID   AAT_GEOSE               Reviewed;         393 AA.
AC   Q59228;
DT   01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1996, sequence version 1.
DT   03-AUG-2022, entry version 87.
DE   RecName: Full=Aspartate aminotransferase;
DE            Short=AspAT;
DE            EC=2.6.1.1;
DE   AltName: Full=Transaminase A;
GN   Name=aspC;
OS   Geobacillus stearothermophilus (Bacillus stearothermophilus).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Geobacillus.
OX   NCBI_TaxID=1422;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=ATCC 12980 / DSM 22 / CCM 2062 / JCM 2501 / NBRC 12550 / NCIMB 8923
RC   / NCTC 10339 / R-35646 / VKM B-510;
RX   PubMed=8837436; DOI=10.1128/aem.62.10.3794-3799.1996;
RA   Bartsch K., Schneider R., Schulz A.;
RT   "Stereospecific production of the herbicide phosphinothricin (glufosinate):
RT   purification of aspartate transaminase from Bacillus stearothermophilus,
RT   cloning of the corresponding gene, aspC, and application in a coupled
RT   transaminase process.";
RL   Appl. Environ. Microbiol. 62:3794-3799(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   -!- 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; X93600; CAA63799.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q59228; -.
DR   SMR; Q59228; -.
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: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; 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..393
FT                   /note="Aspartate aminotransferase"
FT                   /id="PRO_0000123835"
FT   BINDING         38
FT                   /ligand="L-aspartate"
FT                   /ligand_id="ChEBI:CHEBI:29991"
FT                   /evidence="ECO:0000250"
FT   BINDING         124
FT                   /ligand="L-aspartate"
FT                   /ligand_id="ChEBI:CHEBI:29991"
FT                   /evidence="ECO:0000250"
FT   BINDING         174
FT                   /ligand="L-aspartate"
FT                   /ligand_id="ChEBI:CHEBI:29991"
FT                   /evidence="ECO:0000250"
FT   MOD_RES         237
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   393 AA;  42402 MW;  4628CCD998A065A7 CRC64;
     MKLAKRVASL TPSATLAITE KAKELKAAGH DVIGLGAGEP DFNTPQHILD AAIKAMNEGH
     TKYTPSGGLP ALKEEIIKKF ARDQGLDYEP AEVIVCVGAK HALYTLFQVL LDEGDEVIIP
     TPYWVSYPEQ VKLAGGVPVY VEGLEQNHFK ITPEQLKQAI TPRTKAVIIN SPSNPTGMIY
     TAEELKALGE VCLAHGVLIV SDEIYEKLTY GGAKHVSIAE LSPELKAQTV IINGVSKSHS
     MTGWRIGYAA GPKDIIKAMT DLASHSTSNP TSIAQYAAIA AYSGPQEPVE QMRQAFEQRL
     NIIYDKLVQI PGFTCVKPQG AFYLFPNARE AAAMAGCRTV DEFVAALLEE AKVALVPGSG
     FGAPDNVRLS YATSLDALET AVERIHRFME ARA