ID   AAT_THEKO               Reviewed;         364 AA.
AC   O93744;
DT   01-JUN-2001, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-1999, sequence version 1.
DT   03-AUG-2022, entry version 115.
DE   RecName: Full=Aspartate aminotransferase;
DE            Short=AspAT;
DE            EC=2.6.1.1;
DE   AltName: Full=Transaminase A;
GN   Name=aspC; OrderedLocusNames=TK0260;
OS   Thermococcus kodakarensis (strain ATCC BAA-918 / JCM 12380 / KOD1)
OS   (Pyrococcus kodakaraensis (strain KOD1)).
OC   Archaea; Euryarchaeota; Thermococci; Thermococcales; Thermococcaceae;
OC   Thermococcus.
OX   NCBI_TaxID=69014;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=ATCC BAA-918 / JCM 12380 / KOD1;
RA   Jongsareejit B., Fujiwara S., Takagi M., Imanaka T.;
RT   "Enzymatic characteristics of recombinant aspartate aminotransferase from
RT   Pyrococcus kodakaraensis KOD1.";
RL   Submitted (MAR-1998) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-918 / JCM 12380 / KOD1;
RX   PubMed=15710748; DOI=10.1101/gr.3003105;
RA   Fukui T., Atomi H., Kanai T., Matsumi R., Fujiwara S., Imanaka T.;
RT   "Complete genome sequence of the hyperthermophilic archaeon Thermococcus
RT   kodakaraensis KOD1 and comparison with Pyrococcus genomes.";
RL   Genome Res. 15:352-363(2005).
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; AB012002; BAA75925.1; -; Genomic_DNA.
DR   EMBL; AP006878; BAD84449.1; -; Genomic_DNA.
DR   RefSeq; WP_011249215.1; NC_006624.1.
DR   AlphaFoldDB; O93744; -.
DR   SMR; O93744; -.
DR   STRING; 69014.TK0260; -.
DR   EnsemblBacteria; BAD84449; BAD84449; TK0260.
DR   GeneID; 3235126; -.
DR   KEGG; tko:TK0260; -.
DR   PATRIC; fig|69014.16.peg.259; -.
DR   eggNOG; arCOG04333; Archaea.
DR   HOGENOM; CLU_017584_4_3_2; -.
DR   InParanoid; O93744; -.
DR   OMA; NDECYSE; -.
DR   OrthoDB; 32104at2157; -.
DR   PhylomeDB; O93744; -.
DR   Proteomes; UP000000536; 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:0008483; F:transaminase activity; IBA:GO_Central.
DR   GO; GO:0009058; P:biosynthetic process; IEA:InterPro.
DR   GO; GO:0006520; P:cellular amino acid metabolic process; IBA:GO_Central.
DR   Gene3D; 3.40.640.10; -; 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   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; Reference proteome;
KW   Transferase.
FT   CHAIN           1..364
FT                   /note="Aspartate aminotransferase"
FT                   /id="PRO_0000123862"
FT   BINDING         23
FT                   /ligand="L-aspartate"
FT                   /ligand_id="ChEBI:CHEBI:29991"
FT                   /evidence="ECO:0000250"
FT   BINDING         99
FT                   /ligand="L-aspartate"
FT                   /ligand_id="ChEBI:CHEBI:29991"
FT                   /evidence="ECO:0000250"
FT   BINDING         143
FT                   /ligand="L-aspartate"
FT                   /ligand_id="ChEBI:CHEBI:29991"
FT                   /evidence="ECO:0000250"
FT   BINDING         320
FT                   /ligand="L-aspartate"
FT                   /ligand_id="ChEBI:CHEBI:29991"
FT                   /evidence="ECO:0000250"
FT   MOD_RES         200
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   364 AA;  41231 MW;  2F331E69242FF499 CRC64;
     MFNVYEFFNR INEVRPESRL DAGQPDIPVR REIIEEAVES LRRGETGYTS TGGIRELRER
     IAEFEGVSAD EVIVAPGAKI LIAAEIASAK KVAVVSPRWN AYSLIARQFW REVEVIKTTL
     DERWIPRVEE IKADLIIINY PNNPTGRVLS GKEIRGLLDV AEENGVKVLS DEVYAELSFT
     RFTPARELYE NVVTVKGFSK LYSMTGFRLG YAIGERNEIR RIQRFIESTV TCVPPFVQRA
     GVKALELRDE LIKEVRRAYL ERVRMASKML RGFDFVEPEG AFYIFLRTPQ DGMAFAERLL
     SRGVAVFPGM AFGDYPNFIR ISLSGKGLER GLRVIREELE CALESRATEG WEGSSRGVSA
     EGSR