ID   AAT_PYRAB               Reviewed;         389 AA.
AC   Q9V0L2; G8ZGX9;
DT   01-JUN-2001, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-2000, sequence version 1.
DT   03-AUG-2022, entry version 123.
DE   RecName: Full=Aspartate aminotransferase;
DE            Short=AspAT;
DE            EC=2.6.1.1;
DE   AltName: Full=Transaminase A;
GN   Name=aspC; OrderedLocusNames=PYRAB07770; ORFNames=PAB0525;
OS   Pyrococcus abyssi (strain GE5 / Orsay).
OC   Archaea; Euryarchaeota; Thermococci; Thermococcales; Thermococcaceae;
OC   Pyrococcus.
OX   NCBI_TaxID=272844;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=GE5 / Orsay;
RX   PubMed=12622808; DOI=10.1046/j.1365-2958.2003.03381.x;
RA   Cohen G.N., Barbe V., Flament D., Galperin M., Heilig R., Lecompte O.,
RA   Poch O., Prieur D., Querellou J., Ripp R., Thierry J.-C., Van der Oost J.,
RA   Weissenbach J., Zivanovic Y., Forterre P.;
RT   "An integrated analysis of the genome of the hyperthermophilic archaeon
RT   Pyrococcus abyssi.";
RL   Mol. Microbiol. 47:1495-1512(2003).
RN   [2]
RP   GENOME REANNOTATION.
RC   STRAIN=GE5 / Orsay;
RX   PubMed=22057919; DOI=10.1007/s00284-011-0035-x;
RA   Gao J., Wang J.;
RT   "Re-annotation of two hyperthermophilic archaea Pyrococcus abyssi GE5 and
RT   Pyrococcus furiosus DSM 3638.";
RL   Curr. Microbiol. 64:118-129(2012).
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; AJ248285; CAB49691.1; -; Genomic_DNA.
DR   EMBL; HE613800; CCE70174.1; -; Genomic_DNA.
DR   PIR; B75122; B75122.
DR   RefSeq; WP_010867899.1; NC_000868.1.
DR   AlphaFoldDB; Q9V0L2; -.
DR   SMR; Q9V0L2; -.
DR   STRING; 272844.PAB0525; -.
DR   EnsemblBacteria; CAB49691; CAB49691; PAB0525.
DR   GeneID; 1496118; -.
DR   KEGG; pab:PAB0525; -.
DR   PATRIC; fig|272844.11.peg.817; -.
DR   eggNOG; arCOG01130; Archaea.
DR   HOGENOM; CLU_017584_4_3_2; -.
DR   OMA; IHMEVGQ; -.
DR   OrthoDB; 32104at2157; -.
DR   PhylomeDB; Q9V0L2; -.
DR   Proteomes; UP000000810; Chromosome.
DR   Proteomes; UP000009139; 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: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..389
FT                   /note="Aspartate aminotransferase"
FT                   /id="PRO_0000123860"
FT   BINDING         34
FT                   /ligand="L-aspartate"
FT                   /ligand_id="ChEBI:CHEBI:29991"
FT                   /evidence="ECO:0000250"
FT   BINDING         171
FT                   /ligand="L-aspartate"
FT                   /ligand_id="ChEBI:CHEBI:29991"
FT                   /evidence="ECO:0000250"
FT   BINDING         362
FT                   /ligand="L-aspartate"
FT                   /ligand_id="ChEBI:CHEBI:29991"
FT                   /evidence="ECO:0000250"
FT   MOD_RES         233
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   389 AA;  43923 MW;  AC811F1A171A513C CRC64;
     MAMSDRLDLV NPSEIRKLFD IAAGMKDVIS LGIGEPDFDT PQHIKEYAKE ALDMGLTHYG
     PNIGLPELRE AIAEKLKKQN NIEADPNKEI MVLVGANQAF LMGLSAFLKD GEEVLIPTPA
     FVSYAPAVIL AGGKPVEVPT YEENEFRLNV DELKKYVTEK TKALIINSPC NPTGSVLKKK
     DLEEIADFAV EHDLIVISDE VYEHFIYDDV KHYSIASLDG MFERTITVNG FSKTFAMTGW
     RLGFVAAPSW IIEKMVKFQM YNATCPVTFI QYAAAKALRD ERSWKAVEEM RKEYDRRRKL
     VWKRLNEMGL PTVKPKGAFY IFPRIKDTGL TSKEFSELML MEAKVAVVPG SAFGKAGEGY
     VRISYATAYE KLEEAMDRME KVLREKKLT