ID   AAT_SULTO               Reviewed;         399 AA.
AC   Q972A2;
DT   27-SEP-2005, integrated into UniProtKB/Swiss-Prot.
DT   01-DEC-2001, sequence version 1.
DT   03-AUG-2022, entry version 110.
DE   RecName: Full=Aspartate aminotransferase;
DE            Short=AspAT;
DE            EC=2.6.1.1;
DE   AltName: Full=Transaminase A;
GN   Name=aspC; OrderedLocusNames=STK_12250;
OS   Sulfurisphaera tokodaii (strain DSM 16993 / JCM 10545 / NBRC 100140 / 7)
OS   (Sulfolobus tokodaii).
OC   Archaea; Crenarchaeota; Thermoprotei; Sulfolobales; Sulfolobaceae;
OC   Sulfurisphaera.
OX   NCBI_TaxID=273063;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 16993 / JCM 10545 / NBRC 100140 / 7;
RX   PubMed=11572479; DOI=10.1093/dnares/8.4.123;
RA   Kawarabayasi Y., Hino Y., Horikawa H., Jin-no K., Takahashi M., Sekine M.,
RA   Baba S., Ankai A., Kosugi H., Hosoyama A., Fukui S., Nagai Y.,
RA   Nishijima K., Otsuka R., Nakazawa H., Takamiya M., Kato Y., Yoshizawa T.,
RA   Tanaka T., Kudoh Y., Yamazaki J., Kushida N., Oguchi A., Aoki K.,
RA   Masuda S., Yanagii M., Nishimura M., Yamagishi A., Oshima T., Kikuchi H.;
RT   "Complete genome sequence of an aerobic thermoacidophilic Crenarchaeon,
RT   Sulfolobus tokodaii strain7.";
RL   DNA Res. 8:123-140(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 {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the class-I pyridoxal-phosphate-dependent
CC       aminotransferase family. {ECO:0000305}.
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DR   EMBL; BA000023; BAB66267.1; -; Genomic_DNA.
DR   RefSeq; WP_010979245.1; NC_003106.2.
DR   AlphaFoldDB; Q972A2; -.
DR   SMR; Q972A2; -.
DR   STRING; 273063.STK_12250; -.
DR   PRIDE; Q972A2; -.
DR   EnsemblBacteria; BAB66267; BAB66267; STK_12250.
DR   GeneID; 1459224; -.
DR   KEGG; sto:STK_12250; -.
DR   PATRIC; fig|273063.9.peg.1385; -.
DR   eggNOG; arCOG01130; Archaea.
DR   OMA; SVAMTGW; -.
DR   OrthoDB; 32104at2157; -.
DR   Proteomes; UP000001015; 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; Reference proteome;
KW   Transferase.
FT   CHAIN           1..399
FT                   /note="Aspartate aminotransferase"
FT                   /id="PRO_0000123865"
FT   BINDING         42
FT                   /ligand="L-aspartate"
FT                   /ligand_id="ChEBI:CHEBI:29991"
FT                   /evidence="ECO:0000250"
FT   BINDING         179
FT                   /ligand="L-aspartate"
FT                   /ligand_id="ChEBI:CHEBI:29991"
FT                   /evidence="ECO:0000250"
FT   BINDING         372
FT                   /ligand="L-aspartate"
FT                   /ligand_id="ChEBI:CHEBI:29991"
FT                   /evidence="ECO:0000250"
FT   MOD_RES         240
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   399 AA;  45406 MW;  EE5ED3CDE4258581 CRC64;
     MPVDDFSLSA NSISGESTLV YQDVARQVQK TKGIRIINFG IGQPDLPTFA RIREAAKKSL
     DEGFTGYTSA YGIDELRQKI AEHLSSKYES VRKEEVIVTP GAKTALYLAF LLYINPGDEV
     IIFDPSFYSY AEVVKMLGGV PVYVKMKFNE STGFSLNLSE LESKINKKTK MIVLNNPHNP
     TGMVFDPIEI EKLMEITKEK KVLLLSDEIY DYFIYEGKMK SVLEDPDWRD YVIYVNGFSK
     TFSMTGWRLG YVVAKEKVIK KMAEIAANIY TCPTSFAQKG ALAAFESFDE VKEMISLFKK
     RRDIMYEELK KIKGIQVHKS QGAFYMFPFI GEILKKANLS VKDFSLKLIE EKGVTTIPGE
     VFPLEVGKDF VRLSFAVKED DIREGIKRMK EFIDMLMTP