ID   AAT_SULAC               Reviewed;         400 AA.
AC   Q4J8X2;
DT   27-SEP-2005, integrated into UniProtKB/Swiss-Prot.
DT   02-AUG-2005, sequence version 1.
DT   03-AUG-2022, entry version 89.
DE   RecName: Full=Aspartate aminotransferase;
DE            Short=AspAT;
DE            EC=2.6.1.1;
DE   AltName: Full=Transaminase A;
GN   Name=aspC; OrderedLocusNames=Saci_1428;
OS   Sulfolobus acidocaldarius (strain ATCC 33909 / DSM 639 / JCM 8929 / NBRC
OS   15157 / NCIMB 11770).
OC   Archaea; Crenarchaeota; Thermoprotei; Sulfolobales; Sulfolobaceae;
OC   Sulfolobus.
OX   NCBI_TaxID=330779;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 33909 / DSM 639 / JCM 8929 / NBRC 15157 / NCIMB 11770;
RX   PubMed=15995215; DOI=10.1128/jb.187.14.4992-4999.2005;
RA   Chen L., Bruegger K., Skovgaard M., Redder P., She Q., Torarinsson E.,
RA   Greve B., Awayez M., Zibat A., Klenk H.-P., Garrett R.A.;
RT   "The genome of Sulfolobus acidocaldarius, a model organism of the
RT   Crenarchaeota.";
RL   J. Bacteriol. 187:4992-4999(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}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; CP000077; AAY80758.1; -; Genomic_DNA.
DR   RefSeq; WP_011278260.1; NC_007181.1.
DR   AlphaFoldDB; Q4J8X2; -.
DR   SMR; Q4J8X2; -.
DR   STRING; 330779.Saci_1428; -.
DR   EnsemblBacteria; AAY80758; AAY80758; Saci_1428.
DR   GeneID; 3473431; -.
DR   KEGG; sai:Saci_1428; -.
DR   PATRIC; fig|330779.12.peg.1376; -.
DR   eggNOG; arCOG01130; Archaea.
DR   HOGENOM; CLU_017584_4_3_2; -.
DR   OMA; ARFRHFS; -.
DR   Proteomes; UP000001018; 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..400
FT                   /note="Aspartate aminotransferase"
FT                   /id="PRO_0000123863"
FT   BINDING         42
FT                   /ligand="L-aspartate"
FT                   /ligand_id="ChEBI:CHEBI:29991"
FT                   /evidence="ECO:0000250"
FT   BINDING         180
FT                   /ligand="L-aspartate"
FT                   /ligand_id="ChEBI:CHEBI:29991"
FT                   /evidence="ECO:0000250"
FT   BINDING         373
FT                   /ligand="L-aspartate"
FT                   /ligand_id="ChEBI:CHEBI:29991"
FT                   /evidence="ECO:0000250"
FT   MOD_RES         241
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   400 AA;  45189 MW;  1AA1515C2D3EBFD9 CRC64;
     MSLDNFSKGA LAISGETTLL YQDIARSVQK EKGIKIVNFG IGQPDFPTFQ KIRDEAKKAL
     DGGFTAYTSA YGIDELRAKI ASFLSSKYNT NISSKEVIIT PGAKVSLYLA FLLYVNPGDE
     VIIFDPSYYS YPEVVKMLGG KPVYVKMKWR EDTGFSLNLN DLENKITDKT KMVVLNNPHN
     PTGMVFDPKE IDQLIEIAKS KNLIVLSDEI YDYFVYEGKM RSVLEDPDWK NFSIYVNGFS
     KTFSMTGWRL GYVVAKENVI KKMSEIAANV YTCPTSFAQK AAVSAFDTFD DVKKMIDTFK
     KRRDVMYSEL KKIKGIQVNK SQGAFYMFPY LGEILRKSGM STKDFSVNLI KEKGVVTIPG
     EVFPLDAGKE FVRLSFAVDE NVIKEGVQRM SEFINQLMRS