ID   AATC_BOVIN              Reviewed;         413 AA.
AC   P33097; Q2KJF2; Q5E9R4;
DT   01-OCT-1993, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 3.
DT   04-NOV-2026, entry version 167.
DE   RecName: Full=Aspartate aminotransferase, cytoplasmic {ECO:0000250|UniProtKB:P17174};
DE            Short=cAspAT;
DE            EC=2.6.1.1 {ECO:0000250|UniProtKB:P13221};
DE            EC=2.6.1.3 {ECO:0000250|UniProtKB:P13221};
DE   AltName: Full=Cysteine aminotransferase, cytoplasmic;
DE   AltName: Full=Cysteine transaminase, cytoplasmic;
DE            Short=cCAT;
DE   AltName: Full=Glutamate oxaloacetate transaminase 1;
DE   AltName: Full=Transaminase A;
GN   Name=GOT1 {ECO:0000250|UniProtKB:P17174};
OS   Bos taurus (Bovine).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC   Bovinae; Bos.
OX   NCBI_TaxID=9913;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Heart;
RX   PubMed=8224363; DOI=10.1016/0020-711x(93)90698-e;
RA   Aurilia V., Palmisano A., Ferrara L., Cubellis M.V., Sannia G., Marino G.;
RT   "Cloning and sequence analysis of A cDNA encoding bovine cytosolic
RT   aspartate aminotransferase.";
RL   Int. J. Biochem. 25:1505-1509(1993).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RX   PubMed=16305752; DOI=10.1186/1471-2164-6-166;
RA   Harhay G.P., Sonstegard T.S., Keele J.W., Heaton M.P., Clawson M.L.,
RA   Snelling W.M., Wiedmann R.T., Van Tassell C.P., Smith T.P.L.;
RT   "Characterization of 954 bovine full-CDS cDNA sequences.";
RL   BMC Genomics 6:166-166(2005).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=Crossbred X Angus; TISSUE=Liver;
RG   NIH - Mammalian Gene Collection (MGC) project;
RL   Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Biosynthesis of L-glutamate from L-aspartate or L-cysteine.
CC       Important regulator of levels of glutamate, the major excitatory
CC       neurotransmitter of the vertebrate central nervous system. Acts as a
CC       scavenger of glutamate in brain neuroprotection. The aspartate
CC       aminotransferase activity is involved in hepatic glucose synthesis
CC       during development and in adipocyte glyceroneogenesis. Using L-cysteine
CC       as substrate, regulates levels of mercaptopyruvate, an important source
CC       of hydrogen sulfide. Mercaptopyruvate is converted into H(2)S via the
CC       action of 3-mercaptopyruvate sulfurtransferase (3MST). Hydrogen sulfide
CC       is an important synaptic modulator and neuroprotectant in the brain.
CC       {ECO:0000250|UniProtKB:P13221}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=L-aspartate + 2-oxoglutarate = oxaloacetate + L-glutamate;
CC         Xref=Rhea:RHEA:21824, ChEBI:CHEBI:16452, ChEBI:CHEBI:16810,
CC         ChEBI:CHEBI:29985, ChEBI:CHEBI:29991; EC=2.6.1.1;
CC         Evidence={ECO:0000250|UniProtKB:P13221};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:21825;
CC         Evidence={ECO:0000250|UniProtKB:P13221};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=L-cysteine + 2-oxoglutarate = 2-oxo-3-sulfanylpropanoate + L-
CC         glutamate; Xref=Rhea:RHEA:17441, ChEBI:CHEBI:16810,
CC         ChEBI:CHEBI:29985, ChEBI:CHEBI:35235, ChEBI:CHEBI:57678; EC=2.6.1.3;
CC         Evidence={ECO:0000250|UniProtKB:P13221};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:17442;
CC         Evidence={ECO:0000250|UniProtKB:P13221};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=(2S)-2-aminobutanoate + 2-oxoglutarate = 2-oxobutanoate + L-
CC         glutamate; Xref=Rhea:RHEA:70223, ChEBI:CHEBI:16763,
CC         ChEBI:CHEBI:16810, ChEBI:CHEBI:29985, ChEBI:CHEBI:74359;
CC         Evidence={ECO:0000250|UniProtKB:P17174};
CC       PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:70225;
CC         Evidence={ECO:0000250|UniProtKB:P17174};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=3-sulfino-L-alanine + 2-oxoglutarate = 3-sulfinopyruvate + L-
CC         glutamate; Xref=Rhea:RHEA:70295, ChEBI:CHEBI:16810,
CC         ChEBI:CHEBI:29985, ChEBI:CHEBI:61085, ChEBI:CHEBI:140699;
CC         Evidence={ECO:0000250|UniProtKB:P13221};
CC       PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:70297;
CC         Evidence={ECO:0000250|UniProtKB:P13221};
CC   -!- COFACTOR:
CC       Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC   -!- SUBUNIT: Homodimer.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm.
CC   -!- MISCELLANEOUS: In eukaryotes there are cytoplasmic, mitochondrial and
CC       chloroplastic isozymes.
CC   -!- SIMILARITY: Belongs to the class-I pyridoxal-phosphate-dependent
CC       aminotransferase family. {ECO:0000305}.
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DR   EMBL; X66020; CAA46818.1; -; mRNA.
DR   EMBL; BT020856; AAX08873.1; -; mRNA.
DR   EMBL; BC105372; AAI05373.1; -; mRNA.
DR   PIR; I46006; S21560.
DR   RefSeq; NP_803468.1; NM_177502.2.
DR   AlphaFoldDB; P33097; -.
DR   SMR; P33097; -.
DR   FunCoup; P33097; 1917.
DR   STRING; 9913.ENSBTAP00000015873; -.
DR   Allergome; 11908; Bos d AATr.
DR   GlyGen; P33097; 1 site.
DR   PaxDb; 9913-ENSBTAP00000015873; -.
DR   PeptideAtlas; P33097; -.
DR   Ensembl; ENSBTAT00000015873.6; ENSBTAP00000015873.4; ENSBTAG00000011960.6.
DR   Ensembl; ENSBTAT00085023406; ENSBTAP00085037215; ENSBTAG00085019038.
DR   Ensembl; ENSBTAT00090074535; ENSBTAP00090041198; ENSBTAG00090035090.
DR   GeneID; 281206; -.
DR   KEGG; bta:281206; -.
DR   CTD; 2805; -.
DR   VEuPathDB; HostDB:ENSBTAG00000011960; -.
DR   VGNC; VGNC:29501; GOT1.
DR   eggNOG; KOG1412; Eukaryota.
DR   GeneTree; ENSGT00950000183082; -.
DR   HOGENOM; CLU_032440_1_2_1; -.
DR   InParanoid; P33097; -.
DR   OMA; AADLYCW; -.
DR   OrthoDB; 6752799at2759; -.
DR   Reactome; R-BTA-8963693; Aspartate and asparagine metabolism.
DR   Reactome; R-BTA-9856872; Malate-aspartate shuttle.
DR   Proteomes; UP000009136; Chromosome 26.
DR   Bgee; ENSBTAG00000011960; Expressed in retina and 103 other cell types or tissues.
DR   GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR   GO; GO:0120554; F:(2S)-2-aminobutanoate:2-oxoglutarate transaminase activity; ISS:UniProtKB.
DR   GO; GO:0004069; F:L-aspartate:2-oxoglutarate transaminase activity; ISS:UniProtKB.
DR   GO; GO:0047801; F:L-cysteine:2-oxoglutarate transaminase activity; ISS:UniProtKB.
DR   GO; GO:0030170; F:pyridoxal phosphate binding; IEA:InterPro.
DR   GO; GO:0032869; P:cellular response to insulin stimulus; IEA:Ensembl.
DR   GO; GO:0006114; P:glycerol biosynthetic process; ISS:UniProtKB.
DR   GO; GO:0006532; P:L-aspartate biosynthetic process; IBA:GO_Central.
DR   GO; GO:0006533; P:L-aspartate catabolic process; IEA:Ensembl.
DR   GO; GO:0043490; P:malate-aspartate shuttle; IEA:Ensembl.
DR   GO; GO:0051384; P:response to glucocorticoid; IEA:Ensembl.
DR   CDD; cd00609; AAT_like; 1.
DR   FunFam; 3.40.640.10:FF:000044; Aspartate aminotransferase; 1.
DR   Gene3D; 3.90.1150.10; Aspartate Aminotransferase, domain 1; 1.
DR   Gene3D; 3.40.640.10; Type I PLP-dependent aspartate aminotransferase-like (Major domain); 1.
DR   InterPro; IPR004839; Aminotransferase_I/II_large.
DR   InterPro; IPR000796; Asp_trans.
DR   InterPro; IPR004838; NHTrfase_class1_PLP_cs.
DR   InterPro; IPR015424; PyrdxlP-dep_Trfase.
DR   InterPro; IPR015421; PyrdxlP-dep_Trfase_major.
DR   InterPro; IPR015422; PyrdxlP-dep_Trfase_small.
DR   NCBIfam; NF006719; PRK09257.1; 1.
DR   PANTHER; PTHR11879; ASPARTATE AMINOTRANSFERASE; 1.
DR   PANTHER; PTHR11879:SF3; ASPARTATE AMINOTRANSFERASE, CYTOPLASMIC; 1.
DR   Pfam; PF00155; Aminotran_1_2; 1.
DR   PRINTS; PR00799; TRANSAMINASE.
DR   SUPFAM; SSF53383; PLP-dependent transferases; 1.
DR   PROSITE; PS00105; AA_TRANSFER_CLASS_1; 1.
PE   1: Evidence at protein level;
KW   Amino-acid biosynthesis; Aminotransferase; Cytoplasm; Pyridoxal phosphate;
KW   Reference proteome; Transferase.
FT   CHAIN           1..413
FT                   /note="Aspartate aminotransferase, cytoplasmic"
FT                   /id="PRO_0000123877"
FT   BINDING         39
FT                   /ligand="L-aspartate"
FT                   /ligand_id="ChEBI:CHEBI:29991"
FT                   /evidence="ECO:0000250"
FT   BINDING         141
FT                   /ligand="L-aspartate"
FT                   /ligand_id="ChEBI:CHEBI:29991"
FT                   /evidence="ECO:0000250"
FT   BINDING         195
FT                   /ligand="L-aspartate"
FT                   /ligand_id="ChEBI:CHEBI:29991"
FT                   /evidence="ECO:0000250"
FT   BINDING         387
FT                   /ligand="L-aspartate"
FT                   /ligand_id="ChEBI:CHEBI:29991"
FT                   /evidence="ECO:0000250"
FT   MOD_RES         259
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT   CONFLICT        228
FT                   /note="G -> A (in Ref. 1; CAA46818)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   413 AA;  46399 MW;  EB43960F08081DD4 CRC64;
     MAPPSIFAEV PQAQPVLVFK LTADFREDPD PRKVNLGVGA YRTDDSQPWV LPVVRKVEQR
     IANDSSINHE YLPILGLAEF RTCASRLALG DDSPALQEKR VGGVQCLGGT GALRIGAEFL
     ARWYNGTNNK DTPVYVSSPT WENHNGVFIA AGFKDIRSYH YWDAAKRGLD LQGFLNDLEK
     APEFSIFVLH ACAHNPTGTD PTPEQWKQIA SVMKRRFLFP FFDSAYQGFA SGSLEKDAWA
     IRYFVSEGFE LFCAQSFSKN FGLYNERVGN LTVVAKEPDS ILRVLSQMEK IVRITWSNPP
     AQGARIVART LSDPELFNEW TGNVKTMADR ILTMRSELRA RLEALKTPGT WNHITEQIGM
     FSFTGLNPKQ VEYLINEKHI YLLPSGRINM CGLTTKNLEY VATSIHEAVT KIQ
//