AATC_BOVIN
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 03-AUG-2022, entry version 152.
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=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 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=2-oxoglutarate + L-cysteine = 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=2-oxoglutarate + 3-sulfino-L-alanine = 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 STRING; 9913.ENSBTAP00000015873; -.
DR Allergome; 11908; Bos d AATr.
DR PaxDb; P33097; -.
DR PeptideAtlas; P33097; -.
DR PRIDE; P33097; -.
DR Ensembl; ENSBTAT00000015873; ENSBTAP00000015873; ENSBTAG00000011960.
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; WDQNKRQ; -.
DR OrthoDB; 1104596at2759; -.
DR TreeFam; TF314089; -.
DR Reactome; R-BTA-70263; Gluconeogenesis.
DR Reactome; R-BTA-8963693; Aspartate and asparagine metabolism.
DR Proteomes; UP000009136; Chromosome 26.
DR Bgee; ENSBTAG00000011960; Expressed in retina and 103 other tissues.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:0005654; C:nucleoplasm; IEA:Ensembl.
DR GO; GO:0004069; F:L-aspartate:2-oxoglutarate aminotransferase activity; IBA:GO_Central.
DR GO; GO:0047801; F:L-cysteine transaminase activity; ISS:UniProtKB.
DR GO; GO:0004609; F:phosphatidylserine decarboxylase activity; IEA:Ensembl.
DR GO; GO:0030170; F:pyridoxal phosphate binding; IEA:InterPro.
DR GO; GO:0006532; P:aspartate biosynthetic process; IBA:GO_Central.
DR GO; GO:0006533; P:aspartate catabolic process; IEA:Ensembl.
DR GO; GO:0032869; P:cellular response to insulin stimulus; IEA:Ensembl.
DR GO; GO:0055089; P:fatty acid homeostasis; IEA:Ensembl.
DR GO; GO:0019551; P:glutamate catabolic process to 2-oxoglutarate; IEA:Ensembl.
DR GO; GO:0019550; P:glutamate catabolic process to aspartate; IEA:Ensembl.
DR GO; GO:0006114; P:glycerol biosynthetic process; ISS:UniProtKB.
DR GO; GO:0007219; P:Notch signaling pathway; IEA:Ensembl.
DR GO; GO:0006107; P:oxaloacetate metabolic process; IEA:Ensembl.
DR GO; GO:0051384; P:response to glucocorticoid; IEA:Ensembl.
DR Gene3D; 3.40.640.10; -; 1.
DR Gene3D; 3.90.1150.10; -; 1.
DR InterPro; IPR004839; Aminotransferase_I/II.
DR InterPro; IPR000796; Asp_trans.
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 PANTHER; PTHR11879; PTHR11879; 1.
DR Pfam; PF00155; Aminotran_1_2; 1.
DR PRINTS; PR00799; TRANSAMINASE.
DR SUPFAM; SSF53383; SSF53383; 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
