ID   AATC_RABIT              Reviewed;          31 AA.
AC   P12343;
DT   01-OCT-1989, integrated into UniProtKB/Swiss-Prot.
DT   20-FEB-2007, sequence version 2.
DT   25-MAY-2022, entry version 96.
DE   RecName: Full=Aspartate aminotransferase, cytoplasmic {ECO:0000250|UniProtKB:P17174};
DE            Short=cAspAT;
DE            EC=2.6.1.1 {ECO:0000269|PubMed:4030726};
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;
DE   Flags: Fragment;
GN   Name=GOT1 {ECO:0000250|UniProtKB:P17174};
OS   Oryctolagus cuniculus (Rabbit).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Lagomorpha; Leporidae; Oryctolagus.
OX   NCBI_TaxID=9986;
RN   [1]
RP   PROTEIN SEQUENCE OF 2-31, FUNCTION, AND CATALYTIC ACTIVITY.
RC   TISSUE=Liver;
RX   PubMed=4030726; DOI=10.1093/oxfordjournals.jbchem.a135186;
RA   Kuramitsu S., Inoue K., Kondo K., Aki K., Kagamiyama H.;
RT   "Aspartate aminotransferase isozymes from rabbit liver. Purification and
RT   properties.";
RL   J. Biochem. 97:1337-1345(1985).
CC   -!- FUNCTION: Biosynthesis of L-glutamate from L-aspartate or L-cysteine
CC       (PubMed:4030726). Important regulator of levels of glutamate, the major
CC       excitatory neurotransmitter of the vertebrate central nervous system.
CC       Acts as a scavenger of glutamate in brain neuroprotection. The
CC       aspartate aminotransferase activity is involved in hepatic glucose
CC       synthesis during development and in adipocyte glyceroneogenesis. Using
CC       L-cysteine as substrate, regulates levels of mercaptopyruvate, an
CC       important source of hydrogen sulfide. Mercaptopyruvate is converted
CC       into H(2)S via the action of 3-mercaptopyruvate sulfurtransferase
CC       (3MST). Hydrogen sulfide is an important synaptic modulator and
CC       neuroprotectant in the brain (By similarity).
CC       {ECO:0000250|UniProtKB:P13221, ECO:0000269|PubMed:4030726}.
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:0000269|PubMed:4030726};
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   PIR; A27103; A27103.
DR   AlphaFoldDB; P12343; -.
DR   SMR; P12343; -.
DR   STRING; 9986.ENSOCUP00000010617; -.
DR   eggNOG; KOG1412; Eukaryota.
DR   Proteomes; UP000001811; Unplaced.
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:0047801; F:L-cysteine transaminase activity; ISS:UniProtKB.
DR   GO; GO:0008652; P:cellular amino acid biosynthetic process; IEA:UniProtKB-KW.
DR   GO; GO:0006114; P:glycerol biosynthetic process; ISS:UniProtKB.
PE   1: Evidence at protein level;
KW   Amino-acid biosynthesis; Aminotransferase; Cytoplasm;
KW   Direct protein sequencing; Pyridoxal phosphate; Reference proteome;
KW   Transferase.
FT   INIT_MET        1
FT                   /note="Removed"
FT                   /evidence="ECO:0000269|PubMed:4030726"
FT   CHAIN           2..>31
FT                   /note="Aspartate aminotransferase, cytoplasmic"
FT                   /id="PRO_0000123882"
FT   NON_TER         31
SQ   SEQUENCE   31 AA;  3427 MW;  5286CEEAC2FC144C CRC64;
     MAPPSIFAEV PQAQPVLVFK LTADFREDPD P