ID   ALAT1_PIG               Reviewed;          20 AA.
AC   P13191;
DT   01-JAN-1990, integrated into UniProtKB/Swiss-Prot.
DT   01-JAN-1990, sequence version 1.
DT   25-MAY-2022, entry version 106.
DE   RecName: Full=Alanine aminotransferase 1;
DE            Short=ALT1;
DE            EC=2.6.1.2;
DE   AltName: Full=Glutamate pyruvate transaminase 1;
DE            Short=GPT 1;
DE   AltName: Full=Glutamic--alanine transaminase 1;
DE   AltName: Full=Glutamic--pyruvic transaminase 1;
DE   Flags: Fragment;
GN   Name=GPT; Synonyms=AAT1, GPT1;
OS   Sus scrofa (Pig).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Artiodactyla; Suina; Suidae; Sus.
OX   NCBI_TaxID=9823;
RN   [1]
RP   PROTEIN SEQUENCE.
RC   TISSUE=Heart;
RX   PubMed=465450; DOI=10.1021/bi00581a015;
RA   Tanase S., Kojima H., Morino Y.;
RT   "Pyridoxal 5'-phosphate binding site of pig heart alanine
RT   aminotransferase.";
RL   Biochemistry 18:3002-3007(1979).
RN   [2]
RP   GLYCATION AT LYS-11.
RX   PubMed=11330835; DOI=10.1023/a:1007280913732;
RA   Beranek M., Drsata J., Palicka V.;
RT   "Inhibitory effect of glycation on catalytic activity of alanine
RT   aminotransferase.";
RL   Mol. Cell. Biochem. 218:35-39(2001).
CC   -!- FUNCTION: Catalyzes the reversible transamination between alanine and
CC       2-oxoglutarate to form pyruvate and glutamate. Participates in cellular
CC       nitrogen metabolism and also in liver gluconeogenesis starting with
CC       precursors transported from skeletal muscles (By similarity).
CC       {ECO:0000250}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=2-oxoglutarate + L-alanine = L-glutamate + pyruvate;
CC         Xref=Rhea:RHEA:19453, ChEBI:CHEBI:15361, ChEBI:CHEBI:16810,
CC         ChEBI:CHEBI:29985, ChEBI:CHEBI:57972; EC=2.6.1.2;
CC   -!- COFACTOR:
CC       Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC   -!- PATHWAY: Amino-acid degradation; L-alanine degradation via transaminase
CC       pathway; pyruvate from L-alanine: step 1/1.
CC   -!- SUBUNIT: Homodimer.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm.
CC   -!- PTM: Glycation of Lys-11 inactivates the enzyme.
CC   -!- SIMILARITY: Belongs to the class-I pyridoxal-phosphate-dependent
CC       aminotransferase family. Alanine aminotransferase subfamily.
CC       {ECO:0000305}.
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DR   PIR; A14344; A14344.
DR   AlphaFoldDB; P13191; -.
DR   STRING; 9823.ENSSSCP00000006308; -.
DR   PaxDb; P13191; -.
DR   PeptideAtlas; P13191; -.
DR   eggNOG; KOG0258; Eukaryota.
DR   HOGENOM; CLU_014254_3_1_1; -.
DR   SABIO-RK; P13191; -.
DR   UniPathway; UPA00528; UER00586.
DR   Proteomes; UP000008227; Unplaced.
DR   Proteomes; UP000314985; Unplaced.
DR   Genevisible; P13191; SS.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0004021; F:L-alanine:2-oxoglutarate aminotransferase activity; IEA:UniProtKB-EC.
DR   GO; GO:0042853; P:L-alanine catabolic process; IEA:UniProtKB-UniPathway.
DR   Gene3D; 3.40.640.10; -; 1.
DR   InterPro; IPR015421; PyrdxlP-dep_Trfase_major.
PE   1: Evidence at protein level;
KW   Aminotransferase; Cytoplasm; Direct protein sequencing; Glycation;
KW   Glycoprotein; Pyridoxal phosphate; Reference proteome; Transferase.
FT   CHAIN           <1..>20
FT                   /note="Alanine aminotransferase 1"
FT                   /id="PRO_0000123935"
FT   MOD_RES         11
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT   CARBOHYD        11
FT                   /note="N-linked (Glc) (glycation) lysine; in vitro"
FT                   /evidence="ECO:0000269|PubMed:11330835"
FT   NON_TER         1
FT   NON_TER         20
SQ   SEQUENCE   20 AA;  2218 MW;  1C2243A373EC4801 CRC64;
     QELASFHSVS KGFMGECGFR