ID   ALAT1_BOVIN             Reviewed;         496 AA.
AC   A4IFH5;
DT   08-APR-2008, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-2007, sequence version 1.
DT   08-NOV-2023, 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;
GN   Name=GPT; Synonyms=GPT1;
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 [LARGE SCALE MRNA].
RC   STRAIN=Hereford; TISSUE=Hypothalamus;
RG   NIH - Mammalian Gene Collection (MGC) project;
RL   Submitted (MAR-2007) to the EMBL/GenBank/DDBJ databases.
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         Evidence={ECO:0000250};
CC   -!- PATHWAY: Amino-acid degradation; L-alanine degradation via transaminase
CC       pathway; pyruvate from L-alanine: step 1/1.
CC   -!- SUBUNIT: Homodimer. {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the class-I pyridoxal-phosphate-dependent
CC       aminotransferase family. Alanine aminotransferase subfamily.
CC       {ECO:0000305}.
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DR   EMBL; BC134583; AAI34584.1; -; mRNA.
DR   RefSeq; NP_001077209.1; NM_001083740.2.
DR   AlphaFoldDB; A4IFH5; -.
DR   SMR; A4IFH5; -.
DR   STRING; 9913.ENSBTAP00000010309; -.
DR   PaxDb; 9913-ENSBTAP00000010309; -.
DR   GeneID; 539188; -.
DR   KEGG; bta:539188; -.
DR   CTD; 2875; -.
DR   eggNOG; KOG0258; Eukaryota.
DR   HOGENOM; CLU_014254_3_1_1; -.
DR   InParanoid; A4IFH5; -.
DR   OrthoDB; 5472891at2759; -.
DR   TreeFam; TF300839; -.
DR   UniPathway; UPA00528; UER00586.
DR   Proteomes; UP000009136; Unplaced.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0004021; F:L-alanine:2-oxoglutarate aminotransferase activity; IBA:GO_Central.
DR   GO; GO:0030170; F:pyridoxal phosphate binding; IEA:InterPro.
DR   GO; GO:0009058; P:biosynthetic process; IEA:InterPro.
DR   GO; GO:0042853; P:L-alanine catabolic process; IEA:UniProtKB-UniPathway.
DR   CDD; cd00609; AAT_like; 1.
DR   Gene3D; 1.10.287.1970; -; 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; IPR045088; ALAT1/2-like.
DR   InterPro; IPR004839; Aminotransferase_I/II.
DR   InterPro; IPR015424; PyrdxlP-dep_Trfase.
DR   InterPro; IPR015421; PyrdxlP-dep_Trfase_major.
DR   InterPro; IPR015422; PyrdxlP-dep_Trfase_small.
DR   PANTHER; PTHR11751; ALANINE AMINOTRANSFERASE; 1.
DR   PANTHER; PTHR11751:SF308; ALANINE AMINOTRANSFERASE 1; 1.
DR   Pfam; PF00155; Aminotran_1_2; 1.
DR   SUPFAM; SSF53383; PLP-dependent transferases; 1.
PE   2: Evidence at transcript level;
KW   Acetylation; Aminotransferase; Cytoplasm; Phosphoprotein;
KW   Pyridoxal phosphate; Reference proteome; Transferase.
FT   INIT_MET        1
FT                   /note="Removed"
FT                   /evidence="ECO:0000250|UniProtKB:P24298"
FT   CHAIN           2..496
FT                   /note="Alanine aminotransferase 1"
FT                   /id="PRO_0000328385"
FT   MOD_RES         2
FT                   /note="N-acetylalanine"
FT                   /evidence="ECO:0000250|UniProtKB:P24298"
FT   MOD_RES         22
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0000250|UniProtKB:P24298"
FT   MOD_RES         314
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   496 AA;  55275 MW;  EA136706AA816ED0 CRC64;
     MALRAGEHSQ EAANGLKEKV LTLDSMNPYV RRVEYAVRGP IVQRALELEQ ELRQGVKKPF
     TEVIRANIGD AQAMGQIPIT FPRQVLALCV HPDLLNSPDF PDDAKRRAER ILQACGGHSL
     GAYSISAGVQ MIREDVARYI ERRDGGIPAD PNNIFLSTGA SDAIVTVLKL LVTGEGRTRT
     GVLIPIPQYP LYSAALAEFN AVQVDYYLDE ERAWALDVAE LRRALRQARD HCRPRALCVI
     NPGNPTGQVQ TRECIEDVIR FAYEEKLFLL ADEVYQDNVY AESSQFHSFK KVLTEMGPPY
     AAQQELASFH SISKGYMGEC GFRGGYVEVV NMDAAVKQQM QKLRSVRLCP PTPGQVLLDV
     AVSPPAPSDP SFPRFQAERR AVLAELAAKA KLTEQVFNEA PGIRCNPVQG AMYSFPRVQL
     PPRAVQRAQE LGLAPDMFFC LRLLEETGIC VVPGSGFGQR EGTYHFRMTI LPPMEKLRPL
     LEKLSQFHAK FTREYS
//