ID   ALAT2_XENLA             Reviewed;         540 AA.
AC   Q6GM82;
DT   25-JUL-2006, integrated into UniProtKB/Swiss-Prot.
DT   19-JUL-2004, sequence version 1.
DT   03-AUG-2022, entry version 75.
DE   RecName: Full=Alanine aminotransferase 2;
DE            Short=ALT2;
DE            EC=2.6.1.2;
DE   AltName: Full=Glutamate pyruvate transaminase 2;
DE            Short=GPT 2;
DE   AltName: Full=Glutamic--alanine transaminase 2;
DE   AltName: Full=Glutamic--pyruvic transaminase 2;
GN   Name=gpt2;
OS   Xenopus laevis (African clawed frog).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC   Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Xenopus.
OX   NCBI_TaxID=8355;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Kidney;
RG   NIH - Xenopus Gene Collection (XGC) project;
RL   Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Catalyzes the reversible transamination between alanine and
CC       2-oxoglutarate to form pyruvate and glutamate. {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   -!- SIMILARITY: Belongs to the class-I pyridoxal-phosphate-dependent
CC       aminotransferase family. Alanine aminotransferase subfamily.
CC       {ECO:0000305}.
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DR   EMBL; BC074194; AAH74194.1; -; mRNA.
DR   RefSeq; NP_001086104.1; NM_001092635.1.
DR   AlphaFoldDB; Q6GM82; -.
DR   SMR; Q6GM82; -.
DR   GeneID; 444533; -.
DR   KEGG; xla:444533; -.
DR   CTD; 444533; -.
DR   Xenbase; XB-GENE-5824402; gpt.L.
DR   OrthoDB; 477122at2759; -.
DR   UniPathway; UPA00528; UER00586.
DR   Proteomes; UP000186698; Chromosome 6L.
DR   Bgee; 444533; Expressed in kidney and 19 other tissues.
DR   GO; GO:0004021; F:L-alanine:2-oxoglutarate aminotransferase activity; ISS:UniProtKB.
DR   GO; GO:0030170; F:pyridoxal phosphate binding; IEA:InterPro.
DR   GO; GO:0006103; P:2-oxoglutarate metabolic process; ISS:UniProtKB.
DR   GO; GO:0009058; P:biosynthetic process; IEA:InterPro.
DR   GO; GO:0042853; P:L-alanine catabolic process; IEA:UniProtKB-UniPathway.
DR   GO; GO:0042851; P:L-alanine metabolic process; ISS:UniProtKB.
DR   Gene3D; 3.40.640.10; -; 1.
DR   Gene3D; 3.90.1150.10; -; 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; PTHR11751; 1.
DR   Pfam; PF00155; Aminotran_1_2; 1.
DR   SUPFAM; SSF53383; SSF53383; 1.
PE   2: Evidence at transcript level;
KW   Aminotransferase; Pyridoxal phosphate; Reference proteome; Transferase.
FT   CHAIN           1..540
FT                   /note="Alanine aminotransferase 2"
FT                   /id="PRO_0000247535"
FT   MOD_RES         358
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   540 AA;  59796 MW;  D90CC482EA1D7B49 CRC64;
     MSILRGSLRG VLAPNASVVF RSRLPPQLTS ALLCPLRSLS GTPLAEPDGK VTRKMSENGT
     CNRILTLDSM NPCIQKVEYA VRGPIVIRAV ELEKELQQGV KKPFTEVIKA NIGDAHAMGQ
     KPVTFLRQVS AICLYPELMN DNKFPEDVKQ KAARILQACG GHSIGAYSAS QGIEVIRQDV
     AKYIERRDGG ILSDPNNIYL STGASDSIVT MLKLLVSGQG KSRTGVMIPI PQYPLYSAAL
     AELDAVQVNY YLDEENCWAL DINELRRALA EARKHCDPKV LCIINPGNPT GQVQSRKCIE
     DVIRFAAEEN LFLMADEVYQ DNVYAKGCAF HSFKKVLFEM GPKYSETLEL ASFHSTSKGY
     MGECGFRGGY MEVINMDPAV KQQLTKLVSV RLCPPVPGQV LLDVIVNPPK PGEPSYKQFI
     SEKQAVLNNL AEKARLTEEI LNQAPGIRCN PVQGAMYSFP RIHIPEKAIK LAQAEGQAPD
     MFFCMKLLEE TGICVVPGSG FGQREGTHHF RMTILPPTDK LKSLLERLKD FHQKFMDEYS