ID   ALAT2_XENTR             Reviewed;         524 AA.
AC   Q28DB5;
DT   25-JUL-2006, integrated into UniProtKB/Swiss-Prot.
DT   04-APR-2006, sequence version 1.
DT   27-MAR-2024, entry version 95.
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; ORFNames=TEgg035f04.1;
OS   Xenopus tropicalis (Western clawed frog) (Silurana tropicalis).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC   Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Silurana.
OX   NCBI_TaxID=8364;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Egg;
RG   Sanger Xenopus tropicalis EST/cDNA project;
RL   Submitted (MAR-2006) 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; CR855598; CAJ81963.1; -; mRNA.
DR   RefSeq; NP_001016805.1; NM_001016805.2.
DR   AlphaFoldDB; Q28DB5; -.
DR   SMR; Q28DB5; -.
DR   STRING; 8364.ENSXETP00000007336; -.
DR   PaxDb; 8364-ENSXETP00000015516; -.
DR   Ensembl; ENSXETT00000015516; ENSXETP00000015516; ENSXETG00000007140.
DR   GeneID; 549559; -.
DR   KEGG; xtr:549559; -.
DR   AGR; Xenbase:XB-GENE-5824311; -.
DR   CTD; 2875; -.
DR   Xenbase; XB-GENE-5824311; gpt.
DR   eggNOG; KOG0258; Eukaryota.
DR   HOGENOM; CLU_014254_3_1_1; -.
DR   InParanoid; Q28DB5; -.
DR   OrthoDB; 5472891at2759; -.
DR   TreeFam; TF300839; -.
DR   Reactome; R-XTR-8964540; Alanine metabolism.
DR   UniPathway; UPA00528; UER00586.
DR   Proteomes; UP000008143; Chromosome 6.
DR   Bgee; ENSXETG00000007140; Expressed in 2-cell stage embryo and 17 other cell types or 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   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   Aminotransferase; Pyridoxal phosphate; Reference proteome; Transferase.
FT   CHAIN           1..524
FT                   /note="Alanine aminotransferase 2"
FT                   /id="PRO_0000247536"
FT   MOD_RES         342
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   524 AA;  58311 MW;  D932C875D2BBA05E CRC64;
     MDSDLISSRC VWATWNVYNG RSLSGTPLAE RDGKVARKMS ENGTCNRILT LESMNPCIQK
     VEYAVRGPIV IRAVELEKEL QQGVKKPFTE VIKANIGDAH AMGQKPITFL RQVSAICLYP
     ELMNDNKFPE DVKQKAARIL QACGGHSIGA YSASQGIEVI RQDVAKYIER RDGGIQSDPN
     NIYLSTGASD SIVTMLKLLV SGQGKSRTGV LIPIPQYPLY SAALAELNAV QVNYYLDEEN
     CWALDINELR RSLTEARKHC DPKVLCIINP GNPTGQVQSR KCIEDVIRFA AEENLFLMAD
     EVYQDNVYAK GCTFHSFKKV LFEMGPKYSE TVELASFHST SKGYMGECGF RGGYMEVINM
     DPAVKQQLTK LVSVRLCPPV PGQALLDVIV NPPKPGEPSY KQFMAEKQAV LGNLAEKARL
     TEEILNQSPG IRCNPVQGAM YSFPRIHIPE KAIKLAQAEG QAPDMFFCMK LLEETGICVV
     PGSGFGQREG THHFRMTILP PTDKLKSLLE RLKDFHQKFT EEYS
//