ALAT2_XENTR
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 03-AUG-2022, entry version 88.
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.ENSXETP00000015516; -.
DR PaxDb; Q28DB5; -.
DR PRIDE; Q28DB5; -.
DR GeneID; 549559; -.
DR KEGG; xtr:549559; -.
DR CTD; 2875; -.
DR Xenbase; XB-GENE-5824311; gpt.
DR eggNOG; KOG0258; Eukaryota.
DR HOGENOM; CLU_014254_3_1_1; -.
DR InParanoid; Q28DB5; -.
DR OMA; CISRILE; -.
DR OrthoDB; 477122at2759; -.
DR TreeFam; TF300839; -.
DR Reactome; R-XTR-8964540; Alanine metabolism.
DR UniPathway; UPA00528; UER00586.
DR Proteomes; UP000008143; Chromosome 6.
DR Proteomes; UP000790000; Unplaced.
DR Bgee; ENSXETG00000007140; Expressed in 2-cell stage embryo and 17 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..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