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Protein

Alanine aminotransferase 1

Gene

GPT

Organism
Sus scrofa (Pig)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Catalyzes the reversible transamination between alanine and 2-oxoglutarate to form pyruvate and glutamate. Participates in cellular nitrogen metabolism and also in liver gluconeogenesis starting with precursors transported from skeletal muscles (By similarity).By similarity

Catalytic activityi

L-alanine + 2-oxoglutarate = pyruvate + L-glutamate.

Cofactori

Pathwayi

GO - Molecular functioni

  1. L-alanine:2-oxoglutarate aminotransferase activity Source: UniProtKB-EC

GO - Biological processi

  1. L-alanine catabolic process Source: UniProtKB-UniPathway
Complete GO annotation...

Keywords - Molecular functioni

Aminotransferase, Transferase

Keywords - Ligandi

Pyridoxal phosphate

Enzyme and pathway databases

ReactomeiREACT_215786. Amino acid synthesis and interconversion (transamination).
SABIO-RKP13191.
UniPathwayiUPA00528; UER00586.

Names & Taxonomyi

Protein namesi
Recommended name:
Alanine aminotransferase 1 (EC:2.6.1.2)
Short name:
ALT1
Alternative name(s):
Glutamate pyruvate transaminase 1
Short name:
GPT 1
Glutamic--alanine transaminase 1
Glutamic--pyruvic transaminase 1
Gene namesi
Name:GPT
Synonyms:AAT1, GPT1
OrganismiSus scrofa (Pig)
Taxonomic identifieri9823 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaLaurasiatheriaCetartiodactylaSuinaSuidaeSus
ProteomesiUP000008227: Unplaced

Subcellular locationi

GO - Cellular componenti

  1. cytoplasm Source: UniProtKB-SubCell
  2. extracellular vesicular exosome Source: Ensembl
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini‹1 – ›20›20Alanine aminotransferase 1PRO_0000123935Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei11 – 111N6-(pyridoxal phosphate)lysine
Glycosylationi11 – 111N-linked (Glc) (glycation); in vitro

Post-translational modificationi

Glycation of Lys-11 inactivates the enzyme.

Keywords - PTMi

Glycation, Glycoprotein

Proteomic databases

PaxDbiP13191.

Interactioni

Subunit structurei

Homodimer.

Protein-protein interaction databases

STRINGi9823.ENSSSCP00000006308.

Family & Domainsi

Sequence similaritiesi

Phylogenomic databases

eggNOGiCOG0436.

Sequencei

Sequence statusi: Fragment.

P13191-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20
QELASFHSVS KGFMGECGFR
Length:20
Mass (Da):2,218
Last modified:January 1, 1990 - v1
Checksum:i1C2243A373EC4801
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Non-terminal residuei1 – 11
Non-terminal residuei20 – 201

Sequence databases

PIRiA14344.

Cross-referencesi

Sequence databases

PIRiA14344.

3D structure databases

ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi9823.ENSSSCP00000006308.

Proteomic databases

PaxDbiP13191.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Phylogenomic databases

eggNOGiCOG0436.

Enzyme and pathway databases

UniPathwayiUPA00528; UER00586.
ReactomeiREACT_215786. Amino acid synthesis and interconversion (transamination).
SABIO-RKP13191.

Family and domain databases

ProtoNetiSearch...

Publicationsi

  1. "Pyridoxal 5'-phosphate binding site of pig heart alanine aminotransferase."
    Tanase S., Kojima H., Morino Y.
    Biochemistry 18:3002-3007(1979) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE.
    Tissue: Heart.
  2. "Inhibitory effect of glycation on catalytic activity of alanine aminotransferase."
    Beranek M., Drsata J., Palicka V.
    Mol. Cell. Biochem. 218:35-39(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: GLYCATION AT LYS-11.

Entry informationi

Entry nameiALAT1_PIG
AccessioniPrimary (citable) accession number: P13191
Entry historyi
Integrated into UniProtKB/Swiss-Prot: January 1, 1990
Last sequence update: January 1, 1990
Last modified: January 7, 2015
This is version 81 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  2. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.