A0A1B3PDD1 · A0A1B3PDD1_POLVA
- ProteinGlycine N-methyltransferase
- GeneGsmt1
- StatusUniProtKB unreviewed (TrEMBL)
- Amino acids319 (go to sequence)
- Protein existenceEvidence at transcript level
- Annotation score3/5
Function
Catalytic activity
- glycine + S-adenosyl-L-methionine = sarcosine + S-adenosyl-L-homocysteine + H+This reaction proceeds in the forward direction.
Features
Showing features for binding site.
Type | ID | Position(s) | Description | ||
---|---|---|---|---|---|
Binding site | 21 | S-adenosyl-L-methionine (UniProtKB | ChEBI) | |||
Binding site | 30 | S-adenosyl-L-methionine (UniProtKB | ChEBI) | |||
Binding site | 40 | S-adenosyl-L-methionine (UniProtKB | ChEBI) | |||
Binding site | 64 | S-adenosyl-L-methionine (UniProtKB | ChEBI) | |||
Binding site | 85 | S-adenosyl-L-methionine (UniProtKB | ChEBI) | |||
Binding site | 116-117 | S-adenosyl-L-methionine (UniProtKB | ChEBI) | |||
Binding site | 138 | S-adenosyl-L-methionine (UniProtKB | ChEBI) | |||
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | cytosol | |
Molecular Function | folic acid binding | |
Molecular Function | glycine binding | |
Molecular Function | glycine N-methyltransferase activity | |
Molecular Function | identical protein binding | |
Molecular Function | S-adenosyl-L-methionine binding | |
Biological Process | methylation | |
Biological Process | one-carbon metabolic process | |
Biological Process | protein homotetramerization | |
Biological Process | regulation of gluconeogenesis | |
Biological Process | S-adenosylhomocysteine metabolic process | |
Biological Process | S-adenosylmethionine metabolic process | |
Biological Process | sarcosine metabolic process |
Keywords
- Molecular function
- Ligand
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended nameGlycine N-methyltransferase
- EC number
Gene names
Organism names
- Taxonomic lineageEukaryota > Metazoa > Ecdysozoa > Arthropoda > Hexapoda > Insecta > Pterygota > Neoptera > Endopterygota > Diptera > Nematocera > Chironomoidea > Chironomidae > Chironominae > Polypedilum > Polypedilum
Accessions
- Primary accessionA0A1B3PDD1
Subcellular Location
UniProt Annotation
GO Annotation
Structure
Sequence
- Sequence statusFragment
- Length319
- Mass (Da)36,585
- Last updated2016-11-02 v1
- Checksum3C0AFAB8BA0CE9CD
Features
Showing features for non-terminal residue.
Type | ID | Position(s) | Description | ||
---|---|---|---|---|---|
Non-terminal residue | 319 | ||||
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
KU659938 EMBL· GenBank· DDBJ | AOG17737.1 EMBL· GenBank· DDBJ | mRNA |