A0A2K3D5Z7 · CMD1_CHLRE
- Protein5-methylcytosine-modifying enzyme 1
- GeneCMD1
- StatusUniProtKB reviewed (Swiss-Prot)
- Amino acids532 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
Function
function
Dioxygenase that catalyzes DNA modification by mediating the conversion of the modified genomic base 5-methylcytosine (5mC) into 5-glyceryl-methylcytosine (5gmC) (PubMed:31043749, PubMed:33531488).
Catalyzes the conjugation of a glyceryl moiety from L-ascorbate (vitamin C) to the methyl group of 5mC through a carbon-carbon bond (PubMed:31043749, PubMed:33531488).
5gmC DNA modification may be required during photosynthesis as an epigenetic mark that couteracts DNA methylation (PubMed:31043749).
Catalyzes the conjugation of a glyceryl moiety from L-ascorbate (vitamin C) to the methyl group of 5mC through a carbon-carbon bond (PubMed:31043749, PubMed:33531488).
5gmC DNA modification may be required during photosynthesis as an epigenetic mark that couteracts DNA methylation (PubMed:31043749).
Catalytic activity
- a 5-methyl-2'-deoxycytidine in DNA + L-ascorbate + O2 = a (8S,9S)-5-glyceryl-2'-deoxycytidine in DNA + CO2 + glyoxylateThis reaction proceeds in the forward direction.
- a 5-methyl-2'-deoxycytidine in DNA + L-ascorbate + O2 = a (8S,9R)-5-glyceryl-2'-deoxycytidine in DNA + CO2 + glyoxylateThis reaction proceeds in the forward direction.
Cofactor
Note: Binds 1 Fe2+ ion per subunit.
Features
Showing features for binding site.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Binding site | 335-337 | L-ascorbate (UniProtKB | ChEBI) | ||||
Sequence: SLT | ||||||
Binding site | 345 | Fe cation (UniProtKB | ChEBI); catalytic | ||||
Sequence: H | ||||||
Binding site | 347 | Fe cation (UniProtKB | ChEBI); catalytic | ||||
Sequence: D | ||||||
Binding site | 397 | Fe cation (UniProtKB | ChEBI); catalytic | ||||
Sequence: H | ||||||
Binding site | 397-399 | L-ascorbate (UniProtKB | ChEBI) | ||||
Sequence: HGT |
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | nucleus | |
Molecular Function | dioxygenase activity | |
Molecular Function | iron ion binding | |
Molecular Function | methylcytosine to 5-glyceryl-methylcytosine dioxygenase activity | |
Biological Process | 5-methylcytosine catabolic process | |
Biological Process | regulation of photosynthesis |
Keywords
- Molecular function
- Ligand
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended name5-methylcytosine-modifying enzyme 1
- EC number
- Short names5mC-modifying enzyme 1
- Alternative names
Gene names
Organism names
- Strain
- Taxonomic lineageEukaryota > Viridiplantae > Chlorophyta > core chlorophytes > Chlorophyceae > CS clade > Chlamydomonadales > Chlamydomonadaceae > Chlamydomonas
Accessions
- Primary accessionA0A2K3D5Z7
Proteomes
Genome annotation databases
Subcellular Location
Phenotypes & Variants
Disruption phenotype
Decreased 5-glyceryl-methylcytosines (5gmC) DNA modification in the genome (PubMed:31043749).
Reduced fitness of cells during exposure to high light levels (PubMed:31043749).
Defects may be caused by hypermethylation and down-regulation of LHCSR3, a protein-coding gene required for the protection of C.reinhardtii cells from photo-oxidative damage under high light conditions, causing a reduced capacity for photoprotective non-photochemical quenching (PubMed:31043749).
Reduced fitness of cells during exposure to high light levels (PubMed:31043749).
Defects may be caused by hypermethylation and down-regulation of LHCSR3, a protein-coding gene required for the protection of C.reinhardtii cells from photo-oxidative damage under high light conditions, causing a reduced capacity for photoprotective non-photochemical quenching (PubMed:31043749).
Features
Showing features for mutagenesis.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Mutagenesis | 330 | Abolished dioxygenase activity. | ||||
Sequence: A → V | ||||||
Mutagenesis | 345 | Abolished dioxygenase activity. | ||||
Sequence: H → A | ||||||
Mutagenesis | 347 | Abolished dioxygenase activity. | ||||
Sequence: D → A | ||||||
Mutagenesis | 350 | Abolished dioxygenase activity. | ||||
Sequence: D → A |
PTM/Processing
Features
Showing features for chain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Chain | PRO_0000447622 | 1-532 | 5-methylcytosine-modifying enzyme 1 | |||
Sequence: MSVALASEYQLVQNAQLPQRWSQSARKSLAILEATARKEATAQMEAAGGSFCGQFPVDPAFKVLSLEYSAPNPDIARAIRRVDSVPNPPLPSHVVAIQSTAVDADLSLAMGVSLTPGRHTSYLVDARALQQSNSAAVAARKADGDKWGPACDEMFRGCRCVTGQEVVFYTAVKEPAGEVEGGEGSLFKPSFDGPAFRPSWGELSGKATGVVACVLQVPIGKETDIICAEYDNLVSKGQFATVDRFGGDHTVNMTGNALIQNDGKAISKGYAVAHRARVTSNVYGKANDVSLQRLAETVWSVVEKRLSFMPAYRDLVITEQGKPFMLGATATNIISLTENQGVMLHLDTDDGVWTIILWFHRHSGIIAGGEFVLPSLGISFQPLDFTIVVFAANTIVHGTRPLQTTGKIIRWGSSHFLRFKDVNALAQLGAAYGVDELDAKQRDQLEEVDAANSKDGVGAARRVASCMAAERKAAIEAQKAACVRGVVMNPCTGRMPSLLFWQVWRKPPALAVRANAVAGKKRAAADVDFCGA |
Proteomic databases
Expression
Gene expression databases
Interaction
Protein-protein interaction databases
Structure
Family & Domains
Sequence
- Sequence statusComplete
- Length532
- Mass (Da)56,994
- Last updated2018-03-28 v1
- Checksum0F3EC0A73B698B1B
Computationally mapped potential isoform sequences
There are 2 potential isoforms mapped to this entry
Entry | Entry name | Gene name | Length | ||
---|---|---|---|---|---|
A0A2K3D5Z8 | A0A2K3D5Z8_CHLRE | CHLRE_12g553400v5 | 489 | ||
A0A2K3CT20 | A0A2K3CT20_CHLRE | CHLRE_12g553400v5 | 423 |
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
CM008973 EMBL· GenBank· DDBJ | PNW75956.1 EMBL· GenBank· DDBJ | Genomic DNA |