Q9HWH2 · PHZM_PSEAE
- ProteinPhenazine-1-carboxylate N-methyltransferase
- GenephzM
- StatusUniProtKB reviewed (Swiss-Prot)
- Amino acids334 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
Function
function
Involved in the biosynthesis of pyocyanine, a blue-pigmented phenazine derivative, which plays a role in virulence. Converts phenazine-1-carboxylate (PCA) to 5-methylphenazine-1-carboxylate (5-methyl-PCA).
Catalytic activity
- phenazine-1-carboxylate + S-adenosyl-L-methionine = 5-methyl-phenazine-1-carboxylate + S-adenosyl-L-homocysteine
Activity regulation
In vitro, requires PhzS for activity.
Pathway
Secondary metabolite biosynthesis; pyocyanine biosynthesis.
Features
Showing features for binding site.
GO annotations
Aspect | Term | |
---|---|---|
Molecular Function | 5-methyl-phenazine-1-carboxylate N-methyltransferase activity | |
Molecular Function | identical protein binding | |
Molecular Function | O-methyltransferase activity | |
Molecular Function | protein homodimerization activity | |
Molecular Function | S-adenosyl-L-methionine binding | |
Molecular Function | S-adenosylmethionine-dependent methyltransferase activity | |
Biological Process | methylation | |
Biological Process | pyocyanine biosynthetic process |
Keywords
- Molecular function
- Ligand
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended namePhenazine-1-carboxylate N-methyltransferase
- EC number
Gene names
Organism names
- Strain
- Taxonomic lineageBacteria > Pseudomonadota > Gammaproteobacteria > Pseudomonadales > Pseudomonadaceae > Pseudomonas
Accessions
- Primary accessionQ9HWH2
Proteomes
Organism-specific databases
Phenotypes & Variants
Miscellaneous
PTM/Processing
Features
Showing features for chain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Chain | PRO_0000441707 | 1-334 | Phenazine-1-carboxylate N-methyltransferase | |||
Sequence: MNNSNLAAARNLIQVVTGEWKSRCVYVATRLGLADLIESGIDSDETLAAAVGSDAERIHRLMRLLVAFEIFQGDTRDGYANTPTSHLLRDVEGSFRDMVLFYGEEFHAAWTPACEALLSGTPGFELAFGEDFYSYLKRCPDAGRRFLLAMKASNLAFHEIPRLLDFRGRSFVDVGGGSGELTKAILQAEPSARGVMLDREGSLGVARDNLSSLLAGERVSLVGGDMLQEVPSNGDIYLLSRIIGDLDEAASLRLLGNCREAMAGDGRVVVIERTISASEPSPMSVLWDVHLFMACAGRHRTTEEVVDLLGRGGFAVERIVDLPMETRMIVAARA |
Proteomic databases
Structure
Family & Domains
Domain
Contains an N-terminal dimerization domain. The C-terminal region contains the S-adenosyl-L-methionine binding site.
Sequence similarities
Belongs to the class I-like SAM-binding methyltransferase superfamily. Cation-independent O-methyltransferase family.
Phylogenomic databases
Family and domain databases
Sequence
- Sequence statusComplete
- Length334
- Mass (Da)36,357
- Last updated2001-03-01 v1
- Checksum27D9717ECA12A1B5
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
AE004091 EMBL· GenBank· DDBJ | AAG07596.1 EMBL· GenBank· DDBJ | Genomic DNA |