A0A4R3YRR0 · A0A4R3YRR0_9GAMM
- ProteinFAD:protein FMN transferase
- StatusUniProtKB unreviewed (TrEMBL)
- Organism
- Amino acids338 (go to sequence)
- Protein existenceInferred from homology
- Annotation score2/5
Function
Catalytic activity
- L-threonyl-[protein] + FAD = FMN-L-threonyl-[protein] + AMP + H+
Cofactor
Mn2+ (UniProtKB | Rhea| CHEBI:29035 )
Note: Magnesium. Can also use manganese.
Features
Showing features for binding site.
Type | ID | Position(s) | Description | ||
---|---|---|---|---|---|
Binding site | 169 | Mg2+ (UniProtKB | ChEBI) | |||
Binding site | 289 | Mg2+ (UniProtKB | ChEBI) | |||
Binding site | 293 | Mg2+ (UniProtKB | ChEBI) | |||
GO annotations
Aspect | Term | |
---|---|---|
Molecular Function | metal ion binding | |
Molecular Function | transferase activity | |
Biological Process | protein flavinylation |
Keywords
- Molecular function
- Ligand
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended nameFAD:protein FMN transferase
- EC number
- Alternative names
Gene names
Organism names
- Organism
- Strain
- Taxonomic lineageBacteria > Pseudomonadota > Gammaproteobacteria > Lysobacterales > Rhodanobacteraceae > Luteibacter
Accessions
- Primary accessionA0A4R3YRR0
Proteomes
PTM/Processing
Features
Showing features for signal, chain.
Type | ID | Position(s) | Description | ||
---|---|---|---|---|---|
Signal | 1-18 | ||||
Chain | PRO_5039918163 | 19-338 | FAD:protein FMN transferase | ||
Keywords
- PTM
Structure
Sequence
- Sequence statusComplete
- Length338
- Mass (Da)36,303
- Last updated2019-07-31 v1
- MD5 Checksum4EDF68EBBADCBA107336ABA75E7CC45B
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
SMCS01000002 EMBL· GenBank· DDBJ | TCV95665.1 EMBL· GenBank· DDBJ | Genomic DNA |