Q52718 · APBEF_RHOCA
- ProteinFAD:protein FMN transferase
- GenernfF
- StatusUniProtKB reviewed (Swiss-Prot)
- Amino acids523 (go to sequence)
- Protein existenceInferred from homology
- Annotation score3/5
Function
function
Flavin transferase that catalyzes the transfer of the FMN moiety of FAD and its covalent binding to the hydroxyl group of a threonine residue in a target flavoprotein (By similarity).
Is likely involved in the modification of RnfG and RnfD. Required for nitrogen fixation (PubMed:8264535).
Is likely involved in the modification of RnfG and RnfD. Required for nitrogen fixation (PubMed:8264535).
Catalytic activity
- L-threonyl-[protein] + FAD = FMN-L-threonyl-[protein] + AMP + H+
Cofactor
Features
Showing features for binding site.
Type | ID | Position(s) | Description | ||
---|---|---|---|---|---|
Binding site | 277-279 | FAD (UniProtKB | ChEBI) | |||
Binding site | 336 | FAD (UniProtKB | ChEBI) | |||
Binding site | 339 | Mg2+ (UniProtKB | ChEBI) | |||
Binding site | 342 | FAD (UniProtKB | ChEBI) | |||
Binding site | 423-425 | FAD (UniProtKB | ChEBI) | |||
Binding site | 450 | Mg2+ (UniProtKB | ChEBI) | |||
Binding site | 454 | Mg2+ (UniProtKB | ChEBI) | |||
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | plasma membrane | |
Molecular Function | metal ion binding | |
Molecular Function | transferase activity | |
Biological Process | nitrogen fixation |
Keywords
- Molecular function
- Biological process
- Ligand
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended nameFAD:protein FMN transferase
- EC number
- Alternative names
Gene names
Organism names
- Strain
- Taxonomic lineageBacteria > Pseudomonadota > Alphaproteobacteria > Rhodobacterales > Rhodobacter group > Rhodobacter
Accessions
- Primary accessionQ52718
Subcellular Location
UniProt Annotation
GO Annotation
Cell membrane ; Multi-pass membrane protein
Features
Showing features for transmembrane.
Type | ID | Position(s) | Description | ||
---|---|---|---|---|---|
Transmembrane | 88-108 | Helical | |||
Transmembrane | 118-138 | Helical | |||
Transmembrane | 169-189 | Helical | |||
Keywords
- Cellular component
PTM/Processing
Features
Showing features for chain.
Type | ID | Position(s) | Description | ||
---|---|---|---|---|---|
Chain | PRO_0000097379 | 1-523 | FAD:protein FMN transferase | ||
Structure
Family & Domains
Sequence similarities
In the N-terminal section; belongs to the RseC family.
In the C-terminal section; belongs to the ApbE family.
Keywords
- Domain
Family and domain databases
Sequence
- Sequence statusComplete
- Length523
- Mass (Da)54,143
- Last updated1996-11-01 v1
- MD5 ChecksumCB41649DC594152550A96679331FCBB6
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
X72888 EMBL· GenBank· DDBJ | CAA51405.1 EMBL· GenBank· DDBJ | Genomic DNA |