Q9CCK2 · FBIB_MYCLE
- ProteinBifunctional F420 biosynthesis protein FbiB
- GenefbiB
- StatusUniProtKB reviewed (Swiss-Prot)
- Organism
- Amino acids457 (go to sequence)
- Protein existenceInferred from homology
- Annotation score4/5
Function
function
Bifunctional enzyme that catalyzes the GTP-dependent successive addition of multiple gamma-linked L-glutamates to the L-lactyl phosphodiester of 7,8-didemethyl-8-hydroxy-5-deazariboflavin (F420-0) to form polyglutamated F420 derivatives, and the FMNH2-dependent reduction of dehydro-F420-0 to form F420-0.
Catalytic activity
- GTP + L-glutamate + oxidized coenzyme F420-0 = GDP + H+ + oxidized coenzyme F420-1 + phosphate
- GTP + L-glutamate + oxidized coenzyme F420-(gamma-L-Glu)(n) = GDP + H+ + oxidized coenzyme F420-(gamma-L-Glu)(n+1) + phosphate
Cofactor
Protein has several cofactor binding sites:
Mn2+ (UniProtKB | Rhea| CHEBI:29035 )
Note: Binds 2 divalent metal cations per subunit. The ions could be magnesium and/or manganese.
Note: Monovalent cation. The ion could be potassium.
Pathway
Cofactor biosynthesis; coenzyme F420 biosynthesis.
Features
Showing features for binding site.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Binding site | 29-32 | GTP (UniProtKB | ChEBI) | ||||
Sequence: LPEF | ||||||
Binding site | 59 | GTP (UniProtKB | ChEBI) | ||||
Sequence: S | ||||||
Binding site | 64 | GTP (UniProtKB | ChEBI) | ||||
Sequence: K | ||||||
Binding site | 118 | a divalent metal cation 1 (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Binding site | 121 | GTP (UniProtKB | ChEBI) | ||||
Sequence: N | ||||||
Binding site | 159 | a divalent metal cation 1 (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Binding site | 160 | a divalent metal cation 2 (UniProtKB | ChEBI) | ||||
Sequence: T | ||||||
Binding site | 269-273 | FMN (UniProtKB | ChEBI) | ||||
Sequence: RRSVR | ||||||
Binding site | 297 | FMN (UniProtKB | ChEBI) | ||||
Sequence: A | ||||||
Binding site | 329 | coenzyme F420-(gamma-Glu)n (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Binding site | 408 | FMN (UniProtKB | ChEBI) | ||||
Sequence: G | ||||||
Binding site | 445 | FMN (UniProtKB | ChEBI) | ||||
Sequence: R |
GO annotations
Aspect | Term | |
---|---|---|
Molecular Function | coenzyme F420-0:L-glutamate ligase activity | |
Molecular Function | coenzyme F420-1:gamma-L-glutamate ligase activity | |
Molecular Function | GTP binding | |
Molecular Function | metal ion binding | |
Molecular Function | oxidoreductase activity, acting on the CH-CH group of donors, with a flavin as acceptor | |
Biological Process | F420-0 metabolic process |
Keywords
- Molecular function
- Ligand
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended nameBifunctional F420 biosynthesis protein FbiB
Including 2 domains:
- Recommended nameCoenzyme F420:L-glutamate ligase
- EC number
- Alternative names
- Recommended nameDehydro-coenzyme F420-0 reductase
- EC number
Gene names
Organism names
- Organism
- Strain
- Taxonomic lineageBacteria > Actinomycetota > Actinomycetes > Mycobacteriales > Mycobacteriaceae > Mycobacterium
Accessions
- Primary accessionQ9CCK2
Proteomes
Organism-specific databases
PTM/Processing
Features
Showing features for chain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Chain | PRO_0000145778 | 1-457 | Bifunctional F420 biosynthesis protein FbiB | |||
Sequence: MTSSDSHRSAPSPEHGTASTIEILPVAGLPEFRPGDDLSAALAAAAPWLRDGDVVVVTSKVVSKCEGRLVPAPEDTRGRNELRRKLINDETIRVLARKGRTLIIENGLGLVQAAAGVDGSNVGRGELALLPVNPDASAAVLRIGLRAMLGVNVAVVITDTMGRAWRNGQTDVAIGAAGLAVLHNYSGAVDRYGNELVVTEIAVADEVAAATDLVKGKLTAMPVAVVRGLSPTDDGSTAQHLLRNGPDDLFWLGTTEALELGRQQAQLLRRSVRQFSDEPIAAELIETAVAEALTAPAPHHTRPVRFVWLQTPAVRTRLLDRMADKWRLDLASDALPADAIAQRVARGQILYDAPEVIIPFMVPDGAHAYPDAARASAEHTMFIVAVGAAVQALLVALAVRGLGSCWIGSTIFADDLVRAELELPADWEPLGAIAIGYAHEPTDLREPVRVADLLLRK |
Interaction
Protein-protein interaction databases
Structure
Family & Domains
Features
Showing features for region.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Region | 1-253 | Coenzyme F420:L-glutamate ligase | ||||
Sequence: MTSSDSHRSAPSPEHGTASTIEILPVAGLPEFRPGDDLSAALAAAAPWLRDGDVVVVTSKVVSKCEGRLVPAPEDTRGRNELRRKLINDETIRVLARKGRTLIIENGLGLVQAAAGVDGSNVGRGELALLPVNPDASAAVLRIGLRAMLGVNVAVVITDTMGRAWRNGQTDVAIGAAGLAVLHNYSGAVDRYGNELVVTEIAVADEVAAATDLVKGKLTAMPVAVVRGLSPTDDGSTAQHLLRNGPDDLFWLG | ||||||
Region | 254-457 | Dehydro-coenzyme F420-0 reductase | ||||
Sequence: TTEALELGRQQAQLLRRSVRQFSDEPIAAELIETAVAEALTAPAPHHTRPVRFVWLQTPAVRTRLLDRMADKWRLDLASDALPADAIAQRVARGQILYDAPEVIIPFMVPDGAHAYPDAARASAEHTMFIVAVGAAVQALLVALAVRGLGSCWIGSTIFADDLVRAELELPADWEPLGAIAIGYAHEPTDLREPVRVADLLLRK |
Sequence similarities
In the N-terminal section; belongs to the CofE family.
Phylogenomic databases
Family and domain databases
Sequence
- Sequence statusComplete
- Length457
- Mass (Da)48,562
- Last updated2001-06-01 v1
- Checksum42BEF5D8A3333327
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
AL583919 EMBL· GenBank· DDBJ | CAC30267.1 EMBL· GenBank· DDBJ | Genomic DNA |