A0QKC8 · FBIB_MYCA1
- ProteinBifunctional F420 biosynthesis protein FbiB
- GenefbiB
- StatusUniProtKB reviewed (Swiss-Prot)
- Organism
- Amino acids449 (go to sequence)
- Protein existenceInferred from homology
- Annotation score3/5
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 | 21-24 | GTP (UniProtKB | ChEBI) | ||||
Sequence: LPEF | ||||||
Binding site | 51 | GTP (UniProtKB | ChEBI) | ||||
Sequence: S | ||||||
Binding site | 56 | GTP (UniProtKB | ChEBI) | ||||
Sequence: K | ||||||
Binding site | 110 | a divalent metal cation 1 (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Binding site | 113 | GTP (UniProtKB | ChEBI) | ||||
Sequence: N | ||||||
Binding site | 151 | a divalent metal cation 1 (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Binding site | 152 | a divalent metal cation 2 (UniProtKB | ChEBI) | ||||
Sequence: T | ||||||
Binding site | 261-265 | FMN (UniProtKB | ChEBI) | ||||
Sequence: RRSVR | ||||||
Binding site | 289 | FMN (UniProtKB | ChEBI) | ||||
Sequence: A | ||||||
Binding site | 321 | coenzyme F420-(gamma-Glu)n (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Binding site | 400 | FMN (UniProtKB | ChEBI) | ||||
Sequence: G | ||||||
Binding site | 437 | 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 > Mycobacterium avium complex (MAC)
Accessions
- Primary accessionA0QKC8
Proteomes
PTM/Processing
Features
Showing features for chain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Chain | PRO_1000067260 | 1-449 | Bifunctional F420 biosynthesis protein FbiB | |||
Sequence: MSPAGEHGTAAPIEILPVAGLPEFRPGDDLGAAVAKAAPWLRDGDVVVVTSKAVSKCEGRLVPAPADPEERDRLRRKLVDEEAVRVLARKGRTLITENRHGLVQAAAGVDGSNVGRDELALLPLDPDASAAALRARLRELLGVEVAVLVTDTMGRAWRNGQTDAAVGAAGLAVLHGYSGAVDQHGNELLVTEVAIADEIAAAADLVKGKLTAMPVAVVRGLSVTDDGSTARQLLRPGTEDLFWLGTAEAIELGRRQAQLLRRSVRRFSAEPVPAELVREAVAEALTAPAPHHTRPVRFVWLQTPAVRTRLLDAMKDKWRADLAGDGRPAESIERRVARGQILYDAPEVVIPMLVPDGAHSYPDAARTDAEHTMFTVAVGAAVQALLVGLAVRGLGSCWIGSTIFAADLVRAVLGLPADWEPLGAIAIGYAAEPAGPRDPADPGDLLIRK |
Structure
Family & Domains
Features
Showing features for region.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Region | 1-245 | Coenzyme F420:L-glutamate ligase | ||||
Sequence: MSPAGEHGTAAPIEILPVAGLPEFRPGDDLGAAVAKAAPWLRDGDVVVVTSKAVSKCEGRLVPAPADPEERDRLRRKLVDEEAVRVLARKGRTLITENRHGLVQAAAGVDGSNVGRDELALLPLDPDASAAALRARLRELLGVEVAVLVTDTMGRAWRNGQTDAAVGAAGLAVLHGYSGAVDQHGNELLVTEVAIADEIAAAADLVKGKLTAMPVAVVRGLSVTDDGSTARQLLRPGTEDLFWLG | ||||||
Region | 246-449 | Dehydro-coenzyme F420-0 reductase | ||||
Sequence: TAEAIELGRRQAQLLRRSVRRFSAEPVPAELVREAVAEALTAPAPHHTRPVRFVWLQTPAVRTRLLDAMKDKWRADLAGDGRPAESIERRVARGQILYDAPEVVIPMLVPDGAHSYPDAARTDAEHTMFTVAVGAAVQALLVGLAVRGLGSCWIGSTIFAADLVRAVLGLPADWEPLGAIAIGYAAEPAGPRDPADPGDLLIRK |
Sequence similarities
In the N-terminal section; belongs to the CofE family.
Phylogenomic databases
Family and domain databases
Sequence
- Sequence statusComplete
- Length449
- Mass (Da)47,396
- Last updated2007-01-09 v1
- Checksum2338D44B7B2B5957
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
CP000479 EMBL· GenBank· DDBJ | ABK64439.1 EMBL· GenBank· DDBJ | Genomic DNA |