C1AZI2 · C1AZI2_RHOOB
- ProteinFO synthase
- GenefbiC
- StatusUniProtKB unreviewed (TrEMBL)
- Organism
- Amino acids869 (go to sequence)
- Protein existenceInferred from homology
- Annotation score3/5
Function
function
Catalyzes the radical-mediated synthesis of 7,8-didemethyl-8-hydroxy-5-deazariboflavin (FO) from 5-amino-6-(D-ribitylamino)uracil and L-tyrosine.
Catalytic activity
- 5-amino-5-(4-hydroxybenzyl)-6-(D-ribitylimino)-5,6-dihydrouracil + S-adenosyl-L-methionine = 5'-deoxyadenosine + 7,8-didemethyl-8-hydroxy-5-deazariboflavin + H+ + L-methionine + NH4+
Cofactor
Pathway
Cofactor biosynthesis; coenzyme F0 biosynthesis.
GO annotations
Aspect | Term | |
---|---|---|
Molecular Function | 4 iron, 4 sulfur cluster binding | |
Molecular Function | 5-amino-6-(D-ribitylamino)uracil--L-tyrosine 4-hydroxyphenyl transferase activity | |
Molecular Function | 7,8-didemethyl-8-hydroxy-5-deazariboflavin synthase activity | |
Molecular Function | metal ion binding |
Keywords
- Ligand
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended nameFO synthase
- EC number
Gene names
Organism names
- Organism
- Strain
- Taxonomic lineageBacteria > Actinomycetota > Actinomycetes > Mycobacteriales > Nocardiaceae > Rhodococcus
Accessions
- Primary accessionC1AZI2
Proteomes
Interaction
Protein-protein interaction databases
Structure
Family & Domains
Features
Showing features for region, domain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Region | 1-29 | Disordered | ||||
Sequence: MTHSGEESGRPTMLPMPGVPAAPPSGASA | ||||||
Domain | 92-343 | Radical SAM core | ||||
Sequence: VTYSRKVFIPLTRLCRDKCHYCTFVTVPGKLRAEGRGAYLEPDEVLEIARQGAELGCKEALFTLGDRPEDRWPEAKQWLDERGYDSTLDYLRAMSIRVLEETGLLPHLNPGVMSWEEISRLKPVAPSMGMMLETTSTRLFTDKGECHYGSPDKDPAVRLRTLTDAGRLSVPFTTGILVGIGETVRERAESIMAIRKSHKAFGHIQEVIVQNFLAKPDTAMRDAPDAGLEEFRAAIAVSRLLLGPGMRIQSPP | ||||||
Region | 429-448 | Disordered | ||||
Sequence: QTGLAKPGTRPVGLPWQEPD | ||||||
Domain | 552-788 | Radical SAM core | ||||
Sequence: VTYVVNRNINFTNICYTGCRFCAFAQRKGDADAFTLSTDQVADRAWEAHVAGATEVCMQGGIDPELPVTGYADLVRAVKARVPSMHVHAFSPMEIVNGASRGGQSIRDWLTELREAGLDTIPGTAAEILDDEVRWVLTKGKLPTATWVEVVTTAHEVGLRSSSTMMYGHVDNPRHWVGHLRVLSGIQDRTGGFTEFVPLPFVHQSAPLYLAGASRPGPTNRDNRAVHALARIMLHGR | ||||||
Region | 848-869 | Disordered | ||||
Sequence: IGRPARERTTTHARREGRSPAA |
Sequence similarities
In the C-terminal section; belongs to the radical SAM superfamily. CofH family.
In the N-terminal section; belongs to the radical SAM superfamily. CofG family.
Phylogenomic databases
Family and domain databases
Sequence
- Sequence statusComplete
- Length869
- Mass (Da)93,950
- Last updated2009-05-26 v1
- Checksum34FECCE8B1B29947
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
AP011115 EMBL· GenBank· DDBJ | BAH54253.1 EMBL· GenBank· DDBJ | Genomic DNA |