| Entry |
|
|---|
| Name |
7,8-didemethyl-8-hydroxy-5-deazariboflavin synthase;
FO synthase;
fbiC (gene name) (ambiguous);
cofG (gene name)
|
|---|
| Class |
Lyases;
Carbon-nitrogen lyases;
Ammonia-lyases
|
|---|
| Sysname |
5-amino-5-(4-hydroxybenzyl)-6-(D-ribitylimino)-5,6-dihydrouracil ammonia-lyase (7,8-didemethyl-8-hydroxy-5-deazariboflavin-forming)
|
|---|
| Reaction(IUBMB) |
5-amino-5-(4-hydroxybenzyl)-6-(D-ribitylimino)-5,6-dihydrouracil + S-adenosyl-L-methionine = 7,8-didemethyl-8-hydroxy-5-deazariboflavin + NH3 + L-methionine + 5'-deoxyadenosine [RN: R12162]
|
|---|
| Reaction(KEGG) |
|
|---|
| Substrate |
5-amino-5-(4-hydroxybenzyl)-6-(D-ribitylimino)-5,6-dihydrouracil [CPD: C21971];
S-adenosyl-L-methionine [CPD: C00019]
|
|---|
| Product |
7,8-didemethyl-8-hydroxy-5-deazariboflavin [CPD: C19154];
NH3 [CPD: C00014];
L-methionine [CPD: C00073];
5'-deoxyadenosine [CPD: C05198]
|
|---|
| Comment |
The enzyme produces the 7,8-didemethyl-8-hydroxy-5-deazariboflavin (FO) precursor of the redox cofactor coenzyme F420, which is found in methanogens and in various actinobacteria. FO is also produced by some cyanobacteria and eukaryotes. The enzyme, which forms a complex with EC 2.5.1.147, 5-amino-6-(D-ribitylamino)uracil---L-tyrosine 4-hydroxyphenyl transferase, is a radical SAM enzyme that uses the 5'-deoxyadenosyl radical to catalyse the condensation reaction.
|
|---|
| History |
EC 4.3.1.32 created 2010 as EC 2.5.1.77, part transferred 2018 to EC 4.3.1.32
|
|---|
| Pathway |
| ec01120 | Microbial metabolism in diverse environments |
|
|---|
| Orthology |
| K11780 | 7,8-didemethyl-8-hydroxy-5-deazariboflavin synthase |
|
|---|
| Genes |
» show all
|
|---|
| Reference |
|
|---|
| Authors |
Decamps L, Philmus B, Benjdia A, White R, Begley TP, Berteau O |
|---|
| Title |
Biosynthesis of F0, precursor of the F420 cofactor, requires a unique two radical-SAM domain enzyme and tyrosine as substrate. |
|---|
| Journal |
|
|---|
| Reference |
|
|---|
| Authors |
Philmus B, Decamps L, Berteau O, Begley TP |
|---|
| Title |
Biosynthetic versatility and coordinated action of 5'-deoxyadenosyl radicals in deazaflavin biosynthesis. |
|---|
| Journal |
|
|---|
| Other DBs |
| ExplorEnz - The Enzyme Database: | 4.3.1.32 |
| ExPASy - ENZYME nomenclature database: | 4.3.1.32 |
|
|---|
