| Entry |
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| Name |
5-amino-6-(D-ribitylamino)uracil---L-tyrosine 4-hydroxyphenyl transferase;
cofH (gene name);
cbiF (gene name) (ambiguous)
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| Class |
Transferases;
Transferring alkyl or aryl groups, other than methyl groups;
Transferring alkyl or aryl groups, other than methyl groups (only sub-subclass identified to date)
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| Sysname |
5-amino-6-(D-ribitylamino)uracil:L-tyrosine, 4-hydroxyphenyl transferase
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| Reaction(IUBMB) |
5-amino-6-(D-ribitylamino)uracil + L-tyrosine + S-adenosyl-L-methionine = 5-amino-5-(4-hydroxybenzyl)-6-(D-ribitylimino)-5,6-dihydrouracil + 2-iminoacetate + L-methionine + 5'-deoxyadenosine [RN: R12161]
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| Reaction(KEGG) |
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| Substrate |
5-amino-6-(D-ribitylamino)uracil [CPD: C04732];
L-tyrosine [CPD: C00082];
S-adenosyl-L-methionine [CPD: C00019]
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| Product |
5-amino-5-(4-hydroxybenzyl)-6-(D-ribitylimino)-5,6-dihydrouracil [CPD: C21971];
2-iminoacetate [CPD: C15809];
L-methionine [CPD: C00073];
5'-deoxyadenosine [CPD: C05198]
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| Comment |
The enzyme is involved in the production of 7,8-didemethyl-8-hydroxy-5-deazariboflavin (FO), the 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 4.3.1.32, 7,8-didemethyl-8-hydroxy-5-deazariboflavin synthase, is a radical SAM enzyme that uses the 5'-deoxyadenosyl radical to initiate the reaction.
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| History |
EC 2.5.1.147 created 2010 as EC 2.5.1.77, part transferred 2018 to EC 2.5.1.147
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| Pathway |
| ec01120 | Microbial metabolism in diverse environments |
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| Orthology |
| K11781 | 5-amino-6-(D-ribitylamino)uracil---L-tyrosine 4-hydroxyphenyl transferase |
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| Genes |
» show all
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| Reference |
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| Authors |
Decamps L, Philmus B, Benjdia A, White R, Begley TP, Berteau O |
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| Title |
Biosynthesis of F0, precursor of the F420 cofactor, requires a unique two radical-SAM domain enzyme and tyrosine as substrate. |
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| Journal |
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| Reference |
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| Authors |
Philmus B, Decamps L, Berteau O, Begley TP |
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| Title |
Biosynthetic versatility and coordinated action of 5'-deoxyadenosyl radicals in deazaflavin biosynthesis. |
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| Journal |
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| Other DBs |
| ExPASy - ENZYME nomenclature database: | 2.5.1.147 |
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