Information on EC 2.5.1.77 - 7,8-didemethyl-8-hydroxy-5-deazariboflavin synthase

for references in articles please use BRENDA:EC2.5.1.77
Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
Specify your search results
Select one or more organisms in this record:

The enzyme appears in viruses and cellular organisms

EC NUMBER
COMMENTARY hide
2.5.1.77
-
RECOMMENDED NAME
GeneOntology No.
7,8-didemethyl-8-hydroxy-5-deazariboflavin synthase
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
5-amino-6-(D-ribitylamino)uracil + 3-(4-hydroxyphenyl)pyruvate + 2 S-adenosyl-L-methionine + H2O = 7,8-didemethyl-8-hydroxy-5-deazariboflavin + 2 L-methionine + 2 5'-deoxyadenosine + oxalate + NH3
show the reaction diagram
PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
factor 420 biosynthesis
-
-
Methane metabolism
-
-
Microbial metabolism in diverse environments
-
-
SYSTEMATIC NAME
IUBMB Comments
5-amino-6-(1-D-ribitylamino)-2,4(1H,3H)-pyrimidinedione:4-hydroxyphenylpyruvate, 4-methylphenol transferase
Binds a [4Fe-4S] cluster. The cluster is coordinated by 3 cysteines and an exchangeable AdoMet molecule. The first stage of catalysis is reduction of the 2 AdoMet to produce 2 methionine and 2 5'-deoxyadenosin-5-yl radicals that extract a hydrogen from each of the substrates permitting the condensation of the two [1]. The overall reaction catalysed is the transfer of the hydroxybenzyl group from 4-hydroxyphenylpyruvate (HPP) to 5-amino-6-ribitylaminopyrimidine-2,4(1H,3H)-dione to form 7,8-didemethyl-8-hydroxy-5-deazariboflavin (FO). 7,8-Didemethyl-8-hydroxy-5-deazariboflavin is the chromophore of the hydride carrier coenzyme F420 [1].
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
-
SwissProt
Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
metabolism
physiological function
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
5-amino-6-(1-D-ribitylamino)-2,4(1H,3H)-pyrimidinedione + 4-hydroxyphenylpyruvate + H2O
7,8-didemethyl-8-hydroxy-5-deazariboflavin + oxalate + NH3 + 4 H+
show the reaction diagram
5-amino-6-(D-ribitylamino)uracil + 3-(4-hydroxyphenyl)pyruvate + 2 S-adenosyl-L-methionine + H2O
7,8-didemethyl-8-hydroxy-5-deazariboflavin + 2 L-methionine + 2 5'-deoxyadenosine + oxalate + NH3
show the reaction diagram
additional information
?
-
NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
5-amino-6-(1-D-ribitylamino)-2,4(1H,3H)-pyrimidinedione + 4-hydroxyphenylpyruvate + H2O
7,8-didemethyl-8-hydroxy-5-deazariboflavin + oxalate + NH3 + 4 H+
show the reaction diagram
Q57888 and Q58826
synthesis of 7,8-didemethyl-8-hydroxy-5-deazariboflavin, the chromophore of the hydride carrier coenzyme F420. Radical-mediated transfer of the hydroxybenzyl group from 4-hydroxyphenylpyruvate
-
-
?
5-amino-6-(D-ribitylamino)uracil + 3-(4-hydroxyphenyl)pyruvate + 2 S-adenosyl-L-methionine + H2O
7,8-didemethyl-8-hydroxy-5-deazariboflavin + 2 L-methionine + 2 5'-deoxyadenosine + oxalate + NH3
show the reaction diagram
additional information
?
-
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Fe2+
Q57888 and Q58826
CofG and CofH have putative radical S-adenosylmethionine binding motifs, preincubation with S-adenosylmethionine, Fe2+, sulfide, and dithionite stimulates production of 7,8-didemethyl-8-hydroxy-5-deazariboflavin
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
S-adenosyl-L-methionine
Q57888 and Q58826
CofG and CofH have putative radical S-adenosylmethionine binding motifs, preincubation with S-adenosylmethionine, Fe2+, sulfide, and dithionite stimulates production of 7,8-didemethyl-8-hydroxy-5-deazariboflavin
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
sequence shows an N-terminal extension containing a chloroplast transit peptide
Manually annotated by BRENDA team
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
40000
Q57888 and Q58826
1 * 42000 (CofG) + 1 * 40000 (CofH), SDS-PAGE
40806
Q57888 and Q58826
1 * 41985 (CofG) + 1 * 40806 (CofH), calculated from sequence
41985
Q57888 and Q58826
1 * 41985 (CofG) + 1 * 40806 (CofH), calculated from sequence
42000
Q57888 and Q58826
1 * 42000 (CofG) + 1 * 40000 (CofH), SDS-PAGE
111500
x * 114100, calculated, x * 111500, SDS-PAGE
114100
x * 114100, calculated, x * 111500, SDS-PAGE
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
?
x * 114100, calculated, x * 111500, SDS-PAGE
dimer
Q57888 and Q58826
1 * 41985 (CofG) + 1 * 40806 (CofH), calculated from sequence; 1 * 42000 (CofG) + 1 * 40000 (CofH), SDS-PAGE
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
proteolytic modification
sequence shows an N-terminal extension containing a chloroplast transit peptide
Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
expression in Escherichia coli
expression in Escherichia coli, cofG and polyhistidine-tagged cofH are co-expressed
Q57888 and Q58826
gene cofG, DNA and amino acid sequence determination and analysis, phylogenetic analysis; gene cofH, DNA and amino acid sequence determination and analysis, phylogenetic analysis
histidine-tagged FbiC overexpressed in Escherichia coli
Show AA Sequence (1339 entries)
Please use the Sequence Search for a specific query.