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

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The expected taxonomic range for this enzyme is: Eukaryota, Archaea, Bacteria

EC NUMBER
COMMENTARY hide
2.5.1.77
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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
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PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
factor 420 biosynthesis
Methane metabolism
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Microbial metabolism in diverse environments
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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
Q57888: FO synthase subunit 1 (cofG), Q58826: FO synthase subunit 2 (cofH)
Q57888 and Q58826
SwissProt
Manually annotated by BRENDA team
strain BCG
SwissProt
Manually annotated by BRENDA team
strain MC2 155
SwissProt
Manually annotated by BRENDA team
strain MC2 155
SwissProt
Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
physiological function
expression of a PHR1 cDNA in Escherichia coli produces a protein that generates a molecule with characteristics similar to 7,8-didemethyl-8-hydroxy-5-deazariboflavin
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
additional information
?
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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
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additional information
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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
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
histidine-tagged FbiC overexpressed in Escherichia coli
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