Information on EC 1.5.99.15 - dihydromethanopterin reductase (acceptor)

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The expected taxonomic range for this enzyme is: Euryarchaeota

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EC NUMBER
COMMENTARY hide
1.5.99.15
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RECOMMENDED NAME
GeneOntology No.
dihydromethanopterin reductase (acceptor)
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REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
5,6,7,8-tetrahydromethanopterin + oxidized acceptor = 7,8-dihydromethanopterin + reduced acceptor
show the reaction diagram
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PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
Folate biosynthesis
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tetrahydromethanopterin biosynthesis
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methanogenesis from CO2
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SYSTEMATIC NAME
IUBMB Comments
5,6,7,8-tetrahydromethanopterin:acceptor 5,6-oxidoreductase
This archaeal enzyme catalyses the last step in the biosynthesis of tetrahydromethanopterin, a coenzyme used in methanogenesis. The enzyme, characterized from the archaea Methanosarcina mazei and Methanocaldococcus jannaschii, is an iron-sulfur flavoprotein. cf. EC 1.5.1.47, dihydromethanopterin reductase [NAD(P)+].
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ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
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GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
physiological function
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SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
7,8-dihydromethanopterin + reduced acceptor
5,6,7,8-tetrahydromethanopterin + oxidized acceptor
show the reaction diagram
7,8-dihydromethanopterin + reduced dithiothreitol
5,6,7,8-tetrahydromethanopterin + oxidized dithiothreitol
show the reaction diagram
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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
7,8-dihydromethanopterin + reduced acceptor
5,6,7,8-tetrahydromethanopterin + oxidized acceptor
show the reaction diagram
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COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
flavin
iron-sulfur flavoprotein
FMN
bioinformatic analysis reveals the presence of one FMN-binding site. The purified protein shows an absorbance peaks at 380 and 460 nm, characteristic of oxidized FMN
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METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Iron-sulfur cluster
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MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
29000
2 * 29000, SDS-PAGE
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SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
homodimer
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GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
stable when frozen in liquid nitrogen
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STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
labile when exposed to cold storage at 4°C and 20°C or liquid nitrogen temperatures
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Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
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Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
expression in Escherichia coli
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LINKS TO OTHER DATABASES (specific for EC-Number 1.5.99.15)
ExplorEnz
ExPASy
KEGG
MetaCyc
SABIO-RK
NCBI: PubMed, Protein, Nucleotide, Structure, Genome, OMIM
IUBMB Enzyme Nomenclature
PROSITE Database of protein families and domains
SYSTERS
Protein Mutant Database
InterPro (database of protein families, domains and functional sites)