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Information on EC 1.5.99.15 - dihydromethanopterin reductase (acceptor) and Organism(s) Methanocaldococcus jannaschii and UniProt Accession Q57661

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IUBMB Comments
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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Methanocaldococcus jannaschii
UNIPROT: Q57661
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The taxonomic range for the selected organisms is: Methanocaldococcus jannaschii
The expected taxonomic range for this enzyme is: Archaea, Bacteria
Synonyms
mm1854, mj0208, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
archaeal-flavoprotein-like flavoprotein
-
MJ0208
PATHWAY SOURCE
PATHWAYS
-
-
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)+].
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
the enzyme catalyzes the last step of tetrahydromethanopterin biosynthesis
-
-
?
7,8-dihydromethanopterin + reduced dithiothreitol
5,6,7,8-tetrahydromethanopterin + oxidized dithiothreitol
show the reaction diagram
-
-
-
?
7,8-dihydromethanopterin + reduced ferredoxin
5,6,7,8-tetrahydromethanopterin + ferredoxin
show the reaction diagram
-
-
-
?
additional information
?
-
NATURAL SUBSTRATE
NATURAL 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
the enzyme catalyzes the last step of tetrahydromethanopterin biosynthesis
-
-
?
7,8-dihydromethanopterin + reduced ferredoxin
5,6,7,8-tetrahydromethanopterin + ferredoxin
show the reaction diagram
-
-
-
?
COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
Ferredoxin
ferredoxin may serve as an electron donor
-
flavin
iron-sulfur flavoprotein
FMN
the enzyme contains one flavin mononucleotide (FMN)-binding site
[4Fe-4S]-center
the enzyme contains two iron-sulfur cluster sites
additional information
-
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Fe2+
the enzyme contains two [4Fe-4S] cluster sites
Iron-sulfur cluster
iron-sulfur flavoprotein
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
22
assay at room temperature
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
metabolism
the microbial production of methane by methanogenic archaea is dependent on the synthesis of the pterin-containing cofactor tetrahydromethanopterin (H4MPT). The enzyme catalyzing the last step of H4MPT biosynthesis is dihydromethanopterin reductase
physiological function
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
100
purified recombinant His-tagged enzyme, pH 7.0, 15 min, inactivation
GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
stable when frozen in liquid nitrogen
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
recombinant His6-tagged enzyme from Escherichia col strain BE100 [BL21(DE3) RIL] in an anaerobic chamber by heat treatement at 65°C for 5 min, the supernatant is a second time heat treated at 85°C for 15 min,
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expression in Escherichia coli
gene dmrX, recombinant expression of the codon-optimized gene encoding His6-tagged enzyme in Escherichia col strain BE100 [BL21(DE3) RIL]
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Wang, S.; Tiongson, J.; Rasche, M.E.
Discovery and characterization of the first archaeal dihydromethanopterin reductase, an iron-sulfur flavoprotein from Methanosarcina mazei
J. Bacteriol.
196
203-209
2014
Methanocaldococcus jannaschii (Q57661), Methanocaldococcus jannaschii, Methanocaldococcus jannaschii DSM 2661 (Q57661), Methanosarcina mazei (Q8PVV3), Methanosarcina mazei, Methanosarcina mazei DSM 3647 (Q8PVV3)
Manually annotated by BRENDA team
Wang, S.; Tiongson, J.; Rasche, M.E.
Discovery and characterization of the first archaeal dihydromethanopterin reductase, an iron-sulfur flavoprotein from Methanosarcina mazei
J. Bacteriol.
196
203-209
2014
Methanocaldococcus jannaschii (Q57661), Methanocaldococcus jannaschii, Methanocaldococcus jannaschii DSM 2661 (Q57661), Methanosarcina mazei (Q8PVV3), Methanosarcina mazei, Methanosarcina mazei DSM 3647 (Q8PVV3)
Manually annotated by BRENDA team