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Information on EC 4.1.3.44 - tRNA 4-demethylwyosine synthase (AdoMet-dependent) and Organism(s) Pyrococcus abyssi and UniProt Accession Q9V1F9

for references in articles please use BRENDA:EC4.1.3.44
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EC Tree
     4 Lyases
         4.1 Carbon-carbon lyases
             4.1.3 Oxo-acid-lyases
                4.1.3.44 tRNA 4-demethylwyosine synthase (AdoMet-dependent)
IUBMB Comments
This enzyme, which is a member of the superfamily of S-adenosyl-L-methionine-dependent radical (radical AdoMet) enzymes, binds two [4Fe-4S] clusters [3,4]. Carbons C2 and C3 from pyruvate are incorporated into 4-demethylwyosine . The enzyme is found in eukaryotes where it is part of the pathway for wybutosine synthesis, and in archaea, where it is involved in the biosynthesis of archaeal wye bases, such as wyosine, isowyosine, and methylwyosine.
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This record set is specific for:
Pyrococcus abyssi
UNIPROT: Q9V1F9
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The taxonomic range for the selected organisms is: Pyrococcus abyssi
The expected taxonomic range for this enzyme is: Eukaryota, Archaea, Bacteria
Synonyms
ypl207w, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
TYW1
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-
PATHWAY SOURCE
PATHWAYS
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-, -
SYSTEMATIC NAME
IUBMB Comments
tRNAPhe N1-methylguanine,pyruvate acetaldehyde-lyase (tRNAPhe 4-demethylwyosine-forming, decarboxylating, dehydrating)
This enzyme, which is a member of the superfamily of S-adenosyl-L-methionine-dependent radical (radical AdoMet) enzymes, binds two [4Fe-4S] clusters [3,4]. Carbons C2 and C3 from pyruvate are incorporated into 4-demethylwyosine [3]. The enzyme is found in eukaryotes where it is part of the pathway for wybutosine synthesis, and in archaea, where it is involved in the biosynthesis of archaeal wye bases, such as wyosine, isowyosine, and methylwyosine.
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
N1-methylguanine37 in tRNAPhe + pyruvate + S-adenosyl-L-methionine
4-demethylwyosine37 in tRNAPhe + L-methionine + 5'-deoxyadenosine + CO2 + H2O
show the reaction diagram
-
-
-
?
COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
[4Fe-4S]-center
the N-terminal half of the enzyme beside the radical-SAM cysteine triad, contains an additional highly conserved cysteine motif involved in the coordination of a second [4Fe-4S] cluster. This cluster displays a free coordination site that interacts with pyruvate, the second substrate of the reaction
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Iron
protein contains contained up to 8.2 iron and 8.2 sulfide ions per polypeptide chain
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
-
UniProt
Manually annotated by BRENDA team
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
37000
x * 37800, calculated, x * 37000, SDS-PAGE
37800
x * 37800, calculated, x * 37000, SDS-PAGE
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
?
x * 37800, calculated, x * 37000, SDS-PAGE
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
purification and reconstitution of recombinant protein
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expression in Escherichia coli
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Perche-Letuvee, P.; Kathirvelu, V.; Berggren, G.; Clemancey, M.; Latour, J.M.; Maurel, V.; Douki, T.; Armengaud, J.; Mulliez, E.; Fontecave, M.; Garcia-Serres, R.; Gambarelli, S.; Atta, M.
4-Demethylwyosine synthase from Pyrococcus abyssi is a radical-S-adenosyl-L-methionine enzyme with an additional [4Fe-4S](+2) cluster that interacts with the pyruvate co-substrate
J. Biol. Chem.
287
41174-41185
2012
Pyrococcus abyssi (Q9V1F9), Pyrococcus abyssi, Pyrococcus abyssi GE5 / CNCM I-1302 / DSM 25543 (Q9V1F9)
Manually annotated by BRENDA team