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Information on EC 2.4.99.17 - S-adenosylmethionine:tRNA ribosyltransferase-isomerase and Organism(s) Thermotoga maritima and UniProt Accession Q9WZ44

for references in articles please use BRENDA:EC2.4.99.17
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IUBMB Comments
The reaction is a combined transfer and isomerization of the ribose moiety of S-adenosyl-L-methionine to the modified guanosine base in the wobble position in tRNAs specific for Tyr, His, Asp or Asn. It is part of the queuosine biosynthesis pathway.
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This record set is specific for:
Thermotoga maritima
UNIPROT: Q9WZ44
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Word Map
The taxonomic range for the selected organisms is: Thermotoga maritima
The expected taxonomic range for this enzyme is: Bacteria, Archaea
Reaction Schemes
+
7-aminomethyl-7-carbaguanosine34 in tRNA
=
+
+
epoxyqueuosine34 in tRNA
Synonyms
s-adenosylmethionine:trna ribosyltransferase-isomerase, quea enzyme, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
queuosine biosynthesis protein
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S-adenosylmethionine:tRNA ribosyltransferase-isomerase
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QueA enzyme
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queuosine biosynthesis protein QueA
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-
-
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PATHWAY SOURCE
PATHWAYS
-
-, -
SYSTEMATIC NAME
IUBMB Comments
S-adenosyl-L-methionine:7-aminomethyl-7-deazaguanosine ribosyltransferase (ribosyl isomerizing; L-methionine, adenine releasing)
The reaction is a combined transfer and isomerization of the ribose moiety of S-adenosyl-L-methionine to the modified guanosine base in the wobble position in tRNAs specific for Tyr, His, Asp or Asn. It is part of the queuosine biosynthesis pathway.
CAS REGISTRY NUMBER
COMMENTARY hide
149719-25-5
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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
S-adenosyl-L-methionine + 7-aminomethyl-7-deazaguanine34 in tRNA
L-methionine + adenine + epoxyqueuosine34 in tRNA
show the reaction diagram
the enzyme catalyzes the formation of the 2,3-epoxy-4,5-dihydroxycyclopentane ring of the queuosine precursor epoxyqueuosine
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-
?
pI VALUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
8.6
calculated from amino acid sequence
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
-
UniProt
Manually annotated by BRENDA team
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
38529
x * 38529, calculated from amino acid sequence
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
?
x * 38529, calculated from amino acid sequence
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
nanodroplet vapor diffusion method, using 12% (w/v) polyethylene glycol 4000, 0.1 M citric acid at pH 5.0
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
nickel-resin column chromatography, RESOURCE Q column chromatography, and Superdex 200 gel filtration
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expressed in Escherichia coli strain DL41
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Mathews, I.; Schwarzenbacher, R.; McMullan, D.; Abdubek, P.; Ambing, E.; Axelrod, H.; Biorac, T.; Canaves, J.; Chiu, H.; Deacon, A.; DiDonato, M.; Elsliger, M.; Godzik, A.; Grittini, C.; Grzechnik, S.; Hale, J.; Hampton, E.; Han, G.; Haugen, J.; Hornsby,
Crystal structure of S-adenosylmethionine:tRNA ribosyltransferase-isomerase (QueA) from Thermotoga maritima at 2.0 A resolution reveals a new fold
Proteins
59
869-874
2005
Thermotoga maritima (Q9WZ44), Thermotoga maritima
Manually annotated by BRENDA team