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Information on EC 2.8.4.3 - tRNA-2-methylthio-N6-dimethylallyladenosine synthase and Organism(s) Escherichia coli and UniProt Accession P0AEI1

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IUBMB Comments
This bacterial enzyme binds two [4Fe-4S] clusters as well as the transferred sulfur . The enzyme is a member of the superfamily of S-adenosyl-L-methionine-dependent radical (radical AdoMet) enzymes. The sulfur donor is believed to be one of the [4Fe-4S] clusters, which is sacrificed in the process, so that in vitro the reaction is a single turnover. The identity of the electron donor is not known.
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This record set is specific for:
Escherichia coli
UNIPROT: P0AEI1
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The taxonomic range for the selected organisms is: Escherichia coli
The enzyme appears in selected viruses and cellular organisms
Reaction Schemes
N6-dimethylallyladenine37 in tRNA
+
sulfur-(sulfur carrier)
+
2
+
reduced electron acceptor
=
2-(methylsulfanyl)-N6-dimethylallyladenine37 in tRNA
+
+
(sulfur carrier)
+
+
+
electron acceptor
N6-dimethylallyladenine37 in tRNA
+
sulfur-(sulfur carrier)
+
+
reduced electron acceptor
=
2-sulfanyl-N6-dimethylallyladenine37 in tRNA
+
(sulfur carrier)
+
+
+
electron acceptor
+
2-sulfanyl-N6-dimethylallyladenine37 in tRNA
=
+
2-(methylsulfanyl)-N6-dimethylallyladenine37 in tRNA
Synonyms
2-methylthio-N-6-isopentenyl adenosine synthase, MiaB, TM0653, tRNA-i6A37 methylthiotransferase, more
SYSTEMATIC NAME
IUBMB Comments
tRNA (N6-dimethylallyladenosine37):sulfur-(sulfur carrier),S-adenosyl-L-methionine C2-methylthiotransferase
This bacterial enzyme binds two [4Fe-4S] clusters as well as the transferred sulfur [3]. The enzyme is a member of the superfamily of S-adenosyl-L-methionine-dependent radical (radical AdoMet) enzymes. The sulfur donor is believed to be one of the [4Fe-4S] clusters, which is sacrificed in the process, so that in vitro the reaction is a single turnover. The identity of the electron donor is not known.
COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
[4Fe-4S]-center
enzyme MiaB contains both iron and sulfide and an apoprotein form can chelate as much as 2.5-3 iron and 3-3.5 sulfur atoms per polypeptide chain. Under reducing and anaerobic conditions, a [4Fe-4S] cluster is present, whereas [2Fe-2S] and [3Fe-4S] forms are generated under aerobic conditions. Residues Cys157, Cys161, and Cys164 are involved in iron chelation, and the cluster is essential for activity
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
physiological function
enzym MiaB physically interacts with monothiol glutaredoxin, GrxD, and the FeS carrier protein NfuA, with MiaB with affinities compatible with an in vivo function. NfuA is able to transfer its cluster in vitro to MiaB, whereas GrxD is unable to do so. Cells lacking both GrxD and NfuA display a severe defect in in vivo MiaB activity
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
53600
1 * 60000 SDS-PAGE, 1 * 53600, calculated, His-tagged recombinant protein
60000
gel filtration, His-tagged recombinan protein
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
monomer
1 * 60000 SDS-PAGE, 1 * 53600, calculated, His-tagged recombinant protein
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expression in Escherichia coli
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Pierrel, F.; Bjoerk, G.R.; Fontecave, M.; Atta, M.
Enzymatic modification of tRNAs: MiaB is an iron-sulfur protein
J. Biol. Chem.
277
13367-13370
2002
Escherichia coli (P0AEI1)
Manually annotated by BRENDA team
Boutigny, S.; Saini, A.; Baidoo, E.E.; Yeung, N.; Keasling, J.D.; Butland, G.
Physical and functional interactions of a monothiol glutaredoxin and an iron sulfur cluster carrier protein with the sulfur-donating radical S-adenosyl-L-methionine enzyme MiaB
J. Biol. Chem.
288
14200-14211
2013
Escherichia coli (P0AEI1)
Manually annotated by BRENDA team