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Information on EC 2.7.1.180 - FAD:protein FMN transferase and Organism(s) Klebsiella pneumoniae and UniProt Accession B5XRA9

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EC Tree
IUBMB Comments
The enzyme catalyses the transfer of the FMN portion of FAD and its covalent binding to the hydroxyl group of an L-threonine residue in a target flavin-binding protein such as the B and C subunits of EC 7.2.1.1, NADH:ubiquinone reductase (Na+-transporting). Requires Mg2+.
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This record set is specific for:
Klebsiella pneumoniae
UNIPROT: B5XRA9
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The taxonomic range for the selected organisms is: Klebsiella pneumoniae
The expected taxonomic range for this enzyme is: Bacteria, Archaea
Reaction Schemes
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FAD
+
[protein]-L-threonine
=
[protein]-FMN-L-threonine
+
AMP
+
=
[protein]-FMN-L-threonine
+
Synonyms
flavin transferase, flavin-trafficking protein, apbe2, apbe1, fmn transferase, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
FAD:threonine flavin transferases
-
FAD:threonine flavin transferases
-
flavin transferase
SYSTEMATIC NAME
IUBMB Comments
FAD:protein riboflavin-5'-phosphate transferase
The enzyme catalyses the transfer of the FMN portion of FAD and its covalent binding to the hydroxyl group of an L-threonine residue in a target flavin-binding protein such as the B and C subunits of EC 7.2.1.1, NADH:ubiquinone reductase (Na+-transporting). Requires Mg2+.
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
FAD + [protein]-L-threonine
[protein]-FMN-L-threonine + AMP
show the reaction diagram
-
-
-
?
FAD + [Klebsiella pneumoniae cytoplasmic fumarate reductase]-L-threonine
[Klebsiella pneumoniae cytoplasmic fumarate reductase]-FMN-L-threonine + AMP
show the reaction diagram
-
-
-
?
FAD + [NqrC subunit of Vibrio harveyi Na+-translocating NADH:quinone oxidoreductase]-L-threonine
[NqrC subunit of Vibrio harveyi Na+-translocating NADH:quinone oxidoreductase]-FMN-L-threonine + AMP
show the reaction diagram
-
-
-
?
FAD + [protein]-L-serine
[protein]-FMN-L-serine + AMP
show the reaction diagram
45-90% activity compared to threonine as acceptor with wild-type and mutant enzymes
-
-
?
FAD + [protein]-L-threonine
[protein]-FMN-L-threonine + AMP
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
FAD + [protein]-L-threonine
[protein]-FMN-L-threonine + AMP
show the reaction diagram
-
-
-
?
FAD + [Klebsiella pneumoniae cytoplasmic fumarate reductase]-L-threonine
[Klebsiella pneumoniae cytoplasmic fumarate reductase]-FMN-L-threonine + AMP
show the reaction diagram
-
-
-
?
FAD + [protein]-L-threonine
[protein]-FMN-L-threonine + AMP
show the reaction diagram
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
malfunction
lesion in the ApbE2 gene in results in inactive cytoplasmic fumarate reductase, but Na+-translocating NADH:quinone oxidoreductase activity remains unchanged
evolution
FMN residue attached through a phosphoester bond is found in three types of protein architectures-prokaryotic FMN bind and NQR2 RnfD RnfE (PF03116) domains and an about 50-residue N-terminal extension of the ApbE domain in eukaryotic NADH:fumarate oxidoreductases. These three architectures are non-homologous, and their sequences have nothing in common, except for a short motif around the flavinylated residue. The motif common to all three flavinylated architectures can be depicted as Dxx(s/t)(g/s)At/s, where the last residue is the flavin acceptor. It is threonine in all characterized proteins of the first two groups, but it is sporadically replaced by serine in 3.5-5% of their putative homologues
malfunction
physiological function
many flavoproteins belonging to three domain types contain an FMN residue linked through a phosphoester bond to a threonine or serine residue found in a conserved seven-residue motif. The flavinylation reaction is catalyzed by a specific enzyme, ApbE, which uses FAD as a substrate
additional information
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
gene apbE1, frd-apbE operon, recombinant expression in Escherichia coli strain BW25113, ApbE and its target protein are coproduced in the cytoplasm of the recombinant cells
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Bertsova, Y.V.; Kostyrko, V.A.; Baykov, A.A.; Bogachev, A.V.
Localization-controlled specificity of FAD:threonine flavin transferases in Klebsiella pneumoniae and its implications for the mechanism of Na+-translocating NADH:quinone oxidoreductase
Biochim. Biophys. Acta
1837
1122-1129
2014
Klebsiella pneumoniae (B5XP00), Klebsiella pneumoniae (B5XRA9), Klebsiella pneumoniae, Klebsiella pneumoniae 204 (B5XP00), Klebsiella pneumoniae 342 (B5XRA9)
Manually annotated by BRENDA team
Bertsova, Y.V.; Serebryakova, M.V.; Anashkin, V.A.; Baykov, A.A.; Bogachev, A.V.
Mutational analysis of the flavinylation and binding motifs in two protein targets of the flavin transferase ApbE
FEMS Microbiol. Lett.
366
fnz252
2019
Klebsiella pneumoniae (A0A0C7KIE8), Klebsiella pneumoniae
Manually annotated by BRENDA team