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Literature summary for 2.7.1.180 extracted from

  • 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 (2019), FEMS Microbiol. Lett., 366, fnz252 .
    View publication on PubMed
Search for more literature for 2.7.1.180

Cloned(Commentary)

Cloned (Comment) Organism
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 Klebsiella pneumoniae

Protein Variants

Protein Variants Comment Organism
additional information replacement of non-Ala residues in the positions 0, -2, -3 and -6 by Ala, and Ala-1 by Val. Keeping in mind that the position +2 is occupied by a non-typical Gln in FRD, this residue is also replaced by Ala Klebsiella pneumoniae

Localization

Localization Comment Organism GeneOntology No. Textmining
cytoplasm
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 Klebsiella pneumoniae 5737
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Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
FAD + [Klebsiella pneumoniae cytoplasmic fumarate reductase]-L-threonine Klebsiella pneumoniae
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 [Klebsiella pneumoniae cytoplasmic fumarate reductase]-FMN-L-threonine + AMP
-
 ?
FAD + [protein]-L-threonine Klebsiella pneumoniae
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 [protein]-FMN-L-threonine + AMP
-
 ?

Organism

Organism UniProt Comment Textmining
Klebsiella pneumoniae A0A0C7KIE8
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Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
FAD + [Klebsiella pneumoniae cytoplasmic fumarate reductase]-L-threonine
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 Klebsiella pneumoniae [Klebsiella pneumoniae cytoplasmic fumarate reductase]-FMN-L-threonine + AMP
-
 ?
FAD + [NqrC subunit of Vibrio harveyi Na+-translocating NADH:quinone oxidoreductase]-L-threonine
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 Klebsiella pneumoniae [NqrC subunit of Vibrio harveyi Na+-translocating NADH:quinone oxidoreductase]-FMN-L-threonine + AMP
-
 ?
FAD + [protein]-L-serine 45-90% activity compared to threonine as acceptor with wild-type and mutant enzymes Klebsiella pneumoniae [protein]-FMN-L-serine + AMP
-
 ?
FAD + [protein]-L-threonine
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 Klebsiella pneumoniae [protein]-FMN-L-threonine + AMP
-
 ?
FAD + [protein]-L-threonine preferred substrate Klebsiella pneumoniae [protein]-FMN-L-threonine + AMP
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 ?
additional information Klebsiella pneumoniae ApbE can modify both threonine and serine residues in the position 447 of FRD resulting in their similar activities, although serine is modified less readily Klebsiella pneumoniae ?
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Synonyms

Synonyms Comment Organism
apbE
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 Klebsiella pneumoniae
apbE_2
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 Klebsiella pneumoniae
flavin transferase
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 Klebsiella pneumoniae
FRD
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 Klebsiella pneumoniae
frd-apbE
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 Klebsiella pneumoniae

General Information

General Information Comment Organism
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 Klebsiella pneumoniae
malfunction the replacement of the flavin acceptor threonine with alanine completely abolishes the modification reaction, whereas the replacements of conserved aspartate and serine had only minor effects. Effects of other substitutions, including replacing the acceptor threonine with serine, (a 10-55% decrease in the flavinylation degree). Replacements of conserved leucine and threonine residues in the binding pocket that accommodates FMN residue still allows appreciable flavinylation of the NqrC subunit of Vibrio harveyi Na+-translocating NADH:quinone oxidoreductase, despite a profound weakening of the isoalloxazine ring binding and an increase in its exposure to solvent Klebsiella pneumoniae
additional information the flavinylation motif of FRD, D-6A-5I-4S-3G-2A-1T0S+1 Q+2S+3 (zero position corresponds to Thr447 in the amino acid sequence), is mostly typical of FMN bind domain Klebsiella pneumoniae
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 Klebsiella pneumoniae