2.7.1.180: FAD:protein FMN transferase
This is an abbreviated version!
For detailed information about FAD:protein FMN transferase, go to the full flat file.
Word Map on EC 2.7.1.180
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2.7.1.180
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flavinylation
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vibrio
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flavoproteins
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na+-translocating
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nadh:quinone
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phosphoester
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mononucleotide
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fumarate
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cholerae
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klebsiella
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pneumoniae
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na+-nqr
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harveyi
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fluorogenic
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proteobacteria
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prosthetic
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pallidum
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fmn-binding
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redox-active
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metal-dependent
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spirochete
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syphilis
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isoalloxazine
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pyrophosphatase
- 2.7.1.180
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flavinylation
- vibrio
- flavoproteins
-
na+-translocating
-
nadh:quinone
-
phosphoester
- mononucleotide
- fumarate
- cholerae
-
klebsiella
- pneumoniae
- na+-nqr
- harveyi
-
fluorogenic
- proteobacteria
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prosthetic
- pallidum
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fmn-binding
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redox-active
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metal-dependent
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spirochete
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syphilis
- isoalloxazine
- pyrophosphatase
Reaction
Synonyms
AbpE, apbE, ApbE1, ApbE2, apbE_2, FAD:threonine flavin transferases, flavin transferase, flavin-trafficking protein, FMN transferase, FRD, frd-apbE, Ftp, Ftp_Ec, Mg2+-dependent FAD:protein FMN transferase, Mg2+-dependent FMN transferase, More, protein-dependent FMN transferase
ECTree
2.7.1.180 FAD:protein FMN transferaseAdvanced search results
results (
results (Substrates Products
Substrates Products on EC 2.7.1.180 - FAD:protein FMN transferase
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SUBSTRATE 
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
FAD + L-threonyl-[Shewanella oneidensis NqrC protein]
AMP + FMN-L-threonyl-[Shewanella oneidensis NqrC protein] + H+
a high-resolution structure of the Ftp-mediated flavinylated protein of Shewanella oneidensis NqrC identifies an essential lysine in phosphoester-threonyl-FMN bond formation in the posttranslationally modified flavoproteins
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-
?
FAD + [Klebsiella pneumoniae cytoplasmic fumarate reductase]-L-threonine
[Klebsiella pneumoniae cytoplasmic fumarate reductase]-FMN-L-threonine + AMP
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-
-
?
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
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-
-
?
FAD + [periplasmic redox-carrying protein RnfG_Ec]-L-threonine
[periplasmic redox-carrying protein RnfG_Ec]-FMN-L-threonine + AMP
flavinylating via the metal-dependent covalent attachment of FMN
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-
?
FAD + [protein NqrC]-L-threonine
[protein NqrC]-FMN-L-threonine + AMP
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-
-
?
FAD + [protein]-L-serine
[protein]-FMN-L-serine + AMP
45-90% activity compared to threonine as acceptor with wild-type and mutant enzymes
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-
?
FAD + [Shewanella oneidensis protein NqrC]-L-threonine
[Shewanella oneidensis protein NqrC]-FMN-L-threonine + AMP
a subunit (NqrC) of a cytoplasmic membrane redox system (Nqr), detection of an essential lysine residue in phosphoester-threonyl-FMN bond formation in the posttranslationally modified flavoprotein
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-
?
FAD + [Vibrio cholerae protein NqrC]-L-threonine
[Vibrio cholerae protein NqrC]-FMN-L-threonine + AMP
FAD + L-threonyl-[NqrC protein]
AMP + FMN-L-threonyl-[NqrC protein] + H+
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-
-
?
FAD + L-threonyl-[NqrC protein]
AMP + FMN-L-threonyl-[NqrC protein] + H+
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-
-
?
FAD + L-threonyl-[NqrC protein]
AMP + FMN-L-threonyl-[NqrC protein] + H+
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-
-
?
FAD + L-threonyl-[NqrC protein]
AMP + FMN-L-threonyl-[NqrC protein] + H+
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-
-
?
FAD + L-threonyl-[NqrC protein]
AMP + FMN-L-threonyl-[NqrC protein] + H+
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-
-
?
FAD + L-threonyl-[NqrC protein]
AMP + FMN-L-threonyl-[NqrC protein] + H+
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-
-
?
FAD + L-threonyl-[protein]
AMP + FMN-L-threonyl-[protein] + H+
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-
-
?
FAD + L-threonyl-[protein]
AMP + FMN-L-threonyl-[protein] + H+
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-
-
?
FAD + L-threonyl-[protein]
AMP + FMN-L-threonyl-[protein] + H+
RnfG_Ec subunit of the Rnf_Ec-redox system of Escherichia coli
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-
?
FAD + L-threonyl-[protein]
AMP + FMN-L-threonyl-[protein] + H+
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-
-
?
FAD + L-threonyl-[protein]
AMP + FMN-L-threonyl-[protein] + H+
RnfG_Ec subunit of the Rnf_Ec-redox system of Escherichia coli
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-
?
FAD + L-threonyl-[protein]
AMP + FMN-L-threonyl-[protein] + H+
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-
-
?
FAD + L-threonyl-[protein]
AMP + FMN-L-threonyl-[protein] + H+
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-
-
?
FAD + L-threonyl-[protein]
AMP + FMN-L-threonyl-[protein] + H+
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-
-
?
FAD + L-threonyl-[protein]
AMP + FMN-L-threonyl-[protein] + H+
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-
-
?
FAD + L-threonyl-[RnfG protein]
AMP + FMN-L-threonyl-[RnfG protein] + H+
RnfG subunit of the Rnf redox system
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-
?
FAD + L-threonyl-[RnfG protein]
AMP + FMN-L-threonyl-[RnfG protein] + H+
RnfG subunit of the Rnf redox system
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-
?
FAD + L-threonyl-[RnfG protein]
AMP + FMN-L-threonyl-[RnfG protein] + H+
RnfG subunit of the Rnf redox system
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-
?
FAD + L-threonyl-[RnfG protein]
AMP + FMN-L-threonyl-[RnfG protein] + H+
RnfG subunit of the Rnf redox system
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-
?
FAD + L-threonyl-[RnfG protein]
AMP + FMN-L-threonyl-[RnfG protein] + H+
RnfG subunit of the Rnf redox system
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-
?
FAD + L-threonyl-[RnfG protein]
AMP + FMN-L-threonyl-[RnfG protein] + H+
RnfG subunit of the Rnf redox system
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-
?
FAD + [protein]-L-threonine
[protein]-FMN-L-threonine + AMP
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-
-
?
FAD + [protein]-L-threonine
[protein]-FMN-L-threonine + AMP
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-
-
?
FAD + [protein]-L-threonine
[protein]-FMN-L-threonine + AMP
preferred substrate
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-
?
FAD + [protein]-L-threonine
[protein]-FMN-L-threonine + AMP
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-
-
?
FAD + [protein]-L-threonine
[protein]-FMN-L-threonine + AMP
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-
-
?
FAD + [protein]-L-threonine
[protein]-FMN-L-threonine + AMP
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-
-
?
FAD + [Vibrio cholerae protein NqrC]-L-threonine
[Vibrio cholerae protein NqrC]-FMN-L-threonine + AMP
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-
-
?
FAD + [Vibrio cholerae protein NqrC]-L-threonine
[Vibrio cholerae protein NqrC]-FMN-L-threonine + AMP
conserved Lys207 in NqrC can account for the pH dependency
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-
?
additional information
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the flavin-trafficking protein (Ftp) catalyzes the transfer of the FMN moiety of FAD and its covalent binding to the hydroxyl group of a threonine residue in a target flavoprotein (EC 2.7.1.180). The enzyme is capable of flavinylating periplasmic redox-carrying proteins (e.g., RnfG_Ec) via the metal-dependent covalent attachment of FMN. A single amino acid substitution Y60N converts it from an FAD-binding protein to a Mg2+-dependent FAD diphosphatase (Ftp_Tp-like) (EC 3.6.1.18). The engineered protein variant (Ftp_EcY60A) shows Mg2+-dependent FAD diphosphatase activity, but also retains its Mg2+-dependent FMN transferase (EC 2.7.1.180) activity on the protein substrate, indicating that the protein variant enzyme has dual activity. The Ftp_EcY60A protein variant binds FAD, yet rapidly hydrolyzes it and the product FMN dissociates. Substrate binding structures, detailed overview
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additional information
?
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the flavin-trafficking protein (Ftp) catalyzes the transfer of the FMN moiety of FAD and its covalent binding to the hydroxyl group of a threonine residue in a target flavoprotein (EC 2.7.1.180). The enzyme is capable of flavinylating periplasmic redox-carrying proteins (e.g., RnfG_Ec) via the metal-dependent covalent attachment of FMN. A single amino acid substitution Y60N converts it from an FAD-binding protein to a Mg2+-dependent FAD diphosphatase (Ftp_Tp-like) (EC 3.6.1.18). The engineered protein variant (Ftp_EcY60A) shows Mg2+-dependent FAD diphosphatase activity, but also retains its Mg2+-dependent FMN transferase (EC 2.7.1.180) activity on the protein substrate, indicating that the protein variant enzyme has dual activity. The Ftp_EcY60A protein variant binds FAD, yet rapidly hydrolyzes it and the product FMN dissociates. Substrate binding structures, detailed overview
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additional information
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the Escherichia coli enzyme shows no Mg2+-dependent FAD pyrophosphatase (EC 3.6.1.18) activity
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additional information
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the Escherichia coli enzyme shows no Mg2+-dependent FAD pyrophosphatase (EC 3.6.1.18) activity
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additional information
?
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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
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additional information
?
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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
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additional information
?
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the flavin-trafficking protein (Ftp) catalyzes the transfer of the FMN moiety of FAD and its covalent binding to the hydroxyl group of a threonine residue in a target flavoprotein (EC 2.7.1.180). The enzyme is capable of flavinylating periplasmic redox-carrying proteins (e.g., RnfG_Ec) via the metal-dependent covalent attachment of FMN. It also displays FAD diphosphatase activity in vitro, hydrolyzing FAD into FMN and AMP (EC 3.6.1.18). Substrate binding structures, detailed overview
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-
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additional information
?
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the flavin-trafficking protein (Ftp) catalyzes the transfer of the FMN moiety of FAD and its covalent binding to the hydroxyl group of a threonine residue in a target flavoprotein (EC 2.7.1.180). The enzyme is capable of flavinylating periplasmic redox-carrying proteins (e.g., RnfG_Ec) via the metal-dependent covalent attachment of FMN. It also displays FAD diphosphatase activity in vitro, hydrolyzing FAD into FMN and AMP (EC 3.6.1.18). Substrate binding structures, detailed overview
-
-
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additional information
?
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the flavin-trafficking protein (Ftp) catalyzes the transfer of the FMN moiety of FAD and its covalent binding to the hydroxyl group of a threonine residue in a target flavoprotein (EC 2.7.1.180). The enzyme is capable of flavinylating periplasmic redox-carrying proteins (e.g., RnfG_Ec) via the metal-dependent covalent attachment of FMN. It also displays FAD diphosphatase activity in vitro, hydrolyzing FAD into FMN and AMP (EC 3.6.1.18). Substrate binding structures, detailed overview
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additional information
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substrate specificity, overview. FAD cannot be substituted by FMN
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additional information
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the His257 residue plays important roles in catalysis and in enzyme-substrate complex formation and in substrate deprotonation, proposed mechanism of flavin transfer
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additional information
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the His257 residue plays important roles in catalysis and in enzyme-substrate complex formation and in substrate deprotonation, proposed mechanism of flavin transfer
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additional information
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enzyme ApbE covalently attaches flavin residues to threonine residues of Na+-translocating NADH:quinone oxidoreductase maturation, Na+-NQR
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additional information
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enzyme ApbE covalently attaches flavin residues to threonine residues of Na+-translocating NADH:quinone oxidoreductase maturation, Na+-NQR
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?
additional information
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enzyme ApbE covalently attaches flavin residues to threonine residues of Na+-translocating NADH:quinone oxidoreductase maturation, Na+-NQR
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