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
-
prosthetic
- pallidum
-
fmn-binding
-
redox-active
-
metal-dependent
-
spirochete
-
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
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General Information
General Information on EC 2.7.1.180 - FAD:protein FMN transferase
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evolution
malfunction
physiological function
additional information
there likely are two classes of Ftps, one associated with FAD-binding and the other with FAD hydrolysis
evolution
there likely are two classes of Ftps, one associated with FAD-binding and the other with FAD hydrolysis
evolution
there likely are two classes of Ftps, one associated with FAD-binding and the other with FAD hydrolysis
evolution
ApbE is a member of a family of flavin transferases that incorporates flavin mononucleotide (FMN) to subunits of diverse respiratory complexes, which fulfill important homeostatic functions. Enzyme residue His257 is absolutely conserved in the family
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
evolution
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there likely are two classes of Ftps, one associated with FAD-binding and the other with FAD hydrolysis
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evolution
-
there likely are two classes of Ftps, one associated with FAD-binding and the other with FAD hydrolysis
-
evolution
-
there likely are two classes of Ftps, one associated with FAD-binding and the other with FAD hydrolysis
-
evolution
-
there likely are two classes of Ftps, one associated with FAD-binding and the other with FAD hydrolysis
-
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enzyme inactivation results in a complete loss of the quinone reductase activity of Na+-translocating NADH:quinone oxidoreductase
malfunction
lesion in the ApbE1 gene in results in inactive Na+-translocating NADH:quinone oxidoreductase, but cytoplasmic fumarate reductase activity remains unchanged
malfunction
lesion in the ApbE2 gene in results in inactive cytoplasmic fumarate reductase, but Na+-translocating NADH:quinone oxidoreductase activity remains unchanged
malfunction
a single amino acid substitution Y60N converts it from an FAD-binding protein to a Mg2+-dependent FAD diphosphatase (Ftp_Tp-like). 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
malfunction
a single amino acid substitution converts it from an FAD-binding protein to a Mg2+-dependent FAD diphosphatase (Ftp_Tp-like, EC 3.6.1.18)
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
malfunction
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enzyme inactivation results in a complete loss of the quinone reductase activity of Na+-translocating NADH:quinone oxidoreductase
-
malfunction
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lesion in the ApbE1 gene in results in inactive Na+-translocating NADH:quinone oxidoreductase, but cytoplasmic fumarate reductase activity remains unchanged
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malfunction
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lesion in the ApbE2 gene in results in inactive cytoplasmic fumarate reductase, but Na+-translocating NADH:quinone oxidoreductase activity remains unchanged
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ApbE is a modifying enzyme involved in the maturation of flavoproteins. ApbE is the only protein factor required for flavinylation of subunit NqrC in Na+-translocating NADH:quinone oxidoreductase
physiological function
Na+-translocating NADH:quinone oxidoreductase maturation involves covalent attachment of flavin mononucleotide (FMN) residues, catalyzed by flavin transferase encoded by the nqr-associated apbE gene
physiological function
the flavin-trafficking protein (Ftp) catalyzes the transfer of the FMN moiety of FAD to a threonine residue in a target flavoprotein. Both types of Ftps are capable of flavinylating periplasmic redox-carrying proteins (e.g., RnfG_Ec) via the metal-dependent covalent attachment of FMN. Possible mechanism by which flavoproteins are generated, overview
physiological function
the flavin-trafficking protein (Ftp) catalyzes the transfer of the FMN moiety of FAD to a threonine residue in a target flavoprotein. Both types of Ftps are capable of flavinylating periplasmic redox-carrying proteins (e.g., RnfG_Ec) via the metal-dependent covalent attachment of FMN. Possible mechanism by which flavoproteins are generated, overview
physiological function
the flavin-trafficking protein (Ftp) in the syphillis spirochete Treponema pallidum (Ftp_Tp) is a bacterial metal-dependent FAD diphosphatase that hydrolyzes FAD into AMP and FMN in the periplasm. Both types of Ftps are capable of flavinylating periplasmic redox-carrying proteins (e.g., RnfG_Ec) via the metal-dependent covalent attachment of FMN. Possible mechanism by which flavoproteins are generated, overview
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
physiological function
substrate specificity and regulatory mechanisms, overview. Residue H257 is the residue whose deprotonation controls the activity, it plays an important role in the catalytic mechanism of ApbE. Residue His257 is indeed essential for catalysis, but not for substrate binding
physiological function
the enzyme flavinylate the redox subunit, NqrC, via its metal-dependent FMN transferase activity
physiological function
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ApbE is a modifying enzyme involved in the maturation of flavoproteins. ApbE is the only protein factor required for flavinylation of subunit NqrC in Na+-translocating NADH:quinone oxidoreductase
-
physiological function
-
the flavin-trafficking protein (Ftp) catalyzes the transfer of the FMN moiety of FAD to a threonine residue in a target flavoprotein. Both types of Ftps are capable of flavinylating periplasmic redox-carrying proteins (e.g., RnfG_Ec) via the metal-dependent covalent attachment of FMN. Possible mechanism by which flavoproteins are generated, overview
-
physiological function
-
the flavin-trafficking protein (Ftp) catalyzes the transfer of the FMN moiety of FAD to a threonine residue in a target flavoprotein. Both types of Ftps are capable of flavinylating periplasmic redox-carrying proteins (e.g., RnfG_Ec) via the metal-dependent covalent attachment of FMN. Possible mechanism by which flavoproteins are generated, overview
-
physiological function
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the flavin-trafficking protein (Ftp) in the syphillis spirochete Treponema pallidum (Ftp_Tp) is a bacterial metal-dependent FAD diphosphatase that hydrolyzes FAD into AMP and FMN in the periplasm. Both types of Ftps are capable of flavinylating periplasmic redox-carrying proteins (e.g., RnfG_Ec) via the metal-dependent covalent attachment of FMN. Possible mechanism by which flavoproteins are generated, overview
-
physiological function
-
Na+-translocating NADH:quinone oxidoreductase maturation involves covalent attachment of flavin mononucleotide (FMN) residues, catalyzed by flavin transferase encoded by the nqr-associated apbE gene
-
physiological function
-
the flavin-trafficking protein (Ftp) catalyzes the transfer of the FMN moiety of FAD to a threonine residue in a target flavoprotein. Both types of Ftps are capable of flavinylating periplasmic redox-carrying proteins (e.g., RnfG_Ec) via the metal-dependent covalent attachment of FMN. Possible mechanism by which flavoproteins are generated, overview
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the critical residue that contacts the isoalloxazine ring of FAD, is a tyrosine residue in the FAD-binding Ftps
additional information
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the critical residue that contacts the isoalloxazine ring of FAD, is a tyrosine residue in the FAD-binding Ftps
additional information
the critical residue that contacts the isoalloxazine ring of FAD, is a tyrosine residue in the FAD-binding Ftps. FAD binding structure involving residue K207, overview
additional information
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the critical residue that contacts the isoalloxazine ring of FAD, is a tyrosine residue in the FAD-binding Ftps. FAD binding structure involving residue K207, overview
additional information
residue His257 is located in the catalytic site and the mutational substitution does not produce major conformational changes
additional information
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residue His257 is located in the catalytic site and the mutational substitution does not produce major conformational changes
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
additional information
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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