3.6.1.18: FAD diphosphatase
This is an abbreviated version!
For detailed information about FAD diphosphatase, go to the full flat file.
Word Map on EC 3.6.1.18
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3.6.1.18
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3.6.1.9
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3.1.4.1
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pyrophosphatases
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ppi-generating
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nppase
- 3.6.1.18
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3.6.1.9
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3.1.4.1
- pyrophosphatases
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ppi-generating
- nppase
Reaction
Synonyms
5'-nucleotidase, FAD diphosphatase, FAD pyrophosphatase, FADppase, flavin adenine dinucleotide pyrophosphatase, flavine adenine dinucleotide pyrophosphatase, Ftp_Ec, Ftp_Tp-like, metal-dependent FAD pyrophosphatase, Mg2+-dependent FAD pyrophosphatase, More, nucleotide phosphodiesterase, nucleotide pyrophosphatase, riboflavin adenine dinucleotide pyrophosphatase, riboflavine adenine dinucleotide pyrophosphatase, TP0796
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General Information on EC 3.6.1.18 - FAD diphosphatase
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GENERAL INFORMATION 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
evolution
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
physiological function
additional information
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
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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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physiological function
the flavin-trafficking protein (Ftp) catalyzes the transfer of the FMN moiety of FAD to a threonine residue in a target flavoprotein
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
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
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additional information
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
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
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the critical residue that contacts the isoalloxazine ring of FAD, is a tyrosine residue in the FAD-binding Ftps
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