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
-
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
ECTree
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Metals Ions
Metals Ions on EC 2.7.1.180 - FAD:protein FMN transferase
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Ca2+
presence of a Ca2+ ion in metal site 1 in the apo form of mutant Ftp_EcY60N, the Ca2+ ion serves a role in properly positioning substrate and protein residues
Mg2+
additional information
dependent on, metal-dependent enzyme, bimetal center in the crystal structure of Escherichia coli Ftp
Mg2+
required, dependent on, Mg2+ ion is directly involved in catalysis. A single metal ion is bound in the wild-type enzyme and mutant Ftp_EcE169K structures. The inhibited mutant Ftp_EcY60N contains a bimetal Mg2+ center
Mg2+
required for catalysis, Mg2+ does not play a major role in stabilizing the interaction of the protein with FAD, Mg2+ in the preferred divalent cation
identification of a bimetal center in the crystal structure of Escherichia coli Ftp (Ftp_Ec)
additional information
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identification of a bimetal center in the crystal structure of Escherichia coli Ftp (Ftp_Ec)
additional information
divalent cations are essential for ApbE activity, and their removal by EDTA abolishes the activity. ApbE is also able to use other divalent cations, such as Mn2+ and Co2+, obtaining a similar activity compared to Mg2+. The coordination sphere of ApbE enzymes largely determines the specificity of the enzyme for the divalent cation