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
2.7.1.180 FAD:protein FMN transferaseAdvanced search results
results (
results (Engineering
Engineering on EC 2.7.1.180 - FAD:protein FMN transferase
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PROTEIN VARIANTS 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
E169K
K207A
site-directed mutagenesis, the mutant exhibits no detectable in vitro flavinylation activity
Y60A
site-directed mutagenesis, 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
Y60N
H257G
H257T
site-directed mutagenesis, the mutant shows reduced activity compared to wild-type
additional information
E169K
site-directed mutagenesis of the probabale catalytic site residue, the Ftp_EcE169K protein variant does not show binding of FAD, inactive mutant
E169K
site-directed mutagenesis, mutation of the active-site residue results in loss of FAD binding capability
Y60N
site-directed mutagenesis, a single amino acid substitution converts it from an FAD-binding protein to a Mg2+-dependent FAD diphosphatase (Ftp_Tp-like)
Y60N
site-directed mutagenesis, the single amino acid substitution converts it from an FAD-binding protein to a Mg2+-dependent FAD pdiphosphatase (Ftp_Tp-like, EC 3.6.1.18). The Ftp_EcY60A protein variant binds FAD, rapidly hydrolyzes it, and the product FMN dissociates. But the mutant also retains its Mg2+-dependent FMN transferase (EC 2.7.1.180) activity on the protein substrate. As the site of attack for the FMN transferase reaction is the beta-phosphate of the FAD, and given the large distance between the two metals in the ADP-inhibited Ftp_EcY60N structure, it is reasonable to expect that only metal site 2 requires a Mg2+ ion for this activity
H257G
site-directed mutagenesis, the mutant's flavin transfer activity is abolished. After reconstitution, the H257G shows a FAD:protein ratio nearly identical to the wild-type
H257G
site-directed mutagenesis, the turnover rates of His257 mutants are significantly smaller than those of wild-type ApbE, and mutants show increased Km values for both substrates, the pKa of the catalytic residue (pKES1) increases by 2 pH units in the His257 mutants compared to wild-type, the mutant shows reduced activity compared to wild-type
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
additional information
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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
