EC number:3.1.3.102

Enzyme

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EC Tree
     3. Hydrolases
        3.1 Acting on ester bonds
            3.1.3 Phosphoric-monoester hydrolases
ID:3.1.3.102
Description:FMN hydrolase.
Alternative Name: FMN phosphatase.

3D structure

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PDB

References

External Links

UniProtKB Enzyme Link: UniProtKB 3.1.3.102
BRENDA Enzyme Link: BRENDA 3.1.3.102
KEGG Enzyme Link: KEGG3.1.3.102
BioCyc Enzyme Link: BioCyc 3.1.3.102
ExPASy Enzyme Link: ExPASy3.1.3.102
EC2PDB Enzyme Link: EC2PDB 3.1.3.102
ExplorEnz Enzyme Link: ExplorEnz 3.1.3.102
PRIAM enzyme-specific profiles Link: PRIAM 3.1.3.102
IntEnz Enzyme Link: IntEnz 3.1.3.102
MEDLINE Enzyme Link: MEDLINE 3.1.3.102

EC number:3.1.3.102

MSA:

3.1.3.102;
Phylogenetic Tree:

3.1.3.102;
Uniprot:
M-CSA:
RHEA:35587 FMN + H2O = phosphate + riboflavin
RULE(radius=1) [*:1]-[O;H0;+0:2]-[P;H0;+0:3](=[*:4])(-[*:5])-[*:6].[OH2;+0:7]>>[*:1]-[OH;+0:2].[*:4]=[P;H0;+0:3](-[*:5])(-[*:6])-[OH;+0:7]
Reaction
Core-to-Core No scaffolds atoms were exchanged as a result of the reaction

References

TitleAuthorsDatePubMed ID
Catalysis of an Essential Step in Vitamin B2 Biosynthesis by a Consortium of Broad Spectrum Hydrolases.Sarge S, Haase I, Illarionov B, Laudert D, Hohmann HP, Bacher A, Fischer M2015 Nov26316208
An FMN hydrolase of the haloacid dehalogenase superfamily is active in plant chloroplasts.Rawat R, Sandoval FJ, Wei Z, Winkler R, Roje S2011 Dec 922002057
An FMN hydrolase is fused to a riboflavin kinase homolog in plants.Sandoval FJ, Roje S2005 Nov 1816183635
Genome-wide analysis of substrate specificities of the Escherichia coli haloacid dehalogenase-like phosphatase family.Kuznetsova E, Proudfoot M, Gonzalez CF, Brown G, Omelchenko MV, Borozan I, Carmel L, Wolf YI, Mori H, Savchenko AV, Arrowsmith CH, Koonin EV, Edwards AM, Yakunin AF2006 Nov 2416990279