EC number:1.14.14.27

Enzyme

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     1. Oxidoreductases
        1.14 Acting on paired donors, with incorporation or reduction of molecular oxygen
            1.14.14 With reduced flavin or flavoprotein as one donor, and incorporation of one atom of oxygen into the other donor
ID:1.14.14.27
Description:Resorcinol 4-hydroxylase (FADH(2)).

3D structure

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PDB

References

External Links

UniProtKB Enzyme Link: UniProtKB 1.14.14.27
BRENDA Enzyme Link: BRENDA 1.14.14.27
KEGG Enzyme Link: KEGG1.14.14.27
BioCyc Enzyme Link: BioCyc 1.14.14.27
ExPASy Enzyme Link: ExPASy1.14.14.27
EC2PDB Enzyme Link: EC2PDB 1.14.14.27
ExplorEnz Enzyme Link: ExplorEnz 1.14.14.27
PRIAM enzyme-specific profiles Link: PRIAM 1.14.14.27
IntEnz Enzyme Link: IntEnz 1.14.14.27
MEDLINE Enzyme Link: MEDLINE 1.14.14.27

EC number:1.14.14.27

MSA:

1.14.14.27;
Phylogenetic Tree:

1.14.14.27;
Uniprot:
M-CSA:
RHEA:50228 FADH2 + O2 + resorcinol = benzene-1,2,4-triol + FAD + H(+) + H2O
RULE(radius=1) [*:1]-[N;H0;+0:2]1-[*:3]:[*:4]-[NH;+0:5]-[c;H0;+0:6](:[*:7]):[c;H0;+0:8]-1:[nH;+0:9]:[*:10].[*:11]:[cH;+0:12]:[*:13].[O;H0;+0:14]=[O;H0;+0:15]>>[*:1]-[n;H0;+0:2]1:[*:3]:[*:4]:[n;H0;+0:5]:[c;H0;+0:6](:[*:7])-[c;H0;+0:8]:1:[n;H0;+0:9]:[*:10].[*:11]:[c;H0;+0:12](:[*:13])-[OH;+0:14].[OH2;+0:15]
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References

TitleAuthorsDatePubMed ID
Biochemical and genetic analysis of the gamma-resorcylate (2,6-dihydroxybenzoate) catabolic pathway in Rhizobium sp. strain MTP-10005: identification and functional analysis of its gene cluster.Yoshida M, Oikawa T, Obata H, Abe K, Mihara H, Esaki N2007 Mar17158677
Bacterial metabolism of resorcinylic compounds: purification and properties of orcinol hydroxylase and resorcinol hydroxylase from Pseudomonas putida ORC.Ohta Y, Ribbons DW1976 Jan 21280