EC number:1.14.13.33

Enzyme

Download
EC Tree
     1. Oxidoreductases
        1.14 Acting on paired donors, with incorporation or reduction of molecular oxygen
            1.14.13 With NADH or NADPH as one donor, and incorporation of one atom of oxygen into the other donor
ID:1.14.13.33
Description:4-hydroxybenzoate 3-monooxygenase (NAD(P)H).
Alternative Name: 4-hydroxybenzoate 3-hydroxylase.
Cath: 3.30.9.10; 3.50.50.60;

3D structure

Click one PDB to see exact 3D structure provided by NGL.

Note: Use your mouse to drag, rotate, and zoom in and out of the structure. Mouse-over to identify atoms and bonds. Mouse controls documentation.
PDB

References

External Links

UniProtKB Enzyme Link: UniProtKB 1.14.13.33
BRENDA Enzyme Link: BRENDA 1.14.13.33
KEGG Enzyme Link: KEGG1.14.13.33
BioCyc Enzyme Link: BioCyc 1.14.13.33
ExPASy Enzyme Link: ExPASy1.14.13.33
EC2PDB Enzyme Link: EC2PDB 1.14.13.33
ExplorEnz Enzyme Link: ExplorEnz 1.14.13.33
PRIAM enzyme-specific profiles Link: PRIAM 1.14.13.33
IntEnz Enzyme Link: IntEnz 1.14.13.33
MEDLINE Enzyme Link: MEDLINE 1.14.13.33

EC number:1.14.13.33

MSA:

1.14.13.33;
Phylogenetic Tree:

1.14.13.33;
Uniprot:
M-CSA:
RHEA:19477 4-hydroxybenzoate + H(+) + NADPH + O2 = 3,4-dihydroxybenzoate + H2O + NADP(+)
RULE(radius=1) [*:1]-[N;H0;+0:2]1-[CH;+0:3]=[C;H0;+0:4](-[*:5])-[CH2;+0:6]-[CH;+0:7]=[CH;+0:8]-1.[*:9]:[cH;+0:10]:[*:11].[H+;H0:12].[O;H0;+0:13]=[O;H0;+0:14]>>[*:1]-[n+;H0:2]1:[cH;+0:3]:[c;H0;+0:4](-[*:5]):[cH;+0:6]:[cH;+0:7]:[cH;+0:8]:1.[*:9]:[c;H0;+0:10](:[*:11])-[OH;+0:13].[OH2;+0:14]
Reaction
Core-to-Core More

References

TitleAuthorsDatePubMed ID
4-Hydroxybenzoate hydroxylase from Pseudomonas sp. CBS3. Purification, characterization, gene cloning, sequence analysis and assignment of structural features determining the coenzyme specificity.Seibold B, Matthes M, Eppink MH, Lingens F, Van Berkel WJ, Müller R1996 Jul 158706756
P-Hydroxybenzoate hydroxylase and melilotate hydroxylase.Husain M, Schopfer LM, Massey V197830879
Uncovering the protocatechuate 2,3-cleavage pathway genes.Kasai D, Fujinami T, Abe T, Mase K, Katayama Y, Fukuda M, Masai E2009 Nov19717587
Kinetics of proton-linked flavin conformational changes in p-hydroxybenzoate hydroxylase.Frederick KK, Palfey BA2005 Oct 1116201756
Oxygen reactions in p-hydroxybenzoate hydroxylase utilize the H-bond network during catalysis.Ortiz-Maldonado M, Entsch B, Ballou DP2004 Dec 715568817
RHEA:19473 4-hydroxybenzoate + H(+) + NADH + O2 = 3,4-dihydroxybenzoate + H2O + NAD(+)
RULE(radius=1) [*:1]-[N;H0;+0:2]1-[CH;+0:3]=[C;H0;+0:4](-[*:5])-[CH2;+0:6]-[CH;+0:7]=[CH;+0:8]-1.[*:9]:[cH;+0:10]:[*:11].[H+;H0:12].[O;H0;+0:13]=[O;H0;+0:14]>>[*:1]-[n+;H0:2]1:[cH;+0:3]:[c;H0;+0:4](-[*:5]):[cH;+0:6]:[cH;+0:7]:[cH;+0:8]:1.[*:9]:[c;H0;+0:10](:[*:11])-[OH;+0:13].[OH2;+0:14]
Reaction
Core-to-Core More

References

TitleAuthorsDatePubMed ID
Uncovering the protocatechuate 2,3-cleavage pathway genes.Kasai D, Fujinami T, Abe T, Mase K, Katayama Y, Fukuda M, Masai E2009 Nov19717587