EC number:1.14.15.27

Enzyme

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     1. Oxidoreductases
        1.14 Acting on paired donors, with incorporation or reduction of molecular oxygen
            1.14.15 With reduced iron-sulfur protein as one donor, and incorporation of one atom of oxygen into the other donor
ID:1.14.15.27
Description:Beta-dihydromenaquinone-9 omega-hydroxylase.
Alternative Name: CYP128.

3D structure

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PDB

References

External Links

UniProtKB Enzyme Link: UniProtKB 1.14.15.27
BRENDA Enzyme Link: BRENDA 1.14.15.27
KEGG Enzyme Link: KEGG1.14.15.27
BioCyc Enzyme Link: BioCyc 1.14.15.27
ExPASy Enzyme Link: ExPASy1.14.15.27
EC2PDB Enzyme Link: EC2PDB 1.14.15.27
ExplorEnz Enzyme Link: ExplorEnz 1.14.15.27
PRIAM enzyme-specific profiles Link: PRIAM 1.14.15.27
IntEnz Enzyme Link: IntEnz 1.14.15.27
MEDLINE Enzyme Link: MEDLINE 1.14.15.27

EC number:1.14.15.27

MSA:

1.14.15.27;
Phylogenetic Tree:

1.14.15.27;
Uniprot:
M-CSA:
RHEA:56680 beta-dihydromenaquinone-9 + 2 H(+) + O2 + 2 reduced [2Fe-2S]-[ferredoxin] = H2O + omega-hydroxy-beta-dihydromenaquinone-9 + 2 oxidized [2Fe-2S]-[ferredoxin]
RULE(radius=1) [*:1]-[CH3;+0:2].[*:3]-[Fe;H0;+0:4]-[*:5].[*:6]-[Fe;H0;+0:7]-[*:8].[H+;H0:9].[H+;H0:10].[O;H0;+0:11]=[O;H0;+0:12]>>[*:1]-[CH2;+0:2]-[OH;+0:11].[*:3]-[Fe+;H0:4]-[*:5].[*:6]-[Fe+;H0:7]-[*:8].[OH2;+0:12]
Reaction
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References

TitleAuthorsDatePubMed ID
Biosynthesis and Regulation of Sulfomenaquinone, a Metabolite Associated with Virulence in Mycobacterium tuberculosis.Sogi KM, Holsclaw CM, Fragiadakis GK, Nomura DK, Leary JA, Bertozzi CR2016 Nov 1127933784
Structural characterization of a novel sulfated menaquinone produced by stf3 from Mycobacterium tuberculosis.Holsclaw CM, Sogi KM, Gilmore SA, Schelle MW, Leavell MD, Bertozzi CR, Leary JA2008 Oct 1718928249