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:1.14.15.9
Description:Spheroidene monooxygenase.
Alternative Name: Spirilloxanthin monooxygenase.
Acyclic carotenoid 2-ketolase.
2-oxo-spirilloxanthin monooxygenase.

3D structure

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References

External Links

UniProtKB Enzyme Link: UniProtKB 1.14.15.9
BRENDA Enzyme Link: BRENDA 1.14.15.9
KEGG Enzyme Link: KEGG1.14.15.9
BioCyc Enzyme Link: BioCyc 1.14.15.9
ExPASy Enzyme Link: ExPASy1.14.15.9
EC2PDB Enzyme Link: EC2PDB 1.14.15.9
ExplorEnz Enzyme Link: ExplorEnz 1.14.15.9
PRIAM enzyme-specific profiles Link: PRIAM 1.14.15.9
IntEnz Enzyme Link: IntEnz 1.14.15.9
MEDLINE Enzyme Link: MEDLINE 1.14.15.9
MSA:

1.14.15.9;

Phylogenetic Tree:

1.14.15.9;

Uniprot:
M-CSA:
RHEA:33027 4 H(+) + 2 O2 + 4 reduced [2Fe-2S]-[ferredoxin] + spheroidene = 3 H2O + 4 oxidized [2Fe-2S]-[ferredoxin] + spheroiden-2-one
RULE(radius=1) [*:1]-[CH2;+0:2]-[*:3].[*:4]-[Fe;H0;+0:5]-[*:6].[*:7]-[Fe;H0;+0:8]-[*:9].[*:10]-[Fe;H0;+0:11]-[*:12].[*:13]-[Fe;H0;+0:14]-[*:15].[H+;H0:16].[H+;H0:17].[H+;H0:18].[H+;H0:19].[O;H0;+0:20]=[O;H0;+0:21].[O;H0;+0:22]=[O;H0;+0:23]>>[*:1]-[C;H0;+0:2](-[*:3])=[O;H0;+0:20].[*:4]-[Fe+;H0:5]-[*:6].[*:7]-[Fe+;H0:8]-[*:9].[*:10]-[Fe+;H0:11]-[*:12].[*:13]-[Fe+;H0:14]-[*:15].[OH2;+0:21].[OH2;+0:22].[OH2;+0:23]
Reaction
Core-to-Core More

References

TitleAuthorsDatePubMed ID
Novel activity of Rhodobacter sphaeroides spheroidene monooxygenase CrtA expressed in Escherichia coli.Lee PC, Holtzapple E, Schmidt-Dannert C2010 Nov20851979
Catalytic properties of the expressed acyclic carotenoid 2-ketolases from Rhodobacter capsulatus and Rubrivivax gelatinosus.Gerjets T, Steiger S, Sandmann G2009 Feb19136077

RHEA:33035 2-oxospirilloxanthin + 4 H(+) + 2 O2 + 4 reduced [2Fe-2S]-[ferredoxin] = 2,2'-dioxospirilloxanthin + 3 H2O + 4 oxidized [2Fe-2S]-[ferredoxin]
RULE(radius=1) [*:1]-[CH2;+0:2]-[*:3].[*:4]-[Fe;H0;+0:5]-[*:6].[*:7]-[Fe;H0;+0:8]-[*:9].[*:10]-[Fe;H0;+0:11]-[*:12].[*:13]-[Fe;H0;+0:14]-[*:15].[H+;H0:16].[H+;H0:17].[H+;H0:18].[H+;H0:19].[O;H0;+0:20]=[O;H0;+0:21].[O;H0;+0:22]=[O;H0;+0:23]>>[*:1]-[C;H0;+0:2](-[*:3])=[O;H0;+0:20].[*:4]-[Fe+;H0:5]-[*:6].[*:7]-[Fe+;H0:8]-[*:9].[*:10]-[Fe+;H0:11]-[*:12].[*:13]-[Fe+;H0:14]-[*:15].[OH2;+0:21].[OH2;+0:22].[OH2;+0:23]
Reaction
Core-to-Core More

References

TitleAuthorsDatePubMed ID
Novel activity of Rhodobacter sphaeroides spheroidene monooxygenase CrtA expressed in Escherichia coli.Lee PC, Holtzapple E, Schmidt-Dannert C2010 Nov20851979
Catalytic properties of the expressed acyclic carotenoid 2-ketolases from Rhodobacter capsulatus and Rubrivivax gelatinosus.Gerjets T, Steiger S, Sandmann G2009 Feb19136077

RHEA:33039 4 H(+) + 2 O2 + 4 reduced [2Fe-2S]-[ferredoxin] + spirilloxanthin = 2-oxospirilloxanthin + 3 H2O + 4 oxidized [2Fe-2S]-[ferredoxin]
RULE(radius=1) [*:1]-[CH2;+0:2]-[*:3].[*:4]-[Fe;H0;+0:5]-[*:6].[*:7]-[Fe;H0;+0:8]-[*:9].[*:10]-[Fe;H0;+0:11]-[*:12].[*:13]-[Fe;H0;+0:14]-[*:15].[H+;H0:16].[H+;H0:17].[H+;H0:18].[H+;H0:19].[O;H0;+0:20]=[O;H0;+0:21].[O;H0;+0:22]=[O;H0;+0:23]>>[*:1]-[C;H0;+0:2](-[*:3])=[O;H0;+0:20].[*:4]-[Fe+;H0:5]-[*:6].[*:7]-[Fe+;H0:8]-[*:9].[*:10]-[Fe+;H0:11]-[*:12].[*:13]-[Fe+;H0:14]-[*:15].[OH2;+0:21].[OH2;+0:22].[OH2;+0:23]
Reaction
Core-to-Core More

References

TitleAuthorsDatePubMed ID
Novel activity of Rhodobacter sphaeroides spheroidene monooxygenase CrtA expressed in Escherichia coli.Lee PC, Holtzapple E, Schmidt-Dannert C2010 Nov20851979
Catalytic properties of the expressed acyclic carotenoid 2-ketolases from Rhodobacter capsulatus and Rubrivivax gelatinosus.Gerjets T, Steiger S, Sandmann G2009 Feb19136077