Enzyme

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     1. Oxidoreductases
        1.3 Acting on the CH-CH group of donors
            1.3.7 With an iron-sulfur protein as acceptor
ID:1.3.7.15
Description:Chlorophyllide a reductase.

3D structure

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References

External Links

UniProtKB Enzyme Link: UniProtKB 1.3.7.15
BRENDA Enzyme Link: BRENDA 1.3.7.15
KEGG Enzyme Link: KEGG1.3.7.15
BioCyc Enzyme Link: BioCyc 1.3.7.15
ExPASy Enzyme Link: ExPASy1.3.7.15
EC2PDB Enzyme Link: EC2PDB 1.3.7.15
ExplorEnz Enzyme Link: ExplorEnz 1.3.7.15
PRIAM enzyme-specific profiles Link: PRIAM 1.3.7.15
IntEnz Enzyme Link: IntEnz 1.3.7.15
MEDLINE Enzyme Link: MEDLINE 1.3.7.15
MSA:

1.3.7.15;

Phylogenetic Tree:

1.3.7.15;

Uniprot:
M-CSA:
RHEA:48948 3-deacetyl-3-(1-hydroxyethyl)bacteriochlorophyllide a + ADP + 2 oxidized [2Fe-2S]-[ferredoxin] + phosphate = 3-devinyl-3-(1-hydroxyethyl)chlorophyllide a + ATP + H(+) + H2O + 2 reduced [2Fe-2S]-[ferredoxin]
RULE(radius=1) [*:1]-[CH;+0:2](-[*:3])-[CH;+0:4](-[*:5])-[*:6].[*:7]-[Fe+;H0:8]-[*:9].[*:10]-[Fe+;H0:11]-[*:12].[*:13]-[OH;+0:14].[*:15]=[P;H0;+0:16](-[*:17])(-[*:18])-[OH;+0:19]>>[*:1]-[C;H0;+0:2](-[*:3])=[C;H0;+0:4](-[*:5])-[*:6].[*:7]-[Fe;H0;+0:8]-[*:9].[*:10]-[Fe;H0;+0:11]-[*:12].[*:13]-[O;H0;+0:14]-[P;H0;+0:16](=[*:15])(-[*:17])-[*:18].[OH2;+0:19]
Reaction
Core-to-Core More
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References

TitleAuthorsDatePubMed ID
Broadened Substrate Specificity of 3-Hydroxyethyl Bacteriochlorophyllide a Dehydrogenase (BchC) Indicates a New Route for the Biosynthesis of Bacteriochlorophyll a.Lange C, Kiesel S, Peters S, Virus S, Scheer H, Jahn D, Moser J2015 Aug 726088139
Chlorophyllide a oxidoreductase works as one of the divinyl reductases specifically involved in bacteriochlorophyll a biosynthesis.Harada J, Mizoguchi T, Tsukatani Y, Yokono M, Tanaka A, Tamiaki H2014 May 224637023
An unexpectedly branched biosynthetic pathway for bacteriochlorophyll b capable of absorbing near-infrared light.Tsukatani Y, Yamamoto H, Harada J, Yoshitomi T, Nomata J, Kasahara M, Mizoguchi T, Fujita Y, Tamiaki H201323386973
A second nitrogenase-like enzyme for bacteriochlorophyll biosynthesis: reconstitution of chlorophyllide a reductase with purified X-protein (BchX) and YZ-protein (BchY-BchZ) from Rhodobacter capsulatus.Nomata J, Mizoguchi T, Tamiaki H, Fujita Y2006 May 2616571720

RHEA:48944 ADP + bacteriochlorophyllide a + 2 oxidized [2Fe-2S]-[ferredoxin] + phosphate = 3-acetyl-3-devinylchlorophyllide a + ATP + H(+) + H2O + 2 reduced [2Fe-2S]-[ferredoxin]
RULE(radius=1) [*:1]-[CH;+0:2](-[*:3])-[CH;+0:4](-[*:5])-[*:6].[*:7]-[Fe+;H0:8]-[*:9].[*:10]-[Fe+;H0:11]-[*:12].[*:13]-[OH;+0:14].[*:15]=[P;H0;+0:16](-[*:17])(-[*:18])-[OH;+0:19]>>[*:1]-[C;H0;+0:2](-[*:3])=[C;H0;+0:4](-[*:5])-[*:6].[*:7]-[Fe;H0;+0:8]-[*:9].[*:10]-[Fe;H0;+0:11]-[*:12].[*:13]-[O;H0;+0:14]-[P;H0;+0:16](=[*:15])(-[*:17])-[*:18].[OH2;+0:19]
Reaction
Core-to-Core More
Core-to-Core More

References

TitleAuthorsDatePubMed ID
Broadened Substrate Specificity of 3-Hydroxyethyl Bacteriochlorophyllide a Dehydrogenase (BchC) Indicates a New Route for the Biosynthesis of Bacteriochlorophyll a.Lange C, Kiesel S, Peters S, Virus S, Scheer H, Jahn D, Moser J2015 Aug 726088139
Chlorophyllide a oxidoreductase works as one of the divinyl reductases specifically involved in bacteriochlorophyll a biosynthesis.Harada J, Mizoguchi T, Tsukatani Y, Yokono M, Tanaka A, Tamiaki H2014 May 224637023
An unexpectedly branched biosynthetic pathway for bacteriochlorophyll b capable of absorbing near-infrared light.Tsukatani Y, Yamamoto H, Harada J, Yoshitomi T, Nomata J, Kasahara M, Mizoguchi T, Fujita Y, Tamiaki H201323386973
A second nitrogenase-like enzyme for bacteriochlorophyll biosynthesis: reconstitution of chlorophyllide a reductase with purified X-protein (BchX) and YZ-protein (BchY-BchZ) from Rhodobacter capsulatus.Nomata J, Mizoguchi T, Tamiaki H, Fujita Y2006 May 2616571720

RHEA:37051 3-deacetyl-3-vinylbacteriochlorophyllide a + ADP + 2 oxidized [2Fe-2S]-[ferredoxin] + phosphate = ATP + chlorophyllide a + H(+) + H2O + 2 reduced [2Fe-2S]-[ferredoxin]
RULE(radius=1) [*:1]-[CH;+0:2](-[*:3])-[CH;+0:4](-[*:5])-[*:6].[*:7]-[Fe+;H0:8]-[*:9].[*:10]-[Fe+;H0:11]-[*:12].[*:13]-[OH;+0:14].[*:15]=[P;H0;+0:16](-[*:17])(-[*:18])-[OH;+0:19]>>[*:1]-[C;H0;+0:2](-[*:3])=[C;H0;+0:4](-[*:5])-[*:6].[*:7]-[Fe;H0;+0:8]-[*:9].[*:10]-[Fe;H0;+0:11]-[*:12].[*:13]-[O;H0;+0:14]-[P;H0;+0:16](=[*:15])(-[*:17])-[*:18].[OH2;+0:19]
Reaction
Core-to-Core More
Core-to-Core More

References

TitleAuthorsDatePubMed ID
Broadened Substrate Specificity of 3-Hydroxyethyl Bacteriochlorophyllide a Dehydrogenase (BchC) Indicates a New Route for the Biosynthesis of Bacteriochlorophyll a.Lange C, Kiesel S, Peters S, Virus S, Scheer H, Jahn D, Moser J2015 Aug 726088139
Chlorophyllide a oxidoreductase works as one of the divinyl reductases specifically involved in bacteriochlorophyll a biosynthesis.Harada J, Mizoguchi T, Tsukatani Y, Yokono M, Tanaka A, Tamiaki H2014 May 224637023
An unexpectedly branched biosynthetic pathway for bacteriochlorophyll b capable of absorbing near-infrared light.Tsukatani Y, Yamamoto H, Harada J, Yoshitomi T, Nomata J, Kasahara M, Mizoguchi T, Fujita Y, Tamiaki H201323386973
A second nitrogenase-like enzyme for bacteriochlorophyll biosynthesis: reconstitution of chlorophyllide a reductase with purified X-protein (BchX) and YZ-protein (BchY-BchZ) from Rhodobacter capsulatus.Nomata J, Mizoguchi T, Tamiaki H, Fujita Y2006 May 2616571720