KEGG   ENZYME: 1.3.7.15Help
Entry
EC 1.3.7.15                 Enzyme                                 

Name
chlorophyllide a reductase;
bchX (gene name);
bchY (gene name);
bchZ (gene name);
COR
Class
Oxidoreductases;
Acting on the CH-CH group of donors;
With an iron-sulfur protein as acceptor
BRITE hierarchy
Sysname
bacteriochlorophyllide-a:ferredoxin 7,8-oxidoreductase
Reaction(IUBMB)
(1) 3-deacetyl-3-vinylbacteriochlorophyllide a + 2 oxidized ferredoxin [iron-sulfur] cluster + ADP + phosphate = chlorophyllide a + 2 reduced ferredoxin [iron-sulfur] cluster + ATP + H2O + 2 H+ [RN:R09053];
(2) bacteriochlorophyllide a + 2 oxidized ferredoxin [iron-sulfur] cluster + ADP + phosphate = 3-acetyl-3-devinylchlorophyllide a + 2 reduced ferredoxin [iron-sulfur] cluster + ATP + H2O + 2 H+;
(3) 3-deacetyl-3-(1-hydroxyethyl)bacteriochlorophyllide a + 2 oxidized ferredoxin [iron-sulfur] cluster + ADP + phosphate = 3-devinyl-3-(1-hydroxyethyl)chlorophyllide a + 2 reduced ferredoxin [iron-sulfur] cluster + ATP + H2O + 2 H+ [RN:R09060]
Reaction(KEGG)
Substrate
3-deacetyl-3-vinylbacteriochlorophyllide a [CPD:C18152];
oxidized ferredoxin [iron-sulfur] cluster [CPD:C00139];
ADP [CPD:C00008];
phosphate [CPD:C00009];
bacteriochlorophyllide a [CPD:C18155];
3-deacetyl-3-(1-hydroxyethyl)bacteriochlorophyllide a [CPD:C18153]
Product
chlorophyllide a [CPD:C02139];
reduced ferredoxin [iron-sulfur] cluster [CPD:C00138];
ATP [CPD:C00002];
H2O [CPD:C00001];
H+ [CPD:C00080];
3-acetyl-3-devinylchlorophyllide a;
3-devinyl-3-(1-hydroxyethyl)chlorophyllide a [CPD:C18154]
Comment
The enzyme, together with EC 1.1.1.396, bacteriochlorophyllide-a dehydrogenase, and EC 4.2.1.165, chlorophyllide-a 31-hydratase, is involved in the conversion of chlorophyllide a to bacteriochlorophyllide a. These enzymes can act in multiple orders, resulting in the formation of different intermediates, but the final product of the cumulative action of the three enzymes is always bacteriochlorophyllide a. This enzyme catalyses a trans-reduction of the B-ring; the product has the (7R,8R)-configuration. In addition, the enzyme has a latent activity of EC 1.3.7.13, 3,8-divinyl protochlorophyllide a 8-vinyl-reductase (ferredoxin) [4]. The enzyme contains a [4Fe-4S] cluster, and structurally resembles the Fe protein/MoFe protein complex of nitrogenase (EC 1.18.6.1), which catalyses an ATP-driven reduction.
History
EC 1.3.7.15 created 1965 as EC 1.3.99.35, modified 2012, transferred 2016 to EC 1.3.7.15
Pathway
Porphyrin and chlorophyll metabolism
Biosynthesis of secondary metabolites
Orthology
K11333  
3,8-divinyl chlorophyllide a/chlorophyllide a reductase subunit X
K11334  
3,8-divinyl chlorophyllide a/chlorophyllide a reductase subunit Y
K11335  
3,8-divinyl chlorophyllide a/chlorophyllide a reductase subunit Z
Genes
ALV: 
TVI: 
TMB: 
MPUR: 
HHA: 
HHC: 
EBS: 
PDQ: 
RAC: 
LIM: 
LIH: 
HYR: 
RGE: 
RGE_33680(bchZ) RGE_33690(bchY) RGE_33700(bchX)
RBN: 
RDP: 
METR: 
BEB: 
AGC: 
BRA: 
BRADO1618(bchX) BRADO1619(bchY) BRADO1620(bchZ)
BBT: 
BBta_6435(bchZ) BBta_6436(bchY) BBta_6437(bchX)
BRS: 
S23_19180(bchX) S23_19190(bchY) S23_19200(bchZ)
AOL: 
BRO: 
RPA: 
RPA1522(bchX) RPA1523(bchY) RPA1524(bchZ)
RPB: 
RPC: 
RPD: 
RPE: 
RPT: 
RPX: 
BOS: 
MEX: 
MEA: 
Mex_1p2927(bchX) Mex_1p2928(bchY) Mex_1p2929(bchZ)
MDI: 
METDI3496(bchX) METDI3497(bchY) METDI3498(bchZ)
MCH: 
MRD: 
MET: 
MPO: 
MOR: 
META: 
MAQU: 
MPHY: 
MZA: 
MSL: 
RVA: 
BVR: 
BSB: 
BRL: 
RSP: 
RSP_0260(bchZ) RSP_0261(bchY) RSP_0262(bchX)
RSH: 
RSQ: 
RSK: 
RCP: 
JAN: 
Jann_0177(bchZ) Jann_0178(bchY) Jann_0179(bchX)
RDE: 
RD1_0109(bchZ) RD1_0110(bchY) RD1_0111(bchX)
RLI: 
DSH: 
Dshi_3517(bchX) Dshi_3518(bchY) Dshi_3519(bchZ)
RED: 
PTP: 
RSU: 
NHU_04287(bchX) NHU_04289(bchY) NHU_04290(bchZ)
RHM: 
RHC: 
SUAM: 
TOM: 
RMM: 
LVS: 
HBC: 
SPHI: 
SSAN: 
CIJ: 
BLAS: 
ELQ: 
PNS: 
PORL: 
AMV: 
ACMV_18770(bchZ) ACMV_18780(bchY) ACMV_18790(bchX)
RRU: 
RRF: 
RCE: 
RC1_2094(bchX) RC1_2095(bchY) RC1_2096(bchZ)
RPM: 
HMO: 
HM1_0654(bchY) HM1_0655(bchZ) HM1_0659(bchX)
RRS: 
RCA: 
CAU: 
CAG: 
CHL: 
CTM: 
GPH: 
CTE: 
CT1423(bchX) CT1826(bchY) CT2125(bchZ)
CPC: 
CLZ: 
CCH: 
CPH: 
CPB: 
CLI: 
PVI: 
PLT: 
PPH: 
PAA: 
PROC: 
PRS: 
PROS: 
CTS: 
 » show all
Taxonomy
Reference
1  [PMID:16571720]
  Authors
Nomata J, Mizoguchi T, Tamiaki H, Fujita Y
  Title
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.
  Journal
J. Biol. Chem. 281 (2006) 15021-8.
  Sequence
Reference
2  [PMID:23386973]
  Authors
Tsukatani Y, Yamamoto H, Harada J, Yoshitomi T, Nomata J, Kasahara M, Mizoguchi T, Fujita Y, Tamiaki H
  Title
An unexpectedly branched biosynthetic pathway for bacteriochlorophyll b capable of absorbing near-infrared light.
  Journal
Sci. Rep. 3 (2013) 1217.
Reference
3  [PMID:26088139]
  Authors
Lange C, Kiesel S, Peters S, Virus S, Scheer H, Jahn D, Moser J
  Title
Broadened Substrate Specificity of 3-Hydroxyethyl Bacteriochlorophyllide a Dehydrogenase (BchC) Indicates a New Route for the Biosynthesis of Bacteriochlorophyll a.
  Journal
J. Biol. Chem. 290 (2015) 19697-709.
Reference
4  [PMID:24637023]
  Authors
Harada J, Mizoguchi T, Tsukatani Y, Yokono M, Tanaka A, Tamiaki H
  Title
Chlorophyllide a oxidoreductase works as one of the divinyl reductases specifically involved in bacteriochlorophyll a biosynthesis.
  Journal
J. Biol. Chem. 289 (2014) 12716-26.
Other DBs
ExplorEnz - The Enzyme Database: 
IUBMB Enzyme Nomenclature: 
ExPASy - ENZYME nomenclature database: 
BRENDA, the Enzyme Database: 

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