EC                 Enzyme                                 

chlorophyllide a reductase;
bchX (gene name);
bchY (gene name);
bchZ (gene name);
Acting on the CH-CH group of donors;
With an iron-sulfur protein as acceptor
BRITE hierarchy
bacteriochlorophyllide-a:ferredoxin 7,8-oxidoreductase
(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]
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]
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]
The enzyme, together with EC, bacteriochlorophyllide-a dehydrogenase, and EC, 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, 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, which catalyses an ATP-driven reduction.
EC created 1965 as EC, modified 2012, transferred 2016 to EC
ec00860  Porphyrin and chlorophyll metabolism
ec01110  Biosynthesis of secondary metabolites
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
ALV: Alvin_2556 Alvin_2561 Alvin_2562
TVI: Thivi_2003 Thivi_2010 Thivi_2011
TMB: Thimo_3003 Thimo_3004 Thimo_3005
MPUR: MARPU_13265 MARPU_13270 MARPU_13275
TSY: THSYN_31095 THSYN_31100 THSYN_31105
HHA: Hhal_1608 Hhal_1609 Hhal_1610
HHC: M911_10340 M911_10345 M911_10350
PDQ: CL55_00013570 CL55_00013580 CL55_00013590
RAC: RA876_06000 RA876_06005 RA876_06010
LIM: L103DPR2_00972(nifH1) L103DPR2_00973(bchN_1) L103DPR2_00974(chlB_1)
LIH: L63ED372_00628(nifH1) L63ED372_00629(bchN_1) L63ED372_00630(chlB)
RGE: RGE_33680(bchZ) RGE_33690(bchY) RGE_33700(bchX)
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)
BRO: BRAD285_5779(bchZ) BRAD285_5780(bchY) BRAD285_5781(bchX)
RPA: RPA1522(bchX) RPA1523(bchY) RPA1524(bchZ)
BOS: BSY19_4053(bchZ) BSY19_4054(bchY) BSY19_4055
MEA: Mex_1p2927(bchX) Mex_1p2928(bchY) Mex_1p2929(bchZ)
MDI: METDI3496(bchX) METDI3497(bchY) METDI3498(bchZ)
MOR: MOC_3181(bchZ) MOC_3182(bchY) MOC_3183
RSP: RSP_0260(bchZ) RSP_0261(bchY) RSP_0262(bchX)
RCP: RCAP_rcc00687(bchX) RCAP_rcc00688(bchY) RCAP_rcc00689(bchZ)
JAN: Jann_0177(bchZ) Jann_0178(bchY) Jann_0179(bchX)
RDE: RD1_0109(bchZ) RD1_0110(bchY) RD1_0111(bchX)
DSH: Dshi_3517(bchX) Dshi_3518(bchY) Dshi_3519(bchZ)
PTP: RCA23_c29620(bchX) RCA23_c29630(bchY) RCA23_c29640(bchZ)
RSU: NHU_04287(bchX) NHU_04289(bchY) NHU_04290(bchZ)
BLAS: BSY18_3555 BSY18_3556(bchY) BSY18_3557(bchZ)
AMV: ACMV_18770(bchZ) ACMV_18780(bchY) ACMV_18790(bchX)
RCE: RC1_2094(bchX) RC1_2095(bchY) RC1_2096(bchZ)
HMO: HM1_0654(bchY) HM1_0655(bchZ) HM1_0659(bchX)
CTE: CT1423(bchX) CT1826(bchY) CT2125(bchZ)
PROC: Ptc2401_00130(bchB_1) Ptc2401_00667(nifH1_1) Ptc2401_01952
 » show all
1  [PMID:16571720]
Nomata J, Mizoguchi T, Tamiaki H, Fujita Y
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.
J. Biol. Chem. 281 (2006) 15021-8.
2  [PMID:23386973]
Tsukatani Y, Yamamoto H, Harada J, Yoshitomi T, Nomata J, Kasahara M, Mizoguchi T, Fujita Y, Tamiaki H
An unexpectedly branched biosynthetic pathway for bacteriochlorophyll b capable of absorbing near-infrared light.
Sci. Rep. 3 (2013) 1217.
3  [PMID:26088139]
Lange C, Kiesel S, Peters S, Virus S, Scheer H, Jahn D, Moser J
Broadened Substrate Specificity of 3-Hydroxyethyl Bacteriochlorophyllide a Dehydrogenase (BchC) Indicates a New Route for the Biosynthesis of Bacteriochlorophyll a.
J. Biol. Chem. 290 (2015) 19697-709.
4  [PMID:24637023]
Harada J, Mizoguchi T, Tsukatani Y, Yokono M, Tanaka A, Tamiaki H
Chlorophyllide a oxidoreductase works as one of the divinyl reductases specifically involved in bacteriochlorophyll a biosynthesis.
J. Biol. Chem. 289 (2014) 12716-26.
Other DBs
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