EC                  Enzyme                                 

ferredoxin:protochlorophyllide reductase (ATP-dependent);
light-independent protochlorophyllide reductase
Acting on the CH-CH group of donors;
With an iron-sulfur protein as acceptor
BRITE hierarchy
ATP-dependent ferredoxin:protochlorophyllide-a 7,8-oxidoreductase
chlorophyllide a + oxidized ferredoxin + 2 ADP + 2 phosphate = protochlorophyllide a + reduced ferredoxin + 2 ATP + 2 H2O [RN:R06282]
chlorophyllide a [CPD:C02139];
oxidized ferredoxin [CPD:C00139];
ADP [CPD:C00008];
phosphate [CPD:C00009]
protochlorophyllide a [CPD:C02880];
reduced ferredoxin [CPD:C00138];
ATP [CPD:C00002];
H2O [CPD:C00001]
Occurs in photosynthetic bacteria, cyanobacteria, green algae and gymnosperms. The enzyme catalyses trans-reduction of the D-ring of protochlorophyllide; the product has the (7S,8S)-configuration. Unlike EC (protochlorophyllide reductase), light is not required. 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 2011, modified 2013
ec00860  Porphyrin and chlorophyll metabolism
ec01100  Metabolic pathways
ec01110  Biosynthesis of secondary metabolites
K04037  light-independent protochlorophyllide reductase subunit L
K04038  light-independent protochlorophyllide reductase subunit N
K04039  light-independent protochlorophyllide reductase subunit B
SMO: SemoP_p015(chlB)
PPP: 2546744(chlB)
CRE: ChreCp003(chlB) ChreCp009(chlL) ChreCp056(chlN)
CSL: CospP_p010(chlB)
CVR: ChvaP_p015(chlB)
APRO: CP73_p070(chlB) F751_0131
GSL: JL72_p133(chlB)
ALV: Alvin_2639 Alvin_2641 Alvin_2642
TVI: Thivi_2407 Thivi_2409 Thivi_2410
LIM: L103DPR2_00999(chlL) L103DPR2_01001(chlB_2) L103DPR2_01002(bchN_2)
LIH: L63ED372_00655(chlL) L63ED372_00657(bchB) L63ED372_00658(bchN_2)
HYR: BSY239_1284(bchN) BSY239_1285(bchB) BSY239_1287(bchL)
RGE: RGE_33460(bchN) RGE_33470(bchB) RGE_33490(bchL)
METR: BSY238_2464(bchL) BSY238_2466(bchB) BSY238_2467(bchN)
AGC: BSY240_3646(bchN) BSY240_3647(bchB) BSY240_3649(bchL)
BRA: BRADO1639(bchN) BRADO1640(bchB) BRADO1642(bchL)
BBT: BBta_6414(bchL) BBta_6416(bchB) BBta_6417(bchN)
BRS: S23_19380(bchN) S23_19390(bchB) S23_19410(bchL)
BRO: BRAD285_5759(bchL) BRAD285_5761(bchB) BRAD285_5762(bchN)
RPA: RPA1542(bchN) RPA1543(bchB) RPA1545(bchL)
BOS: BSY19_4035(bchN) BSY19_4036(bchB) BSY19_4038(bchL)
MEA: Mex_1p5270(bchL) Mex_1p5272(bchB) Mex_1p5273(bchN)
MDI: METDI5870(bchL) METDI5872(bchB) METDI5873(bchN)
MOR: MOC_2249(bchL) MOC_2251(bchB) MOC_2252(bchN)
MAQU: Maq22A_c01680(nifD) Maq22A_c01685(nifD) Maq22A_c01695(nifH)
BBAR: RHAL1_4916(bchN) RHAL1_4917(bchB) RHAL1_4918(bchL)
BLAG: BLTE_02060(bchN) BLTE_02070(bchB) BLTE_02090(bchL)
RSP: RSP_0285(bchN) RSP_0286(bchB) RSP_0288(bchL)
RCP: RCAP_rcc00662(bchL) RCAP_rcc00664(bchB) RCAP_rcc00665(bchN)
JAN: Jann_0158(bchL) Jann_0160(bchB) Jann_0161(bchN)
RDE: RD1_0136(bchL) RD1_0138(bchB) RD1_0139(bchN)
DSH: Dshi_3534(bchN) Dshi_3535(bchB) Dshi_3537(bchL)
PTP: RCA23_c29890(bchL) RCA23_c29910(bchB) RCA23_c29920(bchN)
RSU: NHU_00211 NHU_00212(bchB) NHU_00214(bchL)
SPHI: TS85_22990(chlL) TS85_23000
BLAS: BSY18_2705(bchL) BSY18_2707(bchB) BSY18_2708(bchN)
AMV: ACMV_18960(bchN) ACMV_18970(bchB) ACMV_18990(bchL)
RCE: RC1_2112(bchL) RC1_2114(bchB) RC1_2115(bchN)
RPM: RSPPHO_00023(bchN) RSPPHO_00024(bchB) RSPPHO_00026(bchL)
HMO: HM1_0685(bchB) HM1_0686(bchN) HM1_0687(bchL)
RXY: Rxyl_0605
SYN: slr0749(chlL) slr0750(chlN) slr0772(chlB)
SYZ: MYO_121700(chlB) MYO_130750(chlL) MYO_130760(chlN)
SYY: SYNGTS_2150(chlB) SYNGTS_3039(chlL) SYNGTS_3040(chlN)
SYT: SYNGTI_2149(chlB) SYNGTI_3038(chlL) SYNGTI_3039(chlN)
SYS: SYNPCCN_2148(chlB) SYNPCCN_3037(chlL) SYNPCCN_3038(chlN)
SYQ: SYNPCCP_2148(chlB) SYNPCCP_3037(chlL) SYNPCCP_3038(chlN)
SYJ: D082_10760(chlN) D082_10780(chlL) D082_15420(chlB)
SYW: SYNW1723(chlN) SYNW1724(chlB) SYNW1725(chlL)
SYC: syc0136_c(chlN) syc0137_c(chlL) syc2256_d(chlB)
SYG: sync_1973(chlN) sync_1974(chlB) sync_1975(chlL)
CYA: CYA_0895(chlB) CYA_2382(chlL) CYA_2385(chlN)
CYB: CYB_1013(chlN) CYB_1016(chlL) CYB_2193(chlB)
TEL: tll2345(chlN) tll2347(chlL) tll2392(chlB)
THN: NK55_02205(chlB) NK55_08865(chlL)
CYI: CBM981_1043(chlN) CBM981_1044(chlB) CBM981_1045(chlL)
HHG: XM38_005160(chlN) XM38_005180(chlL) XM38_005360(chlB)
PSER: ABRG53_3412(chlL) ABRG53_3413(chlB) ABRG53_3414(chlN)
PMA: Pro_0544(chlL) Pro_0545(chlB) Pro_0546(chlN)
PMM: PMM0543(chlL) PMM0544(chlB) PMM0545(chlN)
PMB: A9601_05991(chlL) A9601_06001(chlB) A9601_06011(chlN)
PMC: P9515_06071(chlL) P9515_06081(chlB) P9515_06091(chlN)
PMF: P9303_07931(chlL) P9303_07941(chlB) P9303_07951(chlN)
PMG: P9301_05691(chlL) P9301_05701(chlB) P9301_05711(chlN)
PMH: P9215_06241(chlL) P9215_06251(chlB) P9215_06261(chlN)
PMJ: P9211_05451(chlL) P9211_05461(chlB) P9211_05471(chlN)
PME: NATL1_05971(chlL) NATL1_05981(chlN) NATL1_05991(chlB)
AMR: AM1_1444(chlN) AM1_1445(chlL) AM1_1539(chlB)
MAR: MAE_16230(chlL) MAE_16250(chlN) MAE_53860(chlB)
CYL: AA637_12040(chlB) AA637_12930(chlN) AA637_12935(chlL)
CYT: cce_1954(chlB) cce_4532(chlL) cce_4534(chlN)
ARP: NIES39_L01300(chlB) NIES39_L05610(chlL) NIES39_L05630(chlN)
GVI: gvip017(chlB) gvip327(chlN) gvip328(chlL)
GLJ: GKIL_1146(chlB) GKIL_3933(chlN) GKIL_3934(chlL)
ANA: all5076(chlN) all5078(chlL) alr3441(chlB)
ANB: ANA_C11498 ANA_C12003(bchL) ANA_C12004(bchB) ANA_C12005(bchN)
CTE: CT2150(chlL) CT2151(bchB) CT2152(bchN)
PROC: Ptc2401_02080(bchL) Ptc2401_02081(bchB_3) Ptc2401_02082(chlN)
 » show all
1  [PMID:8199775]
Fujita Y, Matsumoto H, Takahashi Y, Matsubara H
Identification of a nifDK-like gene (ORF467) involved in the biosynthesis of chlorophyll in the cyanobacterium Plectonema boryanum.
Plant Cell Physiol 34:305-14 (1993)
2  [PMID:18358835]
Nomata J, Ogawa T, Kitashima M, Inoue K, Fujita Y
NB-protein (BchN-BchB) of dark-operative protochlorophyllide reductase is the catalytic component containing oxygen-tolerant Fe-S clusters.
FEBS Lett 582:1346-50 (2008)
3  [PMID:20400946]
Muraki N, Nomata J, Ebata K, Mizoguchi T, Shiba T, Tamiaki H, Kurisu G, Fujita Y
X-ray crystal structure of the light-independent protochlorophyllide reductase.
Nature 465:110-4 (2010)
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