ID C3VZT7_9SPER Unreviewed; 469 AA. AC C3VZT7; DT 16-JUN-2009, integrated into UniProtKB/TrEMBL. DT 16-JUN-2009, sequence version 1. DT 29-OCT-2014, entry version 29. DE RecName: Full=Light-independent protochlorophyllide reductase subunit N {ECO:0000256|HAMAP-Rule:MF_00352}; DE Short=DPOR subunit N {ECO:0000256|HAMAP-Rule:MF_00352}; DE Short=LI-POR subunit N {ECO:0000256|HAMAP-Rule:MF_00352}; DE EC=1.3.7.7 {ECO:0000256|HAMAP-Rule:MF_00352}; GN Name=chlN {ECO:0000256|HAMAP-Rule:MF_00352}; GN ORFNames=PLC-486 {ECO:0000313|EMBL:ACP51563.1}; OS Pinus aristata. OG Plastid; Chloroplast {ECO:0000313|EMBL:ACP51563.1}. OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta; OC Spermatophyta; Pinidae; Pinales; Pinaceae; Pinus; Strobus. OX NCBI_TaxID=71623 {ECO:0000313|EMBL:ACP51563.1}; RN [1] {ECO:0000313|EMBL:ACP51563.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=ARIS02 {ECO:0000313|EMBL:ACP51563.1}; RX PubMed=19954512; DOI=10.1186/1741-7007-7-84; RA Parks M., Cronn R., Liston A.; RT "Increasing phylogenetic resolution at low taxonomic levels using RT massively parallel sequencing of chloroplast genomes."; RL BMC Biol. 7:84-84(2009). RN [2] {ECO:0000313|EMBL:ACP51563.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=ARIS02 {ECO:0000313|EMBL:ACP51563.1}; RA Parks M.B., Liston A., Cronn R.C.; RL Submitted (FEB-2011) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Component of the dark-operative protochlorophyllide CC reductase (DPOR) that uses Mg-ATP and reduced ferredoxin to reduce CC ring D of protochlorophyllide (Pchlide) to form chlorophyllide a CC (Chlide). This reaction is light-independent. The NB-protein CC (ChlN-ChlB) is the catalytic component of the complex. CC {ECO:0000256|HAMAP-Rule:MF_00352}. CC -!- CATALYTIC ACTIVITY: Protochlorophyllide a + reduced ferredoxin + 2 CC ATP + 2 H(2)O = chlorophyllide a + oxidized ferredoxin + 2 ADP + 2 CC phosphate. {ECO:0000256|HAMAP-Rule:MF_00352}. CC -!- COFACTOR: Binds 1 [4Fe-4S] cluster per heterodimer. The cluster is CC bound at the heterodimer interface by residues from both subunits. CC {ECO:0000256|HAMAP-Rule:MF_00352}. CC -!- PATHWAY: Porphyrin-containing compound metabolism; chlorophyll CC biosynthesis (light-independent). {ECO:0000256|HAMAP- CC Rule:MF_00352}. CC -!- SUBUNIT: Protochlorophyllide reductase is composed of three CC subunits; ChlL, ChlN and ChlB. Forms a heterotetramer of two ChlB CC and two ChlN subunits. {ECO:0000256|HAMAP-Rule:MF_00352}. CC -!- SUBCELLULAR LOCATION: Plastid, chloroplast {ECO:0000256|HAMAP- CC Rule:MF_00352}. CC -!- SIMILARITY: Belongs to the BchN/ChlN family. {ECO:0000256|HAMAP- CC Rule:MF_00352}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; FJ899567; ACP51563.1; -; Genomic_DNA. DR UniPathway; UPA00670; -. DR GO; GO:0009507; C:chloroplast; IEA:UniProtKB-SubCell. DR GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; IEA:UniProtKB-HAMAP. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0016730; F:oxidoreductase activity, acting on iron-sulfur proteins as donors; IEA:InterPro. DR GO; GO:0016636; F:oxidoreductase activity, acting on the CH-CH group of donors, iron-sulfur protein as acceptor; IEA:UniProtKB-HAMAP. DR GO; GO:0036068; P:light-independent chlorophyll biosynthetic process; IEA:UniProtKB-UniPathway. DR GO; GO:0019685; P:photosynthesis, dark reaction; IEA:InterPro. DR HAMAP; MF_00352; ChlN_BchN; 1. DR InterPro; IPR000510; Nase/OxRdtase_comp1. DR InterPro; IPR005970; Protochl_reductN. DR Pfam; PF00148; Oxidored_nitro; 1. DR PIRSF; PIRSF000162; P_chlorophyll_rd; 1. DR TIGRFAMs; TIGR01279; DPOR_bchN; 1. PE 3: Inferred from homology; KW 4Fe-4S {ECO:0000256|HAMAP-Rule:MF_00352}; KW ATP-binding {ECO:0000256|HAMAP-Rule:MF_00352}; KW Chlorophyll biosynthesis {ECO:0000256|HAMAP-Rule:MF_00352}; KW Chloroplast {ECO:0000313|EMBL:ACP51563.1}; KW Iron {ECO:0000256|HAMAP-Rule:MF_00352}; KW Iron-sulfur {ECO:0000256|HAMAP-Rule:MF_00352}; KW Metal-binding {ECO:0000256|HAMAP-Rule:MF_00352}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00352}; KW Oxidoreductase {ECO:0000256|HAMAP-Rule:MF_00352}; KW Photosynthesis {ECO:0000256|HAMAP-Rule:MF_00352}; KW Plastid {ECO:0000313|EMBL:ACP51563.1}. FT METAL 22 22 Iron-sulfur (4Fe-4S); shared with FT heterodimeric partner. FT {ECO:0000256|HAMAP-Rule:MF_00352}. FT METAL 47 47 Iron-sulfur (4Fe-4S); shared with FT heterodimeric partner. FT {ECO:0000256|HAMAP-Rule:MF_00352}. FT METAL 107 107 Iron-sulfur (4Fe-4S); shared with FT heterodimeric partner. FT {ECO:0000256|HAMAP-Rule:MF_00352}. SQ SEQUENCE 469 AA; 53424 MW; B5B596E08328E30A CRC64; MSTKIDETIT FECETGNYHT FCPISCVSWL YQKIEDSFFL VVGTKTCGYF LQNALGVMIF AEPRYAMAEL EEGDISAHLN DYEELKTLCI RIRKDRDPSV IIWIGTCTTE IIKMDLEGMA PKLEYEIGVP ILVARANGLD YAFTQGEDTV LAVMAHRCPE QEFPIGESKE TKTKTKLFPF PLLKENKLVE YANHPPLVIF GSLPSNLVSQ LDTELRRQFI KVSGWLPAQR YADLPSLGDG VYVCGVNPFL SRTATTLIRR KKCELIVAPF PIGPDGTRAW IERICPVFGI EAQSLEEREE RIWESLKDYL DLVRGKSVFF MGDNLLEISL ARFLIRCGMI VYEIGIPYMD KRYQAAELAL LKDTCIRMCI PIPRIVEKPD NSNQIRRMRE LQPDLAITGM AHANPLGARG IGTKWSVEFT FAQIHGFANA RDVLELVTRP LRRNENLDNL DRTTLVRNNN EFYTSTPMY //