ID C3VZT7_9SPER Unreviewed; 469 AA. AC C3VZT7; DT 16-JUN-2009, integrated into UniProtKB/TrEMBL. DT 16-JUN-2009, sequence version 1. DT 19-JAN-2022, entry version 44. 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; Pinopsida; Pinidae; Conifers I; Pinaceae; Pinus; OC Pinus subgen. 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 massively RT 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 reductase CC (DPOR) that uses Mg-ATP and reduced ferredoxin to reduce ring D of CC protochlorophyllide (Pchlide) to form chlorophyllide a (Chlide). This CC reaction is light-independent. The NB-protein (ChlN-ChlB) is the CC catalytic component of the complex. {ECO:0000256|ARBA:ARBA00025201, CC ECO:0000256|HAMAP-Rule:MF_00352}. CC -!- CATALYTIC ACTIVITY: CC Reaction=2 ADP + chlorophyllide a + oxidized 2[4Fe-4S]-[ferredoxin] + 2 CC phosphate = 2 ATP + 2 H2O + protochlorophyllide a + reduced 2[4Fe- CC 4S]-[ferredoxin]; Xref=Rhea:RHEA:28202, Rhea:RHEA-COMP:10002, CC Rhea:RHEA-COMP:10004, ChEBI:CHEBI:15377, ChEBI:CHEBI:30616, CC ChEBI:CHEBI:33722, ChEBI:CHEBI:33723, ChEBI:CHEBI:43474, CC ChEBI:CHEBI:83348, ChEBI:CHEBI:83350, ChEBI:CHEBI:456216; EC=1.3.7.7; CC Evidence={ECO:0000256|ARBA:ARBA00000802, ECO:0000256|HAMAP- CC Rule:MF_00352}; CC -!- COFACTOR: CC Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883; CC Evidence={ECO:0000256|HAMAP-Rule:MF_00352}; CC Note=Binds 1 [4Fe-4S] cluster per heterodimer. The cluster is bound at CC 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|ARBA:ARBA00004949, CC ECO:0000256|HAMAP-Rule:MF_00352}. CC -!- SUBUNIT: Protochlorophyllide reductase is composed of three subunits; CC ChlL, ChlN and ChlB. Forms a heterotetramer of two ChlB and two ChlN CC subunits. {ECO:0000256|ARBA:ARBA00025959, ECO:0000256|HAMAP- CC Rule:MF_00352}. CC -!- SUBCELLULAR LOCATION: Plastid, chloroplast CC {ECO:0000256|ARBA:ARBA00004229, ECO:0000256|HAMAP-Rule:MF_00352}. CC -!- SIMILARITY: Belongs to the BchN/ChlN family. {ECO:0000256|HAMAP- CC Rule:MF_00352}. CC -!- SIMILARITY: Belongs to the ChlB/BchB/BchZ family. CC {ECO:0000256|ARBA:ARBA00008935}. 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-UniRule. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule. 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-UniRule. 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 DOMAIN 22..438 FT /note="Oxidored_nitro" FT /evidence="ECO:0000259|Pfam:PF00148" FT METAL 22 FT /note="Iron-sulfur (4Fe-4S); shared with heterodimeric FT partner" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00352" FT METAL 47 FT /note="Iron-sulfur (4Fe-4S); shared with heterodimeric FT partner" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00352" FT METAL 107 FT /note="Iron-sulfur (4Fe-4S); shared with heterodimeric FT partner" FT /evidence="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 //