ID C3VZT7_9CONI Unreviewed; 469 AA. AC C3VZT7; DT 16-JUN-2009, integrated into UniProtKB/TrEMBL. DT 16-JUN-2009, sequence version 1. DT 08-FEB-2011, entry version 13. DE RecName: Full=Light-independent protochlorophyllide reductase subunit N; DE Short=DPOR subunit N; DE Short=LI-POR subunit N; DE EC=1.18.-.-; GN Name=chlN; ORFNames=PLC-486; OS Pinus aristata. OG Plastid; Chloroplast. OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta; OC Spermatophyta; Coniferopsida; Coniferales; Pinaceae; Pinus; Strobus. OX NCBI_TaxID=71623; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=ARIS02; 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] RP NUCLEOTIDE SEQUENCE. RC STRAIN=ARIS02; RA Parks M.B., Liston A., Cronn R.C.; RL Submitted (APR-2009) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Uses Mg-ATP and reduced ferredoxin to reduce ring D of CC protochlorophyllide (Pchlide) to form chlorophyllide a (Chlide). CC This reaction is light-independent (By similarity). CC -!- PATHWAY: Porphyrin biosynthesis; chlorophyll biosynthesis (light- CC independent). CC -!- SUBUNIT: Protochlorophyllide reductase is thought to be composed CC of three subunits; chlL, chlN and chlB. Could form a CC heterotetramer of two chlB and two chlN subunits (By similarity). CC -!- SUBCELLULAR LOCATION: Plastid, chloroplast (By similarity). CC -!- SIMILARITY: Belongs to the BchN/ChlN family. 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 GO; GO:0009507; C:chloroplast; IEA:UniProtKB-SubCell. DR GO; GO:0016730; F:oxidoreductase activity, acting on iron-sulfur proteins as donors; IEA:HAMAP. DR GO; GO:0015995; P:chlorophyll biosynthetic process; IEA:UniProtKB-KW. DR GO; GO:0055114; P:oxidation-reduction process; IEA:UniProtKB-KW. 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 Chlorophyll biosynthesis; Chloroplast; Oxidoreductase; Photosynthesis; KW Plastid. 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 //