ID CHLN_CHLAT Reviewed; 478 AA. AC Q19V53; DT 18-MAR-2008, integrated into UniProtKB/Swiss-Prot. DT 20-FEB-2007, sequence version 2. DT 19-FEB-2014, entry version 42. DE RecName: Full=Light-independent protochlorophyllide reductase subunit N; DE Short=DPOR subunit N; DE Short=LI-POR subunit N; DE EC=1.3.7.7; GN Name=chlN; OS Chlorokybus atmophyticus (Soil alga). OG Plastid; Chloroplast. OC Eukaryota; Viridiplantae; Streptophyta; Chlorokybophyceae; OC Chlorokybales; Chlorokybaceae; Chlorokybus. OX NCBI_TaxID=3144; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=SAG 48.80; RX PubMed=17222354; DOI=10.1186/1741-7007-5-2; RA Lemieux C., Otis C., Turmel M.; RT "A clade uniting the green algae Mesostigma viride and Chlorokybus RT atmophyticus represents the deepest branch of the Streptophyta in RT chloroplast genome-based phylogenies."; RL BMC Biol. 5:2-2(2007). 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 (By CC similarity). CC -!- CATALYTIC ACTIVITY: Protochlorophyllide a + reduced ferredoxin + 2 CC ATP + 2 H(2)O = chlorophyllide a + oxidized ferredoxin + 2 ADP + 2 CC phosphate. CC -!- COFACTOR: Binds 1 [4Fe-4S] cluster per heterodimer. The cluster is CC bound at the heterodimer interface by residues from both subunits CC (By similarity). CC -!- PATHWAY: Porphyrin-containing compound metabolism; chlorophyll CC biosynthesis (light-independent). 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 (By similarity). CC -!- SUBCELLULAR LOCATION: Plastid, chloroplast. 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; DQ422812; ABD62180.2; -; Genomic_DNA. DR RefSeq; YP_001019172.1; NC_008822.1. DR GeneID; 4783259; -. DR ProtClustDB; CHL00073; -. 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; ATP-binding; Chlorophyll biosynthesis; Chloroplast; Iron; KW Iron-sulfur; Metal-binding; Nucleotide-binding; Oxidoreductase; KW Photosynthesis; Plastid. FT CHAIN 1 478 Light-independent protochlorophyllide FT reductase subunit N. FT /FTId=PRO_0000324035. FT METAL 22 22 Iron-sulfur (4Fe-4S); shared with FT heterodimeric partner (By similarity). FT METAL 47 47 Iron-sulfur (4Fe-4S); shared with FT heterodimeric partner (By similarity). FT METAL 107 107 Iron-sulfur (4Fe-4S); shared with FT heterodimeric partner (By similarity). SQ SEQUENCE 478 AA; 53597 MW; 955D56E38373FF11 CRC64; MSAMTSDTLT FECETGNYHT FCPISCVAWL YQKIEDSFFL VIGTKTCGYF LQNALGVMIF AEPRYAMAEL EEGDISAQLN DYQELKRLCT QIKQDRNPSV IVWIGTCTTE IIKMDLEGMA PKIEQEIKIP IVVARANGLD YAFTQGEDTV LAAMVERCPG ETKLSEQSQD KGSSKQNFSS TKGLFSILNF NKKAAADTQP QEAEDYIDHP PLVLFGSLPG PVVSQLTLEL KRQKIKVSGW LPSQRYTDLP AVGKGVYVCG VNPFLSRTAT ILMRRRKCKL IGAPFPIGPD GTRAWVEKIC SVFNVEPIGL AERENKIWEG LEDYLQLVRG KSVFFMGDNL LEVSLARFLT RCGMIVYEIG IPYMDKRYQA AELALLEKTC QEMGVPMPRI VEKPDNYNQI QRIRELQPDL AITGMAHANP LEARGISTKW SVEFTFAQIH GFTNARDILE LVTRPLRRNN SLEGLGWTSL VKEGVLSN //