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 24-JUL-2024, entry version 57. DE RecName: Full=Light-independent protochlorophyllide reductase subunit N {ECO:0000255|HAMAP-Rule:MF_00352}; DE Short=DPOR subunit N {ECO:0000255|HAMAP-Rule:MF_00352}; DE Short=LI-POR subunit N {ECO:0000255|HAMAP-Rule:MF_00352}; DE EC=1.3.7.7 {ECO:0000255|HAMAP-Rule:MF_00352}; GN Name=chlN {ECO:0000255|HAMAP-Rule:MF_00352}; OS Chlorokybus atmophyticus (Soil alga). OG Plastid; Chloroplast. OC Eukaryota; Viridiplantae; Streptophyta; Chlorokybophyceae; Chlorokybales; OC 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 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:0000255|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:0000255|HAMAP-Rule:MF_00352}; CC -!- COFACTOR: CC Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883; CC Evidence={ECO:0000255|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:0000255|HAMAP-Rule:MF_00352}; CC -!- PATHWAY: Porphyrin-containing compound metabolism; chlorophyll CC biosynthesis (light-independent). {ECO:0000255|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:0000255|HAMAP-Rule:MF_00352}. CC -!- SUBCELLULAR LOCATION: Plastid, chloroplast. CC -!- SIMILARITY: Belongs to the BchN/ChlN family. {ECO:0000255|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; DQ422812; ABD62180.2; -; Genomic_DNA. DR RefSeq; YP_001019172.1; NC_008822.1. DR AlphaFoldDB; Q19V53; -. DR SMR; Q19V53; -. DR GeneID; 4783259; -. 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 CDD; cd01979; Pchlide_reductase_N; 1. DR Gene3D; 3.40.50.1980; Nitrogenase molybdenum iron protein domain; 2. DR HAMAP; MF_00352; ChlN_BchN; 1. DR InterPro; IPR050293; LIPOR_BchN/ChlN. DR InterPro; IPR000510; Nase/OxRdtase_comp1. DR InterPro; IPR005970; Protochl_reductN. DR NCBIfam; TIGR01279; DPOR_bchN; 1. DR PANTHER; PTHR39429; LIGHT-INDEPENDENT PROTOCHLOROPHYLLIDE REDUCTASE SUBUNIT N; 1. DR PANTHER; PTHR39429:SF3; LIGHT-INDEPENDENT PROTOCHLOROPHYLLIDE REDUCTASE SUBUNIT N; 1. DR Pfam; PF00148; Oxidored_nitro; 1. DR PIRSF; PIRSF000162; P_chlorophyll_rd; 1. DR SUPFAM; SSF53807; Helical backbone' metal receptor; 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 FT /note="Light-independent protochlorophyllide reductase FT subunit N" FT /id="PRO_0000324035" FT BINDING 22 FT /ligand="[4Fe-4S] cluster" FT /ligand_id="ChEBI:CHEBI:49883" FT /ligand_note="ligand shared with heterodimeric partner" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00352" FT BINDING 47 FT /ligand="[4Fe-4S] cluster" FT /ligand_id="ChEBI:CHEBI:49883" FT /ligand_note="ligand shared with heterodimeric partner" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00352" FT BINDING 107 FT /ligand="[4Fe-4S] cluster" FT /ligand_id="ChEBI:CHEBI:49883" FT /ligand_note="ligand shared with heterodimeric partner" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00352" 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 //