ID A0A1C8XRI2_DUNSA Unreviewed; 506 AA. AC A0A1C8XRI2; DT 30-NOV-2016, integrated into UniProtKB/TrEMBL. DT 30-NOV-2016, sequence version 1. DT 10-MAY-2017, entry version 4. 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 ECO:0000313|EMBL:AOH77102.1}; OS Dunaliella salina (Green alga) (Protococcus salinus). OG Plastid; Chloroplast {ECO:0000313|EMBL:AOH77102.1}. OC Eukaryota; Viridiplantae; Chlorophyta; Chlorophyceae; OC Chlamydomonadales; Dunaliellaceae; Dunaliella. OX NCBI_TaxID=3046 {ECO:0000313|EMBL:AOH77102.1}; RN [1] {ECO:0000313|EMBL:AOH77102.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=SQ {ECO:0000313|EMBL:AOH77102.1}; RA Lopez H., Magdaleno D.A., Stephano J.L.; RT "The complete chloroplast genome of Dunaliella salina strain SQ."; RL Submitted (JUL-2016) 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: 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 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; KX530454; AOH77102.1; -; 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:AOH77102.1}; 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:AOH77102.1}. FT DOMAIN 64 483 Oxidored_nitro. {ECO:0000259|Pfam: FT PF00148}. FT METAL 64 64 Iron-sulfur (4Fe-4S); shared with FT heterodimeric partner. FT {ECO:0000256|HAMAP-Rule:MF_00352}. FT METAL 89 89 Iron-sulfur (4Fe-4S); shared with FT heterodimeric partner. FT {ECO:0000256|HAMAP-Rule:MF_00352}. FT METAL 149 149 Iron-sulfur (4Fe-4S); shared with FT heterodimeric partner. FT {ECO:0000256|HAMAP-Rule:MF_00352}. SQ SEQUENCE 506 AA; 56737 MW; DD25C07AD6842100 CRC64; MVKNKKRFPL FQSFKNSSSI PASKNSGLET ANQSILVEPS NETSTAALYS GQFECETGNY HTFCPISCVS WLYQKIEDSF FLVIGTKTCG YFLQNALGVM IFAEPRYAMA ELEESDISAQ LNDYKELKRL CLQIKQDRNP SVIVWIGTCT TEIIKMDLEG MAPTLEAEIG IPIVVARANG LDYAFTQGED TVLAAMAQKC PESLKNVNLP MEVEDQATKT VTSNSSNSTN TDLHISNKQQ KELVLFGSLP TTIANQLQLE LKRQGINVSG WLPSARYSDL PALGENVYVC GINPFLSRTA TSLMRRRKCK LISAPFPIGP DGTRAWVEKI CNVFGIVPTG LEEREKTIWA NLTESINFIK GKSVFFMGDN LLEISLARFL IRCGMIVYEI GIPYMDKRFQ AGELALLEKT CIEMKVPFPR IVEKPDNYYQ IQRIKELKPD LVITGMAHAN PLEARGISTK WSVEFTFAQI HGFTNTKDLL ELVSRPLRRN KNLENHDSLS KTFALQ //